Belongs to the glycosyltransferase 15 family.
Possible glycosyltransferase that transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage.
Present with 2890 molecules/cell in log phase SD medium.
DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.
Present with 3690 molecules/cell in log phase SD medium.
Present with 3260 molecules/cell in log phase SD medium.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM5/TYW2 family.
Present with 656 molecules/cell in log phase SD medium.
S-adenosyl-L-methionine-dependent transferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14) to produce wybutosine-86.
Was originally thought to be a methyltransferase.
tRNA(Phe) from mutant shows accumulation of 4-demethylwyosine (ImG-14) and absence of wybutosine.
Belongs to the purine-cytosine permease (2.A.39) family.
Expression is controlled by the transcription repressors SUM1, HST1 and RFM1.
High-affinity pH-dependent nicotinamide riboside transporter which also transports thiamine with low affinity. Involved in 5-fluorocytosine sensitivity.
May interact with target proteins during translocation into the lumen of the endoplasmic reticulum. May protect unfolded target proteins against degradation and facilitate correct glycosylation (Potential).
Present with 846 molecules/cell in log phase SD medium.
Belongs to the transaldolase family. Type 1 subfamily.
Present with 53000 molecules/cell in log phase SD medium.
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Two isoenzymes seem to be encoded by the same gene.
By calcium shortage, copper deficiency (via MAC1) and the presence of galactose (via GAL4).
Functions in the galactose metabolic pathway via the GAL83 protein and that it may control the level of ENO1.
Present with 721 molecules/cell in log phase SD medium.
May be involved in a late step of spore wall assembly.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family.
Interacts with other septin proteins such as SPR28 to form a ring at the bud neck.
Septins are GTPases involved in cytokinesis that assemble into filaments and form a ring at the cleavage site. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation (By similarity).
Belongs to the VPS10-related sortilin family.
Functions as a sorting receptor in the Golgi compartment required for the intracellular sorting and delivery of soluble vacuolar proteins, like carboxypeptidase Y (CPY) and proteinase A. May execute multiple rounds of sorting by cycling between the late Golgi and a prevacuolar endosome-like compartment. Binds the Golgi-modified P2 form of CPY, and this interaction is dependent on the presence of an intact CPY vacuolar protein sorting signal.
Present with 7210 molecules/cell in log phase SD medium.
The lumenal domain contains two regions of approximately 650 AA that exhibit 20% identity. The cytoplasmic domain serves as a Golgi retention/recycling signal.
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Displays increased levels of spontaneous RAD52 foci in proliferating diploid cells.
Present with 1620 molecules/cell in log phase SD medium.
Reduces benzil stereospecifically to (S)-benzoin. Is probably involved in a pathway contributing to genomic integrity.
Belongs to the serine/threonine dehydratase family.
In response to starvation for tryptophan and branched-chain amino acid imbalance.
Isoleucine allosterically inhibits while valine allosterically activates this enzyme.
Present with 11900 molecules/cell in log phase SD medium.
Present with 2820 molecules/cell in log phase SD medium.
Binds 2 divalent metal cations (By similarity). Shows activity with Mn(2+), Co(2+) and Mg(2+) but shows no activity with Zn(2+) (PubMed:29752939).
Catalyzes the dephosphorylation of the nucleoside 5'-monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and deoxythymidine monophosphate (dTMP).
Present with 2730 molecules/cell in log phase SD medium.
Belongs to the trans-sulfuration enzymes family. MET7 subfamily.
Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia (By similarity).
Present with 2810 molecules/cell in log phase SD medium.
Component of the signal peptidase complex (SPC) composed of a catalytic subunit SEC11 and three accessory subunits SPC1, SPC2 and SPC3 (PubMed:9148931). The complex induces a local thinning of the ER membrane which is used to measure the length of the signal peptide (SP) h-region of protein substrates (By similarity). This ensures the selectivity of the complex towards h-regions shorter than 18-20 amino acids (By similarity). SPC associates with the translocon complex (PubMed:10921929). Interacts with SBH1 and SEB2/SBH2 (PubMed:10921929).
Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (PubMed:8663399). Dispensable for SPC enzymatic activity (PubMed:8663399).
Present with 5550 molecules/cell in log phase SD medium.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase SFM1 family.
Present with 2520 molecules/cell in log phase SD medium.
S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that monomethylates ribosomal protein S3 (RPS3) at 'Arg-146'.
Acts as an allosteric regulator of polarized exocytosis by promoting the targeted fusion of vesicles with the plasma membrane. Coordinates the spatial and temporal nature of both Rab-dependent tethering and SNARE-dependent membrane fusion of exocytic vesicles with the plasma membrane. Required for targeting of the sodium pumping ATPase ENA1 to the Cell Surface, thus being involved in maintenance of ion homeostasis in cells exposed to NaCl stress. May be involved in the targeting of the myosin proteins to their intrinsic pathways. Multicopy suppressor of RHO3. May also participate in the maintenance of cell polarity and bud growth.
Belongs to the oxidase-dependent Fe transporter (OFeT) (TC 9.A.10.1) family.
High affinity iron transporter probably involved in transport of intravacuolar stores of iron.
Present with 486 molecules/cell in log phase SD medium.
Present with 3750 molecules/cell in log phase SD medium.
GLC7 phosphatase-regulatory protein involved in GLC7 subcellular redistribution and chromosome segregation.
Present with 227 molecules/cell in log phase SD medium.
Belongs to the eukaryotic release factor 1 family. Pelota subfamily. Highly divergent.
Involved in the integrity functions of RAM, a conserved signaling network that regulates maintenance of polarized growth and daughter-cell-specific transcription.
Present with 1920 molecules/cell in log phase SD medium.
Belongs to the cyclin family. PCL1,2 subfamily.
By transcription factor SWI5 in a cell cycle-regulated manner. Peaks in late M, early G1 phase (at protein level).
M/G1-specific cyclin partner of the cyclin-dependent kinase (CDK) PHO85. May have a role in bud site selection in G1 phase.
Weakly cell cycle regulated, peaking in S phase.
Involved in spore wall maturation. Thought to catalyze the oxidation of tyrosine residues in the formation of LL-dityrosine a precursor of the spore wall.
Belongs to the SRP1/TIP1 family. Seripauperin subfamily.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Present with 1040 molecules/cell in log phase SD medium.
Protein kinase involved in morphogenesis and cell integrity.
Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts with the ESCRT-0 subunit VPS27.
Present with 129000 molecules/cell in log phase SD medium.
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity; specifically the MCM2-MCM5 association is proposed to be reversible and to mediate a open ring conformation which may facilitate DNA loading. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Necessary for cell growth.
Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5; loaded onto DNA, forms a head-head double hexamer.
Early fractionation of eukaryotic MCM proteins yielded a variety of dimeric, trimeric and tetrameric complexes with unclear biological significance. Specifically a MCM467 subcomplex is shown to have in vitro helicase activity which is inhibited by the MCM2 subunit. The MCM2-7 hexamer is the proposed physiological active complex.
Present with 1690 molecules/cell in log phase SD medium.
Component of the SHU complex composed of at least CSM2, PSY3, SHU1 and SHU2.
Plays a role in a RAD51/RAD54-dependent homologous recombination repair (HRR) pathway to repair MMS-induced lesions during S-phase.
Present with 2157 molecules/cell in log phase SD medium.
May regulate endocytosis by recruiting RSP5 ubiquitin ligase activity to specific plasma membrane proteins in response to extracellular stimuli.
Phosphorylated by the cyclin-CDKs PCL6-PHO85 and PCL7-PHO85.
Present with 49 molecules/cell in log phase SD medium.
Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity).
Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity).
Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity).
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YMR051C ORF.
Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).
Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity).
The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.
The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.
The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues (By similarity).
Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.
Present with 7300 molecules/cell in log phase SD medium.
Belongs to the universal ribosomal protein uS8 family.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Component of the mitochondrial small ribosomal subunit (mt-SSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins.
Modulator of GLC7 type-1 protein phosphatase.
Phosphorylated by the cyclin-CDKs PCL6-PHO85 and PCL7-PHO85. Phosphorylation of Thr-118 inactivates GLC8.
Present with 3440 molecules/cell in log phase SD medium.
Interacts with NUM1, when DYN1 is present.
Present with 752 molecules/cell in log phase SD medium.
Required for viability in the absence of the kinesin-related CIN8 mitotic motor. May be a dynein intermediate chain.
Belongs to the eukaryotic ribosomal protein eS19 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). eS19 is required for proper maturation of the small (40S) ribosomal subunit. Binds to 40S pre-ribosomal particles, probably required after association of NOC4 but before association of ENP1, TSR1 and RIO2 with 20/21S pre-rRNA (PubMed:16159874, PubMed:17726054).
Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).
Disruption of a single RPS19 gene reduces cell growth; a double disruption is lethal. Depletion experiments show the proteins are required for correct maturation of precursor rRNA to generate the 18S small rRNA. A specific site between the 18S and 5.8S precursors (site A2 in ETS1) is not cleaved in disruption mutants. Partially assembled ribosomes are retained in the nucleolus rather than being exported to the cytoplasm. All effects are exacerbated in the double disruption. Increases association of NOC4 with 20S/21S pre-rRNA, decreases association of ENP1, TSR1 and RIO2 with 20S/21S pre-rRNA.
Present with 29000 molecules/cell in log phase SD medium.
Associates with translationally inactive ribosomes in the nonrotated state. LSO2 bridges the decoding sites of the small with the GTPase activating center (GAC) of the large subunit. This position allows accommodation of the DOM34-dependent ribosome recycling system, which splits LSO2-containing ribosomes.
Constitutively expressed. Expression is not regulated by iron unlike the LSO1 paralog.
Mild slow-growth phenotype in response to reduced iron levels (PubMed:26450372). Displays global translation defects during recovery from stationary phase with translation of most genes reduced more than 4-fold. Ribosomes accumulated at start codons, were depleted from stop codons, and showed codon-specific changes in occupancy (PubMed:30208026).
Ribosome-associated protein required for translational recovery after starvation from stationary phase. May facilitate rapid translation reactivation by stabilizing the recycling-competent state of inactive ribosomes.
Binds DNA as a homodimer. Interacts with transcription factor PHO2 and binds cooperatively to PHO5 UAS. Interacts with the cyclin-CDK PHO80-PHO85 and the CDK inhibitor (CKI) PHO81.
Phosphorylated by the cyclin-CDK PHO80-PHO85 at five residues under high-phosphate conditions, preventing PHO4 from activating the structural PHO genes. Phosphorylation of Ser-114 and Ser-128 promotes nuclear export. Phosphorylation of Ser-152 decreases nuclear import. Phosphorylation of Ser-223 decreases the binding affinity for PHO2.
The 9aaTAD motif (residues 75 to 83) is a transactivation domain present in a large number of yeast and animal transcription factors.
Transcriptional activator that regulates the expression of repressible phosphatase under phosphate starvation conditions. Binds to the upstream activating sequence (UAS) of several phosphatase encoding PHO genes. Inhibited by the cyclin-CDK PHO80-PHO85 under high-phosphate conditions.
ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing (PubMed:11585918, PubMed:7883168). Associates directly with chromatin, correlating with transcriptional activity (PubMed:22679025). Required for assembly of mRNA-binding proteins YRA1, NAB2, and MEX67 onto poly(A)+ RNA (PubMed:23721653).
Belongs to the DEAD box helicase family. DDX5/DBP2 subfamily.
Interacts with UPF1. Associates with polysomes.
Present with 33100 molecules/cell in log phase SD medium.
Results in defective assembly of nuclear mRNPs.
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
The gene for DBP2 has an unusual intron both because of its size and because of its location near the 3' end of the gene. It may have a function in an intron-mediated negative feedback loop regulating DBP2 expression.
Involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.
Present with 704 molecules/cell in log phase SD medium.
Essential component of the GPI mannosyltransferase 2 complex. Responsible for the transfer of the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly.
Part of the GPI mannosyltransferase 2 complex composed of GPI18 and PGA1.
Present with 6940 molecules/cell in log phase SD medium.
Belongs to the DNA2/NAM7 helicase family.
ECM32 was originally identified as a DNA helicase and as component of DNA polymerase I.
Interacts with the peptidyl release factors SUP35 and weakly with SUP45.
Present with 736 molecules/cell in log phase SD medium.
Probable RNA helicase, which may be involved in modulation of the translation termination process. Probably unwinds double-stranded RNA. In vitro, unwinds covalently closed, circular DNA in the presence of a DNA topoisomerase TOP1 and replication factor-A protein RFA1.
Sensitivity to drugs that affect translation fidelity. Overexpression results in a nonsense suppression phenotype.
Increases frequency of mitochondrial genome loss.
Present with 1350 molecules/cell in log phase SD medium.
Associates with the mitochondrial ribosome (PubMed:25683707). Component of a multi-subunit COQ enzyme complex (PubMed:25631044).
Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression (PubMed:25683707). Component of a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis (PubMed:25631044).
Present with 1470 molecules/cell in log phase SD medium.
Shows impaired de novo coenzyme Q biosynthesis.
Induced by limited extracellular thiamine levels.
Low affinity thiamine transporter responsible for intake of thiamine. It is possible that the primary function is the uptake of closely related compounds and that thiamine transport is a secondary activity of these proteins.
Component of the 18S U1 snRNP particle, a subcomplex of the spliceosome.
Component of the U1 snRNP particle, which recognizes and binds the 5'-splice site of pre-mRNA. Together with other non-snRNP factors, U1 snRNP forms the spliceosomal commitment complex, that targets pre-mRNA to the splicing pathway.
Present with 782 molecules/cell in log phase SD medium.
Belongs to the bacterial ribosomal protein bL34 family.
Component of the mitochondrial large ribosomal subunit (mt-LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins.
Present with 200 molecules/cell in log phase SD medium.
Component of TORC2, which regulates cell cycle-dependent polarization of the actin-cytoskeleton and cell wall integrity. TORC2 controls polarity of the actin cytoskeleton, which is required for orienting the secretory pathway toward discrete growth sites, via the RHO1/PKC1/MAPK cell integrity pathway.
The target of rapamycin complex 2 (TORC2) is composed of at least AVO1, AVO2, BIT61, LST8, TOR2 and TSC11. TORC2 likely forms a homodimer. Contrary to TORC1, TORC2 does not bind to and is not sensitive to FKBP-rapamycin. AVO1 is required for TORC2 integrity by tethering AVO2 and TSC11 to the complex.
Belongs to the eukaryotic ribosomal protein eL31 family.
Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Present with 57500 molecules/cell in log phase SD medium.
Involved in the control of energetic metabolism and significantly contribute to cell fitness, especially under respiratory growth conditions.
Present with 5530 molecules/cell in log phase SD medium.
Up-regulated under carbon limitation and repressed under high glucose.
Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
Catalytic component of ISW1-type complexes, which act by remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. They are involved in coordinating transcriptional repression, activation and elongation phases. The ISW1A complex represses gene expression at initiation through specific positioning of a promoter proximal dinucleosome. The ISW1B complex acts within coding regions to control the amount of RNA polymerase II released into productive elongation and to coordinate elongation with termination and pre-mRNA processing.
Component of the ISW1A complex, which at least consists of ISW1 and IOC3. Component of the ISW1B complex, which at least consists of ISW1, IOC2 and IOC4.
Present with 1500 molecules/cell in log phase SD medium.
Component of the small ribosomal subunit, ribosomal RNA processing complex (SSU RRP complex). Interacts with PNO1.
Present with 4490 molecules/cell in log phase SD medium.
Required for the synthesis of 40S ribosome subunits. Has a role in processing 20S pre-rRNA into the mature 18S rRNA, where it is required for cleavage at the 3' end of the mature 18S rRNA (D-site). Accompanies the 20S pre-rRNA from the nucleus to the cytoplasm. In association with NIN1, may promote the recruitment of the proteasome to the ribosomal subunits stalled in maturation.
Periodic expression during the cell cycle with a peak at S phase.
Belongs to the Maf family. YhdE subfamily.
Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. Can also hydrolyze the modified nucleotides 5-methyl-UTP (m(5)UTP) and pseudo-UTP. Has weak activity with CTP (PubMed:24210219). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids (PubMed:24210219).
Present with 1940 molecules/cell in log phase SD medium.
Belongs to the prokaryotic/mitochondrial release factor family.
Methylation of glutamine in the GGQ triplet is conserved from bacteria to mammals (By similarity). N5-methylated on Gln-287 by MTQ1.
Mitochondrial peptide chain release factor that directs the termination of translation in response to the peptide chain termination codons UAA and UAG.
Present with 414 molecules/cell in log phase SD medium.
Negative regulator of multiple nitrogen catabolic genes including the allantoin pathway genes.
Sensitive to nitrogen catabolite repression.
ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes (By similarity). Redundant to DED1, may be required in conditions in which DED1 expression is decreased.
Belongs to the DEAD box helicase family. DDX3/DED1 subfamily.
Present with 1480 molecules/cell in log phase SD medium.
Belongs to the universal ribosomal protein uS4 family.
Component of the mitochondrial small ribosomal subunit (mt-SSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. uS3m, uS4m and uS5m form the narrow entry site of the mRNA channel.
Present with 3270 molecules/cell in log phase SD medium.
According to PubMed:17173052 and PubMed:17174896, only DIS3/RRP44 subunit of the exosome core has exonuclease activity.
Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which associates with catalytic subunits DIS3 and RRP6 in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits and peripheral S1 domain-containing components CSL4, RRP4 and RRP40 located on the top of the ring structure.
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes.
Autophagy-related protein required for cytoplasm to vacuole transport (Cvt) and autophagy as a part of the autophagy-specific VPS34 PI3-kinase complex I. This complex is essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. ATG38 is required for the integrity of the active PI3-kinase complex I by maintaining an association between VPS15-VPS34 and ATG1P-VPS30 subcomplexes.
Homodimer. Component of the autophagy-specific VPS34 PI3-kinase complex I composed of VPS15, VPS30, VPS34, ATG14 and ATG38. Interacts directly with ATG14 and VPS34.
Involved in the assembly of the cytochrome oxidase complex. Required for the maturation and subsequent assembly of the mitochondrially encoded COX2, the precursor of subunit 2 of cytochrome oxidase.
May be involved in the control of meiotic sister-chromatid recombination.
Present with 7250 molecules/cell in log phase SD medium.
Affects glycosylation of chitinase and increases sensitivity to calcofluor white and caffeine.
Belongs to the glycosyltransferase 39 family.
PMT1 and PMT2 form a functional heterodimer. The complex interacts with endoplasmic reticulum proteins EMP24, ERV25, ERP1, ERP2, CDC48, HRD1, USA1, YOS9, ERO1, PDI1, UBR1, Cue4, DFM1 and TED1. Forms also a minor complex with PMT3.
Present with 41500 molecules/cell in log phase SD medium.
Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT2 and more rarely with PMT3 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export. Required for incorporation of proteins in the cell wall.
The large luminal loop 5 is essential for mannosyltransferase activity but not for PMT1-PMT2 complex formation.
Present with 2530 molecules/cell in log phase SD medium.
Acts as a regulatory component of the translation initiation factor 2B (eIF2-B or GCD complex), which catalyzes the exchange of eukaryotic initiation factor 2 (eIF-2)-bound GDP for GTP and is regulated by phosphorylated eIF-2. It activates the synthesis of GCN4 in yeast under amino acid starvation conditions by suppressing the inhibitory effects of multiple AUG codons present in the leader of GCN4 mRNA. It may promote either repression or activation of GCN4 expression depending on amino acid availability. GCD6 and GCD7 repress GCN4 expression at the translational level by ensuring that ribosomes which have translated UORF1 will reinitiate at UORF2, -3, or -4 and thus fail to reach the GCN4 start site.
Belongs to the eIF-2B alpha/beta/delta subunits family.
Present with 6650 molecules/cell in log phase SD medium.
Translation initiation factor 2B (eIF2-B) is composed of five different subunits; alpha (GCN3), beta (GCD7), gamma (GCD1), delta (GCD2) and epsilon (GCD6). A regulatory subcomplex comprising GCN3, GCD7 and GCD2 interacts preferentially with phosphorylated eIF-2 and has no exchange activity in vitro.
May assist STE12 in the pheromone-dependent expression of KAR3 and CIK1. Also required for meiosis.
Component of the septin complex which consists of CDC3, CDC10, CDC11, CDC12 and probably SHS1 and rearranges to a cortical collar of highly ordered filaments at the mother-bud-neck. A complex formed by CDC3, CDC10, CDC11 and CDC12 is capable of forming long filaments in vitro and the components seem to be present in a 2:2:2:2 arrangement in vivo. The filaments are proposed to be formed by the end-to-end polymerization of CDC3-CDC12-CDC11 complexes with CDC10 serving as a bridge to bundle the polymers into paired filaments. Component of the GIN4 complex composed of at least BNI5, CDC3, CDC10, CDC11, CDC12, GIN4, NAP1 and SHS1. Self-associates. Interacts with SYP1.
Present with 1170 molecules/cell in log phase SD medium.
Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring approximate 15 minutes before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation.
Probable phospholipase that hydrolyzes phosphatidic acid.
Belongs to the mitochondrial carrier (TC 2.A.29) family.
Involved in the mitochondrial activation of SOD2 by specifically facilitating insertion of the essential manganese cofactor. Has the ability to activate iron regulon in an iron-dependent manner. Responds to calorie restriction (CR) strength.
Loss of mitochondrial manganese superoxide dismutase SOD2 activity due to misincorporation of iron into SOD2 rather than manganese. Normal SOD2 activity when in association with YFH1 deletion. Doesn't impair activity of a cytosolic version of manganese SOD. The iron regulatory transcription factor AFT1 is constitutively active. Accumulates mtDNA mutations. Elevated mitochondrial iron and manganese levels.
Present with 538 molecules/cell in log phase SD medium.
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.
Kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Activates the PBS2 MAP kinase kinase by phosphorylation.
Present with 217 molecules/cell in log phase SD medium.
Belongs to the glycosyltransferase 28 family.
Present with 396 molecules/cell in log phase SD medium.
Probable sterol 3-beta-glucosyltransferase that is not involved in cytoplasm to vacuole transport (Cvt), pexophagy or nonselective autophagy (PubMed:17012830).
Involved in the initiation of assembly of the COPII coat required for the formation of transport vesicles from the endoplasmic reticulum (ER) and the selection of cargo molecules. Also involved in autophagy.
Present with 358 molecules/cell in log phase SD medium.
Mitochondrial rhomboid serine protease processing the mitochondrial membrane fusion regulator MGM1, and the cytochrome c peroxidase (CCP1). Required for TIM11 stability, ATP synthase complex assembly, mitochondrial morphology, cytochrome c (CYC1) storage and mitochondrial genome maintenance.
Belongs to the ribulose-phosphate 3-epimerase family.
Binds 1 divalent metal cation per subunit. Active with Co(2+), Fe(2+), Mn(2+) and Zn(2+).
Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate (By similarity). Involved in the protective response to oxidative stress.
Present with 3310 molecules/cell in log phase SD medium.
May have a role in actin patch assembly.
Present with 1360 molecules/cell in log phase SD medium.
Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts with the ESCRT-0 subunit VPS27. Interacts with KEI1 (via C-terminal region).
Present with 15200 molecules/cell in log phase SD medium.
ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes. Has weak ATP-dependent affinity for dsRNA, but strong ATP-dependent affinity for ssRNA. Acts as a virus host factor involved in the replication of the MBV and the L-A viruses by promoting the negative-strand RNA synthesis. May be involved in recognition of the preinitiation complex and DNA binding of the RNA polymerase III and play a role in mRNA splicing.
Interacts with the L-A virus GAG protein and the whole L-A virus particles.
Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. 6-phosphogluconolactonase subfamily.
Lacks 6-phosphogluconolactonase activity.
May be involved in regulation of tRNA subcellular distribution.
Present with 1160 molecules/cell in log phase SD medium.
Belongs to the helicase family. Yeast subtelomeric Y' repeat subfamily.
Catalyzes DNA unwinding and is involved in telomerase-independent telomere maintenance.
Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family.
Interacts with MID1 to form a Ca(2+) influx channel.
Voltage-gated, high-affinity calcium channel involved in calcium influx in response to some environmental stresses as well as exposure to mating pheromones. Functions together with MID1 to ensure that adequate levels of Ca(2+) are supplied to PMR1 to sustain secretion and growth. Required for growth in low-calcium environments.
Present with 10300 molecules/cell in log phase SD medium.
Pyrophosphorylated by 5-diphosphoinositol pentakisphosphate (5-IP7) (PubMed:15604408). Serine pyrophosphorylation is achieved by Mg(2+)-dependent, but enzyme independent transfer of a beta-phosphate from a inositol pyrophosphate to a pre-phosphorylated serine residue (PubMed:15604408, PubMed:17873058).
Belongs to the V-ATPase proteolipid subunit family.
Proton-conducting pore forming of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:1837023, PubMed:9030535). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:1837023, PubMed:9030535).
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and VOA1) (PubMed:27776355, PubMed:29526695). The decameric c-ring forms the proton-conducting pore, and is composed of eight proteolipid subunits c, one subunit c' and one subunit c'' (PubMed:27776355, PubMed:29526695).
Belongs to the SEC23/SEC24 family. SEC24 subfamily.
COPII is composed of at least five proteins: the SEC23/24 complex, the SEC13/31 complex and SAR1. Interacts with GRH1.
Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex.
Present with 1720 molecules/cell in log phase SD medium.
Component of the TIM23 complex, at least composed of TIM23, TIM17, TIM50 and TIM21. Interacts directly with TIM23. Interacts with TOM22 component of the TOM complex. Released from the TOM23 complex by the PAM complex, leading to protein translocation into the mitochondrial matrix.
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Required to keep the TOM and the TIM23 complexes in close contact. At some point, it is released from the TOM23 complex to allow protein translocation into the mitochondrial matrix. In the complex, it acts as an antagonist of TIM50 by reducing preprotein accumulation at the TOM23 complex and promotes dissociation of the PAM complex from the TIM23 complex.
Present with 3770 molecules/cell in log phase SD medium.
Interacts with MIA40; forms mixed disulfide intermediates with MIA40.
Mitochondrial triacylglycerol (TAG) lipase with activity toward long-chain diacylglycerols (DAGs) and triacylglycerols (TAGs) (PubMed:9544243, PubMed:19959834). Involved in mitochondrial lipid metabolism (PubMed:31483742).
Belongs to the RNA polymerase beta chain family.
Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and RPC2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity).
Present with 1950 molecules/cell in log phase SD medium.
A double deletion of TGL3 and TGL4, the 2 major TGA lipases, leads to fat yeast, rendering growing cells unable to degrade triglycerides.
Lipid particle-localized triacylglycerol (TAG) lipase. The lipid droplet/particle is a lipid storage compartment which serves as a depot of energy and building blocks for membrane lipid biosynthesis. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs, releasing and supplying specific fatty acids to the appropriate metabolic pathways (PubMed:16135509, PubMed:16267052). Also has steryl ester (SE) hydrolase and phospholipase A(2) (PLA(2)) activities, and catalyzes the acylation of lysophosphatidic acid (LPA) (PubMed:20332534). Contributes to early bud formation in late G1 phase of the cell cycle upon phosphorylation and activation by cyclin-dependent kinase 1 (Cdk1/CDC28) (PubMed:19150427).
Phosphorylated and activated by cyclin-dependent kinase 1 (Cdk1/CDC28) (PubMed:19150427). Loses its lipolytic activity in cells lacking nonpolar lipids, but retains its side activity as lysophospholipid acyltransferase (PubMed:27170177).
Phosphorylation at Thr-675 and Ser-890 by Cdk1/CDC28 stimulates enzyme activity in vivo.
Present with 195 molecules/cell in log phase SD medium.
Leads to cold-sensitive growth and elongated buds. Is synthetic lethal with a MUD2 deletant.
Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
Participates in pre-mRNA splicing. Part of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome.
Present with 907 molecules/cell in log phase SD medium.
ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits (PubMed:2408148, PubMed:25579579). Binds 90S pre-ribosomal particles and dissociates from pre-60S ribosomal particles after processing of 27SB pre-rRNA (PubMed:21825077). Required for the normal formation of 18S rRNA through the processing of pre-rRNAs at sites A0, A1 and A2, and the normal formation of 25S and 5.8S rRNAs through the processing of pre-rRNAs at sites C1 and C2 (PubMed:9769101). Also required for recruitment of NOG2 to pre-ribosomes (PubMed:22735702).
Belongs to the DEAD box helicase family. DDX55/SPB4 subfamily.
Component of pre-60S ribosomal complexes.
Present with 5740 molecules/cell in log phase SD medium.
Belongs to the small heat shock protein (HSP20) family.
By heat shock, and under other conditions of stress, such as increased salt concentration and starvation.
Expressed during the entry into stationary phase resulting from glucose limitation.
Not known. One of the major polypeptides produced on heat shock.
Present with 19300 molecules/cell in log phase SD medium.
Expression is induced in response to alpha factor and regulated by the UME6 transcription factor.
Probable transcriptional activator involved in meiotic prophase and synaptonemal complex (SC) assembly.
Component of the spliceosome, where it is associated with snRNP U1. Binds stem loop I of U1 snRNA. Interacts with mRNA.
Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.
In TFIID, TAF10 heterodimerizes with TAF3 and TAF8. The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14. Component of the 1.8 MDa SAGA complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9.
Present with 3400 molecules/cell in log phase SD medium.
Acts as a mitochondrial iron-sulfur (Fe-S) cluster assembly factor that facilitates [4Fe-4S] cluster insertion into a subset of mitochondrial proteins such as lipoyl synthase (LS) and succinate dehydrogenase (SDH) (PubMed:27532773, PubMed:27532772). Required during the last step of iron-sulfur protein assembly when the iron-sulfur cluster is inserted into the target protein (PubMed:27532772). Acts together with NFU1, later than BOL1 and GRX5 in the [4Fe-4S] cluster insertion process (PubMed:27532773). Not required for [2Fe-2S] cluster insertion into mitochondrial proteins (PubMed:27532772).
Increases frequency of mitochondrial genome loss (PubMed:19300474). Cells show a slight decrease of succinate dehydrogenase (SDH) (PubMed:27532772). Cells lacking BOL1 and BOL3 display defects in a subset of mitochondrial [4Fe-4S] enzymes (PubMed:27532773, PubMed:27532772).
Present with 259 molecules/cell in log phase SD medium.
Component of the chromatin-remodeling INO80 complex, at least composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3, IES4, IES6, ACT1, IES2, IES5 and INO80.
Present with 2060 molecules/cell in log phase SD medium.
Significantly increases steady-state mitochondrial magnesium concentration (PubMed:25585246). Rescues the group II RNA splicing defect in the MRS2 and LPE10 deletion mutants (PubMed:25585246).
Transporter of the mitochondrial inner membrane that exports magnesium and thus, plays a key role in mitochondrial Mg(2+) homeostasis.
Belongs to the SF3B complex, a U2 associated sub-complex of the spliceosome. The SF3B complex is composed of at least CUS1, HSH49, HSH155, RDS3 and RSE1. Belongs also to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with RDS3.
Involved in G2/M transition (By similarity). Required for pre-mRNA splicing and endoplasmic reticulum (ER) to Golgi secretion pathway. U2 snRNPs associated protein required for the pre-spliceosome assembly. The involvement in ER to Golgi secretion is probably indirect and due to the splicing of the pre-mRNA coding for SAR1, a small GTP-binding protein required for COPII vesicle formation from the ER.
Induced by pheromone. Down-regulated by RIM101 and inositol.
Belongs to the threonine aldolase family.
Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde.
Present with 106000 molecules/cell in log phase SD medium.
Component of a complex at least composed of FAR3, FAR7, FAR8, FAR10, FAR11 and VPS64.
Participates in the control of the reentry into the cell cycle following pheromone treatment.
Regulates the coordinate transcription of structural MAL1S (maltase) and AGT1 (maltose permease) genes.
Cold-sensitive mutant KRR1-21 is a deletion of amino acids 234-239.
Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3. Interacts with snoRNA U3. Interacts with MPP10, KRI1 and with ribosomal proteins RPS1A, RPS4A, RPS4B, RPS8A, RPS8B, RPS11A, RPS11B, RPS13, RPS24, RPS25, RPL4A, RPL7B, RPL8, RPL23, RPL25 and RPL28.
Present with 4340 molecules/cell in log phase SD medium.
Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. Essential for vegetative growth.
Belongs to the ubiquitin-conjugating enzyme family.
Catalyzes the covalent attachment of ubiquitin to other proteins (PubMed:19920177, PubMed:2154373). Mediates the selective degradation of short-lived and abnormal proteins (PubMed:2154373). The RSP5-UBA1-UBC5 ubiquitin ligase complex ubiquitinates RPO21 forming 'Lys-63'-linked polyubiquitin chains (PubMed:19920177).
Component of the RSP5-UBA1-UBC5 ubiquitin ligase complex composed of E3 RSP5, E1 UBA1 and E2 UBC5.
Present with 981 molecules/cell in log phase SD medium.
Heterotetramer of ERG25, ERG26, ERG27 and ERG28. ERG28 acts as a scaffold to tether ERG27 and other 4,4-demethylation-related enzymes, forming a demethylation enzyme complex, in the endoplasmic reticulum.
Inhibited by FR171456, a natural product with broad antifungal activity.
Present with 2580 molecules/cell in log phase SD medium.
Sterol-4-alpha-carboxylate 3-dehydrogenase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:9811880, PubMed:15995173). ERG26 is a catalytic component of the C-4 demethylation complex that catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group (PubMed:9811880). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672).
Acetylation of histone H3 leads to transcriptional activation. H3K14ac formation by GCN5, a component of the SAGA complex, is promoted by H3S10ph. Further acetylated by GCN5 to form H3K9ac, H3K18ac, H3K23ac, H3K27ac and H3K36ac. H3K14ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. H3K56ac formation occurs predominantly in newly synthesized H3 molecules during G1, S and G2/M of the cell cycle and may be involved in DNA repair.
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. Together with SPT15/TBP, UAF seems to stimulate basal transcription to a fully activated level.
Crotonylation (Kcr) marks active promoters and enhancers and confers resistance to transcriptional repressors.
Mono-, di- and trimethylated by the COMPASS complex to form H3K4me1/2/3. H3K4me activates gene expression by regulating transcription elongation and plays a role in telomere length maintenance. H3K4me enrichment correlates with transcription levels, and occurs in a 5' to 3' gradient with H3K4me3 enrichment at the 5'-end of genes, shifting to H3K4me2 and then H3K4me1. Methylated by SET2 to form H3K36me. H3K36me represses gene expression. Methylated by DOT1 to form H3K79me. H3K79me is required for association of SIR proteins with telomeric regions and for telomeric silencing. The COMPASS-mediated formation of H3K4me2/3 and the DOT1-mediated formation of H3K79me require H2BK123ub1.
Phosphorylated by IPL1 to form H3S10ph in a cell cycle-dependent manner during mitosis and meiosis. H3S10ph is also formed by SNF1, promotes subsequent H3K14ac formation by GCN5, and is required for transcriptional activation through TBP recruitment to the promoters. Dephosphorylation is performed by GLC7.
Present with 213000 molecules/cell in log phase SD medium.
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Histone H3 is a component of the UAF (upstream activation factor) complex, which consists of UAF30, RRN5, RRN9, RRN10, and histones H3 and H4.
To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H3K4me1/2/3 = mono-, di- and trimethylated Lys-5; H3K9ac = acetylated Lys-10; H3K9me1 = monomethylated Lys-10; H3S10ph = phosphorylated Ser-11; H3K14ac = acetylated Lys-15; H3K14me2 = dimethylated Lys-15; H3K18ac = acetylated Lys-19; H3K18me1 = monomethylated Lys-19; H3K23ac = acetylated Lys-24; H3K23me1 = monomethylated Lys-24; H3K27ac = acetylated Lys-28; H3K27me1/2/3 = mono-, di- and trimethylated Lys-28; H3K36ac = acetylated Lys-37; H3K36me1/2/3 = mono-, di- and trimethylated Lys-37; H3K56ac = acetylated Lys-57; H3K64ac = acetylated Lys-65; H3K79me1/2/3 = mono-, di- and trimethylated Lys-80.
Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2.
Component of the TIM22 complex, whose core is composed of TIM18, TIM22 and TIM54, associated with the peripheral proteins MRS5/TIM12 and the 70 kDa heterohexamer composed of TIM9 and TIM10 (or TIM8 and TIM13).
Essential component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as external driving force. Its precise function within the TIM22 complex is unclear.
Alpha-glucosidase with broad substrate specificity for alpha-1,4- and alpha-1,6-glucosides. Not required for isomaltose utilization, but overexpression allows the IMA1 null mutant to grow on isomaltose.
Belongs to the glycosyl hydrolase 13 family.
Present with 166 molecules/cell in log phase SD medium.
Component of the SAC3-THP1 complex, which functions in transcription-coupled mRNA export from the nucleus to the cytoplasm. SAC3-THP1 functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket.
Heterodimer with THP1. The SAC3-THP1 complex interacts with CDC31 and SUS1, and with the mRNA export factor MEX67-MTR2, the TREX complex component SUB2, and the nucleoporin NUP1. SAC3 directly interacts with MEX67, NUP1 and SUB2.
Present with 339 molecules/cell in log phase SD medium.
Associates with the 60S ribosomal subunit of the 80S translational complex.
Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with zinc, cobalt, manganese or divalent iron ions. Has high activity with zinc; zinc cofactor is transferred into the active site region by the ZNG1 zinc chaperone.
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Plays the major role in N-terminal methionine removal. Less efficient when the second residue is Val.
In contract to the MetAP 2 isoform, is not inhibited by the fungal metabolite fumagillin, an antiangiogenic drug.
Present with 19600 molecules/cell in log phase SD medium.
The C6H2-type zinc finger recruits ZNG1, promoting zinc cofactor transfer in the peptidase domain of MAP1.
Component of a SNARE complex that may be the effector of SEC4 function in exocytosis.
Autophosphorylated as part of the catalytic cycle of phosphodiesterase/pyrophosphatase activity.
Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.
Mediates extracellular nucleotide derived phosphate hydrolysis along with NPP2 and PHO5.
Present with 3420 molecules/cell in log phase SD medium.
Up-regulated during phosphate starvation.
Involved, with RAD23 in spindle pole body duplication. Involved in the ubiquitin-proteasome proteolytic pathway.
Present with 3930 molecules/cell in log phase SD medium.
Acts as a DnaJ-like chaperone required for nuclear membrane fusion during mating.
Present with 3180 molecules/cell in log phase SD medium.
Induced during prophase I of meiosis. Requires protein kinase IME2 for initial expression and continued transcription during meiotic divisions. Can autoactivate its own synthesis.
Phosphorylated by pachytene checkpoint kinase IME2, but also phosphorylated in an IME2-independent manner. Phosphorylation probably eliminates SUM1-mediated repression and is also required for full transcriptional activation activity. Phosphorylation of the DNA-binding domain by IME2 does not alter DNA binding affinity.
Transcription factor required for successful completion of meiosis and spore formation. Gets activated after completion of meiotic recombination at the end of prophase I. Recognizes and binds to the middle sporulation element (MSE) 5'-C[AG]CAAA[AT]-3' in the promoter region of stage-specific genes that are required for progression through meiosis and sporulation. Competes for binding to MSE with the transcriptional repressor SUM1, which represses middle sporulation-specific genes during mitosis and early sporulation.
Component of the heterotrimeric kinetochore subcomplex CTF3, which consists of CTF3, MCM16 and MCM22 (PubMed:11782448). The CTF3 subcomplex is part of a larger constitutive centromere-associated network (CCAN) (also known as central kinetochore CTF19 complex in yeast), which is composed of at least AME1, CHL4, CNN1, CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1 (PubMed:12408861, PubMed:22561346). Interacts with CTF19 (PubMed:11782448).
Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Present with 279 molecules/cell in log phase SD medium.
Present with 2300 molecules/cell in log phase SD medium.
Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin-remodeling complex.
Belongs to the eukaryotic ribosomal protein eS7 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). eS7 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835).
Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). Interacts with snoRNA U3. uS11 interacts with MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3 (PubMed:15590835).
N-terminally acetylated by acetyltransferase NatA.
Present with 43500 molecules/cell in log phase SD medium.
Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway.
Present with 36500 molecules/cell in log phase SD medium.
The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein.
Belongs to the DHHC palmitoyltransferase family. AKR/ZDHHC17 subfamily.
It is uncertain whether Met-1 or Met-4 is the initiator.
May be involved in constitutive endocytosis of a-factor receptor STE3.
Present with 815 molecules/cell in log phase SD medium.
The DHHC domain is required for palmitoyltransferase activity.
Belongs to the amino acid-polyamine-organocation (APC) superfamily. YAT (TC 2.A.3.10) family.
Present with 688 molecules/cell in log phase SD medium.
High-copy suppressor of mutant alleles of ATP-dependent RNA helicase DBP5, which is involved in mRNA export from the nucleus. It may also play an important role in a late stage of NAB2-mRNA export.
Interacts with GLE1, NUP42, NAB2, ZDS1 and probably DBP5. Forms a complex with GLE1 and NAB2.
Present with 2733 molecules/cell in log phase SD medium.
Required for translation of the mitochondrial gene for cytochrome c oxidase subunit II (COX2).
Belongs to the BUR kinase complex composed of SGV1/BUR1 and BUR2. Interacts with SGV1.
Component of the BUR kinase complex involved in transcription regulation. This complex phosphorylates 'Ser-120' of the UBC2/RAD6 ubiquitin-conjugating enzyme (E2), leading to monoubiquitination of histone H2B, the localization of the PAF1 complex to the chromatin, and the silencing of telomeric-associated genes. Also required for histone H3 'Lys-4' trimethylation. May phosphorylate the 'Ser-5' of the RBP1 carboxy-terminal domain (CTD) repeats. Necessary for the recovery from pheromone-induced growth arrest in the cell cycle G1 phase. Also required for vegetative growth itself. The kinase activity of the complex requires the presence of BUR2. Overexpression of BUR2 interferes with mitotic chromosome segregation.
Present with 2910 molecules/cell in log phase SD medium.
Expressed periodically during cell division. Requires ACE2, CBK1, MOB2 and SWI5.
May be involved in the establishment of the daughter fate.
Present with 922 molecules/cell in log phase SD medium.
Belongs to the DEAD box helicase family. DEAH subfamily.
Interacts directly with pre-mRNA. According to PubMed:2251118, associated with spliceosomes prior to and throughout step 1 of the splicing reaction. According to PubMed:8943336, it leaves the spliceosome before reaction 1. Interacts with SPP2.
Involved in pre-mRNA splicing. Is required together with ATP and at least one other factor, for the first cleavage-ligation reaction. Functions as a molecular motor in the activation of the precatalytic spliceosome for the first transesterification reaction of pre-mRNA splicing by hydrolyzing ATP to cause the activation of the spliceosome without the occurrence of splicing. Capable of hydrolyzing nucleoside triphosphates in the presence of single-stranded RNAs such as poly(U).
Present with 172 molecules/cell in log phase SD medium.
Interacts with COX1, COX14, MSS51 and SHY1.
Present with 1680 molecules/cell in log phase SD medium.
Required for efficient assembly of cytochrome c oxidase in the mitochondrial inner membrane. Involved in a step coupling MSS51-dependent cotranslational insertion of COX1 to the addition of its heme A and copper B cofactors.
DNA-binding component of a FANCM-MHF complex involved in DNA damage repair and genome maintenance (PubMed:20347428). FANCM-MHF promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork (By similarity). Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly (PubMed:22561346).
The MHF histone-fold complex is a heterotetramer of 2 MHF1-MHF2 heterodimers. Together with MPH1/FANCM, forms the FANCM-MHF complex (PubMed:22325783). Component of the inner kinetochore constitutive centromere-associated network (CCAN) (also known as central kinetochore CTF19 complex in yeast), which is composed of at least AME1, CHL4, CNN1, CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1 (Probable).
Component of the 19S cap proteasome complex composed of at least RPN1, RPN2, RPN3, RPN4, RPN5, RPN6, RPN7, RPN8, RPN9, RPN10, RPN11, RPN12, RPN13, RPT1, RPT2, RPT3, RPT4, RPT5, and RPT6. The 19S subcomplex associates with the 20S proteasome subcomplex to form the functional 26S proteasome.
Component of the 19S cap proteasome complex which acts as a regulatory subunit of the 26S proteasome, involved in the ATP-dependent degradation of ubiquitinated proteins.
Present with 12200 molecules/cell in log phase SD medium.
Belongs to the actin-binding proteins ADF family.
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton. In effect, yeast cofilin increases the rate of actin polymerization by making new ends available for actin subunit addition. Such a protein complex is important for the polarized growth of yeast cells.
Interacts with actin and AIP1 in a ternary complex.
Interacts with NAP1 (via the central domain consisting of amino acids 143 to 362). Copurifies with ribosomes.
Present with 6490 molecules/cell in log phase SD medium.
Acetylation at Lys-112 and Lys-113 by ECO1 is important for genome stability and S phase sister chromatid cohesion.
Belongs to the SMC family. SMC3 subfamily.
Cohesin complexes are composed of the SMC1 and SMC3 heterodimer attached via their SMC hinge domain, MCD1/SCC1 which link them, and IRR1/SCC3, which interacts with MCD1. The cohesin complex also interacts with SCC2, which is required for its association with chromosomes.
Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate.
Present with 2660 molecules/cell in log phase SD medium.
The flexible SMC hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC1, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable MCD1 protein, forming a ring structure (By similarity).
Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family.
Present with 623 molecules/cell in log phase SD medium.
May play a role in the regulation of membrane traffic through the trans-Golgi network.
Present with 2270 molecules/cell in log phase SD medium.
Present with 11400 molecules/cell in log phase SD medium.
Responsible for addition of first and second mannose residues to the outer chain of core N-linked polysaccharides and to O-linked mannotriose. Implicated in late Golgi modifications.
Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Homotetramer. Seems to be able to form heterotetramers composed from more than 1 of the 3 IMPDH gene products (IMD2-4).
Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.
Present with 2970 molecules/cell in log phase SD medium.
Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.
Binds to histones H3 and H4 (PubMed:16959570). Interacts with NOP53.
PPIase that acts as a histone chaperone (PubMed:14981505, PubMed:16846601). Histone proline isomerase that increases the rate of cis-trans isomerization at 'Pro-17' (H3P16), 'Pro-31' (H3P30) and 'Pro-39 (H3P38) on the histone H3 N-terminal tail (PubMed:16959570, PubMed:23888048). H3P16 and H3P30 are the major proline targets with little activity shown against H3P38 (PubMed:23888048). H3P38 isomerization influences SET2-mediated H3K36 methylation thereby regulating gene expression (PubMed:16959570).
Present with 14100 molecules/cell in log phase SD medium.
Belongs to the Mediator complex subunit 19 family.
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.
Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins.
Present with 6116 molecules/cell in log phase SD medium.
According to PubMed:12973301, colocalizes with nascent proteasome. According to PubMed:15778719, associates with proteasome core particles and also forms a complex with regulatory particle-core particle (RP-CP).
Associated component of the proteasome that specifically recognizes acetylated histones and promotes ATP- and ubiquitin-independent degradation of core histones during DNA damage response. Recognizes and binds acetylated histones via its bromodomain-like (BRDL) region and activates the proteasome by opening the gated channel for substrate entry. Binds to the core proteasome via its C-terminus, which occupies the same binding sites as the proteasomal ATPases, opening the closed structure of the proteasome via an active gating mechanism. Involved in DNA damage response in somatic cells: binds to acetylated histones and promotes degradation of histones following DNA double-strand breaks.
Present with 2600 molecules/cell in log phase SD medium.
The YYX motif is required for the association with the proteasome.
The bromodomain-like (BRDL) region specifically recognizes and binds acetylated histones.
Present with 1550 molecules/cell in log phase SD medium.
Was originally thought to be a mitochondrial ribosomal protein.
Plays a direct or indirect role in pre-rRNA processing.
Present with 2100 molecules/cell in log phase SD medium.
Belongs to the 5'-AMP-activated protein kinase beta subunit family.
Beta subunit of the SNF1 kinase complex, which is required for transcriptional, metabolic, and developmental adaptations in response to glucose limitation. Has a structural role, mediating heterotrimer formation, and a regulatory role, defining carbon source-regulated subcellular location and substrate specificity of the SNF1 kinase complex. Promotes the relocalization of the SNF1 kinase complex to the nucleus upon shift to nonfermentable carbon sources.
Component of the SNF1 kinase complex, a heterotrimeric complex composed of the catalytic alpha subunit SNF1, one of the three related beta subunits SIP1, SIP2 or GAL83, and the regulatory gamma subunit SNF4. The beta subunit serves as a bridge between the catalytic and the regulatory subunit. Interacts (via KIS domain) with SNF1. Interacts (via ASC domain) with SNF4. Interacts with REE1.
Present with 3590 molecules/cell in log phase SD medium.
Negatively regulates telomere length by preventing telomere elongation or promoting degradation of the telomere ends. Recruited to telomeres by interaction with the C-terminus of RAP1, which binds directly to telomeric repeat DNA. This may create a negative feedback loop in which the addition of new telomere repeats creates binding sites for inhibitors of telomere length extension. May also influence the balance of transcriptional silencing at telomeres and the silent mating type locus HMR, which is mediated by SIR (Silent Information Regulator) proteins including SIR3 and SIR4. RIF1 competes with SIR proteins for binding to the C-terminus of RAP1. In the absence of RIF1, a limiting cellular pool of SIR proteins may preferentially associate with RAP1 at sub-telomeric loci, causing enhanced telomeric silencing and attenuated silencing of the HMR locus.
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.
The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily.
Interacts with YNR048W/CRF1; interaction is required for proper expression and endoplasmic reticulum (ER) export of either partner.
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids (Probable). Forms a heteromeric phospholipid translocase (PLT) DNF3-CRF1, implicated in the translocation of phospholipids from the outer to the inner leaflet of membrane bilayers. Shares an essential function for cell growth with PLTs DRS2-CDC50 and DNF1/2-LEM3. May be involved in transport from early endosomes to the trans-Golgi network (TGN) (Probable).
Activity enhanced by Mg(2+) ion but inhibited by Ca(2+), Zn(2+) and Be(2+) ions. Inorganic phosphate and ATP are competitive inhibitors, whereas pyrophosphate and AMP have no effect.
PHO13 is dispensable for vegetative growth and sporulation.
Present with 2980 molecules/cell in log phase SD medium.
Component of the CBC complex, which binds co-transcriptionally to the cap of pre-mRNAs and is involved in maturation, export and degradation of nuclear mRNAs. The CBC complex is required for efficient pre-mRNA splicing through efficient commitment complex and spliceosome formation. Together with NPL3, the CBC complex is required for export of mRNAs out of the nucleus. The CBC complex is also involved in nuclear mRNA degradation, probably by directing the mRNAs to the sites of degradation. Affects replication of the positive-strand RNA virus BMV.
Component of the nuclear cap-binding complex (CBC), a heterodimer composed of STO1/CBC1 and CBC2 that interacts with capped RNAs. The complex interacts strongly with the importin subunit alpha SRP1. The SRP1-CBC trimer also binds to capped RNAs, but formation of the importin alpha/beta heterodimer upon binding of KAP95 to SRP1 in the cytoplasm causes dissociation of CBC from the RNA. The CBC complex is part of the commitment complex 1 (CC1), binding to the cap of pre-mRNA and interacting with U1 snRNP subunits MUD2 and SNU56. The CBC complex is part of the NRD1 complex, composed of CBC2, NAB1, NRD1, SEN1 and STO1/CBC2. The CBC complex also interacts with NPL3 and eIF4G (TIF4631 and TIF4632).
In contrast to metazoans, where the CBC complex is involved in the nuclear export of capped U snRNAs, it is believed that in yeast, U snRNAs are not exported from the nucleus and U snRNPs are assembled in the nucleus from RNAs and imported proteins.
Present with 6200 molecules/cell in log phase SD medium.
Belongs to the mitochondrial Rho GTPase family.
Collapsed, globular, or grape-like mitochondria.
Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution (Probable).
Belongs to the cyclin family. Cyclin AB subfamily.
Essential for the control of the cell cycle at the G2/M (mitosis) transition. Interacts with the CDC2 protein kinase to form MPF. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis.
Maximally expressed before mitosis. The levels peak late in the G2 phase of the cell cycle and are at a minimum in G1 phase.
Present with 300 molecules/cell in log phase SD medium.
Belongs to the glycosyl hydrolase 72 family.
Present with 16400 molecules/cell in log phase SD medium.
Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall biosynthesis and morphogenesis (By similarity).
The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
According to PubMed:9512348, it is a component of the 26S proteasome.
Acts as a transcriptional activator of a number of genes encoding proteasomal subunits. Binds to a PACE (proteasome-associated control element) DNA sequence 5'-GGTGGCAAA-3'. Its expression is in turn regulated by the 26S proteasome, thereby providing a negative feedback control mechanism. Required for normal growth at low temperatures.
Mutants grow slowly at low temperatures and show partial mislocalization of nuclear antigens.
Probably interacts with SEC63. Interacts with MUB1, UBR2 and RPN2.
Ubiquitinated by UBR2 in the presence of UBC2; which leads to proteasomal degradation.
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer (PubMed:2941152). Required for mitotic division septum formation during adverse conditions (PubMed:2523889).
Belongs to the pyridoxamine 5'-phosphate oxidase family.
Belongs to the type IA topoisomerase family.
Forms a complex with SGS1 and RMI1. Interacts with SGS1.
Present with 468 molecules/cell in log phase SD medium.
Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand than undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Essential for proper chromosome segregation in both meiosis and mitosis. Weakly relaxes negative supercoils and displays a distinct preference for binding single-stranded DNA. The TOP3-SGS1 protein complex may function as a eukaryotic reverse gyrase introducing positive supercoils into extrachromosomal ribosomal DNA rings.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily.
Phosphorylated by PKA in a TORC1-dependent manner. Phosphorylation at PKA consensus sites RRxS/T decreases upon rapamycin treatment.
Present with 1270 molecules/cell in log phase SD medium.
Belongs to the G-protein coupled receptor GPR1/git3 family.
Seems to associate with GPA2 and act as G protein-coupled receptor that senses glucose and controls filamentous growth. It acts upstream of adenylate cyclase and is required for glucose activation of cAMP synthesis in concert with a glucose phosphorylation-dependent mechanism.
Heterohexamer; composed of 3 copies of TIM9 and 3 copies of TIM10, named soluble 70 kDa complex. Associates with the TIM12 component of the TIM22 complex, whose core is composed of TIM18, TIM22 and TIM54. Interacts with the transmembrane regions of multi-pass transmembrane proteins in transit.
Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. Compared to TIM10, it may have a strong structural role.
The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIM9 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (Probable).
Interacts with the E2 ubiquitin-conjugating enzyme UBC4 and histones H3 and H4.
Present with 1960 molecules/cell in log phase SD medium.
Probable ubiquitin-protein ligase involved in the degradation-related ubiquitination of histones. Contributes to the post-translational regulation of histone protein levels by polyubiquitination of excess histones for subsequent degradation.
Conjugated to ATG12; which is essential for autophagy. Conjugation with ATG12 involves ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme.
Conjugated with ATG12. The ATG5-ATG12 conjugate forms a complex with several units of ATG16. The ATG12-ATG5 conjugate associates also with ATG3.
Involved in cytoplasm to vacuole transport (Cvt) and autophagic vesicle formation. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy). Also required for mitophagy, which eliminates defective or superfluous mitochondria in order to fulfill cellular energy requirements and prevent excess ROS production. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes. ATG12-ATG5 rearranges the ATG3 catalytic center and enhances its E2 activity. Plays a role in the regulation of filamentous growth and chronological longevity.
Present with 606 molecules/cell in log phase SD medium.
Small amount of ATG5-ATG12 conjugate is enough to perform normal autophagy.
Belongs to the eukaryotic ribosomal protein eL20 family.
Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). eL20 forms multiple interactions with RNA and proteins in the central protuberance, connecting components of core functional centers that are locatzed far apart (PubMed:9559554, PubMed:22096102).
Present with 54300 molecules/cell in log phase SD medium.
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. SUS1 associates with the SAC3-THP1 complex. Component of the SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9. Component of the ADA/GCN5 complex that consists of HFI1/ADA1, ADA2, ADA3, SPT20/ADA5 and GCN5 and is probably a subcomplex of SAGA.
Present with 4150 molecules/cell in log phase SD medium.
Transcription regulator. May recruit TATA binding protein (TBP) and possibly other basal factors to bind to the TATA box. Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.
Component of the YIP1-YIF1 complex, composed of at least YIF1, YIP1 and YOS1.
Required for protein transport between endoplasmic reticulum and Golgi apparatus.
GTPase-activating protein (GAP) for the ADP ribosylation factors ARF1 and ARF2. May be involved in the endocytic pathway.
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. NIM1 subfamily.
Present with 1630 molecules/cell in log phase SD medium.
The M-Pol I and M-Pol II complexes possess alpha-1,6-mannosyltransferase activity and are probably involved in the elongation of the mannan backbone of N-linked glycans on cell wall and periplasmic proteins. May also provide alpha-1,2-mannosyltransferase activity to the M-Pol I complex.
The M-Pol I complex contains MNN9 and VAN1. The M-Pol II complex is composed of ANP1, MNN9, MNN10, MNN11 and HOC1.
Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia.
Leads to a clear growth defect on medium containing cysteine or glutathione as sole sulfur source.
Present with 2070 molecules/cell in log phase SD medium.
ATP-dependent RNA helicase required for the 3'-end formation of 5.8S RNA. Cofactor for the exosome complex that unwinds secondary structure in pre-rRNA. Required for nucleocytoplasmic transport of mRNA. May serve as a chaperone which translocates or normalizes the structure of mRNAs in preparation for export. Component of the TRAMP complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates.
Belongs to the helicase family. SKI2 subfamily.
Component of the TRAMP complex (also called TRF4 complex) composed of at least HUL4, MTR4, PAP2/TRF4 and either AIR1 or AIR2.
Present with 12500 molecules/cell in log phase SD medium.
Belongs to the SMC family. SMC1 subfamily.
Present with 5710 molecules/cell in log phase SD medium.
The flexible SMC hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC3, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable MCD1 protein, forming a ring structure.
May be involved in the modulation of rDNA transcription.
Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks.
Component of the Smc5-Smc6 complex which consists of KRE29, MMS21, NSE1, NSE3, NSE4, NSE5, SMC5 and SMC6. Interacts with SMC5 and SMC6. Interacts with NSE3.
Co-chaperone required for the assembly of iron-sulfur (Fe/S) clusters in mitochondria. Stimulates the ATPase activity of its specialized Hsp70 chaperone partner SSQ1, to mediate the transfer of iron-sulfur clusters from ISU1 to GRX5. Binds to the substrate protein ISU1 and targets it to SSQ1.
Increases association between GRX5 and SSQ1 (PubMed:23615440). Inviable vegetative cell population growth (PubMed:26545917).
Present with 2010 molecules/cell in log phase SD medium.
Belongs to the class VI-like SAM-binding methyltransferase superfamily. Isoprenylcysteine carboxyl methyltransferase family.
Mediates C-terminal methylation of the isoprenylated C-terminal cysteine in A-factor mating pheromone and Ras proteins (PubMed:8289819, PubMed:11451995, PubMed:15611058). Does not have a preference for the farnesyl or geranylgeranyl moieties in the model substrates N-acetyl-S-farnesyl-L-cysteine (AFC) and N-acetyl-S-geranylgeranyl-L-cysteine (AGGC) in vitro (PubMed:15611058).
Present with 2690 molecules/cell in log phase SD medium.
Belongs to the carbon-nitrogen hydrolase superfamily.
Deamidates N-terminal Asn and Gln. Component of a targeting complex in the N-end rule pathway.
It is uncertain whether Met-1 or Met-11 is the initiator.
Present with 1640 molecules/cell in log phase SD medium.
Belongs to the small GTPase superfamily. Ran family.
Found in a nuclear export complex with RanGTP, exportin and pre-miRNA (By similarity).
GSP2 expression exhibits carbon source dependency.
GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Not essential for cell viability.
Present with 2460 molecules/cell in log phase SD medium.
Belongs to the chaperonin (HSP60) family.
Chaperone. Required for the assembly of succinate dehydrogenase subunits. Ensures mitochondrial gene expression at elevated temperatures and prevents heat-aggregation of the ribosomal subunit VAR1.
Forms a high molecular mass protein complex of approximately 850 kDa.
Phosphorylated by CDC28, which is required for the early mitotic activity of the APC/C in its CDC20-bound form.
Present with 593 molecules/cell in log phase SD medium.
Belongs to the class V-like SAM-binding methyltransferase superfamily. RKM2 family.
Present with 768 molecules/cell in log phase SD medium.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that trimethylates 60S ribosomal protein L12 (RPL12A and RPL12B) at 'Lys-4' and 'Lys-11'.
Aminopeptidase which cleaves preprotein intermediates that carry destabilizing N-ter amino acid residues after the mitochondrial processing peptidase (MPP) cleavage site and is thus critical for stabilization of the mitochondrial proteome.
Present with 5080 molecules/cell in log phase SD medium.
As accessory component of the DNA polymerase epsilon (DNA polymerase II) participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair. Also functions as component of the ISW2 complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW2 complex is involved in coordinating transcriptional repression and in inheritance of telomeric silencing. It is involved in repression of MAT a-specific genes, INO1, and early meiotic genes during mitotic growth dependent upon transcription factor UME6 and in a parallel pathway to the RPD3-SIN3 histone deacetylase complex.
DNA polymerase epsilon is a heterotetramer consisting of POL2, DPB2, DPB3 and DPB4. Component of the ISW2 complex, which at least consists of ISW2, ITC1, DLS1 and DPB4.
In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.
May be involved in the polarity establishment process. Suppresses the lethality of KEX2-GAS1 double null mutant when overexpressed.
Belongs to the major facilitator superfamily.
Belongs to the pseudouridine synthase TruD family.
Catalyzes pseudouridylation at position 35 in U2 snRNA stem-loop II region which induces particular conformation of the mRNA-U2 snRNA duplex and places the nucleophile in an accessible position for the first step of splicing (PubMed:12426583, PubMed:12682021, PubMed:15611063, PubMed:18435545, PubMed:19114708, PubMed:25219674). Also catalyzes pseudouridylation at position 56 in U2 snRNA (PubMed:21131909). Catalyzes also pseudouridylation at position 50 in 5S rRNA, position 13 in cytoplasmic tRNAs, and position 35 in pre-tRNA(Tyr) (PubMed:14561887, PubMed:18332121, PubMed:25219674, PubMed:35058356). Pseudouridine residues in tRNAs may stabilize the local RNA conformation, favor interactions with protein partners and play an important role in the stabilization of the codon-anticodon interaction with mRNA (PubMed:14561887). Also catalyzes pseudouridylation of mRNAs in response to heat shock: mediates pseudouridylation of mRNAs with the consensus sequence 5'-UGUAR-3' (PubMed:25219674, PubMed:35058356).
Decreased level of pseudouridylated mRNAs.
Interacts with PEX7 (PubMed:12167700, PubMed:9864360, PubMed:23812376, PubMed:11606420). Interacts with PEX13 (PubMed:12167700). Interacts with SES1 (PubMed:12204379, PubMed:17451428).
Monoubiquitinated at Cys-5; acts as a signal for PEX21 extraction and is required for proper export from peroxisomes and recycling.
Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal via its interaction with PEX7 (PubMed:12167700, PubMed:9864360, PubMed:23812376). Interaction with PEX7 only takes place when PEX7 is associated with cargo proteins containing a PTS2 peroxisomal targeting signal (By similarity). PEX7 along with PTS2-containing cargo proteins are then translocated through the PEX13-PEX14 docking complex together with PEX21 (PubMed:23812376). Acts as an activator of the seryl-tRNA synthetase SES1 by increasing its binding to tRNA (PubMed:12204379, PubMed:17451428).
Impairs growth on glycerol carbon source.
Involved in nuclear control of mitochondria.
Present with 2280 molecules/cell in log phase SD medium.
Present with 1140 molecules/cell in log phase SD medium.
Expressed specifically in daughter cells through activation by the transcription factor ACE2. STE12 represses expression of the full-length transcript and induces expression of the short form. STE12-binding to pheromone response elements (PREs) at positions -175 and -161 prevents SPT15 from binding TATA-box 1 and thus it binds TATA-box 2 at position +385 and directs internal transcription initiation at position +452.
The full-length isoform (isoform Long) is a daughter cell-specific cell wall protein required for efficient export of lipids such as acetylated sterols. Acts in detoxification of hydrophobic compounds. Involved in tolerance to organic solvents such as dimethyl sulfoxide (DMSO). Also plays a role as an inhibitor of mating. STE12 is utilized as a repressor of full-length PRY3 transcription, ensuring efficient mating.
There is no evidence that production of the short PRY3 transcript (isoform Short) is anything more than an adventitious by-product of the mechanism responsible for the repression of the full-length transcript. Moreover, no disadvantage is detectable for cells unable to make the short transcript (PubMed:16940175).
May control the production of phosphatidylinositol 4-phosphate (PI4P) by the STT4 PI 4-kinase. Mediates proper localization of STT4 to the plasma membrane.
Originally MSC1 was identified in a screen for mutants that show an increase in meiotic unequal sister-chromatid recombination (SCR).
Present with 1070 molecules/cell in log phase SD medium.
Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily.
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Heterooctamer of 4 alpha and 4 beta chains.
Present with 90200 molecules/cell in log phase SD medium.
Belongs to the glutathione peroxidase family.
By oxidative stress, dependent on transcription factor YAP1 (PubMed:10480913). By oleic acid (PubMed:21763276).
Glutathione peroxidase-like protein that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress (PubMed:10480913, PubMed:11445588). Plays an important role in the oxidative stress-induced response in the presence of Ca(2+). Has peroxidase activity using preferentially thioredoxin as a reducing power. The redox state of the mitochondrial GPX2 is regulated by TRX1 and TRX2 (cytoplasmic thioredoxin), and by TRX3 (mitochondrial matrix thioredoxin) (PubMed:16251189). Involved in sporulation (PubMed:21763276).
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide.
Was originally thought to be a glutathione peroxidase (PubMed:10480913) or a phospholipid hydroperoxide glutathione peroxidase (PubMed:11445588), but functions as an atypical 2-Cys peroxiredoxin using thioredoxin as reducing power instead (PubMed:16251189).
Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks with regressed leading strands and nicked Holliday junctions. Cleavage probably occurs approximately half a helical turn upstream of the free 5'-end in these structures. May be required in mitosis for the processing of stalled replication fork intermediates arising spontaneously or subsequent to treatment with DNA damaging agents such as methylmethane sulfonate (MMS), camptothecin (CPT) or UV. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI). This involves consecutive cleavage of D-loops and nicked Holliday junctions leading to sister chromatid crossover. In contrast to MSH4-MSH5 dependent crossover, double Holliday junctions do not seem to be involved. Spore formation and viability are severely impaired in deletion strains.
Two distinct classes of meiotic crossovers have been demonstrated in budding yeast. Class I crossovers exhibit crossover interference and require MSH4 and MSH5 for their resolution, while class II crossovers exhibit no crossover interference and require MUS81 and MMS4. While class I crossovers represent the majority of crossovers in S.cerevisiae, they are virtually absent in S.pombe which lacks orthologs of MSH4 and MSH5.
Cells are viable and do not display any phenotype.
Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Contributes to growth on fatty acids.
Belongs to the C/M/P thioester hydrolase family.
Belongs to the MIP/aquaporin (TC 1.A.8) family.
Could be the product of a pseudogene. This is the C-terminal part of aquaporin-2. In strain S288c and many laboratory strains, a natural 11 bp deletion in position 109 leads to a frameshift, which disrupts the gene coding for this protein and produces two ORFs YLL052C and YLL053C. A contiguous sequence for aquaporin-2 can be found in strain Sigma 1278B (AC P0CD89).
GTPase-activating protein which accelerates the GTP hydrolysis rate of YPT1 and SEC4. Involved in ER to Golgi trafficking and polarized exocytosis.
Interacts with GYL1 and RVS167; and is part of SEC4-containing complexes.
Involved in DNA replication and cell separation during budding.
Present with 2840 molecules/cell in log phase SD medium.
May be involved in membrane protein folding (PubMed:19325107). Required for localization of MPS3 to the nuclear envelope (PubMed:23275891).
Present with 3250 molecules/cell in log phase SD medium.
Present with 7950 molecules/cell in log phase SD medium.
RNA-binding protein that binds specific categories of mRNAs, including those that contain upstream open reading frames (uORFs) and internal ribosome entry sites (IRES). Probably involved in translational regulation.
Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription.
Present with 1900 molecules/cell in log phase SD medium.
TAF4 heterodimerizes with TAF12, forming ultimately an octamer consisting of a TAF6/TAF9 heterotetramer core flanked by TAF4/TAF12 dimers on either side, similar to the histone H2A/H2B/H3/H4 octamer. The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14.
Open reading frame exhibits genomic organization compatible with a translational readthrough-dependent mode of expression.
Has phosphatidylinositol transfer activity. Involved in the regulation of the phospholipid composition of plasma- and endomembranes. Altering plasma membrane composition may provide a possible mechanism for multidrug resistance. Contributes to efficient phospholipase D1 activation and phospholipase B1 inhibition in the regulation of phospholipid turnover. Forms a complex with phosphatidylserine decarboxylase PSD2 that seems essential for maintenance of vacuolar phosphatidylethanolamine (PE) levels (PubMed:20016005).
Interacts with phosphatidylserine decarboxylase PSD2.
Present with 5040 molecules/cell in log phase SD medium.
Belongs to the universal ribosomal protein uL6 family.
Present with 76000 molecules/cell in log phase SD medium.
Required for respiratory growth, stability of the mitochondrial genome and for proper assembly or maintenance of mitochondrial proteins.
Component of the SKI complex composed of at least SKI2, SKI3 and SKI8. The SKI complex interacts with SKI7, which makes the link between the SKI complex and the exosome in order to perform mRNA degradation.
Component of the SKI complex involved in 3'-mRNA degradation pathway. Represses dsRNA virus propagation by specifically blocking translation of viral mRNAs, perhaps recognizing the absence of CAP or poly(A). Essential for cell growth only in the presence of M1 replicon.
Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).
Present with 5770 molecules/cell in log phase SD medium.
Required for formation of the 2-thio group of the 5-methoxycarbonylmethyl-2-thiouridine modified base in some tRNAs.
By the alkylating agent methyl methanesulfonate (MMS).
Interacts with ribosome biogenesis factors ARC1, CKA2 and GUS1.
Present with 861 molecules/cell in log phase SD medium.
Probable serine/threonine-protein kinase that may be involved in ribosome biogenesis.
Belongs to the V-ATPase 116 kDa subunit family.
Present with 55714 molecules/cell in log phase SD medium.
Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:1491220, PubMed:8798414, PubMed:11278748). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:1491220, PubMed:11278748). Is present only in vacuolar V-ATPase complexes; enzymes containing this subunit have a 4-fold higher ratio of proton transport to ATP hydrolysis than complexes containing the Golgi/endosomal isoform and undergo reversible dissociation of V1 and V0 in response to glucose depletion (PubMed:8798414, PubMed:11278748).
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and VOA1).
Component of the ER-mitochondria encounter structure (ERMES) or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34. Associates with the mitochondrial outer membrane sorting assembly machinery SAM(core) complex, which consists of SAM35, SAM37 and SAM50, to form a SAM(holo) complex.
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the TOM40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of TOM40 with the receptor TOM22 and small TOM proteins. Can associate with the SAM(core) complex as well as the MDM12-MMM1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the TOM40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Belongs to the protein kinase superfamily. ADCK protein kinase family.
Present with 2470 molecules/cell in log phase SD medium.
Involved in middle stages of meiosis. Redundant with SPS22 for the organization of the beta-glucan layer of the spore wall.
Present with 238 molecules/cell in log phase SD medium.
Binds to the SH3 domains of the type I myosins MYO3 and MYO5.
Involved in the regulation of actin cytoskeleton.
Belongs to the DASH complex SPC34 family.
Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. The DASH ring complex may both stabilize microtubules during chromosome attachment in anaphase A, and allow the chromosome to remain attached to the depolymerizing microtubule in anaphase B. Microtubule depolymerization proceeds by protofilament splaying and induces the kinetochore-attached ring to slide longitudinally, thereby helping to transduce depolymerization energy into pulling forces to disjoin chromatids.
The DASH complex is an approximately 210 kDa heterodecamer, which consists of ASK1, DAD1, DAD2, DAD3, DAD4, DAM1, DUO1, HSK3, SPC19 and SPC34, with an apparent stoichiometry of one copy of each subunit. DASH oligomerizes into a 50 nm ring composed of about 16 molecules that encircles the microtubule. Integrity of the complex and interactions with central kinetochore proteins are regulated by the spindle assembly checkpoint kinase IPL1.
Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily.
Expressed exclusively during sporulation (at protein level).
Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in spore wall assembly.
Belongs to the acetyltransferase family. NAA40 subfamily.
N-alpha-acetyltransferase that specifically mediates the acetylation of the N-terminal residues of histones H4 and H2A.
Belongs to the small GTPase superfamily. Rho family. CDC42 subfamily.
Interacts with BEM4; the interaction is direct (PubMed:8754839). Interacts with AXL2 (PubMed:17460121). Interacts with RGA1 (PubMed:7498791).
Involved in development of cell polarity during the cell division cycle, and essential for bud emergence. Affects signaling in the pheromone-response pathway through the STE20 protein kinase. Negatively regulated by the GTPase-activating proteins RGA1, BEM3, and BEM4.
Interacts with CDC48; the interaction is likely to result in CDC5 degradation.
Present with 556 molecules/cell in log phase SD medium.
Required for anaphase spindle elongation.
AAA-cassette D1 is required for interaction with PEX6. ATP-binding in AAA-cassette D2 is required for interaction with PEX6. ATP-binding and hydrolysis in AAA-cassette D2 is required for proper function in PEX5 dislocation.
Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling (PubMed:15634331, PubMed:16007078, PubMed:16911527, PubMed:26170309, PubMed:26066397, PubMed:29321502). Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel (PubMed:26170309, PubMed:26066397, PubMed:29321502). Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5 (PubMed:29321502).
Interacts with PEX6; forming the PEX1-PEX6 AAA ATPase complex, which is composed of a heterohexamer formed by a trimer of PEX1-PEX6 dimers (PubMed:15634331, PubMed:16007078, PubMed:26170309, PubMed:26066397, PubMed:29321502). The PEX1-PEX6 heterooligomers associate with the peroxisomal importomer via interaction of PEX6 with the peroxisomal membrane anchor PEX15 (PubMed:16911527).
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. In yeast, the dimeric form of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta, epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j and k.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity).
Component of the 90S and 60S pre-ribosomal particles.
Involved in ribosome biogenesis and cell polarity. Required for the synthesis of both 40S and 60S ribosomal subunits and may also play some direct role in correct positioning of the mitotic spindle during mitosis.
Component of the PAF1 complex which consists of at least CDC73, CTR9, LEO1, PAF1 and RTF1.
Present with 1110 molecules/cell in log phase SD medium.
The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2.
Between 15 and 30 minutes due to fermentation progress.
Is probably involved in a pathway contributing to genomic integrity.
Present with 4280 molecules/cell in log phase SD medium.
By pheromones during mating, through the regulation by the STE12 transcription factor. Also induced in respiratory-deficient cells.
Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
Activates endogenous long-chain fatty acids (LCFA) by esterification of the fatty acids into metabolically active CoA-thioesters for subsequent degradation or incorporation into phospholipids (PubMed:8206942). Acts preferentially on C16 and C18 fatty acids with a cis-double bond at C-9-C-10 (PubMed:8206942).
Belongs to the ATP-dependent AMP-binding enzyme family.
Present with 6440 molecules/cell in log phase SD medium.
The FACS motif is required for catalytic activity and substrate specificity.
Involved in CDC48-dependent protein degradation through the ubiquitin/proteasome pathway.
Present with 6630 molecules/cell in log phase SD medium.
Belongs to the transient receptor potential (TRP) ion channel family.
May be responsible for the transport of FAD into the endoplasmic reticulum lumen, where it is required for oxidative protein folding.
Involved in regulation of L3 expression and stability and plays a role in early 60S ribosomal subunit assembly. May be required for proper assembly of pre-ribosomal particles during early ribosome biogenesis, presumably by targeting L3 onto the 35S precursor rRNA.
May be involved in cell wall organization and biogenesis.
Important for bud site selection. Seems to be a regulatory subunit of the BUD14-GLC7 type-I phosphatase complex. The BUD14-GLC7 complex is necessary to regulate microtubule dynamics at the cortex and may function as a specific activator of the dynein complex.
Belongs to the mitochondrion-specific ribosomal protein mL41 family.
Present with 2250 molecules/cell in log phase SD medium.
The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel.
The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. PRE3 and PRE4 are necessary for the peptidyl-glutamyl-peptide-hydrolyzing activity.
The side chain of Thr-20 acts as nucleophile, and the N-terminal amino group acts as proton acceptor.
This subunit is necessary for the peptidylglutamyl-peptide hydrolyzing activity.
ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping by activating the decapping enzyme DCP1 (PubMed:11780629, PubMed:12032091, PubMed:11696541, PubMed:12730603, PubMed:15703442. PubMed:15706350). Is involved in G1/S DNA-damage checkpoint recovery, probably through the regulation of the translational status of a subset of mRNAs (PubMed:15166134). May also have a role in translation and mRNA nuclear export (PubMed:12930949). Required for sporulation (PubMed:12930949). Blocks autophagy in nutrient-rich conditions by, at least partly, binding and repressing the expression of a set of ATG genes, including ATG3, ATG7, ATG8, ATG19, ATG20, ATG22 and SNX4/ATG24 (PubMed:26098573).
Associated with the CCR4-NOT complex and possibly other big complexes (PubMed:9504907, PubMed:12930949). Interacts with CDC39/NOT1 (PubMed:11696541). Interacts with DCP1, LSM1, and POP2 (PubMed:9504907, PubMed:11780629). Interacts with IGO1 (PubMed:20471941). Interacts with PAT1 and with KEM1, the major 5'-3' exonuclease (PubMed:11780629, PubMed:12032091).
Belongs to the DEAD box helicase family. DDX6/DHH1 subfamily.
Leads to an increased in autophagy flux (PubMed:26098573). Causes an accumulation of ATG3, ATG7, ATG8, ATG19, ATG20, ATG22 and SNX4/ATG24 transcripts in nutrient-replete conditions (PubMed:26098573).
Present with 42900 molecules/cell in log phase SD medium.
In concert with FKH1, plays a role in directionality of mating type switching by controlling which donor mating-type locus is inserted into MAT locus during mating type switching.
Leads to a defect in donor preference during mating-type switching (PubMed:27257873). Does not affect FKH1's overlapping role with FKH2 of regulation of the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle (PubMed:27257873).
Present with 2120 molecules/cell in log phase SD medium.
Enzyme activity is tightly regulated to prevent the accumulation of reactive oxygen species in the endoplasmic reticulum. Reversibly down-regulated by the formation of disulfide bonds between Cys-150 and Cys-295.
Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI1 to transfer oxidizing equivalent. Also able to oxidize directly the PDI related protein MPD2. Does not oxidize all PDI related proteins, suggesting that it can discriminate between PDI1 and related proteins. Reoxidation of ERO1 probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress.
May function both as a monomer and a homodimer.
The C-terminal part (437-563) is required for the association with the endoplasmic reticulum lumen membrane.
The Cys-100/Cys-105 and Cys-352/Cys-355 disulfide bonds constitute the redox-active center. The Cys-100/Cys-105 disulfide bond may accept electron from PDI1 and funnel them to the active site disulfide Cys-352/Cys-355.
Component of the Smc5-Smc6 complex which consists of KRE29, MMS21, NSE1, NSE3, NSE4, NSE5, SMC5 and SMC6. Interacts with NSE5.
Belongs to the heat shock protein 70 family.
Chaperone required for protein translocation and folding in the endoplasmic reticulum.
Interacts with the heat shock protein 70 (HSP70) KAR2, and this stimulates nucleotide exchange on KAR2. KAR2 in turn acts to stimulate the ATPase activity of LHS1.
Present with 137 molecules/cell in log phase SD medium.
Present with 2370 molecules/cell in log phase SD medium.
Deletion causes a slow growth phenotype on synthetic medium at 37 degrees Celsius and leads to decreased transcription. Deletion has no effect on ribosome biogenesis or frequency of recombination. Deletion is synthetically lethal with a deletion of each of the THO complex subunits HPR1, MFT1, THO2, and THP2.
Interacts with the TREX complex and RNA polymerase II.
Involved in transcription. Probably functions as a transcriptional activator.
Negative regulator of Ras-cAMP pathway. Involved in transcriptional regulation of galactose-inducible genes.
Plays a role in vacuolar arginine transport. Involved in pH homeostasis. May be involved in ion homeostasis together with IST2. Not necessary for mitochondrial function or ATP synthase degradation.
Belongs to the mitochondrion-specific ribosomal protein mL49 family.
Present with 1700 molecules/cell in log phase SD medium.
Molecular chaperone that binds nascent RNA polymerase III transcripts, stabilizing these RNAs against exonucleases. Required for the 3' endonucleolytic cleavage that matures tRNA precursors and for efficient folding of certain pre-tRNAs. Cooperates with GCD14 in the maturation of a subset of RNA polymerase III transcripts. Functions also in the assembly of certain RNA polymerase II-transcribed RNAs into RNPs. Binds and stabilizes newly synthesized U6 snRNA as well as precursors of U3 snRNA from degradation. Facilitates efficient Sm protein binding, thus assisting formation of the U4/U6 snRNP. Required for Ty3 normal transposition frequency.
Phosphorylation is not required for the roles tRNA and snRNP biogenesis.
Belongs to the eukaryotic ribosomal protein eS24 family.
N-terminally acetylated by acetyltransferase NatA. Also partially acetylated by NatC.
Present with 6160 molecules/cell in log phase SD medium.
May be involved in the regulation of telomere length.
Component of the ER membrane protein complex (EMC), which is composed of EMC1, EMC2, EMC3, EMC4, EMC5 and EMC6.
Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins (PubMed:29809151). Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed:29809151). Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed:29809151). It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins (By similarity).
Component of the SWR1 chromatin remodeling complex composed of at least ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4, SWC5, SWC7 and SWR1, and perhaps BDF1.
Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Involved in chromosome stability.
Interacts with YIP1 and the Rab GTPases SEC4, YPT1, YPT6, YPT10, YPT11, YPT31, YPT32 and YPT52.
Present with 5500 molecules/cell in log phase SD medium.
Cells show oxidative stress-related import deficiencies and growth defect on oleic acid (PubMed:21665945). Peroxisomes are clustered (PubMed:21665945). Cells display defects in peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) (PubMed:21665945).
Deubiquitinase involved in peroxisome import by mediating deubiquitination of the peroxisomal import receptor PEX5 (PubMed:21665945). Catalyzes deubiquitination of both monoubiquitiated and polyubiquitinated forms of PEX5 following its retrotranslocation into the cytosol, resetting PEX5 for a subsequent import cycle (PubMed:21665945).
Interacts with PEX6; promoting association with the PEX1-PEX6 ATPase complex.
Present with 1420 molecules/cell in log phase SD medium.
Alternate catalytic subunit of the 1,3-beta-glucan synthase (GS) complex. Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall. Involved in cell wall synthesis, maintenance and remodeling.
Belongs to the glycosyltransferase 48 family.
Cells are hypersensitive to immunosuppressant drugs FK506 and cyclosporin A (CsA) due to the inhibition of calcineurin phosphatase activity by the receptor-drug complexes and is dependent on calcineurin for vegetative growth. It confers a slow growth phenotype which is partially suppressed by exogenously added Ca(2+) and exacerbated by EGTA. Simultaneous disruption of CNA1 and CNA2 or CNB1 is lethal in FKS1-1. Disruption of FPR1 or CPR1 results in the loss of hypersensitivity. Overexpression of CNA1 or CNA2, in conjunction with CNB1, results in a significant decrease in hypersensitivity to FK506 and CsA. FKS1-8 mutant is sensitive to FK506 and cyclosporin A, has increased tendency to lyse and exhibits slow growth that is improved by the addition of osmotic stabilizing agents. It is more sensitive to the drugs when grown on galactose compared to dextrose. ETG1-1 mutant is resistant to the cell wall active echinocandins, which are inhibitors of 1,3-beta-D-glucan synthase. ETG1-4 mutant is hypersensitive to the chitin synthase inhibitor nikkomycin Z. Deletion of FKS1 leads to hypersensitivity to echinocandin-like antifungal lipopeptide caspofungin, a 1,3-beta-glucan synthase inhibitor. Deletion mutant also displays a 30% reduction in 1,3-beta-glucan and 15% reduction in alkali-insoluble 1,6-beta-glucan compared to wild-type. Increases cellular chitin level (PubMed:17142567). Increases chitin chain length (PubMed:17142567).
Component of the 1,3-beta-glucan synthase (GS) complex, composed of two alternate catalytic subunits FKS1 or GSC2, and a regulatory subunit RHO1. Interacts with RHO1, which is a GTP-binding protein.
During vegetative growth. Expressed periodically during the cell cycle.
Belongs to the methyltransferase superfamily. LCMT family.
S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the final 2 independent reactions, methylation of the alpha-carboxy group of wybutosine-72 to form wybutosine-58, and methoxycarbonylation of alpha-amino group of wybutosine-58 through the fixation of CO(2) to complete wybutosine.
Component of the GPI transamidase complex. Involved in transfer of GPI to proteins.
Forms a complex with CDC91, GPI16, GPI8 and GAA1.
Present with 7520 molecules/cell in log phase SD medium.
Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Present with 2330 molecules/cell in log phase SD medium.
ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA.
Belongs to the DEAD box helicase family. DDX18/HAS1 subfamily.
Interacts with RRP1. Associates in the nucleolus with the 60S and pre-60S ribosomal subunits. It has also been isolated with the nuclear pore complex.
Transcription depends partially on SET1.
Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily.
Major phosphatase responsible for tyrosine dephosphorylation of MAP kinases FUS3 and HOG1 to inactivate their activity; it also has important roles, along with MSG5, in the inactivation of FUS3 following pheromone stimulation.
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
Present with 7670 molecules/cell in log phase SD medium.
Belongs to the universal ribosomal protein uL24 family.
Component of the mitochondrial large ribosomal subunit (mt-LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. uL24m forms the wall of the exit tunnel.
A soluble form is probably produced by proteolytic cleavage at the cell surface (shedding).
Belongs to the flocculin family. Highly divergent.
Homophilic binding protein that enables kin discrimination in heterogeneous yeast populations by mediating homotypic cell-cell interactions during flocculation, a reversible and asexual process in which cells adhere to form aggregates (flocs) (PubMed:32286952, PubMed:25960408, PubMed:27547826, PubMed:17921350, PubMed:22129043). Plays a role in cell-substrate adhesion, haploid invasive growth, diploid pseudohyphae formation and biofilm (flor) development (PubMed:18001350, PubMed:11027318, PubMed:11157168, PubMed:16043420, PubMed:17921350, PubMed:20619652, PubMed:8710886, PubMed:8955395). Adhesive activity is inhibited by mannose, but not by glucose, maltose, sucrose or galactose (PubMed:16043420, PubMed:22129043).
In the reference strain S288C, the transcriptional activator FLO8 contains an internal in-frame stop codon, leading to impaired FLO11 expression in this strain.
The Flo11 domain contains aromatic residues that form two hydrophobic bands on the surface of the protein that confer homophilic binding (PubMed:32286952, PubMed:25960408, PubMed:22129043). The hydrophobic bands are lined by stretches of acidic residues that may sensitise the protein to environmental pH (PubMed:25960408). The domain is required for biofilm formation (PubMed:25960408). The domain does not interact with mannose or calcium ions (PubMed:22129043, PubMed:25960408).
The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By similarity).
The number of the intragenic tandem repeats varies between different S.cerevisiae strains. There is a linear correlation between protein size and the extend of adhesion: the more repeats, the stronger the adhesion properties and the greater the fraction of flocculating cells (By similarity).
Component of the U5 snRNP complex that is required for spliceosome assembly and for pre-mRNA splicing. Involved in splicing pre-mRNA of the A1 cistron and other genes that are important for cell growth.
Heterodimer (Probable). Interacts with PRP8 (via RNase H homology domain and MPN domain), competing with BRR2 for the same binding site. Component of a U5 snRNP complex that contains at least the U5 snRNA, PRP8, SNU114, AAR2, SMB1, SMD1, SMD2, SMD3, SME1, SMX2 and SMX3, but is not a component of the U4/U6-U5 tri-snRNP complex.
Phosphorylated on serine and tyrosine residues.
Present with 7330 molecules/cell in log phase SD medium.
Belongs to the transcriptional coactivator PC4 family.
Plays a role in the release of TFIIB from the transcription complex during transcription initiation. Binds to TFIIB and specifically inhibits the formation of the TBP-TFIIB-promoter complexes.
Present with 7820 molecules/cell in log phase SD medium.
Involved in sporulation and maintenance of the mitochondrial DNA. Is probably involved in a pathway contributing to genomic integrity.
Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.
Catalyzes the formation of pyruvate and succinate from 2-methylisocitrate during the metabolism of endogenous propionyl-CoA. Does not act on isocitrate.
Present with 1084 molecules/cell in log phase SD medium.
Repressed by glucose and induced by ethanol and threonine.
Essential for cell growth (PubMed:10749875). Inhibits early G-protein signaling events following pheromone stimulation (PubMed:10749875). Inhibits the folding activity of the chaperonin-containing T-complex (CCT) CCT2 which leads to inhibition of cytoskeletal actin folding (PubMed:17429077). Plays a role in cell cycle progression in G1/S phase (PubMed:17429077).
Impaired growth, cytoskeletal disruptions caused by actin polarization defects, and abberent nuclear segregation caused by misoriented mitotic spindles (PubMed:17429077). Cells are enlarged or do not bud, caused by cell cycle arrest in G1/S phase (PubMed:17429077).
Interacts with the G protein beta-gamma subunit complex (STE4-STE18 complex) (PubMed:10749875). Interacts with CCT2; this interaction leads to inhibition of CCT complex mediated actin folding (PubMed:17429077).
Present with 7700 molecules/cell in log phase SD medium.
Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Ubiquitin is encoded by 4 different genes. UBI1 and UBI2 genes code for a single copy of ubiquitin fused to the ribosomal proteins L40. UBI3 is a polyprotein with one copy of ubiquitin fused to ribosomal protein S37. UBI4 is a polyprotein containing 5 exact head to tail repeats of ubiquitin.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.
Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol (By similarity).
Decrease of translation termination efficacy and an increase in mRNAs half-lives and longer mRNA poly(A) tails.
Monomer and homodimer (PubMed:20630870, PubMed:20040577). Interacts with FRK1, eRF1 (SUP1), eRF3 (SUP35) and polyadenylate-binding protein PAB1. Interacts with ETT1 (PubMed:16809762, PubMed:20489023).
Present with 8910 molecules/cell in log phase SD medium.
Prolyl 3,4-dihydroxylase that catalyzes 3,4-dihydroxylation of 'Pro-64' of small ribosomal subunit uS12 (RPS23A and RPS23B), thereby regulating protein translation termination efficiency. Part of a messenger ribonucleoprotein (mRNP) complex at the 3'-UTR of mRNAs. It associates specifically with components of the translation termination complex and is involved in both translation termination and in regulation of normal mRNA decay through translation termination-coupled poly(A) shortening.
In the C-terminal section; belongs to the PGAP2IP family.
In the N-terminal section; belongs to the PGAP2 family.
Involved in the maintenance of cell wall integrity. Required for the replacement of the diacylglycerol moiety by ceramides during GPI-anchor maturation.
The PGAP2-like region interacts with the PGAP2IP-like region.
Associates with the nuclear pore complex (NPC). Interacts with GSP2, NUP1, NUP2, TOA1, TOA2 and WTM1.
Nuclear transport factor (karyopherin) involved in protein transport between the cytoplasm and nucleoplasm. Required for the nuclear import of the complex composed the large subunit (TOA1) and the small subunit (TOA2) of the general transcription factor IIA (TFIIA). Required for the nuclear import of the RNR2-RNR4 heterodimer, also called beta-beta' subunit, which corresponds to the small subunit of the ribonucleotide reductase (RNR). May play a role in regulation of pleiotropic drug resistance.
Present with 9760 molecules/cell in log phase SD medium.
Belongs to the phosphohexose mutase family.
Minor phosphoglucomutase isozyme that catalyzes the interconversion of glucose 1-phosphate and glucose 6-phosphate (PubMed:5784209). Constitutes about 10-20% of the phosphoglucomutase activity in the cell (PubMed:14264884, PubMed:5231755). Key enzyme in hexose metabolism. The forward reaction is an essential step in the energy metabolism of galactose since the product of the galactose pathway enzymes in yeast is glucose 1-phosphate. The reverse reaction is an essential step for biosynthesis when carbon sources other than galactose are the energy source because glucose 1-phosphate is the starting point for the synthesis of UDP-glucose, which acts as a precursor for the synthesis of oligosaccharides and trehalose (PubMed:14264884).
Present with 9820 molecules/cell in log phase SD medium.
Belongs to the thiolase-like superfamily. HMG-CoA synthase family.
Hydroxymethylglutaryl-CoA synthase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (PubMed:12702274). ERG13 condenses acetyl-CoA with acetoacetyl-CoA to form hydroxymethylglutaryl-CoA (HMG-CoA) (PubMed:12702274). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthase ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases HMG1 and HMG2 which are derived from a single ancestral HMGR gene by gene duplication (PubMed:32679672).
Present with 34800 molecules/cell in log phase SD medium.
Belongs to the WD repeat G protein beta family.
G proteins are composed of 3 units, alpha, beta and gamma. The beta-gamma subunit complex (STE4-STE18 complex) interacts with PLP1 and PLP2. Interacts with SYG1.
Implicated in the a- and alpha-factor response pathway. The beta and gamma chains of the putative yeast mating response pathway G protein play a positive role in initiation of the mating response. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Present with 2050 molecules/cell in log phase SD medium.
Belongs to the ABC transporter superfamily. ABCG family. PDR (TC 3.A.1.205) subfamily.
Acts as catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. CCR4 has 3'-5' RNase activity with a strong preference for polyadenylated substrates and also low exonuclease activity towards single-stranded DNA. Discovered because of its role in the control of ADH2 gene expression. It is required for the expression of genes involved in non-fermentative growth and it mediates or is required for the action of the SPT6 and SPT10 genes.
Present with 2780 molecules/cell in log phase SD medium.
Subunit of the 1.0 MDa CCR4-NOT core complex that contains CCR4, CAF1, NOT1, NOT2, NOT3, NOT4, NOT5, CAF40 and CAF130. In the complex interacts with NOT1. The core complex probably is part of a less characterized 1.9 MDa CCR4-NOT complex.
The 169 C-terminal residues are important for deadenylase activity.
To yeast high affinity methionine permease (MUP1).
Very low affinity permease for methionine.
Interacts with SCC2 to form the cohesin loading complex.
Involved in sister chromatid cohesion (PubMed:10882066). Forms a complex with SCC2, which is required for the association of the cohesin complex with chromosomes (PubMed:10882066, PubMed:26038942). Binds to the nucleosome-free promoter regions of ribosomal protein genes and tRNA genes (PubMed:25173104).
Belongs to the major facilitator superfamily. Allantoate permease family.
Involved in the uptake of nicotinic acid.
ATP-dependent DNA helicase involved in DNA damage repair by homologous recombination and in genome maintenance (PubMed:10880470, PubMed:15126389, PubMed:15634678, PubMed:16121259). Capable of unwinding D-loops (PubMed:19136626). Plays a role in limiting crossover recombinants during mitotic DNA double-strand break (DSB) repair (PubMed:19136626). Prevents crossovers between ectopic sequences by removing substrates for MUS81-MMS4 or RAD1-RAD10 cleavage (PubMed:24119400). Component of a FANCM-MHF complex which promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork (Probable) (PubMed:22912599). Binds to flap-structured DNA but not to non-flap nicked DNA, and participates in Okazaki fragment processing by stimulating the endonuclease activities of FEN1 and DNA2 (PubMed:19181670). Involved in recombination donor preference during mating-type switching via interaction with FKH1 (PubMed:27257873).
Belongs to the DEAD box helicase family. DEAH subfamily. FANCM sub-subfamily.
Causes transiant accumulation of ectopic joint molecules (JMs) (PubMed:24119400). Leads to a defect in donor preference during mating-type switching (PubMed:27257873). Does not affect FKH1's overlapping role with FKH2 of regulation of the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle (PubMed:27257873).
Interacts with the MHF histone-fold complex composed of MHF1 and MHF2 to form the FANCM-MHF complex (By similarity). Interacts with FHK1 (PubMed:27257873).
Phosphorylation at both Thr-776 and Thr-785 is required for the interaction with FKH1.
Endoplasmic reticulum-Golgi intermediate compartment membrane
Functions with VOA1 in assembly of the integral membrane sector (also called V0 sector) of the V-ATPase in the endoplasmic reticulum. Escorts the assembled V0 sector in COPII vesicles. Also required for normal packaging of the SNARE BOS1 and possibly the ER to Golgi transport receptor ERV29.
Component of the RPD3C(L) complex composed of at least ASH1, CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6.
Component of the RPD3C(L) histone deacetylase complex (HDAC) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events.
Present with 3060 molecules/cell in log phase SD medium.
Present with 5240 molecules/cell in log phase SD medium.
Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily.
Mitochondrial metal transporter involved in mitochondrial iron accumulation.
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner (PubMed:15870080, PubMed:16428434, PubMed:8146662, PubMed:8276800, PubMed:8354406, PubMed:8810243, PubMed:9405361, PubMed:9724747, PubMed:35143841). Endogenous substrates include ABF2, ACO2, ILV1, ILV2, LSC1, LYS4, MGM101 and several oxidized proteins. The 2 nucleic acid-binding proteins ABF2 and MGM101 are protected from degradation by PIM1 when they are bound to DNA (PubMed:16428434, PubMed:20150421, PubMed:28377575).
Homohexamer (PubMed:35143841) (Probable). Organized in a ring with a central cavity (PubMed:10359790). The ATP-binding and proteolytic domains (AP-domain) form a hexameric chamber (PubMed:35143841). Oligomerization is independent of its proteolytic activity and the autocatalytic maturation of its subunits (PubMed:9724747).
Present with 14500 molecules/cell in log phase SD medium.
Associates with the mitochondrial ribosome.
Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression.
Present with 504 molecules/cell in log phase SD medium.
Belongs to the cytochrome c oxidase subunit 2 family.
Binds a dinuclear copper A center per subunit.
Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of 12 subunits. The complex is composed of a catalytic core of 3 subunits COX1, COX2 and COX3, encoded in the mitochondrial DNA, and 9 supernumerary subunits COX4, COX5A (or COX5B), COX6, COX7, COX8, COX9, COX12, COX13 and COX26, which are encoded in the nuclear genome (PubMed:7851399, PubMed:30598556, PubMed:30598554). The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a dimer of ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), resulting in 2 different assemblies (supercomplexes III(2)IV and III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556, PubMed:30598554).
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix (Probable). COX2 is a catalytic core subunit which transfers the electrons from cytochrome c via its dinuclear copper A center (CU(A)) to the BNC of the COX1 (PubMed:30598554).
The N-terminal sequence of COX2 is processed by IMP1.
Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is involved in meiotic sporulation through regulating IME2 expression, and is also essential for 2-micron plasmid maintenance and for normal REP1 protein localization.
Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin.
Heterochromatin spreading downstream of the silent mating-type locus HMR.
Required to stabilize mitochondrial cytochrome C oxidase subunit 2 (COX2) and to translocate the C-terminal domain of COX2 through the inner membrane.
Component of the endosomal sorting complex required for transport II (ESCRT-II), which consists of 2 copies of VPS25, 1 copy of SNF8, and 1 copy of VPS36. The ESCRT-II complex interacts directly with the VPS20 subunit of the ESCRT-III complex.
Component of the endosomal sorting complex required for transport II (ESCRT-II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex.
Belongs to the PPP phosphatase family. PP-6 (PP-V) subfamily.
Functions in the late cell cycle G1 phase for progression into the S phase, possibly associated in two separate complexes with the phosphorylated forms of p155 and p190, two high MW proteins.
Inactivated in a complex with phosphatase methylesterase PPE1 (PP2Ai). Interacts with phosphatase 2A activator RRD1, which can reactivate PP2Ai by dissociating the catalytic subunit from the complex. Forms a ternary complex with RRD1-TAP42.
Involved in the dephosphorylation of the large subunit of RNA polymerase II. Is required in late G1 for normal G1 cyclin expression, bud initiation and expression of certain genes that are periodically expressed during late G1. Associates with the SAP proteins in a cell cycle-dependent manner.
Present with 3970 molecules/cell in log phase SD medium.
Not known; its elevated expression suppresses the conditional cell cycle defects associated with UBC3/CDC34 mutations.
Positive transcriptional factor that acts as a component of the stress responsive system. Recognizes and binds to the stress response element (STRE) which is involved in the response to various forms of stress (heat, oxidative, osmotic, etc.). Involved in the regulation of the CTT1, DDR2, HSP12 genes. May be regulated via WHI2-PSR1 complex phosphatase activity.
Present with 125 molecules/cell in log phase SD medium.
The 9aaTAD motif (residues 261 to 269) is a transactivation domain present in a large number of yeast and animal transcription factors.
Belongs to the polysaccharide deacetylase family.
Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin to form chitosan and acetate (PubMed:9133736, PubMed:11812231). Chitosan is a component of the spore wall (PubMed:9133736).
Can hydrolyze human UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders. It can do so despite of the fact that the C-terminal 'Gly-76' of ubiquitin has been substituted for a tyrosine in UBB(+1).
Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or RUB1. Preferentially cleaves ubiquitin from peptides and small adducts.
Belongs to the histidine acid phosphatase family.
Glycosylated during secretion across the membrane.
Present with 1460 molecules/cell in log phase SD medium.
S.cerevisiae has 2 types of acid phosphatase: one is constitutive and the other is repressible by inorganic phosphate.
Associates with the 90S pre-ribosome. Interacts with RNA helicase DHR2 and RNA helicase-like protein UTP25.
Ribosome biogenesis factor required for cleavage of pre-rRNA at A0, A1 and A2 sites. Essential for the incorporation of UTP25 in pre-ribosomes.
Induced at very late stage of sporulation.
Serves a protective function during the early stages of spore wall formation, and contributes to spore wall maturation.
The program of events of meiosis and spore formation reflects the sequential expression of at least four temporally distinct classes of sporulation-specific genes, SPS100 and SPS101 genes define a distinct class of very late sporulation genes.
Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family.
Component of the inner kinetochore constitutive centromere-associated network (CCAN) (also known as central kinetochore CTF19 complex in yeast), which is composed of at least AME1, CHL4, CNN1, CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1.
Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly (PubMed:22561346).
Highly specific phosphatase involved in the metabolism of ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of tRNA splicing. + phosphate.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM61 family.
Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA (PubMed:10779558, PubMed:9851972). GCD14 is also required for repression of GCN4 mRNA translation by the upstream open reading frames (uORFs) under conditions of amino acid sufficiency (PubMed:9539420).
Heterotetramer; composed of two copies of TRM6/GCD10 and two copies of TRM61/GCD14.
Present with 7220 molecules/cell in log phase SD medium.
Phosphatidylglycerophosphatase involved in the biosynthesis of cardiolipin (CL), a unique dimeric phosphoglycerolipid predominantly present in mitochondrial membranes and which has important functions for cellular energy metabolism, mitochondrial dynamics and the initiation of apoptotic pathways. Required for the stability of respiratory chain supercomplexes and for growth at elevated temperature, in presence of ethidium bromide or in absence of prohibitins.
Present with 1540 molecules/cell in log phase SD medium.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Binds to 80S ribosomes (PubMed:12692531, PubMed:14976550, PubMed:15316019). Interacts with the 40S ribosomal subunit protein RPL9A; the interaction is direct (PubMed:14976550). Interacts with the 60S ribosomal subunit proteins RPL12A; the interaction is direct (PubMed:14976550). Interacts with RPS23A; the interaction is direct (PubMed:14976550). Interacts with 18S rRNA; the interaction is direct (PubMed:14976550). Interacts with 25S rRNA; the interaction is direct (PubMed:14976550). Interacts with RPL0 (PubMed:12410829).
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Diphthamide can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A, thus abolishing its function.
Inhibited by fusidic acid and sordarin, which prevent the release of eEF2 from the ribosome after the translocation step (PubMed:9452424, PubMed:12692531, PubMed:14976550). While fusidic acid acts on all eukaryotic eEF2, sordarin specifically binds and inhibits only selected fungal eEF2 (PubMed:9452424).
Present with 160782 molecules/cell in log phase SD medium.
Component of the NOP7 complex, composed of ERB1, NOP7 and YTM1. The complex is held together by ERB1, which interacts with NOP7 via its N-terminal domain and with YTM1 via a high-affinity interaction between the seven-bladed beta-propeller domains of the 2 proteins. The NOP7 complex associates with the 66S pre-ribosome (PubMed:16287855). Also interacts with NOG1 (PubMed:16888624). May also associate with the origin recognition complex (ORC complex) (PubMed:12110181).
Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome.
Essential gene. Reduced assembly of 60S ribosomes and accumulation of halfmer polyribosomes.
Expression is down-regulated prior to the diauxic shift.
Present with 4530 molecules/cell in log phase SD medium.
Belongs to the phytoene/squalene synthase family.
Expression is increased in mutants with phenotypes consistent with known sterol biosynthetic mutations (ERG3, ERG7, ERG24) (PubMed:10209263). The sterol inhibitors zaragozic acid and ketoconazole, which target squalene synthase and the C-14 sterol demethylase respectively, also cause an increase in expression (PubMed:10209263). Heme mutants increase ERG9 expression while anaerobic conditions decrease expression (PubMed:10209263). Additionally, the heme activator protein transcription factors HAP1 and HAP2/3/4, the yeast activator protein transcription factor yAP-1, and the phospholipid transcription factor complex INO2/4 regulate ERG9 expression (PubMed:10209263).
Impairs the production of ergosterol and leads to a 6-fold increase in the synthesis of polyprenols.
Present with 10800 molecules/cell in log phase SD medium.
Squalene synthase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:1807826, PubMed:2068081, PubMed:8323279, PubMed:9742963). ERG9 produces squalene from 2 farnesyl pyrophosphate moieties (PubMed:1807826, PubMed:8323279). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672).
Assembles into a complex with MCM5/CDC46. Interacts with MCM10.
Present with 1730 molecules/cell in log phase SD medium.
Required for initiation of chromosomal DNA replication. Acts at the origin of replication. Also has a role in minichromosome maintenance.
Belongs to the prefoldin subunit alpha family.
Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
Heterohexamer of two PFD-alpha type and four PFD-beta type subunits.
Present with 2900 molecules/cell in log phase SD medium.
Translation factor specific for subunit 6 of the mitochondrial ATPase. Required for assembly of the CF(0) component of the ATPase.
May be involved in protein-linked oligosaccharide phosphorylation since the deletion reduces the negative charge of the cell surface.
Present with 329 molecules/cell in log phase SD medium.
Compared to higher eukaryotes TAF1, yeast TAF1 lacks the C-terminal bromodomains and C-terminal kinase activity. The TFIID interacting proteins BDF1 and BDF2 may substitute for these domains.
The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14.
Acetyl-CoA acetyltransferase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (PubMed:7989303, PubMed:5571829). ERG10 catalyzes the formation of acetoacetyl-CoA from acetyl-CoA (PubMed:7989303, PubMed:5571829). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthase ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases HMG1 and HMG2 which are derived from a single ancestral HMGR gene by gene duplication (PubMed:32679672).
Belongs to the thiolase-like superfamily. Thiolase family.
Induced by low intracellular sterol levels (PubMed:8754796). Also highly induced by cold conditions (PubMed:12039763).
Present with 60895 molecules/cell in log phase SD medium.
Expression is induced by nitrogen limitation in a GLN3 and GAT1-independent manner.
Leads to vacuolar defects as well as defects in the terminal steps of autophagy, when PCR1 is also deleted (PubMed:29514932). The PCR1/ATG42 double deletion abrogates also the production ofphytochelatin and the degradation of glutathione-S-conjugates (PubMed:17408619, PubMed:19897216).
Vacuolar serine-type carboxypeptidase involved in vacuolar zymogen activation, breakdown of the autophagic body, and autophagosome-dependent protein synthesis (PubMed:29514932). Plays a key role in phytochelatin (PC) synthesis from glutathione (GSH) by cleaving the Gly from GSH and form the PC-peptides of the structure (gamma-Glu-Cys)2-Gly (PubMed:17408619). Also involved in resistance to xenobiotics via the degradation of glutathione-S-conjugates (PubMed:19897216).
Acyltransferase that catalyzes the sn-2-specific, acyl-CoA-dependent acylation of lysophosphatidic acid (LPA) to phosphatidic acid (PA) in lipid particles (PubMed:9401016). Together with ALE1, plays a central role in PA biosynthesis. PA is the intermediate, from which all glycerophospholipids are synthesized (PubMed:17890783). Can also acylate lysophosphoinositol (LPI) and lysophosphoserine (LPS) (PubMed:17675291). The fatty acyl substrates include 18:1-acyl-CoA, 14:0-acyl-CoA, 12:0-acyl-CoA and 10:0-acyl-CoA (PubMed:20694142).
Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YDR316W-A ORF.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family.
GTPase activity is stimulated in the presence of 60S subunits.
GTPase involved in the biogenesis of the 60S ribosomal subunit and translational activation of ribosomes. Together with SDO1, may trigger the GTP-dependent release of TIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating TIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Inhibits GTPase activity of ribosome-bound EF-2.
Present with 7770 molecules/cell in log phase SD medium.
Central component of the spindle assembly checkpoint which is a feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. Thought to be recruited to unattached kinetochores by MAD1. During checkpoint activity, MAD2 is relayed from the MAD1-MAD2 complex to the mitotic checkpoint complex (MCC). MCC and presumably the MAD2-CDC20 subcomplex inhibit the ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) by preventing its activation by CDC20.
Component of the mitotic checkpoint complex (MCC) which consists of MAD2, MAD3, BUB3 and CDC20, and of the MAD2-CDC20 subcomplex, both of which appear to be assembled during mitoisis independently of the kinetochore. In mitose-arrested cells, MAD2-CDC20 occurs in a larger amount than MCC. Interacts with CDC20 and BUB3.
Present with 450 molecules/cell in log phase SD medium.
An increased rate of escape of mtDNA to the nucleus, no growth on nonfermentable carbon sources at 37 degrees Celsius, a cold-sensitive defect in growth on fermentable carbon sources, lethality in rho- (cytoplasmic petite) cells.
Catalytic subunit of the mitochondrial inner membrane i-AAA protease supercomplex required for mitochondrial inner membrane protein turnover. The protease is probably ATP-dependent. Important to maintain the integrity of the mitochondrial compartment. Required both for the degradation of unassembled subunit 2 of cytochrome c oxidase (COX2) and for efficient assembly of mitochondrial respiratory chain. Binds unfolded substrates in an ATPase-independent manner; binding of folded COX2, a physiological substrate, requires an active ATPase but when COX2 is destabilized an active ATPase is no longer necessary.
Component of the mitochondrial inner membrane i-AAA protease supercomplex composed of MGR1, MGR3 and YME1. Interacts directly with MGR1.
In the C-terminal section; belongs to the peptidase M41 family.
In the N-terminal section; belongs to the AAA ATPase family.
Present with 20100 molecules/cell in log phase SD medium.
Belongs to the amino acid/polyamine transporter 2 family.
Probable amino acid transporter of unknown specificity.
Could be the product of a pseudogene unlikely to encode a functional protein. The ORF corresponds to a fragmentary flocculin piece with sequence similarity to FLO1. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set.
Could be the product of a pseudogene. The ORF corresponds to a fragmentary flocculin piece with sequence similarity to FLO1.
Belongs to the class V-like SAM-binding methyltransferase superfamily.
Present with 7880 molecules/cell in log phase SD medium.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates 60S ribosomal protein L42 (RPL42A and RPL42B) at 'Lys-40'.
Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with RDS3.
Contacts pre-mRNA on both sides of the branch site early in spliceosome assembly.
Present with 521 molecules/cell in log phase SD medium.
Belongs to the TRAFAC class YlqF/YawG GTPase family.
GTPase required for 60S ribosomal subunit export to the cytoplasm.
In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.
Present with 7130 molecules/cell in log phase SD medium.
Belongs to the major facilitator superfamily. CAR1 family.
Up-regulated in cells exhibiting reduced susceptibility to azoles.
Belongs to the eukaryotic RPC9 RNA polymerase subunit family.
Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. Forms a Pol III subcomplex with RPC25/RPC8. Interacts with BURF1/TDS4.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. The RPC25/RPC8-RPC17/RPC9 subcomplex may bind Pol III transcripts emerging from the adjacent exit pore during elongation.
Present with 2930 molecules/cell in log phase SD medium.
Belongs to the MICOS complex subunit Mic10 family.
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Component of the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MIC10, MIC12, MIC19, MIC26, MIC27 and MIC60. This complex was also known under the names MINOS or MitOS complex. Interacts with OM45 and POR1.
Partially altered shape of the mitochondrial network with condensed, fragmented mitochondria accumulating at the periphery of cells. 60-70% of mitochondria exhibit an increased inner membrane surface and stacks of lamellar cristae disconnected from the inner boundary membrane.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. YchF/OLA1 subfamily.
By hydrogen peroxide and during DNA replication stress.
Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP.
Monomer (By similarity). Interacts with the 26S proteasome subunit RPT6.
Present with 36803 molecules/cell in log phase SD medium.
Belongs to the imidazoleglycerol-phosphate dehydratase family.
Induced by histidine starvation in a GCN4-dependent manner.
Dephosphorylates a number of phosphatidylinositols (PIs) like phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), but also phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Controls the cellular levels and subcellular distribution of phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-bisphosphate. Specifically functions within the early endocytic pathway and actin organization.
In the central section; belongs to the inositol 1,4,5-trisphosphate 5-phosphatase family.
The SAC1 domain is capable of hydrolyzing phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
Belongs to the succinate/malate CoA ligase beta subunit family.
Heterodimer of an alpha and a beta subunit.
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA (PubMed:9874242). The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit (By similarity).
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
Binds 1 pyridoxal phosphate per subunit.
Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Present with 15900 molecules/cell in log phase SD medium.
Interacts with snoRNA U3 (PubMed:15590835). Interacts with MPP10 (PubMed:15590835). Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3 (PubMed:15590835). Interacts with UBP10 (PubMed:22902402, PubMed:26149687).
Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Component of the HRD1 ubiquitin ligase complex which contains the E3 ligase HRD1, its cofactors HRD3, USA1 and DER1, substrate recruiting factor YOS9 and CDC48-binding protein UBX2 (PubMed:16873066, PubMed:32327568). Within the complex, interacts with USA1 (via C-terminus) (PubMed:20005842, PubMed:32327568). In ERAD-L, HRD3 and YOS9 jointly bind misfolded glycoproteins in the endoplasmic reticulum (ER) lumen (PubMed:32327568). Movement of ERAD-L substrates through the ER membrane is facilitated by HRD1 and DER1 which have lateral gates facing each other and which distort the membrane region between the lateral gates, making it much thinner than a normal phospholipid bilayer (PubMed:32327568). Substrates insert into the membrane as a hairpin loop with one strand interacting with DER1 and the other with HRD1 (PubMed:32327568). The HRD1 complex interacts with the heterotrimeric CDC48-NPL4-UFD1 ATPase complex which is recruited by UBX2 via its interaction with CDC48 and which moves ubiquitinated substrates to the cytosol for targeting to the proteasome (PubMed:16873066).
Component of the endoplasmic reticulum-associated degradation (ERAD) pathway. Specifically required for the ERAD-L pathway which mediates the degradation of proteins with misfolded lumenal domains within the endoplasmic reticulum (ER). Facilitates retrotranslocation of misfolded proteins from the ER lumen through the ER membrane in conjunction with HRD1 (PubMed:32327568). Both proteins have lateral gates facing each other and distort the membrane region between the lateral gates, making it much thinner than a normal phospholipid bilayer (PubMed:32327568). Substrates insert into the membrane as a hairpin loop with one strand interacting with DER1 and the other with HRD1 (PubMed:32327568).
Impaired degradation of proteins with misfolded lumenal domains such as CPY*, a mutant, misfolded form of carboxypeptidase Y which is a known ERAD-L substrate. Degradation of proteins with misfolded intramembrane domains is not affected.
N-terminally acetylated by acetyltransferase NatB which enhances DER1 stability and is required for ERAD-L function.
Up-regulated by the unfolded protein response (UPR).
Belongs to the bacterial ribosomal protein bS21 family.
Present with 149 molecules/cell in log phase SD medium.
Belongs to the eukaryotic ribosomal protein eL43 family.
Present with 44600 molecules/cell in log phase SD medium.
Present with 45500 molecules/cell in log phase SD medium.
Required for the accumulation of coenzyme A in the mitochondrial matrix.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YML040W ORF.
Interacts with KTI11/DPH3; the interaction is direct.
Together with KTI11; associates with the elongator complex and is required for tRNA Wobble base modifications mediated by the elongator complex (PubMed:18466297, PubMed:25543256). Association with the elongator complex is mediated via interaction with KTI11 (PubMed:18466297, PubMed:25543256). The elongator complex is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:25543256). Together with KTI11; also required for diphthamide biosynthesis; diphthamide is a post-translational modification of histidine which occurs in elongation factor 2 (PubMed:25543256). May participate in regulatory interactions between microtubules and the cell cycle (PubMed:8070652).
Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
Inhibited by diphenylene iodonium (DPI).
NADH-dependent cytochrome b5 reductase that reduces coenzyme Q6 at the plasma membrane and mediates lifespan extension by calorie restriction by shifting fermentative to respiratory metabolism, probably through modulating the NAD(+)/NADH ratio.
Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.
Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Single-stranded DNA endonuclease involved in excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Essential for the incision step of excision-repair.
Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with RDS3. Interacts with LEA1.
Involved in pre-mRNA splicing. This protein is associated with snRNP U2. It binds stem loop IV of U2 snRNA.
Belongs to the complex I LYR family. SDHAF1 subfamily.
Interacts with SDH2 within an SDH1-SDH2 subcomplex.
OXPHOS incompetent because of a profound and specific reduction of complex II activity.
Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit SDH2 of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. Acts together with SDHAF3 (SDH7).
Forms a complex composed of CDC48, NPL4, UFD1, DOA1, SHP1 and deubiquitinase OTU1; within the complex interacts with CDC48 and DOA1/UFD3.
Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Participates in the regulation of the ubiquitin conjugation pathway involving CDC48 by hindering multiubiquitination of substrates at the CDC48 chaperone. May be indirectly involved in PIS1 gene expression.
Present with 2770 molecules/cell in log phase SD medium.
The OTU domain mediates the hydrolase activity and the interaction with CDC48.
Directly involved in telomere replication. Associates with telomerase and during its interaction with CDC13, telomerase activity is promoted.
Present with 1050 molecules/cell in log phase SD medium.
Interacts with NOP1 and NOP58. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.
Present with 13500 molecules/cell in log phase SD medium.
Required for 60S ribosomal subunit synthesis.
By phosphorylation. The catalytic activity is inhibited by soraphen A, a polyketide isolated from the myxobacterium Sorangium cellulosum and a potent inhibitor of fungal growth.
Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. Involved in the synthesis of very-long-chain fatty acid synthesis which is required to maintain a functional nuclear envelope. Required for acylation and vacuolar membrane association of VAC8 which is necessary to maintain a normal morphology of the vacuole.
Present with 20200 molecules/cell in log phase SD medium.
Repressed in presence of fatty acids. Repressed 3-fold by lipid precursors, inositol and choline, and also controlled by regulatory factors INO2, INO4 and OPI1.
Heterotetramer of ERG25, ERG26, ERG27 and ERG28. ERG28 acts as a scaffold to tether ERG27 and other 4,4-demethylation-related enzymes, forming a demethylation enzyme complex, in the endoplasmic reticulum. Interacts with ERG25, ERG26 and ERG27. Also interacts with ERG1, ERG3, ERG5, ERG6 and ERG11.
Part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:11160377, PubMed:12119386, PubMed:15522820, PubMed:15995173). ERG28 has a role as a scaffold to help anchor the catalytic components of the C-4 demethylation complex ERG25, ERG26 and ERG27 to the endoplasmic reticulum (PubMed:12119386, PubMed:15522820, PubMed:15995173). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672).
Present with 377 molecules/cell in log phase SD medium.
Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of at least PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. Interacts with the phosphorylated CTD domain of RPB1/RNA polymerase II.
Present with 639 molecules/cell in log phase SD medium.
RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Involved in poly(A) site recognition. May be involved in coupling transcription termination and mRNA 3'-end formation.
Transposon Ty1-A (YARCTy1-1) contains a frameshift at position 610, which disrupts the ORF coding for protein TY1B.
Ty1-A is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Ty1-PR1 is a highly expressed element. Induced under amino acid starvation conditions by GCN4.
Belongs to the exosome component 10/RRP6 family.
Component of the RNA exosome complex. The catalytically inactive RNA exosome core (Exo-9) complex associates with catalytic subunits DIS3 and RRP6 in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits and peripheral S1 domain-containing components CSL4, RRP4 and RRP40 located on the top of the ring structure. RRP6 specifically is part of the nuclear form of the RNA exosome complex; the association appears to be mediated by Exo-9 and not by DIS3. Interacts with LRP1. Interacts with NPL3, NOP53 and PAP1.
Deletion mutant is impaired in growth at all temperatures and is nonviable at 37 degrees Celsius. It is defective in the 3' processing of the 5.8S rRNA and accumulates a discrete species, 5.8S + 30, that is 3' extended by about 30 nucleotides. Deletion also causes an accumulation of 7S RNA and 5' ETS and increases the level of poly(A)+ mRNA.
Nuclear-specific catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP6 has 3'-5' exonuclease activity which is not modulated upon association with Exo-9 suggesting that the complex inner RNA-binding path is not used to access its active site.
Present with 2160 molecules/cell in log phase SD medium.
Members of the DUP240 multigene family are specific to S.cerevisiae sensu strictu. Cells lacking all 10 DUP240 proteins show no obvious alterations in mating, sporulation and cell growth.
Present with 1695 molecules/cell in log phase SD medium.
Binds human HTN3/histatin-5, a peptide from saliva, and mediates its fungicidal activity. Interacts with NAP1.
May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A functional difference between SSA1 and SSA2 proteins is expected. SSA2 can participate in the ATP-dependent disassembly of clathrin-coated vesicles.
Present with 364000 molecules/cell in log phase SD medium.
May play a role in a switch from carbohydrate utilizing metabolism to fatty acid utilizing metabolism.
Strong, by heat shock, by entry in the stationary growth phase, and by cAMP, probably via the activity of a cAMP-dependent protein kinase. By glucose starvation and by fatty acids.
Functions in the SND pathway, a SRP (signal recognition particle) and GET (guided entry of tail-anchored proteins) independent pathway for targeting a broad range of substrate proteins to the endoplasmic reticulum. SND functions in parallel to GET in targeting proteins with downstream hydrophobic motifs.
Present with 1250 molecules/cell in log phase SD medium.
Co-chaperone that binds to the molecular chaperone Hsp70 (SSA1 and SSA2). Regulates Hsp70 ATPase activity (By similarity). Required for recovery from heat shock.
Interacts with HSC82, HSP104, MDY2, SSA1 and SSA2.
Present with 9424 molecules/cell in log phase SD medium.
Glycosyltransferase that transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage. Required for addition of mannosylphosphate in yeast mannan. Recognizes any oligosaccharides with at least one alpha-1,2-linked mannobiose unit.
Present with 4380 molecules/cell in log phase SD medium.
Belongs to the eukaryotic ribosomal protein eL15 family.
Component of the SEA complex composed of at least IML1/SEA1, RTC1/SEA2, MTC5/SEA3, NPR2, NPR3, SEA4, SEC13 and SEH1.
Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis.
Component of the origin recognition complex (ORC) composed of at least ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6.
Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication.
Present with 2170 molecules/cell in log phase SD medium.
Belongs to the universal ribosomal protein uL13 family.
Localized to sites of polarized growth and is required for efficient mating and bipolar budding.
Probable protease. Involved in axial budding.
DIG2 and DIG1 are negative regulators of the filamentation and pheromone induced mating program. DIG1 and DIG2 inhibit the transcriptional activity of STE12 by direct protein-protein interaction. DIG2 binds to the DNA binding domain (DBD) of STE12 and thus inhibits transcription when overexpressed.
Forms a complex with DIG1, STE12 and either FUS3 or KSS1. The interaction of FUS3 with STE12 depends on the presence of both DIG1 and DIG2. STE12 is lost from FUS3/DIG1/DIG2 complex after pheromone treatment. DIG1 and DIG2 have also been reported to interact with CLN1 and CLN2.
Phosphorylated by FUS3 and KSS1, in a pheromone-stimulated manner.
Present with 1310 molecules/cell in log phase SD medium.
Belongs to the universal ribosomal protein uS15 family.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
The reaction catalyzed by ACOAT is highly reversible. Moreover this enzyme may transaminate ornithine, although this activity should be of little importance at physiological pH.
catalyzes the conversion of N-acetylglutamate-gamma-semialdehyde (NAGSA) to N-acetylornithine in arginine biosynthesis.
Probable transporter. Does not act in the transport of monocarboxylic acids across the plasma membrane.
Induced by alpha-pheromone. Repressed by the ALPHA2-MCM1 repressor.
Required for receptor inhibition of inappropriately expressed a-factor receptor (STE3) in MAT a cells. Inhibits signaling by relocalizing the G protein beta-gamma (STE4-STE18) subunit to intracellular membranes. May also be a mechanism for the down-regulation of the mating pheromone response after the zygotic fusion event, promoting the transition of the new diploid cell to vegetative growth.
Belongs to the eukaryotic ribosomal protein eL41 family.
Present with 4910 molecules/cell in log phase SD medium.
Belongs to the TFIIF alpha subunit family.
Phosphorylated on Ser and other residues by TAF1 and casein kinase II-like kinases.
TFIIF is a general transcription initiation factor that binds to RNA polymerase II. Its functions include the recruitment of RNA polymerase II to the promoter bound DNA-TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for non-specific DNA, allowing for the subsequent recruitment of TFIIE and TFIIH, and facilitating RNA polymerase II elongation.
TFIIF is composed of three different subunits: TFG1/RAP74, TFG2/RAP30 and TAF14.
Component of the UAF (upstream activation factor) complex which consists of UAF30, RRN5, RRN9, RRN10, and histones H3 and H4.
Component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. Together with SPT15/TBP UAF seems to stimulate basal transcription to a fully activated level.
Conjugated with HUB1. HUB1 has not the classical C-terminal Gly residue, so it is still unknown how conjugation may occur.
Polarity-determining protein which forms a conjugate with the ubiquitin-like modifier HUB1. Involved in bud site selection and cellular morphogenesis during conjugation. Required for pseudohyphal growth.
Present with 672 molecules/cell in log phase SD medium.
Belongs to the PPP phosphatase family. PP-2B subfamily.
Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.
Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity.
Present with 7110 molecules/cell in log phase SD medium.
Was originally thought to originate from a rabbit cDNA library and was known as protein phosphatase 2Bw (PP2Bw).
Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the MCD1/SCC1 subunit of the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis.
Interacts directly with MCD1 in cohesin complex. Cohesin complexes are composed of the SMC1 and SMC3 heterodimer attached via their hinge domain, MCD1 which link them, and IRR1/SCC3, which interacts with MCD1. The cohesin complex also interacts with SCC2, which is required for its association with chromosomes. Interacts with LIN1.
Present with 4090 molecules/cell in log phase SD medium.
Belongs to the cytochrome c oxidase subunit 6B family.
Involved in the maturation of the mitochondrial respiratory chain complex IV subunit MT-CO2/COX2. Thereby, may regulate early steps of complex IV assembly. Mitochondrial respiratory chain complex IV or cytochrome c oxidase is the component of the respiratory chain that catalyzes the transfer of electrons from intermembrane space cytochrome c to molecular oxygen in the matrix and as a consequence contributes to the proton gradient involved in mitochondrial ATP synthesis. May also be required for efficient formation of respiratory supercomplexes comprised of complexes III and IV.
The Cx9C/Cx10C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system and the subsequent transfer of disulfide bonds by dithiol/disulfide exchange reactions to the newly imported protein.
Required for normal microtubule organization.
Interacts with phosphatidylinositol 3-phosphate.
Belongs to the eukaryotic ribosomal protein eL36 family.
Present with 5370 molecules/cell in log phase SD medium.
Belongs to the actin family. ARP1 subfamily.
Core component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding (By similarity). The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. ARP1 forms the backbone filament of the dynactin rod structure and serves as the scaffold for the remaining subunits. Required for proper orientation of the mitotic spindle.
Present with 1580 molecules/cell in log phase SD medium.
Self-associates to form an actin-like filament of 8-10 monomers. Component of the dynactin complex composed of at least ARP1, JNM1, NIP100 and ARP10. Dynactin comprises a short rod of the ARP1 filament attached to ARP10 at its pointed-end and probably associated with the capping protein at its barbed-end. The rod is implicated in dynein cargo binding. A sidearm formed by NIP100 projects from the ARP1 filament and is implicated in motor binding (By similarity).
Plays a role in the sorting and targeting of vacuolar proteases.
Present with 6080 molecules/cell in log phase SD medium.
3'-5' RNA exonuclease that trims the 3' end of oligo(U) tracts of the pre-U6 small nuclear RNA (snRNA) molecule, leading to the formation of a U6 snRNA 3' end-terminated with a 2',3'-cyclic phosphate (PubMed:28887445). In a second step acts as a cyclic phosphodiesterase that hydrolyzes a U6 snRNA 3' end-terminated with a 2',3'-cyclic phosphate to a U6 snRNA 3'-end-terminated with a 3' phosphate (PubMed:28887445, PubMed:22899009). Participates in the U6 snRNA 3' end processing that prevents U6 snRNA degradation (PubMed:28887445, PubMed:23190533, PubMed:22899009). Could be involved in aerobic respiration (PubMed:14690591).
Belongs to the 2H phosphoesterase superfamily. USB1 family.
Present with 6780 molecules/cell in log phase SD medium.
Putative uridine kinase identified in a screen for mutants with increased levels of rDNA transcription.
Part of the multisubunit TRAPP (transport protein particle) II complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33, TRS65, TRS120 and TRS130. Interacts directly with TRS65.
Specific subunit of the TRAPP II complex, a highly conserved vesicle tethering complex that functions in the late Golgi as a guanine nucleotide exchanger (GEF) for the Golgi YPT1 GTPase. TRS120 plays a role in the YPT GEF activity of TRAPP II in concert with the two other TRAPP II-specific subunits TRS65 and TRS130.
Involved in MBF1-mediated mitochondrial morphogenesis.
Present with 4110 molecules/cell in log phase SD medium.
Component of the mitochondrial inner membrane i-AAA protease supercomplex composed of MGR1, MGR3 and YME1. With MGR3, forms a subcomplex that binds to YME1 and to substrates to facilitate proteolysis. Interacts directly with YME1.
Component of the mitochondrial inner membrane i-AAA protease supercomplex required for mitochondrial inner membrane protein turnover. Together with MGR3, functions in an adapter complex that targets substrates to the i-AAA protease for degradation. Required for growth of cells lacking the mitochondrial genome.
Present with 3410 molecules/cell in log phase SD medium.
Belongs to the eukaryotic ribosomal protein eL8 family.
Binds to the C'/D and B/C motifs in U3 snoRNA. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1. Binds to the 5'-stem-loop of U4 snRNA. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.
Common component of the spliceosome and rRNA processing machinery. In association with the spliceosomal U4/U6.U5 tri-snRNP particle, required for splicing of pre-mRNA. In association with box C/D snoRNPs, required for processing of pre-ribosomal RNA (rRNA) and site-specific 2'-O-methylation of substrate RNAs. Essential for the accumulation and stability of U4 snRNA, U6 snRNA, and box C/D snoRNAs.
Belongs to the universal ribosomal protein uS14 family.
Present with 573 molecules/cell in log phase SD medium.
Required for the degradation of gamma-aminobutyric acid (GABA), which is important for utilization of GABA as nitrogen source and for oxidative stress tolerance. Deaminates GABA to succinate semialdehyde, which in turn is converted to succinate by the succinate-semialdehyde dehydrogenase UGA2. Cannot transaminate beta-alanine (BAL).
Subject to nitrogen catabolite repression. Expression is low in the presence of the preferred nitrogen sources, and up-regulated by GABA.
Belongs to the aconitase/IPM isomerase family.
Catalyzes the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.
Constitutively expressed with a small induction when both glutamate and lysine are missing.
Has very little effect on growth on nonfermentable carbon sources.
Present with 4670 molecules/cell in log phase SD medium.
The fermenting yeast S.cerevisiae has 2 aconitases, ACO1 essential for the citric acid cycle, and ACO2 specifically and exclusively contributing to lysine biosynthesis. In contrast, in respiring filamentous fungi the ACO2 homologs (acoB) seem enzymatically inactive and the ACO1 homolog (acoA) is solely responsible for these functions.
Inhibition of cell growth. Defects in processing of the rRNA components of the 60S ribosomal subunit and accumulation of the corresponding polyadenylated pre-rRNAs. Some delay in the maturation of the 35S primary transcript and 32S pre-rRNA. Delay in 20S pre-rRNA formation and a severe delay in mature 25S and 5.8S rRNA formation, with accumulation of the 35S, 32S, 27S, 26S and 7S pre-rRNAs and a 5' extended form of the 25S rRNA. Complete loss of synthesis of the mature 25S rRNA. Appearance at a low level of aberrant 23S species. Shorter 18S and 5.8S rRNA at the 5' end. Imbalance in the 40S:60S ratio and defects in progression beyond the 27S stage of 25S rRNA maturation during 60S biogenesis. Decreased ribosomes and polysomes and presence of halfmers.
Interacts with CBF5, FPR3, FPR4, NOP2, PIH1, RRN3, RRP6 and PAP2. Interacts with pre-60S ribosomal particles.
Late-acting factor in the nuclear maturation of 60S ribosomal subunits, which is required for normal acquisition of export competence. Required for the export of the large subunit. Acts to stimulate the RNase activity of the exosome complex, and may recruit the exosome to 7S pre-rRNA for processing. Associates with numerous RNAs including the 27S and 7S pre-rRNAs and the box H/ACA snoRNA snR37. Also interacts (via N-terminal region) with the mature 25S rRNA and the mature 5.8S rRNA.
Present with 1600 molecules/cell in log phase SD medium.
Exhibits cold sensitivity and leads to internal accumulation of precursor CPY.
Functions in the SND pathway, a SRP (signal recognition particle) and GET (guided entry of tail-anchored proteins) independent pathway for targeting a broad range of substrate proteins to the endoplasmic reticulum. SND functions in parallel to GET in targeting proteins with downstream hydrophobic motifs (PubMed:27905431). Involved in vacuolar processing and morphology (PubMed:21912603).
Interacts with SND1, PHO88/SND3 and the translocon complex subunit SEC61. ENV10/SND2 and PHO88/SND3 form a complex with the translocon in the endoplasmic reticulum membrane.
Component of the SWR1 chromatin-remodeling complex composed of at least ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4, SWC5, SWC7 and SWR1, and perhaps BDF1. Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, TRA1 and YNG2. Interacts with YAF9. Interacts with EAF1.
Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair.
Present with 2230 molecules/cell in log phase SD medium.
Binds 3 calcium ions via the second, third and fourth EF-hand.
Present with 7160 molecules/cell in log phase SD medium.
Regulator of phosphatidylinositol 4-kinase PIK1.
Displays elevated rates of loss of heterozygosity (LOH) (PubMed:18562670). A combined deletion of the LOH1/OSW4 and IRC18/OSW6 has reduced dityrosine incorporation in the outer spore wall (PubMed:23966878).
During sporulation. Repressed during vegetative growth by HST1 and RFM1.
Involved in spore wall assembly (PubMed:23966878). May be involved in maintaining genome integrity (PubMed:18562670).
Could be the product of a pseudogene. Although strongly related to DNA helicases, it lacks the helicase domains, suggesting that it has no helicase activity.
Interacts with MBA1. Binds to mitoribosomes in order to recruit them to the mitochondrial inner membrane.
Involved in mitochondrial potassium homeostasis through the mitochondrial K(+)/H(+) exchange regulation (PubMed:11907266, PubMed:15138253). With MBA1, plays a role in ribosomal translation and protein insertion into the inner membrane (PubMed:20427570).
Leads to the absence of respiratory complexes III and IV in mitochondrial inner membrane when MBA1 is also missing.
Present with 7390 molecules/cell in log phase SD medium.
The matrix-exposed C-terminus contains a 14-3-3-like domain which is necessary and sufficient for interaction with mitochondrial ribosomes.
Necessary for the structural stability of L-A double-stranded RNA-containing particles. Necessary for growth at 37 degrees Celsius as well as for maintenance of the killer plasmid.
Belongs to the snRNP Sm proteins family. SmF/LSm6 subfamily.
Component of the Sm core complex, present in spliceosomal snRNP U1, U2, U4/U6 and U5. The core complex contains SMB1, SMD1, SMD2, SMD3, SME1, SMX3 and SMX2 (Sm proteins B, D1, D2, D3, E, F and G, respectively), and is probably a heptameric ring structure. SMX3 specifically interacts with SME1. Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (By similarity).
Present with 2570 molecules/cell in log phase SD medium.
Causes lethality under aerobic growth conditions (PubMed:16630279, PubMed:29773647). Affects the methyl sterol oxidase reaction performed by the C4-methylsterol monooxygenase ERG25 and leads to an increase in intermediate sterols and a corresponding decrease in zymosterol and ergosterol production (PubMed:29773647). Impairs Fe-S cluster synthesis via increased degradation of YFH1 (PubMed:29773647). Leads to increased mitochondrial oxidants (PubMed:29773647). Leads to an increased accumulation of iron from the culture media (PubMed:23892078).
Part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:23892078). ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25 (PubMed:23892078). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672).
Plays a role in maintaining mitochondrial and plasma membrane integrity and consequently impacting the iron homeostasis, respiratory metabolism and antioxidant response (PubMed:9180083, PubMed:16135527, PubMed:16630279, PubMed:23892078, PubMed:29773647).
Present with 2950 molecules/cell in log phase SD medium.
Involved in the clustering of telomeres at the nuclear periphery, forming discrete subcompartments that accumulate a complex of histone-binding silencing factors like SIR4. Required for SIR4-mediated anchoring and partitioning of plasmids.
Belongs to the histone-like Alba family.
Component of nuclear RNase P and RNase MRP complexes. RNase P consists of an RNA moiety and at least 9 protein subunits including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RPP1 and RPR2. RNase MRP complex consists of an RNA moiety and at least 10 protein subunits including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RMP1, RPP1 and SNM1, many of which are shared with the RNase P complex.
Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.
Activated through localization to mitochondria in specific growth phases.
Belongs to the neutral sphingomyelinase family.
Eliminates endogenous IPS-PLC activities.
Responsible for the hydrolysis of the phosphosphingolipids (IPS), inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide (MIPC), and mannosyldiinositol phosphorylceramide (M(IP)2C) (PubMed:11006294). Regulates sphingolipid metabolism in mitochondria, especially the formation of alpha-hydroxylated very long chain phytoceramides. The generated ceramides contribute to the normal function of mitochondria (PubMed:17880915). Also active on sphingomyelin (SM), but this activity is probably not physiologically relevant (PubMed:11006294).
Component of the 7-subunit TFIIH core complex composed of XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in NER. The core complex associates with the 3-subunit CTD-kinase module TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription.
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
Present with 2340 molecules/cell in log phase SD medium.
Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl-tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it binds methionyl-tRNAi to 40S subunits in a codon-dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a GTP-dependent manner. Specifically associates with both 40S subunits and 80S ribosomes.
Ubiquitinated, probably leading to its degradation. May explain why it has a short half-life of 17 minutes.
Required for the nitrogen-regulated transport of amino acid permeases GAP1 and PUT4 from the Golgi to the cell surface.
Sensitive to high hydrostatic pressure (mechanical stress).
Acts as essential component of the kinetochore MIND complex, which is required for the spindle checkpoint and kinetochore integrity. MIND plays a role in establishing a bipolar spindle-kinetochore interaction by joining kinetochore subunits contacting DNA to those contacting microtubules. NSL1 facilitates the attachment of two of the DASH complex components, DAD2 and SPC19, to the kinetochore in a microtubule-dependent manner.
Component of the MIND kinetochore complex, which is composed of at least MTW1, NNF1, NSL1 and DSN1. Interacts with DSN1.
Present with 3710 molecules/cell in log phase SD medium.
Component of the CHS5/6 complex composed of the 4 CHAPS proteins BCH1, BCH2, BUD7, and CHS6 as well as at least CHS5 and GTP-bound ARF1. The complex interacts with the cargo protein CHS3.
Member of the CHS5-ARF1P-binding proteins (CHAPS) which mediates export of specific cargo proteins, including chitin synthase CHS3.
Present with 2540 molecules/cell in log phase SD medium.
Belongs to the universal ribosomal protein uL1 family.
Present with 7000 molecules/cell in log phase SD medium.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily.
Negative regulator of the cell cycle acting downstream of the cAMP-dependent protein kinase. Part of a glucose-sensing system involved in growth control in response to glucose availability. Phosphorylates POP2.
Ty1-LR4 is a highly expressed element. Induced under amino acid starvation conditions by GCN4.
Component of the RENT complex which is composed of at least NET1, CDC14 and SIR2 (PubMed:12056824, PubMed:11511359). Interacts with NSI1 (PubMed:22362748).
Has a role in chromosome maintenance and is involved in mitotic exit. Inhibits the action of CDC14 by sequestering it in the nucleolus. Also binds to RNA polymerase I and stimulates rRNA synthesis. Influences RDNA chromatin by tethering SIR2 to rDNA in the nucleolus.
Present with 1590 molecules/cell in log phase SD medium.
Component of the pheromone signal transduction pathway. It mediates pheromone signals acting between STE20 and STE11. It is absolutely required for pheromone-induced transcription of FUS1. May play a role in cell-cycle arrest in response to pheromone.
May be regulated at the phosphorylation level, and by the mating type of the cell and depends on an intact pheromone-response pathway.
Acts as component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. NOT2 is required for the integrity of the complex. The NOT protein subcomplex negatively regulates the basal and activated transcription of many genes. Preferentially affects TC-type TATA element-dependent transcription. Could directly or indirectly inhibit component(s) of the general transcription machinery.
Forms a NOT protein complex that comprises NOT1, NOT2, NOT3, NOT4 and NOT5. Subunit of the 1.0 MDa CCR4-NOT core complex that contains CCR4, CAF1, NOT1, NOT2, NOT3, NOT4, NOT5, CAF40 and CAF130. In the complex interacts with NOT1 and NOT5. The core complex probably is part of a less characterized 1.9 MDa CCR4-NOT complex.
Component of the PAF1 complex which consists of at least CDC73, CTR9, LEO1, PAF1 and RTF1. Interacts with FACT subunits POB3 and SPT16.
Belongs to the glutaredoxin family. YDR286C subfamily.
Interacts with SKP1. Component of the probable SCF(DAS1) complex containing CDC53, SKP1, RBX1 and DAS1.
Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins (By similarity).
Component of the origin recognition complex (ORC) composed of at least ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. Interacts with ORC3, ORC5 and TAH11.
It is uncertain whether Met-1 or Met-3 is the initiator.
Component of the HIR complex, composed of HIR1, HIR2, HIR3 and HPC2 (PubMed:16264190, PubMed:16303565, PubMed:9001207, PubMed:9504914). This complex may consist of one copy of HIR1 and HIR3 and two copies of HIR2 and HPC2 (PubMed:16264190). The HIR complex interacts with ASF1 (PubMed:11404324, PubMed:11412995). Interacts with SNF2 (PubMed:10445029). Interacts with SNF5 (PubMed:10445029). Interacts with SWI3 (PubMed:10445029). Interacts with RTT106 (PubMed:19683497). May interact with SPT4 (PubMed:9504914). May self-associate (PubMed:9504914).
Component of the HIR complex, which cooperates with ASF1 to promote replication-independent chromatin assembly. The HIR complex is also required for the periodic repression of three of the four histone gene loci during cell cycle as well as for autogenous regulation of the HTA1-HTB1 locus by H2A and H2B. DNA-binding by the HIR complex may repress transcription by inhibiting nucleosome remodeling by the SWI/SNF complex. The HIR complex may also be required for transcriptional silencing of centromeric, telomeric and mating-type loci in the absence of CAF-1.
Decreases nucleosomal density (PubMed:19683497). Increases HTA1 RNA level; simultaneous disruption RTT109 alleviates the effect (PubMed:19683497). Abolishes localization of RTT106 to the HTA1-HTB1 promoter (PubMed:19683497).
Belongs to the GHMP kinase family. GalK subfamily.
Associates with translating polyribosomes. Interacts with GIR2, TMA46, YAP1 and YGR250C.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.
Present with 11700 molecules/cell in log phase SD medium.
Present with 3280 molecules/cell in log phase SD medium.
Induced under aerobic conditions and repressed under anaerobic conditions.
The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble form, and which forms a parallel in-register beta-sheet in its amyloid form.
Transcription factor that affects the expression of a large set of genes. Recognizes and binds to the consensus sequence 5'-[CAT]AGG[TC]A-3' in the promoter region. Plays a major role in the repression of a specific subset of hypoxic genes (e.g. ANB1, DAN1 and HEM13) under aerobic conditions. Acts synergistically with the transcription factor ROX1 to recruit the general repression complex SSN6-TUP1 to the promoter of hypoxic genes. Represses transcription of ergosterol biosynthetic genes. Negatively regulates pheromone-induced gene expression. Can act as a transcriptional activator (e.g. of genes like CYC1, SUC2 and the Ty long terminal repeat delta promoter).
[MOT3+] is the prion form of MOT3. [MOT3+] is the result of a conformational change of the cellular MOT3 protein that becomes self-propagating and infectious. This conformational change generates a form of MOT3 that assembles into amyloid fibrils. [MOT3+]-aggregates sequester soluble MOT3, resulting in a loss-of-function phenotype for MOT3. [MOT3+] can be cured by GdnHCl and by inactivation of the molecular chaperone HSP104, which is required for [MOT3+] propagation. It is speculated that prion properties of transcription factors may generate an optimized phenotypic heterogeneity that buffers yeast populations against diverse environmental insults.
Present with 892 molecules/cell in log phase SD medium.
Acts as component of the general transcription and DNA repair factor IIH (TFIIH or factor B), which is essential for both basal and activated transcription, and is involved in nucleotide excision repair (NER) of damaged DNA. TFIIH has CTD kinase and DNA-dependent ATPase activity, and is essential for polymerase II transcription in vitro.
Component of the transcription factor IIH (TFIIH) holo but not the TFIIH core complex. Component of a complex consisting of KIN28, CCL1 and TFB3; the KIN28-CCL1 dimer is known as the TFIIK complex.
Present with 3050 molecules/cell in log phase SD medium.
Component of the Arp2/3 complex composed of ARP2, ARP3, ARC40/p41-ARC, ARC35/p34-ARC, ARC18/p21-ARC, ARC19/p20-ARC and ARC16/p16-ARC.
Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.
Component of a peripheral membrane protein complex consisting of DSL1, SEC39/DSL3 and TIP20. Bound to a SNARE complex consisting of UFE1, USE1, SEC20 and SEC22 or YKT6 through direct interaction of TIP20 with SEC20. Binds the coatomer complex through direct interaction with RET2/COPD and RET1/COPA. Binds TIP20 and SEC39/DSL3.
Present with 8970 molecules/cell in log phase SD medium.
Required for protein transport between the Golgi and the endoplasmic reticulum. May tether coatomer-coated retrograde transport vesicles to the ER membrane through interaction with coatomer as well as the SNARE complex. May contribute to the stabilization of the SNARE complex.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
Interacts with NOP53. Interacts with TRM112.
Present with 18700 molecules/cell in log phase SD medium.
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 2870 (m5C2870) in 25S rRNA. Required for 60S ribosomal subunit synthesis and processing.
Component of the Smc5-Smc6 complex which consists of KRE29, MMS21, NSE1, NSE3, NSE4, NSE5, SMC5 and SMC6. Interacts with NSE3.
Interacts (via its WD repeats) with ubiquitin.
Present with 589 molecules/cell in log phase SD medium.
The N-terminal WD repeats are involved in ubiquitin-binding.
Ubiquitin-binding protein involved in the resistance to phenanthroline, sanguinarine, nordihydroguaiaretic acid (NDGA), isopropyl (N-3-chloro-phenyl)-carbamate (IPCPC) and guanosine 5'-O-(2-thiodiphosphate).
Belongs to the eukaryotic NMN adenylyltransferase family.
Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate to form deamido-NAD(+) (NaAD). Key enzyme in both de novo and salvage pathways for NAD(+) biosynthesis. Predominantly acts in the salvage pathways via NMN.
Expression is high in early log-phase and significantly drops as cells enter late log phase.
Present with 5130 molecules/cell in log phase SD medium.
Belongs to the universal ribosomal protein uS13 family.
Present with 112000 molecules/cell in log phase SD medium.
Present with 48100 molecules/cell in log phase SD medium.
Belongs to the SMC family. SMC2 subfamily.
Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.
Forms a heterodimer with SMC4. Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: BRN1, YCS4 and YCG1/YCS5.
Present with 3290 molecules/cell in log phase SD medium.
The flexible SMC hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with SMC4, forming a V-shaped heterodimer.
Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily.
Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NBP35 and two labile, bridging clusters between subunits of the NBP35-CFD1 heterotetramer.
Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery (PubMed:12970194, PubMed:15660135, PubMed:17401378). Required for maturation of extramitochondrial Fe-S proteins (PubMed:12970194, PubMed:15660135, PubMed:17401378, PubMed:22362766, PubMed:31040179). The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins (PubMed:17401378, PubMed:22362766). Nucleotide binding/hydrolysis seems to be critcal for loading of Fe-S clusters onto CFD1 and NBP35 (PubMed:22362766). Required for biogenesis and export of both ribosomal subunits, which may reflect a role in assembly of the Fe/S clusters in RLI1, a protein which performs rRNA processing and ribosome export (PubMed:15660135).
Heterotetramer of 2 NBP35 and 2 CFD1 chains.
Inviable (PubMed:12970194). Decreases cytosolic iron-sulfur (Fe-S) protein assembly (PubMed:31040179).
Encoded from partially processed COB mRNA that terminates with the in-frame coding sequence of the third intron.
Forms a ribonucleoprotein complex composed of maturase bI3 and 2 dimers of MRS1 that assemble around the bI3 RNA.
In the C-terminal section; belongs to the LAGLIDADG endonuclease family.
In the N-terminal section; belongs to the cytochrome b family.
Mitochondrial mRNA maturase required for splicing of intron 3 of the cytochrome b (COB) gene, containing its own coding sequence. In vivo splicing requires the formation of a ribonucleoprotein complex together with the imported mitochondrial RNA-splicing protein MRS1. The complex seems to stimulate the intrinsic ribozyme activity of intron bI3 through binding to and stabilizing specific secondary and tertiary structure elements in the RNA.
By aromatic amino acids in the growth medium. Expression also induced in ARO8 mutants grown on minimal ammonia medium.
General aromatic amino acid transaminase involved in several otherwise unrelated metabolic pathways. Mainly involved in tryptophan degradation. Active with phenylalanine, tyrosine and tryptophan as amino donors and with phenylpyruvate, hydroxyphenylpyruvate and pyruvate as amino acceptors. Does not accept glutamate or 2-oxoglutarate as substrates. Also active with methionine, leucine, glutamine and kynurenine. Catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) in the methionine salvage pathway primarily using aromatic amino acids (tyrosine, phenylalanine and tryptophan) as the amino donors. Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA) with pyruvate as amino acceptor.
Acts together with EMP24 and ERV25 in cargo exit from the endoplasmic reticulum.
Belongs to the XRCC4-XLF family. XLF subfamily.
Interacts with the BRCT domain of DNL4 and with NEJ1. The DNL4-LIF1 complex interacts with POL4.
Present with 876 molecules/cell in log phase SD medium.
Stabilizes DNL4. Involved in non-homologous repair of DNA double-strand breaks.
During meiosis is involved in homologous recombination and during vegetative growth it is necessary for DNA repair. It probably regulates the 5'-3' exonuclease degradation of double strand breaks either at the initiation stage or a later stage.
Belongs to the acetyltransferase family.
Component of the N-terminal acetyltransferase A (NatA) complex, which is composed of ARD1, NAT1 and NAT5.
N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (PubMed:25886145). Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides (PubMed:25886145). Non-essential component of the NatA N-terminal acetyltransferase (PubMed:14517307).
Belongs to the uroporphyrinogen decarboxylase family.
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Present with 9220 molecules/cell in log phase SD medium.
Belongs to the metallo-dependent hydrolases superfamily. TatD-type hydrolase family.
Binds 2 divalent metal cations per subunit.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. ASM4 may form a subcomplex with NUP53, NDC1, and NUP170.
Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. FG repeat types and their physico-chemical environment change across the NPC from the nucleoplasmic to the cytoplasmic side.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). May have a mitosis control function (By similarity).
Present with 2740 molecules/cell in log phase SD medium.
The RRM Nup35-type domain might be involved in the control of mitosis.
Belongs to the HDA2/3 family. HDA3 subfamily.
Heterodimer with HDA2. Component of the HDA1 histone deacetylase complex composed of at least one HDA1 homodimer and one HDA2/HDA3 heterodimer. Interacts with HDA1 and HDA3.
Present with 1100 molecules/cell in log phase SD medium.
Required for activity of HDA1 histone deacetylase complex. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.
Interacts with HSL1 and SWE1. Interacts with the amino-terminal regulatory domain of STE20.
Phosphorylated in a cell cycle-dependent manner.
Present with 1180 molecules/cell in log phase SD medium.
S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that can catalyze both the mono- and symmetric (type II) dimethylation of the guanidino nitrogens of arginine residues in target proteins (PubMed:18515076). Involved in the control of the cell cycle at the G2/M (mitosis) transition. Cooperates with HSL1 to hyperphosphorylate SWE1, thereby targeting SWE1 for polyubiquitination and subsequent degradation (PubMed:10490630, PubMed:10490648). Acts as a negative regulator of the filamentous growth-signaling pathway through inhibition of STE20 (PubMed:10411908).
Involved in mRNA splicing. Helps to stabilize the U1 snRNP-5' splice site interaction.
Involved in sporulation and affects the sphingolipid composition of the plasma membrane. Probably involved in endocytosis.
Present with 17000 molecules/cell in log phase SD medium.
Belongs to the methyltransferase superfamily. METL family.
Mitochondrial methyltransferase which suppresses respiratory defects caused by OXA1 mutations when overexpressed.
Present with 1430 molecules/cell in log phase SD medium.
Belongs to the chorismate synthase family.
Present with 2310 molecules/cell in log phase SD medium.
Homodimer (Probable). Interacts (via SAM domain) with STE50 (via SAM domain). Interacts with PBS2 and SHO1.
Serine/threonine protein kinase required for cell-type-specific transcription and signal transduction in yeast. It is thought that it phosphorylates the STE7 protein kinase which itself, phosphorylates the FUS3 and or KSS1 kinases.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. Binds to the nuclear basket of the NPC through NUP60 in a (GSP1, GSP2) GTPase-GTP-dependent manner. Interacts through its FG repeats with nuclear transport factors. Interacts with KAP122.
Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. FG repeat types and their physico-chemical environment change across the NPC from the nucleoplasmic to the cytoplasmic side: FXFG repeats are especially abundant in NUPs on the nucleoplasmic side (in a highly charged environment and enriched in Ser and Thr).
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). As one of the FG repeat nucleoporins NUP2 is involved in interactions with and guidance of nuclear transport receptors such as SRP1-KAP95 (importin alpha and beta) through the NPC. Like the closely related NUP1 it also plays an important role in disassembling and recycling SRP1-KAP95 to the cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1-KAP95-cargo complex in the nucleus, NUP2 binds through its N-terminus to the SRP1 nuclear localization signal (NLS) binding site, thus accelerating the release of the NLS-cargo. SRP1 in turn is released from NUP2 by binding of the GSP1-GTP associated export factor CSE1. NUP2 may also have a chromatin boundary/insulator activity through indirect interaction with genomic DNA via CSE1 and blocking of heterochromatin spreading.
Present with 2960 molecules/cell in log phase SD medium.
Present with 14600 molecules/cell in log phase SD medium.
Effector of VPS34 phosphatidylinositol 3-phosphate kinase signaling. Regulates the cytoplasm to vacuole transport (Cvt) vesicle formation. Plays a role in ATG protein retrieval from the pre-autophagosomal structure (PAS) and is especially required for autophagy-dependent cycling of ATG9.
Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.
Expressed during the transition between the late exponential and stationary growth phases, coincident with maximal glycogen accumulation.
Present with 1230 molecules/cell in log phase SD medium.
Belongs to the adenylyl cyclase class-3 family.
Plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP.
The presence of GTP-bound RAS2 protein is required in order to elicit a magnesium-dependent adenylyl cyclase activity.
Activated by a monovalent cation that binds near, but not in, the active site. The most likely occupant of the site in vivo is potassium. Ion binding induces a conformational change that may alter substrate affinity.
Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.
Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
Present with 1780 molecules/cell in log phase SD medium.
Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Component of the cell wall. Required for anaerobic growth.
In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis.
Present with 91600 molecules/cell in log phase SD medium.
Strongly inhibited by the polyol (sugar alcohol) phosphate D-glucitol 6-phosphate (D-sorbitol 6-phosphate) (PubMed:30240188). Also inhibited by the polyol (sugar alcohol) phosphate D-ribitol 5-phosphate (PubMed:30240188).
Belongs to the cytochrome c oxidase VIIa family.
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Alpha(2)-beta(2). The alpha component is a flavoprotein, the beta component is a hemoprotein.
Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
Catalyzes the reduction of sulfite to sulfide, one of several activities required for the biosynthesis of L-cysteine from sulfate.
Activated by tyrosine and threonine phosphorylation by MKK1 and MKK2.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.
Dually phosphorylated on Thr-190 and Tyr-192, which activates the enzyme.
Present with 3230 molecules/cell in log phase SD medium.
Serine/threonine protein kinase involved in a signal transduction pathway that plays a role in yeast cell morphogenesis and cell growth. This pathway seems to start by SMP3; then involve the kinase PKC1 that may act the BCK1 kinase that then phosphorylates MKK1 and MKK2 which themselves phosphorylate the SLT2/MPK1 kinase which itself then phosphorylates and activates the transcription factor RLM1. Directly phosphorylates BCY1 upon TOR complex 1 (TORC1) inhibition.
The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
t-SNARE that functions in transport from the endosome to the late Golgi and on the endocytic pathway.
Belongs to the AB hydrolase superfamily.
Mediates the hydrolysis of steryl esters, thereby playing a central role in lipid metabolism. Under heme-deficient conditions, it constitutes the major steryl ester hydrolase, suggesting that it plays a central role in mobilization of steryl esters under anaerobic conditions.
Under heme-deficiency conditions. Heme-deficient induction requires ROX3.
Required for survival upon exposure to K1 killer toxin. Involved in the resistance to unfolded protein response (UPR)-inducing agents.
Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1. Interacts with PRP38.
Component of the spliceosome and rRNA processing machinery. In association with the spliceosomal U4/U6.U5 tri-snRNP particle, required for splicing of pre-mRNA.
Present with 2510 molecules/cell in log phase SD medium.
Present with 7750 molecules/cell in log phase SD medium.
Transcriptional modulator with roles in meiotic regulation and silencing. Acts either as an adapter to facilitate nuclear import by KAP122 of the RNR2-RNR4 herodimer, also called beta-beta' subunit, which corresponds to the small subunit of the ribonucleotide reductase (RNR); or as an anchor to retain RNR2-RNR4 in the nucleus.
Homodimer; disulfide-linked. Interacts with RNR1.
Phosphorylated by DUN1, a downstream effector of the Mec1/Rad53 checkpoint pathway, in response to DNA damage. This promotes ubiquitination of SML1 and targets it for degradation by the 26S proteasome.
Present with 18800 molecules/cell in log phase SD medium.
Strong inhibitor of ribonucleotide reductase (RNR1) and is involved in regulating dNTP production.
Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit family.
Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. RPB4 and RPB7 form a subcomplex that protrudes from the 10-subunit Pol II core complex. The RPB4-RPB7 subcomplex probably associates with TFG1. Interacts with NRD1 and PAT1.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB7 is part of a subcomplex with RPB4 that binds to a pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The RPB4-RPB7 subcomplex binds single-stranded DNA and RNA. The RPB4-RPB7 subcomplex recruits FCP1 to Pol II.
Present with 6420 molecules/cell in log phase SD medium.
Mediates the formation of endoplasmic reticulum (ER)-mitochondria encounter structure (ERMES) foci, thereby contributing to the formation of ER-mitochondrial contact sites.
Belongs to the TRAPP small subunits family. BET5 subfamily.
Component of the TRAPP I, TRAPP II and TRAPP III complexes which act as guanine nucleotide exchange factors (GEF) for YPT1. TRAPP I plays a key role in the late stages of endoplasmic reticulum to Golgi traffic. TRAPP II plays a role in intra-Golgi transport. TRAPP III plays a role in autophagosome formation. Required for sporulation. Has a role late in meiosis following DNA replication.
Part of the multisubunit TRAPP (transport protein particle) I complex composed of BET3, BET5, TRS20, TRS23, TRS31 and TRS33. Part of the multisubunit TRAPP (transport protein particle) II complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33, TRS65, TRS85, TRS120 and TRS130. Part of the multisubunit TRAPP (transport protein particle) III complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33 and TRS85.
Involved in microtubule stability and kinetochore function. May be involved in protein N-terminus acetylation and/or proteasome biogenesis.
Riboflavin transporter involved in riboflavin (vitamin B2) uptake. Does not act in the transport of monocarboxylic acids across the plasma membrane.
Acts in signal transduction. Activates CDC42 and RHO5.
Present with 1750 molecules/cell in log phase SD medium.
Belongs to the eukaryotic ribosomal protein eS12 family.
Belongs to the class-I aminoacyl-tRNA synthetase family.
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Present with 996 molecules/cell in log phase SD medium.
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria (PubMed:19556461). Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria (PubMed:8089172, PubMed:9628893, PubMed:27469264). The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex (PubMed:17410204). Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids (PubMed:11266455, PubMed:12454062, PubMed:14981098).
Homodimer (By similarity). Component of the ER-mitochondria encounter structure (ERMES) or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34 (PubMed:13679517, PubMed:17410204, PubMed:19556461). A MMM1 homodimer associates with one molecule of MDM12 on each side in a pairwise head-to-tail manner, and the SMP-LTD domains of MMM1 and MDM12 generate a continuous hydrophobic tunnel for phospholipid trafficking (By similarity).
Loss of mitochondrial integrity (PubMed:26370498). Abolishes growth on non-fermentable carbon source (glycerol with ethanol) (PubMed:26370498, PubMed:27280386). Slow growth on fermentable carbon source (glucose) (PubMed:26370498, PubMed:27280386). Synthetic lethal with VPS13 (PubMed:26370498, PubMed:27280386).
Present with 2490 molecules/cell in log phase SD medium.
The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers.
Was originally (PubMed:12972421 and PubMed:8089172) proposed to be inserted into either the outer or inner mitochondrial membrane, yet more recent data indicates that it is instead inserted into the ER.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YLR227W-A ORF.
Appears to modulate the timing of budding to obtain an appropriate cell size independent of the DNA replication cycle. Transcription factor involved in both heat resistance and flocculation.
Present with 937 molecules/cell in log phase SD medium.
Involved in pheromone-induced morphogenesis and efficient mating, perhaps as a cytoskeletal protein.
Present with 274 molecules/cell in log phase SD medium.
Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family.
With EMP70 and TMN3, plays a critical role in the late stages of a nutrient-controlled pathway notably regulating FLO11 gene expression. Acts downstream of RAS2 and TOR. Essential for cell adhesion and filamentous growth. May play a role as effector of cellular copper homeostasis.
Present with 432 molecules/cell in log phase SD medium.
Required for arginine biosynthesis. Transports ornithine synthesized from glutamate in the mitochondrial matrix to the cytosol, where it is converted to arginine.
May be involved in actin cytoskeleton organization and biogenesis.
Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty2 RNA and initiation of reverse transcription (By similarity).
Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein, and this cleavage is a prerequisite for subsequent processing at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity).
Produced by +1 ribosomal frameshifting between codon Leu-431 and Gly-432 of the YOR343W-A ORF.
Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty2 retrotransposons belong to the copia elements (pseudoviridae).
Belongs to the universal ribosomal protein uS17 family.
Present with 1200 molecules/cell in log phase SD medium.
Has actin-binding and actin-bundling activity. Stabilizes actin filaments against disassembly.
Present with 1578 molecules/cell in log phase SD medium.
Belongs to the histone deacetylase family. HD type 1 subfamily.
Present with 4420 molecules/cell in log phase SD medium.
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity).
Expressed periodically during the glycolytic and respiratory oscillations cycles.
Hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce N-acylethanolamines (NAEs).
Present with 178 molecules/cell in log phase SD medium.
Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by guanine nucleotide-exchange factor (GEF) CDC25 and inactivated by GTPase-activating proteins (GAPs) IRA1 and IRA2.
Belongs to the small GTPase superfamily. Ras family.
Farnesylated by RAM1-RAM2, which is required for targeting RAS2 to the cytoplasmic site of the endoplasmic reticulum, where proteolytic processing of the C-terminus by RCE1 and methylation of the resulting carboxyl group by STE14 occurs.
Palmitoylated by the ERF2-SHR5 complex, which is required for proper plasma membrane localization of RAS2.
Present with 19800 molecules/cell in log phase SD medium.
RAS2 is necessary for a normal response to nutrient limitations, in general, disruption of the RAS2 locus results in an overall premature starvation response.
The S.cerevisiae Ras proteins modulate the activity of the adenylate cyclase catalytic subunit and therefore affect the biosynthesis of cyclic-AMP.
May be involved in the regulation of gene expression responses of environment-sensing pathways.
Present with 1240 molecules/cell in log phase SD medium.
By multistress. Expression is controlled by the MSN2 and MSN4 transcriptional regulators.
May play an important role in the response of cells to diverse environmental stresses.
Present with 784 molecules/cell in log phase SD medium.
Thiamine-regulated, high affinity import carrier of pyridoxine, pyridoxal and pyridoxamine.
Seems to be involved in the uptake of several cations and of histidinol.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIA subfamily.
Interacts with its cargot receptor EXP1 for its transport within the cell and maturation.
Phosphorylated on multiple Ser and Thr residues.
Present with 1260000 molecules/cell in log phase SD medium.
The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses.
The prion state [GAR+] is provoked by the interaction of the two proteins STD1 and PMA1. It involves a complex between a small fraction of the cellular complement of PMA1, and STD1, a much lower-abundance protein, and it is transmissible by non-Mendelian, cytoplasmic inheritance. [GAR+] makes cells resistant to the glucose-associated repression of alternative carbon sources. In contrast to other prion forms, [GAR+] cannot be cured by GdnHCl or by inactivation of the molecular chaperone HSP104.
There are two plasma membrane ATPases in yeast. This is the major isoform.
May function in G-protein coupled signal transduction.
Present with 1400 molecules/cell in log phase SD medium.
Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity).
Present with 5410 molecules/cell in log phase SD medium.
Belongs to the transferase hexapeptide repeat family.
Belongs to the snRNP Sm proteins family.
Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step. The LSM1-LSM7 complex binds RNA with a preference for poly-U ends.
Component of the heptameric LSM1-LSM7 complex that forms a seven-membered ring structure with a donut shape. The LSm subunits are arranged in the order LSM1, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. Except for LSM1, where a C-terminal helix crosses the ring structure to form additional interactions with LSM3 and LSM6, each subunit interacts only with its two neighboring subunits. The LSM1-LSM7 complex interacts with PAT1; within the complex PAT1 has direct interactions with LSM2 and LSM3.
Present with 3490 molecules/cell in log phase SD medium.
Could be the product of a pseudogene. This is the C-terminal part of a putative glutamine--fructose-6-phosphate aminotransferase. Strain S288c has a frameshift in position 258, which disrupts the gene coding for this protein and produces two ORFs YMR084W and YMR085W. A contiguous sequence for this protein can be found in strain YJM789 (AC A6ZME2).
Forms a ternary complex with RSP5 and UBP2.
Modulates the activity of the RSP5 HECT ubiquitin-protein ligase through its mediation of the interaction between RSP5 and the deubiquitinase UBP2. Involved in regulation of cell wall homeostasis.
Present with 5930 molecules/cell in log phase SD medium.
Heterodimer; disulfide-linked (Probable). Interacts with SAG1.
Receptor binding subunit of the a-agglutinin heterodimer. S.cerevisiae a and alpha cells express the complementary cell surface glycoproteins a-agglutinin and alpha-agglutinin, respectively, which interact with one another to promote cellular aggregation during mating.
Belongs to the glutaminase PdxT/SNO family.
Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of a SNZ isoform.
Lipid transport protein (LTP) involved in non-vesicular transfer of lipids between membranes. Functions in phosphoinositide-coupled directional transport of various lipids by carrying the lipid molecule in a hydrophobic pocket and transferring it between membranes through the cytosol. Involved in maintenance of intracellular sterol distribution and homeostasis (PubMed:11238399, PubMed:15173322). May serve as a sensor of PI4P levels at PM-ER membrane contact site, regulating PI4P phosphatase SAC1 activity (PubMed:21295699). May be involved in ergosterol transport from the plasma membrane (PM) to the ER, however it does not bind sterols directly (PubMed:16585271, PubMed:23791945). Plays a role in the positive regulation of vesicular transport of ceramide from the ER to the Golgi, negatively regulating COPII-mediated ER export of cargos (PubMed:24213531).
The FFAT (two phenylalanines in an acidic tract) motif is required for interaction with SCS2 and proper localization of the protein.
The GOLD (Golgi dynamics) domain is predicted to mediate diverse protein-protein interactions.
The OSBP-related domain (ORD) mediates binding of sterols and phospholipids. It displays an incomplete beta-barrel containing a central hydrophobic tunnel that can accommodate a single lipid molecule with a flexible lid covering the tunnel entrance. The ORD can bind two membranes simultaneously. It has at least two membrane-binding surfaces; one near the mouth of the lipid-binding pocket and a distal site that can bind a second membrane. These structural features correlate with the phosphatidylinositol 4-phosphate (PI(4)P)-coupled lipid transport optimized in closely apposed membranes, such as organelle contact sites. The lipid transfer cycle starts from the association of the LTP with a donor membrane, which accompanies conformational changes that uncover the ligand-binding pocket. The tunnel opening is generally mediated by displacement of the lid covering the binding pocket allowing uptake or release of a lipid molecule. The LTPs extract the lipid from the membrane by providing a hydrophobic environment as well as specific interaction. Dissociation from the donor membrane shifts the conformation to a closed form. Then, the LTPs loaded with a cargo lipid diffuse through the aqueous phase. Lid opening may be induced by the interaction of a hydrophobic side of the lid with the target membranes (Probable). The OSH3 ORD does not accept sterols due to the small hydrophobic tunnel (PubMed:23791945).
The PH domain weakly binds to phosphoinositides.
Belongs to the class-II aminoacyl-tRNA synthetase family.
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Present with 33800 molecules/cell in log phase SD medium.
Produced by alternative initiation at 2 upstream redundant non-AUG codons in-frame of the first AUG used for isoform Cytoplasmic.
Activated by Ser-520 phosphorylation by HOG1.
Autophosphorylated. Phosphorylated by HOG1 at Ser-520 after osmotic stress.
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.
Present with 1790 molecules/cell in log phase SD medium.
Serine/threonine-protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment.
Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter.
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.
Forms a complex with CDC91, GPI17, GPI8 and GAA1.
It is uncertain whether Met-1 or Met-9 is the initiator.
The disulfide bond between GPI8 and GPI16 is important for normal enzyme activity.
Subtilisin-related protease involved in the formation of a protective dityrosine layer required for spore wall assembly. Identified in a screen for mutants with increased levels of rDNA transcription.
Transposon Ty1-A (YARCTy1-1) contains a frameshift at position 610, which disrupts the ORF coding for protein TY1B. This is the truncated, C-terminal part of TY1B translated from an in-frame start codon, and it is probably not functional.
Component of the spindle pole body (SPB), acting as the connector of microtubule arrays in the cytoplasm and the nucleoplasm, is involved in nuclear positioning before chromosome segregation, SPB separation, spindle formation, chromosome segregation, nuclear migration into the bud, nuclear reorientation after cytokinesis and nuclear fusion during conjugation. The SPB half-bridge, which is tightly associated with the cytoplasmic side of the nuclear envelope and the SPB, is playing a key role as the starting structure for and in the initiation of SPB duplication in G1. At the SPB half-bridge CDC31 interacts with KAR1, MPS3 and SFI1 (PubMed:12486115, PubMed:14504268). Interacts with KIC1 (PubMed:9813095). Interacts with VPS13 (PubMed:28122955). Associates with nuclear pore complexes (NPCs) (PubMed:10684247).
Functions as a component of the spindle pole body (SPB) half-bridge (PubMed:10684247, PubMed:11156974, PubMed:12486115, PubMed:14504268, PubMed:8070654). At the SPB, it is recruited by KAR1 and MPS3 to the SPB half-bridge and involved in the initial steps of SPB duplication (PubMed:11156974, PubMed:12486115, PubMed:14504268, PubMed:8070654). Also involved in connection with the protein kinase KIC1 in the maintenance of cell morphology and integrity (PubMed:9813095). May play a role in vesicle-mediated transport, in a VPS13-dependent manner (PubMed:28122955).
Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis.
Present with 20600 molecules/cell in log phase SD medium.
5-phosphoribose 1-diphosphate synthase involved in nucleotide, histidine, and tryptophan biosynthesis. Active in heteromultimeric complexes with other 5-phosphoribose 1-diphosphate synthases (PRS2, PRS3, PRS4 and PRS5).
Belongs to the ribose-phosphate pyrophosphokinase family.
Present with 5280 molecules/cell in log phase SD medium.
Belongs to the tellurite-resistance/dicarboxylate transporter (TDT) family.
Involved in efflux of free sulfite. Mutations in the SSU1 gene cause sensitivity to sulfite.
Component of a heterotrimeric complex containing IMP3, IMP4 and MPP10. Interacts with snoRNA U3. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3. Interacts with the SSU processome subunits EMG1, IMP3, IMP4, KRR1, NOC4/UTP19, NOP1, RPS4A, RPS4B, RPS6A, RPS6B, RPS7A, RPS7B, RPS9A, RPS9B, RPS14A, RPS14B, UTP1-UTP18, UTP20-UTP22 and UTP25.
Involved in nucleolar processing of pre-18S ribosomal RNA. Required for the early cleavages at sites A0, A1 and A2 during 18S ribosomal pre-RNA processing.
Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily.
Decreases translation of proteins required for detoxification of reactive oxygen species (PubMed:33260587). Sensitive to hydrogen peroxide (PubMed:33260587). Increases GRX1 mRNA level during vegetative growth (PubMed:33260587). Normal vegetative cell population growth on glucose, galactose, and glycerol carbon sources, at high temperature, and at standard temperature (PubMed:9778796, PubMed:33260587). Normal mating and sporulation (PubMed:9778796).
Expressed in vegetatively growing cells at very low levels.
Increases in mild (0.5 mM) hydrogen peroxide stress, and decreases in stronger (1 mM) hydrogen peroxide stress.
Ribosome-dependent ATPase that promotes the translation of proteins required for detoxification of reactive oxygen species (PubMed:33260587). Required for the ATP-dependent release of deacylated tRNA from the ribosomal E-site during protein biosynthesis (By similarity). Stimulates the eEF1A-dependent binding of aminoacyl-tRNA to the ribosomal A-site, which has reduced affinity for tRNA as long as the E-site is occupied (By similarity).
Tube-forming lipid transport protein which may bind to phosphatidylinositols and may affect phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P2) distribution.
Component of the mitochondrial inner membrane peptidase (IMP) complex which at least consists of IMP1, IMP2 and SOM1.
Non-catalytic component of the mitochondrial inner membrane peptidase (IMP) complex. IMP catalyzes the removal of signal peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. SOM1 facilitates cleavage of a subset of IMP substrates.
Accumulation of Cys-Gly dipeptide and enhanced GSH toxicity.
Catalytic component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond. Functions also in a DUG2-DUG3-independent manner as a dipeptidase with high specificity for Cys-Gly and no activity toward tri- or tetrapeptides.
Homodimer. Component of the GSH degradosomal complex composed of at least DUG1, DUG2 and DUG3.
Present with 22300 molecules/cell in log phase SD medium.
Functions as a component of the DNA-binding general transcription factor complex TFIID, the RNA polymerase II associated general transcription factor complex TFIIF, and the chromatin-remodeling complex SWI/SNF (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:9618449). Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:9618449). TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:9618449). TFIIF is essential for the initiation of transcription by RNA polymerase II (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:9618449). TFIIF functions include the recruitment of RNA polymerase II to the promoter bound DNA-TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for non-specific DNA, allowing for the subsequent recruitment of TFIIE and TFIIH, and facilitating RNA polymerase II elongation (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:9618449, PubMed:30385749). TAF14 acts as a chromatin reader that specifically recognizes and binds histones that are acylated (PubMed:26341557, PubMed:27089029). Recognizes and binds histone H3 acetylated or crotonylated at 'Lys-9' (H3K9ac and H3K9cr, respectively), with some preference for crotonylated lysine (PubMed:26341557, PubMed:27089029, PubMed:30385749). Component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes (PubMed:12672490). It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors (PubMed:12672490). Component of the histone acetyltransferase NuA3 complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3 (PubMed:17157260). In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation (PubMed:17157260). Does not bind DNA (PubMed:30385749).
Present with 3100 molecules/cell in log phase SD medium.
The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14. TFIIF is composed of three different subunits: TFG1/RAP74, TFG2/RAP30 and TAF14. Component of the SWI/SNF global transcription activator complex. The 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29. Component of the chromatin-remodeling INO80 complex, at least composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3, IES4, IES6, ACT1, IES2, IES5 and INO80. Component of the NuA3 complex, composed of at least NTO1, SAS3, TAF14, YNG1 and EAF6.
The YEATS domain specifically recognizes and binds acylated histones (acetylated and crotonylated) (PubMed:26341557, PubMed:27089029, PubMed:30385749). Binds crotonylated lysine through a non-canonical pi-pi-pi stacking mechanism (PubMed:27089029, PubMed:30385749).
There is no homolog of TAF14 present in the TFIIF complexes of higher eukaryotes.
Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin remodeling complex.
Present with 28900 molecules/cell in log phase SD medium.
The active factor is excreted into the culture medium by haploid cells of the A mating type and acts on cells of the opposite mating type (type alpha). It mediates the conjugation process between the two types by inhibiting the initiation of DNA synthesis in type alpha cells and synchronizing them with type A.
Belongs to the universal ribosomal protein uS19 family.
Acts as a receptor for reticulophagy. Directs autophagic sequestration of folded tubules/sheets derived from the cortical endoplasmic reticulum (cER) and the cytoplasmic endoplasmic reticulum (cytoER) into autophagosomes. Is not required for the cytoplasm-to-vacuole targeting pathway, mitophagy, pexophagy, and non-selective autophagy.
Induced in absence of NAP1 (PubMed:12788058). Expression is increased by rapamycin, which mimics nitrogen starvation by inactivating the TORC1 complex (PubMed:26040717).
Partially blocks reticulophagy, and the double ATG39/ATG40 knockout almost completely blocks this pathway. Leads to a more densely reticulated cytoplasmic endoplasmic reticulum (cER).
Present with 1890 molecules/cell in log phase SD medium.
Does not affect boron tolerance (PubMed:19414602). Impairs methylammonium (MA) transport and toxicity (PubMed:24707045).
Expression is induced by neocarzinostatin (PubMed:11562456). Expression is induced during G2 phase of cell cycle (PubMed:16278933). Expression is slightly up-regulated upon exposure to boric acid (PubMed:19414602). The AMF1 promoter contains 8 predicted enhancer box (E-box) transcription factor binding domains (PubMed:24707045).
Low affinity ammonium transporter of the plasma membrane (PubMed:24707045). May be involved in drug resistance through pumping them out of the cell (By similarity).
Belongs to the HAD-like hydrolase superfamily.
Magnesium-dependent phosphatase which may act as a tyrosine phosphatase.
Present with 6190 molecules/cell in log phase SD medium.
Assembly of polyisoprenoid side chains. The polyprenyl synthase of coenzyme Q biosynthesis catalyzes the formation from isopentenyl diphosphate of all trans-polyprenyl pyrophosphates generally ranging in length of between 6 and 10 isoprene units depending on the species.
Belongs to the FPP/GGPP synthase family.
Present with 1560 molecules/cell in log phase SD medium.
Involved in regulation of invasive growth.
Positive regulator of URA1 and URA3 expression.
Component of the inner kinetochore constitutive centromere-associated network (CCAN) (also known as central kinetochore CTF19 complex in yeast), which is composed of at least AME1, CHL4, CNN1, CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1 (PubMed:22561346). NKP1 interacts directly with OKP1 and AME1 (By similarity).
Belongs to the ATPase epsilon chain family.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Belongs to the histone deacetylase family. HD type 2 subfamily.
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
Belongs to the RNA cytidine acetyltransferase family. NAT10 subfamily.
Interacts with TAN1 (PubMed:25653167). Associates with 90S pre-ribosomal particles (PubMed:12150911).
Leads to a strong inhibition of 18S rRNA synthesis (PubMed:25653167). Deletion results in an altered alkali-soluble beta-glucan phenotype (PubMed:12150911). Heterozygous mutants show haploinsufficiency in K1 killer toxin resistance (PubMed:12663529).
RNA cytidine acetyltransferase with specificity toward both 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine (ac4C) at positions 1280 and 1773 in 18S rRNA. Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis (PubMed:25086048, PubMed:25653167). Catalyzes the formation of ac4C at position 12 in serine and leucine tRNAs. Requires the tRNA-binding adapter protein TAN1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation (PubMed:25653167).
Is probably a Ser/Thr-protein kinase that may function in initiation of DNA synthesis and also in late nuclear division.
Present with 3320 molecules/cell in log phase SD medium.
Activity of the enzyme is Mn(2+)-dependent and enhanced in the presence of pyrophosphate (PPi).
Catalytic subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain VTC4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation (PubMed:19390046). The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen (PubMed:25315834, PubMed:19390046). PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase (PubMed:25315834). The VTC complex also plays a role in vacuolar membrane fusion (PubMed:11102525, PubMed:11823419, PubMed:12584253). Required for SEC18/NSF activity in SNARE priming, membrane binding of LMA1 and V(0) trans-complex formation (PubMed:11823419). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important intracellular signaling molecules. Inositol polyphosphate binding promotes vacuolar polyphosphate synthesis (PubMed:27080106). The VTC complex is required for microautophagy. It is a constituent of autophagic tubes and is required for scission of microautophagic vesicles from these tubes (PubMed:17079729).
Present with 8710 molecules/cell in log phase SD medium.
The SPX domain has very high affinity for inositol polyphosphates, such as myo-inositol hexakisphosphate and 5-diphospho-myo-inositol pentakisphosphate (5-InsP7), and moderate affinity for inorganic pyrophosphate. Its affinity for inorganic phosphate is 2 to 3 orders of magnitude lower (Probable). SPX domains may integrate inositol pyrophosphates (PP-InsP)-dependent signaling to adapt cytosolic phosphate concentrations to different metabolic situations (Probable).
The VTC core complex is an integral membrane heterooligomer composed of the catalytic subunit VTC4 and the accessory subunits VTC1, VTC2 and VTC3. The complex exists in 2 different sub-complexes: VTC1-VTC2-VCT4 and VCT1-VTC3-VTC4. The VCT1-VTC3-VTC4 subcomplex is mostly found on the vacuolar membrane. The VTC1-VTC2-VCT4 subcomplex is observed in the cell periphery, probably ER and nuclear envelope, but localizes to the vacuole under phosphate starvation. Each subunit contains 3 transmembrane helices. VTC1 is a small membrane protein without hydrophilic domain. VTC2, VTC3 and VTC4 are related and have 2 hydrophilic domains that face the cytosol, an N-terminal SPX domain and the central core domain. The central core in VTC4 is the catalytic domain, with the essential catalytic lysine replaced by isoleucine and leucine in VTC2 and VTC3, respectively (PubMed:19390046). The core complex associates with the accessory subunit VTC5 (PubMed:27587415). The complex interacts with the v-SNARE NYV1 and with the V(0) subunit of V-ATPase VPH1 (PubMed:11823419).
Present with 143 molecules/cell in log phase SD medium.
This protein is probably a serine/threonine protein kinase.
Ty1-DR4 is a highly expressed element. Induced under amino acid starvation conditions by GCN4.
ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon.
Belongs to the DEAD box helicase family. eIF4A subfamily.
Component of the eIF4F complex, which composition varies with external and internal environmental conditions. It is composed of at least eIF4A (TIF1/TIF2), eIF4E (TIF45) and eIF4G (TIF4631 or TIF4632) (By similarity). Interacts with eIF4G1/TIF4631 and eIF4G2/TIF4632.
TIF1 and TIF2 code for the same protein.
Auxiliary transcriptional regulator of sulfur amino acid metabolism. Involved in the transcriptional activation of MET28.
Interacts with the RNA polymerase RPB1 subunit and specifically with the trimethylated H3 histone H3K4me3.
Negative regulator of transcription elongation.
The PHD domain is involved in the binding to H3K4me3.
Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.
Metal-independent phosphatase active against a broad range of phosphorylated substrates including nucleoside tri- and diphosphates, phosphorylated organic acids, and amino acids. Shows no activity against phytic acid, phosphorylated carbohydrates, and nucleoside monophosphates.
Present with 8300 molecules/cell in log phase SD medium.
Belongs to the universal ribosomal protein uS2 family.
Present with 6890 molecules/cell in log phase SD medium.
Acts to sequester alpha-tubulin from interaction with beta-tubulin, raising the possibility that it plays a regulatory role in the formation of the tubulin heterodimer.
Regulates the transcription of a set of genes, many of which encode membrane proteins. Among the genes regulated are YGR138C and YRO2. Does not seem to be dependent on copper.
Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET5 subfamily.
Present with 5000 molecules/cell in log phase SD medium.
Putative protein lysine methyltransferase that acts as a virus host factor involved in the replication of positive-strand RNA viruses like the MBV.
Belongs to the eukaryotic ribosomal protein eL24 family.
Present with 36900 molecules/cell in log phase SD medium.
Present with 2190 molecules/cell in log phase SD medium.
Acts as an inhibitor of GDB1, enhancing the ability of cells to store glucose as glycogen.
Expression increases during wine fermentation.
Part of the multisubunit TRAPP (transport protein particle) II complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33, TRS65, TRS120 and TRS130. Interacts with YPT31 and YPT32.
Specific subunit of the TRAPP II complex, a highly conserved vesicle tethering complex that functions in the late Golgi as a guanine nucleotide exchange factor (GEF) for the Golgi YPT1 GTPase. TRS130 plays a role in the YPT GEF activity of TRAPP II in concert with the two other TRAPP II-specific subunits TRS65 and TRS120. Required for both the cytoplasm-to-vacuole targeting (Cvt) pathway and starvation-induced autophagy through its role in ATG8 and ATG9 trafficking.
Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate.
Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate.
Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
In yeast, there are two genes coding for AdoMet synthase.
Present with 22000 molecules/cell in log phase SD medium.
Belongs to the nucleoporin interacting component (NIC) family.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NIC96 is part of three NPC subcomplexes, interacting with NSP1 of the NUP57 subcomplex (NIC96, NSP1, NUP49, NUP57), with NUP120 of the NUP84 subcomplex (SEH1, NUP85, NUP120, NUP145C, SEC13, NUP84, NUP133), and with NUP53 of the NUP53-NUP59-NUP170 subcomplex. The interaction with NUP53 is cell cycle dependent. NIC96 is also associated with the distal ring of the nuclear basket and interacts here with MLP2, which forms together with MLP1 nuclear pore-attached intranuclear filaments.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NIC96, which is localized to the core of the NPC and the distal ring of the nuclear basket, is required for de novo assembly of NPCs. It is involved in nuclear GSP1 import.
Present with 15500 molecules/cell in log phase SD medium.
Interacts with PRM9. Binds to SEC23/24 of COPII coated vesicles.
May be involved in endoplasmic reticulum exit trafficking of proteins.
Present with 1254 molecules/cell in log phase SD medium.
DNA-binding protein that acts probably as a transcription factor.
Leads to cell death when overexpressing the camptothecin mimetic TOP1-T(722)A mutant.
Negative regulator of the transcriptional complex INO2-INO4 in response to phospholipid precursor availability. When precursors become limiting, OPI1 is retained at the endoplasmic reticulum (ER) and INO2-INO4 activates INO1 and other genes required for phospholipid biosynthesis, whereas abundant precursor availability results in targeting of OPI1 to the nucleus to repress transcription of these genes. Binds directly to phosphatidic acid, which is required for ER targeting and may act as sensing mechanism for precursor availability, as phosphatidic acid becomes rapidly depleted upon phospholipid biosynthesis.
Present with 1281 molecules/cell in log phase SD medium.
The FFAT motif is required for interaction with SCS2 and proper localization of the protein.
Autophosphorylated mainly on serine residues.
Homodimer; in response to the accumulation of unfolded proteins.
Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto-activation. The active endoribonuclease domain splices HAC1 precursor mRNA to produce the mature form which then induces transcription of UPR target genes.
The kinase domain is activated by trans-autophosphorylation. Kinase activity is required for activation of the endoribonuclease domain.
CTDK-I consists of three subunits, CTK1, CTK2 and CTK3 (also called alpha, beta and gamma). Interacts with CTK1. Heterodimerization with CTK2 is required to protect this subunit from degradation.
Gamma subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. CTDK-I phosphorylates 'Ser-5' if the CTD substrate is not phosphorylated at 'Ser-5', but will phosphorylate 'Ser-2' of a CTD substrate if 'Ser-5' is already phosphorylated. CTDK-I is also more reactive toward substrates that are prephosphorylated at 'Ser-2' or 'Ser-5' compared with an unphosphorylated CTD substrate, therefore efficiently creating doubly phosphorylated CTD repeats. Involved in RNA polymerase I transcription and RNA polymerase II transcriptional elongation, and as part of the CTDK-I complex, pre-mRNA 3'-end processing and SET2 mediated H3K36 methylation. Together with CTK2, required for CTK1 CTD kinase activation. Required for DNA damage induced transcription. Involved in the adaptation to alternative carbon sources, including galactose, glycerol and ethanol, but not raffinose. Required for the integrity of the rDNA locus.
Null mutants are viable, but grow more slowly than wild-type cells at 30 degrees Celsius. They are cold-sensitive, failing to grow at 12 degrees Celsius. They display flocculent growth in liquid media and they show abnormal cell morphologies, for example, a significant fraction of the cells are greatly enlarged. Deletion mutant is sensitive to the DNA synthesis inhibitor hydroxyurea (HU) and UV irradiation.
Present with 2640 molecules/cell in log phase SD medium.
Ubiquitinated. Ubiquitination leads to degradation by the 26S proteasome pathway.
Homodimer. Binds to the TIM22 translocation complex during import.
Mitochondrial dicarboxylic transporter catalyzing the exchange of dicarboxylic acids like malate and succinate for inorganic phosphate. Required for growth on ethanol and acetate.
Present with 3390 molecules/cell in log phase SD medium.
The C-terminal Solcar repeat is required for association with the TIM22 translocation complex during import.
Belongs to the inositol phosphokinase (IPK) family.
Impairs nuclear mRNA export, slows cell growth, increases cellular InsP3 170-fold and decreases InsP6 100-fold.
Inositol phosphate kinase with both monophosphoinositol and diphosphoinositol polyphosphate synthase activities. Able to phosphorylate inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) on both the carbon-3 and carbon-6 positions to synthesize inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4) and inositol 1,4,5,6-tetrakisphosphate (Ins(1,4,5,6)P4), and then to subsequently phosphorylate and convert either isomer of InsP4 to inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) (PubMed:10574768, PubMed:10683435, PubMed:11311242). Its predominant in vivo catalytic function is to convert Ins(1,4,5)P3 to Ins(1,4,5,6)P4 to Ins(1,3,4,5,6)P5 via 6- and 3-kinase activities (PubMed:15944147). It can also use Ins(1,3,4,5,6)P5 as a substrate and act as a diphosphoinositol polyphosphate synthase to generate two different isomers of PP-InsP4 (PubMed:11311242). Has also a role in transcription regulation. Forms a complex with ARG80, ARG81 and MCM1 (ArgR-MCM1), which coordinates the expression of arginine anabolic and catabolic genes in response to arginine. Recruits ARG80 and MCM21 to stabilize them (PubMed:3298999, PubMed:8043104, PubMed:10632874). Neither the kinase activity nor inositol phosphates are required for the formation of ArgR-MCM1 transcriptional complexes on DNA promoter elements and the control of arginine metabolism (PubMed:11119723, PubMed:10720331, PubMed:12828642, PubMed:22992733). In contrast, only the catalytic activity is required for PHO gene repression by phosphate and for NCR gene activation in response to nitrogen availability, indicating a role for inositol pyrophosphates in these controls (PubMed:12828642). Inositol polyphosphates may be involved in the regulation of chromatin remodeling of transcription (PubMed:12434012). Regulates nuclear mRNA export via inositol phosphate metabolism (PubMed:10390371, PubMed:10683435). Also has lipid kinase activity, transforming the lipid inositol phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) into phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) in the nucleus (PubMed:16123124). Its kinase activity is necessary for the propagation of most [PSI+] prion variants (PubMed:28923943).
Present with 2720 molecules/cell in log phase SD medium.
The expression of this protein is not effected by the presence of arginine.
Non-catalytic component of the proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. This subunit may participate in the trypsin-like activity of the enzyme complex.
RNA-binding protein involved in post-transcriptional regulation. Negatively regulates expression of HO by binding to the 3'-UTR of HO mRNA. Predominantly binds to mRNAs encoding chromatin modifiers and spindle pole body components. Recognizes and binds to 5'-TGTAA[CT]A[AT]TA-3' in the 3'-UTR of target mRNAs. Multicopy suppressor of POP2 mutation. Required for high temperature growth.
Essential component of a cytosolic Fe/S protein assembly machinery. Required for maturation of extramitochondrial Fe/S proteins. May play a role in the transfer of pre-assembled Fe/S clusters to target apoproteins.
Belongs to the diphosphomevalonate decarboxylase family.
Diphosphomevalonate decarboxylase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (PubMed:8626466, PubMed:9244250). MVD1/ERG19 converts diphosphomevalonate into isopentenyl diphosphate (PubMed:8626466). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD1/ERG19 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (PubMed:32679672).
Present with 13700 molecules/cell in log phase SD medium.
Acts in ubiquitin metabolism and is necessary for the control of single-copy DNA replication.
Belongs to the ZIP transporter (TC 2.A.5) family.
Low-affinity zinc transport protein. Active in zinc-replete cells and is time-, temperature- and concentration-dependent and prefers zinc over other metals as its substrate.
Negatively regulates early sporulation-specific genes. Seems to exert its function by positively regulating the Ras/cAMP pathway. Required for growth under alkaline conditions. Acts synergetically with MDS3.
Catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC) from chorismate and glutamine. Required for the synthesis of 4-aminobenzoate (PABA), an important component in tetrahydrofolate biosynthesis.
In the C-terminal section; belongs to the anthranilate synthase component I family.
The PABA component provides the glutamine amidotransferase activity.
The PABB component catalyzes the formation of ADC by binding chorismate and ammonia.
GDP-GTP exchange factor (GEF) for the small GTPase BUD1/RSR1. Regulates the activity of BUD1 together with BUD2 which is a GTPase-activating protein (GAP) of BUD1. Required to produce both the axial and bipolar patterns of bud site selection. Determines the orientation of division axis. Overexpression can suppress mutations in PRP20 which is the GEF for GSP1. May be a cytoplasmic GEF for GSP1. Might also act on the Ras-like protein CDC42. Appears to bind to Ras proteins but not to activate them.
Interacts with AXL2, BEM1, GSP1 and in haploid cells with AXL1.
Present with 2110 molecules/cell in log phase SD medium.
Causes mitochondria to cluster within cells.
Expression is increased in intermediate compared to fully aerobic conditions.
May associate with the eukaryotic translation initiation factor 3 (eIF-3) complex. Associates with the 80S ribosome.
mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.
Belongs to the YCR102c/YLR460c/YNL134c family.
Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Present with 3870 molecules/cell in log phase SD medium.
Involved in biosynthesis of fatty acids in mitochondria.
Present with 1760 molecules/cell in log phase SD medium.
Forms a heterodimer with SLX1. Interacts with RAD1; catalytic subunit of the RAD1-RAD10 endonuclease. Interacts with RTT107.
Phosphorylated by ATR (MEC1) and ATM (TEL1) upon DNA damage. This appears to be required for the function with the RAD1-RAD10 endonuclease.
Regulatory subunit that interacts with and increases the activity of different structure-specific endonucleases. Has several distinct roles in protecting genome stability by resolving diverse forms of deleterious DNA structures. Component of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for simple Y, 5'-flap and replication fork-like structures. It cleaves the strand bearing the 5'-non-homologous arm at the branch site junction and generates ligatable, nicked products from the 5'-flap or replication fork substrates. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. Has Holliday junction resolvase activity in vitro. Interacts with the structure-specific RAD1-RAD10 endonuclease and promotes RAD1-RAD10-dependent 3'-non-homologous tail removal (NHTR) during repair of double-strand breaks by single-strand annealing. SLX4 also promotes recovery from DNA-alkylation-induced replisome stalling during DNA replication by facilitating the error-free mode of lesion bypass. This does not require SLX1 or RAD1-RAD10, but probably RTT107.
Although strongly related to dimethyladenosine transferase proteins, it lacks the methyltransferase activity. Dimethyladenosine transferase methylates the 2 adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 12S mitochondrial rRNA in most species. This explains why 12S rRNA is not methylated in S.cerevisiae.
Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family.
Mitochondrial transcription factor that confers selective promoter recognition on the core subunit of the yeast mitochondrial RNA polymerase. Interacts with DNA in a non-specific manner.
Present with 9380 molecules/cell in log phase SD medium.
Present with 5350 molecules/cell in log phase SD medium.
3'-to-5' exoribonuclease specific for small oligoribonucleotides.
Belongs to the oligoribonuclease family.
Part of a complex that includes BRX1, RPF1, RPF2 and SSF1 or SSF2.
Present with 8150 molecules/cell in log phase SD medium.
Required for biogenesis of the 60S ribosomal subunit.
A cysteine residue is required for ubiquitin-thioester formation.
Belongs to the UPL family. K-HECT subfamily.
E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
Present with 7380 molecules/cell in log phase SD medium.
ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/RAD3 is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription. XPD/RAD3 acts by forming a bridge between TFIIK and the core-TFIIH complex. Involved in the maintenance of the fidelity of DNA replication.
Belongs to the helicase family. RAD3/XPD subfamily.
Present with 14400 molecules/cell in log phase SD medium.
Can promote the transfer of one strand of a double-stranded DNA molecule to a homologous single strand and thus may be involved in recombination.
Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.
Present with 6260 molecules/cell in log phase SD medium.
S-II binds to RNA-polymerase II in the absence of transcription.
Required for efficient assembly of cytochrome c oxidase in the mitochondrial inner membrane. Involved in a step that couples MSS51-COX14-dependent regulation of COX1 translation to early steps of cytochrome c oxidase assembly.
Belongs to the PEX28-32 family. PEX30/31 subfamily.
Belongs to the methylenetetrahydrofolate reductase family.
Belongs to the proteasome inhibitor PI31 family.
Plays a role in the establishment of transcriptional silencing boundaries, preventing the propagation of heterochromatic silencing.
Produced by +1 ribosomal frameshifting between codon Leu-431 and Gly-432 of the YBL100W-A ORF.
Component of the Golgi-associated retrograde protein (GARP) complex, also called VFT (VPS fifty-three) complex, composed of VPS51, VPS52, VPS53 and VPS54. Interacts also with TLG1, YPT6 and ARL1.
Involved in retrograde transport from early and late endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1 to the Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles.
Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
Catalytic component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling.
Component of the SWR1 chromatin-remodeling complex composed of at least ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4, SWC5, SWC7 and SWR1, and perhaps BDF1.
Heterodimer of SLM1-SLM2. Binds phosphatidylinositol 4,5-bisphosphate, which is required for function. Interacts with the TORC2 subunits AVO2, BIT61 and TOR2. Interacts with the calcineurin catalytic subunits CNA1 and CNA2.
Phosphorylated by the target of rapamycin complex 2 (TORC2) and dephosphorylated by serine/threonine-protein phosphatase 2B (calcineurin).
Present with 5190 molecules/cell in log phase SD medium.
Together with SLM2, effector of the TORC2- and calcineurin-signaling pathways. Phosphorylated and activated by TORC2 under favorable growth conditions. Mediates actin polarization via inhibition of calcineurin-dependent transcription. Upon nutrient limitation or environmental stress, gets dephosphorylated by calcineurin. Dephosphorylation inhibits its interaction with TORC2, thereby antagonizing TORC2 signaling and mediating calcineurin-dependent actin depolarization. Also functions in heat-induced, calcineurin-mediated uracil permease (FUR4) endocytosis.
3'-phosphoadenosine 5'-phosphate (pAp) is an inhibitor of KEM1. Sodium-induced GCN4 expression reduces pAp accumulation by activating HAL2 expression, and therefore maintains mRNA degradation capacity which is likely to be important for the accurate and rapid adaptation of gene expression to salt stress.
Belongs to the 5'-3' exonuclease family.
Both strand exchange and nuclease activities require magnesium, for the strand exchange activity, calcium can replace magnesium when the linear ds-DNA has been first resected with an exogenous endonuclease.
Multifunctional protein that exhibits several independent functions at different levels of the cellular processes. 5'-3' exonuclease component of the nonsense-mediated mRNA decay (NMD) which is a highly conserved mRNA degradation pathway, an RNA surveillance system whose role is to identify and rid cells of mRNA with premature termination codons and thus prevents accumulation of potentially harmful truncated proteins. The NMD pathway has a second role regulating the decay of wild-type mRNAs, and especially mRNAs that are important for telomere functions. Participate in CTH2-mediated and VTS1-mediated mRNA turnover. Involved in the degradation of several hypomodified mature tRNA species and participates in the 5'-processing or the degradation of the snoRNA precursors and rRNA processing. Involved in defense against virus and suppresses viral RNA recombination by rapidly removing the 5'-truncated RNAs, the substrates of recombination, and thus reducing the chance for recombination to occur in the parental strain. Required for the assembly of the virus-like particles of the Ty3 retrotransposon and contributes to the efficient generation of narnavirus 20S RNA by playing a major role in the elimination of the non-viral upstream sequences from the primary transcripts. Degrades single-stranded DNA (ss-DNA) and can renature complementary ss-DNA as well as catalyzes the formation of heteroduplex DNA from circular ss-DNA and homologous linear ds-DNA in vitro. Acts as a microtubule-associated protein which interacts with cytoplasmic microtubules through beta-tubulin and promotes in vitro assembly of tubulin into microtubules. Associates with microtubule functions such as chromosome transmission, nuclear migration, and SPB duplication. Has also a role in G1 to S transition and is involved in nuclear fusion during karyogamy. Required for the expression of ROK1 at the post-transcriptional level and for the alpha-factor induction of the karyogamy genes KAR3 and KAR4. Plays a role in filamentous growth.
Mutations affect nuclear fusion, leed to reduced chromosome stability and defects in spindle pole body duplication and/or separation as well as loss of viability under conditions of nitrogen starvation. Homozygous diploids are unable to sporulate. Leads also to arrest in pachytene and deficiency in meiotic recombination and sensitivity to oleate.
Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome.
Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty4 retrotransposons belong to the copia elements (pseudoviridae).
DNA-binding protein that recognizes sequence-specific replication termini (Ter sites) within rDNA (PubMed:14576157). Binds to rDNA terminator elements and mediates efficient RNA polymerase I transcription termination (PubMed:22805593). Required for rDNA silencing at the non-transcribed spacer 1 (NTS1). Promotes the association of SIR2 with NTS1 and contributes to maintenance of rDNA stability (PubMed:22362748).
Decreases the association of SIR2 with NTS1, decreases rDNA stability and shortens replicative lifespan.
Interacts with FOB1 (PubMed:14576157, PubMed:22362748). Interacts with the RENT complex subunits NET1 and SIR2 (PubMed:22362748).
Component of a SNARE complex consisting of UFE1, USE1, SEC20 and SEC22 or YKT6. Interacts with TIP20 through its cytoplasmic domain.
SNARE required for targeting and fusion of Golgi-derived retrograde transport vesicles with the ER.
Component of 250-400 kDa complexes called cytochrome oxidase assembly intermediates or COA complexes composed at least COA3, COX14, COX5A, SHY1 and SSC1. Interacts with COX1 and MSS51.
Required for assembly of cytochrome c oxidase (complex IV). With COX14, regulates negatively COX1 translation and is involved in MSS51 association with newly synthesized COX1.
Belongs to the phosphoglycerate mutase family.
Probable phosphomutase that may have a function related to the manipulation of phosphate groups on carbohydrates. Reduces trehalose-6-phosphate levels when overexpressed in TPS2-deleted cells. Reduces 5'-Phosphoribosyl-4-carboxamide-5-aminoimidazole (AICAR) levels, a metabolic intermediate at the crossroads between AMP and histidine biosynthesis pathways, when overexpressed in a ADE3-ADE16-ADE17 triple deletant.
Lipid transport protein (LTP) involved in non-vesicular transfer of lipids between membranes. Functions in phosphoinositide-coupled directional transport of various lipids by carrying the lipid molecule in a hydrophobic pocket and transferring it between membranes through the cytosol. Involved in maintenance of intracellular sterol distribution and homeostasis (PubMed:15173322). Binds and transports sterol (PubMed:20008566). Plays a role in the positive regulation of vesicular transport of ceramide from the ER to the Golgi, negatively regulating COPII-mediated ER export of cargos (PubMed:24213531).
Present with 1069 molecules/cell in log phase SD medium.
The OSBP-related domain (ORD) mediates binding of sterols and phospholipids. It displays an incomplete beta-barrel containing a central hydrophobic tunnel that can accommodate a single lipid molecule with a flexible lid covering the tunnel entrance. The ORD can bind two membranes simultaneously. It has at least two membrane-binding surfaces; one near the mouth of the lipid-binding pocket and a distal site that can bind a second membrane. These structural features correlate with the phosphatidylinositol 4-phosphate (PI(4)P)-coupled lipid transport optimized in closely apposed membranes, such as organelle contact sites. The lipid transfer cycle starts from the association of the LTP with a donor membrane, which accompanies conformational changes that uncover the ligand-binding pocket. The tunnel opening is generally mediated by displacement of the lid covering the binding pocket allowing uptake or release of a lipid molecule. The LTPs extract the lipid from the membrane by providing a hydrophobic environment as well as specific interaction. Dissociation from the donor membrane shifts the conformation to a closed form. Then, the LTPs loaded with a cargo lipid diffuse through the aqueous phase. Lid opening may be induced by the interaction of a hydrophobic side of the lid with the target membranes.
The PH domain strongly binds to phosphoinositides and is required for targeting the protein to the membrane.
Belongs to the glutamine synthetase family.
Present with 346000 molecules/cell in log phase SD medium.
The submitted sequence does not correspond to the sequence published in the paper.
Has a role in de-ubiquitination. In conjunction with UBP3, cleaves ubiquitin, leading to the subsequent mono-ubiquitination of sec23.
Heterotetramer with UBP3; contains two molecules of BRE5 and two molecules of UBP3 (PubMed:12778054, PubMed:17632125). Forms a complex composed of CDC48, DOA1, deubiquitinase UBP3 and probably BRE5 (PubMed:20508643). Within the complex, interacts (via C-terminus) with CDC48; the interaction is direct and UBP3-independent (PubMed:20508643).
Interacts with glycogen synthase 2 (GSY2); possibly also interacts with phosphatase 1 (GLC7).
Interacts directly with ADY3 and YOR129C. Interacts with ADY4. Probable component of a SPB complex composed of ADY3, SSP1, DON1, MPC54, SPO21/MPC70, NUD1 and CNM67.
Involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. Required for the proper formation of the spindle pole body (SPB) outer plaque. May connect the outer plaque to the central plaque embedded in the nuclear envelope.
Meiosis-specific. Expressed from 3 to 9 hours after induction of sporulation.
The length of the coiled coil are required to adjust the space between outer plaque and the central plaque.
Homodimer and interacts with SIR4 and RAP1 C-terminus. Interacts with MCM10.
N-terminal acetylation by NatA is important for transcriptional silencing activity.
The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure. Involves the compaction of chromatin fiber into a more condensed form.
Citrate synthase is found in nearly all cells capable of oxidative metabolism.
Decreased growth related to mitochondrial dysfunction.
Monomer and homodimer (PubMed:28076776). Exists as an inactive monomer when phosphorylated (PubMed:28076776). Homodimerization is dependent on dephosphorylation of Ser-462 by PTC7 and is required for activity (PubMed:28076776).
Phosphorylation at Ser-462 inhibits catalytic activity. Dephosphorylation at Ser-462 by PTC7 enhances catalytic activity.
Phosphorylation at Ser-462. Dephosphorylated at Ser-462 by PTC7.
Specific citrate synthase with catalytic activity only with acetyl-CoA.
Predicted to be involved in rRNA processing.
Belongs to the proteasome subunit S5B/HSM3 family.
Interacts with RPT1, RPT2, RPT3, RPT5, RPT6, RPN1 and RPN2. Part of transient complex (BP1) containing HSM3, RPT1, RPT2 and RPT5 formed during the assembly of the 26S proteasome.
Involved in DNA mismatch repair in slow-growing cells. Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the 19S regulatory complex (RC).
Simultaneous disruption of CBR1 results in resistance to diphtheria toxin and K.lactis killer toxin.
The outer membrane form may mediate the reduction of outer membrane cytochrome b5 (PubMed:8001120). The soluble inter-membrane space form may transfer electrons from external NADH to cytochrome c, thereby mediating an antimycin-insensitive, energy-coupled oxidation of external NADH by yeast mitochondria (PubMed:8001120). Involved in the reduction of D-erythroascorbyl free radicals (PubMed:11420140). May play a minor role in complementing the function of CBR1 as a DPH3 reductase in the first step of diphthamide biosynthesis and tRNA Wobble base mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine) formation (PubMed:27694803).
There are two isoforms of NADH-cytochrome b5 reductase, a 34 kDa form (p34) and a 32 kDa form (p32). The p34 form becomes firmly anchored to the outer mitochondrial membrane after an incomplete translocation arrest. The p32 form is formed after translocation of the p34 precursor to the inner mitochondrial membrane, where it is processed by mitochondrial inner membrane peptidase (IMP) complex and released to the intermembrane space.
Belongs to the peptidase M28 family. M28B subfamily.
Present with 112 molecules/cell in log phase SD medium.
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. cAMP subfamily.
Lipid transport protein (LTP) involved in non-vesicular transfer of lipids between membranes. Functions in phosphoinositide-coupled directional transport of various lipids by carrying the lipid molecule in a hydrophobic pocket and transferring it between membranes through the cytosol. Involved in maintenance of intracellular sterol distribution and homeostasis (PubMed:20008566, PubMed:15173322, PubMed:16136145, PubMed:22162133). Involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum. Specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is delivered to the ER-localized PI4P phosphatase SAC1 for degradation. Thus, by maintaining a PI4P gradient at the ER/Golgi interface, SAC1 may drive PS transport (PubMed:25849868, PubMed:16136145, PubMed:22162133). Displays a similar affinity for PI4P and sterols (PubMed:22162133). Binds sterol and PI4P in a mutually exclusive manner (PubMed:22162133). Involved in ergosterol transport from the plasma membrane (PM) to the ER (PubMed:16585271). Mediates sterol transport from the ER to mitochondria (PubMed:29487131). Involved in the negative regulation of Golgi-derived transport vesicle biogenesis (PubMed:8978672). Plays a role in the positive regulation of vesicular transport of ceramide from the ER to the Golgi, negatively regulating COPII-mediated ER export of cargos (PubMed:24213531).
Present with 32200 molecules/cell in log phase SD medium.
The ArfGAP1 lipid packing sensor (ALPS) motif is a membrane-binding motif that is sensitive to curvature.
Binds to microtubules. Homodimer; each monomer can bind via its TOG domains to two alpha/beta-tubulin heterodimers. Interacts with SPC72. Associates with the NDC80 complex.
Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. May play a role in the attachment, organization, and/or dynamics of microtubule ends at the spindle pole body. Stabilizes both cytoplasmic and nuclear microtubules. Promotes mitotic spindle elongation in anaphase. Has microtubule polymerase activity by accelerating microtubule growth and inhibiting catastrophe. The polymerase activity is proposed to involve a tethering mechanism at the microtubule plus end: a curved, longitudinally microtubule lattice-associated tubulin heterodimer (that cannot be incorporated into the microtubule lattice) is bound via one TOG domain while the other TOG domain binds to an unpolymerized tubulin heterodimer leading to lateral association of these tubulin heterodimers; polymerization-induced straightening of the tubulin heterodimer releases the polymerase (PubMed:11309422, PubMed:25172511, PubMed:16567500, PubMed:25097237). Is involved in regulation of kinetochore-microtubule attachments in a tension-dependent manner involving its association with the NDC80 complex; the function may be independent of its microtubule polymerase activity. Can either stabilize or destabilize kinetochore attachments, depending on the level of kinetochore tension and whether the microtubule tip is assembling or disassembling (PubMed:27156448).
Mutations in STU2 suppress a cold-sensitive mutation in TUB2.
Present with 1660 molecules/cell in log phase SD medium.
The TOG (tumor overexpressed gene) domains are composed of six (for the most part non-canonical) HEAT repeats each. Intra-HEAT loops are positioned along a face of the TOG domain and bind to a single alpha/beta-tubulin heterodimer. Two sets of TOG domains may wrap around a single free tubulin heterodimer accompanied by a open-to-closed conformational change of the STU2 homodimer. Both, TOG 1 and TOG 2 bind curved alpha/beta-tubulin with comparable affinity; the two TOG domains bind noncooperatively to two tubulin heterodimers. Free unpolymerized tubulin-binding is predominantly mediated by TOG 1, association with the microtubules plus ends is mediated by TOG 2 in cooperation with a C-terminal basic domain.
The coiled coil domain mediates homodimerization.
Catalyzes the attachment of methionine to tRNA(Met) in a two-step reaction: methionine is first activated by ATP to form Met-AMP and then transferred to the acceptor end of tRNA(Met).
Component of a yeast aminoacyl-tRNA synthase (aaRS) complex formed by methionyl-tRNA synthase MES1, glutamyl-tRNA synthase GUS1 and the tRNA aminoacylation cofactor ARC1 in a stoichiometric complex. Interacts (via N-ter) with ARC1 (via N-ter). Can also form a stable binary complex with ARC1 that is functional in terms of aminoacylation. ARC1 increases the affinity for cognate tRNAs due to the presence of a tRNA binding domain in the middle and C-terminal part of ARC1.
Present with 85000 molecules/cell in log phase SD medium.
'De respuesta a estres' means stress response in Spanish.
Aldose reductase with a broad substrate specificity. Reduces the cytotoxic compound methylglyoxal (MG) to acetol and (R)-lactaldehyde under stress conditions. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation (PubMed:11525399). In pentose-fermenting yeasts, aldose reductase catalyzes the reduction of xylose into xylitol. The purified enzyme catalyzes this reaction, but the inability of S.cerevisiae to grow on xylose as sole carbon source indicates that the physiological function is more likely methylglyoxal reduction (Probable) (PubMed:11722921).
Belongs to the aldo/keto reductase family.
By osmotic, ionic, oxidative and heat stress.
Present with 12851 molecules/cell in log phase SD medium.
Expression is repressed in medium containing both glucose and glutamate (PubMed:3023912). Expression is up-regulated by the presence of C2-compounds such as acetate (PubMed:25982115).
Leads to glutamate auxotrophy and poor growth on rich medium containing lactate, a nonfermentable carbon source, when CIT1 is also deleted.
Peroxisomal citrate synthase involved in the citrate homeostasis (PubMed:3023912, PubMed:25982115). Catalyzes the condensation of acetyl coenzyme A and oxaloacetate to form citrate (PubMed:3023912, PubMed:25982115). Citrate synthase is the rate-limiting enzyme of the tricarboxylic acid (TCA) cycle (Probable).
Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(UCC1), which leads to its degradation by the proteasome (PubMed:25982115). Ubiquitination is prevented by oxaloacetate, suggesting the existence of an oxaloacetate-dependent positive feedback loop that stabilizes CIT2 (PubMed:25982115).
Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily.
Essential transmembrane GTPase, which mediates mitochondrial fusion (PubMed:9685359, PubMed:9786948, PubMed:10562274, PubMed:11266460, PubMed:15297626, PubMed:15760898, PubMed:16624808, PubMed:19812251, PubMed:21385840, PubMed:21502136, PubMed:23317502, PubMed:27253069). Fusion proceeds through several steps; first mitochondria are tethered together, then brought into close contact, followed by the formation of a docking ring around contact areas, and finally membrane fusion (PubMed:27253069). Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondrial morphology, which is balanced between fusion and fission, mediated by FZO1 and DNM1, respectively (PubMed:10562274). Functions antagonistically with DNM1 (PubMed:10562274). Probably acts by forming membrane contact sites that mediate mitochondrial membrane fusion (PubMed:27253069). Mitochondrial docking and fusion requires GTP hydrolysis (PubMed:15297626, PubMed:19812251, PubMed:27253069). Mitochondrial fusion promotes also increased lifespan.
Homodimer (PubMed:16624808, PubMed:21385840, PubMed:19812251). Dimerization depends on GTP binding (PubMed:16624808, PubMed:21385840, PubMed:19812251). Component of a large multiprotein complex of 800 kDa (PubMed:9685359). Binds the cytoplasmic domain of UGO1 which binds MGM1 through its intermembrane space domain (PubMed:15087460, PubMed:12808034). Interacts with MDM30 (PubMed:21385840, PubMed:21502136, PubMed:16735578). Interacts with UBP2 and UBP12 (PubMed:23317502). Interacts (when ubiquitinated) with DOA1; the interaction recruits FZO1 to CDC48 and promotes FZO1 proteasomal degradation (PubMed:27044889).
Present with 1000 molecules/cell in log phase SD medium.
The GTPase domain may regulate the interaction with UGO1 since FZO1 lacking the GTPase domain binds 5-fold higher amount of UGO1 than full-length FZO1. The coiled-coil heptad repeat domains HRN, HR1 and HR2 are required for the oligomerization and function in mitochondrial fusion.
Ubiquitinated at Lys-398 and Lys-464 (PubMed:19812251, PubMed:23317502, PubMed:27044889). MDM30 and UGO1 are involved in ubiquitination (PubMed:18353967, PubMed:21385840, PubMed:21502136). Deubiquitinated by UBP2 and UBP12 (PubMed:23317502). UBP2 and UBP12 recognize distinct ubiquitin chains on FZO1 that have opposing effects on mitochondrial fusion (PubMed:23317502). UBP2 removes ubiquitin chains that initiate proteolysis of FZO1 and inhibit fusion (PubMed:23317502). UBP12 recognizes ubiquitin chains that stabilize FZO1 and promote mitochondrial fusion. UBP12 deubiquitylates FZO1 only after oligomerization (PubMed:23317502).
Acts as an inhibitor of cap-dependent translation. Competes with eIF4G1/TIF4631 and EAP1 for binding to eIF4E/TIF45 and interferes with the formation of the eIF4F complex, inhibiting translation and stabilizing mRNA. Binding affinity for eIF4E/TIF45 is 10-fold less than that of eIF4G1/TIF4631. Required for induction of pseudohyphal growth in response to nitrogen limitation, probably by regulating STE12 translation.
Phosphorylated by casein kinase II complex (CK2).
Present with 26900 molecules/cell in log phase SD medium.
Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
Homodimer; disulfide-linked, upon oxidation.
Present with 4820 molecules/cell in log phase SD medium.
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events (PubMed:10681558, PubMed:11741925, PubMed:15210711). Can act alternatively as peroxidase and molecular chaperone. Oxidative stress and heat shock exposure cause a reversible shift of the protein structure from low MW species to high MW complexes, triggering a peroxidase-to-chaperone functional switch. The chaperone function of the protein enhances resistance to heat shock (PubMed:15163410).
Belongs to the RecA family. RAD51 subfamily.
Part of a repair/recombination complex that includes RAD51, RAD52 and RAD54. Interacts with HED1, RDH54 and SAW1.
Present with 6960 molecules/cell in log phase SD medium.
RAD51 is cell cycle regulated, peaking around the G1-to-S transition.
Required both for recombination and for the repair of DNA damage caused by X-rays. Its function may be modulated by interaction with other repair proteins. RAD52 interacts directly with RAD51, via its C-terminus. Forms a nucleoprotein filament with DNA as an early intermediate in recombination.
Belongs to the ThrE exporter (TC 2.A.79) family.
This is a truncated version of a ThrE family protein. Strain S288c has a frameshift in position 382, which disrupts the gene coding for this protein and produces two ORFs YJL107C and YJL108C. A contiguous sequence for a S.cerevisiae ThrE family protein can be found in strain YJM789 (AC A6ZQL9).
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids (Potential). Seems to be involved in ribosome assembly.
Component of the Asi complex, which contains ASI1, ASI2 and ASI3 (PubMed:25236469). Interacts directly with ASI1 (PubMed:17085444).
Part of the nuclear inner membrane (INM)-specific branch of the ER-associated degradation (ERAD) pathway, required for the elimination of misfolded proteins in the INM, a specialized ER subdomain. Required for ERG11 degradation (PubMed:25236469). Negative regulator of SPS-sensor signaling. Together with ASI2 and ASI3, prevents the unprocessed precursor forms of STP1 and STP2 that escape cytoplasmic anchoring from inducing SPS-sensor-regulated genes in the absence of inducing signals (PubMed:17085444). Controls amino acid permease (AAP) gene expression in response to amino acid availability, a process mediated by the transcription factors STP1 and STP1 (PubMed:11454748).
In the N-terminal section; belongs to the HSF family.
Involved in cell surface assembly and regulation of the gene related to flocculation (asexual cell aggregation). Mutations in SFL1 causes constitutive cell aggregation.
Interacts with SWP82. Component of the SWI/SNF global transcription activator complex. The 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29.
Involved in transcriptional activation. Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
AAA-cassette D1 is required for interaction with PEX1. ATP-binding in AAA-cassette D1 is required for attachment to PEX15. ATP-binding and hydrolysis in AAA-cassette D2 is required for release from PEX15 and proper function in PEX5 dislocation.
Interacts with PEX1; forming the PEX1-PEX6 AAA ATPase complex, which is composed of a heterohexamer formed by a trimer of PEX1-PEX6 dimers (PubMed:15634331, PubMed:16007078, PubMed:26170309, PubMed:26066397, PubMed:29321502). Interacts with PEX15; anchors PEX1-PEX6 heterooligomers to the peroxisomal membrane and mediates their association with the peroxisomal importomer (PubMed:12808025). Interacts with UBP15 (PubMed:21665945).
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YML045W-A ORF.
Belongs to the ubiquitin-activating E1 family. ULA1 subfamily.
Heterodimer of UBA3 and ULA1. The complex binds NEDD8 and UBC12 (By similarity).
Regulatory subunit of the dimeric UBA3-ULA1 E1 enzyme. E1 activates NEDD8/RUB1 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBC12.
Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters.
Present with 8500 molecules/cell in log phase SD medium.
Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.
The HXXXXD motif is essential for acyltransferase activity.
Belongs to the Clp1 family. Clp1 subfamily.
Causes defective 3'-end formation and transcriptional read-through.
Component of the cleavage factor IA (CF IA) complex, which is a heterohexameric complex with 2:2:1:1 stoichiometry of RNA14, RNA15, PCF11 and CLP1. It contains 2 copies of an RNA14-RNA15 dimer and 1 copy of CLP1-PCF11. The complex interacts with the cleavage factor HRB1/CF IB to form the cleavage factor I (CF I) complex, and binds to RNA. Interacts directly with PCF11. Interacts with the CPF components CFT1, PTA1, PFS2, YSH1 and SSU72.
Component of the cleavage factor IA (CF IA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation. Associates with HRB1/CF IB to form the cleavage factor I (CF I) complex. CF I is required for correct positioning of a larger protein complex, the cleavage and polyadenylation factor (CPF) complex, which contains the catalytic subunits executing mRNA cleavage and polyadenylation. CLP1 mediates interactions between CF IA and CPF factors. CLP1 is also involved in maintaining the CF IA interaction with the C-terminal domain of RNA Pol II largest subunit via PCF11, which links pre-mRNA 3'-end processing to transcription termination.
May lack the polyribonucleotide 5'-hydroxyl-kinase and polynucleotide 5'-hydroxyl-kinase activities that are characteristic of the human ortholog.
Associates with the pre-60S ribosomal particle.
Belongs to the universal ribosomal protein uL10 family.
Component of the ribosome assembly machinery. Nuclear paralog of the ribosomal protein P0, it binds pre-60S subunits at an early stage of assembly in the nucleolus, and is replaced by P0 in cytoplasmic pre-60S subunits and mature 80S ribosomes.
Present with 18200 molecules/cell in log phase SD medium.
Belongs to the mitochondrion-specific ribosomal protein mL60 family.
Interacts with NOP8 and RRP43. Interacts with pre-ribosome complex. May bind to RNA.
Present with 5170 molecules/cell in log phase SD medium.
Required for proper 27S pre-rRNA processing and 60S ribosome subunit assembly.
Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis. May be involved in telomere capping.
Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which associates with catalytic subunits DIS3 and RRP6 in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits and peripheral S1 domain-containing components CSL4, RRP4 and RRP40 located on the top of the ring structure. Interacts with LRP1.
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP45 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation.
Present with 4800 molecules/cell in log phase SD medium.
Although strongly related to the LPD1 dihydrolipoyl dehydrogenase, it lacks the redox-active disulfide bond suggesting that it has no dehydrogenase activity.
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Present with 6400 molecules/cell in log phase SD medium.
Component of the pre-66S ribosomal particle. Interacts with NOP7 and RRP1.
Essential gene. Abrupt growth arrest prior to substantial depletion of ribosomal subunits. Fails to synthesize the 25S and 5.8S rRNA components of the 60S ribosomal subunit, and exonucleolytic 5' processing of 5.8S rRNA is strongly inhibited. Arrests at cytokinesis and fails to assemble a contractile actin ring at the bud neck.
Involved in the biogenesis of the 60S ribosomal subunit. Required for pre-rRNA processing and cytokinesis. Associates with the precursors of the 25S and 5.8S rRNAs.
Dimer of alpha and beta chains (PubMed:11739794). A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.
Present with 5590 molecules/cell in log phase SD medium.
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers (PubMed:11739794). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Covalently linked to beta-1,3-glucan of the inner cell wall layer via an alkali-sensitive ester linkage between the gamma-carboxyl group of glutamic acids, arising from a specific glutamine within the PIR1/2/3 repeat, and hydroxyl groups of glucoses of beta-1,3-glucan chains (By similarity). The alkali-sensitive linkage is induced by low pH.
Positively regulated by cell integrity signaling through MPK1 in response to cell wall perturbation. Induction is dependent on transcription factor RLM1. Down-regulated during anaerobic growth. Up-regulated by low pH.
Present with 67000 wall-bound molecules/cell in log phase YPD medium.
The strains CLIB 410 and CLIB 630 haplotype Ha2, contain large deletions that remove most of the protein.
May have a role in protecting cells from metalloid-induced proteotoxicity.
Present with 9520 molecules/cell in log phase SD medium.
Absent in G1-arrested cells and accumulates in G2-M.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Haspin subfamily.
Periodically phosphorylated during the cell cycle with a phosphorylation peak during mitosis and hyperphosphorylated after DNA damage.
Serine/threonine haspin-like protein kinase involved in cell cycle regulation.
The KEN and D (destructive) boxes are required for the cell cycle-controlled ALK2 degradation by the anaphase promoting complex (APC) pathway.
The protein kinase domain is predicted to be catalytically inactive. However, weak kinase activity was experimentally demonstrated.
Component of the telomerase complex involved in telomere replication. Stimulates RNA/DNA heteroduplex unwinding which favors the telomere replication by the telomerase.
Homodimer. Component of the telomerase complex composed of EST1, EST2, EST3 and the RNA component TLC1. Interacts with the telomerase RNA component TLC1 in presence of EST2.
Produced by ribosomal frameshifting between codon Leu-92 and Val-93.
Produced from conventional translation of the YIL009C-A ORF. There is no apparent role for isoform 2 in the cell.
Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. In an initial step, the signal sequence seems to bind simultaneously to SEC61 and SEC62. SEC62 and SEC63 are required for interactions between SEC61 and translocating polypeptides. SEC62 may affect SEC1-polypeptide interactions by increasing the affinity of targeting pathways for SEC61 and/or by modifying SEC61 to allow more efficient polypeptide interaction. A cycle of assembly and disassembly of Sec62/63 complex from SEC61 may govern the activity of the translocon. SEC62 is essential for cell growth.
Component of the heterotetrameric Sec62/63complex composed of SEC62, SEC63, SEC71 and SEC72. The Sec62/63 complex associates with the Sec61 complex to form the Sec complex.
Present with 16500 molecules/cell in log phase SD medium.
Belongs to the free Met sulfoxide reductase family.
Catalyzes the reversible oxidation-reduction of the R-enantiomer of free methionine sulfoxide to methionine. Does not act on S-enantiomer of free methionine sulfoxide or R-enantiomer of dabsylated methionine sulfoxide. Involved in protection against oxidative stress.
Present with 2610 molecules/cell in log phase SD medium.
Single deletion of fRMsr has complete growth inhibition on methionine-R-sulfoxide medium and fRMsr and MXR1 double deletion completely blocks the growth on both methionine-R-sulfoxide and methionine-S-sulfoxide medium. FRMsr and MXR2 double deletion has no effect on growth on methionine-S-sulfoxide medium. Single mutant or any of the double mutants show no growth defects in methionine medium, even the fRMsr, MXR1 and MXR2 triple deletion mutant is viable and grows similarly to wild-type. Single deletion of fRMsr has an increased sensitivity to oxidative stress and a decreased life span of 18% compared to wild-type. FRMsr and MXR1, as well as fRMsr and MXR2 double mutants, and fRMsr, MXR1 and MXR2 triple mutant show 20% reduction in life span compared with wild-type cells.
Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Belongs to the trans-sulfuration enzymes family.
Activated by nucleotides, including ATP, GTP, CTP, UTP, and ADP (PubMed:35997162). Activated by copper, manganese, calcium and magnesium ions; copper and manganese restore activity following inactivation by EDTA (ethylenediaminetetraacetic acid) (PubMed:35997162). Inhibited by metal chelators including EDTA, EGTA (ethylene glycol bis(2-aminoethyl)tetraacetic acid), and 1,10-phenanthroline (PubMed:35997162). Inhibited by copper, zinc, and iron ions (PubMed:35997162). Also inhibited by dithiothreitol p-mercuribenzenesulfonic acid, N-ethylmaleimide, protoporphyrin, hemin, protamine and triarginine (PubMed:35997162).
Belongs to the peptidase M16 family. PreP subfamily.
Decreases processing of mitochondrial precursor proteins (PubMed:25176146). Impairs mitochondrial function; increases levels of reactive oxygen species (ROS) in cells, impairs oxygen consumption and decreases the membrane potential (PubMed:25176146). Simultaneous disruption of the mitochondrial-processing peptidase subunit MAS1 or the mitochondrial peptidase OCT1 results in synthetic lethality in respiratory conditions (PubMed:25176146). Decreases processing and activity of SOD2 (PubMed:35997162).
Degrades mitochondrial transit peptides after their cleavage in the intermembrane space or in the matrix, and presequence peptides; clearance of these peptides is required to keep the presequence processing machinery running (PubMed:15772085, PubMed:25176146). Preferentially cleaves the N-terminal side of paired basic amino acid residues (PubMed:35997162). Also degrades other unstructured peptides (PubMed:25176146). May function as an ATP-dependent peptidase as opposed to a metalloendopeptidase (PubMed:35997162).
Monomer and homodimer; homodimerization is induced by binding of the substrate.
Present with 6140 molecules/cell in log phase SD medium.
Interacts with MET30. Tethered to DNA through two alternate complexes associating MET4 with MET28 and either MET31 or MET32. Interacts with MET28 and CBF1 through its leucine zipper to form a heteromeric complex.
Positive trans-acting factor capable of stimulating the transcription of the MET genes from the methionine biosynthetic pathway. MET4, MET28 and CBF1 are required for full induction of MET25 and MET16 gene transcription. MET4 controls as well the derepression of MET6. Required for the transcription of genes necessary for sulfur amino acid biosynthesis. Involved in the transcription activation of MET28 and MET30. Required for MET3 gene expression via assembly of the MET4-MET28-MET31 and MET4-MET28-MET32 complexes. Involved in response to cadmium and arsenic. Cadmium-activated MET4 also induces glutathione biosynthesis.
Present with 1300 molecules/cell in log phase SD medium.
Regulated by the general amino acid control.
The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Transcriptional activation function is inhibited by the elevation of intracellular S-adenosylmethionine (AdoMet), but is activated by cadmium and arsenic which leads to phosphorylation and prevents ubiquitination. Inactivation by oxidative stress induced by hydrogen peroxide promotes ubiquitination.
Mitochondrial GTP/GDP transporter required for GTP uptake and GDP exit from mitochondria. Involved in mitochondrial iron transport and essential for mitochondrial genome maintenance.
Interacts with RTN1; this interaction is negatively regulated by SEY1. Interacts with SEY1 and YOP1.
Plays a role in tubular endoplasmic reticulum network formation and maintenance. Works in conjunction with the ER shaping proteins (reticulons RTN1 and RTN2, YOP1), and in antagonism to SEY1 to maintain the network in a dynamic equilibrium. May counterbalance SEY1-directed polygon formation by promoting polygon loss through ring closure.
Present with 3830 molecules/cell in log phase SD medium.
Catalyzes the hydroxylation of 2-hexaprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis (PubMed:16624818, PubMed:8621692, PubMed:9452453, PubMed:23940037). Has also a structural role in the COQ enzyme complex, stabilizing COQ3 and COQ4 polypeptides (PubMed:16624818).
Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9.
Dephosphorylation by PTC7 leads to activation.
Phosphorylated (PubMed:23940037). Dephosphorylated by PTC7; dephosphorylation is essential for enzyme activation (PubMed:23940037).
Was originally thought to be involved in carbon catabolite repression (PubMed:8557031). It has later been demonstrated that the catabolite-regulation defect in COQ7 mutants was a secondary effect of the respiration deficiency in ubiquinone-deficient mutants and could be rescued by the addition of exogenous ubiquinone (PubMed:9452453).
May be involved in mitochondrial organization and biogenesis.
Produced by +1 ribosomal frameshifting between codon Leu-431 and Gly-432 of the YDR034C-C ORF.
Acts as component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors, like MATALPHA2, MIG1, RFX1 and SKO1. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex.
Associates with TUP1 to form the CYC8-TUP1 (or TUP1-SSN6) corepressor complex that is composed of 4 copies of TUP1 and one copy of CYC8. Interacts with MATALPHA2, CTI6, MIG1, TUP1, SUT1, RFX1, PGD1, HOS1, HOS2 and RPD3.
Present with 3890 molecules/cell in log phase SD medium.
[OCT+] is the prion form of CYC8. [OCT+] is the result of a conformational change of the cellular CYC8 protein that becomes self-propagating and infectious. [OCT+]-aggregates sequester soluble CYC8, resulting in increased levels of iso-2-cytochrome c, defects in sporulation and mating, higher levels of invertase derepression and increased flocculation, reminiscent of a partial loss of function of the CYC8-TUP1 corepressor complex. [OCT+] can be cured by GdnHCl and by inactivation of the molecular chaperone HSP104, which is required for [OCT+] propagation. It is speculated that prion properties of transcription factors may generate an optimized phenotypic heterogeneity that buffers yeast populations against diverse environmental insults.
Alpha subunit of the heterotrimeric guanine nucleotide-binding protein (G protein) that mediates mating pheromone signal transduction. Binding of alpha-factor or a-factor to its cognate transmembrane receptor STE2 and STE3, respectively, allows the receptor to serve as a guanine nucleotide exchange factor (GEF) on GPA1. The exchange of GDP for GTP on the G protein alpha subunit alters its interaction with the G protein beta subunit STE4, leading to dissociation of the G protein beta-gamma dimer STE4-STE18. The dissociated subunits activate downstream effectors to activate the mating response pathway and induce changes necessary to produce mating-competent cells. STE4-STE18 activate the downstream pheromone signaling MAP kinase cascade leading to expression of mating-specific genes, inducing cell cycle arrest in G1, promoting polarized cell growth to form mating projections (shmoos), and establishing the changes in plasma membrane, cell wall and nuclear envelope to permit cell-cell fusion (plasmogamy) and fusion of the two haploid nuclei (karyogamy). GPA1 transmits a signal that requires direct binding to the effector enzyme PI3K located at the endosome, promoting increased PI3 production. The intrinsic GTPase activity of GPA1 determines the duration of signaling, and is dramatically accelerated by the RGS protein SST2. In unstimulated cells, GDP-bound GPA1 sequesters the G protein beta-gamma subunit STE4-STE18, preventing it from activating the downstream effectors. Also down-regulates the signal by inhibiting the pheromone-induced accumulation of FUS3 in the nucleus.
Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by the G protein coupled receptors (GPCRs) STE2 and STE3, which serve as guanine nucleotide-exchange factors (GEFs), and inactivated by SST2, probably acting as a GTPase-activating protein (GAP).
Belongs to the G-alpha family. G(q) subfamily.
Contains an 'insertion' sequence of 109 residues which is not present in other G-protein alpha chains.
G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. In its GDP-bound form, binds to the G protein beta-gamma dimer STE4-STE18. Directly interacts with the beta subunit STE4. Probably forms preactivation complexes with unligated receptors STE2 and STE3. Interacts with FUS3. Pheromone-induced activation of GPA1 increases its association with FUS3. Interacts with SCP160. SCP160 binds specifically to the GTP-bound form of GPA1. Interacts with the phoshpatidylinositol 3-kinase (PI3K) subunits VPS15 and VPS34 at the endosome. The GTP-bound form of GPA1 binds directly and selectively to the catalytic subunit VPS34, while the GDP-bound form binds to VPS15, which appears to function as an alternative G protein beta subunit for GPA1. Interacts with regulators of G protein signaling (RGS) proteins MDM1, RAX1, RGS2 and SST2, but SST2 alone binds preferentially to the transition state conformation of GPA1, indicating that it acts as a GAP for this G protein.
Monoubiquitination targets the protein for degradation to the vacuole, and polyubiquitination tags the protein for degradation by the proteasome. This may be an additional signaling regulation mechanism.
N-myristoylation by NMT1 is pheromone-stimulated and required for palmitoylation of Cys-3. This lipid modification anchors the protein to membranes. Depalmitoylated by YLR118C/APT1.
Present with 9920 molecules/cell in log phase SD medium.
Present with 84300 molecules/cell in log phase SD medium.
Required for transport of secretory proteins from the Golgi complex. Catalyzes the transfer of phosphatidylinositol (PI) and phosphatidylcholine (PC) between membranes in vitro. Essential for viability and secretion (PubMed:2466847, PubMed:2215682). Exchanges its bound phospholipid with phospholipid monomers that reside in membrane bilayers (PubMed:16997918). Regulates specific trans-Golgi export pathways, like transport from endosomes to the trans-Golgi or transport from the plasma membrane to the vacuole at the level of the endosome (PubMed:19129178). Increased membrane curvature and lipid unsaturation levels at the trans-Golgi membrane promotes membrane binding and phospholipid transfer of SEC14. Thus, SEC14 may act at the trans-Golgi membrane to exchange lipids and promote vesicle formation (PubMed:32828847). The phosphatidylcholine-bound form of SEC14 represses the CDP-choline pathway activity by inhibiting CCTase, the rate-determining enzyme of the CDP-choline pathway (PubMed:7816798). PI binding/transfer is dispensable for function in vivo (PubMed:10488334). Required for trafficking and localization of lipid raft proteins to the plasma membrane (PubMed:23383173).
The inhibitor activity of SEC14 is controlled by whether PI or PC is bound to SEC14. The pPC-bound form of SEC14 is an inhibitor, while the PI-bound form is not. The phospholipid binding/exchange activity of SEC14 represents a mechanism by which the regulatory activity of SEC14 is itself controlled.
Belongs to the FIT family. Yeast FIT2A/YFT2 subfamily.
Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (By similarity). Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen (By similarity). This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis (PubMed:26504167) (By similarity). May directly bind to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis (By similarity). May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation (PubMed:29526591) (By similarity). May play a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Involved in phospholipid biosynthesis (PubMed:29417057) (By similarity).
Belongs to the eukaryotic ribosomal protein eL21 family.
Kinase activity is inhibited by phosphorylation and activated by dephosphorylation by CDC14.
Phosphorylation by CDK1 reduces the binding to the mother spindle pole body. The extent of phosphorylation gradually increases during cell-cycle progression until some point during late anaphase/telophase when it is rapidly dephosphorylated by CDC14. Phosphorylation inhibits kinase activity and dephosphorylation by CDC14 activates CDC15.
Protein kinase of the mitotic exit network (MEN) essential for late nuclear division in the mitotic cycle. Promotes mitotic exit by phosphorylating DBF2 and directly switching on DBF2 kinase activity. Involved in the localization of DBF2 and DBF20 to the neck which is necessary to undergo cytokinesis. Plays a role in segregation of chromosomes during recovery from spindle checkpoint activation. Required for spindle pole localization of CDK1 and inactivation of CDC2 kinase activity at the end of mitosis. Required for spindle disassembly after meiosis II and plays a role in spore morphogenesis.
The region between residues 360 and 702 is essential for function and is required for self-association and for binding to spindle pole bodies.
The region between residues 751 and 974 is an auto-inhibitory domain which inhibits MEN signaling.
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
The exocyst complex is composed of SEC3, SEC5, SEC6, SEC8, SEC10, SEC15, EXO70 and EXO84.
Needed for the assembly of the mitochondrial F1-F0 complex at high temperature.
Interacts with FIR1. Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. Component of the APT complex, which is a subcomplex of CPF, and is composed of PTI1, SYC1, SSU72, GLC7, REF2, PTA1 and SWD2.
Present with 7450 molecules/cell in log phase SD medium.
RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Negative regulator of poly(A) synthesis. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation. REF2 is required for 3'-end formation of snoRNAs.
Belongs to the glycosyl hydrolase 32 family.
Isoform Secreted is glycosylated. Isoform Intracellular is not glycosylated.
Produced by alternative initiation at Met-21 of isoform Secreted.
Component of the Asi complex, which contains ASI1, ASI2 and ASI3.
Belongs to the sirtuin family. Class I subfamily.
NAD-dependent histone deacetylase, which contributes together with HST4 to histone H3 'Lys-56' deacetylation, regulation of telomeric silencing, proper cell cycle progression, DNA damage control, DNA recombination, and genomic maintenance.
Present with 319 molecules/cell in log phase SD medium.
Present with 647 molecules/cell in log phase SD medium.
Regulates cell surface growth, bud formation and morphogenesis. May act indirectly by regulating factor(s) involved in these processes.
May be involved in growth at elevated pH and presence of calcium.
Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. Component of the APT complex, which is a subcomplex of CPF, and is composed of PTI1, SYC1, SSU72, GLC7, REF2, PTA1 and SWD2.
Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation. PTI1 is required for 3'-end formation of snoRNAs.
Binds 2 magnesium or manganese ions per subunit. Manganese is about 20 times more efficient than magnesium.
It has a serine and a weak tyrosine phosphatase activity with ratios of serine to tyrosine phosphatase activity as high as 200:1. It is essential for growth or germination at 37 degrees Celsius. May have a role in the heat shock response. Involved in tRNA splicing and cell separation.
Present with 1520 molecules/cell in log phase SD medium.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. NCD subfamily.
Essential for yeast nuclear fusion during mating. KAR3 is a bifunctional protein having a kinesin-like motor domain joined to a distinct microtubule binding domain. It may mediate microtubule sliding during nuclear fusion and possibly mitosis. May interact with spindle microtubules to produce an inwardly directed force acting upon the poles. KAR3 function antagonizes CIP8 and KIP1 outward force action. KAR3 motor activity is directed toward the microtubule's minus end.
KAR3 contains two globular domains separated by an alpha-helical coiled coil. The N-terminal portion of KAR3 contains a microtubule association domain distinct from the kinesin-like C-terminal domain.
Homocysteine S-methyltransferase involved in the conversion of S-adenosylmethionine (AdoMet) to methionine to control the methionine/AdoMet ratio. Converts also S-methylmethionine (SMM) to methionine.
Present with 60300 molecules/cell in log phase SD medium.
Up-regulated in response to high extracellular methionine.
Involved in nonsense-mediated decay of mRNAs containing premature stop codons.
Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP (PubMed:12597897). Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate to form deamido-NAD(+) (NaAD). Key enzyme in both de novo and salvage pathways for NAD(+) biosynthesis (By similarity). Predominantly acts in the salvage pathways via NMN (PubMed:11884393).
Expression is slightly induced in late log phase.
E3 RING-finger protein, member of the UBC2/RAD6 epistasis group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA. The UBC2-RAD18 complex cooperates with RAD5 and the UBC13-MMS2 dimer to attach mono-ubiquitin chains on 'Lys-164' of POL30, which is necessary for PRR. The UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine.
Homodimer. Interacts with E2 UBC2, forming a complex with ubiquitin ligase activity. The UBC2-RAD18 complex interacts itself with the UBC13-MMS2 ubiquitin ligase complex through direct interactions of both RAD18 and UBC13 with RAD5. Interacts also with UBC9. Binds single strand DNA.
Present with 206 molecules/cell in log phase SD medium.
Belongs to the DNA mismatch repair MutS family.
Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. MSH6 provides substrate-binding and substrate specificity to the complex. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs. Acts mainly to repair base-base and single insertion-deletion mismatches that occur during replication, but can also repair longer insertion-deletion loops (IDLs), although with decreasing efficiency as the size of the extrahelical loop increases. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis by the MutS alpha complex is crucial for MMR. Both subunits bind ATP, but with differing affinities, and their ATPase kinetics are also very different. MSH6 binds and hydrolyzes ATP rapidly, whereas MSH2 catalyzes ATP at a substantially slower rate. Binding to a mismatched base pair suppresses MSH6-catalyzed ATP hydrolysis, but not the activity of MSH2. ATP binding to both subunits is necessary to trigger a change in MutS alpha interaction with mismatched DNA, converting MutS alpha into a sliding clamp capable of hydrolysis-independent movement along DNA, and also facilitates formation of ternary complexes containing MutS and MutL proteins and the mismatch. May also be involved in resolution of recombination intermediates.
Heterodimer consisting of MSH2-MSH6 (MutS alpha). Forms a ternary complex with MutL alpha (MLH1-PMS1). MutS alpha interacts with proliferating cell nuclear antigen (PCNA/POL30). This interaction is disrupted upon binding of MutS alpha to mismatch DNA.
Present with 5330 molecules/cell in log phase SD medium.
The PIP box serves as a PCNA(POL30)-recognition and -binding motif.
Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the genomic RNA-nucleocapsid complex.
Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein, and this cleavage is a prerequisite for subsequent processing at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs.
Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome.
Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein.
Nucleocapsid protein p11 (NC) forms the nucleocore that coats the retro-elements dimeric RNA. Binds these RNAs through its zinc fingers (By similarity). Promotes primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty3 RNA and initiation of reverse transcription.
Produced by +1 ribosomal frameshifting between codon Ala-285 and Val-286 of the YGR109W-A ORF.
Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty3 retrotransposons belong to the gypsy-like elements (metaviridae).
Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends.
The protease is a homodimer, whose active site consists of two apposed aspartic acid residues.
Subject to nitrogen catabolite repression (NCR). Not found in cells grown on rich nitrogen sources like ammonia, glutamine or glutamate, but is found in cells that have been subjected to nitrogen starvation or have been grown on a poor nitrogen source such as proline.
There are 4 copies for L-asparaginase 2 in yeast. The 4 identical copies ASP3-1, ASP3-2, ASP3-3 and ASP3-4 are arranged in tandem repeats located near a ribosomal DNA cluster.
Yeast contains 2 L-asparaginase isoenzymes: cytoplasmic L-asparaginase I, and cell wall L-asparaginase II.
Belongs to the mitochondrial carrier (TC 2.A.29) family. SLC25A38 subfamily.
Mitochondrial glycine transporter that imports glycine into the mitochondrial matrix. Plays an important role in providing glycine for the first enzymatic step in heme biosynthesis, the condensation of glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the mitochondrial matrix.
Yeasts grow well on the fermentable carbon source dextrose, but only poorly aerobically on glycerol, indicating a defect in respiration. Furthermore, the deletion strain is unable to reduce sodium nitroprusside, indicating that the defect is likely in heme biosynthesis. Nitroprusside reduction can be rescued by supplementation of the medium with either glycine or 5-aminolevulinate (ALA) (PubMed:19412178). In combination with a disruption of MCX1, abrogates mitochondrial respiration (PubMed:25957689).
Component of the NTR complex (NTC-related complex), composed of NTR1, NTR2 and PRP43. Interacts with CLF1 and NTR2. Interacts with PRP43 and PRP45.
Involved in pre-mRNA splicing and spliceosome disassembly. Promotes release of excised lariat intron from the spliceosome by acting as a receptor for PRP43. This targeting of PRP43 leads to disassembly of the spliceosome with the separation of the U2, U5, U6 snRNPs and the NTC complex.
Belongs to the universal ribosomal protein uL23 family.
Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). uL23 is associated with the polypeptide exit tunnel (PubMed:9559554, PubMed:22096102).
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. uL23 is a major component of the universal docking site for these factors at the polypeptide exit tunnel.
Component of the SAC3-THP1 complex, which functions in transcription-coupled mRNA export from the nucleus to the cytoplasm. SAC3-THP1 functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket. THP1 binds to RNA in vitro.
Heterodimer with THP1. The SAC3-THP1 complex interacts with CDC31 and SUS1, and with the mRNA export factor MEX67-MTR2, the TREX complex component SUB2, and the nucleoporin NUP1.
Belongs to the tRNA pseudouridine synthase TruA family.
Mitochondrial-specific pseudouridine synthase catalyzing the formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of mitochondrial transfer RNAs.
Binds 1 thiamine pyrophosphate per subunit.
Catalyzes a carbon-carbon cleavage reaction; cleaves a 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde.
Peroxisomal targeting signal 1 (PTS1) is a tripeptide located at the C-terminus of more than 95% of all peroxisomal matrix proteins. The prototypical PTS1 is the terminal tripeptide SKL (serine-lysine-leucine) but the consensus of PTS1 is defined as [S/A/H/C/E/P/Q/V] [K/R/H/Q] [L/F]. However, this description of the PTS1 consensus must probably be expanded beyond the terminal tripeptide.
Mannosyltransferase involved in adding the 4th and 5th mannose residues of O-linked glycans.
Essential for proper morphogenesis of the vacuole. May exist as structural reinforcement on the surface of the vacuolar membrane and be required for maintenance against rupture by osmotic pressure.
Possibly multimeric. Associates with VAM3.
Present with 2360 molecules/cell in log phase SD medium.
Transport of phosphate groups from the cytosol to the mitochondrial matrix.
Heterodimer with TFC6. Component of the TFIIIC complex composed of TFC1, TFC3, TFC4, TFC6, TFC7 and TFC8. The subunits are organized in two globular domains, tauA and tauB, connected by a proteolysis-sensitive and flexible linker. Interacts with SPT15 and directly with TFC6.
TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauB domain of TFIIIC that binds boxB DNA promoter sites of tRNA and similar genes. Plays a role in TFIIB assembly through its interaction with SPT15/TBP. Essential for cell viability.
Ty1-JR1 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Ty1-LR3 is a highly expressed element. Induced under amino acid starvation conditions by GCN4.
Ty1-ML2 is a highly expressed element. Induced under amino acid starvation conditions by GCN4.
Belongs to the TRAPP small subunits family. TRAPPC4 subfamily.
Component of the TRAPP I, TRAPP II and TRAPP III complexes which act as guanine nucleotide exchange factors (GEF) for YPT1. TRAPP I plays a key role in the late stages of endoplasmic reticulum to Golgi traffic. TRAPP II plays a role in intra-Golgi transport. TRAPP III plays a role in autophagosome formation.
Present with 3130 molecules/cell in log phase SD medium.
Involved in amino acid permease processing and required for the efficient translocation of structurally related amino acid permeases from the endoplasmic reticulum to the plasma membrane. SHR3 may function as a permease-specific 'adaptor' molecule that functions in conjunction with the SEC62/SEC63 complex. Yeast cells may require SHR3 to expedite the processing of permeases to ensure their rapid expression at the plasma membrane in response to changing environmental conditions.
Present with 6510 molecules/cell in log phase SD medium.
Belongs to the methyltransferase superfamily. RRP8 family.
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of adenine 645 in 25S rRNA. Required both for ribosomal 40S and 60S subunits biogenesis. Required for efficient pre-rRNA cleavage at site A2. Also involved in telomere length regulation and maintenance.
Required for the assembly of cytochrome c oxidase.
Associated with the 60S pre-ribosomal particles. Interacts with NAP1.
Present with 3640 molecules/cell in log phase SD medium.
Required for 60S pre-ribosomal subunits export to the cytoplasm. May also be required for 60S ribosomal subunit maturation and accumulation. Involved in G1 events and passage through start, and possibly actin cytoskeleton organization.
Binds F-actin, but not G-actin. Interacts with the ARP2/3 complex. Interacts with APP1, ARK1, PRK1, SCP1, SRV2 and YIR003W via its SH3 domain. Interacts with the SH3 domain of RVS167 and with SLA1.
Regulates ARP2/3 complex-mediated actin assembly. Recruits ARP2/3 complex to sides of preexisting actin filaments, which may promote nucleation or stabilization of filament branches. Binds to actin filaments, but not actin monomers. Actin binding is required for ARP2/3 complex activation. May also have a role in linking the actin cytoskeleton to endocytosis. recruits components of the endocytotic machinery to cortical actin patches, known sites of endocytosis.
The actin depolymerizing factor homology (ADF) domain mediates actin filament binding.
Component of the pre-66S ribosomal particle. Interacts with NOP7, RRP1 and RRP15 (By similarity).
Involved in the biogenesis of the 60S ribosomal subunit.
Present with 2860 molecules/cell in log phase SD medium.
Required for respiratory activity and maintenance and expression of the mitochondrial genome.
Cell wall protein that participates directly in adhesive cell-cell interactions during yeast flocculation, a reversible, asexual and Ca(2+)-dependent process in which cells adhere to form aggregates (flocs) consisting of thousands of cells. The lectin-like protein sticks out of the cell wall of flocculent cells and selectively binds mannose residues in the cell walls of adjacent cells. Activity is inhibited by mannose, but not by glucose, maltose, sucrose or galactose.
For many industrial applications in which the yeast S.cerevisiae is used, e.g. beer, wine and alcohol production, appropriate flocculation behavior is one of the most important characteristics of a good production strain. The ability of yeast cells to flocculate is of considerable importance, as it provides an effective, environment-friendly, simple and cost-free way to separate yeast cells from the fermentation product at the end of fermentation.
Capable of resolving Holliday junctions. Specific for 4-way junctions. Seems to be important for the maintenance of mitochondrial DNA. Cleaves fixed junctions at the point of strand exchange. Cleaves after 5'-CT-3' sequence.
Belongs to the RIC1 family. Highly divergent.
Present with 78 molecules/cell in log phase SD medium.
The RIC1-RGP1 complex acts as a guanine nucleotide exchange factor (GEF), which activates YPT6 by exchanging bound GDP for free GTP. It is thereby required for efficient fusion of endosome-derived vesicles with the Golgi. The RIC1-RGP1 participates in the recycling of SNC1, presumably by mediating fusion of endosomal vesicles with the Golgi compartment. May also be indirectly involved in the transcription of both ribosomal protein genes and ribosomal RNA.
Component of the mitochondrial outer membrane sorting assembly machinery (SAM or TOB) complex, which at least consists of SAM35, SAM37 and SAM50. SAM37 interacts with TOM70.
Component of the mitochondrial outer membrane sorting assembly machinery (SAM or TOB) complex, which is required for the sorting of proteins with complicated topology, such as beta-barrel proteins, to the mitochondrial outer membrane after import by the TOM complex.
Expression is induced in the stationary phase.
Forms an active dehydrodolichyl diphosphate synthase complex with NUS1.
With NUS1, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER).
Forms conjugate with SPH1 and HBT1. Involved in morphogenesis.
Component of the CHS5/6 complex composed of the 4 CHAPS proteins BCH1, BCH2v, BUD7, and CHS6 as well as at least CHS5 and GTP-bound ARF1. The complex interacts with the cargo protein CHS3.
Member of the CHS5-ARF1P-binding proteins (CHAPS) which mediates export of specific cargo proteins, including chitin synthase CHS3. May be involved in positioning the proximal bud pole signal.
Confers resistance to the sphingolipid biosynthesis inhibitor drug myriocin (ISP-1). Inactivates ISP-1 by converting it into N-acetyl-myriocin. Cooperates with YPK1 in mediating resistance to myriocin.
Interacts with STE11 through the respective SAM domains.
Involved in growth arrest during conjugation. May interact with the G protein alpha subunit.
Present with 1670 molecules/cell in log phase SD medium.
Phosphorylated by CDC28, probably in association with G1 cyclin CLN2.
Weakly suppresses a RAD53 null mutation when overexpressed.
Belongs to the peroxisomal targeting signal receptor family.
Interacts (via WxxxF/Y and LVxEF motifs) with PEX14; promoting translocation through the PEX13-PEX14 docking complex.
Monoubiquitinated at Cys-6 by PEX2 during PEX5 passage through the retrotranslocation channel: monoubiquitination acts as a signal for PEX5 extraction and is required for proper export from peroxisomes and recycling (PubMed:15632140, PubMed:17452527, PubMed:35768507). Ubiquitination at Cys-6 is UBC4-independent but requires the presence of PEX4 (PubMed:17550898, PubMed:17452527). When PEX5 recycling is compromised, polyubiquitinated at Lys-18 and Lys-24 by PEX10 during its passage through the retrotranslocation channel, leading to its degradation (PubMed:15283676, PubMed:15536088, PubMed:17452527, PubMed:35768507). Ubiquitination at Lys-18 and Lys-24 are UBC4-dependent (PubMed:15283676, PubMed:15536088, PubMed:17550898). Monoubiquitination at Cys-6 and polyubiquitination at Lys-18 and Lys-24 are removed by UBP15 in the cytosol, resetting PEX5 for a subsequent import cycle (PubMed:21665945).
Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) (PubMed:8265627, PubMed:7980572, PubMed:14562106, PubMed:35768507). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14 docking complex along with cargo proteins (PubMed:9094717). PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle (PubMed:35768507).
The TPR repeats mediate interaction with proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type).
The WxxxF/Y motifs mediate interaction with PEX14, promoting association with the PEX13-PEX14 docking complex.
The amphipathic helix 1 and 2 (AH1 and AH2, respectively) are required for PEX5 retrotranslocation and recycling. AH2 mediates interaction with lumenal side of the PEX2-PEX10-PEX12 ligase complex, while AH1 is required for extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex.
Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by the guanine nucleotide-exchange factor (GEF) VPS9 and inactivated by GTPase-activating proteins (GAPs) GYP1 and GYP3.
Belongs to the small GTPase superfamily. Rab family.
Interacts in its active GTP-bound form with PEP7/VAC1.
Present with 8759 molecules/cell in log phase SD medium.
Required for protein transport to the vacuole. Involved in two vesicle trafficking steps to the prevacuolar compartment (PVC), regulating the docking of endosomes and Golgi vesicles to the PVC by interacting with PEP7/VAC1 on the PVC membrane and promoting SNARE complex formation.
Present with 1390 molecules/cell in log phase SD medium.
Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.
Deaminates adenosine-37 to inosine in tRNA-Ala.
Required for the insertion of integral membrane proteins into the mitochondrial inner membrane. Essential for the activity and assembly of cytochrome c oxidase. Plays a central role in the translocation and export of the C-terminal part of the COX2 protein into the mitochondrial intermembrane space.
Present with 14800 molecules/cell in log phase SD medium.
Regulatory protein involved in Cu/Fe utilization and stress resistance. Involved in basal level transcription of FRE1 and H(2)O(2)-induced transcription of CTT1. Regulates the transcription of CTR1 and CTR3 via the copper ion responsive elements in their promoters. Required for degradation of CTR1.
Belongs to the eukaryotic ribosomal protein eS1 family.
Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). eS1 interacts directly with uS11 and eS26, which form part of the mRNA exit tunnel (PubMed:9559554, PubMed:22096102).
Present with 92400 molecules/cell in log phase SD medium.
Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.
Belongs to the adenosylhomocysteinase family.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YGR038C-A ORF.
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC24 specifically recruits cargo proteins like BET1 or SYS1 to the COPII vesicles. The SEC23/24 complex is also involved in internalization of plasma membrane proteins like the maltose transporter.
The COPII coat is composed of at least 7 proteins: the SEC23/24 complex, the SEC13/31 complex, SFB2, SFB3 and the protein SAR1. Interacts with BET1, EMP24, GRH1, SEC22, SED5 and SYS1.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YJR026W ORF.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. Interacts with POM152 and NIC96.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP188 probably plays an important role in NPC assembly and organization.
Belongs to the dethiobiotin synthetase family.
Dethiobiotin synthetase involved in the biotin biosynthesis pathway.
Aberrant morphology characterized by intraperoxisomal vesicles or invaginations.
By oleic acid. Transcriptionally up-regulated by YRM1 along with genes involved in multidrug resistance. Expression is also dependent on RSF1 and RSF2 for transcriptional induction during growth on glycerol-based medium.
Has acyl esterase, lipase and phospholipase A activity.
Present with 2350 molecules/cell in log phase SD medium.
The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). Has ATPase activity.
Component of the PAM complex, at least composed of SSC1 (mtHsp70), MGE1, TIM44, PAM16/TIM16, PAM17 and PAM18/TIM14. Forms part of the receptor complex that consists of at least 3 different proteins (TIM17, TIM23, TIM44).
Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Recruits mitochondrial HSP70 and its co-chaperone (MGE1) to drive protein translocation into the matrix using ATP as an energy source.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Present with 5750 molecules/cell in log phase SD medium.
Catalyzes the isomerization of citrate to isocitrate via cis-aconitate, a step in the citric acid cycle. Can also provide minor contributions to the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis. Also plays an essential role in mtDNA maintenance. May directly protect mtDNA from accumulation of point mutations and ssDNA breaks as a component of mitochondrial nucleoids, or by preventing accumulation of iron citrate thereby alleviating its detrimental effects in mitochondria.
Essential for growth on nonfermentable carbon sources and for biosynthesis of glutamate. Causes a dramatic increase in cellular citrate levels.
Highly induced in the absence of glutamate. Induction is further increased when both glutamate and lysine are missing.
Monomer. Binds to mitochondrial DNA (mtDNA) and identified as component of mitochondrial nucleoids.
Present with 96700 molecules/cell in log phase SD medium.
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.
Required for cell growth and for the G2->M transition of the cell division cycle. Mediates a protein kinase cascade; it activates BCK1 which itself activates MKK1/MKK2.
GTPase-activating protein (GAP) for CDC42 and/or RHO1.
Present with 254 molecules/cell in log phase SD medium.
Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain VTC4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation (PubMed:19390046). The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen (PubMed:25315834, PubMed:19390046). PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase (PubMed:25315834). The VTC complex also plays a role in vacuolar membrane fusion (PubMed:11102525, PubMed:11823419). Required for SEC18/NSF activity in SNARE priming, membrane binding of LMA1 and V(0) trans-complex formation (PubMed:11823419). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important intracellular signaling molecules. Inositol polyphosphate binding promotes vacuolar polyphosphate synthesis (PubMed:27080106).
Present with 2630 molecules/cell in log phase SD medium.
May regulate the transcription of maltase and maltose permease genes.
The gene is not associated with corresponding maltase and maltose permease genes on chromosome 16 as it is the case for the other functional maltose fermentation loci, so its transcription regulation activity is speculative.
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication. DOC1 is required, together with the coactivators CDH1 and CDC20, for recognition and binding of the substrates.
Present with 1364 molecules/cell in log phase SD medium.
Belongs to the oligopeptide OPT transporter family.
High affinity transporter for glutathione. Also transports tetra- and pentapeptides like the opioids leucine enkephalin (Tyr-Gly-Gly-Phe-Leu) and methionine enkephalin (Tyr-Gly-Gly_Phe-Met) across the cell membrane.
Present with 2870 molecules/cell in log phase SD medium.
Associates with nascent pre-60S particles that have not yet entered the translating pool, and is released from mature 60S subunits. Interacts with pre-60S factors NMD3, LSG1, and TIF6.
Pre-60S-associated cytoplasmic factor involved in the cytoplasmic maturation of the 60S subunit. May act redundantly with REI1 to directly promote a stabilizing structural rearrangement in cytoplasmic 60S subunit maturation independent on the REI1-specific ARX1 recycling.
Present with 2240 molecules/cell in log phase SD medium.
Belongs to the eukaryotic ribosomal protein eS21 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). eS21 is required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Has a physiological role leading to 18S rRNA stability (PubMed:14627813).
N-terminally acetylated by acetyltransferase NatB.
Present with 15300 molecules/cell in log phase SD medium.
Reduction in growth rate, a decrease in free 40S subunits, an increase in the amount of free 60S subunits and a decrease in polysome size.
Interacts with the 35S, 23S and 20S pre-rRNAs and with the U3 snoRNA.
Involved in ribosome biogenesis. Required for normal pre-rRNA processing in internal transcribed spacer 1 (ITS1). May be involved in the movements of the replication forks.
Present with 3670 molecules/cell in log phase SD medium.
Transiently up-regulated during the initial 15 minutes of dough-fermentation.
By the DNA-damaging agent methyl methanesulphonate (MMS) (at protein level).
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.
Phosphorylation on Ser-62 impairs ATP synthase dimerization.
Coiled-Coils at the N-terminal half are essential for interaction with VPS30 and VPS34 and autophagy.
Component of the autophagy-specific VPS34 PI3-kinase complex I composed of VPS15, VPS30, VPS34, ATG14 and ATG38. Interacts directly with ATG38.
Nitrogen starvation or rapamycin treatment rapidly causes a more than 20-fold induction of expression. The expression is dependent on GLN3.
Required for cytoplasm to vacuole transport (Cvt) and autophagy as a part of the autophagy-specific VPS34 PI3-kinase complex I. This complex is essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. ATG14 mediates the specific binding of the VPS34 PI3-kinase complex I to the preautophagosomal structure (PAS).
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.
Regulates the coordinate transcription of structural MAL3S (maltase) and MAL3T (maltose permease) genes.
Belongs to the fungal cytochrome c oxidase subunit 7a family.
Present with 35500 molecules/cell in log phase SD medium.
Allosterically activated by ATP (PubMed:8141771). ATP binding is a prerequisite to magnesium and substrate binding (By similarity). ATP binds to 2 of the subunits in the homotetramer inducing a closure of these 2 subunits and the release of the C-terminal loop, thereby activating the enzyme (By similarity).
IMP-specific 5'-nucleotidase involved in IMP (inosine 5'-phosphate) degradation.
Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues. Acts on the two major protein phosphatase 2A catalytic subunits, PPH21 and PPH22.
Interacts with the G1/S-specific cyclin PCL1.
Involved in exit from mitosis and pseudohyphal differentiation.
Phosphorylated by the cyclin-CDK complex PCL1-PHO85.
Acidic phospholipids or fatty acids are important for the ferrochelatase activity.
Catalyzes the ferrous insertion into protoporphyrin IX.
Ferrochelatase interacts with protoprophyrinogen oxidase, and associates with complex 1 of the respiratory chain.
Present with 22700 molecules/cell in log phase SD medium.
The leader peptide may be processed in two proteolytic steps, first between Ser-23 and Phe-24, second and by a different protease, to yield the mature protein.
Belongs to the AB hydrolase superfamily. Lipase family.
Lipases catalyze the hydrolysis of the ester bond of tri-, di- and monoglycerides of long-chain fatty acids into fatty acids and glycerol.
It is uncertain whether Met-1 or Met-31 is the initiator.
Non-catalytic component of the proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. PRE3 and PRE4 are necessary for the peptidyl-glutamyl-peptide-hydrolyzing activity.
Present with 16900 molecules/cell in log phase SD medium.
The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with CIC1.
Belongs to the bZIP family. YAP subfamily.
Homodimer (By similarity). Interacts with the C-terminal, cytoplasmic tail of the multidrug resistance ABC transporter PDR5.
One of 8 closely related fungi-specific YAP proteins (YAP1 to YAP8), which all seem to be transcription activators of the environmental stress response and metabolism control pathways and to have similar but not identical DNA binding specificities.
Transcription activator involved in the regulation of genes expressed in response to environmental changes. When overexpressed it activates transcription of the multidrug resistance ABC transporter PDR5, thus conferring resistance to the fungicide fluconazole (FCZ) and cycloheximide. When overexpressed, it also confers, independent of PDR5, increased resistance to 4-nitroquinoline-N-oxide (4-NQO) (By similarity). Preferentially binds 5'-TTACTAA-3'.
Appears to be specifically required for the splicing of the terminal intron (bI5) of the cytochrome b pre-mRNA. Can also stimulates the splicing of the omega intron of the precursor of large ribosomal RNA.
Co-chaperone that binds to the molecular chaperone HSP82 and stimulates its ATPase activity. Although not essential, it confers thermotolerance when intracellular levels of HSP82 are limiting.
Present with 8528 molecules/cell in log phase SD medium.
Interacts with the 40S ribosomal subunit.
The PUA and the SUI1 domains may be involved in RNA binding.
ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Belongs to the DEAD box helicase family. DDX56/DBP9 subfamily.
Binds with high affinity to SRP1 only in the presence of RanGTP. The complex is dissociated by the RanGTP-binding protein YRB1.
Export receptor for importin alpha (SRP1). Mediates importin-alpha re-export from the nucleus to the cytoplasm after import substrates have been released into the nucleoplasm.
Present with 23500 molecules/cell in log phase SD medium.
Involved in the uptake of non-siderophore and siderophore sources of iron. Has a role in the retention of iron in the cell wall and periplasmic space.
Interacts with SKP1. Component of the probable SCF(SKP2) complex containing CDC53, SKP1, RBX1 and SKP2. May interact with ribosomes.
Stabilizes the adenosylphosphosulfate kinase MET14 which leads to accumulation H(2)S and SO(2).
Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins (By similarity). Regulates protein levels of sulfur metabolism enzymes. The SCF(SKP2) complex may regulate some transcription factors or regulators of cysteine and methionine biosynthesis.
Belongs to the eukaryotic mitochondrial porin family.
Consists mainly of membrane-spanning sided beta-sheets. 19 strands distributed along the entire VDAC protein, have the potential to adopt transmembrane beta pleated sheet structures, which rolled together may form a 'beta-barrel' type structure, possessing pore dimensions.
Forms a channel through the cell membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. Is the major permeability factor of the mitochondrial outer membrane.
Belongs to the inositol monophosphatase superfamily.
Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Regulates the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS. Involved in salt tolerance. Confers resistance to lithium.
Component of the global genome repair (GGR) complex composed of at least ABF1, RAD7 and RAD16. Interacts with PSE1.
Contains 2 important clusters of amino acid residues in the C terminus (C-terminal sequence 1 or CS1, residues 624 to 628; and CS2, residues 639 to 662). CS1 specifically participates in transcriptional silencing and/or repression in a context-dependent manner, whereas CS2 is universally required for all functions of ABF1.
Extensively phosphorylated on Ser and Thr residues.
General regulatory factor (GRF) that contributes to transcriptional activation of a large number of genes, as well as to DNA replication, silencing and telomere structure. Involved in the transcription activation of a subset of ribosomal protein genes. Binds the ARS-elements found in many promoters. Binds to the sequence 5'-TCN(7)ACG-3'. Influences on genome-wide nucleosome occupancy and affects chromatin structure, and probably dynamics. As a component of the global genome repair (GGR) complex, promotes global genome nucleotide excision repair (GG-NER) which removes DNA damage from nontranscribing DNA. Component of the regulatory network controlling mitotic and meiotic cell cycle progression.
Component of the RPD3C(L) histone deacetylase complex (HDAC). Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. ASH1 is necessary to repress HO in daughter cells to block mating-type switching through its binding to HO promoter 5'-YTGAT-3' sites. Also involved in pseudohyphal growth.
Present with 1800 molecules/cell in log phase SD medium.
The ASH1 mRNA is transported to the daughter cell before cytokinesis where translation produces the protein to block mating-type switching. The ASH1 mRNA 3'-UTR and the mRNA localization machinery that are essential to restrict accumulation to the bud.
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (By similarity).
Could regulate export of the bud site and axial growth sites selection protein AXL2 and possibly other secretory proteins from the endoplasmic reticulum in COPII-coated vesicles. Seems to be required for axial budding pattern in haploid cells.
Defects in cell polarity. Strains homozygous for ERV14 deletion do not sporulate.
Required for the ingression of the plasma membrane into the bud neck at the end of cytokinesis, leading to the separation of the mother and daughter cells. Stimulates the synthesis of the primary septum (PS) by CHS2.
The C2 domain is essential for membrane ingression during cytokinesis, but not for recruitment to the actomyosin ring.
Component of the SWI/SNF global transcription activator complex. The 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29.
Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase subunit family.
Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes. Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA. Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits: RPO21, RPB2, RPB3, RPB4, RPB5, RPO26, RPB7, RPB8, RPB9, RPB10 and RPC10. Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits.
DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. RNA polymerase complexes are composed of mobile elements that move relative to each other. In Pol II, RPB5 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. Seems to be the major component in this process.
Belongs to the two pore domain potassium channel (TC 1.A.1.8) family.
Targets and/or maintains KAR3 at the spindle pole body during vegetative growth.
Important for mitochondrial DNA (mtDNA) stability and repair. Recognizes and binds to base-base and small insertion-deletion mismatches in mtDNA. ATP binding and hydrolysis is crucial for function. Binding to a mismatched base pair attenuates ATP hydrolysis. Also involved in proper sorting of mtDNA during mtDNA transmission.
Present with 7350 molecules/cell in log phase SD medium.
Expression shows a peak at the start of the cell cycle just before bud emergence in late G1 phase.
Interacts with BEM1, BUD3, BUD4, BUD5, CDC24 and CDC42.
O-glycosylated by PMT4 and N-glycosylated. O-glycosylation increases activity in daughter cells by enhancing stability and promoting localization to the plasma membrane. May also be O-glycosylated by PMT1 and PMT2.
Ref.5 refers to this gene as REV7. REV7 is however the adjacent gene.
Required for haploid cells axial budding pattern. Acts as an anchor to help direct new growth components and/or polarity establishment components like the BUD5 GTP/GDP exchange factor to localize at the cortical axial budding site. Regulates septin organization in late G1 independently of its role in polarity-axis determination.
Component of the Golgi to ER traffic (GET) complex, which is composed of GET1, GET2 and GET3. Within the complex, GET1 and GET2 form a heterotetramer which is stabilized by phosphatidylinositol binding and which binds to the GET3 homodimer (PubMed:32910895).
Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Together with GET2, acts as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. The GET complex cooperates with the HDEL receptor ERD2 to mediate the ATP-dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER. Involved in mitochondrial distribution and morphology.
Present with 8120 molecules/cell in log phase SD medium.
Belongs to the MICOS complex subunit Mic60 family.
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway.
Component of the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MIC10, MIC12, MIC19, MIC26, MIC27 and MIC60. This complex was also known under the names MINOS or MitOS complex. Interacts with TOM22 and TOM40 in a MICOS-independent manner, resulting in coupling with the outer membrane. Interacts with MIA40, OM45 and POR1.
Increases frequency of mitochondrial genome loss and leads to altered mitochondrial morphology. Moderately reduces mitochondrial membrane potential and import efficiency of preproteins that are transported into or across the inner membrane via TIM23 complex. Impairs precursor protein import via the MIA pathway. 60-70% of mitochondria exhibit an increased inner membrane surface and stacks of lamellar cristae disconnected from the inner boundary membrane.
Present with 5730 molecules/cell in log phase SD medium.
Component of the RSP5-BUL1/2 ubiquitin ligase complex composed of at least RSP5 and BUL1 or BUL2 (PubMed:8668140, PubMed:9931424). Component of the RSP5-UBA1-UBC5 ubiquitin ligase complex composed of E3 RSP5, E1 UBA1 and E2 UBC5 (Probable). Forms also a ternary complex with RUP1 and UBP2 (PubMed:15933713). Interacts (via WW domains) with LSB1 (PubMed:22000681). Interacts (via WW domains) with PIN3/LSB2 (PubMed:22000681). Interacts (via WW domains) with RCR1 (via PY motifs) (PubMed:17213653). Interacts with UBP2; the interaction is direct (PubMed:19920177). Interacts with HSE1 (PubMed:15086794, PubMed:17079730). Interacts with LAS17 (PubMed:22000681). Interacts with ROG3 (PubMed:12163175). Interacts with ROD1 (PubMed:12163175). Interacts with RVS167 (PubMed:22000681). Interacts with ubiquitin (PubMed:21399621).
E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:19920177, PubMed:7708685, PubMed:15933713). Component of a RSP5 ubiquitin ligase complex which specifies polyubiquitination and intracellular trafficking of the general amino acid permease GAP1 as well as other cell surface proteins like GAP1, FUR4, MAL61, PMA1 and STE2 (PubMed:8596462). The RSP5-BUL1/2 complex is also necessary for the heat-shock element (HSE)-mediated gene expression, nitrogen starvation GLN3-dependent transcription, pressure-induced differential regulation of the two tryptophan permeases TAT1 and TAT2 and sorting efficiency into multivesicular bodies (PubMed:15247235, PubMed:16864574, PubMed:17079730, PubMed:14560004, PubMed:12821147, PubMed:15020711, PubMed:9931424). The RSP5-UBA1-UBC5 ubiquitin ligase complex ubiquitinates RPO21 forming 'Lys-63'-linked polyubiquitin chains (PubMed:19920177, PubMed:9858558). Plays a role in tolerance to o-dinitrobenzene (PubMed:12163175). Involved in actin cytoskeleton organization and dynamics (PubMed:22000681). Ubiquitinates the LAS17-binding proteins LSB1 and PIN3/LSB2 without directing them for degradation and affects LAS17 levels in a SLA1-dependent and LSB1/2-independent manner (PubMed:22000681).
The ubiquitination appears to be the result of an intramolecular transfer of ubiquitin.
Present with 12000 molecules/cell in log phase SD medium.
The alpha and beta forms are probably products of the same gene with different post-translational modifications.
The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.
Binds the RNA motif 5'-AAUAA[U/C]AUUCUU-3' in the 3'-UTR of mitochondrial mRNAs (PubMed:33876744, PubMed:10441495, PubMed:10905425). Involved in the processing or stability of mitochondrial mRNAs (PubMed:33876744, PubMed:17194787, PubMed:17194786).
Phosphorylated (PubMed:10905425). Phosphorylation promotes binding to RNA (PubMed:10905425).
Component of the mitotic checkpoint complex (MCC) which consists of MAD2, MAD3, BUB3 and CDC20. Interacts with CDC20 and BUB3.
Component of the spindle assembly checkpoint which is a feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. Component of the mitotic checkpoint complex (MCC) which inhibits the ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) by preventing its activation by CDC20.
Present with 3170 molecules/cell in log phase SD medium.
To yeast protein kinase BUB1 in its non-catalytic N-terminal domain.
Lipid particle-localized triacylglycerol (TAG) lipase. The lipid droplet/particle is a lipid storage compartment which serves as a depot of energy and building blocks for membrane lipid biosynthesis. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs, releasing and supplying specific fatty acids to the appropriate metabolic pathways (PubMed:16135509). Also catalyzes the acylation of lysophosphatidic acid (LPA) (PubMed:20016004).
Loses its lipolytic activity in cells lacking nonpolar lipids, but retains its side activity as lysophospholipid acyltransferase.
Belongs to the cytochrome c-type heme lyase family.
Lyase that catalyzes the covalent linking of the heme group to the cytochrome C1 apoprotein to produce the mature functional cytochrome.
Cysteine protease that plays a key role in cytoplasm to vacuole transport (Cvt) and autophagy by mediating both proteolytic activation and delipidation of ATG8 (PubMed:11038174, PubMed:11100732, PubMed:11149920, PubMed:11904149, PubMed:16680092, PubMed:18701704, PubMed:18725539, PubMed:8050581, PubMed:8224160, PubMed:9649430, PubMed:28330855, PubMed:28821724, PubMed:28704456). Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (PubMed:11038174, PubMed:11100732, PubMed:11149920, PubMed:11904149, PubMed:16680092, PubMed:18701704, PubMed:18725539, PubMed:8050581, PubMed:8224160, PubMed:9649430). The protease activity is required for proteolytic activation of ATG8: cleaves the C-terminal amino acid of ATG8 to reveal a C-terminal glycine (PubMed:11038174, PubMed:11100732, PubMed:11149920, PubMed:11904149, PubMed:16680092, PubMed:18701704, PubMed:18725539, PubMed:8050581, PubMed:8224160, PubMed:9649430). ATG8 ubiquitin-like activity requires the exposure of the glycine at the C-terminus for its conjugation to phosphatidylethanolamine (PE) and its insertion to membranes, which is necessary for autophagy (PubMed:11038174, PubMed:11100732, PubMed:11149920, PubMed:11904149, PubMed:16680092, PubMed:18701704, PubMed:18725539, PubMed:8050581, PubMed:8224160, PubMed:9649430). The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (PubMed:17632063). In addition to the protease activity, also catalyzes deconjugation of PE-conjugated forms of ATG8 during macroautophagy: ATG8 delipidation is required to release the protein from membranes, which facilitates multiple events during macroautophagy, and especially for efficient autophagosome biogenesis, the assembly of ATG9-containing tubulovesicular clusters into phagophores/autophagosomes, and for the disassembly of PAS-associated ATG components (PubMed:22240591, PubMed:22652539, PubMed:28330855, PubMed:28821724, PubMed:28704456). ATG8 delipidation by ATG4 also recycles ATG8-PE generated on inappropriate membranes to maintain a reservoir of unlipidated ATG8 that is required for autophagosome formation at the PAS (PubMed:22240591, PubMed:22652539).
Expression is induced upon starvation, through the action of transcription factors GCN2 and GCN4.
Formation of a disulfide bond between Cys-338 and Cys-394 leads to reduced autophagy (PubMed:25483965). The disulfide bond is reduced by thioredoxin (PubMed:25483965).
Interacts with ATG8 (PubMed:16680092, PubMed:9649430, PubMed:28287329, PubMed:28330855, PubMed:28821724). Interacts with TUB1 and TUB2 (PubMed:9649430).
Phosphorylation at Ser-307 by ATG1 inhibits autophagy: it takes place on autophagosome membranes and decreases its interaction with ATG8, thereby impairing deconjugation of PE-conjugated forms of ATG8.
Present with 3300 molecules/cell in log phase SD medium.
The APEAR motif (ATG8-PE association region) plays a key role in ATG4 recruitment to autophagosomal membranes and ATG8 deconjugation (PubMed:28330855). The LIR (LC3-interacting region act cooperatively) and APEAR motifs for the interaction with ATG8 (PubMed:28287329, PubMed:28330855).
Belongs to the ABC transporter superfamily. ABCE family.
Component of the multifactor complex (MFC) composed of at least RLI1, the eIF2 subunit SUI2, TIF5/eIF5, and the eIF3 subunits PRT1, HCR1, NIP1, RPG1, TIF34 and TIF35. The complex associates with pre-initiation complexes. Interacts with the complex YAE1:LTO1; the complex bridges the interaction between the CIA complex and RLI1 (PubMed:23318452).
Component of the multifactor complex (MFC) involved in translation initiation. Required for the binding of MFC to the 40S ribosome. Required for the processing and nuclear export of the 60S and 40S ribosomal subunits.
Present with 6280 molecules/cell in log phase SD medium.
By the genotoxic agents methyl methanesulfonate (MMS), bleomycin and cisplatin.
Interacts with KRE6, LSB3, LSB5 and YSC84.
Present with 8580 molecules/cell in log phase SD medium.
In response to nutrient limitation. Repressed by high glucose concentrations.
May be involved in cellular adaptations prior to stationary phase.
To yeast sporulation-specific protein SPS100.
Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of at least PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. Component of the APT complex, which is a subcomplex of CPF, and is composed of PTI1, SYC1, SSU72, GLC7, REF2, PTA1 and SWD2.
Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation, including snoRNAs and snRNAs.
Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA).
Acts as a component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromers and in several promoters.
Component of the CBF3 copmplex, which is formed of CBF3A/CBF2, CBF3B/CEP3, CBF3C/CTF13 and CBF3D.
Cell wall protein that participates directly in adhesive cell-cell interactions during yeast flocculation, a reversible, asexual and Ca(2+)-dependent process in which cells adhere to form aggregates (flocs) consisting of thousands of cells. The lectin-like protein sticks out of the cell wall of flocculent cells and selectively binds mannose residues in the cell walls of adjacent cells. Activity is inhibited by mannose, glucose, maltose and sucrose. Also involved in cell-substrate adhesion, haploid invasive growth and diploid pseudohyphae formation.
Belongs to the eukaryotic ribosomal protein eS8 family.
Present with 3480 molecules/cell in log phase SD medium.
Accumulates in large amounts when cell wall integrity is compromised.
Serine/threonine-protein kinase involved in the SLT2 mitogen-activated (MAP) kinase signaling pathway that regulates cell wall integrity. May also be involved in the mating pheromone and the CWI MAPK pathways.
Belongs to the tRNA-intron endonuclease family.
Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. It probably carries the active site for 3'-splice site cleavage.
Heterotetramer composed of SEN2, SEN15, SEN34 and SEN54. Interacts directly with SEN15.
The tRNA splicing endonuclease complex is present with 100 molecules/cell.
Phosphorylates both NADH and NAD(+), with a twofold preference for NADH. Anti-oxidant factor and key source of the cellular reductant NADPH.
Present with 4650 molecules/cell in log phase SD medium.
Component of the M-Pol I complex which contains MNN9 and VAN1.
Involved in regulation of the phosphorylation of a number of proteins, some of which appear to be important in cell growth control.
Present with 4750 molecules/cell in log phase SD medium.
The M-Pol I complex possesses alpha-1,6-mannosyltransferase activity and is probably involved in the elongation of the mannan backbone of N-linked glycans on cell wall and periplasmic proteins.
Component of the COMPASS (Set1C) complex which consists of SET1(2), BRE2(2), SPP1(2), SDC1(1), SHG1(1), SWD1(1), SWD2(1), and SWD3(1).
The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently activates gene expression by regulating transcription elongation and plays a role in telomere length maintenance.
Could act as an H1-type linker histone. Has been shown to bind DNA.
Present with 6560 molecules/cell in log phase SD medium.
Required for the processing and/or for the stability of the CYTB and COX1 intron-containing pre-mRNAs and of the ATP6 transcript. Could be a stem-loop RNA-binding protein that plays a role in determining RNA stability.
Component of the phosphatidylinositol N-acetylglucosaminyltransferase (GPI-GlcNAc transferase) complex composed of at least GPI1, GPI2, GPI3, GPI15, GPI19 and ERI1.
Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.
Belongs to the adaptor complexes medium subunit family.
Component of the AP-1-related (AP-1R) complex, an adapter protein complex that mediates of cargo protein sorting in clathrin-coated vesicles (PubMed:26658609). AP-1R has a specific role in SNARE SNC1 sorting (PubMed:26658609). In contrast to the APM1-containing AP-1 complex, AP-1R is incapable of sorting CHS3 (PubMed:26658609).
Component of the AP-1R complex composed of at least APM2, APL4 and APS1 (PubMed:26658609). Interacts with MIL1 (PubMed:26658609). Interacts with APL2 (PubMed:10564262).
Leads to sensitivity to cationic amphiphilic drugs (CADs) such as sertraline.
Heterodimer with HOP2. MND1-HOP2 binds preferentially to dsDNA.
Required for proper homologous chromosome pairing and efficient cross-over and intragenic recombination during meiosis. Stimulates DMC1-dependent homologous strand assimilation, which is required for the resolution of meiotic double-strand breaks.
Activated by VAC14 and VAC7. VAC14 acts as a specific osmotic response regulator.
Component of the PI(3,5)P2 regulatory complex, composed of ATG18, FIG4, FAB1, VAC14 and VAC7. VAC14 nucleates the assembly of the complex and serves as a scaffold.
The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate (PubMed:16492811, PubMed:9811604). Required for endocytic-vacuolar pathway and nuclear migration (PubMed:9751732, PubMed:16492811, PubMed:9811604). The product of the reaction, PI(3,5)P2 is an important regulator of vacuole homeostasis perhaps by controlling membrane flux to and/or from the vacuole (PubMed:9811604, PubMed:9763421). PI(3,5)P2 regulates the transition between trans-SNARE complex formation and vacuole membrane fusion (PubMed:30427760). Hyperosmotic shock-induced increase in the levels of PtdIns(3,5)P2 requires the presence of VAC7, VAC14, and/or FIG4 (PubMed:16492811).
The chaperone-containing TCP1 (CCT) domain is essential for the interaction with the scaffold protein VAC14.
The conserved cysteine-rich (CCR) domain contacts intramolecularly the C-terminus, including the kinase domain, and this interaction negatively regulates PI(3) 5-kinase activity.
Interacts with itself. Interacts with KTR3, MNN2 and MNN5.
Plays a role in retention of a subset of membrane proteins in the early Golgi compartments. Facilitates endoplasmic reticulum to Golgi transport of mannosyltransferases MNN2 and MNN5.
Present with 1810 molecules/cell in log phase SD medium.
Component of the phosphatidylinositol N-acetylglucosaminyltransferase (GPI-GlcNAc transferase) complex composed of at least GPI1, GPI2, GPI3, GPI15, GPI19 and ERI1 (Probable). Interacts with GPI2 (PubMed:16278447).
Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis. Involved in cell wall biosynthesis.
Belongs to the glutaredoxin family. Monothiol subfamily.
Belongs to the aldehyde dehydrogenase family.
Cytoplasmic aldehyde dehydrogenase involved in ethanol oxidation. Required for pantothenic acid production through the conversion of 3-aminopropanal to beta-alanine, an intermediate in pantothenic acid (vitamin B5) and coenzyme A (CoA) biosynthesis.
Expression is under the control of MSN2 and MSN4, and is induced during diauxic shift and osmotic stress.
Associates with the nucleopore complex. Interacts with LHP1, PAB1, RPL11, RPL16, RPL25, RPL31A in order to import them into the nucleus. Interacts also with the nucleopore complex proteins (nucleoporins) NSP1, NUP1, NUP116 and NUP159.
Nuclear transport factor (karyopherin) involved in protein transport between the cytoplasm and nucleoplasm. Required for the nuclear import of ribosomal proteins (RPL11, RPL16, RPL25, RPL31A), the poly(A)-binding protein PAB1, the HO endonuclease or the tRNA and snRNA chaperone LHP1. Indirectly involved in nuclear mRNA export through its PAB1 nuclear import activity.
Present with 16300 molecules/cell in log phase SD medium.
Putative chaperone involved in protein folding. Interferes with propagation of [PSI+] prion when overproduced.
Present with 39900 molecules/cell in log phase SD medium.
Acetylated by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex, to form H2AK4ac and H2AK7ac.
Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Glutamine methylation at Gln-106 (H2AQ105me) by NOP1 is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex (PubMed:24352239).
In contrast to vertebrates and insects, its C-terminus is not monoubiquitinated.
Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases MEC1/ATR and TEL1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A interacts with ARP4, a shared component of the NuA4 histone acetyltransferase complex and the INO80 and SWR1 chromatin remodeling complexes, and serves to recruit first NuA4, mediating histone H4 acetylation, and subsequently the INO80/SWR1 complexes, facilitating DNA resection, to DSB sites. Gamma-H2A is required for sequestering cohesin around the break site, which is important for efficient post-replicative double-strand break repair by homologous recombination, holding the damaged chromatid close to its undamaged sister template. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated by PPH3, a component of the histone H2A phosphatase complex (HTP-C). Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint.
Present with 32100 molecules/cell in log phase SD medium.
Sumoylated to from H2AK126su. May lead to transcriptional repression.
The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Interacts with NAP1.
To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H2AK4ac = acetylated Lys-5; H2AK7ac = acetylated Lys-8; H2AK126su = sumoylated Lys-127; H2AS128ph = phosphorylated Ser-129.
Belongs to the ERCC1/RAD10/SWI10 family.
Component of the nucleotide excision repair factor 1 (NEF1) complex consisting of RAD1, RAD10 and RAD14. Interacts with SAW1.
Involved in nucleotide excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Along with RAD1 forms an endonuclease that specifically degrades single-stranded DNA.
Interacts with SKP1. Component of the probable SCF(UFO1) complex containing CDC53, SKP1, RBX1 and UFO1.
Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates.
Belongs to the low molecular weight phosphotyrosine protein phosphatase family.
Present with 3500 molecules/cell in log phase SD medium.
Belongs to the eukaryotic ribosomal protein eL14 family.
Present with 35100 molecules/cell in log phase SD medium.
Essential light chain for the class II conventional myosin MYO1. Acts also as light chain for the class V unconventional myosin MYO2 and for IQG1. Involved in the assembly of the contractile actomyosin ring at the bud neck during cytokinesis by recruiting IQG1 to the bud neck. Also required for chitin and MYO2-dependent secretory vesicle deposition to the center of the bud neck for septum formation. May stabilize MYO2 by binding to its IQ domains. Its major function is probably not to regulate MYO1 activity, but rather to coordinate actin ring formation and targeted membrane deposition during cytokinesis via its interactions with MYO1, IQG1 and MYO2.
Interacts with MYO1, MYO2 and IQG1 by binding to their IQ domains. Interacts with SEC4.
Its expression is meiotically induced and required the IME1 protein.
MER1 is synthesized only during meiosis.
Required for chromosome pairing and genetic recombination. MER1 may function to bring the axial elements of the synaptonemal complex corresponding to homologous chromosomes together by initiating recombination. MER1 might be responsible for regulating the MER2 gene and/or gene product.
Interacts with PMT4 and WW domain of RSP5.
Regulates chitin deposition in the cell wall.
The PY motif is recognized directly by the WW domains of RSP5.
Transmembrane domain is required, and the cytoplasmic region conserved between RCR1 and RCR2 is also essential, to endow resistance to Congo red.
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
By anaerobic growth conditions and other conditions leading to accumulation of cytosolic NADH.
Catalyzes the production of glycerol under anaerobic growth conditions. Glycerol production serves as a redox sink by consuming the excess cytosolic NADH during anaerobic metabolism.
It is uncertain whether Met-1 or Met-49 is the initiator.
Leads to poor growth under anaerobic conditions (PubMed:9171333). Does not produce detectable glycerol, is highly osmosensitive and fails to grow under anoxic conditions, when GPD1 is also deleted (PubMed:9171333).
Present with 8966 molecules/cell in log phase SD medium.
Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate.
Belongs to the AAA ATPase family. BCS1 subfamily.
Essential for the expression of the Rieske iron-sulfur protein.
Present with 1990 molecules/cell in log phase SD medium.
Covalently linked to beta-1,3-glucan of the inner cell wall layer via an alkali-sensitive ester linkage between the gamma-carboxyl group of glutamic acids, arising from a specific glutamine within the PIR1/2/3 repeat, and hydroxyl groups of glucoses of beta-1,3-glucan chains.
Induced during anaerobic growth and by cold shock and glucose.
The number of the intragenic tandem repeats varies between different S.cerevisiae strains.
Involved in transcriptional activation. Component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Central component of the TOM (translocase of outer membrane) receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore.
Forms part of the preprotein translocase complex of the outer mitochondrial membrane (TOM complex) which consists of at least 7 different proteins (TOM5, TOM6, TOM7, TOM20, TOM22, TOM40 and TOM70). In the complex, interacts with TOM22.
Present with 5680 molecules/cell in log phase SD medium.
Expression is repressed by anoxia. Expression is decreased during transition to slow growing or stationary phases.
Involved in the remodeling of the cell wall during the various phases of yeast culture development and under various environmental conditions. Required for the maintenance of the CLB5 kinase activity.
Leads to increased resistance to zymolyase treatment.
Activated by tyrosine and threonine phosphorylation after pheromone treatment.
Dually phosphorylated on Thr-180 and Tyr-182 by STE7 in response to pheromone induction, which activates the enzyme. Activated FUS3 initiates a feedback signal, down-regulating phosphorylation of both, FUS3 and KSS1.
In the nucleus, FUS3 forms a complex with DIG1, DIG2 and STE12. The interaction of FUS3 with STE12 depends on the presence of both DIG1 and DIG2. STE12 is lost from FUS3/DIG1/DIG2 complex after pheromone treatment. During its activation and phosphorylation, FUS3 forms a membrane-associated complex with the scaffold protein STE5, the MAPKK STE7, the MAPKKK STE11, and the G-protein beta subunit GBB/STE4; interacting directly with STE7 and STE5.
Present with 8480 molecules/cell in log phase SD medium.
Together with closely related KSS1, FUS3 is the final kinase in the signal transduction cascade regulating activation/repression of the mating and filamentation pathways, induced by pheromone and nitrogen/carbon limitation, respectively. Phosphorylated FUS3 activates the mating but suppresses the filamentation pathway, whereas activated KSS1 activates both pathways. Pheromone-activated FUS3 functions by inhibiting the binding of the transcriptional activator STE12 to filamentation specific genes while inducing its binding to and activity at mating specific genes. Non-activated FUS3 has a repressive effect on STE12 transcriptional activity. KSS1 can partially compensate for the lack of FUS3 but mating efficiency is reduced and the filamentation program is partially activated upon pheromone signaling. FUS3 phosphorylates STE7, STE5, FAR1, DIG1, DIG2 and STE12.
Could be the product of a pseudogene unlikely to encode a functional protein. Although strongly related to DNA helicases, it lacks the helicase ATP-binding domains, suggesting that it has no helicase activity. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set.
Could be the product of a pseudogene. Although strongly related to DNA helicases, it lacks the helicase ATP-binding domains, suggesting that it has no helicase activity.
Putative serine/threonine-protein kinase that may be involved in rRNA transcription and ribosome biogenesis.
Belongs to the ATPase gamma chain family.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Present with 28100 molecules/cell in log phase SD medium.
PubMed:12898710 reports two tandemly repeated copies of ATP3 (ATP3a and ATP3b) on the right arm of chromosome II in several laboratory strains, including S288c. This has not been confirmed by the yeast genome sequencing project.
Belongs to the SRP receptor beta subunit family.
Component of the signal recognition particle (SRP) complex receptor (SR) (By similarity). Ensures, in conjunction with the SRP complex, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (By similarity). May mediate the membrane association of SR (By similarity).
Heterodimer of an alpha and a beta chain.
Present with 8250 molecules/cell in log phase SD medium.
May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi.
The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins.
Lysophosphatidic acid acyltransferase involved in membrane remodeling leading to increased organic solvent tolerance. Involved in resistance to azoles and copper.
The isooctane tolerance of organic-solvent tolerant strain KK-21 may result from the alteration of the expression of several genes including ICT1, due to the loss of their proper regulation.
Present with 2130 molecules/cell in log phase SD medium.
This protein is involved in processing of the 5' terminus and the intervening sequences of cytochrome b pre-mRNA.
Belongs to the ABC transporter superfamily. ABCD family. Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily.
Involved in the import of activated long-chain fatty acids from the cytosol to the peroxisomal matrix.
The GAL3 gene is a member of the family of galactose inducible, glucose-repressible genes (which include GAL1, GAL2, GAL7, GAL10, GAL80, and MELI).
The GAL3 regulatory function is required for rapid induction of the galactose system. At normal induction, galactose in the presence of the GAL3 protein may lead to the induction of the GAL genes, including GAL1. Then the galactokinase protein (GAL1) in the presence of galactose may reinforce the induction leading to a higher expression level. Upon depletion of galactose, the inducing activity of the galactokinase protein may decrease, after which transcription of the GAL genes, including GAL1, may decrease.
Component of a SNARE complex consisting of SED5, BOS1, BET1 and SEC22 or YKT6. Interacts with YIF1 and YIP1.
SNARE required for targeting and fusion of ER-derived transport vesicles with the Golgi complex.
Essential component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for the maturation of extramitochondrial Fe/S proteins.
Present with 5640 molecules/cell in log phase SD medium.
Proteolytically removes the C-terminal three residues of farnesylated proteins, including the a-factor mating pheromone and RAS.
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) composed of at least BLI1, BLS1, CNL1, KXD1, SNN1 and VAB2.
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in endosomal cargo sorting.
Belongs to the lipid-translocating exporter (LTE) (TC 9.A.26.1) family.
Involved in inducible protoporphyrin IX influx and heme efflux.
Interacts with MAK21/NOC1 and NOC3. Forms a nucleolar complex with MAK21 that binds to 90S and 66S pre-ribosomes, as well as a nuclear complex with NOC3 that binds to 66S pre-ribosomes.
Involved in the intranuclear transport of ribosomal precursors.
Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin to form chitosan and acetate (PubMed:9133736). Chitosan is a component of the spore wall (PubMed:9133736).
Belongs to the eIF-2B alpha/beta/delta subunits family. MtnA subfamily.
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
COPII is composed of at least five proteins: the SEC23/24 complex, the SEC13/31 complex and SAR1. Binds to SED5. Interacts with GHR1.
Although reported constituent of the mitochondrial small ribosomal subunit (PubMed:11278769), it has not been identified in the structure of the yeast mitoribosome (PubMed:28154081), indicating that RSM22 only transiently interacts with the mitoribosome.
Associates with mitochondrial ribosomes.
Belongs to the methyltransferase superfamily. Rsm22 family.
Probable S-adenosyl-L-methionine-dependent RNA methyltransferase (PubMed:19351663, PubMed:24651469). May provide the activity for methylation of the rRNA of the small mitochondrial subunit, which is required for the assembly and stability of the mitochondrial ribosome (PubMed:22689777). Has no protein methyltransferase activity (PubMed:24651469).
Functions as an activator subunit for the DBF2 protein kinase. Binds to DBF2, which is required for the phosphorylation and activation of DBF2 by the upstream kinase CDC15 in late anaphase. DBF2-MOB1 is part of the mitotic exit network (MEN) signaling cascade, which regulates release from the nucleus and activity of phosphatase CDC14. Required for inactivation of mitotic cyclin-dependent kinase for exit from mitosis, cytokinesis and G1 gene transcription.
Interacts with protein kinase DBF2 to form the MEN DBF2-MOB1 kinase complex.
Present with 5020 molecules/cell in log phase SD medium.
Belongs to the universal ribosomal protein uL29 family.
Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). uL29 is associated with the polypeptide exit tunnel (PubMed:9559554, PubMed:22096102).
Present with 19100 molecules/cell in log phase SD medium.
Belongs to the activator 1 small subunits family.
Component of ATP-dependent clamp loader (RFC and RFC-like) complexes for DNA clamps, such as the POL30/PCNA homotrimer and the checkpoint clamp DDC1:MEC3:RAD17 complex. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA. Component of the replication factor C (RFC or activator 1) complex which loads POL30/PCNA and acts during elongation of primed DNA templates by DNA polymerase delta and epsilon. RFC has an essential but redundant activity in sister chromatid cohesion establishment. Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. Component of the RFC-like RAD24-RFC complex which loads the checkpoint clamp DDC1:MEC3:RAD17 complex and is involved in DNA repair pathways. Component of the RFC-like ELG1-RFC complex which appears to have a role in DNA replication, replication fork re-start, recombination and repair. RFC2 binds ATP and single-stranded DNA.
Present with 4610 molecules/cell in log phase SD medium.
Replication factor C (RFC) is a heteropentamer of subunits RFC1, RFC2, RFC3, RFC4 and RFC5 and forms a complex with POL30/PCNA in the presence of ATP. Component of the RAD24-RFC complex which consists of RAD14, RFC2, RFC3, RFC4 and RFC5 and associates with the checkpoint clamp DDC1:MEC3:RAD17 complex. Component of the ELG1-RFC complex which consists of ELG1, RFC2, RFC3, RFC4 and RFC5. Component of the CTF18-RFC complex, which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. RFC2 interacts with ECO1.
Belongs to the universal ribosomal protein uS11 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). uS11 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835).
Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). uS11 interacts with eS1 forming part of the mRNA exit tunnel (PubMed:9559554, PubMed:22096102). uS11 interacts with snoRNA U3. uS11 interacts with MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3 (PubMed:15590835).
Present with 3370 molecules/cell in log phase SD medium.
With EMP70 and TMN2, plays a critical role in the late stages of a nutrient-controlled pathway notably regulating FLO11 gene expression. Acts downstream of RAS2 and TOR. Essential for cell adhesion and filamentous growth. May play a role as effector of cellular copper homeostasis.
Nucleocapsid protein p9 (NC) forms the nucleocore that coats the retro-elements dimeric RNA. Binds these RNAs through its zinc fingers (By similarity). Promotes primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty3 RNA and initiation of reverse transcription.
The N-terminal domain of NC, but not its zinc finger, is required for nucleoprotein complex formation and its chaperone activities.
Expressed in aerobic conditions and under genotoxic stress (PubMed:10601195, PubMed:15878181). Expression is increased during respiratory growth and regulated by the heme activator protein transcriptional activation complex (PubMed:24318983).
Mitochondrial cardiolipin-specific phospholipase which deacylates de novo synthesized cardiolipin (CL). Part of the remodeling process of cardiolipin, which involves deacylation-reacylation of premature cardiolipin. Has a strong substrate preference for palmitic acid residues and generates monolysocardiolipin (MLCL) for TAZ1-dependent reacylation with unsaturated fatty acids (PubMed:19244244, PubMed:23637464). The hydrolytic selectivity of the enzyme toward C16-CL substrates contributes to the preservation of C18:1-containing CL species (PubMed:27982579). Has high specificity towards peroxidized cardiolipids CL(OX). Required to mitigate oxidative stress by removing CL(OX) (PubMed:29935382).
Important for the export of protein containing nuclear export signal (NES) out of the nucleus. Stimulates the GTPase activity of GSP1.
Present with 3620 molecules/cell in log phase SD medium.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.
Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups. Required for the modification of both mitochondrial and cytoplasmic tRNAs.
Isoform 2 is N-acetylated by NatC at position 1. N-acetylation is necessary for targeting of the protein to the inner nuclear membrane.
Component of a peripheral membrane protein complex consisting of DSL1, SEC39/DSL3 and TIP20. Bound to a SNARE complex consisting of UFE1, USE1, SEC20 and SEC22 or YKT6 through direct interaction of TIP20 with SEC20. Interacts with DSL1, SEC39/DSL3 and the cytoplasmic domain of SEC20.
Present with 6020 molecules/cell in log phase SD medium.
Required for protein transport between the Golgi and the endoplasmic reticulum. May contribute to tethering of coatomer-coated retrograde transport vesicles to the ER membrane through interaction with and stabilization of the SNARE complex.
Belongs to the ATPase alpha/beta chains family.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).
Interacts with snoRNA U3. Interacts with MPP10. Interacts (via WD repeats) with UTP18. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.
Present with 2020 molecules/cell in log phase SD medium.
The WD repeats are grouped into two tandem seven-bladed beta-propeller regions.
Present with 5860 molecules/cell in log phase SD medium.
Transcription elongation factor implicated in the maintenance of proper chromatin structure in actively transcribed regions.
By ethanol or acetate as sole carbon sources. Repressed by glucose.
Transports cytoplasmic succinate, derived from isocitrate by the action of isocitrate lyase in the cytosol, into the mitochondrial matrix in exchange for fumarate.
Belongs to the thiamine pyrophosphokinase family.
Essential protein, it is the only enzyme in yeast capable of synthesizing thiamine pyrophosphate (TPP).
Expression requires the positive regulatory factors THI2 and THI3 (PubMed:8394343). Incompletely repressed by exogenous thiamine pyrophosphokinase (PubMed:8394343).
Component of the Sm core complex, present in spliceosomal snRNP U1, U2, U4/U6 and U5. The core complex contains SMB1, SMD1, SMD2, SMD3, SME1, SMX3 and SMX2 (Sm proteins B, D1, D2, D3, E, F and G, respectively), and is probably a heptameric ring structure. SME1 specifically interacts with SMX2 and SMX3. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
Involved in pre-mRNA splicing. Binds and is required for the stability of snRNA U1, U2, U4 and U5 which contain a highly conserved structural motif called the Sm binding site. Involved in cap modification.
Accessory component of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:29526695). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:29526695).
Component of RNase MRP complex which consists of an RNA moiety and at least 10 protein subunits including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RMP1, RPP1 and SNM1, many of which are shared with the RNase P complex.
Essential component of the MRP ribonucleoprotein endoribonuclease that cleaves mitochondrial primer RNA sequences.
Associates with RNA polymerase II. Part of a complex consisting of RPB1, RBP2, RPB3, RPB4, RPB5, RPB7, SPT5, DST1 and IWR1.
Directs RNA polymerase II nuclear import. Binds RNA polymerase II in the active center cleft between the two largest subunits in the cytoplasm. Then uses an N-terminal bipartite nuclear localization signal that may be recognized by karyopherin alpha to direct the polymerase II complex nuclear import. In the nucleus, is displaced from polymerase II complex by transcription initiation factors and nucleic acids, enabling its export and recycling.
Due to the effects of deletion on gene expression, was originally thought to be a general transcription factor (PubMed:19679657). Further studies clearly suggest that it is involved in nuclear localization of the RNA polymerase II complex (PubMed:21504834).
Leads to a K1 killer toxin hypersensitivity and pleiotropic effects on gene expression.
Present with 1080 molecules/cell in log phase SD medium.
Involved in translation initiation. May be the homolog of mammalian eIF4B and be part of an RNA helicase. STM1/TIF3 is a non-essential gene.
Present with 24000 molecules/cell in log phase SD medium.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). eL40 is essential for translation of a subset of cellular transcripts, including stress response transcripts, such as DDR2 (PubMed:23169626).
Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
In the C-terminal section; belongs to the eukaryotic ribosomal protein eL40 family.
In the N-terminal section; belongs to the ubiquitin family.
The 60S ribosomal protein L40 is present with 40000 molecules/cell in log phase SD medium.
Ubiquitin is encoded by several different genes. UBI1 and UBI2 genes code for a single copy of ubiquitin fused to the ribosomal proteins eL40. UBI3 is a polyprotein with one copy of ubiquitin fused to ribosomal protein eS31. UBI4 is a polyprotein containing 5 exact head to tail repeats of ubiquitin.
Component of the central kinetochore, which mediates the attachment of the centromere to the mitotic spindle by forming essential interactions between the microtubule-associated outer kinetochore proteins and the centromere-associated inner kinetochore proteins. Required for establishing bipolar spindle-microtubule attachments and proper chromosome segregation.
Component of the heterotrimeric kinetochore subcomplex CTF3, which consists of CTF3, MCM16 and MCM22 (PubMed:11782448). The CTF3 subcomplex is part of a larger constitutive centromere-associated network (CCAN) (also known as central kinetochore CTF19 complex in yeast), which is composed of at least AME1, CHL4, CNN1, CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1 (PubMed:12408861, PubMed:22561346). Interacts with CTF19 (PubMed:11782448, PubMed:12589047). Interacts with CHL4 (PubMed:12589047).
Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family.
Mitochondrial 3-hydroxyacyl-thioester dehydratase involved in fatty acid biosynthesis. Required for respiratory growth and for normal mitochondrial morphology.
Present with 799 molecules/cell in log phase SD medium.
Component of the ISW2 complex, which at least consists of ISW2, ITC1, DLS1 and DPB4. May form a stable subcomplex with ISW2.
Functions as component of the ISW2 complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW2 complex is involved in coordinating transcriptional repression and in inheritance of telomeric silencing. It is involved in repression of MAT a-specific genes, INO1, and early meiotic genes during mitotic growth dependent upon transcription factor UME6 and in a parallel pathway to the RPD3-SIN3 histone deacetylase complex. ITC1 is required for nucleosome-stimulated ATPase activity and chromatin-remodeling activity of the complex. Required for the repression of MATa a-specific genes.
Belongs to the apolipoprotein O/MICOS complex subunit Mic27 family.
Component of the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MIC10, MIC12, MIC19, MIC26, MIC27 and MIC60. This complex was also known under the names MINOS or MitOS complex.
Increases frequency of mitochondrial genome loss. Partially altered shape of the mitochondrial network with condensed, fragmented mitochondria accumulating at the periphery of cells. 20-40% of mitochondria exhibit an increased inner membrane surface and stacks of lamellar cristae disconnected from the inner boundary membrane.
Acts as an accessory factor in the activation of sulfur amino acids metabolism genes. Possesses no intrinsic transcription activation abilities. Binds to the MET16 promoter as a complex with MET4 and CBF1. Enhances the DNA-binding activity of CBF1.
Expression requires MET4, and is repressed by an increase of intracellular S-adenosylmethionine (AdoMet).
Interacts with MET4 to form a heteromeric complex which also includes CBF1. Forms two alternate complexes associating MET28 with MET4 and either MET31 or MET32. Binds to DNA through the MET4-MET28-CBF1 complex.
Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.
Required for cell size and shape control, bud site selection, bud emergence, actin cytoskeletal organization, mitotic spindle orientation/positioning, and mating projection formation in response to mating pheromone.
Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. In association with PAT1, LSM1-LSM7 binds directly to RNAs near the 3'-end and prefers oligoadenylated RNAs over polyadenylated RNAs. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 di-snRNP, spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. Component of a nucleolar LSM2-LSM7 complex, which associates with the precursor of the RNA component of RNase P (pre-P RNA) and with the small nucleolar RNA (snoRNA) snR5. It may play a role in the maturation of a subset of nucleolus-associated small RNAs.
Component of the heptameric LSM1-LSM7 complex that forms a seven-membered ring structure with a doughnut shape. The LSm subunits are arranged in the order LSM1, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. Except for LSM1, where a C-terminal helix crosses the ring structure to form additional interactions with LSM3 and LSM6, each subunit interacts only with its two neighboring subunits. The LSM1-LSM7 complex interacts with PAT1; within the complex PAT1 has direct interactions with LSM2 and LSM3. LSM1-LSM7 associates also with PAT1 and XRN1. Component of the heptameric LSM2-LSM8 complex that forms a seven-membered ring structure with a doughnut shape; an RNA strand can pass through the hole in the center of the ring structure. The LSm subunits are arranged in the order LSM8, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. LSM2-LSM8 associates with PAT1 and XRN1. Component of a LSM2-LSM7 complex, which consists of at least LSM2, LSM3, LSM4, LSM5, LSM6 and LSM7. It is not known whether another protein replaces the missing LSm to form a novel heptameric complex. Component of the spliceosome U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
Binds to the promoters of genes with functions important for the G1/S (start) transition; primarily genes involved in pheromone response, polarized growth and transcription.
Present with 284 molecules/cell in log phase SD medium.
Regulated in a cell cycle-dependent manner, peaking in G1 phase. Appears exclusively during the G1 and S phases (at protein level). Negatively regulated by transcription factor SBF (SWI4-SWI6 cell-cycle box binding factor).
Present with 3040 molecules/cell in log phase SD medium.
Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium (PubMed:12686616). Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:12686616). Accelerates proteasomal breakdown of ubiquitinated proteins as it disassembles free ubiquitin chains that would compete with ubiquitinated proteins to bind to the proteasome (PubMed:9305625).
Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.
Essential for protein sorting in meiotic cell division of S.cerevisiae; it binds microtubules. Could also be involved in microtubule-associated motility. Necessary for membrane protein retention in a late Golgi compartment. Interacts with the MVP1 protein.
Present with 5960 molecules/cell in log phase SD medium.
Homooligomer. Participates in a complex of about 300 kDa.
Required for the maintenance of the structure of the mitochondrial inner membrane. Involved in mitochondrial morphology. Causes growth arrest when highly overexpressed.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YNL284C-A ORF.
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids (Potential). Leads to neomycin-resistance when overexpressed. Required for traffic between late Golgi and early endosomes.
Involved in the regulation of the onset of mitosis. Involved in a pathway that coordinates cell proliferation and differentiation. Implicated in spindle pole body (SPD) duplication. Dual specificity kinase that can phosphorylate serine, threonine and tyrosine residues. Phosphorylates the SPC29 and SPC110 spindle pole body components.
Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase family.
Regulates the phosphatidylinositol (4,5)-diphosphate levels on the cytoplasmic surface of the endoplasmic reticulum and thereby regulates secretion. Does not utilize phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), nor phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P).
Component of the CBF3 copmplex, which is formed of CBF3A/CBF2, CBF3B/CEP3, CBF3C/CTF13 and CBF3D. CBF2 strongly interacts with BIR1. Interacts with the central kinetochore protein CTF19.
Present with 1710 molecules/cell in log phase SD medium.
Transcriptional regulator of pseudohyphal growth.
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Present with 96300 molecules/cell in log phase SD medium.
10-fold decrease in D-tyrosyl-tRNA(Tyr) deacylase activity, growth becomes more sensitive to D-tyrosine and is inhibited at 0.1 mM D-Tyr (PubMed:10766779, PubMed:10918062). Growth is also inhibited in the presence of 0.3 mM D-leucine; wild-type cells grow well in up to 0.3 mM D-Tyr and 10 mM D-Leu (PubMed:10918062). No growth differences observed in the presence of the other D-amino acids (PubMed:10918062).
A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs (Probable). Hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr) (PubMed:10766779). May also deacylate mischarged D-leucyl-tRNA(Leu) (PubMed:10918062). Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS (By similarity). Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site (By similarity). By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality (By similarity).
Present with 291000 molecules/cell in log phase SD medium.
The activity is regulated by glucose levels. Activated by fructose-1,6-bisphosphate.
Belongs to the PI3/PI4-kinase family. ATM subfamily.
Interacts with LCD1, which is required for localization MEC1 to the RPA complex. Interacts directly with the RPA subunits RFA1 and RFA2.
Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Recruited in complex with protein LCD1 by the single-strand-binding protein complex RPA to DNA lesions in order to initiate the DNA repair by homologous recombination, after the MRX-complex and TEL1 are displaced. Phosphorylates LCD1 and RPA2, a subunit of RPA, involved in DNA replication, repair and recombination. Phosphorylates RAD9, CHK1 and RAD53, which leads to the activation of the CHK1 and RAD53 kinases involved in DNA damage repair cascade. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of DNA damage, also involved in the regulation of DNA damage response mechanism. Phosphorylates also SLX4 and RTT107 which are proteins involved in genome stability. Required for cell growth and meiotic recombination.
Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.
Present with 3140 molecules/cell in log phase SD medium.
Required for N-linked oligosaccharide assembly. Has a role in the last step of the synthesis of the Man(5)GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum.
The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.
FUS1 remains essentially unexpressed in vegetative cells, but is strongly induced by incubation of haploid cells with the appropriate mating pheromone.
Required for cell fusion. Negatively regulates Sho1p signaling to ensure efficient cell fusion.
Component of the elongator complex which consists of ELP1/IKI3, ELP2, ELP3, ELP4, ELP5/IKI1 and ELP6 (PubMed:11435442, PubMed:11390369, PubMed:11689709, PubMed:27974378, PubMed:27872205). The elongator complex is composed of two copies of the Elp123 subcomplex (composed of ELP1/IKI3, ELP2 and ELP3) and two copies of the Elp456 subcomplex (composed of ELP4, ELP5/IKI1 and ELP6) (PubMed:27974378, PubMed:27872205). The Elp123 subcomplex forms a two-lobed scaffold, which binds the Elp456 subcomplex asymmetrically (PubMed:27974378, PubMed:27872205). In each lobe, ELP2 is tightly sandwiched between ELP1/IKI3 and ELP3 (PubMed:31309145). The Elp123 subcomplex binds tRNA through ELP1/IKI3 and ELP3 and can bind 2 tRNAs simultaneously (PubMed:31309145). tRNA-binding by the Elp123 subcomplex induces conformational rearrangements which precisely position the targeted anticodon base in the active site (PubMed:31309145). The Elp456 subcomplex binds tRNA and has ATPase activity (PubMed:22556426, PubMed:22343726). ELP4 interacts with KTI12 (PubMed:15772087).
Component of the elongator complex, a multiprotein complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:15769872, PubMed:18755837). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:29332244). It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin) (PubMed:11296232). May also be involved in sensitivity to Pichia inositovora toxin (PubMed:13680368).
The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification.
May be involved in phosphate metabolism.
Belongs to the cyclophilin-type PPIase family. PPIase B subfamily.
Induced by ER stress caused by treatment with tunicamycin.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Belongs to the STXBP/unc-18/SEC1 family.
Essential for vacuolar protein sorting. Function in membrane traffic between the Golgi and the vacuole.
Present with 5660 molecules/cell in log phase SD medium.
Component of the TOM (translocase of outer membrane) receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM20 and TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore.
Forms part of the TOM (translocase of outer membrane) complex that consists of at least 7 different proteins (TOM5, TOM6, TOM7, TOM20, TOM22, TOM40 and TOM70). In the complex interacts with TOM22. Interacts with TOM37.
Present with 45300 molecules/cell in log phase SD medium.
Belongs to the DNA photolyase class-1 family.
Binds 1 5,10-methenyltetrahydrofolate (MTHF) non-covalently per subunit.
Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation.
There are only 150-300 molecules of photolyase per yeast cell.
Belongs to the aerobic coproporphyrinogen-III oxidase family.
Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
Belongs to the eukaryotic ribosomal protein eL19 family.
Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). eL19 lies in close proximity to the binding site for eukaryotic initiation factor eIF4G (PubMed:9559554, PubMed:22096102).
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. eL19 may play a role in the last stages of translation initiation, in particular subunit joining and shedding/releasing factors.
Present with 225000 molecules/cell in log phase SD medium.
Present with 97700 molecules/cell in log phase SD medium.
Acts as essential component of the translation initiation factor 2B (eIF2-B or GCD complex), which catalyzes the exchange of eukaryotic initiation factor 2 (eIF-2)-bound GDP for GTP and is regulated by phosphorylated eIF-2. It activates the synthesis of GCN4 in yeast under amino acid starvation conditions by suppressing the inhibitory effects of multiple AUG codons present in the leader of GCN4 mRNA. It may promote either repression or activation of GCN4 expression depending on amino acid availability. GCD2 is also required for cell viability. Its function can partially be replaced by GCN3 under normal growth conditions in GCD2-defective mutants, under AA starvation conditions GCN3 is an antagonist (GCN4 translational activator).
Plays a role in sister chromatid separation.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors.
Belongs to the UTP23/FCF1 family. FCF1 subfamily.
Essential protein involved in pre-rRNA processing and 40S ribosomal subunit assembly. Required for the early cleavage steps of 35S rRNA at the A(0), A(1), and A(2) sites.
Component of the heterotetrameric kinetochore subcomplex COMA, which consists of AME1, CTF19, MCM21 and OKP1 (PubMed:10323865, PubMed:14633972). The COMA subcomplex is part of a larger constitutive centromere-associated network (CCAN) (also known as central kinetochore CTF19 complex in yeast), which is composed of at least AME1, CHL4, CNN1, CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1 (PubMed:12408861, PubMed:22561346). COMA binds the centromeric nucleosome-binding protein MIF2, and to the outer kinetochore MIND subcomplex (By similarity). CTF19 interacts with the CTF3 complex subunits CTF3, MCM16 and MCM22 as well as CHL4 and IML3 (PubMed:11782448, PubMed:12589047). Interacts with the N-terminal domain of centromeric nucleosome protein CSE4 and with the CBF3 complex subunit A (CBF2) (PubMed:10958698).
Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore COMA complex, which connects centromere-associated proteins and the outer kinetochore. COMA interacts with other inner kinetochore proteins to form the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
General amino acid permease with broad substrate specificity.
Belongs to the SWR1 complex at least composed of ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4, SWC5, SWR1 and HTZ1. Interacts with HTZ1.
Participates in the catalytic exchange of histone H2A for the H2A variant HTZ1, an euchromatin-specific factor, leading to chromatin remodeling and changes in transcription of targeted genes. Indirectly involved in vacuolar protein sorting.
E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC1 and UBC7 E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of endoplasmic reticulum proteins (ERQC), also called ER-associated degradation (ERAD). Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). In ERAD-L, facilitates retrotranslocation of misfolded proteins from the ER lumen through the ER membrane in conjunction with DER1 (PubMed:32327568). Both proteins have lateral gates facing each other which form a channel through the ER membrane and which distort the membrane region between the lateral gates, making it much thinner than a normal phospholipid bilayer (PubMed:32327568). Substrates insert into the membrane as a hairpin loop with one strand interacting with DER1 and the other with HRD1. ERAD-L substrates are ubiquitinated through HRD1 in conjunction with the E2 ubiquitin-conjugating enzymes UBC1 and UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via the action of the CDC48-NPL4-UFD1 ATPase complex and targeted to the proteasome. ERAD-M substrates are processed by the same HRD1-HRD3 core complex, but only a subset of the other components is required for ERAD-M.
Impaired degradation of proteins with misfolded intramembrane or lumenal domains.
Monomer (PubMed:32327568). Has also been shown to form homodimers (PubMed:28682307). However, dimer assembly is likely to be non-physiological (PubMed:32327568). Forms homooligomers in a USA1-dependent manner (PubMed:20005842, PubMed:21074049). However, can function as a monomer in ERAD-L so the role of USA1-dependent oligomerization remains unclear (PubMed:32327568). Component of the HRD1 ubiquitin ligase complex which contains the E3 ligase HRD1, its cofactors HRD3, USA1 and DER1, substrate recruiting factor YOS9 and CDC48-binding protein UBX2 (PubMed:16873066). Within the complex, interacts directly with HRD3 and USA1 and indirectly with DER1 (PubMed:11018054, PubMed:16619026, PubMed:20005842, PubMed:21074049, PubMed:28682307). In ERAD-L, HRD3 and YOS9 jointly bind misfolded glycoproteins in the endoplasmic reticulum (ER) lumen (PubMed:32327568). Movement of ERAD-L substrates through the ER membrane is facilitated by HRD1 and DER1 which have lateral gates facing each other and which distort the membrane region between the lateral gates, making it much thinner than a normal phospholipid bilayer (PubMed:32327568). Substrates insert into the membrane as a hairpin loop with one strand interacting with DER1 and the other with HRD1 (PubMed:32327568). The HRD1 complex interacts with the heterotrimeric CDC48-NPL4-UFD1 ATPase complex which is recruited by UBX2 via its interaction with CDC48 and which moves ubiquitinated substrates to the cytosol for targeting to the proteasome (PubMed:16873066, PubMed:16619026). The HRD1 complex interacts with the ERAD substrates HMG1 and HMG2 (PubMed:11390656). Interacts with the associated E2 ubiquitin conjugating enzymes UBC1 and UBC7 with its membrane anchor CUE1 (PubMed:11146622).
Belongs to the glycosyl hydrolase 17 family.
Glucanases possibly play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation.
Present with 38000 wall-bound molecules/cell in log phase YPD medium.
By maltose and maltotriose. Repressed by glucose.
High-affinity uptake of maltose and maltotriose. Also transports alpha-methylglucoside, glucose and turanose but not melezitose or trehalose.
Belongs to the universal ribosomal protein uS3 family.
Present with 146000 molecules/cell in log phase SD medium.
Ubiquitinated at 'Lys-212' by HEL2/UBC4.
Interacts with GSP1/GSP2, polyadenylate-binding protein PAB1 and PRP40.
Present with 7080 molecules/cell in log phase SD medium.
Receptor for the leucine-rich nuclear export signal (NES).
Binds to MCB elements (Mlu I cell cycle box) found in the promoter of most DNA synthesis genes. Transcriptional activation by MBF has an important role in the transition from G1 to S phase. It may have a dual role in that it behaves as an activator of transcription at the G1-S boundary and as a repressor during other stages of the cell cycle.
Component of the transcription complex MCB-binding factor (MBF) composed of SWI6 and MBP1. Interacts with MSA1.
Produced by +1 ribosomal frameshifting between codon Leu-431 and Gly-432 of the YFL002W-B ORF.
Produced by +1 ribosomal frameshifting between codon Leu-431 and Gly-432 of the YGR161W-A ORF.
Involved in nucleotide excision repair (NER) of damaged ribosomal DNA (rDNA). Required for the repair of the RNA polymerase I-transcribed strand of rDNA.
Transcriptional activator of promoters containing ATF/CREB sites. Can independently stimulate transcription through ATF/CREB sites. Important for a variety of biological functions including growth on non-optimal carbon sources.
Interacts with NCS6 and URM1. May act by forming a heterodimer with NCS6.
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation and in invasive and pseudohyphal growth. Inhibits replication of Brome mosaic virus.
Present with 2990 molecules/cell in log phase SD medium.
Stimulates specifically the GTPase activity of YPT6.
Involved in resistance to compounds that target ergosterol biosynthesis, including fenpropimorph, dyclonine, and alverine citrate. Since a deletion in the absence of these compounds does not have an effect on growth, is more likely to be involved in compound availability.
Belongs to the sterol desaturase family. SCS7 subfamily.
Binds 2 Zn(2+) ions per subunit that likely form a catalytic dimetal center.
Causes a lack of alpha-hydroxylated very long chain fatty acids in yeast sphingolipids. This confers resistance to syringomycin E, an antifungal cyclic lipodepsinonapeptide produced by Pseudomonas syringae.
Ceramide hydroxylase involved in the hydroxylation of sphingolipid-associated very long chain fatty acids (PubMed:9353282, PubMed:9368039, PubMed:26977056, PubMed:9559540, PubMed:16652392, PubMed:19074599). Postulated to hydroxylate the very long chain fatty acid of dihydroceramides and phytoceramides at C-2 (PubMed:9368039, PubMed:26977056).
The histidine box domains may contain the active site and/or be involved in metal ion binding.
Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme.
LPD1 is a homodimer. Eukaryotic pyruvate dehydrogenase (PDH) complexes are organized as a core consisting of the oligomeric dihydrolipoamide acetyl-transferase (E2), around which are arranged multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and protein X (E3BP) bound by non-covalent bonds. LPD1 is a component of the glycine decarboxylase complex (GDC), which is composed of four proteins: P, T, L and H.
Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase complex, which catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Acts also as component of the glycine cleavage system (glycine decarboxylase complex), which catalyzes the degradation of glycine.
Present with 24600 molecules/cell in log phase SD medium.
The active site is a redox-active disulfide bond.
Belongs to the ferric reductase (FRE) family.
By transcription factor AFT2 upon iron deprivation.
Metalloreductase responsible for reducing vacuolar iron and copper prior to transport into the cytosol. Catalyzes the reduction of Fe(3+) to Fe(2+) and Cu(2+) to Cu(+), respectively, which can then be transported by the respective vacuolar efflux systems to the cytosol.
Can suppress the lethality due to deletion of SIT4, and partially the defects due to BCY1 disruption. Is implicated in the control of the cell cycle G1 phase.
Several alleles of SSD1 exist in different yeast strains.
Cell wall protein that participates directly in adhesive cell-cell interactions during yeast flocculation, a reversible, asexual and Ca(2+)-dependent process in which cells adhere to form aggregates (flocs) consisting of thousands of cells. The lectin-like protein sticks out of the cell wall of flocculent cells and selectively binds mannose residues in the cell walls of adjacent cells. Activity is inhibited by mannose, but not by glucose, maltose, sucrose or galactose. Also involved in cell-substrate adhesion.
The number of the intragenic tandem repeats varies between different S.cerevisiae strains. There is a linear correlation between protein size and the extend of adhesion: the more repeats, the stronger the adhesion properties and the greater the fraction of flocculating cells. The Ser/Thr-rich repeats are also important for proper cell wall targeting of the protein.
Belongs to the methyltransferase superfamily. Tam family.
Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate and 3-isopropylmalate at high affinity and of other molecules like cis-aconitate, isocitrate, and citrate at lower velocities and affinities. The function of trans-aconitate methylation appears to be in reducing the toxicity of this spontaneous breakdown product of cis-aconitate. The role of 3-isopropylmalate methylation is unclear but may represent a metabolic branch at 3-isopropylmalate, where some of the material is taken in the pathway leading to leucine and some is taken in a pathway to the 3-isopropylmalate methyl ester, a molecule that provides a signal to switch from vegetative to invasive growth in response to amino acid starvation.
Component of TORC1, which regulates multiple cellular processes to control cell growth in response to environmental signals. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls ribosome biogenesis via control of rRNA, ribosomal protein and tRNA gene expression, and rRNA processing. TORC1 positively controls protein biosynthesis by regulation of mRNA stability, translation initiation factor activity, and high-affinity amino acid permeases that serve to provide amino acids for use by the translation machinery. TORC1 also promotes growth by sequestering a number of nutrient and general stress-responsive transcription factors in the cytoplasm. TORC1 negatively controls macroautophagy, a process to recycle surplus cytoplasmic mass under nutrient starvation conditions. KOG1 may have a role in binding and recruiting substrates of TORC1.
The target of rapamycin complex 1 (TORC1) is composed of at least KOG1, LST8, TCO89 and either TOR1 (TORC1-A) or TOR2 (TORC1-B) (PubMed:12408816, PubMed:12631735, PubMed:16394584). Interacts with PIB2; following activation of PIB2 by glutamine or cysteine (PubMed:29698392). TORC1 binds to and is inhibited by FKBP-rapamycin (PubMed:12408816).
Belongs to the adaptor complexes small subunit family.
Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits.
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (PubMed:9058184). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex (PubMed:9058184).
By stress, probably through the induction by the transcription factor PDR1.
Transcription factor that binds to the VHRE consensus sequence in promoters of VHT1 and BIO5, and regulates their biotin-dependent expression.
ADIPOR-like receptor involved in zinc metabolism either by altering membrane sterol content or by directly altering cellular zinc levels.
Expression is regulated by the zinc metabolism transcription factor ZAP1 via its promoter ZRE element (zinc-responsive element).
Deubiquitinating enzyme involved in telomere and HM loci silencing, which is the repression of chromatin structure which leads to a stop in the transcription of nearby genes (PubMed:9755194, PubMed:10490600, PubMed:14623890). Targets histone H2B for deubiquitination, thus helping to localize SIR2 to the telomere (PubMed:15721261, PubMed:17028327, PubMed:22056669). At silent chromatin, including telomeres and the rDNA locus, not only maintains low H2B 'Lys-123' ubiquitination (H2BK123Ub), but also low H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively) (PubMed:15721261, PubMed:15988024). Controls the proliferating-cell nuclear antigen PCNA/POL30 deubiquitination which is crucial for keeping TLS polymerases in check as well as for down-regulating the error-free bypass (PubMed:22829782). Deubiquitinates and stabilizes RPA190, the largest subunit of RNA polymerase I, to achieve optimal levels of ribosomes and cell growth (PubMed:22902402). Protects also nutrient transporters such as GAP1 from ubiquitin-dependent endocytosis (PubMed:11352638).
Exhibits reduced silencing and a corresponding decrease in the level of SIR4 (PubMed:10490600). Reduces also the level of the low-affinity, high-capacity transporter of amino acids GAP1 (PubMed:11352638). Leads to alterations in expression of subtelomeric genes together with a broad change in the whole transcriptional profile, closely parallel to that induced by oxidative stress (PubMed:14623890). Results also in extrachromosomal rDNA circles (ERCs) accumulation (PubMed:17028327). Accumulates also mono- and di-ubiquitinated PCNA/POL30 in response to DNA damage and replicative stress (PubMed:22829782). Leads to reduced pre-rRNAs, mature rRNAs, and translating ribosomes (PubMed:22902402).
Interacts with SIR4 (PubMed:10490600, PubMed:26149687). Interacts with the proliferating-cell nuclear antigen PCNA/POL30 (PubMed:22829782). Interacts with DHR2 and UTP22 (PubMed:22902402, PubMed:26149687).
Residues 109-145 within the N-terminal intrinsically disordered regions (IDR) constitute the binding module for SIR4 which required to coordinate the UBP10-SIR4 interaction, but also to direct UBP10's functional role in telomere chromatin silencing (PubMed:26149687).
Residues 167-208 within the N-terminal intrinsically disordered regions (IDR) constitute the binding module for UTP22 which is required to coordinate the UBP10-UTP22 interaction (PubMed:26149687).
Residues 2-27 within the N-terminal intrinsically disordered regions (IDR) constitute the binding module for DHR2 which is required to coordinate the UBP10-DHR2 interaction (PubMed:26149687).
Belongs to the KCH1 low affinity K(+) transporter family.
Expression is strongly induced during the response to alpha-factor.
Leads to high-affinity Ca(2+) influx system (HACS) deficiency (PubMed:21252230, PubMed:23204190). Causes a large increase of cell death in response to mating pheromone, when KCH1 is also deleted (PubMed:23204190).
Low affinity potassium transporter that, with KCH1, participates in high-affinity Ca(2+) influx system (HACS) activation during the response to mating pheromone (PubMed:21252230, PubMed:23204190). Directly promotes K(+) influx and HACS may electrochemically respond to this K(+) influx (PubMed:23204190). KCH1 and PRM6/KCH2 act at the apex of the calcium signaling pathway that is used for survival during prolonged exposures to mating pheromones (PubMed:23204190).
Belongs to the dolichyldiphosphatase family.
Causes an elevation in dolichyl diphosphate levels.
Non-essential protein which is required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides. Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl monophosphate at a much lower rate. Does not act on phosphatidate.
Belongs to the CitM (TC 2.A.11) transporter family.
Expression is constitutive and independent of inorganic phosphate concentration and PHO4 activity.
Ubiquitinated by RSP5. RSP5-mediated ubiquitination initiates internalization and degradation by the endocytic pathway.
Vacuolar phosphate transporter that probably exports phosphate from the vacuolar lumen to the cytosol.
Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase subunit family.
Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB11 is part of the core element with the central large cleft. Seems to be involved transcript termination.
Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1. Interacts (via C-terminus) with CWC21. Interacts (via N-terminus) with PRP8 (via SCwid domain).
Component of the U5 snRNP complex required for pre-mRNA splicing. Binds GTP.
Ty1-DR5 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Ty1-ER2 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Ty1-GR3 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Ty1-LR1 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Ty1-MR2 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Belongs to the importin beta family. Importin beta-2 subfamily.
Binds to nucleoporin FxFG but not PSFG repeat regions.
Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for arginine/glycine-rich nuclear localization signals (rg-NLS) and PY-NLS in cargo substrates. Its predominant cargo substrate seems to be mRNA-binding proteins. Required for nuclear transport of NAB2, HRP1/NAB4 and TFG2. Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins (PubMed:8849456, PubMed:9488461, PubMed:10506153, PubMed:19366694). The complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:11423015). At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo. Efficient GTP-Ran-mediated substrate release requires RNA (PubMed:10506153). The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:11423015).
Interacts with Ran (GSP1) (PubMed:9321403, PubMed:10506153); interacts specifically with the GTP-bound form of Ran (GTP-Ran), protecting it from GTP hydrolysis and nucleotide exchange (PubMed:9321403). Interacts with nucleoporins NUP1, NUP100 and NUP116 (PubMed:8849456). Interacts with NAB2 and HRP1/NAB4; via their rg-NLS (PubMed:9488461, PubMed:10506153). Interacts with TFG2; via its PY-NLS (PubMed:19366694).
Monomer; increments in mitochondrial iron uptake induce stepwise assembly of species ranging from trimers to 24-mers. Interacts with ISU1. Interacts with YHB1, SDH1, SDH2, AIM45 and CIR1.
Processed in two steps by mitochondrial processing peptidase (MPP). MPP first cleaves the precursor to intermediate form and subsequently converts the intermediate to mature size protein.
Promotes the biosynthesis of heme as well as the assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. Plays a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+). Can store large amounts of the metal in the form of a ferrihydrite mineral by oligomerization. May be involved in regulation of the mitochondrial electron transport chain.
GTPase-activating protein (GAP) for ARF1 and ARF2. Involved in intracellular vesicular transport. Required for transport from the trans-Golgi network. Implicated in the regulation of retrograde transport from the Golgi to the ER and in actin cytoskeletal organization. May be involved in the maintenance of mitochondrial morphology, possibly through organizing the actin cytoskeleton in Saccharomyces.
Present with 9560 molecules/cell in log phase SD medium.
Heterohexamer; composed of 3 copies of TIM8 and 3 copies of TIM13, named soluble 70 kDa complex. Associates with the TIM22 complex, whose core is composed of TIM18, TIM22 and TIM54. Interacts with the transmembrane regions of multi-pass transmembrane proteins in transit.
Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIM8-TIM13 complex is non essential and only mediates the import of few proteins under precise conditions, while the predominant TIM9-TIM10 70 kDa complex is crucial and mediates the import of much more proteins. Strictly required for import of TIM23 in some conditions, when a low membrane potential exists in the mitochondria.
The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIM8 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (Probable).
Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which associates with catalytic subunits DIS3 and RRP6 in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits and peripheral S1 domain-containing components CSL4, RRP4 and RRP40 located on the top of the ring structure. Interacts with LRP1/RRP47.
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP4 as peripheral part of the Exo-9 complex is thought to stabilize the hexameric ring of RNase PH-domain subunits.
Present with 4840 molecules/cell in log phase SD medium.
Was originally (PubMed:9390555 and PubMed:8600032) thought to have exonuclease activity but it was later shown (PubMed:17173052 and PubMed:17174896) that only DIS3/RRP44 subunit of the exosome core has this activity.
Present with 2140 molecules/cell in log phase SD medium.
Component of the ASTRA chromatin remodeling machinery complex composed of at least RVB1, RVB2, TRA1, TEL2, TT1 and TTI2. Component of the TTT complex composed of TEL2, TTI1 and TTI2. Interacts with TEL2 and TTI2.
Component of the ASTRA complex involved in chromatin remodeling.
Activator of G1-specific transcription factors, MBF and SBF. Promotes both the timing of G1-specific gene transcription and cell cycle initiation. Associates with SBF- and MBF-regulated target promoters and this binding is maximal during the G1 phase, prior to maximum budding. Affects cell cycle initiation by advancing the timing of transcription of G1-specific genes. Overexpression advances the timing of SBF-dependent transcription and budding. Depletion delays both indicators of cell cycle initiation.
Expressed periodically during the cell cycle with peak mRNA levels occurring at the late M/early G1 phase, prior to budding, and levels decrease rapidly as cells enter into the S phase. In early G1 peak occurs (at protein level).
Interacts with transcription complexes SCB-binding factor (SBF) and MCB-binding factor (MBF) at their target promoters. Interacts with MBP1 and SWI6.
Component of the RPD3 histone deacetylase complex RPD3C(L) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. DOT6 binds to sequences containing the core CGATG, which resembles the PAC (Polymerase A and C) motif.
Component of the RPD3C(L) complex composed of at least ASH1, CTI6, DEP1, DOT6, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, TOD6; UME1 and UME6.
Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
Catalytic subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDH1 and SDH2 form the catalytic dimer. Electrons flow from succinate to the FAD bound to SDH1, and sequentially through the iron-sulfur clusters bound to SDH2 and enter the membrane dimer formed by SDH3 and SDH4.
Component of complex II composed of four subunits: a flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a large and a small subunit. Interacts with EMI5/SDH5; interaction is required for FAD attachment.
Present with 10400 molecules/cell in log phase SD medium.
Acts as a component of the m-AAA protease complex which is a ATP-dependent metalloprotease mediating degradation of non-assembled mitochondrial inner membrane proteins. The complex is necessary for the assembly of mitochondrial respiratory chain and ATPase complexes. Function both in post-translational assembly and in the turnover of mistranslated or misfolded polypeptides.
Component of the 850 kDa m-AAA protease complex (YTA10-12) which consists of multiple copies of RCA1 and AFG3.
Present with 11500 molecules/cell in log phase SD medium.
Present with 2220 molecules/cell in log phase SD medium.
Serine/threonine-protein kinase involved in the control of sugar metabolism and translation. Phosphorylates UGP1, which is required for normal glycogen and beta-(1,6)-glucan synthesis. This phosphorylation shifts glucose partitioning toward cell wall glucan synthesis at the expense of glycogen synthesis. Phosphorylates also the glycogen synthase GSY2 and the translation factors CAF20, TIF11 and SRO9.
Belongs to the class V-like SAM-binding methyltransferase superfamily. RKM1 family.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates elongation factor 1-alpha (TEF1/TEF2) at 'Lys-30'.
Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
High affinity uptake of sulfate into the cell.
Irreversibly catalyzes the reduction of fumarate to succinate. Together with the second isozyme of soluble fumarate reductase (OSM1), essential for anaerobic growth. Involved in maintaining redox balance. Reduction of fumarate is the main source of succinate during fermentation, and under anaerobic conditions, the formation of succinate is strictly required for the reoxidation of FADH(2).
Present with 7620 molecules/cell in log phase SD medium.
Belongs to the ABC transporter superfamily.
Cooperates for the ATP-dependent vacuolar transport of bilirubin and glutathione conjugates.
Levels increase in early stationary phase.
Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (PubMed:9090384, PubMed:19687296, PubMed:22471590, PubMed:11370741, PubMed:35768507). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (PubMed:35768507). PEX12 also regulates PEX5 recycling by activating the E3 ubiquitin-protein ligase activity of PEX10 (PubMed:35768507). When PEX5 recycling is compromised, PEX12 stimulates PEX10-mediated polyubiquitination of PEX5, leading to its subsequent degradation (PubMed:35768507).
Component of the PEX2-PEX10-PEX12 retrotranslocation channel, composed of PEX2, PEX10 and PEX12.
The RING-type zinc-finger is degenerated and only coordinates one zinc ions, preventing E3 ubiquitin-protein ligase activity.
The three subunits of the retrotranslocation channel (PEX2, PEX10 and PEX12) coassemble in the membrane into a channel with an open 10 Angstrom pore (By similarity). The RING-type zinc-fingers that catalyze PEX5 receptor ubiquitination are positioned above the pore on the cytosolic side of the complex (By similarity).
Cleavable component of the cohesin complex involved in chromosome cohesion during cell cycle. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by ESP1 and dissociates from chromatin, allowing sister chromatids to segregate.
Cleaved by ESP1 at the onset of anaphase.
Interacts directly with IRR1/SCC3 in cohesin complex. Cohesin complexes are composed of the SMC1 and SMC3 heterodimer attached via their hinge domain, MCD1/SCC1 which link them, and IRR1, which interacts with MCD1. The cohesin complex also interacts with SCC2, which is required for its association with chromosomes.
Phosphorylated by CDC5/Polo-like kinase at the onset of anaphase. Phosphorylation takes places at proximity to cleavage sites and is required for an efficient cleavage by ESP1.
The C-terminal part associates with the head of SMC1, while the N-terminal part binds to the head of SMC3.
Acts as component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. The NOT protein subcomplex negatively regulates the basal and activated transcription of many genes. Preferentially affects TC-type TATA element-dependent transcription. Could directly or indirectly inhibit component(s) of the general transcription machinery.
Present with 1380 molecules/cell in log phase SD medium.
Subunit of the 1.0 MDa CCR4-NOT core complex that contains CCR4, CAF1, CAF120, NOT1, NOT2, NOT3, NOT4, NOT5, CAF40 and CAF130. In the complex interacts with NOT1. The core complex probably is part of a less characterized 1.9 MDa CCR4-NOT complex.
Belongs to the eukaryotic RPA49/POLR1E RNA polymerase subunit family.
Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA. Forms a TFIIF-like heterodimer with RPA34; the heterodimer formed by RPA34 and RPA49 can be dissociated from the Pol I core giving rise to a 12 subunit form A* of Pol I (formerly called pol A) that shows impaired transcript elongation activity and increased sensitivity to alpha-amanitin. The heterodimer formed by RPA34 and RPA49 stabilizes subunit RPA12 and stimulates RPA12-dependent RNA cleavage.
DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. The heterodimer formed by RPA34 and RPA49 stimulates transcript elongation by Pol I. Subunit RPA49 can bind both single-stranded and double-stranded DNA.
Belongs to the protein-tyrosine phosphatase family.
Present with 4070 molecules/cell in log phase SD medium.
Selectively cleaves the beta-phosphate at the 5-position of soluble inositol pyrophosphates. Converts 5-diphosphoinositol tetrakisphosphate (5-PP-InsP(4)) into inositol pentakisphosphate (InsP(5)), 5-diphosphoinositol pentakisphosphate (5-PP-IP(5) or 5-InsP(7)) into inositol hexakisphosphate (IP(6) or InsP(6)), and 1,5-bisdiphosphoinositol tetrakisphosphate (1,5-PP-IP(5) or InsP(8)) into 1-diphosphoinositol pentakisphosphate (1-PP-IP(5) or 1-InsP(7)) (PubMed:26828065, PubMed:29540476). Modulates inositol pyrophosphate metabolism that may have an influence in stress response (PubMed:26828065). Plays a role in actin filament organization and endocytosis (PubMed:15020461). Functions as a prion suppressing factor possibly due to its phosphatase activity against inositol pyrophosphates, which are signal transduction molecules involved in prion propagation (PubMed:28923943).
Belongs to the Orn/Lys/Arg decarboxylase class-II family.
Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
Homodimer (PubMed:2669750). Only the dimer is catalytically active, as the active sites are constructed of residues from both monomers (By similarity).
Inhibited by antizyme (AZ) OAZ1 in response to polyamine levels. AZ inhibits the assembly of the functional homodimer by binding to ODC monomers and targeting them for ubiquitin-independent proteolytic destruction by the 26S proteasome.
Increases frequency of mitochondrial genome loss and sensitivity to freeze-thaw stress and high concentrations of glucose.
May interact with the nuclear pore complex.
Forms a NOT protein complex that comprises NOT1, NOT2, NOT3, NOT4 and NOT5. Subunit of the 1.0 MDa CCR4-NOT core complex that contains CCR4, CAF1, NOT1, NOT2, NOT3, NOT4, NOT5, CAF40 and CAF130. The core complex probably is part of a less characterized 1.9 MDa CCR4-NOT complex.
Was originally thought to be CDC39 (which is in fact NOT1).
Protein involved in the regulation of cell wall assembly and 1,3-beta-glucan synthesis, possibly through the transcriptional regulation of cell wall glucan and chitin synthesis.
By copper deprivation, and repressed by copper sufficiency.
Required for high affinity copper (probably reduced Cu I) transport into the cell.
Positive transcriptional factor that acts as a component of the stress responsive system. Recognizes and binds to the stress response element (STRE) which is involved in the response to various forms of stress (heat, oxidative, osmotic, etc.). Involved in the regulation of the CTT1, DDR2, HSP12 genes.
the 9aaTAD motif (residues 237 to 245) is a transactivation domain present in a large number of yeast and animal transcription factors.
Belongs to the DNA polymerase type-B family.
Catalytic component of the DNA polymerase epsilon complex which participates in chromosomal DNA replication (PubMed:1537345). Required during synthesis of the leading DNA strands at the replication fork, binds at/or near replication origins and moves along DNA with the replication fork (PubMed:31488849). Has 3'-5' proofreading exonuclease activity that corrects errors arising during DNA replication (PubMed:12124389).
DNA polymerase epsilon is a heterotetramer consisting of POL2, DPB2, DPB3 and DPB4.
Present with 1970 molecules/cell in log phase SD medium.
The CysA-type zinc finger is required for PCNA-binding.
The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes.
The DNA polymerase activity domain resides in the N-terminal half of the protein, while the C-terminus is necessary for complexing subunits B and C.
Involved in resistance to arsenic compounds.
Binds to the promoters of genes with functions important for the G1/S (start) transition; primarily genes involved in DNA synthesis and repair, chromosome segregation, nuclear division and transcription.
Regulated in a cell cycle-dependent manner, peaking in G1 phase. Negatively regulated by transcription factor SBF (SWI4-SWI6 cell-cycle box binding factor).
Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family.
Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. Can bind to DNA (in vitro).
In contrast to other lysine histone methyltransferases, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones.
Ubiquitination of histone H2B by the RAD6/UBC2-BRE1 complex to form H2BK123ub1 is required for efficient DOT1 methyltransferase activity on histone H3. Interaction with DNA is required for optimal histone methyltransferase activity.
Belongs to the class I-like SAM-binding methyltransferase superfamily. MenG/UbiE family.
Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. Interacts with COQ3.
Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Present with 8100 molecules/cell in log phase SD medium.
Component of the outer cell wall layer. Required for stability of the cell wall and for optimal growth. Required for resistance against several antifungal and cell wall-perturbing agents and for tolerance to heat shock.
Covalently linked to beta-1,3-glucan of the inner cell wall layer via an alkali-sensitive ester linkage between the gamma-carboxyl group of glutamic acids, arising from specific glutamines within the PIR1/2/3 repeats, and hydroxyl groups of glucoses of beta-1,3-glucan chains.
O-glycosylated. Extensively O-mannosylated.
Positively regulated by signaling through MPK1 in response to cell wall perturbation. Induced by heat shock and nitrogen starvation. Expression is also regulated by the ACE2 and SWI5 transcription factors.
The PIR1/2/3 repeats are required for the covalent linkage to the cell wall (By similarity). Their number varies among different strains of S.cerevisiae.
The propeptide is cleaved off in the late Golgi. While both peptides are secreted, only a fraction of the mature glycoprotein is incorporated into the cell wall.
Required for HMG2-induced endoplasmic reticulum-remodeling.
Involved in mitochondrial distribution and morphology.
Belongs to the PEX28-32 family. PEX32 subfamily.
Involved in ribosome biogenesis, probably through modulation of rDNA transcription.
Associated with snR10 and snR11 small nuclear RNAs.
Functions in the transition of mRNAs from translation to an mRNP complex destined for decapping. High-copy-number suppressor of decapping defects. Overexpression suppresses decapping defects in both DCP1-2 and DCP2-7 mutations. Acts to promote translational repression of mRNA in conjunction with DHH1 and subsequent mRNA localization to P bodies. Promotes translational repression of mRNA during glucose deprivation.
Present with 12800 molecules/cell in log phase SD medium.
Component of the SRP (signal recognition particle) receptor (SR). Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system. GTP hydrolysis may enhance the fidelity of and provide unidirectionality to the targeting reaction. It is important but not essential for cell growth. May be directly involved in mitochondrial protein import.
Present with 2000 molecules/cell in log phase SD medium.
The NG domain, also named G domain, is a special guanosine triphosphatase (GTPase) domain, which forms a guanosine 5'-triphosphate (GTP)-dependent complex with a homologous NG domain in the signal recognition particle (SRP) complex subunit SRP54 (By similarity). The two NG domains undergo cooperative rearrangements upon their assembly, which culminate in the reciprocal activation of the GTPase activity of one another (By similarity). GTPase induced rearrangement of SR drives SRP-mediated cotranslational protein translocation into the ER (By similarity).
The SRX domain is sufficient for interaction with GTP-bound SRP102/SR-beta.
Tubulin-folding protein; involved in the early step of the tubulin folding pathway.
Acts as component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover.
Activated by N- and C-terminal proteolytic cleavage. Protease B (PrB/PRB1) processing requires at least 4 cleavages. First, the signal peptide is removed from the 76 kDa preproprotease B by signal peptidase in the ER. Then, PrB removes its own Pro-region (in trans) at the N-terminus, producing a 39 kDa form before exiting the ER. In the Golgi complex, the C-terminal Post-region of the 40 kDa proprotease B undergoes protease A (PrA/PEP4)-mediated processing to a 37 kDa intermediate, which in turn is quickly processed again by PrB in trans to yield the 31 kDa mature PrB.
Glycosylated. Preproprotease B is a 76 kDa unglycosylated precursor that enters the endoplasmic reticulum (ER), where it receives one Asn-linked and an undetermined number of non-Asn-linked carbohydrate side chains. In the Golgi complex, the 39 kDa form becomes 40 kDa, due to elaboration of the Asn-linked side chain. The ultimate processing step removes a peptide containing the Asn-linked chain. Mature PrB has only non-Asn-linked carbohydrates.
Vacuolar proteinase B involved in protein degradation in the vacuole. Among other substrates, acts on carboxypeptidase Y (cpY/PRC1) to activate it by processing its Pro-peptide. Required for meiosis and spore formation, and for optimal survival in stationary phase.
[beta] is the prion form of PrB. In contrast to other prions, [beta] is not the result of a conformational change of the cellular PrB, but distinguishes itself by autoactivation in trans. Usually, PrB is already involved in its own maturatiuon, but PrA plays a critical role. PrpA mutants lack PrB. However, in growth conditions that favor PRB1 expression, PrB activity persists in PrA mutants due to autocleavage of PrB in trans. This condition is stably transmitted to daughter cells in mitosis. [beta] can be cured by growing in PRB1-repressing conditions. Once a cell has lost PrB activity, it remains stably inactive. Thus, there are 2 alternative states, that are chromosomally identical, but phenotypically distinct. Since PrA is able to activate PrB, normal cells always carry the [beta] prion. Its absence and transmission are only observable in the absence of PrA.
Interacts with the TFIID subunit TAF7 and with acetylated histones H3 and H4.
Phosphorylated by the casein kinase CK2 complex.
Transcription factor involved in the expression of a broad class of genes including snRNAs. Required for sporulation and DNA-damage repair. Prevents the spreading of SIR silencing at telomeres and protects histone H4, but not H3, from deacetylation.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
Present with 2760 molecules/cell in log phase SD medium.
S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 2270 (Gm2270) in the 21S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA. This modification seems to be important for the normal accumulation of the mitochondrial large ribosomal subunit.
Component of the 45S U1.U2.U4/U6.U5 penta-snRNP particle, a subcomplex of the spliceosome.
Present with 167 molecules/cell in log phase SD medium.
Promotes the assembly of newly synthesized U4 snRNA into the U4/U6 snRNP particle. Required for splicing of pre-mRNA.
Involved in negative regulation of the TOR signaling pathway in response to type of available nitrogen source. Indirectly activates the PP2A phosphatase SIT4 via interaction with its suppressor TAP42. This interaction is enhanced under nitrogen limitation conditions. Also has a role in regulation of NPR1 in response to nitrogen limitation.
Phosphorylation. Dephosphorylated by SIT4.
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.
Component of the AMP-activated protein kinase complex also known as the SNF1 kinase complex (Snf1c), a heterotrimeric complex composed of an alpha subunit (SNF1), a regulatory subunit beta (GAL83 and substoichiometric alternate beta subunits SIP1 and SIP2), and a regulatory subunit gamma (SNF4) (PubMed:2557546, PubMed:2481228, PubMed:7813428, PubMed:9121458, PubMed:15719021, PubMed:17851534). Interacts with the transcriptional activator SIP4 (PubMed:8628258). Interacts with SAK1 (PubMed:12748292, PubMed:16847059). Interacts with CTK1 (PubMed:16182287): Interacts with adenylate cyclase CYR1 (PubMed:26309257).
Expression of the SNF1 gene itself is not glucose repressible (PubMed:6366513).
Phosphorylation at Thr-210 in response to glucose limitation leads to activation of kinase activity (PubMed:11486005, PubMed:12748292). ADP, but not AMP, protects the enzyme from dephosphorylation at Thr-210 by GLC7 (PubMed:22019086).
Serine/threonine protein kinase essential for release from glucose repression (PubMed:3526554, PubMed:6366512, PubMed:3049551, PubMed:1944227, PubMed:8289797, PubMed:8628258, PubMed:25869125). Catalytic subunit of the AMP-activated protein kinase complex also known as the SNF1 kinase complex (Snf1c), a central regulator of cellular energy homeostasis, which, in response to a fall in intracellular ATP levels, activates energy-producing pathways and inhibits energy-consuming processes (PubMed:8289797, PubMed:26667037). The complex phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, leading to transcriptional activation through TBP recruitment to the promoters (PubMed:15719021). The complex also negatively regulates the HOG1 MAPK pathway in ER stress response including unfolded protein response (UPR) (PubMed:25730376, PubMed:26394309). Under nutrient/energy depletion, the complex phosphorylates and activates PAS kinase PSK1 which in turn activates PBS1, leading to the inhibition of the TORC1 signaling pathway (PubMed:25428989). SNF1 also interacts and phosphorylates adenylate cyclase CYR1 and negatively regulates the protein kinase A signaling pathway (PubMed:26309257). Also phosphorylates and regulates the transcriptional activator CAT8 (PubMed:15121831).
Sumoylation by the SUMO (E3) ligase MMS21 leads to inhibition by interaction of SUMO attached to Lys-549 with a SUMO-interacting sequence motif located near the active site of SNF1, and by targeting SNF1 for glucose-induced destruction via the SLX5-SLX8 (SUMO-directed) ubiquitin ligase (PubMed:24108357).
The kinase activity is positively regulated by SNF4 via sequestration of the SNF1 auto-inhibitory domain (AID) (PubMed:2557546, PubMed:17851534).
The regulatory domain (RS) also called auto-inhibitory domain (AID) inhibits kinase activity of the protein kinase domain (KD) (PubMed:19474788, PubMed:20823513). The AID is sequestered by SNF4 within the AMP-activated protein kinase complex which might correspond to the activated SNF1 form (PubMed:17851534).
The ubiquitin-associated domain (UBA) localized within the AID dampens kinase activation, probably by restraining SNF1-SNF4 associations (PubMed:25869125). Moreover, the UBA domain influences life span in a FKH1- and FKH2-dependent mechanism (PubMed:25869125).
Belongs to the acetyltransferase family. ECO subfamily.
Binds specifically to CHL12, RFC1, RFC2, RFC3, RFC4, RFC5 and RAD24 when members of an RFC complex. Interacts with CHL1 and MPS3.
Required for establishment of sister chromatid cohesion during S phase but not for its further maintenance during G2 or M phases or for loading the cohesin complex onto DNA. Interacts with the three known alternate replication factor C (RFC) complexes, suggesting that these complexes have essential but redundant activity in cohesion establishment. Acts by acetylating the cohesin complex component SMC3. In vitro, possesses acetyltransferase activity where it can acetylate itself and components of the cohesin complex (MCD1, IRR1 and PDS5), but is unable to acetylate histones.
Component of the 20S proteasome chaperone. Forms a heterodimer with IRC25 that binds to proteasome precursors. Interacts with POP2.
Involved in 20S proteasome assembly, facilitating the alpha-ring formation. Involved in maintenance of telomere length.
Present with 2210 molecules/cell in log phase SD medium.
Belongs to the aspartate-semialdehyde dehydrogenase family.
By high concentrations of Met (general AA biosynthesis control).
Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.
Present with 18400 molecules/cell in log phase SD medium.
Belongs to the RSC7/SWP82 family. RSC7 subfamily.
Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. Together with HTL1, LDB7, RSC3, RSC30 components, defines a fungal-specific module within the RSC complex that plays a role in many cellular functions including the maintenance of cell wall integrity. Acidic protein important for nuclear protein localization.
Interacts with ARP7, ARP9, RSC3, RSC8, RSC30 and STH1. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin. Component of a fungal-specific module (HTL1-LDB7-NPL6-RSC3-RSC30) within the RSC complex.
Present with 3510 molecules/cell in log phase SD medium.
Belongs to the TPT transporter family. SLC35D subfamily.
Present with 98 molecules/cell in log phase SD medium.
This is a truncated version of GDP-mannose transporter 2. Strain S288c has a stop codon in position 73, which disrupts the gene coding for this protein and produces two ORFs YER039C-A and YER039C. A contiguous sequence for GDP-mannose transporter 2 can be found in strain Lalvin EC1118 (AC C8Z742).
Essential determinant for high-affinity spermidine transport. Required for the activation of the plasma membrane proton pump PMA1 via phosphorylation of 'Ser-899'.
Belongs to the ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily.
Functions as a pleiotropic drug pump at the plasma membrane to clear toxic substances from the cytosol. Organic anion transporter involved in the detoxification of a wide range of toxic environmental organic anions that contain carboxyl groups (PubMed:8663018). Required for tolerance to reveromycin A, tautomycin and leptomycin B (PubMed:8663018). Required for oligomycin resistance (PubMed:8524254, PubMed:10082567). Required for rhodamine B resistance. Mediates the ATP-dependent efflux of rhodamine B (PubMed:9575223). Involved in cadmium detoxification. Displays an energy-dependent efflux of cadmium and glutathione, suggesting that YOR1 transports both compounds as a bis-glutathionato-cadmium Cd-(GS)(2) complex (PubMed:16814918). Confers resistance to rhodamine 6G and to doxorubicin (PubMed:17950691).
Present with 3610 molecules/cell in log phase SD medium.
A mutant confers resistance to trichodermin, a trichotecene toxin produced by plant-pathogenic fungi.
Belongs to the universal ribosomal protein uL3 family.
Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). uL3 forms together with ES39L one of the contact sites for the signal recognition particle that targets ribosomes to the endoplasmic reticulum membrane (PubMed:9559554, PubMed:24865971, PubMed:22096102).
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:24865971, PubMed:22096102). The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules (PubMed:22096102). The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain (PubMed:22096102). The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). uL3 plays a role in coordinating processes of accommodating the aminoacyl-tRNA in the PTC (PubMed:22096102).
Methylation at His-243 by HPM1 is required for proper 60S subunit assembly and promotes translational elongation fidelity.
Belongs to the prefoldin subunit beta family.
Interacts directly with HST1 and SUM1. Required for the interaction between HST1 and SUM1.
Tethering factor required for histone deacetylase HST1-mediated repression. Probably involved in targeting HST1 to a subset of SUM1-regulated genes.
Present with 56 molecules/cell in log phase SD medium.
Seems to be involved in the anchoring of CDC24 to the membrane of polarized growth sites.
Belongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family.
Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC). Can also catalyze the first methylation reaction of PE to PMME in the absence of PE methyltransferase CHO2.
Expression is repressed by inositol and choline. The 5' flanking region contains two copies of the CATRTGAA motif and a 5'-AAACCCACACATG-3' GRFI site, which are involved in the regulation of expression. OPI1 and SIN3 play the role of repressors for OPI3 expression whereas UME6 is an activator of OPI3 expression.
Present with 5890 molecules/cell in log phase SD medium.
Active permease is phosphorylated (PubMed:7798155). The addition of glutamine causes rapid dephosphorylation and inactivation of the permease (PubMed:7798155).
Expression is repressed by ammonia (PubMed:2194797). Expression is induced by polyamines (PubMed:15707981). Both GLN3 and NIL1 bind the 5'-GATAAG-3' motif within the GAP1 promoter to activate transcription (PubMed:8636059).
General amino-acid permease involved in the uptake of all the naturally occurring L-amino-acids, related compounds such as ornithine and citrulline, some D-amino acids, toxic amino acid analogs such as azetidine-2-carboxylate, and the polyamines putrescine and spermidine (PubMed:5474888, PubMed:10467005, PubMed:10373490, PubMed:10953083, PubMed:14968425, PubMed:15707981). Senses its transport substrates to set an appropriate level of transporter activity at the cell surface (PubMed:21471002). Required for FLO11 expression and invasive growth (PubMed:22844449).
Ubiquitination by RSP5 and the RSP5-associated proteins BUL1 and BUL2, leads the addition of poly-ubiquitin chains being specifically formed by linkage through the lysine 63 residue of ubiquitin and mediates ammonium-induced endocytosis and degradation in the vacuole (PubMed:9614172, PubMed:10194416, PubMed:11500494, PubMed:11352928, PubMed:14523026, PubMed:15039776).
Component of a cytoskeletal structure that is required for the formation of endocytic vesicles at the plasma membrane level.
Mutations in this gene results in sensitivity to carbon, nitrogen and sulfur starvation.
Component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain. SSZ1 is required for ZUO1 to function efficiently as a J-protein for SSB1/SSB2. Also involved in pleiotropic drug resistance by post-translational activation of transcription factor PDR1.
Does not seem to bind unfolded protein substrates, as its C-terminal putative peptide-binding domain is not required for its function.
Neither ATP binding nor ATP hydrolysis is required for SSZ1 function.
Present with 73600 molecules/cell in log phase SD medium.
RAC is a heterodimer of the Hsp70/DnaK-type chaperone SSZ1 and the Hsp40/DnaJ-type chaperone ZUO1. RAC associates with ribosomes via ZUO1.
Component of a SNARE complex consisting of UFE1, USE1, SEC20 and SEC22 or YKT6.
Autoacetylation at Lys-168 is required for proper function.
Histone acetyltransferase (HAT) subunit of the SAS complex, a multiprotein complex that acetylates 'Lys-16' of histone H4 and 'Lys-14' of histone H3. The SAS complex is however unable to acetylate nucleosomal histones. The complex is involved in transcriptional silencing at telomeres and at HML locus. Also involved in rDNA silencing and G0 control.
Interacts with CAC1. Component of the SAS complex, at least composed of SAS2, SAS4 and SAS5. These three proteins constitute the core of the complex and are sufficient to acetylate histones. SAS4 is essential for HAT activity of the complex, while SAS5 is required for maxiaml HAT activity.
Involved in vesicular protein trafficking.
Present with 3190 molecules/cell in log phase SD medium.
Increases the periodicity of transcriptional and metabolic oscillation.
Present with 85 molecules/cell in log phase SD medium.
Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes like PCK1. Involved in restriction of Ty1 transposition.
Belongs to the glutamate 5-kinase family.
Belongs to the class IV-like SAM-binding methyltransferase superfamily.
May function as a N-methyl-N'nitro-N-nitrosoguanidine (MNNG) export permease.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
Interacts (via myosin motor domain) with SHE4; this interaction is important for proper localization and may regulate the interaction of the motor domain with actin. Interacts (via SH3 domain) with VRP1; this interaction is required for localization to sites of polarized growth and may regulate the interaction of the tail domain with actin. Interacts (via SH3 domain) with PAN1; this interaction is important for late stages of endocytopsis. Interacts (via SH3 domain) with BBC1 and LAS17. Interacts (via C-terminal acidic tail) with ARC19 and ARC40; ARC19 and ARC40 are Arp2/3 complex subunits.
One of two redundant type-I myosins implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions redundantly with LAS17 as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated actin assembly. Functions together with the NPF PAN1 in late stages of endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but not constitutive endocytosis of the G protein-coupled receptor STE2.
Phosphorylation of the TEDS site (Ser-357) is required for the polarization of the actin cytoskeleton and for ligand-induced, but not for constitutive internalization of STE2. Phosphorylation probably activates the myosin-I ATPase (By similarity). Ser-357 is phosphorylated by CLA4 and STE20 in vitro.
Present with 155 molecules/cell in log phase SD medium.
The myosin motor domain displays actin-stimulated ATPase activity and generates a mechanochemical force.
The tail domain participates in molecular interactions that specify the role of the motor domain. It is composed of several tail homology (TH) domains, namely a putative phospholipid-binding myosin tail domain (also named TH1), an Ala- and Pro-rich domain (TH2), followed by an SH3 domain and a C-terminal acidic domain (TH3).
Belongs to the phosphatase 2A regulatory subunit B family.
PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules.
The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.
Present with 12300 molecules/cell in log phase SD medium.
Plays a role in a RAD51/RAD54-dependent homologous recombination repair (HRR) pathway to repair MMS-induced lesions during S-phase. Required for error-free repair of spontaneous and induced DNA lesions to protect the genome from mutation.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YHR214C-C ORF.
Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. In contrast to the other IMPDH alleles IMD3 and IMD4, the enzymatic activity of IMD2 seems to be intrinsically drug resistant.
Induced by MPA resulting in resistance to the drug. Repressed by nutrient limitation.
Present with 7870 molecules/cell in log phase SD medium.
Belongs to the peptidase S26 family. IMP1 subfamily.
Catalytic component of the mitochondrial inner membrane peptidase (IMP) complex. IMP catalyzes the removal of signal peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. The two catalytic IMP subunits seem to have non-overlapping substrate specificities. IMP1 substrates include nuclear encoded CYB2, mitochondrially encoded COX2, NADH-cytochrome b5 reductase and GUT2.
By transcription factor SBF (SWI4-SWI6 cell-cycle box binding factor) in a cell cycle-regulated manner. Peaks in G1 phase.
Forms a cyclin-CDK complex with PHO85 (PubMed:7973730, PubMed:9032248). Interacts with HMS1, NCP1 and NPA3 (PubMed:15082539, PubMed:9032248). Interacts with DMA1 (PubMed:23264631).
G1/S-specific cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Essential for the control of the cell cycle at the G1/S (start) transition. The PCL1-PHO85 cyclin-CDK holoenzyme is involved in phosphorylation of the CDK inhibitor (CKI) SIC1, which is required for its ubiquitination and degradation, releasing repression of b-type cyclins and promoting exit from mitosis. Together with cyclin PCL2, positively controls degradation of sphingoid long chain base kinase LCB4. PCL1-PHO85 phosphorylates LCB4, which is required for its ubiquitination and degradation. PCL1-PHO85 also phosphorylates HMS1, NCP1 and NPA3, which may all have a role in mitotic exit.
Phosphorylated by PHO85; necessary for interaction with DMA1 and subsequent degradation.
Ubiquitinated by E3 ubiquitin ligase DMA1 in response to nutrient condition; this targets PCL1 for destruction.
Belongs to the Tim17/Tim22/Tim23 family.
Component of the TIM23 complex, at least composed of TIM23, TIM17, TIM50 and TIM21 (PubMed:15797382, PubMed:27265872). The complex interacts with the TIM44 component of the PAM complex (PubMed:15797382).
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Present with 1210 molecules/cell in log phase SD medium.
The disulfide bond is required for stabilization of the TIM23 complex.
Interacts with PAM16/TIM16 and is recruited by the PAM complex.
Plays a role in mitochondrial biogenesis and protein folding. Participates in the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner, probably by stimulating activity of mtHSP70 (SSC1).
Involved in amino acid efflux from the vacuole to the cytoplasm. Capable of transporting large neutral amino acids including tyrosine, glutamine, asparagine, isoleucine and leucine.
Mediator of diverse signals that repress RNA polymerase III transcription. Inhibits the de novo assembly of TFIIIB onto DNA.
Belongs to the archaeal Rpo12/eukaryotic RPC10 RNA polymerase subunit family.
Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes. Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA. Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits: RPO21, RPB2, RPB3, RPB4, RPB5, RPO26, RPB7, RPB8, RPB9, RPB10 and RPC10. Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. Interacts, via its C-terminus, with TFIIIC subunit TFC4.
DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively. RNA polymerases are composed of mobile elements that move relative to each other. In Pol II, the core element with the central large cleft comprises RPB3, RBP10, RPB11, RPB12 and regions of RPB1 and RPB2 forming the active center.
Loss of N(1)-methyladenine(2142) in 25S rRNA. Confers anisomycin and peroxide sensitivity to the cells as well as slight defects in ribosome subunit joining.
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of adenine 2142 in 25S rRNA. N(1)-methyladenine(2142) in 25S rRNA is present in helix 65, a region that accounts for most of the intersubunit surface of the large subunit.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.
Cyclin-dependent kinase that acts as a master regulator of the mitotic and meiotic cell cycles (By similarity). Required to drive the G1-S transition (PubMed:2664468). More than 200 substrates have been identified (PubMed:14574415). Substrate specificity is in part regulated by the bound cyclin protein (By similarity). Phosphorylates YTA7 during S-phase to promote transcription of histones (PubMed:22156209).
Forms a stable but non-covalent complex with the CKS1 protein and with a cyclin.
Phosphorylation at Thr-18 or Tyr-19 inactivates the enzyme, while phosphorylation at Thr-169 activates it.
Present with 6670 molecules/cell in log phase SD medium.
Catalyzes the covalent attachment of ubiquitin to other proteins. Capable, in vitro, to ubiquitinate histone H2A.
Interacts with CDC53. Component of the E3 ubiquitin ligase complexes SCF with CDC53, SKP1/CBF3D, HRT1 and some F-box proteins like MET30 and CDC4.
Mediates the initiation of DNA replication (transition of G1 to S phase in cell cycle). Essential component of the E3 ubiquitin ligase complex SCF (SKP1-CUL1-F-box protein), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Involved in the regulation of methionine biosynthesis genes and in the degradation of CDC6 together with CDC4 and CDC53.
Present with 8170 molecules/cell in log phase SD medium.
The acidic C-terminal extension is essential for the cell cycle function.
Belongs to the eukaryotic ribosomal protein eL39 family.
Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). eL39 interacts with YIH1 (PubMed:22404850).
Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9. Component of the ADA/GCN5 complex that consists of HFI1/ADA1, ADA2, ADA3, SPT20/ADA5 and GCN5 and is probably a subcomplex of SAGA. Component of the 0.8 MDa ADA complex, which at least consists of ADA2, ADA3, AHC1 and GCN5. ADA2 interacts with GCN5.
Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. ADA preferentially acetylates nucleosomal histones H3 (to form H3K14ac and H3K18ac) and H2B.
Involved in rRNA-processing at A0, A1 and A2 sites through its action in U18 and U24 snoRNA 3'-end final trimming. Negative regulator of telomerase through competition for binding to EST2 with TLC1.
Present with 3850 molecules/cell in log phase SD medium.
Belongs to the FIT family. Fungal FIT2B/SCS3 subfamily.
Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate. Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen (By similarity). This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis (PubMed:26504167, PubMed:29526591, PubMed:32915949) (By similarity). May directly bind to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis (By similarity). May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation (PubMed:29526591) (By similarity). May play a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Involved in phospholipid biosynthesis (PubMed:7706223, PubMed:29417057, PubMed:32915949) (By similarity).
Present with 9600 molecules/cell in log phase SD medium.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YLR035C-B ORF.
Present with 5480 molecules/cell in log phase SD medium.
RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase that dephosphorylates 'Ser-5' of the CTD and regulates RNA polymerase II during the transition from 'Ser-5' to 'Ser-2' phosphorylation.
ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (PubMed:24474793). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity).
The matrix-open state (m-state) is inhibited by the membrane-permeable bongkrekic acid (BKA) (PubMed:24474793). The cytoplasmic-open state (c-state) is inhibited by the membrane-impermeable toxic inhibitor carboxyatractyloside (CATR) (PubMed:24474793).
The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. At least 2 of the odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue.
Leads to high-affinity Ca(2+) influx system (HACS) deficiency (PubMed:21252230, PubMed:23204190). Causes a large increase of cell death in response to mating pheromone, when PRM6/KCH2 is also deleted (PubMed:23204190).
Low affinity potassium transporter that, with PRM6/KCH2, participates in high-affinity Ca(2+) influx system (HACS) activation during the response to mating pheromone (PubMed:21252230, PubMed:23204190). Directly promotes K(+) influx and HACS may electrochemically respond to this K(+) influx (PubMed:23204190). KCH1 and KCH2 act at the apex of the calcium signaling pathway that is used for survival during prolonged exposures to mating pheromones (PubMed:23204190).
In contrast to other aldo/keto reductase 2 proteins, it lacks the N-terminal half which contains the active site. It is therefore unlikely that it acts as a functional oxydoreductase.
Interacts with ODC/SPE1 and thereby sterically blocks ODC homodimerization.
Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis in response to increased intracellular polyamine levels (PubMed:15538383). Binds to ODC/SPE1 monomers, inhibiting the assembly of the functional ODC homodimer, and targets the monomers for ubiquitin-independent proteolytic destruction by the 26S proteasome (PubMed:18089576).
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
This is one of two catalases in S.cerevisiae; the other is catalase A, which is the peroxisomal form.
Interacts with snoRNA U3. Interacts with MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.
Primarily required at the G2/M phase. Essential for viability: involved in nucleolar processing of pre-18S ribosomal RNA as part of the ribosomal small subunit (SSU) processome.
When overexpressed, has a role in the structure of silenced chromatin. Overproduction causes derepression of gene expression at both HML and HMR, as well as at the rDNA locus and at telomeres.
Autoregulated. Induced upon growth on fatty acids.
The PIP2-OAF1 heterodimer acts as a transcriptional activator to induce the transcription of genes encoding proteins involved in fatty acid beta-oxidation, a response called oleic acid induction, when cells grow on fatty acids as sole carbon source. Recognizes and binds to the oleate response element (ORE) (or peroxisome box), two inverted CGG triplets spaced by 14 to 18 intervening nucleotides, in the promoter region of a number of genes (such as CTA1, FOX1 to FOX3, FAA2, PAS8, PAS10, etc.) for peroxisomal proteins. Activity is inhibited by OAF1 under non-inducing conditions. Activity is repressed by glucose.
the 9aaTAD motif (residues 985 to 993) is a transactivation domain present in a large number of yeast and animal transcription factors.
Membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. It plays a role in fatty-acid desaturation and is also involved in several steps of the sterol biosynthesis pathway, particularly in the 4-demethylation of the 4,4'-dimethyl zymosterol.
Present with 5390 molecules/cell in log phase SD medium.
May be involved in a process influencing telomere capping.
Diubiquitinated in a cell cycle-regulated manner. Ubiquitination first appears in late G(1) and persists throughout S phase.
Present with 1860 molecules/cell in log phase SD medium.
Required for DNA synthesis. Required for entry into or completion of S phase. Involved in DNA replication and seems to participate in the activation of the pre-replication complex (pre-RC) and in transcription elongation. May play a role as a key coordinator in assembling the replication fork. Proposed to function at replication origins following the binding of the MCM2-7 complex prior to the recruitment of CDC45. Probably is required to stimulate phosphorylation of the MCM2-7 complex by the CDC7-DBF4 kinase complex. May recruit the DNA polymerase alpha:primase complex to replication origins and is required to maintain it on chromatin independently of CDC45. May also play a role in transcriptional silencing.
Self-associates; assembles into large homomultimeric complexes of approximately 800 kDa. Associates with the MCM2-7 complex and the DNA polymerase alpha:primase complex. Interacts with ORC1, ORC2, MCM2, MCM3, CDC54/MCM4, MCM6, CDC47/MCM7, RFA2, CDC45, POL1, PRI2, POL12, SIR2 and SIR3. The diubiquitinated form interacts with POL30/PCNA C-terminus.
The zinc finger-like domain binds a zinc ion and is involved in self-association.
Component of the HRD1 ubiquitin ligase complex which contains the E3 ligase HRD1, its cofactors HRD3, USA1 and DER1, substrate recruiting factor YOS9 and CDC48-binding protein UBX2 (PubMed:16873065, PubMed:16873066, PubMed:16845381). Within the complex, interacts directly with HRD1 and YOS9 (via N-terminus) (PubMed:11018054, PubMed:22262864, PubMed:28682307). In ERAD-L, HRD3 and YOS9 jointly bind misfolded glycoproteins in the endoplasmic reticulum (ER) lumen (PubMed:32327568). Movement of ERAD-L substrates through the ER membrane is facilitated by HRD1 and DER1 which have lateral gates facing each other and which distort the membrane region between the lateral gates, making it much thinner than a normal phospholipid bilayer (PubMed:32327568). Substrates insert into the membrane as a hairpin loop with one strand interacting with DER1 and the other with HRD1 (PubMed:32327568). The HRD1 complex interacts with the heterotrimeric CDC48-NPL4-UFD1 ATPase complex which is recruited by UBX2 via its interaction with CDC48 and which moves ubiquitinated substrates to the cytosol for targeting to the proteasome (PubMed:16873066, PubMed:16619026). The HRD1 complex interacts with the ERAD substrates HMG1 and HMG2 (PubMed:11390656). Interacts with KAR2 (PubMed:16873065).
Component of the endoplasmic reticulum quality control (ERQC) system involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). ERAD-L substrates are ubiquitinated through HRD1 in conjunction with the E2 ubiquitin-conjugating enzymes UBC1 and UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via the action of the CDC48-NPL4-UFD1 ATPase complex and targeted to the proteasome. ERAD-M substrates are processed by the same HRD1-HRD3 core complex, but only a subset of the other components is required for ERAD-M. Stabilizes the HRD1 ubiquitin-protein ligase. Also functions in recruiting misfolded protein substrates in conjunction with YOS9.
Affects mitochondrial activities and leads to an increase in intermediate sterols and a corresponding decrease in zymosterol and ergosterol production.
Belongs to the sterol desaturase family.
C-4 methylsterol oxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:8552601, PubMed:12880870, PubMed:29773647). ERG25 is a catalytic component of the C-4 demethylation complex that catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols (PubMed:8552601, PubMed:12880870). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672).
Heterotetramer of ERG25, ERG26, ERG27 and ERG28. ERG28 acts as a scaffold to tether ERG27 and other 4,4-demethylation-related enzymes, forming a demethylation enzyme complex, in the endoplasmic reticulum. Interacts with ERG27 and ERG28.
Present with 77100 molecules/cell in log phase SD medium.
Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation. Required for targeting MDV1 to the mitochondria. Regulates the assembly of DNM1 into punctate structures, in the mitochondrial tubules, promoting mitochondrial membrane constriction and/or division.
Present with 2410 molecules/cell in log phase SD medium.
The C-terminus is required for mitochondrial localization, while the N-terminus is necessary for mitochondrial fission.
Interacts with the clathrin adapter GGA2, and VPS27.
Involved in the recruitment of clathrin to the Golgi network and endosomes to form clathrin coated vesicles. Plays a role in the trafficking of clathrin between the Golgi network and endosomes. Binds to membranes enriched in phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) and, in association with VPS27, is involved in protein sorting at the multivesicular body (MVB).
Involved in the mitochondrial expression of subunits 6 and 8 of the F0-F1 ATP synthase.
AMP deaminase plays a critical role in energy metabolism.
Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family.
Present with 3910 molecules/cell in log phase SD medium.
Interacts with CDC3, CDC10, CDC11, CDC12, EDE1 and EPS15.
Multi-functional protein that contributes to the endocytic process, but also to events that occur at the neck during budding and/or cytokinesis. Plays a role as an endocytic adapters with membrane-tubulation activity that associates with transmembrane cargo proteins and initiates the formation of endocytic sites. Contributes to the stabilization of the nascent clathrin-coated pit. Also plays a role in late endocytosis by mediating vesiculation. Involved in the regulation of cell cycle-dependent dynamics of the septin cytoskeleton by promoting septin turnover in different cell cycle stages. May act through the RHO2 signaling pathway to repolarize cortical actin patches in profilin-deficient cells.
Monomer. Interacts with the FAD-linked sulfhydryl oxidase ERV1 and with the substrate proteins COX17, TIM9, and TIM13, forming transient intermolecular disulfide bridges. Interacts with FCJ1.
Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Forms a redox cycle with ERV1 that involves a disulfide relay system. Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria. The oxidized form of MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS. Reduced MIA40 is reoxidized by FAD-linked sulfhydryl oxidase ERV1.
The CHCH domain contains a conserved twin Cys-X(9)-Cys motif which is required for import and stability of MIA40 in mitochondria.
Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which associates with catalytic subunits DIS3 and RRP6 in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits and peripheral S1 domain-containing components CSL4, RRP4 and RRP40 located on the top of the ring structure. Interacts with NIP7 and NOP8. Interacts strongly with RRP46.
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP43 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation.
O-glycosylated in the Ser/Thr-rich regions.
Plasma membrane signaling mucin that promotes activation of the MAPK for the filamentous growth pathway. Partially redundant with the SHO1 osmosensing branch for the activation of STE11.
Present with 1320 molecules/cell in log phase SD medium.
May function as a transcriptional activator. Increased dosage of MSN1 restores invertase expression in yeast mutants defective in the SNF1 protein kinase, and msn1 disruption reduced derepression of invertase in the wild-type. May affect SUC2 expression. Expression of MSN1 enhances growth in iron-limiting conditions.
Present with 491 molecules/cell in log phase SD medium.
Belongs to the WD repeat PROPPIN family.
Contains a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2).
Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage. Essential for maturation of proaminopeptidase I.
The L/FRRG motif is essential for the cytoplasm to vacuole transport (Cvt) pathway and for the recruitment of ATG8 and ATG16 to the PAS in nutrient-rich medium and in both its recruitment to and dissociation from the PAS under starvation conditions.
Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site. Also zinc has been proposed to be the physiological cofactor for yeast.
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Plays only a minor role in N-terminal methionine removal. Less efficient when the second residue is Val, Gly, Cys or Thr.
Irreversibly inhibited by the fungal metabolite fumagillin, an antiangiogenic drug. Subject to product inhibition by cytosolic methionine.
By proline and is regulated by a common control element encoded by the PUT3 gene.
Present with 17200 molecules/cell in log phase SD medium.
Belongs to the putative lipase ROG1 family.
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. Together with SPT15/TBP UAF seems to stimulate basal transcription to a fully activated level.
Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes.
Present with 524000 molecules/cell in log phase SD medium.
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Histone H4 is a component of the UAF (upstream activation factor) complex which consists of UAF30, RRN5, RRN9, RRN10, and histones H3 and H4.
Belongs to the zinc-containing alcohol dehydrogenase family.
Present with 11600 molecules/cell in log phase SD medium.
Interacts with NOP14 and MPP10. Interacts with snoRNA U3. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.
Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm. Its subcellular location and association with pre-40S subunit are unaffected by RPS19 disruptions, suggesting it acts before the ribosomal protein.
Although it belongs to the XPG/RAD2 endonuclease family, only two of the seven Asp residues involved in Mg(2+) binding are conserved suggesting that it has no nuclease activity.
Belongs to the XPG/RAD2 endonuclease family.
Interacts (via C-terminus) with PBP1 (via C-terminus).
Involved in 3'-UTR mediated RNA regulation (PubMed:15082763). Binds to RNA-binding and RNA regulatory proteins (PubMed:15082763). Complexes with PAB1-binding protein to promote mRNA interactions with poly(A)-binding protein (PubMed:15082763). Promotes mating-type switching in mother cells by positively regulating HO expression (PubMed:15082763).
Normal vegetative cell population growth rate and morphology (PubMed:15082763). Decreases expression from the HO locus (PubMed:15082763).
Present with 3430 molecules/cell in log phase SD medium.
Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (SSC1) via its interaction with PAM18/TIM14. May act by positioning PAM18/TIM14 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation.
Homodimer and heterodimer with PAM18. Homodimerization may not be relevant in vivo, while heterodimerization is essential for activity regulation of mtHSP70. Component of the PAM complex, at least composed of mtHsp70, MGE1, TIM44, PAM16, PAM17 and PAM18. Interacts with MDJ2.
The J-like region, although related to the J domain does not stimulate ATPase activity of mtHSP70. It nevertheless mediates the heterodimerization with the J domain of PAM18 and is therefore essential for PAM complex function.
Involved in gross chromosomal rearrangements (GCRs) and telomere healing.
General amino acid permease with broad substrate specificity. Can also transport carnitine.
Involved in a novel pathway of export of proteins that lack a cleavable signal sequence. May be part of the export machinery or may also be a substrate for non-classical export.
Required for cell viability in cells lacking mitochondrial DNA.
Belongs to the glycosyl hydrolase 76 family.
Required for normal synthesis of the cell wall.
Associates with nascent pre-60S particles that have not yet entered the translating pool, and is released from mature 60S subunits. Interacts with pre-60S factors ARX1 and RPL24. Interacts with JJJ1.
Pre-60S-associated factor involved in the cytoplasmic maturation of the 60S subunit. Involved in the dissociation and recycling of other late pre-60S factors like ARX1, TIF6 and ALB1 before newly synthesized large ribosomal subunits enter translation. Cooperates with the co-chaperone JJJ1 in the release of the nuclear-export factor ARX1. May act redundantly with REH1 to directly promote a stabilizing structural rearrangement in cytoplasmic 60S subunit maturation independent on ARX1 recycling.
Present with 830 molecules/cell in log phase SD medium.
Catalyzes the irreversible reduction of 2,3-butanediol to (S)-acetoin in the presence of NADH.
Expression is controlled by the PDR1 transcription factor and the glucose-responsive transcription factor RGT1.
Present with 3090 molecules/cell in log phase SD medium.
Ty1-DR6 is a highly expressed element. Induced under amino acid starvation conditions by GCN4.
Ty1-ER1 is a highly expressed element. Induced under amino acid starvation conditions by GCN4.
Ty1-LR2 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Ty1-PL is a highly expressed element. Induced under amino acid starvation conditions by GCN4.
Present with 6210 molecules/cell in log phase SD medium.
Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two-step reaction: L-tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) (PubMed:8509419, PubMed:3535890, PubMed:10588711, PubMed:10677221, PubMed:10766779). The specificity determinants on tRNA(Tyr) are the base pair C1-G72, the discriminator residue A73, and the three anticodon bases G34, U35 and A36 (PubMed:10677221). Also involved in nuclear tRNA export (PubMed:10588711). Also attaches D-Tyr to tRNA(Tyr), this reaction is about 150-fold less efficient than attachment of L-Tyr (PubMed:10766779).
Inhibited by N-ethylmaleimide and p-chloromercuribenzoate.
Present with 2710 molecules/cell in log phase SD medium.
Catalyzes the stereospecific dehydration of (2S,3S)-2-methylcitrate (2-MC) to yield the cis isomer of 2-methyl-aconitate.
Interacts with the large ribosome subunit of mitochondrial ribosome (PubMed:14657017, PubMed:22904327). Interacts directly with MRP20 (PubMed:14657017). Interacts with OXA1 (PubMed:25609543).
Leads to reduced steady-state levels and activities of the mitochondrial ATP/ADP carrier protein AAC2.
Mitochondrial inner membrane insertase that mediates the insertion of both mitochondrion-encoded precursors and nuclear-encoded proteins from the matrix into the inner membrane. Links mitoribosomes with the inner membrane (PubMed:22904327). Forms pores capable of accommodating translocating protein segments (PubMed:22829595). Essential for the activity and assembly of cytochrome c oxidase (PubMed:22904327). Plays a central role in the translocation and export of the N-terminal part of the COX2 protein into the mitochondrial intermembrane space.
Present with 6550 molecules/cell in log phase SD medium.
MRS3 suppresses a mitochondrial splice defect in the first intron of the COB gene. It may act as a carrier, exerting its suppressor activity via modulation of solute concentrations in the mitochondrion (possibly of cations).
Belongs to the ammonia transporter channel (TC 1.A.11.2) family.
Present with 3820 molecules/cell in log phase SD medium.
Transporter for ammonium (both charged and uncharged NH3 and NH4) to use as a nitrogen source. The affinity of MEP2 is about twenty times higher than that of MEP1. MEP3 has the lowest affinity.
Interacts with nucleoporin complex NUP84 and MTR2. Interacts with MIP6.
Involved in the export of mRNA from the nucleus to the cytoplasm.
Present with 2830 molecules/cell in log phase SD medium.
The NTF2 domain heterodimerizes with MTR2. The formation of this heterodimer is essential for mRNA export and binds to all of the nucleoporin-FG-repeats.
The RNA-binding domain is conserved in most NXF proteins but may be absent in yeasts.
The leucine-rich repeats and the NTF2-domain are essential for the export of mRNA from the nucleus.
Has a role in the DNA error-free postreplication repair (PRR) pathway. The UBC13/MMS2 heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'.
Transcription factor involved in the induction of hypoxic gene transcription when the cells are shifted from aerobiosis to anaerobiosis. Involved in sterol uptake.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YPL257W-A ORF.
Present with 6900 molecules/cell in log phase SD medium.
Belongs to the DHHC palmitoyltransferase family. PFA5 subfamily.
Able to suppress the functional loss of YPT1. SLY1 is essential for cell viability. May interact indirectly, or directly with YPT1.
Present with 5780 molecules/cell in log phase SD medium.
As part of the replication protein A (RPA/RP-A), a single-stranded DNA-binding heterotrimeric complex, may play an essential role in DNA replication, recombination and repair. Binds and stabilizes single-stranded DNA intermediates, preventing complementary DNA reannealing and recruiting different proteins involved in DNA metabolism. Binds to single-stranded sequences participating in DNA replication in addition to those mediating transcriptional repression (URS1) and activation (CAR1). Stimulates the activity of a cognate strand exchange protein (SEP1). It cooperates with T-AG and DNA topoisomerase I to unwind template DNA containing the simian virus 40 origin of DNA replication.
Belongs to the replication factor A protein 1 family.
Component of the heterotrimeric canonical replication protein A complex (RPA). Interacts with POB3.
Present with 4100 molecules/cell in log phase SD medium.
Required for replication of brome mosaic virus (BMV), a positive-strand RNA virus.
AMPK is a heterotrimer of an alpha catalytic subunit (SNF1), a beta (SIP1, SIP2 or GAL83) and a gamma non-catalytic subunits (SNF4). Note=Interaction between SNF1 and SNF4 is inhibited by high levels of glucose.
Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (SNF1) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.
Belongs to the 5'-AMP-activated protein kinase gamma subunit family.
Leads to a decrease in the length of G1 with respect to the wild-type strain along with a smaller difference in the cell cycle length of parent and daughter cells.
The 4 CBS domains mediate binding to nucleotides. Of the 4 potential nucleotide-binding sites, 2 are occupied, designated as sites 2 and 3 based on the CBS modules that provide the acidic residue for coordination with the 2'- and 3'-hydroxyl groups of the ribose of AMP. Site 3 can bind either AMP, ADP or ATP (AMP, ADP or ATP 2). Site 2 binds specifically ADP (ADP 1) and is likely to be responsible for protection of a conserved threonine in the activation loop of the alpha catalytic subunit through conformational changes induced by binding of ADP (PubMed:22019086).
Ubiquitin carboxyl-terminal hydrolase that recognizes ubiquitin chains that stabilize FZO1 and promote mitochondrial fusion. UBP12 deubiquitylates FZO1 only after oligomerization.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NUP145C is part of the heptameric 0.5 MDa autoassembling NUP84 NPC subcomplex (NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1). NUP145N may bind homomeric RNA and interacts through its FG repeats with karyopherins. Interacts with MLP1 and MLP2.
Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. FG repeat types and their physico-chemical environment change across the NPC from the nucleoplasmic to the cytoplasmic side: GLFG repeats are especially abundant in NUPs in the central region (lacking a charged environment but are enriched in Ser, Thr, Gln, and Asn).
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP145 is autocatalytically cleaved in vivo in 2 polypeptides which assume different functions in the NPC. NUP145N as one of the FG repeat nucleoporins participates in karyopherin interactions and contains part of the autocatalytic cleavage activity. NUP145C as part of the NUP84 complex is involved in nuclear poly(A)+ RNA and tRNA export. It is also required for normal NPC distribution (probably through interactions with MLP1 and MLP2) and NPC assembly, as well as for normal nuclear envelope organization.
NUP145 is autocatalytically cleaved in NUP145N and NUP145C.
Present with 4630 molecules/cell in log phase SD medium.
Binds 1 heme c group covalently per subunit.
By low oxygen levels (hypoxia) at the level of transcription. Not expressed until the oxygen concentration is below 0.5 uM O(2).
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of ubiquinol-cytochrome c oxidoreductase. Cytochrome c then transfers this electron to the dinuclear copper A center (CU(A)) of the COX2 subunit of cytochrome oxidase, the final protein carrier in the mitochondrial electron-transport chain. Isoform 2 (CYC7) is the predominant cytochrome c under anaerobic/hypoxic conditions.
Belongs to the sphingosine N-acyltransferase family.
Component of the ceramide synthase complex that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward hexacosanoyl-CoA (C26:0-CoA) (PubMed:12869556, PubMed:11694577). N-acylates sphinganine and phytosphingosine bases to form dihydroceramides and phytoceramides, respectively (PubMed:12869556). Redundant with LAC1. Facilitates ER-to-Golgi transport of GPI-anchored proteins. Involved in the aging process. Deletion of LAG1 results in a pronounced increase (approximately 50%) in mean and in maximum life span.
Homodimer (PubMed:12791253). Interacts with MPS3 (PubMed:18039933). Interacts with RIS1 (PubMed:9271422). Interacts with SIR1, SIR2 and SIR3 (PubMed:11722841). Interacts with YKU80 (PubMed:14551211). Interacts with UBP10 (PubMed:10490600, PubMed:26149687).
The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR (PubMed:18039933). The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure (PubMed:18039933). Involves the compaction of chromatin fiber into a more condensed form (PubMed:18039933).
Forms a complex with MON1. Interacts with YPT7.
In complex with MON1, is required for multiple vacuole delivery pathways including the cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and endocytosis. The CCZ1-MON1 complex acts at the fusion of vesicles with the vacuole, through its regulation of the SNARE complex during the coordinated priming and docking stages of fusion, and particularly at the stage of tethering/docking (PubMed:10407278, PubMed:11069774, PubMed:11590240, PubMed:12208507, PubMed:12364329, PubMed:14662743, PubMed:15184059, PubMed:15721293). The CCZ1-MON1 complex acts as a guanine nucleotide-exchange factor (GEF) for Rab-type GTPase YPT7, promoting nucleotide exchange on YPT7 and triggering endosomal maturation by activating YPT7 on late endosomes (PubMed:20797862).
Component of the oligosaccharyltransferase (OST) complex, which appears to exist in two assemblies comprising OST1, OST2, OST4, OST5, STT3, SWP1, WPB1, and either OST3 or OST6 (PubMed:10677492, PubMed:16297388, PubMed:16096345, PubMed:15886282, PubMed:9405463, PubMed:29301962). OST assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains OST1 and OST5, subcomplex 2 contains STT3, OST3, and OST4, and subcomplex 3 contains OST2, WBP1, and SWP1 (PubMed:29301962).
Present with 4030 molecules/cell in log phase SD medium.
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.
Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.
In TFIID, TAF12 heterodimerizes with TAF4, forming ultimately an octamer consisting of a TAF6/TAF9 heterotetramer core flanked by TAF4/TAF12 dimers on either side, similar to the histone H2A/H2B/H3/H4 octamer. The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14. Component of the 1.8 MDa SAGA complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9.
Present with 930 (+/-45) molecules/cell in log phase SD medium.
Low-affinity phosphate transporter involved in the control of cellular phosphate levels.
Present with 1010 molecules/cell in log phase SD medium.
Expressed at 6 of 8 hours of sporulation with maximal transcript accumulation occurring at 8 to 12 hours, a time at which the meiotic events if sporulation have been completed and the deposition of spore wall components is beginning.
Not essential for sporulation. Might be a component of the cell wall.
Associates with pre-60S ribosomes in the nucleoplasm (PubMed:11583615, PubMed:12374754, PubMed:15260980, PubMed:19737519). Interacts (via its hexameric AAA ATPase ring) with the RIX1 complex (via RIX1); this interaction is crucial for recruitment of MDN1 to the pre-ribosomal particle (PubMed:15260980, PubMed:26619264). Interacts (via VWFA/MIDAS domain) with YTM1 (via UBL domain) (PubMed:20542003). Interacts (via VWFA/MIDAS domain) with RSA4 (via UBL domain) (PubMed:19737519, PubMed:20542003).
Nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits. Functions at successive maturation steps to remove ribosomal factors at critical transition points, first driving the exit of early pre-60S particles from the nucleolus and then driving late pre-60S particles from the nucleus (PubMed:15260980, PubMed:15528184, PubMed:19737519, PubMed:20542003). At an early stage in 60S maturation, mediates the dissociation of the NOP7 complex (YTM1-ERB1-NOP7) from early pre-60S particles, rendering them competent for export from the nucleolus to the nucleoplasm (PubMed:20542003). Subsequently recruited to the nucleoplasmic particles through interaction with the RIX1 complex. This binding is only possible if the 5S RNP at the central protuberance has undergone the rotation to complete its maturation (PubMed:26619264). After remodeling, removes the ribosome biogenesis factor RSA4 in an ATP hydrolysis-driven step from pre-60S ribosomal subunits, rendering them competent for export from the nucleoplasm to the cytoplasm (PubMed:19737519, PubMed:20542003). Activates the GTPase activity of NOG2, which disengages from the pre-60S particle upon GTP hydrolysis, thus freeing its binding site for the nuclear export factor NMD3 (PubMed:24240281).
The protein has several distinct domains, an N-terminal extension (35 kDa), followed by an ATPase domain containing a hexameric ring of six tandem AAA protomers (between 28 and 40 kDa each), a linker domain (260 kDa), an Asp/Glu-rich domain (approximately 70 kDa) and a C-terminal VWFA domain (30 kDa) that possesses a MIDAS (metal ion-dependent adhesion site). The ring-like ATPase head domain associates with the RIX1 complex on the pre-ribosome, while the flexible tail protrudes from the molecule.
Component of the dynactin complex composed of at least ARP1, JNM1, NIP100 and ARP10. Dynactin comprises a short rod of ARP1 polymers attached to ARP10 at its pointed-end and probably associated with the capping protein at its barbed-end. The rod structure is implicated in dynein cargo binding. A sidearm formed by NIP100 projects from the ARP1 filament and is implicated in motor binding (By similarity). Interacts with ARP1.
Component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding (By similarity). The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. JNM1 is associated with the rod and links it to the projecting sidearm. Required for proper nuclear migration during the mitotic cell cycle and for astral microtubule development.
Putative transcription factor involved in the regulation of the activity of the cAMP/protein kinase A pathway. Involved in sterol uptake.
Component of the 20S proteasome chaperone. Forms a heterodimer with POC4 that binds to proteasome precursors. Interacts with POP2.
Involved in 20S proteasome assembly, facilitating the alpha-ring formation.
Present with 1820 molecules/cell in log phase SD medium.
Produced by +1 ribosomal frameshifting between codon Leu-431 and Gly-432 of the YLR410W-A ORF.
Component of the TRAMP (TRF4) complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates like cryptic transcripts generated by RNA polymerase II and III, or hypomethylated pre-tRNAi-Met. Both complexes polyadenylate RNA processing and degradation intermediates of snRNAs, snoRNAs and mRNAs that accumulate in strains lacking a functional exosome. AIR2 also inhibits the methylation of NPL3 mediated by HMT1 through its interaction with HMT1.
Component of the TRAMP complex (also called TRF4 complex) composed of at least HUL4, MTR4, PAP2/TRF4 and either AIR1 or AIR2. Interacts with HMT1 and NPL3. The interaction with NPL3 requires the presence of HMT1. Interacts directly with PAP2.
Acts as non-essential component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from SEC61 may govern the activity of the translocon. SEC72 may be involved in signal peptide recognition for a defined subset of leader peptides, or may increase the efficiency of unusual or 'difficult' secretory precursors to the translocation pore, it may be that this protein binds charged leader peptides to the membrane until they engage the translocation apparatus.
Component of the heterotetrameric Sec62/63complex composed of SEC62, SEC63, SEC71 and SEC72. The Sec62/63 complex associates with the Sec61 complex to form the Sec complex. May interact with protein YLR301W. Part of a complex consisting of KAR2, SEC63, SEC66 and SEC72.
Present with 5290 molecules/cell in log phase SD medium.
Probable transcription factor required for superficial pseudohyphal development in response to nitrogen starvation.
Inclusion body (IB) resident protein that interacts strongly with lipid droplet (LD) proteins. Involved in LD-mediated IB clearing after protein folding stress, probably by enabling access to the IBs of an LD-stored soluble sterol derivative that acts as chaperone in inclusion clearing.
Interacts with lipid droplet proteins PET10 and PDR16.
Present with 4980 molecules/cell in log phase SD medium.
Methyltransferase which mediates trimethylation of 'Lys-78' of cytochrome c (CYC1).
Present with 2940 molecules/cell in log phase SD medium.
The SET-like region, although related with the SET domain is not detected by any prediction method.
Catalytic component of the RPD3 histone deacetylase complexes RPD3C(L) and RPD3C(S) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events.
Component of the RPD3C(L) complex composed of at least ASH1, CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6. Component of the RPD3C(S) complex composed of at least EAF3, RCO1, RPD3, SIN3, and UME1. Interacts with RPD3.
The NEE-box motif is required for the association to RPD3.
Essential role in pre-mRNA splicing. Also essential for entry into mitosis (G2/M progression) as well as for chromosome segregation during mitosis.
Seems to play a role in cell morphogenesis.
Belongs to the bile acid:sodium symporter (BASS) (TC 2.A.28) family.
Expression is positively regulated by calcium/calcineurin signaling through the sole CDRE element (5'-TTAGCCTC-3') in its promoter.
Solute carrier protein that negatively regulates the cytosolic calcium homeostasis in response to high levels of extracellular calcium.
Has a role in the negative regulation of gluconeogenesis. Required for vacuolar catabolite degradation of fructose-1,6-bisphosphatase (FBPase).
Altered structural conformation of the ribosome in close proximity to cytosine 2278 (m5C2278) in 25S rRNA, leading to impaired translational fidelity, and promote recruitment of a distinct subset of oxidative stress-responsive mRNAs into polysomes.
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 2278 (m5C2278) in 25S rRNA (PubMed:23913415, PubMed:25125595, PubMed:25635753). Loss of m5C2278 in 25S rRNA results in anisomycin hypersensitivity (PubMed:23913415).
Component of ATP-dependent clamp loader (RFC and RFC-like) complexes for DNA clamps, such as the POL30/PCNA homotrimer and the checkpoint clamp DDC1:MEC3:RAD17 complex. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA. Component of the replication factor C (RFC or activator 1) complex which loads POL30/PCNA and acts during elongation of primed DNA templates by DNA polymerase delta and epsilon. RFC has an essential but redundant activity in sister chromatid cohesion establishment. Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. Component of the RFC-like RAD24-RFC complex which loads the checkpoint clamp DDC1:MEC3:RAD17 complex and is involved in DNA repair pathways. Component of the RFC-like ELG1-RFC complex which appears to have a role in DNA replication, replication fork re-start, recombination and repair.
Replication factor C (RFC) is a heteropentamer of subunits RFC1, RFC2, RFC3, RFC4 and RFC5 and forms a complex with POL30/PCNA in the presence of ATP. Component of the RAD24-RFC complex which consists of RAD14, RFC2, RFC3, RFC4 and RFC5 and associates with the checkpoint clamp DDC1:MEC3:RAD17 complex. Component of the ELG1-RFC complex which consists of ELG1, RFC2, RFC3, RFC4 and RFC5. Component of the CTF18-RFC complex, which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. RFC4 interacts with ECO1.
Has a stop codon at position 56, which shortens the ORF when compared to other seripauperin family members.
Cells have more than three vacuoles with a grape-like assembly.
Oligomer (PubMed:18442980). Interacts with YIP1 (PubMed:11278413).
Present with 1759 molecules/cell in log phase SD medium.
Required to generate and maintain the structure of the tubular endoplasmic reticulum network and the vacuole (PubMed:25646439, PubMed:32432369). Induces high curvature in membranes and causes membrane tubule formation (Probable). Involved in membrane/vesicle trafficking (PubMed:12427979).
The short lumenal loops between transmembrane domains 1 and 2 and between transmembrane domains 3 and 4 may impart a wedge-like configuration, thus deforming membranes.
Ty1-MR1 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Belongs to the eukaryotic ribosomal protein eS4 family.
Present with 102000 molecules/cell in log phase SD medium.
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP40 as peripheral part of the Exo-9 complex is thought to stabilize the hexameric ring of RNase PH-domain subunits.
Present with 6050 molecules/cell in log phase SD medium.
Associates with 90S and pre-40S pre-ribosomal particles. Interacts with CKA1, CKA2, CKB1, CKB2, PWP2, UTP15, UTP17 and UTP22.
Component of the 90S pre-ribosome involved in the maturation of rRNAs. Required for early cleavages of the pre-RNAs in the 40S ribosomal subunit maturation pathway.
Involved in invasion during filamentous growth.
Transcription factor involved in the regulation of gene expression upon nutrient starvation. Recognizes and binds to the post-diauxic-shift element 5'-T[AT]AGGGAT-3' in the promoter region. Can act as a transcriptional activator (e.g. of stress genes like SSA3, HSP12 and HSP26) as well as a repressor (e.g. of pyrophosphate phosphatase DPP1). GIS1 also acts as a DNA damage-responsive transcriptional repressor of photolyase PHR1.
Component of the ELG1-RFC complex which consists of ELG1, RFC2, RFC3, RFC4 and RFC5.
Involved in the negative control of telomere length and in telomeric silencing through a replication-mediated pathway. May have a role in Okazaki fragment maturation. Required for S-phase progression. Component of the RFC-like ELG1-RFC complex which appears to have a role in DNA replication, replication fork re-start, recombination and repair.
Accumulates in response to hyperosmostic conditions.
Component of the EKC/KEOPS complex composed of at least BUD32, CGI121, GON7, KAE1 and PCC1; the whole complex dimerizes.
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. GON7 likely plays a supporting role to the catalytic subunit KAE1 in the complex. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Present with 2180 molecules/cell in log phase SD medium.
Belongs to the homoserine dehydrogenase family.
Present with 48900 molecules/cell in log phase SD medium.
Probably catalytic subunit of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication. APC11 is required to recruit the ubiquitin-conjugating enzyme E2 to the APC/C.
Present with 1850 molecules/cell in log phase SD medium.
The CUE domain binds ubiquitin, which may facilitate intramolecular monoubiquitination.
Interacts with SLY1, STF1, SFB3 and GOS1.
Required for vesicular transport between the endoplasmic reticulum and the Golgi complex. Acts as a target organelle soluble NSF attachment protein receptor (t-SNARE).
Binds to the CRE motif 5'-TGACGTCA-3' and acts as a repressor of transcription of the SUC2 gene and most probably other genes.
Present with 8550 molecules/cell in log phase SD medium.
Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from the precursors of K1, K2 and K28 killer toxins and a-factor (mating pheromone). Involved in the programmed cell death caused by defective N-glycosylation and contributes also to the active cell death program induced by acetic acid stress or during chronological aging. Promotes cell fusion by proteolytically processing substrates that act in parallel to PRM1 as an alternative fusion machine, as cell wall components, or both.
Belongs to the Mediator complex subunit 14 family.
Non-catalytic component of the proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. This subunit has a chymotrypsin-like activity.
Present with 21800 molecules/cell in log phase SD medium.
Belongs to the NTC complex (or PRP19-associated complex), composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2, and PRP19. The NTC complex associates with the spliceosome after the release of the U1 and U4 snRNAs and forms the CWC spliceosome subcomplex (or CEF1-associated complex) reminiscent of a late-stage spliceosome composed also of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8, PRP9, PRP11, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNU114, SPP2, RSE1 and YJU2. Interacts with CEF1, ISY1, MUD2, NTC20, PRP22, PRP40, PRP46, SYF1, SYF2, and the ORC2 subunit of the origin recognition complex.
Involved in pre-mRNA splicing and cell cycle progression. Required for the spliceosome assembly by promoting the functional integration of the U4/U6.U5 tri-snRNP particle into the U1-, U2-dependent pre-spliceosome. Also recruits PRP19 to the spliceosome, as a component of the NTC complex (or PRP19-associated complex). The association of the NTC complex to the spliceosome mediates conformational rearrangement or stabilizes the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation. Required for initiation of the DNA replication by binding the RNA replication origins, probably through its interaction with the origin recognition complex (ORC).
Additional factor that functions in concert with eIF-2 and the initiator tRNA in directing the ribosome to the proper start site of translation.
The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a multifactor complex (MFC) that may bind to the 40S ribosome. Interacts with NIP1.
Belongs to the precorrin methyltransferase family.
Siroheme synthase involved in methionine biosynthesis.
Peptidyl-tRNA hydrolase involved in the recycling of tRNA-Lys from diacetyl-lysyl-tRNA-Lys and is important for mitochondrial function.
Expression is under the control of the RFX1 transcription factor.
In the C-terminal section; belongs to the phosphoglycerate mutase family.
Present with 3380 molecules/cell in log phase SD medium.
Synthesis and degradation of fructose 2,6-bisphosphate.
Present with 3460 molecules/cell in log phase SD medium.
Required for normal beta-1,6-glucan synthesis.
Plays a central role as a glucosyl donor in cellular metabolic pathways.
Interacts with the TFIID subunit TAF7 and with histone H4.
Transcription factor involved in the expression of a broad class of genes including snRNAs. Required for sporulation and DNA-damage repair. Prevents the spreading of SIR silencing at telomeres and protects histone H4, but not H3, from deacetylation (By similarity).
Has a calcium-dependent calmodulin-binding activity. Required for normal growth at various temperatures.
Increases a few-fold upon upshift to 37 degrees Celsius.
Present with 71700 molecules/cell in log phase SD medium.
Starvation of yeast cells may stimulate activity of IME1 through a post-translational mechanism.
Transcription factor required for sporulation and for early sporulation-specific genes expression. Positive regulator of SME1/IME2 expression. Directly activates expression of SLZ1 during meiosis.
Positive regulator of thiamine biosynthesis.
Acts as an E3 ligase mediating SUMO/Smt3 attachment to SMC5 and YKU70. Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks.
Component of the Smc5-Smc6 complex which consists of KRE29, NSE1, NSE2/MMS21, NSE3, NSE4, NSE5, SMC5 and SMC6.
Present with 2800 molecules/cell in log phase SD medium.
Belongs to the anthranilate phosphoribosyltransferase family.
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA), the second step in tryptophan biosynthesis.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. BimC subfamily.
Required for assembly of the mitotic spindle. Interacts with spindle microtubules to produce an outwardly directed force acting upon the poles. Following spindle assembly, CIN8 and KIP1 apparently act to oppose a force that draws separated poles back together. This force seems to be mediated by KAR3.
Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, RAN-dependent mechanism. Required for nuclear import of Ho endonuclease and RFP1, and involved in rRNA-processing and assembly or export of 60S ribosomal subunits.
Interacts with GTP-bound GSP1 and RFP1. Associates with the nuclear pore complex.
Present with 6300 molecules/cell in log phase SD medium.
Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of STP22, VPS28, SRN2 and MVB12 in a 1:1:1:1 stoichiometry. Interacts with STP22 and SRN2.
Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Appears to be involved in cargo sorting and release of the ESCRT-I complex from the MVBs.
Belongs to the PpiC/parvulin rotamase family.
Essential PPIase specific for phosphoserine and phosphothreonine N-terminal to the proline residue. Required for efficient pre-mRNA 3'-end processing and transcription termination, probably by inducing conformational changes by proline-directed isomerization in the C-terminal domain (CTD) of RPB1, thereby altering cofactor binding with the RNA polymerase II transcription complex. Also targets the SIN3-RPD3 histone deacetylase complex (HDAC).
Inhibited by 5-hydroxy-1,4-naphthoquinone (juglone), but not by FK506 or cyclosporin A.
Interacts with the RNA polymerase II largest subunit (RPB1) and with the SIN1-RDP3 HDAC subunit SIN3.
Present with 4401 molecules/cell in log phase SD medium.
The WW domain binds to the phosphorylated tandem 7 residues repeats of RPB1.
Belongs to the tubulin--tyrosine ligase family.
Present with 1770 molecules/cell in log phase SD medium.
Probable P-body-associated tubulin--tyrosine ligase.
Although related to histidine acid phosphatase proteins, it lacks the conserved active sites, suggesting that it has no phosphatase activity.
Belongs to the histidine acid phosphatase family. VIP1 subfamily.
Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4 (PubMed:17412958). Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4 (By similarity). Required for maintaining cellular integrity, normal growth and interactions with the ARP complex (PubMed:10388810). Acts as a regulator of the PHO80-PHO85 cyclin/cyclin-dependent kinase (CDK) complex, thereby regulating signaling of phosphate availability (PubMed:17412959). Required for the function of the cortical actin cytoskeleton, possibly by participating in correct F-actin localization and ensuring polarized growth (PubMed:10388810). Regulates polarized growth and modulates interphase microtubule cytoskeleton. Regulates microtubule dynamics without the requirement of microtubule plus-end tracking protein Mal3. Required for growth zone selection (By similarity).
Present with 8810 molecules/cell in log phase SD medium.
The N-terminal kinase domain produces inositol polyphosphates. The C-terminal acid phosphatase-like domain binds inositol polyphosphates and negatively regulates their accumulation. The C-terminal domain reduces the amount of inositol pyrophosphates in a dose-dependent manner in vitro.
Interacts with snoRNA U3. Interacts with MPP10 and UTP25. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3. In the absence of snoRNA3, forms a complex with other t-UTPs. This complex can associate with pre-18S ribosomal RNAs.
Involved in nucleolar processing of pre-18S ribosomal RNA. Also has a role in nuclear tRNA export. It acts between the steps of tRNA maturation/aminoacylation and its subsequent translocation out of the nucleus. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I together with a subset of U3 proteins required for transcription (t-UTPs).
Present with 16800 molecules/cell in log phase SD medium.
Forms a ternary complex with DMC1 and SAE3.
Involved in meiotic DNA-break repair. Required for the recruitment of DCM1 to meiosis recombination hot spots.
Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
Catalyzes the synthesis of phosphatidylinositol (PtdIns).
Divalent metal cations; Mn(2+) or Mg(2+).
Myo-inositol-containing phospholipids are of crucial importance in the control of cellular functions.
Present with 3810 molecules/cell in log phase SD medium.
Component of the CFIA complex, which is composed of RNA14, RNA15, PCF11 and CLP1. Interacts with FIP1, PFS2, YSH1 and probably also with RNA15. Probably interacts with the phosphorylated CTD domain of RPB1/RNA polymerase II.
Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex.
Present with 4010 molecules/cell in log phase SD medium.
Associates with the SIT4 protein phosphatase catalytic subunit in a cell-cycle-dependent manner.
Hyperphosphorylated in the absence of SIT4.
Positive regulator of protein phosphatase SIT4. Involved in directing expression of TOR-repressed genes and in dephosphorylation of NPR1 in response to nutrient starvation. Negatively modulates K(+) efflux of the cell by the Na(+)-K(+)/H(+) antiporter NHA1.
Stationary phase-essential protein not required for growth on nonfermentable carbon sources.
Autophagy-specific protein that functions with ATG13, ATG29, and CIS1/ATG31 in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles, through interacting with and regulating ATG1 kinase activity. Plays particularly a role in pexophagy and nucleophagy. With ATG13, is required for ATG1 activation by autophosphorylation of 'Thr-226'. Recruits ATG9 to the pre-autophagosomal structure. Also plays a role in regulation of filamentous growth.
Forms a complex with ATG13, ATG29 and CIS1/ATG31. The ATG17-ATG29-ATG31 complex interacts with the ATG1-ATG13 complex. Forms a complex with SNX4 and ATG20. Interacts with ATG11 and the conserved oligomeric Golgi (COG) complex subunits COG1, COG3 and COG4.
Belongs to the copper transporter (Ctr) (TC 1.A.56) family. SLC31A subfamily.
Provides bioavailable copper via mobilization of vacuolar copper stores and export to the cytoplasm.
Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.
Component of the COMPASS (Set1C) complex which consists of SET1(2), BRE2(2), SPP1(2), SDC1(1), SHG1(1), SWD1(1), SWD2(1), and SWD3(1). Interacts with MEC3.
Belongs to the eukaryotic ribosomal protein eS10 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). eS10 plays a role as a positive regulator of the GCN2 kinase activity by stimulating GCN1-mediated GCN2 activation (PubMed:25437641).
Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). eS10 interacts with GCN1 (via middle region); this interaction is direct and promotes GCN2 kinase activity (PubMed:25437641).
Present with 54100 molecules/cell in log phase SD medium.
Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the MCD1/SCC1 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by securin/PDS1 protein. It also promotes anaphase spindle elongation. A component of the FEAR (CDC14 early anaphase release) network which promotes CDC14 release from the nucleolus during early anaphase. Cleaves SLK19.
It is inactivated via its interaction with PDS1, which probably covers its active site. PDS1 degradation at anaphase, liberates it and triggers MCD1 cleavage.
May bind calcium. Interacts with PDS1. Interacts with MCD1.
Belongs to the DASH complex DAD1 family.
Present with 7500 molecules/cell in log phase SD medium.
Autoacetylates in an intermolecular reaction.
Belongs to the acetyltransferase family. GNAT subfamily.
N-acetyltransferase that acetylates histone H4 at 'Lys-8'. Also acetylates polyamines like putrescine, spermidine and spermine (PubMed:23775086). Acts on a wide range of D-amino acids. Catalyzes the N-acetylation through an ordered bi-bi mechanism, in which acetyl-CoA is the first substrate to be bound and CoA is the last product to be liberated (PubMed:15375647). D-amino acids are toxic for the cell and their N-acetylation, preceding removal from cells, plays an important role in detoxification of D-amino acids (PubMed:10600387, PubMed:16362288).
Active as '1-Cys' thiol transferase against beta-hydroxyethyl disulfide (HED), as dehydroascorbate reductase and as dimethylarsinic acid reductase, while not active against the standard GST substrate 1-chloro-2,4-dinitrobenzene (CDNB).
Belongs to the GST superfamily. Omega family.
Up-regulated by tert-butyl hydroperoxide (t-BOOH) in an MSN2/4-dependent manner.
Belongs to the DNA polymerase type-A family.
Involved in the replication of mitochondrial DNA.
ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK. It recognizes H3K4me. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. Acts in opposition to the FACT complex in regulating polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the pol I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome.
Belongs to the SNF2/RAD54 helicase family.
Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9. Interacts with RTF1, SPT5 and with the FACT subunits POB3 and SPT16.
The 2 chromodomains are involved in the binding to the histone H3 methyllysine at position 4 (H3K4me3).
The CHD1 helical C-terminal domain (CHCT) binds DNA and nucleosomes.
Required for pre-rRNA processing and 40S ribosomal subunit assembly. Seems to act in the processing of 35S rRNA at the A(0), A(1), and A(2) cleavage sites.
Belongs to the mitochondrion-specific ribosomal protein mS41 family.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (PubMed:25609543, PubMed:28154081). mS41 is involved in telomere length regulation and required for survival upon exposure to K1 killer toxin (PubMed:12663529, PubMed:16552446).
Participates in the control of the reentry into the cell cycle following pheromone treatment. Involved in vacuolar protein sorting.
Heterodimers with NPA3/GPN1 or GPN3 (PubMed:21844196, PubMed:23324351). Binds to RNA polymerase II (RNAPII) (By similarity).
Present with 9230 molecules/cell in log phase SD medium.
Small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import (PubMed:23267056). Required for establishment of sister chromatid cohesion (PubMed:18439903).
Belongs to the mitochondrion-specific ribosomal protein mS23 family.
Belongs to the 2-oxoacid dehydrogenase family.
Present with 7970 molecules/cell in log phase SD medium.
The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
Transcriptionally regulated by glucose and activated by the HAP2 and HAP3 proteins.
Interacts with COX18. This interaction may be essential for its insertion into mitochondrial inner membrane.
Probably involved in mitochondrial export. Confers resistance to the anti-pneumocystis carinii drug pentamidine. May act by the removal of pentamidine, or its damage targets, from the matrix by an active-transport mechanism.
Putative tyrosine-protein phosphatase required for protection against superoxide stress. Involved in cell-cycle delay in response to linoleic acid hydroperoxide (LoaOOH).
Present with 8530 molecules/cell in log phase SD medium.
The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. This unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib.
The side chain of Thr-76 acts as nucleophile, and the N-terminal amino group acts as proton acceptor.
This subunit is necessary for chymotryptic activity and degradation of ubiquitinated proteins.
Present with 80 molecules/cell in log phase SD medium.
The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. CDC23 interacts directly with SWM1 and binds the destruction box (D-box) of the substrate cyclin CLB2.
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer (Probable). Required for septum formation (Probable).
Present with 1130 molecules/cell in log phase SD medium.
Belongs to the cyclin family. Cyclin C subfamily.
CCL1 and KIN28 form the TFIIK complex, a component of TFIIH holo complex. Component of a complex consisting of KIN28, CCL1 and TFB3.
Present with 8700 molecules/cell in log phase SD medium.
Regulatory component of the TFIIK complex (KIN28-CCL1 dimer) which is the protein kinase component of transcription factor IIH (TFIIH) and phosphorylates the C-terminal domain of RNA polymerase II during transition from transcription to elongation after preinitiation complex (PIC) formation, thereby positively regulating transcription. TFIIH (or factor B) is essential for both basal and activated transcription, and is involved in nucleotide excision repair (NER) of damaged DNA. TFIIH has DNA-dependent ATPase activity and is essential for polymerase II transcription in vitro.
Present with 3120 molecules/cell in log phase SD medium.
Divalent metal cations. Prefers magnesium or manganese.
Present with 10500 molecules/cell in log phase SD medium.
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
Transcribed during late G1 and S-phase, repressed in G2.
Allosterically activated by its substrate, pyruvate.
Fusel oils and acyloins are important flavor and aroma compounds in yeast-fermented products contributing to the quality of beverages and food, e.g. fusel oils in whiskey, contrary to common believe, seem to alleviate hangover. In general they are desirable at low concentrations, whereas high concentrations may spoil the product. By adjusting growth conditions and substrate their production is sought to be influenced. Due to their broad substrate tolerance pyruvate decarboxylases are important biocatalysts for chemoenzymatic syntheses, both by fermentation and in vitro, e.g. in the production of ephedrine, vitamin E, or phenylethanol (rose flavor).
Present with 471316 molecules/cell in log phase SD medium.
Protein expression is strongly induced by high concentrations of fermentable carbon sources, under anaerobic growth conditions, and by thiamine limitation, but is repressed by the presence of PDC1 (independent of its catalytic activity) and thiamine.
Second most abundant of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-keto-acids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids derived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate), valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate), isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins.
Belongs to the peptidase C2 family. PalB/RIM13 subfamily.
Interacts with SNF7, which may act together with RIM20 as a scaffold to recruit RIM13 to its substrate RIM101.
Required for the proteolytic cleavage of the transcriptional repressor RIM101 in response to alkaline ambient pH, which is necessary for sporulation and invasive growth. Probably the protease that cleaves RIM101.
Decreases the levels of monounsaturated PC species and increased those of diunsaturated PC species. Does not significantly affect phosphatidylethanolamine, phosphatidylinositol, and phosphatidylserine profiles.
Glycerophosphocholine acyltransferase (GPCAT) that utilizes acyl-CoA to acylate glycero-3-phosphocholine (GPC), forming lysophosphatidylcholine (LPC) (PubMed:18430972, PubMed:27758859). Shows broad acyl specificities with a preference for 16:0-CoA, polyunsaturated acyl-CoA, and the hydroxylated ricinoleoyl-CoA (PubMed:18430972, PubMed:27758859). Catalyzes also the acylation of glycero-3-phosphoethanolamine (GPE) with acyl-CoA (PubMed:27758859). In addition to acyl-CoA, GPCAT efficiently utilizes LPC and lysophosphatidylethanolamine (LPE) as acyl donors in the acylation of GPC (PubMed:27758859). Contributes to the maintenance of phosphatidylcholine (PC) homeostasis and might also have specific functions in acyl editing of PC, such as transferring acyl groups modified at the sn-2 position of PC to the sn-1 (PubMed:27758859). Involved in postsynthetic PC remodeling that produces more saturated PC species (PubMed:30514764).
The GPCAT activity is sensitive to N-ethylmaleimide, phenanthroline, and divalent cations including Ca(2+), Mg(2+), Mn(2+) and Zn(2+) (PubMed:18430972). The activity is also inhibited by glycerol-3-phosphate (G3P) (PubMed:27758859).
Aspartyl aminopeptidase that contributes to peptide degradation both in the cytosol and the vacuole. Cells may respond to environmental conditions by changing the distributions of the cytosolic enzyme to the vacuole when cells need more active vacuolar degradation.
Tetrahedron-shaped homododecamer built from six homodimers.
The metalloproteases inhibitors EDTA and 1.10-phenanthroline both inhibit the activity, whereas bestatin, an inhibitor of most aminopeptidases, does not affect enzyme activity.
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). Also a component of the nuclear pore complex where it may contribute to the stable association of the Nup82 subcomplex with the NPC (PubMed:17546040, PubMed:23223634, PubMed:25646085).
Belongs to the dynein light chain family.
Homodimer (PubMed:17546040, PubMed:23223634, PubMed:25646085). Cytoplasmic dynein consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits which present intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs). Component of the nuclear pore complex (NPC) (PubMed:17546040). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof (PubMed:17546040). Part of the NUP82 subcomplex (PubMed:17546040, PubMed:25646085, PubMed:23223634). In the complex, interacts directly with Nup159 (PubMed:17546040, PubMed:25646085, PubMed:23223634).
Belongs to the GTP cyclohydrolase I family.
GTP cyclohydrolase 1 is the first enzyme in the biosynthetic pathway leading to folic acid.
Leads to folinic acid auxotrophy, and lacks any detectable specific enzymatic activity.
Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
In strain S288c and many other laboratory strains, a natural frameshift in position 294 results in a shortened C-terminus when compared to wild-type alleles. It is however not the different C-terminus, but rather 2 polymorphisms at positions 121 and 255 that lead to loss of water transport activity.
Water channel required to facilitate the transport of water across membranes. Involved in sporulation, freeze tolerance and osmotolerance (By similarity). Is non-functional in most laboratory strains.
Promotes the exchange of CDC42-bound GDP by GTP. Controls the polarity of calmodulin, and the calcium regulatory process of bud emergence. CDC24 may be involved in the initial selection and organization of the budding site.
Maybe involved in N-terminal acetylation of proteins. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover.
Belongs to the eukaryotic AdoMetDC family.
Binds 1 pyruvoyl group covalently per subunit.
Catalyzes the decarboxylation of S-adenosylmethionine, a key step in the biosynthetic pathway for spermidine and spermine. It is essential for normal growth, sporulation, and maintenance of ds-RNA virus.
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Present with 7060 molecules/cell in log phase SD medium.
The RIC1-RGP1 complex acts as a guanine nucleotide exchange factor (GEF), which activates YPT6 by exchanging bound GDP for free GTP. It is thereby required for efficient fusion of endosome-derived vesicles with the Golgi. The RIC1-RGP1 participates in the recycling of SNC1, presumably by mediating fusion of endosomal vesicles with the Golgi compartment.
Has a role in telomere length regulation and telomere end protection. Acts as an inhibitor of telomerase loading through its interaction with CDC13.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) (By similarity).
Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Homodimer. The tRNA molecule binds across the dimer (By similarity).
Present with 405 molecules/cell in log phase SD medium.
Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
Cooperates with the reticulon proteins RTN1 and RTN2 and the tubule-shaping DP1 family protein YOP1 to generate and maintain the structure of the tubular endoplasmic reticulum network. Has GTPase activity, which is required for its function in ER organization.
Interacts with RTN1 and YOP1; GTP binding is not required for these interactions.
Present with 2265 molecules/cell in log phase SD medium.
Activity is decreased by glutathione and ammonium ion.
Belongs to the gamma-glutamyltransferase family.
Catalyzes the transfer of the gamma-glutamyl moiety of glutathione (GSH) and other gamma-glutamyl compounds to amino acids and peptides. Major GSH-degrading enzyme, catalyzing the hydrolytic release of L-glutamate from GSH. Plays a role in the turnover of the vacuolar GSH, serving as an alternative nitrogen source during nitrogen starvation.
Cleaved by autocatalysis into a large and a small subunit.
Heterodimer composed of a light and a heavy chain. The active site is located in the light chain.
Induced upon nitrogen starvation. Repressed by ammonium ions. 6-diazo-5-oxo-L-norleucine and L-azaserine are irreversible inhibitors whereas serine-borate is a reversible inhibitor.
Interacts with the AAA ATPase VPS4; regulates OSH7 membrane association. VPS4 is required for membrane dissociation of OSH7.
ipid transport protein (LTP) involved in non-vesicular transfer of lipids between membranes. Functions in phosphoinositide-coupled directional transport of various lipids by carrying the lipid molecule in a hydrophobic pocket and transferring it between membranes through the cytosol. Involved in maintenance of intracellular sterol distribution and homeostasis (PubMed:15173322). Involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane. Specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the PM in exchange for PI4P, which is delivered to the ER-localized PI4P phosphatase SAC1 for degradation. Thus, by maintaining a PI4P gradient at the ER/PM interface, SAC1 drives PS transport (PubMed:23934110, PubMed:26206936). Binds phosphatidylserine and PI4P in a mutually exclusive manner (PubMed:26206936).
Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with BRR2, ECM2, PRP18 and PRP22.
Essential protein involved in the second catalytic step of pre-mRNA splicing. Involved in the selection of 3'-type splice sites; this selection could be done via a 3'-splice site-binding factor, PRP16.
Present with 1490 molecules/cell in log phase SD medium.
The CCHC-type zinc finger probably plays a role in the ability of SLU7 to bypass the requirement for PRP18.
Present with 2380 molecules/cell in log phase SD medium.
Required for pre-mRNA splicing and maintenance of stable U6 small nuclear RNA levels. Implicated in the formation of stable and biologically active snRNP structures. As part of the U4/U6.U5 tri-snRNP particle, dispensible for spliceosome assembly, but required for conformational changes, which result in U4 snRNA release and the subsequent catalytic activation of the spliceosome.
Is not essential for haploid growth, but may affect diploid formation.
Expression is dependent upon the presence of the cell wall integrity pathway mitogen-activated protein kinase SLT2 and its downstream transcription factor RLM1.
Hypersensitive to cell wall-perturbing agent calcofluor white (CFW) at 37 degrees Celsius. A similar phenotype is observed at 30 degrees Celsius, although the severity is decreased. Decreased expression of genes contributing to cell wall organization during vegetative growth.
Belongs to the universal ribosomal protein uL5 family.
Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). uL5 forms a heterotrimeric complex with uL18/RPL5 and SYO1. Interaction of this complex with KAP104 allows the nuclear import of the heterotrimer (PubMed:23118189).
Present with 39000 molecules/cell in log phase SD medium.
Calcineurin-dependent protein required for growth under high NaCl, alkaline pH and cell wall stress.
Interacts with the 2 calcineurin A subunits CNA1 and CMP2, and with HPH2/FRT2.
Phosphorylated. Is dephosphorylated by calcineurin.
Present with 251 molecules/cell in log phase SD medium.
Required for proper cell morphogenesis and cell separation after mitosis. Functions in the RAM (regulation of ACE2 activity and cellular morphogenesis) signaling network and is required for proper ACE2 localization and CBK1 kinase activity.
Activator protein that regulates the ubiquitin ligase activity and substrate specificity of the anaphase promoting complex/cyclosome (APC/C). At the metaphase-to-anaphase transition, recognizes and binds proteins containing a D-box including the B-type cyclins CLB2 and CLB5, HSL1 and securin PDS1, and recruits them in a C-box-dependent manner to the APC/C for ubiquitination and subsequent proteolysis. Required for sister chromatid separation and disassembly of the mitotic spindle. Target of the spindle checkpoint pathway through participation in the mitotic checkpoint complex (MCC) and the MAD2-CDC20 subcomplex. MCC and presumably the MAD2-CDC20 subcomplex inhibit the ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) by preventing its activation by CDC20 until proper attachment of all chromosomes to the spindle.
Belongs to the WD repeat CDC20/Fizzy family.
Component of the mitotic checkpoint complex (MCC) which consists of MAD2, MAD3, BUB3 and CDC20, and of the MAD2-CDC20 subcomplex, both of which appear to be assembled during mitoisis independently of the kinetochore. In mitose-arrested cells, MAD2-CDC20 occurs in a larger amount than MCC. MCC associates with the with the APC/C complex. Interacts with MAD2, MAD3, BUB3, HSL1 and PDS1.
Expressed in late S and M phase of the cell cycle. Degraded in G1 by the APC/C in its CDH1-bound form.
The C-box is required for the association with the APC/C complex.
The KEN box is required for the association with the APC/C complex.
The N-terminal destruction box (D-box) acts as a recognition signal for degradation via the ubiquitin-proteasome pathway.
Produced by +1 ribosomal frameshifting between codon Leu-362 and Gly-363 of the YHL009W-A ORF.
Proteolytically processed into capsid protein (CA), Ty4 protease (PR), integrase (IN) and reverse transcriptase/ribonuclease H (RT) proteins (Probable). Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein, and this cleavage is a prerequisite for subsequent processing at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity).
Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1. Interacts with the pre-mRNA-splicing helicase BRR2 and the ubiquitin-like modifier HUB1.
Component of the U4/U6.U5 tri-snRNP particle, one of the building blocks of the spliceosome. Required for pre-mRNA splicing.
Transcription factor involved in the regulation of multidrug resistance genes. Acts in concert with YRR1.
Belongs to the heat shock protein 90 family.
Expressed constitutively and induced by high temperatures dependent on transcription factor HSF1. According to PubMed:2674684, it is constitutively expressed at low levels, however, due to the specificity of the antibody, this result is unsure.
Homodimer. Interacts with the co-chaperones AHA1, CDC37, CNS1, CPR6, CPR7, HCH1, SBA1, SSE1 and STI1. CNS1, CPR6, CPR7 and STI1. Interacts directly with the substrates GCN2, HAP1 and STE11.
Inhibited by geldanamycin, macbecin I and radicicol, which bind to the ATP-binding pocket. Co-chaperones CDC37, SBA1 and STI1 reduce ATPase activity. Co-chaperones AHA1 and HCH1 increase ATPase activity.
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.
Present with 444943 molecules/cell in log phase SD medium.
The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperones AHA1, CDC37, CNS1, CPR6, CPR7, HCH1, SBA1, SSE1 and STI1. CNS1, CPR6, CPR7 and STI1.
Beta subunit of the SNF1 kinase complex, which is required for transcriptional, metabolic, and developmental adaptations in response to glucose limitation. Has a structural role, mediating heterotrimer formation, and a regulatory role, defining carbon source-regulated subcellular location and substrate specificity of the SNF1 kinase complex. Involved in the regulation of aging. Acts as a negative regulator of nuclear SNF1 activity in young cells by sequestering its activating gamma subunit at the plasma membrane.
Component of the SNF1 kinase complex, a heterotrimeric complex composed of the catalytic alpha subunit SNF1, one of the three related beta subunits SIP1, SIP2 or GAL83, and the regulatory gamma subunit SNF4. The beta subunit serves as a bridge between the catalytic and the regulatory subunit. Interacts (via KIS domain) with SNF1. Interacts (via ASC domain) with SNF4.
Induced upon shift to nonfermentable carbon sources.
Required for expression of the mitochondrial gene for cytochrome c oxidase subunit 3 (COX3). PET122 seems to work by directly interacting with the small ribosomal subunit to promote translation initiation on the COX3 mRNA.
Belongs to the DNA/RNA non-specific endonuclease family.
The active site contains 1 hydrated divalent metal cation that has only 1 direct interaction with the protein; all other interactions are via water molecules.
This enzyme has both RNase and DNase activity.
Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).
Dual specificity mitochondrial citrate and methylcitrate synthase with similar catalytic efficiency with both acetyl-CoA and propionyl-CoA.
Leads to an accumulation of acetate and of isobutanol.
Nucleotidase with XMP as the best in vitro substrate. Low catalytic efficiencies of YKL033W-A observed with XMP and other substrates suggest that these could be secondary activities for this protein, and its primary substrate is not yet identified. May possess pseudouridine 5'-phosphatase activity and together with dTTP/UTP pyrophosphatase YOR111W might constitute a pathway for the detoxification of pseudouridine 5'-triphosphate (Psi-UTP) and -monophosphate (Psi-UMP).
Belongs to the 2H phosphoesterase superfamily. CPD1 family.
Involved in the metabolism of ADP-ribose 1',2'-cyclic phosphate which is produced as a consequence of tRNA splicing.
Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins, such as mitochondrial carrier family members, into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps. Mediates the insertion of precursor proteins in a 3 step process. After the precursor is tethered to the translocase without losing energy from the Delta(psi), 2 energy-requiring steps are needed. First, Delta(psi) acts on the precursor protein and promotes its docking in the translocase complex. Then, Delta(psi) and an internal signal peptide together induce rapid gating transitions in one pore and closing of the other pore and drive membrane insertion to completion.
Transport of citrate across inner mitochondrial membrane.
Deletion produces no detectable phenotype.
E3 ubiquitin-protein ligase which probably functions outside the N-end rule pathway, since it lacks the residues essential for the degradation of N-end rule substrates. Mediates RPN4 ubiquitination and subsequent degradation.
The RING-H2 zinc finger is an atypical RING finger with a His ligand in place of the fourth Cys of the classical motif.
4'-phosphopantetheine is transferred from CoA to a specific serine of the Acyl carrier domain by the C-terminal PPT domain. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Belongs to the thiolase-like superfamily. Fungal fatty acid synthetase subunit alpha family.
Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.
Inhibited by cerulenin by covalent binding to active site of the ketoacyl synthase (KS) region.
[Alpha(6)beta(6)] hexamers of two multifunctional subunits (alpha and beta).
Present with 17100 molecules/cell in log phase SD medium.
Component of the checkpoint clamp complex composed of DDC1, MEC3 and RAD17. The interaction with MEC3 is performed in a RAD17-dependent manner. The checkpoint clamp complex loads onto DNA in an ATP-dependent manner through its interaction with the RFC-RAD4 checkpoint clamp loader complex. Interacts with the DNA polymerase zeta subunit REV7 and DPB11.
Component of the checkpoint clamp complex involved in the surveillance mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. Associates with sites of DNA damage and modulates the MEC1 signaling pathway and the activation of RAD53 in response to DNA damage at phase G1. The complex also physically regulates DNA polymerase zeta-dependent mutagenesis by controlling the access of polymerase zeta to damaged DNA.
Phosphorylated during cell cycle S-phase and in response to DNA damage. This phosphorylation is MEC14 dependent. Also hosphorylated by CDC28.
Involved in the unfolded protein response (UPR), a transcriptional response which up-regulates genes that enable cells to cope with misfolded, endoplasmic reticulum-retained proteins. UPR is part of the endoplasmic reticulum quality control (ERQC) which prevents the exit of misfolded secretory and membrane proteins from the endoplasmic reticulum.
Heterodimer of a catalytic subunit alpha (ROT2) and a subunit beta (GTB1).
Subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins. Specifically required for the cleavage of the final glucose.
Catalyzes the covalent attachment of ubiquitin to other proteins.
Forms a complex with the serine/threonine kinase MEC1 which activates checkpoint signaling upon genotoxic stresses. The MEC1-LCD1 complex is recruited by the single-strand-binding protein complex RPA to DNA lesions in order to initiate the DNA repair by homologous recombination, after the MRX-complex and TEL1 are displaced. Required for the recruitment of MEC1 to DNA lesions, the activation of CHK1 and RAD53 kinases and phosphorylation of RAD9 in response to DNA damage. Required for cell growth and meiotic recombination.
Phosphorylated by MEC1 in a cell cycle dependent manner and in response to DNA damage.
Interacts with snoRNA U3. Interacts with MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3. In the absence of snoRNA3, forms a complex with other t-UTPs. This complex can associate with pre-18S ribosomal RNAs.
Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I together with a subset of U3 proteins required for transcription (t-UTPs).
Present with 5440 molecules/cell in log phase SD medium.
Forms part of complex II containing four subunits: a flavoprotein (FP), an iron-sulfur protein (IP) and a cytochrome b composed of a large and a small subunit.
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in system II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDH3 and SDH4 form the membrane dimer that anchors the catalytic dimer formed by SDH1 and SDH2 to the matrix surface of the mitochondrial inner membrane. Electrons originating from the catalytic dimer enter the membrane dimer for ubiquinone reduction.
Present with 7920 molecules/cell in log phase SD medium.
Belongs to the CND1 (condensin subunit 1) family.
Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: BRN1, YCS4 and YCG1/YCS5.
Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase.
Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer), which bind to DNA mismatches thereby initiating DNA repair. MSH2 seems to act as a scaffold for the other MutS homologs that provide substrate-binding and substrate specificity. When bound, heterodimers bend the DNA helix and shield approximately 20 base pairs. MutS alpha acts mainly to repair base-base and single insertion-deletion mismatches that occur during replication, but can also repair longer insertion-deletion loops (IDLs), although with decreasing efficiency as the size of the extrahelical loop increases. MutS beta acts mainly to repair IDLs from 2 to 13 nucleotides in size, but can also repair base-base and single insertion-deletion mismatches. After mismatch binding, MutS alpha or beta form a ternary complex with a MutL heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. Both subunits bind ATP, but with differing affinities, and their ATPase kinetics are also very different. MSH6 binds and hydrolyzes ATP rapidly, whereas MSH2 catalyzes ATP at a substantially slower rate. Binding to a mismatched base pair suppresses MSH6-catalyzed ATP hydrolysis, but not the activity of MSH2. ATP binding to both subunits is necessary to trigger a change in MutS alpha interaction with mismatched DNA, converting MutS alpha into a sliding clamp capable of hydrolysis-independent movement along DNA, and also facilitates formation of ternary complexes containing MutS and MutL proteins and the mismatch. MutS beta also has a role in regulation of heteroduplex formation during mitotic and meiotic recombination. MutS beta binds to DNA flap structures predicted to form during recombination, and is required for 3' non-homologous tail removal (NHTR). MutS beta-binding alters the DNA conformation of its substrate at the ds/ssDNA junction and may facilitate its recognition and/or cleavage by the downstream nucleotide excision repair (NER) RAD1-RAD10 endonuclease.
Heterodimer consisting of MSH2-MSH6 (MutS alpha) or MSH2-MSH3 (MutS beta). Both heterodimers form a ternary complex with MutL alpha (MLH1-PMS1). MutS beta also forms a ternary complex with MutL beta (MLH1-MLH3), and possibly with a MLH1-MLH2 heterodimer. Both heterodimers interact with proliferating cell nuclear antigen (PCNA/POL30). This interaction is disrupted upon binding of the MutS heterodimers to mismatch DNA. Interacts with SAW1.
Homooligomer. Interacts with PEX25 and PEX34.
Present with 382 molecules/cell in log phase SD medium.
Required for regulation of peroxisome size and number. Also promotes peroxisome division and biogenesis.
Serine hydrolase of unknown specificity.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YDR261C-C ORF.
Transposon YDRCTy1-3 (YDRCTy1-3) contains a 425 bp deletion at position 1596, which truncates the ORF coding for protein TY1B when compared to other Ty1 elements. It is probably not functional.
Interacts with ABP1, which is required for proper actin patch localization.
Present with 1323 molecules/cell in log phase SD medium.
Protein kinase involved in the regulation of actin cytoskeleton organization and endocytosis (PubMed:9885245, PubMed:10087264, PubMed:11694597, PubMed:11739778). Phosphorylates PAN1 which disrupts the interaction between PAN1 and END3, and between PAN1 and SLA1 (PubMed:9885245, PubMed:11739778, PubMed:13679512). Phosphorylates SCD5 (PubMed:12956961, PubMed:13679512). Preferentially, phosphorylates substrates on threonine residues in a [L/I/V/M]-x-x-[Q/N/T/S]-x-T-G motif (PubMed:9885245, PubMed:11739778, PubMed:12956961, PubMed:13679512).
Viable (PubMed:9885245). At the restrictive temperature of 37 degrees Celsius, loss of asymmetric localization of cortical actin patches and, delay in emergence and bud growth resulting in the accumulation of unbudded cells (PubMed:9885245).
Interacts with transcription complexes SCB-binding factor (SBF) and MCB-binding factor (MBF). Interacts with SWI4.
Belongs to the SSU72 phosphatase family.
Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation. SSU72 is required for 3'-end formation of snoRNAs.
Processively dephosphorylates Ser-5 of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (RPB1).
Component of the 20S proteasome chaperone. Forms a heterodimer with ADD66 that binds to proteasome precursors.
Present with 80200 molecules/cell in log phase SD medium.
DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs, facilitating single-stranded DNA (ssDNA) production by the EXO1 and SGS1 machinery. Promotes gene silencing at heterochromatin by regulating the chromatin structure within or around silent loci. Also required for heterochromatin organization at centromeres.
Impaired ability to repair double-strand breaks (DSBs).
Present with 6800 molecules/cell in log phase SD medium.
Was initially reported to contain a CUE domain (PubMed:19956593). However, no CUE domain is predicted by prediction tools and the CUE-like region does not show no affinity for ubiquitinated histones (PubMed:20075079).
Transports either thiamine or, rather, a related metabolite involved in the thiamine biosynthesis pathway.
Stimulates specifically the GTPase activity of SEC4, YPT6 and YPT36. Inactivates YPT6 during recycling between the endosome and the Golgi compartments.
Present with 8370 molecules/cell in log phase SD medium.
A C-terminal deletion renders yeast hypersensitive to UV light.
ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of XPB/SSL2, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB/SSL2 is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription (PubMed:8269516, PubMed:7693549, PubMed:7961739, PubMed:8202161, PubMed:7813015, PubMed:8631896). XPB/SSL2 acts as a double-stranded DNA translocase promoting DNA opening by tracking along the nontemplate promoter strand, rotating and inserting DNA into the Pol II active site cleft, leading to DNA unwinding. May also use this translocase mechanism during DNA repair rather than physically wedging open damaged DNA (PubMed:25775526).
Belongs to the helicase family. RAD25/XPB subfamily.
Present with 825 molecules/cell in log phase SD medium.
Belongs to the class II aldolase/RraA-like family.
Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
Competitively inhibited by oxalate, a pyruvate enolate analog.
Divalent metal cation. Has preference for nickel ions for the HMG aldolase activity. Has preference for cobalt and zinc ions for the OAA decarboxylase activity.
Homotrimer. Forms a ring-like structure with a central cavity.
Homooligomer. Interacts with CDC5, KAR1, KIN4, SPC97, SPC98, STU2 and TUB4.
Spindle pole body component that acts as the gamma-tubulin complex-binding protein of the SPB outer plaque. Anchors cytoplasmic microtubules at the at the half bridge of the spindle pole body (SPB) and accordingly functions in nuclear position and spindle orientation, including anaphase spindle migration into the bud. Recruits KIN4 kinase to both SPBs when cytoplasmic microtubules are defective. Links cytoplasmic microtubules with spindle orientation checkpoint (SPOC) components and, therefore, could function as part of the sensors of spindle orientation defects. Is strictly required for mating and karyogamy.
Present with 4220 molecules/cell in log phase SD medium.
Thiosulfate sulfurtransferase which catalyzes the transfer of sulfane sulfur from thiosulfate to cyanide.
Component of the spindle pole body (SPB) required for the proper execution of spindle pole body (SPB) duplication. Potential role in cross-linking filaments or anchoring other molecules. It is essential for growth.
Homodimer. Component of the SPC110 complex containing at least CMD1, SPC29 and SCP110. Interacts with SPC97 and SPC98.
Involved in bud site selection. Required for resistance to the DNA-damaging agent methyl methanesulfonate (MMS).
Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament (By similarity).
Present with 13400 molecules/cell in log phase SD medium.
Involved in 5'-end processing of mitochondrial COB, 15S rRNA, and RPM1 transcript. May also have a role in 3'-end processing of the COB pre-mRNA.
In the C-terminal section; belongs to the TrpB family.
In the N-terminal section; belongs to the TrpA family.
Belongs to the acetyl-CoA hydrolase/transferase family.
Present with 4890 molecules/cell in log phase SD medium.
Presumably involved in regulating the intracellular acetyl-CoA pool for fatty acid and cholesterol synthesis and fatty acid oxidation. It may be involved in overall regulation of acetylation during melatonin synthesis.
Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
Highly expressed during logarithmic phase of growth. Down-regulated during the stationary phase.
Involved in the biosynthesis of the branched chain amino acids leucine, isoleucine, and valine. Catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) in the methionine salvage pathway primarily using branched chain amino acids (leucine, isoleucine, and valine) as the amino donors. Appears to be involved in the regulation of the transition from G1 to S phase in the cell cycle. High copy suppressor of a temperature-sensitive mutation in the ABC transporter, ATM1.
Mainly expressed on ammonium-glucose exponential cultures (biosynthetic conditions), and repressed in the presence of leucine, isoleucine or valine.
Present with 87300 molecules/cell in log phase SD medium.
The ERF2-SHR5 complex is a palmitoyltransferase specific for Ras proteins (PubMed:12193598, PubMed:12379641, PubMed:7532279). Palmitoylates RAS2, which is required for its proper plasma membrane localization (PubMed:12193598, PubMed:12379641, PubMed:7532279).
Anion/proton exchange transporter involved in iron and copper cation homeostasis. Involved in intracellular iron metabolism during growth on fermentable and non fermentable carbon sources. Required for proper copper-loading and maturation of multicopper oxidase FET3. Important for adjusting intracellular compartment pH to more alkaline pH under iron limitation. May also transport chloride ions through the plasma membrane.
Belongs to the chloride channel (TC 2.A.49) family.
Homodimer (By similarity). Interacts with GET3.
Proteolytically processed in the secretory pathway by protease KEX2 within the first extracellular loop. However, both the N- and C-terminal products of the cleavage reaction are required for assembly of a functional channel.
Was originally thought to be a voltage-gated ClC-type chloride channel.
Belongs to the DHHC palmitoyltransferase family. PFA3 subfamily.
Palmitoyltransferase specific for VAC8. Palmitoylates VAC8 at one or more of its N-terminal cysteine residues, which is required for its proper membrane localization.
Present with 2133 molecules/cell in log phase SD medium.
Probable efflux transporter. Confers resistance to the azole derivative fluconazole (FCZ).
DNA helicase which participates in several chromatin remodeling complexes, including the SWR1 and the INO80 complexes. The SWR1 complex mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. The INO80 complex remodels chromatin by shifting nucleosomes. Its ability to induce transcription of some phosphate-responsive genes is modulated by inositol polyphosphates. The INO80 complex is involved in DNA repair by associating to 'Ser-129' phosphorylated H2A histones as a response to DNA damage. During transcription may recruit SPT15/TBP to the TATA-boxes of involved genes. Required for box C/D and box H/ACA snoRNA accumulation and involved in pre-rRNA processing.
Present with 3030 molecules/cell in log phase SD medium.
Probably forms a homohexamer. Interacts with RVB1 and may form heterododecamers with RVB1. Component of the SWR1 chromatin remodeling complex composed of at least ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4, SWC5, SWC7 and SWR1, and perhaps BDF1. Component of the chromatin-remodeling INO80 complex, at least composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3, IES4, IES6, ACT1, IES2, IES5 and INO80. Belongs also to the R2TP complex composed of at least RVB1, RVB2, TAH1 and PIH1. Interacts with SPT15/TBP.
Fungal signal recognition particle (SRP) complex consists of a 7S RNA molecule (scR1) and at least six protein subunits: SRP72, SRP68, SRP54, SEC65, SRP21 and SRP14. At least SRP14, SRP21, SRP68 and SRP72 are proposed to get assembled together with scR1 RNA as a pre-SRP complex in the nucleolus which is exported to the cytoplasm.
Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the arrest of nascent chain elongation during membrane targeting.
Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. Controls phosphorylation and abundance of PDS1 to prevent anaphase entry. Also helps prevent mitotic exit.
Catalyzes triacylglycerol (TAG) formation by an acyl-CoA independent pathway. The enzyme specifically transfers acyl groups from the sn-2 position of a phospholipid to diacylglycerol (DAG), thus forming an sn-1-lysophospholipid (PubMed:10747858, PubMed:10829075, PubMed:32349126). The preferred acyl donors are phosphatidylethanolamine (PE) and phosphatidylcholine (PC). Also capable of using broad acyl donors such as phosphatidic acid (PA), phosphatidylserine (PS), phosphatidylglycerol (PG) and phosphatidylinositol (PI), as well as monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG), and acyl-CoA, and it is more likely to use unsaturated acyl donors. As acyl acceptors, it prefers 1,2- over 1,3-diacylglycerol (DAG). Additionally, has esterification activity that can utilize methanol as acyl acceptor to generate fatty acid methyl esters (FAME) (PubMed:30706417). Can also utilize ceramide instead of DAG, acylating the ceramides by attaching a fatty acid to the hydroxy group on the first carbon atom of the long-chain base to produce 1-O-acylceramides (PubMed:22738231). Involved in lipid particle synthesis from the endoplasmic reticulum, promoting localized TAG production at discrete ER subdomains (PubMed:32349126). Relocates from the endoplasmic reticulum to a subdomain of the inner nuclear membrane upon nutrient starvation, where it provides a site of TAG synthesis, which is coupled with nuclear membrane remodeling (PubMed:31422915).
Nuclear serine protease which mediates apoptosis through proteolysis of the apoptotic inhibitor BIR1.
Present with 3150 molecules/cell in log phase SD medium.
Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SETD6 subfamily.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates 60S ribosomal protein L42 (RPL42A and RPL42B) at 'Lys-55'.
Belongs to the peroxiredoxin family. Prx5 subfamily.
Biochemical and mutational analysis assigned Cys-120 as the resolving cysteine (C(R)) (PubMed:9888818). However, crystal structures showed that Cys-120 is deeply buried within the protein and revealed formation of a disulfide bond between the peroxidatic cysteine Cys-62 and the therefore more likely C(R) Cys-31 (PubMed:22474296, Ref.21).
Conjugated to URM1, a ubiquitin-like protein.
Present with 16228 molecules/cell in log phase SD medium.
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys Prx, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Preferentially eliminates organic peroxides rather than hydrogen peroxide (PubMed:10391912, PubMed:9988687, PubMed:10681558). Relays alkyl hydroperoxides as a signal to the transcription factor CAD1/YAP2 by inducing the formation of intramolecular disulfide bonds in CAD1, which causes its nuclear accumulation and activation (PubMed:20145245). Involved in cellular Mn(2+) homeostasis (PubMed:10635552).
Belongs to the oxygen-dependent FAD-linked oxidoreductase family.
Can oxidize L-gulono-1,4-lactone as well as D-arabinono-1,4-lactone and L-galactono-1,4-lactone.
Mitochondrial antiporter which catalyzes the transport of citrate and oxoglutarate across the membrane. Also shows specificity for oxaloacetate, and to a lesser extent succinate and fumarate. Transports isocitrate, cis-aconitate and L-malate with very low efficiency. Does not show uniporter activity. Helps to maintain normal citrate levels and NADPH/NADP(+) ratios under conditions of oxidative stress. In addition, associates with the mitochondrial nucleoid and binds DNA in vitro, although the relevance of these data in vivo is unclear.
Shows slow growth and respiration defects in minimal medium. Shows growth defects in acetate-supplemented medium; the phenotype is enhanced by addition of hydrogen peroxide (increased oxidative stress) and/or double knockout of YHM2 and ZWF1. The cytosolic NADPH/NADP(+) ratio is decreased compared to wild type; this effect is enhanced in the presence of hydrogen peroxide. The mitochondrial NADPH/NADP(+) ratio is increased, but only in the presence of hydrogen peroxide. Levels of cytosolic citrate are reduced, but only in the presence of hydrogen peroxide. Levels of cytosolic oxoglutarate are reduced, but only in the presence of hydrogen peroxide; the effect is enhanced by double knockout of YHM2 and ZWF1. Cells show a very small increase in levels of reactive oxygen species (ROS) following hydrogen peroxide treatment; in double knockouts of YHM2 and ZWF1 there is a large increase in ROS. Overexpression suppresses the temperature-sensitive growth defect of ABF2 in glucose-rich medium.
Strongly inhibited by mersalyl, p-chloromercuribenzenesulfonate, mercuric chloride, N-ethylmaleimide, pyridoxal 5'-phosphate, bathophenanthroline, and tannic acid. Partially inhibited by alpha-cyanocinnamate and bromescol purple. Weakly inhibited by butylmalonate and phenylsuccinate. Not inhibited by 1,2,3-benzenetricarboxylate or carboxyatractyloside.
Was originally proposed to function in mitochondrial DNA replication and maintenance.
Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]). eIF-5 is essential for cell viability.
Monomer. Interacts with NIP1 and SUI3. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a multifactor complex (MFC) that may bind to the 40S ribosome. TIF32, NIP1 and TIF5/eIF-5 comprise a minimal 40S-ribosome-binding unit.
Present with 48300 molecules/cell in log phase SD medium.
Produced by alternative initiation at Met-18 of isoform Long.
Present with 68400 molecules/cell in log phase SD medium.
G proteins are composed of 3 units, alpha, beta and gamma. GPG1 interacts with the beta subunits GBP1 and GPB2.
Gamma subunit of a guanine nucleotide-binding protein (G protein). G proteins are involved as modulators or transducers in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Involved in the determination of the cAMP level according to nutritional conditions, most probably as a regulator of cAMP phosphodiesterase. Required for the control of pseudohyphal and haploid invasive growth.
Catalyzes the attachment of asparagine to tRNA(Asn) in a two-step reaction: asparagine is first activated by ATP to form Asn-AMP and then transferred to the acceptor end of tRNA(Asn).
Acts as essential component of the translation initiation factor 2B (eIF2-B or GCD complex), which catalyzes the exchange of eukaryotic initiation factor 2 (eIF-2)-bound GDP for GTP and is regulated by phosphorylated eIF-2. It activates the synthesis of GCN4 in yeast under amino acid starvation conditions by suppressing the inhibitory effects of multiple AUG codons present in the leader of GCN4 mRNA. It may promote either repression or activation of GCN4 expression depending on amino acid availability. GCD1 stabilizes the interaction between eIF-2 and GCD6 and stimulates the catalytic activity in vitro.
Belongs to the eIF-2B gamma/epsilon subunits family.
Present with 9530 molecules/cell in log phase SD medium.
Translation initiation factor 2B (eIF2-B) is composed of five different subunits; alpha (GCN3), beta (GCD7), gamma (GCD1), delta (GCD2) and epsilon (GCD6). A catalytic subcomplex comprising GCD1 and GCD6 interacts with both, phosphorylated and non-phosphorylated eIF-2 and has exchange activity in vitro.
Present with 37500 molecules/cell in log phase SD medium.
Involved in induction of programmed cell death in response to reactive oxygen species (ROS) (PubMed:16962064). May be involved in sterol transfer between intracellular membranes (PubMed:26001273).
Monomer. Interacts with RBD2, YIF1, YIP1 and YIP5.
Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)).
Catalyzes the first step in the biosynthesis of coenzyme A from vitamin B5, where cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine.
Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is involved in transcriptional regulation. Heterodimer of ARP9 and ARP7 functions with HMG box proteins to facilitate proper chromatin architecture. Heterodimer formation is necessary for assembly into RSC complex. Part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Forms a heterodimer with ARP7. Interacts with LDB7 and NPL6. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin. Component of the SWI/SNF global transcription activator complex. The 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29.
Belongs to the SF3b complex composed of CUS1, HSH49, HSH155, RCP1, RDS3 and RSE1.
Involved in pre-mRNA splicing. Required for the SF3b integrity and prespliceosome assembly.
Belongs to the small GTPase superfamily. Arf family.
GTP-binding protein involved in Golgi vesicle trafficking (PubMed:15356266, PubMed:34830155). May modulate vesicle budding and uncoating within the Golgi apparatus (PubMed:15356266). May recruit the lipid transfer protein VPS13 to Golgi membranes (PubMed:34830155). Recruits polyadenylate-binding protein PAB1 to COPI vesicles, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA (PubMed:15356266).
Interacts with RUD3 (PubMed:15356266, PubMed:15504911, PubMed:19141284, PubMed:20601958). Interacts with VPS13 (via C-terminal part); the interaction is direct (PubMed:34830155).
Negative regulator of the Ras-cyclic AMP pathway. Negatively regulate the activity of normal but not mutationally activated Ras proteins. The down-regulatory effect of RPI1 requires the presence of one of the two Ras GTPase activators, IRA1 and IRA2.
Present with 1340 molecules/cell in log phase SD medium.
Belongs to the Rieske iron-sulfur protein family.
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 10 subunits. The complex is composed of 3 respiratory subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10 (PubMed:1657998, PubMed:2538628, PubMed:10873857, PubMed:11880631, PubMed:18390544, PubMed:30598554). The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a monomer or a dimer of cytochrome c oxidase (complex IV, CIV), resulting in 2 different assemblies (supercomplexes III(2)IV and III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556, PubMed:30598554). RIP1 interacts with QCR10 on the intermembrane space (IMS) side, and with QCR9 (PubMed:30598556, PubMed:30598554).
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (Probable). The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster (PubMed:18390544). It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q(0) site in cytochrome b (COB) to cytochrome c1 (CYT1) (PubMed:1657998, PubMed:2538628) (Probable).
Processed by both the mitochondrial processing peptidase (MPP) and the mitochondrial intermediate protease (MIP). Initially, MPP removes 22 amino acids from the newly imported precursor in the mitochondrial matrix. This proteolytic processing is then followed by a second proteolytic cleavage by MIP, which removes an octapeptide to generate mature-sized RIP1.
The Rieske protein is a high potential 2Fe-2S protein.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family.
Belongs to the deoxyhypusine hydroxylase family.
Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.
Component of the RPD3C(L) histone deacetylase complex (HDAC) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. SDS3 is required for the HDAC activity of the complex and for the RPD3-SIN3 association.
Present with 105 molecules/cell in log phase SD medium.
Interacts with ribosomes. Interacts with ABP1.
Involved in mitochondrial migration along actin filaments.
Belongs to the GPI inositol-deacylase family.
Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins. Required for the transport of misfolded protein to the Golgi, although dipensable for the transport of many normal proteins.
Required for vacuolar assembly. Provides the t-SNARE function in a late step of the vacuolar assembly. Required for homotypic vacuole membrane fusion, autophagy and fusion of biosynthetic transport vesicles with the vacuole. Required for the delivery of alpha-factor receptor-ligand complexes to the vacuole.
Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily.
Binds to ribosomes (PubMed:9670014, PubMed:1394434, PubMed:27917864). Binds close to the ribosomal tunnel exit via contacts with both ribosomal proteins RPL35, RPL39 and RPL19, and rRNA (By similarity). Directly interacts with nascent polypeptides. This interaction is dependent on the ribosome-associated complex (RAC) (PubMed:11929994, PubMed:23332755). Interacts with SSE1 (PubMed:23332755).
Expression decreases after heat shock or during growth to stationary phase (PubMed:6761581, PubMed:2651414). Up-regulated upon carbon upshift and down-regulated upon amino acid limitation in an HSF1-dependent manner (PubMed:10322015). Interacts with SSE1 (PubMed:16219770, PubMed:16221677). Interacts with FES1 (By similarity).
Present with 104000 molecules/cell in log phase SD medium.
Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.
Associates with the 60S ribosomal subunit.
Involved in the biogenesis of the 60S ribosomal subunit and translational activation of ribosomes. Together with the EF-2-like GTPase RIA1, may trigger the GTP-dependent release of TIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating TIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export.
Present with 5060 molecules/cell in log phase SD medium.
Phosphorylated by SNF1 in absence of glucose. The phosphorylation is required for induction of transcription of gluconeogenic genes.
Transcription factor which regulates the expression of genes for gluconeogenesis, the TCA cycle, and glucose metabolism. Involved in the cell wall remodeling process and drug resistance.
Belongs to the glycosyl hydrolase 81 family.
Cleaves internal linkages in 1,3-beta-glucan (PubMed:12455695). Involved in the dissolution of the mother-daughter septum during cell separation (PubMed:12455695).
Present with 64 molecules/cell in log phase SD medium.
With SBE2, is involved in cell wall integrity and polarity processes like bud growth, through the transport of CHS3 and UTR2 to sites of growth.
Belongs to the eukaryotic ribosomal protein eL34 family.
Present with 21000 molecules/cell in log phase SD medium.
Forms homooligomers. Interacts (via the SH3 domain) with PBS2. Interacts with FUS1, STE11, STE50 and RNA polymerase II.
Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity. Detects changes in external osmolarity and activates PBS2 through the stimulation of STE11 and targets PBS2 to the plasma membrane. PBS2 activation leads to changes in glycerol production that helps to balance the intracellular and external osmotic pressures. Activates also HOG1 in response to heat stress and mediates resistance to oxidative stress. Involved in the regulation of the mating pathway. May be a receptor that feeds into the pseudohyphal growth pathway.
Autoacetylation at Lys-367 is required for proper function.
Catalytic component of the histone acetyltransferase NuA3 complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation. In vitro, SAS3 acetylates free histones H3 and H4. It is involved in silencing the HMR locus.
Component of the NuA3 complex, composed of at least NTO1, SAS3, TAF14, YNG1 and EAF6. SAS3 interacts with CDC68/SPT16.
Probable phosphatase. Involved in the response to sodium and lithium ion stress (but not to potassium or sorbitol stress) by inducing transcription of the sodium pump ENA1/PMR2. Acts through a calcineurin-independent pathway and is functionally redundant with PSR1. Also involved in the general stress response; acts together with WHI2 to activate stress response element (STRE)-mediated gene expression, possibly through dephosphorylation of MSN2.
Acts as probably catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. In vitro, POP2 has 3'-exoribonuclease activity with a preference for poly(A) RNAs, but also degrades poly(U) and poly(C) RNAs. Is part of a glucose-sensing system involved in growth control in response to glucose availability.
Divalent metal cations. Mg(2+) is the most probable.
Present with 4590 molecules/cell in log phase SD medium.
Forms a functional homodimer and may form a heterodimer with PMT6. Interacts with RCR1.
Leads to diminished MID2 O-mannosylation.
Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a homodimeric complex to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. Specifically acts on secretory proteins with an ER-luminally oriented Ser/Thr-rich region flanked by a membrane anchor such as FUS1, AXL2, GAS1, KEX2, MID2, WSC1, WSC2, OPY2, PRM5, RAX2, or YNL176.
Ty1-BR is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Repressed by glucose and increased expression upon nitrogen depletion.
Transcription factor involved in the regulation of fermentation and aerobic oxidation. Acts as a repressor of CYC1, which is involved in electron flow through the mitochondria under aerobic condition. Required for pseudohyphal formation upon nitrogen starvation. May be involved in viability at stationary phase and aging.
Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. Together with HTL1, NPL6, RSC3, RSC30 components, defines a fungal-specific module within the RSC complex that plays a role in many cellular functions including the maintenance of cell wall integrity. May be involved in the transfer of mannosylphosphate (MP) groups into N-linked oligosaccharides.
Interacts with STH1, RSC3 and ARP9. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin. Component of a fungal-specific module (HTL1-LDB7-NPL6-RSC3-RSC30) within the RSC complex.
Cleavage of N-terminal methionine and N-terminal acetylation by NAT1/ARD1.
Major of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-ketoacids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids derived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate), valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate), isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins.
Protein expression is strongly induced by high concentrations of fermentable carbon sources and under anaerobic growth conditions and is repressed by ethanol. Protein expression level is also autoregulated through an unknown mechanism.
Belongs to the radical SAM superfamily. Biotin synthase family.
Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
Involved in cell wall beta(1->6) glucan synthesis.
Co-assembles with BUD4 at bud sites. BUD4 and BUD3 may cooperate to recognize a spatial landmark (the neck filaments) during mitosis and they subsequently become a landmark for establishing the axial budding pattern in G1.
Forms a complex with TBP which binds TATA DNA with high affinity but with altered specificity.
Regulates transcription in association with TATA binding protein (TBP). Removes TBP from the TATA box via its C-terminal ATPase activity. Both transcription activation and repression require its ATPase activity.
Identified in the GID complex. In the absence of glucose, the complex contains VID30/GID1, the E3 ubiquitin-ligase RMD5/GID2, VID28/GID5, GID7, GID8, and FYV10/GID9. When cells are shifted to glucose-containing medium, VID24/GID4 is induced and becomes part of the complex (PubMed:22645139). Within the GID complex, interacts directly with RMD5/GID2 and FYV10/GID9, and recruits VID24/GID4 to the complex when cells are shifted to glucose-containing medium (PubMed:22645139).
Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium (PubMed:12686616). Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:12686616).
Belongs to the uracil-DNA glycosylase (UDG) superfamily. UNG family.
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Not involved in strand-directed mismatch repair.
Induced in late G1 and early S phase of the cell cycle.
Belongs to the mitochondrion-specific ribosomal protein mL50 family.
Homotrimer (PubMed:15201901). Interacts with RAD30 (PubMed:11545742). Interacts with MCM10 (PubMed:16782870). Interacts with UBP10 (PubMed:22829782).
Lys-164 is deubiquitinated by UBP10 (PubMed:22829782).
Monoubiquitinated on Lys-164 by the UBC2/RAD18 complex upon DNA damage, and then polyubiquitinated through 'Lys-63'-linkage by UBC13/MMS2. Ubiquitination is required for UBC2-mediated DNA repair.
Sumoylated on Lys-164, and to a lesser extent on Lys-127 by the UBC9/SIZ1 complex during S-phase; which impairs ubiquitination and function in DNA repair.
This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair.
Could be the product of a pseudogene. Contains only the N-ter part of the functional aspartic proteinases.
Displays increased levels of spontaneous RAD52 foci in proliferating diploid cells (PubMed:18085829). A combined deletion of the LOH1/OSW4 and IRC18/OSW6 has reduced dityrosine incorporation in the outer spore wall (PubMed:23966878).
In respiratory-deficient cells and by heat.
ECM22 and UPC2 (in combination) null mutants are not viable.
Present with 79 molecules/cell in log phase SD medium.
Transcription factor involved in sterol uptake and regulation of sterol biosynthesis. Binds to sterol regulatory elements (SRE) with the consensus sequence 5'-TCGTATA-3' present in ERG2 and ERG3 promoters and regulates transcription of ERG2 and ERG3 in response to sterol levels. Seems to be involved in activation of DAN2 and DAN3 cell wall mannoproteins.
Belongs to the TrkH potassium transport family.
This protein is required for low-affinity potassium transport.
Contains PCR fragment of strain VP102-10A.
This is a truncated version of an UPF0508 family protein. Strain S288c has a tandem insertion of a Ty1 transposon in position 742, which disrupts the gene coding for this protein and produces two ORFs YJR030C and YJR025C-A. A contiguous sequence of this protein can be found in strain YJM789 (AC A6ZPZ1).
Cells show slow growth, fragmented mitochondria and have a 50-fold reduced level of s-MGM1. These defects can be complemented by human PRELI or bypassed by growth on a nonfermentable carbon source.
Interacts with MDM35 (PubMed:20622808, PubMed:20657548, PubMed:26071602, PubMed:26071601, PubMed:26235513). Found associated with a 170 kDa complex.
Required for maintenance of normal mitochondrial morphology (PubMed:16754953, PubMed:26071601). Required for PCP1-dependent processing of MGM1 (PubMed:16754953). The UPS1:MDM35 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space (PubMed:26071602, PubMed:26071601, PubMed:26235513). Phosphatidic acid release requires dissociation of the UPS1:MDM35 complex (PubMed:26235513). Phosphatidic acid import is required for cardiolipin (CL) synthesis in the mitochondrial inner membrane (PubMed:26071602). With UPS2, controls the level of cardiolipin in mitochondria (PubMed:19506038). Cardiolipin is a unique phospholipid with four fatty acid chains and is present mainly in the mitochondrial inner membrane where it stabilizes the electron transport chain supercomplex between complexes III and IV through direct interaction of their subunits.
Homomultimer. Forms a complex with SIR3 and SIR4 (PubMed:9122169). Component of the RENT complex, at least composed of SIR2, CDC14 and NET1 (PubMed:10219244, PubMed:10219245). The RENT complex interacts with FOB1 (PubMed:12923057). Interacts with ESC8 (PubMed:12399377). Interacts with and ZDS2 (PubMed:10662670). Interacts with MCM10 (PubMed:16328881). Interacts with SLX5 (PubMed:18086879). Interacts with NSI1 (PubMed:22362748).
Its activity is increased by calorie restriction, which slows the pace of aging and increases maximum lifespan. Activated by resveratrol (3,5,4'-trihydroxy-trans-stilbene), which is found in red wine.
Its stability is directly linked to life span, which is extended when it is present in high dosage. Conversely, its absence shortens life span.
NAD-dependent deacetylase, which participates in a wide range of cellular events including chromosome silencing, chromosome segregation, DNA recombination and the determination of life span. Involved in transcriptional repression of the silent mating-type loci HML and HMR and telomeric silencing via its association with SIR3 and SIR4. Plays a central role in ribosomal DNA (rDNA) silencing via its association with the RENT complex, preventing hyperrecombination, and repressing transcription from foreign promoters, which contributes to extending life span. Probably represses transcription via the formation of heterochromatin structure, which involves the compaction of chromatin fiber into a more condensed form, although this complex in at least one case can still bind euchromatic levels of positive transcription regulators. Although it displays some NAD-dependent histone deacetylase activity on histone H3K9Ac and H3K14Ac and histone H4K16Ac in vitro, such activity is unclear in vivo and may not be essential.
Present with 3350 molecules/cell in log phase SD medium.
The reported ADP-ribosyltransferase activity of sirtuins is likely some inefficient side reaction of the deacetylase activity and may not be physiologically relevant.
Was originally thought to be an ADP-ribosyltransferase.
Component of centromeric nucleosomes, where DNA is wrapped around a histone octamer core (PubMed:32004465, PubMed:14581449). The octamer contains two molecules each of H2A, H2B, CSE4/CENPA and H4 assembled in one CSE4-H4 heterotetramer and two H2A-H2B heterodimers (PubMed:32004465, PubMed:14581449). Interacts with the inner kinetochore (PubMed:14581449). Interacts with the central kinetochore protein CTF19 (PubMed:10958698). Interacts with YTA7 (PubMed:32079723).
Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. Required for functional chromatin architecture at the yeast 2-micron circle partitioning locus and promotes equal plasmid segregation.
Mutation in CSE4 causes chromosome non-disjunction and cell cycle arrest at mitosis.
Ubiquitinated (Probable). Is degraded through ubiquitin-mediated proteolysis when not protected by its association to the kinetochore (Probable).
Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.
Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II). Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. Required for respiration and the maintenance of the mitochondrial compartment.
Homodimer or in a complex with other proteins (PubMed:11509667). Interacts with ARS1 (PubMed:8195160).
Positively regulated by the zinc-responsive transcriptional regulator ZAP1.
Was originally (PubMed:8195160) thought to be a nuclear protein involved in transcriptional regulation of genes required for the functional assembly of mitochondrial respiratory proteins. This was later proven not to be the case (PubMed:11509667).
COT1 has a paralog, ZRC1, that arose from the whole genome duplication.
Contains 3 histidine repeat motifs between the 4th and 5th transmembrane, exposed to the cytoplasm, that may be involved in the binding site of zinc.
Expression is increased in response to DNA replication stress.
Reduces zinc transport into the vacuole and hence limit the over-accumulation of zinc caused by the deletion of ZRT3.
Vacuolar transporter that regulates zinc homeostasis by mediating zinc transport and storage into the vacuole (PubMed:9712830, PubMed:10856230, PubMed:12556516). Plays a role in resistance to zinc shock resulting from sudden influx of zinc into cytoplasm (PubMed:12556516). May also participate in the regulation of cobalt levels under normal physiological conditions and may be important in the supply of metal that is required for metalloenzyme or cofactor synthesis (PubMed:1508175, PubMed:18930916). Involved in the resistance to cobalt and rhodium ions (PubMed:1508175).
Components of the endosome-vacuole trafficking pathway that regulates nutrient transport. May be involved in processes which determine whether plasma membrane proteins are degraded or routed to the plasma membrane. Confers leflunomide resistance when overexpressed.
Belongs to the eukaryotic GSH synthase family.
Belongs to the Mediator complex subunit 8 family.
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. MED8 binds to the consensus sequence 5'-[AC][AG]GAAAT-3' in both the UAS of SUC2 and the DRS2 of HXK2.
Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. MED8 interacts directly with SRB5/MED18. Interacts also with Hexokinase B (HXK2). Interacts with TBP1.
Interacts with TVP18, TVP23, YIP1 and YIP5. Interacts with SEC4, YPT1, YPT6, YPT7, YPT10, YPT11, YPT31, YPT32 and YPT52; These proteins are all Rab GTPases.
May be involved in proper membrane localization of Rab GTPases.
ATG12-ATG5 induces reorientation of the ATG3 structure, increasing conjugation activity of ATG3.
Acetylated by NuA4 complex acetyltransferase ESA1 at Lys-19 and Lys-48. Acetylation regulates autophagy by controlling ATG8 interaction and lipidation. Deacetylated by histone deacetylase RPD3.
E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy.
Expression is increased during filamentous growth and controlled by the RSF2 transcription factor.
Monomer. Interacts with ATG8 through an intermediate thioester bond between Cys-234 and the C-terminal Gly of ATG8. Also interacts with the 40 amino acid C-terminal region of the E1-like ATG7 enzyme. Interacts also with the ATG12-ATG5 conjugate.
The N-terminal region (residues 1-7) is involved in phosphatidylethanolamine-binding and is required for ATG8-PE conjugation.
The flexible region (FR) is required for ATG7-binding.
The handle region (HR) contains the ATG8 interaction motif (AIM) and mediates binding to ATG8. It is crucial for the cytoplasm-to-vacuole targeting pathway.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
Interacts with RSP5 via its 2 PY-motifs.
Mediates resistance to o-dinitrobenzene, calcium and zinc.
Present with 386 molecules/cell in log phase SD medium.
The PY-motifs are required for the interaction with RSP5 ubiquitin-ligase and important for resistance to o-dinitrobenzene.
Interacts with OXA1 and MDM38. Binds to mitoribosomes in order to recruit them to the mitochondrial inner membrane.
Leads to a reduced growth rate on non-fermentable carbon sources, which is more pronounced at high temperature (PubMed:8690083, PubMed:18727146). Shows defects in the membrane insertion of nascent chains resulting in the accumulation of the precursor form of subunit 2 of cytochrome oxidase (PubMed:20427570, PubMed:25609543).
Mitochondrial inner membrane-associated mitoribosome receptor that spatially aligns the mitoribosome exit tunnel with the membrane insertion machinery and allows cotranslational protein membrane insertion.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). uS2 is required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits (PubMed:9973221, PubMed:14627813).
Present with 60900 molecules/cell in log phase SD medium.
This protein appears to have acquired a second function as a laminin receptor specifically in the vertebrate lineage. This protein does not bind laminin.
Binds to membranes enriched in phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin. Negatively regulated via phosphorylation.
Has a role in the negative regulation of gluconeogenesis. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degradation (Vid) vesicles. This is an indirect role and requires cyclophilin A.
Contains a beta-propeller domain involved in specific binding of phosphatidylinositol 3,5-bisphosphate.
Involved in piecemeal microautophagy of the nucleus (micronucleophagy).
ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (PubMed:2165073). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity).
The matrix-open state (m-state) is inhibited by the membrane-permeable bongkrekic acid (BKA). The cytoplasmic-open state (c-state) is inhibited by the membrane-impermeable toxic inhibitor carboxyatractyloside (CATR).
The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. Odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue.
Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of free histone H4 in the cytoplasm. The complex is also found in the nucleus, however it is not certain that it modifies histone H4 when packaged in chromatin. Histone H4 'Lys-12' acetylation is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Component of the HAT-B complex composed of at least HAT1 and HAT2. In the cytoplasm, this complex binds to the histone H4 tail. In the nucleus, the HAT-B complex has an additional component, the histone H3/H4 chaperone HIF1.
Alpha-glucosidase with specificity for isomaltose, maltose, and palatinose.
Transcriptionally regulated by PDR8. Expression is increased in response to the addition of maltose, isomaltose, and alpha-methylglucopyranoside.
Conjugation to phosphatidylethanolamine (PE) leads to homodimerization. Interacts with ATG1, ATG3, ATG4, ATG7, ATG12, ATG32, ATG34 and the C-terminal 10 residues domain of ATG19. Interacts also with the endoplasmic reticulum to Golgi v-SNARE protein BET1 and the vacuolar v-SNARE protein NYV1. Interacts with the UBX domain-containing protein SHP1.
The C-terminal Arg-117 residue of ATG8 is removed by ATG4 to expose Gly-116 at the C-terminus (PubMed:11038174, PubMed:11149920, PubMed:16680092). This Gly-116 forms then a thioester bond with the 'Cys-507' of ATG7 (E1-like activating enzyme) before being transferred to the 'Cys-234' of ATG3 (the specific E2 conjugating enzyme), in order to be finally amidated with phosphatidylethanolamine (PubMed:11100732, PubMed:15277523, PubMed:20615880, PubMed:17632063, PubMed:17699586, PubMed:18725539, PubMed:19285500, PubMed:23064152, PubMed:22539722, PubMed:28330855, PubMed:20428927). This lipid modification anchors ATG8 to membranes and can be reversed by ATG4, releasing soluble ATG8 (PubMed:22240591, PubMed:22622160, PubMed:22652539, PubMed:28330855).
Ubiquitin-like modifier involved in cytoplasm to vacuole transport (Cvt) vesicles and autophagosomes formation. With ATG4, mediates the delivery of the vesicles and autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. Moreover not only conjugation, but also subsequent ATG8-PE deconjugation is an important step required to facilitate multiple events during macroautophagy, and especially for efficient autophagosome biogenesis, the assembly of ATG9-containing tubulovesicular clusters into phagophores/autophagosomes, and for the disassembly of PAS-associated ATG components. Also plays a role in regulation of filamentous growth.
Up-regulated upon starvation conditions. Expression is under the control of UME6 which acts along with a histone deacetylase complex including SIN3 and RPD3 to regulate negatively ATG8 levels and subsequent autophagic activity.
May be involved in sterol transfer between intracellular membranes.
Belongs to the very long-chain fatty acids dehydratase HACD family.
Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Component of the 7-subunit TFIIH core complex composed of XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in NER. The core complex associates with the 3-subunit CTD-kinase module TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription (PubMed:7961739, PubMed:7813015, PubMed:14500720). Interacts with XPC/RAD4. XPC/RAD4 recruits TFIIH to the NER machinery (PubMed:23295669). Interacts with the NER 3'-endonuclease XPG/RAD2. XPG/RAD2 displaces XPC/RAD4 from the repair complex (PubMed:22373916, PubMed:23295669).
Present with 5150 molecules/cell in log phase SD medium.
Present with 43300 molecules/cell in log phase SD medium.
Interacts with septin proteins, primarily with CDC11. Interacts with SWE1 and NAP1.
Involved in regulation of bud growth during cell cycle and in septin organization. Plays a role in cell wall synthesis.
Component of the Snt2C complex composed of SNT2, ECM5 and RPD3. Interacts with the E2 ubiquitin-conjugating enzyme UBC4 and histones H3 and H4. Binding is enhanced to methylated histone H3K36me3.
Transcriptional regulator that, together with ECM5, recruits histone deacetylase RPD3 to a small number of promoters of stress-response genes in response to oxidative stress (PubMed:23878396). Probable ubiquitin-protein ligase involved in the degradation-related ubiquitination of histones. Contributes to the post-translational regulation of histone protein levels by polyubiquitination of excess histones for subsequent degradation (PubMed:22570702).
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YER159C-A ORF.
Belongs to the deoxyhypusine synthase family.
Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Present with 7600 molecules/cell in log phase SD medium.
Negative regulatory component of the MBF complex involved in cell-cycle-dependent transcription.
Present with 2880 molecules/cell in log phase SD medium.
The MBF complex is composed of at least SWI6, MBP1 and NRM1.
ATP-dependent helicase involved mating type switching and in silencing interference through its interaction with the silencing regulator SIR4. Cooperates with UBC4 and UBC5 to mediate ubiquitination of SUMO conjugates.
Interacts with CDC3, CDC11, EBP2, SIR4, UBC4 and SUMO/SMT3.
Belongs to the SWR1 complex at least composed of ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4, SWC5, SWR1 and HTZ1.
Participates in the catalytic exchange of histone H2A for the H2A variant HZT1, an euchromatin-specific factor, leading to chromatin remodeling and changes in transcription of targeted genes. Indirectly involved in vacuolar protein sorting.
Interacts (via KKVRF motif) with phosphatase GLC7.
Phosphorylation by PRK1 and/or AKL1 on Thr-416, Thr-450 and Thr-490 of repeats 1-1, 1-2 and/or 1-3 negatively regulates SCD5 function in endocytosis and actin cytoskeleton organization.
Regulates both fluid phase and receptor-mediated endocytosis (PubMed:12356757, PubMed:12956961). Involved in vesicular transport at a late stage of the secretory pathway (PubMed:8688556). Regulates actin cytoskeleton organization (PubMed:12356757, PubMed:12956961).
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1), a complex involved in endosomal cargo sorting.
Belongs to the MsrB Met sulfoxide reductase family.
Methionine-R-sulfoxide reductase which catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. Protects iron-sulfur clusters from oxidative inactivation along with MXR1. Involved in the regulation of lifespan.
Acts in the GPI biosynthetic pathway between GlcNAc-PI synthesis and GPI transfer to protein. Required for the formation of complete GPI precursors CP1 and CP2.
Involved in meiotic recombination. Facilitate crossovers between homologs during meiosis.
Two distinct classes of crossovers have been demonstrated in budding yeast. Class I is MSH4/MSH5 dependent and exhibits crossover interference. Class II is MUS81/MMS4 dependent and exhibits no interference.
Affects O-mannosylation activity only when PTM1 and PTM2 are absent.
PMT3 and PMT5 form a functional heterodimer. Forms also a minor complex with PMT1.
Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT5 and more rarely with PMT1 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. Seems to have redundant activity to PMT2.
Specifically induced upon tunicamycin, DTT as well as rhodanine-3-acetic acid derivative OGT2468 treatment.
UDP-N-acetylglucosamine pyrophosphorylase that utilizes N-acetylglucosamine-1-phosphate as substrate (PubMed:9603950). Together with AGM1, is involved in the production of UDP-N-acetylglucosamine from N-acetylglucosamine-6-phosphate (PubMed:9603950).
Belongs to the DNA repair enzymes AP/ExoA family.
DNA repair enzyme that cleaves apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA.
Probably binds two magnesium or manganese ions per subunit.
Part of a checkpoint which monitors spindle integrity and prevents premature exit from mitosis. This cell-cycle arrest depends upon inhibition of the G-protein TEM1 by the BFA1/BUB2 complex.
Activates long-chain fatty acids (LCFA) by esterification of the fatty acids into metabolically active CoA-thioesters for subsequent degradation or incorporation into phospholipids. Also facilitates the transport of LCFAs into the cell, either by active transport or by decreasing the intracellular LCFA concentration (PubMed:7962057, PubMed:11477098, PubMed:12601005). Contributes, with FAA1, to the activation of imported myristate (PubMed:7962057). Also involved in long-chain base (LCB) uptake. In contrast ot LCFA uptake, LCB uptake does not require ATP, suggesting that the enzyme is directly involved in LCB uptake (PubMed:27136724). Involved in the sphingolipid-to-glycerolipid metabolic pathway, converting the shingolipid metabolite hexadecenoic acid to hexadecenoyl-CoA, which is then further converted to glycerolipids (PubMed:22633490).
Present with 31200 molecules/cell in log phase SD medium.
Component of the SPC110 complex containing at least CMD1, SPC29, SPC42 and SCP110.
Forms a polymeric layer at the periphery of the spindle pole body (SPB) central plaque which has an essential function during SPB duplication and may facilitate attachment of the SPB to the nuclear membrane.
Induced by anaerobic conditions, hypoxia and cold. Repressed by heme.
Transcription factor that is involved in activation of anaerobic genes such as DAN/TIR cell wall mannoprotein genes and YML083c. Appears to bind to anaerobic response elements (AR1) with the consensus sequence 5'-TCGTTYAG-3' present in the promoter regions of DAN/TIR genes. Involved in sterol uptake and regulation of the sterol biosynthesis. Binds to sterol regulatory elements (SRE) with the consensus sequence 5'-TCGTATA-3' present in ERG2 and ERG3 promoters. May be involved in down-regulation of CWP2 during anaerobic adaptation.
Necessary for cell polarization during vegetative growth. May link the cytoskeleton to morphogenic determinants on the cell surface.
Belongs to the PA-phosphatase related phosphoesterase family.
Catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Together with LPP1, regulates intracellular DGPP and PA levels, which are phospholipid molecules believed to play a signaling role in stress response. Can also use lysophosphatidic acid (LPA) and phosphatidylglycerophosphate as substrates. Substrate preference is DGPP > LPA > PA. Activity is independent of a divalent cation ion and insensitive to inhibition by N-ethylmaleimide.
Induced by the transcription factor ZAP1 during zinc depletion and negatively regulated by the transcription factor GIS1 predominantly during nutrient limitation. Induced by inositol supplementation.
Inhibited by sodium fluoride (NaF) and pyrophosphate. Strongly inhibited by manganese ion and, to a lower extent, by magnesium and calcium ions. Also inhibited by Cu(2+) ion. In an indirect manner, it is also inhibited by the zinc ion which is able to form a complex with DGPP and prevent the enzyme from removing the phosphate from the substrate. Not inhibited by N-ethylmaleimide.
Present with 3038 molecules/cell in log phase SD medium.
The phosphatase sequence motif I (including Arg-125) and II (including His-169) are part of the cytoplasmic loop 2 and phosphatase sequence motif III (including His-223) is part of the cytoplasmic loop 3.
Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit APL4 and beta-type subunit APL2), a medium adaptin (mu-type subunit APM1) and a small adaptin (sigma-type subunit APS1). AP-1 interacts with clathrin.
Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The AP-1 complex interacts directly with clathrin. AP57 is probably a subunit of the Golgi membrane adaptor.
Belongs to the TALE/M-ATYP homeobox family.
Binds DNA with a high specificity as a heterotetramer consisting of an ALPHA2 dimer and an MCM1 dimer. Also binds DNA with a high specificity as a heterodimer of A1 and ALPHA2 in a/alpha diploid cells. Interacts with the general transcription repressor complex SSN6/TUP1.
Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Silenced copy of ALPHA2 at HML.
Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Transcriptional corepressor that binds cooperatively with MCM1 to a 31-basepair DNA sequence termed the a-specific gene (asg) operator, to repress the transcription of a-cell-specific genes. Additionally, in a/alpha diploid cells, binds cooperatively with the A1 protein to a 21-basepair DNA sequence termed the haploid-specific gene (hsg) operator, to repress transcription of haploid-specific genes and of MATALPHA1.
Only present in alpha-cells and in a/alpha diploid cells.
The C-terminal tail domain is disordered in the monomer, even when bound to DNA. In the ternary complex with A1 and DNA, 16 residues (Ile-190 to Leu-205) of the C-terminal tail undergo a conformational change, becoming ordered and contacting the A1 homeodomain.
The N-terminal domain is required for the interaction with the WD repeats of TUP1 and for dimerization.
The homeobox domain binds to DNA and interacts with the TPR repeats of SSN6.
The unstructured, flexible linker domain contains eight residues (Leu-114 to Gln-121), which, in the presence of MCM1, adopt a beta-fold and mediate the cooperative interaction to MCM1.
There are three genetic loci for mating type genes in S.cerevisiae. MAT is the expression locus that determines the mating type of the cell, whereas HML (containing HMLALPHA1 and HMLALPHA2) and HMR (containing HMRA1 and HMRA2) represent silenced repositories of mating type information. The mating type is determined by the MAT locus, which contains either a copy of HML or of HMR. Diploid cells are usually heterozygous for the MAT locus.
Belongs to the acetyltransferase family. GCN5 subfamily.
Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. SUS1 associates with the SAC3-THP1 complex. Component of the SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9. Component of the ADA/GCN5 complex, that consists of HFI1/ADA1, ADA2, ADA3, SPT20/ADA5 and GCN5 and is probably a subcomplex of SAGA. Component of the 0.8 MDa ADA complex, which at least consists of ADA2, ADA3, AHC1 and GCN5. GCN5 interacts with ADA2.
Histone acetyltransferase that acetylates histone H2B to form H2BK11ac and H2BK16ac, histone H3 to form H3K9ac, H3K14ac, H3K18ac, H3K23ac, H3K27ac and H3K36ac, with a lower preference histone H4 to form H4K8ac and H4K16ac, and contributes to H2A.Z acetylation (PubMed:10026213, PubMed:11545749, PubMed:16543222, PubMed:16543223, PubMed:17189264). Acetylation of histones gives a specific tag for epigenetic transcription activation and elongation (PubMed:10026213, PubMed:11545749, PubMed:16543222, PubMed:16543223, PubMed:17189264, PubMed:19822662). Operates in concert with certain DNA-binding transcriptional activators such as GCN4 or HAP2/3/4 (PubMed:10026213, PubMed:11545749, PubMed:16543222, PubMed:16543223, PubMed:17189264). Its acetyltransferase activity seems to be dependent on the association in different multisubunit complexes (PubMed:10026213, PubMed:11545749, PubMed:16543222, PubMed:16543223, PubMed:17189264). Functions as histone acetyltransferase component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and ADA (PubMed:10026213, PubMed:12186975, PubMed:9154821). SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes (PubMed:10026213). At the promoters, SAGA is required for recruitment of the basal transcription machinery (PubMed:10026213). It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8) (PubMed:10026213). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac) (PubMed:10026213). SAGA interacts with DNA via upstream activating sequences (UASs) (PubMed:10026213). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation (PubMed:12186975). The ADA histone acetyltransferase complex preferentially acetylates nucleosomal histones H3 (to form H3K14ac and H3K18ac) and H2B, leading to transcription regulation (PubMed:9154821). SLIK is proposed to have partly overlapping functions with SAGA (PubMed:12446794, PubMed:15647753). It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus (PubMed:15647753). In addition to histone acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA) and is able to mediate histone crotonylation (PubMed:31699900).
Homotrimer. Monomer. Homotrimeric in its unliganded state. Undergoes a trimer-monomer transition upon acetyl-lysine substrate binding.
Inhibited by ADP-ribose and nicotinamide.
NAD-dependent histone deacetylase that is involved in nuclear silencing events. Derepresses subtelomeric silencing and increases repression in nucleolar (rDNA) silencing. Its function is negatively regulated by active nuclear export.
Present with 5260 molecules/cell in log phase SD medium.
Present with 8760 molecules/cell in log phase SD medium.
The N-terminal domain binds to adenylyl cyclase, thereby enabling adenylyl cyclase to be activated by upstream regulatory signals, such as Ras. The C-terminal domain is required for normal cellular morphology and growth control.
Component of a COP9 signalosome-like (CSN) complex, composed of RRI1/CSN5, CSN9, RRI2/CSN10, PCI8/CSN11, CSN12 and CSI1. In the complex, it probably interacts directly with RRI1/CSN5, CSN9, RRI2/CSN10 and CSI1. Interacts with SEM1 and THP3.
Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes. The CSN complex is involved in the regulation of the mating pheromone response. CSN12 forms a complex with THP3 that is recruited to transcribed genes and required for transcription elongation.
Present with 1510 molecules/cell in log phase SD medium.
Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
Histone methyltransferase that trimethylates histone H3 'Lys-36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression. The methyltransferase activity requires the recruitment to the RNA polymerase II, which is CTK1 dependent.
Interacts with the RNA polymerase II hyperphosphorylated CTD. Interacts with CYC8.
The AWS and SET domains are necessary for transcription repression.
Belongs to the metallophosphoesterase superfamily. MPPE1 family.
Present with 583 molecules/cell in log phase SD medium.
Probable metallophosphoesterase which may participate in recombinational repair of double -strand breaks.
Not known; weak suppressor of a mutant of the subunit AC40 of DNA dependent RNA polymerase I and III.
Present with 12900 molecules/cell in log phase SD medium.
Cells with a reduced level of SEC39 show a defect in post-translational processing of PRC1/CPY.
Component of a peripheral membrane protein complex consisting of DSL1, SEC39/DSL3 and TIP20. Bound to a SNARE complex consisting of UFE1, USE1, SEC20 and SEC22 or YKT6 through direct interaction of TIP20 with SEC20. Interacts with TIP20 and DSL1.
Constituent of COPII-coated endoplasmic reticulum-derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi (PubMed:11157978, PubMed:12426381). The C-terminal Ile-Leu motif is required for exit from the endoplasmic reticulum (PubMed:12426381). Facilitates retrograde transport from the Golgi to the endoplasmic reticulum (PubMed:12426381).
Present with 3000 molecules/cell in log phase SD medium.
Belongs to the polyprenol kinase family.
Involved in the synthesis of the sugar donor Dol-P-Man which is required in the synthesis of N-linked and O-linked oligosaccharides and for that of GPI anchors. It is required for spore germination. Has an essential role in cellular metabolism.
Belongs to the RNA polymerase beta' chain family.
Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA.
DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. RPA190 and RPA135 both contribute to the polymerase catalytic activity and together form the Pol I active center. In addition, subunit RPA12 contributes a catalytic zinc ribbon that is required for RNA cleavage by Pol I. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA190 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition.
Belongs to the adenylate kinase family. AK6 subfamily.
Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has also ATPase activity (By similarity). Involved in 18S rRNA maturation. Required for cleavage of the 20S pre-rRNA at site D in the cytoplasm. Involved in oxidative stress response. Required for POS9-dependent target gene transcription upon oxidative stress.
Interacts with RPS14B. Not a structural component of 43S pre-ribosomes, but transiently interacts with them with them by binding to RPS14.
Present with 8350 molecules/cell in log phase SD medium.
Required for cytoplasm to vacuole transport (Cvt) vesicle formation and efficient autophagy. Plays a role in ATG protein retrieval from the pre-autophagosomal structure (PAS) and is especially required for autophagy-dependent cycling of ATG9. Also plays a role in regulation of filamentous growth.
Essential protein which may be involved in threonine biosynthesis.
Belongs to the mitochondrion-specific ribosomal protein mS38 family.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (PubMed:25609543, PubMed:28154081). mS38 is also involved in the splicing of the COX1 mRNA (PubMed:16339141).
Belongs to the eukaryotic ribosomal protein eS27 family.
Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety in natural or engineered linear fusion proteins, irrespective of their size or the presence of an N-terminal extension to ubiquitin (PubMed:12778054, PubMed:17632125). Plays a role in regulation of silencing by interacting with SIR4 (PubMed:8752220). Also, in conjunction with BRE5, cleaves ubiquitin, leading to the subsequent mono-ubiquitination of SEC23 (PubMed:12778054). Required for ribophagy, a process which relocalizes ribosomal particles into the vacuole for degradation in response to starvation (PubMed:20508643).
Heterotetramer with BRE5; contains two molecules of BRE5 and two molecules of UBP3 (PubMed:12778054, PubMed:17632125). Forms a complex composed of CDC48, DOA1, deubiquitinase UBP3 and probably BRE5. Within the complex interacts directly with DOA1 and CDC48 in a BRE5-independent manner (PubMed:20508643).
Constituent of COPII-coated endoplasmic reticulum-derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. The C-terminal di-lysine motif is required for exit from the endoplasmic reticulum. Required directly for packaging glycosylated pro-alpha-factor into COPII vesicles. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum.
In TFIID, TAF13 heterodimerizes with TAF11, but they do not seem to form a heterotetramer like TAF6/TAF9. The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14.
Microtubule binding protein that promotes the stabilization of dynamic microtubules. Required for separation of the spindle poles during mitotic spindle formation. May cross-link overlapping antiparallel microtubules in the spindle midzone.
Self-associates. Interacts with microtubules via the TUB2 subunit.
Cells have a slow growth phenotype that is exacerbated at 37 degrees Celsius. Deletion mutants have a significant pre-mRNA leakage at 25 degrees Celsius.
Component of the 45S U1.U2.U4/U6.U5 penta-snRNP particle, a subcomplex of the spliceosome. Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Belongs to the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3 and PML1. Subunit of the U2 snRNP. Interacts with RDS3.
Required for pre-mRNA splicing and spliceosome assembly. As part of the pre-mRNA retention and splicing (RES) complex, required for nuclear pre-mRNA retention and efficient splicing. Required for MER1-activated splicing.
Associates with the ORC complex and the MCM2-7 helicase complex. Interacts with CDC4, CDC28, DIA2, ORC1, and TOM1.
Phosphorylated by CDC28. Phosphorylation is a prerequisite to ubiquitination and degradation.
Plays a crucial role in forming the pre-replicative complexes. Interacts with the origin recognition complex (ORC) and MCM2-7 helicase complex leading to the linking of those complexes and loading of the replicative helicase MCM2-7 onto the pre-replicative complexes. Required for the initiation of DNA replication and then actively participates in the suppression of nuclear division.
Transcribed at the end of mitosis, but in cells with a prolonged G1 phase there is a second burst of transcription in late G1.
Ubiquitinated by the E3 ubiquitin ligase complex SCF(CDC4), DIA2, and TOM1; and targeted to the 26S proteasome for degradation.
Abundant in stationary phase (G0) cells. mRNA levels rapidly decrease upon exit from G0.
Belongs to the cyanamide dehydrase family.
Cyanamide hydratase involved in the detoxification and/or utilization of cyanamide, a toxic nitrile compound distributed widely in the environment.
DDI2 and DDI3 are duplicated genes located on different chromosomes, with identical ORF sequences and only one nucleotide difference in their promoter (up to 1 kb) regions.
Expression is induced by DNA-damaging agents such as methyl methanesulfonate (MMS) or dimethyl sulfate (DMS) (PubMed:18485869, PubMed:25847245). Massively induced by cyanamide (PubMed:25847245).
The double deletion of DDI2 and DDI3 compromizes cellular resistance to cyanamide by impairing its metabolization.
Interacts with SNF7 with its BRO1 domain. Interacts with RIM101 with its C-terminal domain, probably binding to its two YPX[LI] motifs.
Present with 2881 molecules/cell in log phase SD medium.
Required for the proteolytic cleavage of the transcriptional repressor RIM101 in response to alkaline ambient pH, which is necessary for sporulation and invasive growth. May act as a scaffold protein that recruits the calpain-like protease RIM13 via SNF7 to its substrate RIM101.
May participate in assembly and/or disassembly of proteins imported into the mitochondrion. HSP60 are ATPases and have affinity for unfolded proteins.
Required for (1->6)-beta-D-glucan synthesis and normal cell growth.
Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family.
Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA. Interacts with RPA2/RPA135. Peripheral subunit that binds the catalytic zinc ion that is required for RNA cleavage. The heterodimer formed by RPA34 and RPA49 stabilizes subunit RPA12 and stimulates RPA12-dependent RNA cleavage. Involved in the recruitment of RPA49 to Pol I.
DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. Proposed to contribute to the polymerase catalytic activity and form the polymerase active center together with the two largest subunits. Subunit RPA12 contributes a catalytic zinc ribbon that is required for RNA cleavage by Pol I. Involved in transcriptional termination.
Present with 8450 molecules/cell in log phase SD medium.
Multiply phosphorylated in a cell-cycle-dependent manner with the major phosphorylation occurring in mitosis.
Acts as essential component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events.
Component of the conserved oligomeric Golgi (COG or Sec34/Sec35) complex which consists of eight different proteins COG1-COG8.
The side chain of Thr-30 acts as nucleophile, and the N-terminal amino group acts as proton acceptor.
Present with 952 molecules/cell in log phase SD medium.
Present with 66400 molecules/cell in log phase SD medium.
Component of the TOM (translocase of outer membrane) receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. TOM6 is involved in assembly and stability of the TOM complex.
Forms part of the TOM (translocase of outer membrane) complex that consists of at least 7 different proteins (TOM5, TOM6, TOM7, TOM20, TOM22, TOM40 and TOM70).
Impaired respiratory growth and sensitivity to 4-(N-(S-glutathionylacetyl)amino) phenylarsenoxide (GSAO).
Component of the N-terminal acetyltransferase A (NatA) complex, which is composed of ARD1, NAT1 and NAT5. Can self-associate. NAT1 associates with the nascent polypeptide chain and the ribosome.
Non-catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover. NAT1 anchors ARD1 and NAT5 to the ribosome and may present the N termini of nascent polypeptides for acetylation.
Involved in the uptake of non-siderophore sources of iron and the siderophores ferrioxamine B and ferrichrome. Has a role in the retention of iron in the cell wall and periplasmic space.
Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of STP22, VPS28, SRN2 and MVB12 in a 1:1:1:1 stoichiometry. Interacts with STP22 and MVB12.
Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for normal endocytic and biosynthetic traffic to the yeast vacuole.
Component of the TFIIIC complex composed of TFC1, TFC3, TFC4, TFC6, TFC7 and TFC8. The subunits are organized in two globular domains, tauA and tauB, connected by a proteolysis-sensitive and flexible linker. Interacts with TFC1, TFC4 and TFC6.
TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauB domain of TFIIIC that binds boxB DNA promoter sites of tRNA and similar genes. TFC3 is essential for cell viability. Cooperates with TFC6 in DNA binding.
Transcription factor that regulates CIT2 gene expression. Binds to two identical sites oriented as inverted repeats 28 bp apart in a regulatory upstream activation sequence element (UASR) in the CIT2 promoter. The core binding site is 5'-GGTCAC-3'.
the 9aaTAD motifs are transactivation domains present in a large number of yeast and animal transcription factors.
Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Belongs to the proteasome subunit S3 family.
Present with 16700 molecules/cell in log phase SD medium.
The 26S proteasome is composed of a core protease, known as the 20S proteasome, capped at one or both ends by the 19S regulatory complex (RC). The RC is composed of at least 18 different subunits in two subcomplexes, the base and the lid, which form the portions proximal and distal to the 20S proteolytic core, respectively (By similarity).
Belongs to the snRNP core protein family.
C-terminal extension may function as a nuclear localization signal (NLS).
Component of the Sm core complex, present in spliceosomal snRNP U1, U2, U4/U6 and U5. The core complex contains SMB1, SMD1, SMD2, SMD3, SME1, SMX3 and SMX2 (Sm proteins B, D1, D2, D3, E, F and G, respectively), and is probably a heptameric ring structure. Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
Present with 2400 molecules/cell in log phase SD medium.
lays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (PubMed:8430095). Also binds telomerase RNA and is required for its accumulation (PubMed:10490028).
Components of the endosome-vacuole trafficking pathway that regulates nutrient transport. May be involved in processes which determine whether plasma membrane proteins are degraded or routed to the plasma membrane (By similarity).
In the C-terminal section; belongs to the trehalose phosphatase family.
In the N-terminal section; belongs to the glycosyltransferase 20 family.
Phosphatase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process.
The trehalose synthase complex is composed of the two catalytic subunits TPS1 and TPS2, and at least one of the two regulatory subunits TPS3 or TSL1.
Essential component of the U1 snRNP particle, which recognizes and binds the 5'-splice site of pre-mRNA. Together with other non-snRNP factors, U1 snRNP forms the spliceosomal commitment complex, that targets pre-mRNA to the splicing pathway. U1 snRNP is cotranscriptionally recruited to intron-containing genes. Required for U1 snRNP biogenesis.
Belongs to the universal ribosomal protein uL14 family.
Present with 2500 molecules/cell in log phase SD medium.
In complex with CCZ1, is required for multiple vacuole delivery pathways including the cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and endocytosis. The CCZ1-MON1 complex acts at the fusion of vesicles with the vacuole, through its regulation of the SNARE complex during the coordinated priming and docking stages of fusion, and particularly at the stage of tethering/docking (PubMed:12134085, PubMed:12364329, PubMed:12387888, PubMed:14662743, PubMed:15721293). The CCZ1-MON1 complex acts as a guanine nucleotide-exchange factor (GEF) for Rab-type GTPase YPT7, promoting nucleotide exchange on YPT7 and triggering endosomal maturation by activating YPT7 on late endosomes (PubMed:20797862).
Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Component of the mitochondrial small ribosomal subunit. Mature mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S subunit contains at least 33 different proteins and 1 molecule of RNA (15S). The 54S subunit contains at least 45 different proteins and 1 molecule of RNA (21S).
Involved in the assembly of cytochrome c oxidase.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.
Methyltransferase that catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. Both the D-stem and T-stem structures of tRNAs are required for efficient methyltransferase activity.
Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2.
mRNA splicing factors, PRP9, PRP11, and PRP21, are necessary for binding of the U2 snRNP to the pre-mRNA in an early step of spliceosome assembly.
During the catalytic reaction, a sulfide is transferred from Cys-205 to a reaction intermediate, generating a dehydroalanine residue.
Expressed at high levels in the early stationary phase of batch cultures growing on molasses, an industrial medium.
Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance.
Belongs to the eukaryotic ribosomal protein eS6 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). eS6 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835).
Present with 38800 molecules/cell in log phase SD medium.
Present with 66000 molecules/cell in log phase SD medium.
Associates with the SIT4 phosphatase in a cell cycle dependent manner. May be directly or indirectly involved in SIT4-dependent functions in budding and in normal G1 cyclin expression (By similarity).
Interacts with the 40S and 60S ribosomal subunits. Interacts with microtubules.
Involved in protein synthesis. Involved in microtubule stabilization.
Present with 27800 molecules/cell in log phase SD medium.
Probable transcription activator linked to cell cycle that induces transcription activation of genes in the environmental stress response and metabolism control pathways, like the closely related YAP5.
Belongs to the eukaryotic RPC34/RPC39 RNA polymerase subunit family.
Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. Interacts with BRF1/TDS4.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Involved in recruitment of Pol III to the preinitiation complex. Involved in the configuration of an initiation-competent form of RNA polymerase.
Necessary for use of certain peptides as sole nitrogen source. May also cleave intracellularly generated peptides to recycle amino acids for protein synthesis.
The transmembrane domain contains polar residues that mediate the recognition by TUL1.
Ubiquitinated. Ubiquitination mediates sorting into internal vesicles in late endosomes. TUL1 is required for ubiquitination.
yscS is synthesized as one polypeptide chain precursor which after carbohydrate modification in the secretory pathway yields two active precursor molecules. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble.
GTPase-activating protein for the ADP ribosylation factor (ARF) family. Involved in retrograde vesicular transport from the Golgi to the endoplasmic reticulum.
Negative regulator of cell wall integrity (CWI) in unstressed cells, probably by inhibiting protein kinase PKH1/PHK2 activity and regulating their downstream CWI pathways PKC1-MAP kinase pathway and protein kinase YPK1 pathway. Activity may be regulated by the transient increase of sphingolipid long chain bases (LCBs) during heat stress.
Phosphorylated by PKH1 and PKH2. Phosphorylation is inhibited by sphingolipid long chain bases (LCBs).
Belongs to the clathrin heavy chain family.
Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. In yeast, it is involved in the retention of proteins in an intracellular membrane compartment, presumably the trans-Golgi.
Clathrin triskelions, composed of 3 heavy chains and 3 light chains, are the basic subunits of the clathrin coat. Interacts with the auxilin-like clathrin uncoating factor SWA2. Interacts with INP53.
Present with 28700 molecules/cell in log phase SD medium.
The C-terminal third of the heavy chains forms the hub of the triskelion. This region contains the trimerization domain and the light-chain binding domain involved in the assembly of the clathrin lattice.
The N-terminal seven-bladed beta-propeller is formed by WD40-like repeats, and projects inward from the polyhedral outer clathrin coat. It constitutes a major protein-protein interaction node (By similarity).
Belongs to the CND2 (condensin subunit 2) family.
Hydrolyzes sugar alcohol (polyol) phosphates (PubMed:30240188). Dephosphorylates a variety of substrates, including: sn-glycerol 1-phosphate (D-glycerol 3-phosphate), D-ribitol 5-phosphate, D-sorbitol 6-phosphate (D-glucitol 6-phosphate), and D-erythrose 4-phosphate (PubMed:30240188). Prevents accumulation of toxic levels of polyol phosphates, which can impair glycolysis by inhibiting glucose-6-phosphate isomerase (PubMed:30240188).
Impairs the ability to metabolize cellular polyol phosphates which may build up to toxic levels in cells.
Present with 12600 molecules/cell in log phase SD medium.
Unlike the glycerol-1-phosphate phosphohydrolases, this enzyme cannot hydrolyze L-glycerol 3-phosphate (sn-glycerol 3-phosphate) and is therefore not associated with EC 3.1.3.21 / RHEA:11476.
Interacts with NIP7 and RRP43. Together with DBP6, URB1, URB2 and RSA3, forms an RNA-independent complex, which is required during early maturation of nascent 60S ribosomal subunits.
Required for 60S ribosomal subunit synthesis. May be involved in assembly reactions occurring within late pre-ribosomal particles.
Belongs to the NADH dehydrogenase family.
External NADH dehydrogenase required for optimum cellular growth with a number of nonfermentable carbon sources, including ethanol. With NDE1, performes the mitochondrial oxidation of cytosolic NADH under these growth conditions. Regulates the mitochondrial glycerol-3-phosphate dehydrogenase, GUT2, also involved in cytosolic NADH oxidation.
A combined deletion of the OSW7 and SHE10 has reduced dityrosine incorporation in the outer spore wall.
Abnormal prospore membrane formation (PubMed:22611022, PubMed:24036347). Abolishes localization of VPS13 to the prospore membrane (PubMed:24036347). Accumulation of vesicles within the prospore membrane lumen and reduction of phosphatidylinositol in the membrane (PubMed:24036347). Abnormal spore wall formation; the first three layers are synthesized but abnormally deposited and the dityrosine layer is missing (PubMed:22611022). Sporulation specific septins are mislocalized (PubMed:22611022).
Expressed during sexual reproduction; expression increases during meiosis II (at protein level).
Interacts (via PxP motif) with VPS13 (via SHR-BD domain); during prospore membrane formation.
Recruits the lipid transfer protein VPS13 to the prospore membrane during sporulation, thereby aiding prospore membrane formation.
Acts as essential component of the kinetochore MIND complex, which is required for the spindle checkpoint and kinetochore integrity. MIND plays a role in establishing a bipolar spindle-kinetochore interaction by joining kinetochore subunits contacting DNA to those contacting microtubules.
Component of the MIND kinetochore complex, which is composed of at least MTW1, NNF1, NSL1 and DSN1. Interacts with NSL1.
Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is required for transcription of ribosomal protein genes and genes involved in the integrity of the cell wall. Together with HTL1, LDB7, NPL6, RSC3 components, defines a fungal-specific module within the RSC complex that plays a role in many cellular functions including the maintenance of cell wall integrity.
Forms a heteromer with RSC3. Interacts with NPL6. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin. Component of a fungal-specific module (HTL1-LDB7-NPL6-RSC3-RSC30) within the RSC complex.
Component of a COP9 signalosome-like (CSN) complex, composed of at least RRI1/CSN5, CSN9, RRI2/CSN10, PCI8/CSN11, CSN12 and CSI1. In the complex, it probably interacts directly with CSN12.
Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes. The CSN complex is involved in the regulation of the mating pheromone response.
Belongs to the peptidase C19 family. UBP8 subfamily.
Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. UBP8 interacts with SGF11. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, TAF10 and TAF9.
Functions as histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. Together with SGF11, is required for histone H2B deubiquitination.
Present with 1030 molecules/cell in log phase SD medium.
The UBP-type zinc finger domain is required for the interaction with the SAGA complex.
Component of the global genome repair (GGR) complex composed of at least ABF1, RAD7 and RAD16 (PubMed:10601031). Interacts with ELC1 (PubMed:19920177).
Component of the global genome repair (GGR) complex which promotes global genome nucleotide excision repair (GG-NER) which removes DNA damage from nontranscribing DNA. This protein is one of 10 proteins (RAD1, 2,3,4,7,10,14, 16,23 and MMS19) involved in excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents.
Mutants with mutations in the RAD7, RAD14, RAD16, and RAD23 genes show partial incision defectiveness.
Component of a heterotrimeric complex containing IMP3, IMP4 and MPP10. Interacts with MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.
Required for the early cleavages at sites A0, A1 and A2 during 18S ribosomal pre-RNA processing.
Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M).
Early stages of growth after spore germination.
Present with 8940 molecules/cell in log phase SD medium.
Accumulates recombination intermediates blocked at the RAD1/RAD10-dependent 3' flap cleavage step. Abolishes association of RAD1 at single-strand annealing (SSA) intermediates. Insensitive to MMS, HU, or phleomycin treatment. Doesn't sensitize cells to UV lesions. Substantially increases the rDNA recombination rate.
Catalyzes 3'-non-homologous tail removal of RAD1/RAD10-dependent single-strand annealing recombination intermediates. Plays a key role in targeting RAD1/RAD10 complex to 3'-flap cleavage substrate in recombination. Also contributes to the integrity of ribosomal DNA arrays.
Interacts with MSH2, MSH3, RAD1, RAD10, RAD51 and RAD52.
Acts as a component of the essential kinetochore-associated NDC80 complex, which is involved in chromosome segregation and spindle checkpoint activity.
Component of the NDC80 complex, which consists of NDC80, NUF2, SPC24 and SPC25. The NDC80 complex is formed by two subcomplexes, NDC80-NUF2 and SPC24-SPC25, which are joined end-to-end through their coiled-coil domains. It has a rod-like structure with a length of 570 Angstroms and globular domains at either end. The NDC80-NUF2 globular domains are probably directed to microtubules, the SPC24-SPC25 globular domains to the centromere. NDC80 probably interacts with SMC1 and SMC2. Also interacts with KIN3. Interacts with DMC1.
Belongs to the mitochondrial pyruvate carrier (MPC) (TC 2.A.105) family.
Grows more slowly in amino acid-free medium (SD), when combined with disruption of MPC2.
Mainly expressed when grown on lactate containing growth medium (PubMed:22628554). Expression regulated by osmotic and alkaline stresses (PubMed:15299026, PubMed:16087739, PubMed:17334841). Under the control of the SKO1 transcription factor (PubMed:16087739).
Mediates the uptake of pyruvate into mitochondria.
Present with 6750 molecules/cell in log phase SD medium.
The functional 150 kDa pyruvate import complex is a heteromer of MPC1 and either MPC2 or MPC3.
Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L-allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate.
Present with 3210 molecules/cell in log phase SD medium.
Belongs to the major facilitator superfamily. DHA1 family. Polyamines/proton antiporter (TC 2.A.1.2.16) subfamily.
By transcription factor HAA1 in response to acetaldehyde accumulation.
Cell membrane polyamine/proton antiporter, involved in the detoxification of excess polyamines in the cytoplasm. Recognizes spermine, but not spermidine.
Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family.
Forms homooligomers. Interacts with MRS2.
Mitochondrial inner membrane magnesium transporter required for mitochondrial magnesium homeostasis. Modulates the conductance of the MRS2 channel. Involved in the splicing of mRNA group II introns in mitochondria by affecting mitochondrial magnesium concentrations, which are critical for group II intron splicing.
N-glycosylated. Glycosylation is important for correct localization of the protein.
Forms oligomers and is present in high-molecular-mass complexes. Interacts with ARL1.
Involved in vesicular transport between an endosomal compartment and the Golgi apparatus.
The GRIP domain may serve as a Golgi targeting domain through its interaction with the ARL1 Golgi protein.
Belongs to the type II topoisomerase family.
Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes.
Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils.
In yeast topoisomerase II can substitute topoisomerase I for the relaxing activity.
Phosphorylation enhances the activity. Stimulates decatenation activity.
Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane. Cleaves precursor proteins of respiratory components, including subunits of the electron transport chain and tricarboxylic acid cycle enzymes, and components of the mitochondrial genetic machinery, including ribosomal proteins, translation factors, and proteins required for mitochondrial DNA metabolism.
Simultaneous disruption of the mitochondrial presequence protease CYM1 results in synthetic lethality in respiratory conditions.
Belongs to the RecA family. RAD55 subfamily.
Required for radiation resistance and meiotic viability and presumably acts in recombination and recombinational DNA repair pathways.
Belongs to the universal ribosomal protein uS9 family.
Belongs to the P-Pant transferase superfamily. AcpS family.
Catalyzes the transfer of a 4'-phosphopantetheine moiety from coenzyme A to a serine residue of acceptor proteins, such as alpha-aminoadipate reductase. Necessary for alpha-aminoadipate reductase activity.
Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family.
Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34 (PubMed:8516295, PubMed:11717393, PubMed:12407181, PubMed:18160037, PubMed:24153184, PubMed:24153182). The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA. Component of the RNA polymerase III (Pol III) complex consisting of at least 17 subunits (PubMed:8516295, PubMed:10384303, PubMed:10393904). Interacts with the RPC19/RPAC2 (PubMed:8516295) and RPC53/RPC4 (PubMed:10393904). Interacts with retrotransposons Ty integrase, targeting Ty1, Ty2 and Ty4 integration upstream of pol III-transcribed genes (PubMed:25931562).
DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I (Pol I) and III (Pol III) which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively. RPC40 is part of the polymerase core and may function as a clamp element that moves to open and close the cleft (PubMed:18160037, PubMed:24153182, PubMed:24153184). Plays an important role in targeting retrotransposons Ty integration upstream of pol III-transcribed genes such as tRNA genes, allowing Ty1, Ty2 and Ty4 to proliferate and yet minimizing genetic damage (PubMed:25931562).
Present with 13000 molecules/cell in log phase SD medium.
Binds 2 magnesium or manganese ions per subunit.
Responsible, together with PTC3, for the dephosphorylation of the cyclin-dependent protein kinase CDC28.
Belongs to the SIMIBI class G3E GTPase family. ZNG1 subfamily.
Zinc chaperone that directly transfers zinc cofactor to target metalloproteins, thereby activating them (PubMed:35584675). Catalyzes zinc insertion into the active site of methionine aminopeptidase MAP1, which function to cleave the initiator methionine from polypeptides during or after protein translation (PubMed:35584675). Mechanistically, the N-terminal psi-PxLVp motif binds to the C6H2-type zinc finger of inactive form of MAP1 (PubMed:35584675). After formation of the docked complex, zinc is transferred from the CXCC motif in the GTPase domain of ZNG1 to the zinc binding site in the peptidase domain of MAP1 in a process requiring GTP hydrolysis (PubMed:35584675). GTP/GDP exchange is required for release of active MAP1 (PubMed:35584675).
Putative cyclin-dependent kinase (CDK) inhibitor necessary and sufficient for PHO pathway-dependent down-regulation of low-affinity phosphate transport.
Regulated by phosphate, probably through its PHO4-binding elements in the promoter.
Acts as a component of chromatin assembly factor 1 (CAF-1), which assembles histone octamers onto replicating DNA in vitro. It performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. p90 may facilitate the efficient and timely assembly of histones into telomeric chromatin.
Component of chromatin assembly factor 1 (CAF-1), which is composed of MSI1/p50, CAC2/p60 and RLF2/CAC1/p90. RLF2 interacts with SAS2.
Cleaves internal linkages in 1,3-beta-glucan.
May play a role in insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
As part of the replication protein A (RPA/RP-A), a single-stranded DNA-binding heterotrimeric complex, may play an essential role in DNA replication, recombination and repair. Binds and stabilizes single-stranded DNA intermediates, preventing complementary DNA reannealing and recruiting different proteins involved in DNA metabolism (By similarity). Stimulates the activity of a cognate strand exchange protein (SEP1).
Belongs to the replication factor A protein 3 family.
Component of the heterotrimeric canonical replication protein A complex (RPA).
Belongs to the membrane-bound acyltransferase family.
Broad specificity membrane-bound O-acyltransferase that mediates the incorporation of unsaturated acyl chains into the sn-2 position of various lysophospholipids. Preferentially acylates lysophosphocholine (LPC), but also lysophosphoethanolamine (LPE), lysophosphatidylglycerol (LPG), lysophosphatidic acid (LPA), lysophosphoethanolamine (LPE), lysophosphoinositol (LPI), and lysophosphoserine (LPS) (PubMed:17996202, PubMed:17652094, PubMed:17726007, PubMed:17675291, PubMed:17890783). Prefers an acyl residue to an alkyl residue at the sn-1 position of lysophospholipid acceptors. Accepts acyl chains in acyl-CoA from C-2 to C-20, and shows strong preference for unsaturated acyl-CoAs with 16-20 carbons (PubMed:17890783). Together with SLC1, plays a central role in phosphatidic acid (PA) biosynthesis. PA is the intermediate, from which all glycerophospholipids are synthesized (PubMed:17890783). Can also introduce an acyl chain at the sn-1 position of the lysophosphatidylcholine analog 1-hydroxy-2-hexadecyl-sn-glycero-3-phosphocholine (HHPC) (PubMed:29782033).
Belongs to the clathrin light chain family.
CLC1 binds calcium, and calmodulin in presence of calcium.
Clathrin coats are formed from molecules containing 3 heavy chains and 3 light chains. Interacts with the auxilin-like clathrin uncoating factor SWA2.
Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. In yeast, it is involved in the retention of proteins in an intracellular membrane compartment, presumably the trans-Golgi. The yeast light chain is important for cell growth. The light chain may help to properly orient the assembly/ disassembly of the clathrin coats.
Erroneous sequence assembling in the Ser-rich region leading to a longer sequence.
Involved in cell wall organization and biosynthesis.
Probable mannoprotein called haze protective factor from wine that is able to prevent visible wine protein haze formation. This mannoprotein showed haze-protective activity against wine proteins and BSA when either was heated in white wine.
Belongs to the glycosyl hydrolase 18 family. Chitinase class III subfamily.
Belongs to the eukaryotic RPB8 RNA polymerase subunit family.
Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes. Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA. Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits: RPO21, RPB2, RPB3, RPB4, RPB5, RPO26, RPB7, RPB8, RPB9, RPB10 and RPC10. Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. Directly interacts with POLR2A.
DNA-dependent RNA polymerases catalyze the transcription. of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.
Component of the SAS complex, a multiprotein complex that acetylates 'Lys-16' of histone H4 and 'Lys-14' of histone H3. The SAS complex is however unable to acetylate nucleosomal histones. The complex is involved in transcriptional silencing at telomeres and at HML locus. Also involved in rDNA silencing. In the complex, SAS5 is required for maximal histone acetyltransferase (HAT) activity of the complex, suggesting that it may be required to stabilize the complex or help in substrate recognition.
Component of the SAS complex, at least composed of SAS2, SAS4 and SAS5. These three proteins constitute the core of the complex, and are sufficient to acetylate histones.
Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins).
Present with 14300 molecules/cell in log phase SD medium.
The activity of this enzyme increases in presence of mating pheromone (transcriptional regulation).
Forms SNARE complexes with the t-SNAREs VAM3 and VAM7, and the v-SNAREs NYV1 and YKT6 on vacuolar membranes, which are involved in biosynthetic transport pathways to the vacuole and in homotypic vacuole fusion. Forms SNARE complexes with the cis-Golgi t-SNARE SED5 and the v-SNAREs SFT1 and YTK6, which are involved in retrograde traffic to the cis-Golgi compartment. Forms SNARE complexes with the t-SNAREs TLG1 and TLG2, and either the v-SNARE SNC1 or SNC2, which are involved in traffic from early endosomes to the trans-Golgi network (TGN). Forms SNARE complexes with the t-SNAREs PEP12 and either SYN8 or TLG1, and the v-SNARE SNC1, which are involved in traffic from the TGN to the prevacuolar compartment (PVC).
t-SNARE found in various SNARE complexes involved in multiple transport pathways. The composition of the t-SNARE complexes is specific for a limited number of v-SNAREs and therefore allows only the vesicles carrying the matching v-SNARE to fuse.
Component of the 7-subunit TFIIH core complex composed of XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in NER. The core complex associates with the 3-subunit CTD-kinase module TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription (PubMed:7961739, PubMed:14500720, PubMed:9235928). Interacts with TFB5 (PubMed:19172752).
Present with 8900 molecules/cell in log phase SD medium.
Plays a role in facilitating the assembly of some protein complexes inside the mitochondria. It may initiate the events that lead to refolding of imported precursors in the matrix space.
Belongs to the small GTPase superfamily. Rho family.
Leads to resistance to oxidants such as H(2)O(2) (PubMed:25598154). Impairs apoptotic phenotype after H(2)O(2) treatment (PubMed:25598154). Leads to hyper-resistance to cell wall stress agents such as calcofluor white and Congo red (PubMed:25598154).
Small GTPase that negatively regulates a MAP kinase branch, downstream of SLT2, of the PKC1-mediated signal transduction pathway (PubMed:12118069). With its specific guanine nucleotide exchange factor (GEF), the heterodimeric complex DCK1/LMO1, relocates to mitochondria upon oxidative stress and triggers cell death (PubMed:25598154). The DCK1/LMO1/RHO5 signaling module that mediates mitochondrial turnover under nitrogen starvation conditions via mitophagy (PubMed:25598154). The DCK1/LMO1/RHO5 signaling module also plays a role in cell wall integrity signaling (PubMed:25598154).
Allosteric enzyme whose activity is greatly influenced by the end products of its metabolic pathway, dCTP and dTTP.
Belongs to the cytidine and deoxycytidylate deaminase family.
Catalyzes the hydrolytic deamination of dCMP to yield dUMP, the nucleotide substrate for thymidylate synthetase.
Transports tetra- and pentapeptides. Does not transport glutathione.
Belongs to the Nudix hydrolase family. NudC subfamily.
mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some RNAs; in contrast to the canonical N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Mediates the hydrolysis of some nucleoside diphosphate derivatives (PubMed:11361135).
Belongs to the mitochondrion-specific ribosomal protein mL54 family.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (PubMed:24675956, PubMed:25609543). mL54 may have a meiosis-specific role as it accumulates during the middle stage of sporulation (PubMed:15543521).
DsRNA-specific nuclease that cleaves eukaryotic pre-ribosomal RNA at the U3 snoRNP-dependent A0 site in the 5'-external transcribed spacer (ETS) and in the 3'-ETS. In vitro, cleaves synthetic 5'-ETS RNA A0 site in the absence of snoRNA or other factors. Has an essential growth function in addition to pre-rRNA processing.
Present with 4970 molecules/cell in log phase SD medium.
Acidic protein, which assembles histones into an octamer (in vitro). Involved in the regulation of the localization and the function of the septins during mitosis. Involved in the function of B-type cyclins.
Belongs to the nucleosome assembly protein (NAP) family.
Component of the GIN4 complex composed of at least BNI5, CDC3, CDC10, CDC11, CDC12, GIN4, NAP1 and SHS1 which forms a ring at the bud neck (PubMed:12058072). Homodimer (in-vitro) (PubMed:16432217). Interacts with the B-type cyclin CLB2 (PubMed:7622566). Interacts with 60S ribosomal protein L18 (RPL18A or RPL18B), CKA2, CKI1, eukaryotic elongation factor 1 complex eEF1A (TEF1 or TEF2), FOL1, HSC82, HTA2, HTB2, HTZ1, KAP114, KCC4, NIS1, SSA1, SSA2, SSB1, SSC1, SHM1, SIP5 and TCO89 (PubMed:18086883). Interacts with NBA1 (PubMed:18086883). Interacts with histone H3/H4 heterodimers (PubMed:27036862).
Exhibits a large proportion of multinucleate cells. Elongated buds. The percentage of elongated buds is significantly increased when GIN4 or CKI1 is also deleted. Small decrease in the percentage of cells with elongated buds is observed in NAP1 and CKA2 double mutant. NAP1 and CKI1 double mutant exhibits increased sensitivity to benomyl. Increased resistance to benomyl in NAP1 and CKA2 double mutant.
NAP-I was previously referred to as AP-I.
Phosphorylation by CK2 is required for normal progression through S phase. CK2 phosphorylation is not required for correct bud formation nor histone binding.
Present with 8070 molecules/cell in log phase SD medium.
The acidic domains are probably involved in the interaction with histones.
Expression is increased in response to the addition of maltose, isomaltose, and alpha-methylglucopyranoside.
Major isomaltase (alpha-1,6-glucosidase) required for isomaltose utilization. Preferentially hydrolyzes isomaltose, palatinose, and methyl-alpha-glucoside, with little activity towards isomaltotriose or longer oligosaccharides. Does not hydrolyze maltose.
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Involved in cell cycle progression and meiosis.
Interacts with H3K4me3 and to a lesser extent with H3K4me2. Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, TRA1 and YNG2.
The PHD-type zinc finger mediates the binding to H3K4me3.
Belongs to the bacterial ribosomal protein bL36 family.
Component of the mitochondrial large ribosomal subunit (mt-LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. bL36m has a zinc binding site.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (PubMed:25609543, PubMed:24675956). bL36m may be involved in a process influencing telomere capping (PubMed:18845848, PubMed:20691087).
Present with 500 molecules/cell in log phase SD medium.
Palmitoyltransferase specific for casein kinase 1. Palmitoylates isoforms YCK1 and YCK2 at both C-terminal cysteine residues, which is required for their proper plasma membrane localization. Required for constitutive endocytosis of a-factor receptor STE3 and both constitutive and pheromone-induced endocytosis of alpha-factor receptor STE2.
Present with 4072 molecules/cell in log phase SD medium.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.
Binds 1 monovalent cation per monomer in the active site, which can be sodium or potassium. This structural cofactor stabilizes the GTP-bound 'on' state, and may also act as a transition state stabilizer of the hydrolysis reaction.
Plays a role in translation initiation (PubMed:9624054). Translational GTPase that catalyzes the joining of the 40S and 60S subunits to form the 80S initiation complex with the initiator methionine-tRNA in the P-site base paired to the start codon (PubMed:12507428, PubMed:12471154, PubMed:12008673). GTP binding and hydrolysis induces conformational changes in the enzyme that renders it active for productive interactions with the ribosome (PubMed:25478828). The release of the enzyme after formation of the initiation complex is a prerequisite to form elongation-competent ribosomes (PubMed:12507428, PubMed:18976658, PubMed:19029250). Stimulates 20S pre-rRNA cleavage to mature 18S rRNA by PIN-domain endonuclease NOB1 (PubMed:22751017).
Belongs to the universal ribosomal protein uL22 family.
Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). uL22 is associated with the polypeptide exit tunnel (PubMed:9559554, PubMed:22096102).
Essential in pre-tRNA processing. Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation.
Present with 3730 molecules/cell in log phase SD medium.
Homodimer. Binds DNA with a high specificity in complex with mating-type protein ALPHA1. Also binds DNA with a high specificity as a heterotetramer consisting of an ALPHA2 dimer and an MCM1 dimer. Interacts with YHP1 and YOX1, possibly leading to its inactivation. Interacts with ARG80 and ARG82.
Transcription factor required for the efficient replication of minichromosomes and the transcriptional regulation of early cell cycle genes. Activates transcription of ECB-dependent genes during the G1/M phase. Genes that contain a ECB (early cell box) element in their transcription regulatory region are transcribed only during G1/M phases. Interacts with the alpha-2 repressor or with the alpha-1 activator thereby regulating the expression of mating-type-specific genes. With ARG80, ARG81 and ARG82, coordinates the expression of arginine anabolic and catabolic genes in response to arginine.
Required for normal DNA replication. Phosphorylated in response to DNA replication stress. Phosphorylation allows it to mediate the activation of RAD53.
Component of the INA complex (INAC) that promotes the biogenesis of mitochondrial F(1)F(0)-ATP synthase. INAC facilitates the assembly of the peripheral stalk and promotes the assembly of the catalytic F(1)-domain with the membrane-embedded F(0)-domain.
Component of the inner membrane assembly (INA) complex, composed of INA17 and INA22. Interacts with a subset of F(1)F(0)-ATP synthase subunits of the F(1)-domain and the peripheral stalk.
May play a role in RNA metabolism, rRNA-processing, and in a process influencing telomere capping.
Present with 2430 molecules/cell in log phase SD medium.
Belongs to the ubiquitin-activating E1 family. UBA3 subfamily.
Catalytic subunit of the dimeric UBA3-ULA1 E1 enzyme. E1 activates NEDD8/RUB1 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBC12.
Heterodimer of UBA3 and ULA1. Interacts with NEDD8 and UBC12 (By similarity).
Belongs to the WD repeat coronin family.
Cleaves proteins C-terminally to the most C-terminal basic residue. Can process the alpha-mating factor precursor. Required for cell wall integrity.
Present with 4320 molecules/cell in log phase SD medium.
Belongs to the PNP/MTAP phosphorylase family.
The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine and inosine (By similarity).
Belongs to the CWC complex (or CEF1-associated complex), a spliceosome subcomplex composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with SLU7.
Involved in pre-mRNA splicing. Facilitates the cooperative formation of U2/U6 helix II in association with stem II in the spliceosome. Binds to RNA.
Present with 4260 molecules/cell in log phase SD medium.
Involved in apoptosis. May play a role in nuclear function controlling cellular proliferation coupled to mitochondrial biogenesis. Causes impaired growth when overexpressed.
Expressed periodically during cell division. Regulated by the SBF complex which is one critical regulator of the start of the cell cycle.
Transcriptional activator which promotes cell cycle recovery with CLN2, after pheromone induced G1 arrest, probably inhibiting the ability of STE20 to activate the pheromone response pathway. Binds the promoters of genes that function in cell cycle regulation, cytoskeletal organization, and spindle assembly. May also be involved in stress-resistance.
The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. MND2 interacts directly with APC1, APC5 and CDC23.
Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.
Interacts with NCS2 and URM1. May act by forming a heterodimer with NCS2. Component of a large molecular weight complex of more than 250 kDa.
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation. May also be involved in protein urmylation and in invasive and pseudohyphal growth.
In aerobic conditions. Expression is regulated by copper levels and the MAC1 copper-responsive transcription factor.
May be involved in mitochondrial iron or copper homeostatis.
Belongs to the glycosyltransferase 22 family.
Catalyzes the transfer of mannose from Dol-P-Man to lipid-linked oligosaccharides.
Required to activate transcription of PDR3, a gene involved in retrograde regulation of multidrug resistance, a phenomenon that takes place in cells that have lost their mitochondrial genome. Also required for ubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. Its precise role in H2BK123ub1 formation however is unclear and is independent of retrograde regulation of multidrug resistance function.
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Is constitutively expressed at moderate levels.
Component of the FEAR (CDC14 early anaphase release) network which promotes CDC14 release from the nucleolus during early anaphase and is required for the efficient segregation of telomeric and nucleolar regions. Although BNS1 can partially compensate for a lack of SPO12 function when overexpressed, it does not appear to play any role in controlling meiotic nuclear division.
Catalyzes the production of cysteine from cystathionine in the reverse transsulfuration pathway for the biosynthesis of sulfur-containing amino acids cysteine and methionine. In this pathway, homocysteine sulfur is converted to cysteine sulfur (Probable). Also has cystathionine beta-lyase and cystathionine gamma-synthase activities in vitro. Cystathionine beta-lyase may be physiological, while cystathionine gamma-synthase activity is not, as the required substrate O-succinyl-L-homoserine(OSH) does not occur naturally in S.cerevisiae (PubMed:8335636).
Present with 38300 molecules/cell in log phase SD medium.
As part of the ribosome quality control complex (RQC), a ribosome-associated complex, mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes as well as their ubiquitin-mediated proteasomal degradation. Thereby, frees ribosomes from the stalled translation complex and prevents the accumulation of nascent polypeptide chains that are potentially toxic for the cell (PubMed:23178123). RQC2 is responsible for selective recognition of stalled 60S subunits by recognizing an exposed, nascent chain-conjugated tRNA moiety (PubMed:25349383). RQC2 is important for the stable association of the E3 ubiquitin-protein ligase RKR1/LTN1 to the complex (PubMed:23479637). RQC2 is also able to recruit alanine- and threonine-charged tRNA to the A site and directs the elongation of stalled nascent chains independently of mRNA or 40S subunits, leading to non-templated C-terminal Ala and Thr extensions (CAT tails) (PubMed:25554787, PubMed:32934225). CAT tails induce a HSF1-dependent heat shock response (PubMed:25554787). CAT tails also promote the RKR1/LTN1-mediated ubiquitination of incompletely synthesized nascent polypeptides and their subsequent proteasomal degradation (PubMed:32934225).
Component of the ribosome quality control complex (RQC), composed of the E3 ubiquitin ligase RKR1/LTN1, RQC1 and RQC2, as well as CDC48 and its ubiquitin-binding cofactors associated with the 60S ribosomal subunit (PubMed:23178123, PubMed:23479637, PubMed:25349383). RQC2 binds to the 40S-binding surface of tRNAs (PubMed:25554787).
Belongs to the bacterial ribosomal protein bL27 family.
Component of multiple cullin-RING ligases (CRLs) composed of 4 subunits: the RING protein HRT1, the cullin RTT101, a linker protein MMS1, and one of many alternative substrate receptors belonging to a protein family described as DCAF (DDB1- and CUL4-associated factor). Component of a RTT101(MMS1-MMS22) complex with the substrate receptor MMS22. This complex further interacts with RTT107 and CTF4 to form RTT101-MMS1-MMS22-RTT107 and RTT101-MMS1-MMS22-CTF4 complexes respectively. Component of a RTT101(MSS1-CRT10) complex with the substrate receptor CRT10. Component of a RTT101(MSS1-ESC2) complex with the potential substrate receptor ESC2. Component of a RTT101(MSS1-ORC5) complex with the potential substrate receptor ORC5. Interacts with RTT101 (via N-ter). Interacts (via N-ter) with MMS22 (via C-ter). Interacts with CRT10.
Component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes (CRLs), which mediate the ubiquitination of target proteins. The CRL associates with CDC34 as the E2 ubiquitin-conjugating enzyme. The functional specificity of the CRL depends on the type of the associated substrate receptor protein. RTT101(MMS1-MMS22) promotes fork progression through damaged DNA or natural pause sites by stabilizing replication proteins like the replication fork-pausing complex (FPC) and leading-strand polymerase at stalled replication forks. RTT101(MMS1-MMS22) ubiquitinates the acetylated histones H3K56ac-H4 at lysine residues H3K121, H3K122 and H3K125. Ubiquitination is required for efficient histone deposition during replication-coupled nucleosome assembly, probably by facilitating the transfer of H3-H4 from ASF1 to other chaperones involved in histone deposition. RTT101(MMS1-CRT10) may regulate nucleotide synthesis through transcriptional regulation of ribonucleotide reductase. RTT101(MMS1) is also involved in the non-functional rRNA decay (NRD) of 25S rRNA through the selective, ubiquitination-dependent degradation of nonfunctional ribosomal particles. Involved in the regulation of TY1 transposition.
Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Alpha adaptin is a subunit of the plasma membrane adaptor. Facilitates interaction between APL1 and APS2.
Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit APL3 and beta-type subunit APL1), a medium chain (mu-type subunit APM4) and a small adaptin (sigma-type subunit APS2).
Belongs to the adaptor complexes large subunit family.
Belongs to the peroxisomal membrane protein PXMP2/4 family.
Belongs to the Dus family. Dus4 subfamily.
Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs (PubMed:14970222). Specifically modifies U20a and U20b in cytoplasmic tRNAs (PubMed:14970222). Also able to mediate dihydrouridylation of some mRNAs, thereby affecting their translation (By similarity).
Deletion leads to fluconazole resistance.
Dosage dependent suppressor of PKC1 deletion and MPK1 deletion. Involved in cell lysis.
Homotetramer (By similarity). Interacts with NAP1.
In eukaryotes there are two forms of the enzymes: a cytosolic one and a mitochondrial one.
Present with 17700 molecules/cell in log phase SD medium.
Activated by hypophosphorylated form of ATG13 (present in nitrogen starvation conditions). Also activated by autophopsphorylation of Thr-226 and inhibited by phosphorylation of Ser-34.
Autophosphorylated at Thr-226 and Ser-390. The phosphorylation state may play a role in the induction of protein degradation upon starvation. Phosphorylation at Thr-226 within the activation loop is required for protein kinase activity whereas phosphorylation at Ser-34 leads to inhibition of kinase activity. Phosphorylation of Ser-508 and Ser-515 by PKA is required to induce autophagy but not for kinase activity.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. APG1/unc-51/ULK1 subfamily.
Homodimer. Dimerization requires the presence of ATG13. Forms a ternary complex with ATG13 and ATG17. Interacts also with ATG11.
Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (PubMed:18818209, PubMed:21576396, PubMed:22768199, PubMed:23230142). Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates (PubMed:21228276). Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9 (PubMed:14723849, PubMed:20855505, PubMed:24905091, PubMed:24440502). Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8 (PubMed:28821724). Finally, ATG1 is also required for the maintenance of cell viability under starvation and for glycogen storage during stationary phase. Plays a role in genome stability through suppression of abnormal mitosis under starvation, and in regulation of filamentous growth.
The LIR motif is required for the interaction with ATG8 and for the association of ATG1 with autophagosomes.
Belongs to the kynurenine formamidase family.
Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.
Cells exhibit slow growth in the absence of nicotinate.
The main chain amide nitrogen atoms of the second glycine and its adjacent residue in the HGGXW motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. CGI121 acts as an allosteric effector that regulates the t(6)A activity of the complex. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators. CGI121 is not required for tRNA modification.
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Activated by the glutamine sensor PIB2 in nutrient-rich conditions.
Increases cellular levels of glutamine and alanine during high hydrostatic pressure (mechanical stress) (PubMed:32801125). Sensitive to high hydrostatic pressure (mechanical stress) (PubMed:32801125).
It is uncertain whether Met-1 is the initiator.
It may act on another substrate or phosphorylate a different position in the phosphatidylinositol ring.
Phosphatidylinositol 3-kinase homolog, component of TORC1, which regulates multiple cellular processes to control cell growth in response to environmental signals. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls ribosome biogenesis via control of rRNA, ribosomal protein and tRNA gene expression, and rRNA processing. TORC1 positively controls protein biosynthesis by regulation of mRNA stability, translation initiation factor activity, and high-affinity amino acid permeases that serve to provide amino acids for use by the translation machinery. TORC1 also promotes growth by sequestering a number of nutrient and general stress-responsive transcription factors in the cytoplasm. TORC1 negatively controls macroautophagy, a process to recycle surplus cytoplasmic mass under nutrient starvation conditions. TORC1 controls many of these processes via TIP41-TAP42-mediated inhibition of the type 2A-related phosphatases PP2A and SIT4 (PubMed:10198052, PubMed:10329624, PubMed:10604478, PubMed:10995454, PubMed:11741537, PubMed:15620355, PubMed:7606777, PubMed:8741837, PubMed:9539725, PubMed:9843498, PubMed:28993463). In nutrient-rich conditions, responsible for the phosphorylation of AGC S6 kinase (S6K) YPK3, activating YPK3 kinase activity and promoting phosphorylation of ribosomal protein S6 (PubMed:25767889). Phosphorylates kinase SCH9 at 6 amino acids in the C-terminus, activating SCH9 kinase activity to properly regulate ribosome biogenesis, translation initiation, and entry into stationary phase (PubMed:17560372).
The target of rapamycin complex 1 (TORC1) is composed of at least KOG1, LST8, TCO89 and either TOR1 (TORC1-A) or TOR2 (TORC1-B) (PubMed:12408816, PubMed:12631735). Interacts with PIB2; following activation of PIB2 by glutamine or cysteine (PubMed:34535752, PubMed:29698392, PubMed:28483912). TORC1 binds to and is inhibited by FKBP-rapamycin (PubMed:12408816, PubMed:7606777).
Belongs to the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3 and PML1.
Required for efficient splicing and pre-mRNA nuclear retention.
Belongs to the G-protein coupled receptor 4 family.
Receptor for the peptide pheromone a factor.
Belongs to the eukaryotic initiation factor 4G family.
Component of the eIF4F complex, which composition varies with external and internal environmental conditions. It is composed of at least eIF4A (TIF1/TIF2), eIF4E (TIF45) and eIF4G (TIF4631 or TIF4632) (By similarity). Interacts with PAT1 in a RNA-dependent manner.
Component of the eIF4F complex, which interacts with the mRNA cap structure and serves as an initial point of assembly for the translation apparatus. Stimulates translation by interaction with polyadenylate-binding protein PAB1, bringing the 5'- and 3'-ends of the mRNA in proximity. The formation of this circular mRNP structure appears to be critical for the synergistic effects of the cap and the poly(A) tail in facilitating translation initiation, recycling of ribosomes, and mRNA stability. TIF4632 is probably essential when TIF4631 is missing.
Monomer (Probable). Interacts with NOP53.
Present with 138 molecules/cell in log phase SD medium.
Required for efficient transcription initiation by RNA polymerase I. Interacts with Pol I in the absence of template DNA and stimulates recruitment of Pol I, but does not remain as part of stable preinitiation complex.
Has a role in the initiation of DNA replication. Required at S-phase checkpoint. Required for the association of PSF1 with origins. Also required for the proper activation of RAD53 in response to DNA damage and replication blocks. Multicopy suppressor of DPB2 mutation. Overexpression restores the growth defect conferred by POL2 mutation.
Present with 540 molecules/cell in log phase SD medium.
Key component of the cytosolic iron-sulfur protein assembly (CIA) machinery that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. Acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as RAD3/XPD and DNA2, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription.
Functions in the SND pathway, a SRP (signal recognition particle) and GET (guided entry of tail-anchored proteins) independent pathway for targeting a broad range of substrate proteins to the endoplasmic reticulum. SND functions in parallel to GET in targeting proteins with downstream hydrophobic motifs (PubMed:27905431). Involved in inorganic phosphate uptake (PubMed:8709965). Also involved in telomere length regulation and maintenance (PubMed:16552446).
Interacts with ENV10/SND2. ENV10/SND2 and PHO88/SND3 form a complex with the translocon in the endoplasmic reticulum membrane.
Present with 61800 molecules/cell in log phase SD medium.
Minor mitochondrial aldehyde dehydrogenase isoform. Plays a role in regulation or biosynthesis of electron transport chain components. Involved in the biosynthesis of acetate during anaerobic growth on glucose.
Present with 23300 molecules/cell in log phase SD medium.
The activity increases in the presence of K(+) ions: 15-fold with NADP and 40-fold with NAD, respectively.
Belongs to the glycosyl hydrolase 37 family.
Involved in RNA processing and negative regulation of glucose repression. Regulates the level of two antigens, P43 and P70. Binds to protein phosphatase type 1. Functions with REG2 and SNF1 protein kinase to regulate growth. Might regulate SNF1 directly or indirectly.
Present with 2560 molecules/cell in log phase SD medium.
Sorting receptor involved in the transport of vacuolar enzymes from the Golgi complex to the vacuole. Involved in the delivery and maturation of PEP4 (vacuolar proteinase A) and PRB1 (vacuolar proteinase B).
Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1 subfamily.
Mitochondrial GTPase involved in assembly of the large ribosomal subunit (PubMed:12808030). Plays a role in expression of the mitochondrial translational machinery (PubMed:12808030).
Belongs to the acetate uptake transporter (AceTr) (TC 2.A.96) family.
Transporter protein required for ammonia export and acetate uptake and resistance. Necessary for up-regulation and down-regulation of meiotic plaque (MP) component levels in a dependency on external acetate. Has a role in ascus formation.
Present with 8200 molecules/cell in log phase SD medium.
Interacts with RTT102, SWP82 and the N-terminus of SNF2. Component of the SWI/SNF global transcription activator complex. The 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29.
Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
FMN1 is essential for growth on rich medium.
The subcellular location of this enzyme needs further confirmation.
Belongs to the universal ribosomal protein uS5 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). uS5 is important for the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835).
Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). Interacts with snoRNA U3. Interacts with MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3 (PubMed:15590835).
Belongs to the Nudix hydrolase family. DCP2 subfamily.
Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (PubMed:10508173, PubMed:11139489, PubMed:11741542). Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (PubMed:12554866). Decapping is the major pathway of mRNA degradation in yeast and occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body (PubMed:10508173, PubMed:11139489, PubMed:11741542). Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degradation of their transcripts (PubMed:19779198).
Component of the decapping complex composed of DCP1 and DCP2 (PubMed:10508173, PubMed:11741542, PubMed:14758354). Interacts with mRNA, LSM2, LSM4 and LSM8 (PubMed:10900456). Interacts with EDC3 (PubMed:18678652).
Increases autophagy activity through accumulation of autophagy-related proteins in nutrient-replete conditions (PubMed:19779198).
RNA-binding protein involved in the specific removal of group I introns in mitochondrial encoded transcripts. Maintains the stability of the small subunit mitochondrial 15S rRNA and thus the expression of the mitochondrial genome.
Functions in the homeostasis of manganese ions.
Component of the RPD3C(L) complex composed of at least ASH1, CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6. Interacts with CYC8.
Component of the RPD3C(L) histone deacetylase complex (HDAC). Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. CTI6 links the SAGA coactivator to the CYC8-TUP1 corepressor. Involved in transcription regulation of heme-regulated genes and required for GCN5 recruitment, histone H3 acetylation and SPT15/TBP binding to promoters.
Component of the ISW2 complex, which at least consists of ISW2, ITC1, DLS1 and DPB4.
Functions as component of the ISW2 complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW2 complex is involved in coordinating transcriptional repression and in inheritance of telomeric silencing. It is involved in repression of MAT a-specific genes, INO1, and early meiotic genes during mitotic growth dependent upon transcription factor UME6 and in a parallel pathway to the RPD3-SIN3 histone deacetylase complex. DLS1 is partially required for the ISW2 complex chromatin remodeling activity and is not required for its interaction with chromatin.
Component of the transcription complex SCB-binding factor (SBF) composed of SWI6 and SWI4. Interacts with MSA2.
Part of a complex involved in cell-cycle-dependent transcription. SWI4 and SWI6 are required for formation of the cell-cycle box factor-DNA complex. The repeated element in the upstream region of HO (5'-CACGAAAA-3') is called the cell cycle box (CCB).
Interacts with the phosphatase PP2A catalytic subunits PPH21 and PPH22. Forms a ternary complex with PPH21-TAP42.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for TAP42-associated PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex. Acts also inhibitory at high concentrations. Involved in the regulation of cell cycle progression, mitotic spindle formation and bud morphogenesis.
Belongs to the universal ribosomal protein uL15 family.
Ty1-NL2 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
ATP-binding RNA helicase involved in mitochondrial RNA metabolism. Required for maintenance of mitochondrial DNA.
Belongs to the DEAD box helicase family. MRH4 subfamily.
May play a role in chromosome segregation through establishment of sister chromatid cohesion.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (PubMed:25609543, PubMed:28154081). uS17m may have a meiosis-specific role as it accumulates during the middle stage of sporulation (PubMed:15543521).
Hyperphosphorylated after treatment with rapamycin in a TAP42-dependent manner.
Belongs to the fungal fatty acid synthetase subunit beta family.
Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.
Present with 91800 molecules/cell in log phase SD medium.
This ORF was incorrectly assigned as MEI4.
Transcriptional activator of promoters containing ATF/CREB sites. Can independently stimulate transcription through ATF/CREB sites. Important for a variety of biological functions including growth on non-optimal carbon sources. Regulates the expression of COS8. Has efficient silencing blocking activities.
Belongs to the ferric reductase (FRE) family. AIM14 subfamily.
Probable cell surface metalloreductase. May be involved in iron or copper homeostasis (By similarity).
N- and C-terminal domains are encoded in separate ORFs that are translated into one protein via a +1 frameshift (PubMed:9467951). ABP140 mRNA translation follows a cotranslational transport: mRNA is transported to the distal pole of the mother cell, independently of the SHE machinery, and follows a translational coupling, in which ABP140 mRNA is tethered to actin cables via its nascent protein product and is transported to the distal pole by actin retrograde flow (PubMed:21792172).
Produced by ribosomal frameshifting between codon Leu-277 and Gly-278.
S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Thr) and tRNA(Ser) (PubMed:21518804, PubMed:21518805, PubMed:28003514). N(3)-methylcytidine methylation of tRNA(Thr) requires the N6-threonylcarbamoylation of tRNA (t6A37) by the EKC/KEOPS complex as prerequisite (PubMed:28003514). N(3)-methylcytidine methylation of tRNA(Ser) requires the formation of N(6)-dimethylallyladenosine(37) (i6A37) by MOD5 as prerequisite (PubMed:28003514). Methylation of tRNA(Ser) is also stimulated by SES1 (PubMed:28003514). Binds F-actin and shows weak F-actin cross-linking activity (PubMed:9467951).
Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily.
Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates.
Core regulatory subunit of the histone H2A phosphatase complex, which dephosphorylates H2AS128ph (gamma-H2A) that has been displaced from sites of DNA lesions in the double-stranded DNA break repair process. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint.
Present with 7010 molecules/cell in log phase SD medium.
Regulatory subunit 3 (R3) of the histone H2A phosphatase complex (HTP-C) consisting of PPH3, PSY2 and PSY4. Interacts with SPT4, SPT5 and TIP41.
Belongs to the V-ATPase e1/e2 subunit family.
Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:14594803). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:14594803).
It is uncertain whether Met-1 or Met-2 is the initiator.
Inhibitory regulator of the Ras-cyclic AMP pathway. Stimulates the GTPase activity of Ras proteins.
Up-regulated by a wide range of conditions, such as intracellular iron depletion, carbon source restriction, high temperature, high osmotic stress, cold stress, unfolded protein response, and high hydrostatic pressure. The promoter contains several binding sites for the stress response transcription factors MSN2, MSN4 and HSF1. Down-regulated when treated with different antifungal drugs from the azole class.
Belongs to the NTC complex (or PRP19-associated complex), composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2, and PRP19. The NTC complex associates with the spliceosome after the release of the U1 and U4 snRNAs and forms the CWC spliceosome subcomplex (or CEF1-associated complex) reminiscent of a late-stage spliceosome composed also of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8, PRP9, PRP11, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNU114, SPP2, RSE1 and YJU2. Interacts with CLF1, ISY1, NTC20, PRP19, PRP46, SYF1 and SYF2.
Involved in pre-mRNA splicing and cell cycle control. Required for the binding of the NTC complex (or PRP19-associated complex) components to the spliceosome to mediate conformational rearrangement or to stabilize the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation. Its absence leads to an arrest of the cell cycle, possibly due to the inefficient splicing of TUB1.
Belongs to the Mediator complex subunit 18 family.
Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. SRB5/MED18 interacts directly with MED8 and SRB2/MED20.
Present with 1011 molecules/cell in log phase SD medium.
Homotetramer. Interacts with coatomer complex. May interact with ARF1.
Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Mediates the cis and medial Golgi localization of mannosyltransferases through direct binding of their cytosolic domains. Involved in vacuolar protein sorting.
Belongs to the eukaryotic ribosomal protein eL18 family.
Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). eL18 interacts with NAP1 (PubMed:18086883).
Present with 63700 molecules/cell in log phase SD medium.
Belongs to the phosphoglycerate kinase family.
Present with 314000 molecules/cell in log phase SD medium.
Present with 1055 molecules/cell in log phase SD medium.
Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. Prevents actin filament assembly by forming a 1:1 complex with actin monomers, and inhibits the nucleotide exchange reaction of actin monomers (By similarity).
Belongs to the actin-binding proteins ADF family. Twinfilin subfamily.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YPR158C-C ORF.
Catalytic subunit of the NatB N-terminal acetyltransferase, which catalyzes acetylation of the amino-terminal methionine residues of all proteins beginning with Met-Asp or Met-Glu and of some proteins beginning with Met-Asn, Met-Gln or Met-Met. NatB acetylates TPM1 protein and regulates tropomyocin-actin interactions, it is presumed to N-acetylate 15% of all yeast proteins.
Component of the N-terminal acetyltransferase B (NatB) complex, which is composed of NAT3 and MDM20.
Belongs to the PAPS reductase family. FAD1 subfamily.
Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.
Competitively inhibited by NAD(+). Inhibited by mercurials such as p-chloromercuribenzoate (PCMB) and HgCl(2). Enzymatic activity increases under anaerobic conditions.
Monomer (PubMed:14930). Component of the 2-(3-amino-3-carboxypropyl)histidine synthase complex composed of DPH1, DPH2, KTI11/DPH3 and a NADH-dependent reductase, predominantly CBR1 (PubMed:27694803). Interacts with KTI11/DPH3 (PubMed:27694803). Interacts with STE20 (PubMed:17895367).
NADH-dependent reductase for KTI11/DPH3 and cytochrome b5 (PubMed:14930, PubMed:10622712, PubMed:27694803, PubMed:31463593, PubMed:34154323). Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (PubMed:31463593, PubMed:34154323, PubMed:27694803). DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising KTI11/DPH3 and a NADH-dependent reductase, predominantly CBR1 (PubMed:31463593, PubMed:34154323). By reducing KTI11/DPH3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), mediated by the elongator complex (PubMed:27694803). The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes (PubMed:10622712). Plays a role in bud morphology (PubMed:17895367).
Protein levels are highest during exponential growth phase and lowest in stationary phase.
Simultaneous disruption of MCR1 results in resistance to diphtheria toxin and zymocin.
Component of the RQT (ribosome quality control trigger) complex, composed of SLH1, CUE3, and RQT4 (PubMed:28757607, PubMed:32203490). Interacts with CUE3 (PubMed:28757607). Interacts with RQT4 (PubMed:28757607). Interacts with HEL2 (PubMed:28757607, PubMed:28223409). Associates with translating ribosomes (PubMed:28757607).
Defective activation of the ribosome quality control (RQC) pathway (PubMed:28757607, PubMed:28223409). Mildly defective ribosome stalling induced by RNA arrest sequences (PubMed:28223409). Sensitive to anisomycin (stalls ribosomes in the rotated state) (PubMed:28757607).
Involved in activation of the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation (PubMed:28757607, PubMed:28223409, PubMed:32203490). Drives the splitting of stalled ribosomes that are polyubiquitinated in a HEL2-dependent manner, as part of the ribosome quality control trigger (RQT) complex (PubMed:28757607, PubMed:32203490). Also represses the translation of non-poly(A) mRNAs together with SKI2 (PubMed:10922069). May block translation by inhibiting translation initiation factor 5B (FUN12) action on mRNAs lacking a 3' poly(A) structure (PubMed:11438647). Involved in antiviral defense, preventing L-A dsRNA virus propagation by specifically blocking translation of viral mRNAs (PubMed:10922069).
Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class II DHOase subfamily.
Catalyzes the conversion of ureidosuccinic acid (USA) to dihydroorotate, the third step of the de novo pyrimidine biosynthetic pathway.
Present with 12700 molecules/cell in log phase SD medium.
Forms a complex with CDC91, GPI16, GPI17 and GAA1.
Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein.
In the C-terminal section; belongs to the cytidine and deoxycytidylate deaminase family.
In the N-terminal section; belongs to the pseudouridine synthase RluA family.
Involved in riboflavin biosynthesis. Converts 2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1H,3H)-pyrimidinedione 5'-phosphate.
Responsible for synthesis of pseudouridine from uracil-32 in cytoplasmic transfer RNAs.
Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains.
Present with 4930 molecules/cell in log phase SD medium.
Required for proper folding and/or the stability of a subset of proteins in the endoplasmic reticulum. Aids the autocatalytic processing of PRB1. Component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the mannosyltransferase GPI14.
Belongs to the ATP phosphoribosyltransferase family.
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of the enzymatic activity (By similarity).
Interacts with NTH1 (via N-terminus when phosphorylated by PKA); the interaction is direct and activates NTH1 (PubMed:22320399). Interacts with FIN1 (PubMed:12551942).
Present with 47600 molecules/cell in log phase SD medium.
Interacts with the cullin CDC53. Interacts with ubiquitin via its UBA-like domain. Interacts with RUB1/NEDD8.
Required for neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity. Does not act by preventing deneddylation, but rather facilitates neddylation, possibly by acting with HRT1/RBX1 to recruit the Nedd8-charged E2 UBC12 to the cullin component of SCF-type complexes.
Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 snRNP, U4/U6.U5 snRNP, and free U6 snRNP). It binds directly to the U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. It probably also is involved in degradation of nuclear pre-mRNA by targeting them for decapping. LSM2 binds specifically to the 3'-terminal U-tract of U6 snRNA. LSM2-LSM8 probably is involved in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM2, probably in a complex that contains LSM2-LSM7 but not LSM1 or LSM8, associates with the precursor of the RNA component of RNase P (pre-P RNA) and may be involved in maturing pre-P RNA. LSM2 is required for processing of pre-tRNAs, pre-rRNAs and U3 snoRNA.
Component of the heptameric LSM1-LSM7 complex that forms a seven-membered ring structure with a doughnut shape. The LSm subunits are arranged in the order LSM1, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. Except for LSM1, where a C-terminal helix crosses the ring structure to form additional interactions with LSM3 and LSM6, each subunit interacts only with its two neighboring subunits. The LSM1-LSM7 complex interacts with PAT1; within the complex PAT1 has direct interactions with LSM2 and LSM3. Component of the heptameric LSM2-LSM8 complex that forms a seven-membered ring structure with a doughnut shape; an RNA strand can pass through the hole in the center of the ring structure. The LSm subunits are arranged in the order LSM8, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. LSM2-LSM8 associates with PAT1 and XRN1. A complex comprising LSM2-LSM7 without LSM1 or LSM8 may exist. Likewise, LSM2 and LSM3 can assemble into a doughnut structure that binds PAT1 (in vitro). Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
Disruption of the MLF3 gene causes increased sensitivity to the immunosuppressant leflunomide.
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 10 subunits. The complex is composed of 3 respiratory subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10 (PubMed:10873857, PubMed:11880631, PubMed:18390544, PubMed:30598554). The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a monomer or a dimer of cytochrome c oxidase (complex IV, CIV), resulting in 2 different assemblies (supercomplexes III(2)IV and III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556, PubMed:30598554). Interacts with the transmembrane segment of RIP1 (PubMed:30598556).
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Present with 4550 molecules/cell in log phase SD medium.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. GLE1 interacts with the NUP82 subcomplex via NUP42. It also interacts with GFD1 and the ATP-dependent RNA helicase DBP5.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved in a terminal step of poly(A)+ mRNA transport through the NPC probably by binding the ATP-dependent RNA helicase DBP5 and GFD1 at the cytoplasmic side of the NPC. These interactions are thought to be important for the dissociation of transport proteins such as the heterogeneous nuclear ribonucleoprotein (hnRNP) NAB2 from exported mRNA.
Belongs to the DEAD box helicase family. DEAH subfamily. PRP16 sub-subfamily.
Influences the fidelity of branchpoint recognition in yeast splicing. This is RNA-dependent ATPase which is essential for viability. It may mediate one of the many ATP-requiring steps of spliceosome assembly and that accuracy of branchpoint recognition may be coupled to ATP binding and/or hydrolysis.
Component of the nuclear pore complex (NPC)-associated TREX-2 complex (transcription and export complex 2), composed of at least SUS1, SAC3, THP1, SEM1, and CDC31. TREX-2 contains 2 SUS1 chains. The TREX-2 complex interacts with the mRNA export factors MEX67, MTR2 and SUB2, and the nucleoporin NUP1. Component of the 1.8 MDa SAGA transcription coactivator-HAT complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Within the SAGA complex, SUS1, SGF11, SGF73 and UBP8 form an additional subcomplex of SAGA called the DUB module (deubiquitination module). Interacts directly with THP1, SAC3, SGF11 and with the RNA polymerase II. Interacts with YRA1 and MEX67.
Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is involved in RNA polymerase II-dependent regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). Within the SAGA complex, participates in a subcomplex with SGF11, SGF73 and UBP8 required for deubiquitination of H2B and for the maintenance of steady-state H3 methylation levels. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket. TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. SUS1 has also a role in mRNP biogenesis and maintenance of genome integrity through preventing RNA-mediated genome instability. Has a role in response to DNA damage induced by methyl methane sulfonate (MMS) and replication arrest induced by hydroxyurea. May also be involved in cytoplasmic mRNA decay by interaction with components of P-bodies.
The gene for SUS1 bears 2 introns, and its expression is highly regulated by splicing, translation and decay. The presence of the introns thereby play a key role for SUS1 function in yeast.
By heat stress dependent on the heat shock transcription factor HSF1 and the general stress transcription factors MSN2 and MSN4. Expressed at a higher level in respiring cells than in fermenting cells. Expressed in stationary phase cells and spores (at protein level).
Has 2 AAA ATPase type nucleotide-binding domains (NBDs) per monomer, a low-affinity, high-turnover site (NBD1) and a high-affinity site (NBD2) with a 300-fold slower rate of hydrolysis. There is allosteric regulation between the 2 sites. ATP binding to NBD1 triggers binding of polypeptides and stimulates ATP hydrolysis at NBD2. Nucleotide binding to NBD2 is crucial for oligomerization.
Homohexamer, forming a ring with a central pore. The hexamer is stabilized by high protein concentrations and by ADP or ATP. Oligomerization influences ATP hydrolysis activity at NBD2. Interacts with YDJ1. Interacts (via C-terminal DDLD tetrapeptide) with CNS1, CPR7 and STI1 (via TPR repeats); under respiratory growth conditions.
Inhibited by micromolar concentrations of guanidinium chloride. Inhibits the ATPase activity, but does not dissociate the hexameric protein.
Present with 32800 molecules/cell in log phase SD medium.
Required, in concert with Hsp40 (YDJ1) and Hsp70 (SSA1) and small Hsps (HSP26), for the dissociation, resolubilization and refolding of aggregates of damaged proteins after heat or other environmental stresses. Extracts proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by components of the Hsp70/Hsp40 chaperone system. Substrate binding is ATP-dependent, and release of bound polypeptide is triggered by ATP hydrolysis. Also responsible for the maintenance of prions by dissociating prion fibrils into smaller oligomers, thereby producing transmissible seeds that can infect daughter cells during mitosis and meiosis. Loss of HSP104 can cure yeast cells of the prions [PSI+], [URE3] and [PIN+]. Excess HSP104 can also specifically cure cells of [PSI+].
The C-terminal extension is involved in oligomerization.
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Present with 78900 molecules/cell in log phase SD medium.
The eukaryotic translation initiation factor 3 (eIF-3) core complex is composed of TIF32, PRT1, NIP1, TIF34 and TIF35. A subcomplex of TIF32, NIP1 and PRT1 mediates the interaction with eIF-1, TIF5/eIF-5 and HCR1. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a multifactor complex (MFC) that may bind to the 40S ribosome. TIF32, NIP1 and TIF5/eIF-5 comprise a minimal 40S-ribosome-binding unit. NIP1 interacts with TIF5/eIF-5 and SUI1.
May interact with CHS3 and seems to be an adapter (along with SKT5) to link CHS3 to septins.
Acts as a endogenous target of the ribosome quality control (RQC) pathway (PubMed:32203490). During translation, the nascent chain has a propensity to stall ribosomes, thereby stimulating activation of the RQC pathway (PubMed:32203490).
Belongs to the glycosyltransferase 8 family. Glycogenin subfamily.
Self-glucosylating initiator of glycogen synthesis. Catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues. These chains act as primers for the elongation reaction catalyzed by glycogen synthase. Capable of transferring glucosyl residues to unbound acceptors such as free oligoglucans or oligoglucan derivatives.
Mitochondrial targeting of PHB2 is ensured by a bipartite non-cleavable presequence at the N-terminus.
Present with 2850 molecules/cell in log phase SD medium.
Prohibitin probably acts as a holdase/unfoldase for the stabilization of newly synthesized mitochondrial proteins.
The mitochondrial prohibitin complex consists of two subunits (PHB1 and PHB2), assembled into a membrane-associated ring-shaped supercomplex of approximately 1 mDa.
During assembly of the complex, component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs) which contains CBF5, NAF1, NHP2 and NOP10 proteins. Interacts with SHQ1. Interacts directly with CBF5. Interacts with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (RPB1).
RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex and disappears during maturation of the complex and is replaced by GAR1 to yield mature H/ACA snoRNPs complex. Acts as a competitive binder for CBF5 probably required to prevent non-cognate RNAs from being loaded during transport of the particle by inducing a non-productive conformation of CBF5.
The central region (136-221) reveals a striking structural homology with the core domain of GAR1.
May act as an E3 ligase mediating SUMO/Smt3 attachment to septins. May be involved in chromosome maintenance.
In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.
In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.
Mitochondrial isozyme of C-1-tetrahydrofolate synthase. The trifunctional enzyme catalyzes the interconversion of the one-carbon derivatives of tetrahydrofolate (THF) between different oxidation states by the enzymatic activities 10-formyltetrahydrofolate synthetase, 5,lO-methenyltetrahydrofolate cyclohydrolase, and 5,lO-methylenetetrahydrofolate dehydrogenase.
This trifunctional enzyme consists of two major domains: an N-terminal part containing the methylene-THF dehydrogenase and cyclohydrolase activities and a larger C-terminal part containing formyl-THF synthetase activity.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type V subfamily.
Contains a large substrate-binding pocket that recognizes alpha-helical transmembranes, which alternately faces the endoplasmic reticulum lumen and cytosol, while remaining accessible to the lipid bilayer through a lateral opening (PubMed:32973005). The translocase alternates between two conformations: inward-open (E1) and outward-open (E2) states (PubMed:32973005). Undergoes a series of conformational changes with ATP-binding, phosphorylation of the Asp active site and subsequent dephosphorylation in a Post-Albers cycle (i.e., E1 -> E1-ATP -> E1P-ADP -> E1P -> E2P -> E2-Pi -> E1) (PubMed:32973005). A substrate transmembrane helix with a short, preferentially positively charged lumenal segment binds to the outward-open pocket and the E2P-to-E1 transition flips the transmembrane by a switch from the outward-open to inward-open conformation (PubMed:32973005).
Endoplasmic reticulum translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum (PubMed:22918956, PubMed:32973005). Acts as a dislocase that mediates the ATP-dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane (PubMed:32973005). Specifically binds mitochondrial tail-anchored transmembrane proteins: has an atypically large substrate-binding pocket that recognizes and binds moderately hydrophobic transmembranes with short hydrophilic lumenal domains (PubMed:32973005).
Impaired mitochondrial transmembrane tail-anchored protein localization, characterized by mitochondrial transmembrane tail-anchored protein accumulation at the endoplasmic reticulum (PubMed:22918956). In addition, a wide spectrum of phenotypes is observed, including induction of the endoplasmic reticulum unfolded protein response, defects in lipid and sterol homeostasis, and dysregulated protein N-glycosylation, topogenesis and turnover (PubMed:12058017, PubMed:22918956, PubMed:24392018).
Present with 1870 molecules/cell in log phase SD medium.
The ATPase activity is stimulated by phosphatidylinositol 4-phosphate (PI4P).
Was initially thought to mediate ion transport such as calcium or manganese (PubMed:12058017, PubMed:24392018). However, different publications have shown that it does not act as an ion transporter (PubMed:22745129, PubMed:32353073, PubMed:32973005). Specifically binds moderately hydrophobic transmembrane with short hydrophilic lumenal domains that misinsert into the endoplasmic reticulum (PubMed:32973005).
Interacts with ARF3 (in GTP-bound form). Interacts with CNM67.
Involved in actin patch polarization. Required for maintaining a proper budding pattern in yeast cells. Required for proper polarized localization of the ADP-ribosylation factor ARF3 at the plasma membrane.
Mainly expressed in dividing cells, but not in stationary phase cells (at protein level).
Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (By similarity). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs (PubMed:12897126, PubMed:20802481, PubMed:26101253). Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1) (PubMed:12897126, PubMed:20802481). Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates (PubMed:20802481). Stimulates exoribonuclease activity of RAT1, allowing it to degrade RNAs with stable secondary structure more effectively (PubMed:20802481). Required for the processing of nuclear mRNA and rRNA precursors (PubMed:10805743, PubMed:12612077, PubMed:16131592). May promote termination of transcription by RNA polymerase II (PubMed:15565157).
Interacts with RAT1, RTT103 and pre-60S ribosomal subunits.
Belongs to the pyrroline-5-carboxylate reductase family.
Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline, the final step in proline biosynthesis.
Component of two distinct SNARE complexes consisting of SED5, BOS1, BET1 and SEC22 or UFE1, USE1, SEC20 and SEC22. YKT6 can probably replace SEC22 as subunit of either complex. Interacts with SEC24, YIF1 and YIP1.
Deletion of SEC22 is viable. Overexpression of SEC22 suppresses deletion of YPT1.
Nonessential SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER.
Component of the elongator complex which consists of ELP1/IKI3, ELP2, ELP3, ELP4, ELP5/IKI1 and ELP6 (PubMed:11435442, PubMed:11689709, PubMed:27974378, PubMed:27872205). The elongator complex is composed of two copies of the Elp123 subcomplex (composed of ELP1/IKI3, ELP2 and ELP3) and two copies of the Elp456 subcomplex (composed of ELP4, ELP5/IKI1 and ELP6) (PubMed:27974378, PubMed:27872205, PubMed:25960406). The Elp123 subcomplex forms a two-lobed scaffold, which binds the Elp456 subcomplex asymmetrically (PubMed:27974378, PubMed:27872205). In the complex, ELP2 interacts with ELP1/IKI3 (PubMed:12139626). In each lobe, ELP2 is tightly sandwiched between ELP1/IKI3 and ELP3 (PubMed:31309145). The Elp123 subcomplex binds tRNA through ELP1/IKI3 and ELP3 and can bind 2 tRNAs simultaneously (PubMed:31309145). tRNA-binding induces conformational rearrangements which precisely position the targeted anticodon base in the active site (PubMed:31309145). The Elp456 subcomplex binds tRNA and has ATPase activity (PubMed:22343726). Interacts with KTI11/DPH3 (PubMed:27694803, PubMed:18627462).
Component of the elongator complex, a multiprotein complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:15769872, PubMed:18755837, PubMed:31309145). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:29332244). It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin) (PubMed:11296232). May also be involved in sensitivity to Pichia inositovora toxin (PubMed:13680368). ELP2 binds to microtubules (PubMed:25960406). Independently, ELP2 may be involved in polarized exocytosis (PubMed:15138274, PubMed:15780940).
Folds into a two seven-bladed beta-propeller structure which is required for elongator complex assembly and association with microtubules.
Present with 6090 molecules/cell in log phase SD medium.
Component of the HOPS complex which is composed of PEP5, VPS16, PEP3, VPS33, VPS39 and VPS41. HOPS associates with phosphoinositides and the PX domain of VAM7. Interacts with VAM7 and VPS39.
Required for vacuolar assembly and vacuolar traffic. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion.
Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of at least PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. Interacts with FIP1 and YSH1.
RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB.
Belongs to the WD repeat WDR12/YTM1 family.
Component of the NOP7 complex, composed of ERB1, NOP7 and YTM1. The complex is held together by ERB1, which interacts with NOP7 via its N-terminal domain and with YTM1 via a high-affinity interaction between the seven-bladed beta-propeller domains of the 2 proteins. The NOP7 complex associates with the 66S pre-ribosome (PubMed:12110181, PubMed:16287855, PubMed:26657628). Interacts (via UBL domain) with MDN1 (via VWFA/MIDAS domain) (By similarity) (PubMed:20542003, PubMed:26601951).
Induced 4.5-fold when shifted from galactose to glucose medium (at protein level).
Has a calcium-dependent calmodulin-binding activity.
Component of the SPT4-SPT5 complex. Interacts with SHE2.
The SPT4-SPT5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. The complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene. Structural and functional component of the centromeric and heterochromatic loci linking chromatin structure with kinetochore function and gene silencing.
Was originally thought to be involved in the transcription initiation step.
Component of the plasma membrane SPS (SSY1-PTR3-SSY5) amino acid sensor complex.
Down-regulated after extracellular amino-acid addition.
Protease component of the SPS-sensor system, which regulates the expression of several amino acid-metabolizing enzymes and amino acid- and peptide-permeases in response to extracellular amino acid levels by controlling the activity of two transcription factors, STP1 and STP2. Catalyzes the activation of these transcription factors, which are synthesized as latent cytoplasmic precursors, by proteolytic removal of an N-terminal inhibitory domain containing cytoplasmic retention motifs. SSY5 binds as an inactive protease complex to STP1. In response to extracellular amino acids and dependent on the other SPS-sensor components, the inhibitory propeptide is induced to dissociate, and thereby enables the catalytic domain to process STP1.
The propeptide is autoproteolytically cleaved from the catalytic domain but remains associated, forming an inactive protease complex. This processing occurs even in the absence of signaling.
Belongs to the peroxin-2832 family. Peroxin-28 subfamily.
Involved in the regulation of peroxisome number, size and distribution.
Required for vesicle fusion with the plasma membrane.
Belongs to the MINDY deubiquitinase family. FAM63 subfamily.
Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins. Has endodeubiquitinase activity.
Component of the 2-(3-amino-3-carboxypropyl)histidine synthase complex composed of DPH1, DPH2, KTI11/DPH3 and a NADH-dependent reductase, predominantly CBR1 (PubMed:12940988, PubMed:27694803, PubMed:18627462, PubMed:23645155). Interacts with DPH1 (PubMed:12940988, PubMed:27694803, PubMed:18627462, PubMed:23645155). Interacts with DPH2 (PubMed:12940988, PubMed:27694803, PubMed:18627462). Interacts with CBR1 (PubMed:27694803). Interacts with elongation factor 2 (PubMed:12940988). Interacts with ATS1/KTI13; the interaction is direct (PubMed:25604895, PubMed:25543256, PubMed:18627462). Interacts with the 40S ribosomal protein RPS7A (PubMed:12940988). Interacts with the 40S ribosomal protein RPS19A (PubMed:12940988). Interacts with the elongator complex subunit IKI3/ELP1 (PubMed:12940988, PubMed:18986986, PubMed:27694803). Interacts with the elongator complex subunit ELP2 (PubMed:12940988, PubMed:18986986, PubMed:27694803, PubMed:18627462). Interacts with the elongator complex subunit ELP3 (PubMed:12940988, PubMed:18986986, PubMed:27694803). Interacts with the elongator complex subunit ELP5 (PubMed:18627462).
Present with 8400 molecules/cell in log phase SD medium.
Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (PubMed:15485916, PubMed:18627462, PubMed:24422557, PubMed:27694803, PubMed:31463593, PubMed:34154323, PubMed:25543256). DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising KTI11/DPH3 and a NADH-dependent reductase, predominantly CBR1 (PubMed:24422557, PubMed:27694803, PubMed:31463593, PubMed:34154323). Acts as an electron donor to reduce the Fe-S cluster in DPH1-DPH2 keeping the [4Fe-4S] clusters in the active and reduced state (PubMed:34154323). Restores iron to DPH1-DPH2 iron-sulfur clusters which have degraded from [4Fe-4S] to [3Fe-4S] by donating an iron atom to reform [4Fe-4S] clusters, in a manner dependent on the presence of elongation factor 2 and SAM (PubMed:34154323). Together with ATS1; associates with the elongator complex and is required for tRNA Wobble base modifications mediated by the elongator complex (PubMed:25543256, PubMed:27694803, PubMed:18627462). The elongator complex is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:25543256).
Sensitive to caffeine, paromycin, and thermal stress (PubMed:18627462). Resistance to diphtheria toxin, sordarin and zymocin (PubMed:27694803, PubMed:18627462).
The DPH-type metal-binding (MB) domain can also bind zinc. However, iron is the physiological binding partner as zinc binding impairs the protein electron donor function.
S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 18 (Gm18) in various tRNAs.
Does not affect SDH or TIM22 complex formation.
Homolog of SDH3, but seems not to be a stoichiometric subunit of either the succinate dehydrogenase (SDH) complex or the mitochondrial inner membrane translocase TIM22 complex.
Siderophore-iron reductase responsible for reducing extracellular iron prior to import. Catalyzes the reductive uptake of Fe(3+) bound to di- and trihydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane.
Histone H3 and H4 specific chaperone component of the nuclear histone acetyltransferase B (HAT-B) complex. Involved in chromatin assembly and telomere silencing.
Homodimer (PubMed:27618665). The homodimer interacts with a histone tetramer containing H3 and H4; the interaction is direct (PubMed:24946827, PubMed:27618665). The homodimer interacts with heterodimeric histone H2A and H2B; the interaction is direct (PubMed:24946827, PubMed:27618665). Component of the nuclear histone acetyltransferase B (HAT-B) complex composed of at least HAT1, HAT2 and HIF1 (PubMed:14761951, PubMed:15099519). Does not interact with HAT1 in the absence of HAT2 (PubMed:14761951, PubMed:24946827). Interacts with histones H3 and H4 in a HAT1/HAT2 dependent manner (PubMed:14761951, PubMed:15099519). Interaction with heterotetrameric histone H3 and H4 precludes interaction with dimeric histone H2A and H2B, irrespective of the fact that their binding involves non-identical regions of the protein (PubMed:24946827, PubMed:27618665).
The N-terminal TPR repeat region contains an acidic patch that is important for interaction with histones (PubMed:24946827, PubMed:27618665). A C-terminal, highly polar region mediates interaction with dimeric histone H2A and H2B, but is not involved in interaction with heterotetrameric histone H3 and H4 (PubMed:27618665).
Component of the SWR1 chromatin-remodeling complex composed of at least ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4, SWC5, SWC7 and SWR1, and perhaps BDF1. Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, TRA1 and YNG2. Interacts with SWC4.
Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4 and H2A. The NuA4 complex is also involved in DNA repair. Yaf9 may also be required for viability in conditions in which the structural integrity of the spindle is compromised.
The coiled-coil domain is required for assembly into the NuA4 complex.
Catalyzes the aminoacylation of histidyl-tRNA in both the cytoplasm and the mitochondrion.
Present with 26800 molecules/cell in log phase SD medium.
Produced by alternative initiation at Met-21 of isoform Mitochondrial.
May be involved in vacuolar protein sorting.
Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle.
May be involved in intra-Golgi transport.
Present with 2650 molecules/cell in log phase SD medium.
Component of the TRAMP (TRF4) and TRAMP5 complexes which have a poly(A) RNA polymerase activity and are involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates like cryptic transcripts generated by RNA polymerase II and III, or hypomethylated pre-tRNAi-Met. Both complexes polyadenylate RNA processing and degradation intermediates of snRNAs, snoRNAs and mRNAs that accumulate in strains lacking a functional exosome. AIR1 also inhibits the methylation of NPL3 mediated by HMT1 through its interaction with HMT1.
Component of the TRAMP complex (also called TRF4 complex) composed of at least HUL4, MTR4, PAP2/TFR4 and either AIR1 or AIR2. Component of the TRAMP5 complex composed of at least AIR1, MTR4 and TRF5. Interacts with HMT1 and NPL3. The interaction with NPL3 requires the presence of HMT1.
Present with 6540 molecules/cell in log phase SD medium.
Binding to MAS2 is required for catalytic activity (PubMed:9654444, PubMed:9299349). Inhibited by high levels (> 1uM) of zinc (PubMed:9654444). Inhibited by metal chelators ethylenediaminetetraacetic acid (EDTA) and O-phenanthroline (PubMed:9654444).
Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (PubMed:2007593, PubMed:9299349, PubMed:9654444). Preferentially, cleaves after an arginine at position P2 (By similarity).
Heterodimer of MAS2 (alpha) and MAS1 (beta) subunits, forming the mitochondrial processing protease (MPP) in which MAS2 is involved in substrate recognition and binding and MAS1 is the catalytic subunit.
GDP-GTP exchange factor for TEM1, a Ras-like protein, component of the mitotic exit network (MEN). Activation of TEM1 by LTE1 in the bud ultimately leads to activation of CDC15 followed by the release of CDC14 from the nucleolus, which then inactivates cyclin-dependent kinases (CDKs) activity by several mechanism. Required for TEM1 localization to the bud cortex during mitotic exit. Fine-tunes the timing of the mitotic exit and couples this event with cytokinesis.
Interacts with CDC24, CDC42, KEL1, KEL2, RAS2 and TEM1.
Involved in proprotein-processing like proalpha factor-processing in the secretory pathway.
Phosphorylated by CDC28 in a cell cycle-dependent manner and in response to nocodazole. Dephosphorylion by CDC14 triggers LTE1 release from bud cortex during the exit of mitosis.
Present with 304 molecules/cell in log phase SD medium.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YBR012W-A ORF.
Encoded on the antisense strand of the nuclear 25S rDNA.
May be involved in mtDNA stability or mitochondrial gene expression regulation at the post-transcriptional level.
Belongs to the endopolyphosphatase PPN1 family.
Catalyzes the hydrolysis of inorganic polyphosphate (polyP) chains of many hundreds of phosphate residues into shorter lengths both by cleaving phosphate from the chain end and by fragmenting long-chain polymers into shorter ones. The limited digestion products are 1 and 3 P(i) residues (PubMed:11102525, PubMed:11447286, PubMed:15170373, PubMed:15342119, PubMed:15792812, PubMed:8900207, Ref.16). Also releases phosphate from dATP. dATP phosphohydrolase activity is about 7-fold lower than the exopolyphosphatase activity (Ref.16).
Divalent metal cations. Exopolyphosphatase activity is predominant in the presence of Co(2+), while endopolyphosphatase activity is predominant in the presence of Mg(2+) (PubMed:8900207, PubMed:25742176). Co(2+) is more effective than Mn(2+) for dATP phosphohydrolase activity (Ref.16).
Inactivation of PPN1 leads to the inhibition of expression of both exopolyphosphatase PPX1 and high-molecular-mass exopolyphosphatase not encoded by PPX1.
N-glycosylated (Probable). N-glycosylation is essential for the protease-mediated maturation.
Processing by proteases in the vacuole is required for activation.
Ubiquitinated. Ubiquitination mediates sorting into internal vesicles in late endosomes. TUL1 and RSP5 are required for ubiquitination. Other cytoplasmic Lys residues than Lys-6 may also be ubiquitinated.
Substrate-binding subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA (PubMed:10779558, PubMed:9851972). Also required for repression of GCN4 mRNA translation by the upstream open reading frames (uORFs) under conditions of amino acid sufficiency (PubMed:7542616).
In the C-terminal section; belongs to the eukaryotic ribosomal protein eS31 family.
Interacts directly with MPC54, CNM67, SPO21/MPC70, ADY3 and ADY4. Probable component of a spindle pole boby (SPB) complex composed of ADY3, SSP1, DON1, MPC54, SPO21/MPC70, NUD1 and CNM67.
Involved in astral microtubule organization by binding SCP72 to the outer plaque in a cell-cycle dependent manner. Required for the mitotic exit by facilitating the binding of TEMP1 to CDC15. Also involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation.
Phosphorylated from S/G2 phase until the end of mitosis.
By glucose and fructose, but not by galactose or maltose.
Component of the GINS complex which is a heterotetramer of SLD5, PSF1, PSF2 and PSF3. Interacts with PSF1 and SLD5.
Functions as part of the GINS complex which plays an essential role in the initiation of DNA replication by binding to DNA replication origins and facilitating the assembly of the DNA replication machinery.
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP46 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation.
Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is essential for mitotic growth and required for cell cycle progression.
Interacts directly with STH1. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin.
Present with 3940 molecules/cell in log phase SD medium.
Forms a stable complex with ATG17 and ATG29. Interacts directly with ATG29. The ATG17-ATG29-ATG31 complex interacts with the ATG1-ATG13 complex. Note=The interaction with the ATG1-ATG13 complex is induced by starvation.
Plays a role in starvation-induced autophagy. Involved in mitophagy. Functions with ATG17 and ATG29 at the preautophagosomal structure (PAS) in order to form normal autophagosomes under starvation conditions. May be involved in microtubule function, such as chromosome segregation and karyogamy.
Required for peroxisome inheritance. Acts as the peroxisome-specific receptor for the myosin V motor MYO2.
Despite weak sequence similarities, may correspond to the subunit B of a SPO11-containing topoisomerase 6 complex specifically required for meiotic recombination. Retains some of the structural features of the ancestral archaeal Top6B subunit (AC O05207).
Interacts with REC104; seems to form a functional unit with REC104. REC102-REC104 interacts with SKI8-SPO11 and this interaction is required for proper subcellular location of the proteins during the initiation of recombination. Interacts with MEI4, REC114 and SPO11.
Meiosis-specific. mRNA is spliced only during meiosis.
Reduces meiotic recombination several hundred fold. Specifically affects meiosis, and does not have any detectable mitotic phenotype.
Required for formation of the SPO11-mediated double-strand breaks (DSBs) that initiate meiotic recombination. May mediate the interaction between SPO11 subunits during meiosis. Also needed for homolog chromosome pairing, synaptonemal complex formation, and for the proper timing of the first meiotic division. Not required for mitosis and mitotic DNA repair mechanisms.
Present with 7400 molecules/cell in log phase SD medium.
Probable alcohol acetyltransferase that uses acetyl-CoA to synthesize acetate esters from various alcohols (Probable). Not involved in the synthesis of ethyl acetate (PubMed:28356220).
Processed by both the mitochondrial processing peptidase (MPP) and the mitochondrial octapeptidyl aminopeptidase (OCT1).
The gene contains the nested antisense gene NAG1.
Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of gene expression. 52 binding sites have been identified, distributed over 15 chromosomes. A member of the general regulatory factors (GRFs) which act as genome partitioners. Acts as a chromatin insulator which are known as STARs (Subtelomeric anti-silencing region). STARs prevent negative or positive transcription influence by extending across chromatin to a promoter.
Present with 6380 molecules/cell in log phase SD medium.
Belongs to the 6-phosphogluconate dehydrogenase family.
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family.
Carboxylation allows a single lysine to coordinate two zinc ions.
Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. Involved in the utilization of purines as secondary nitrogen sources, when primary sources are limiting.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase NEP1 family.
Depletion of EMG1 affects growth and leads to strong ribosome biogenesis defects, with defects in 20S pre-rRNA and mature 18S rRNA species.
Homodimer. Interacts with snoRNA U3. Interacts with NOP14 and MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.
S-adenosyl-L-methionine-dependent pseudouridine N(1)-methyltransferase that methylates pseudouridine at position 1189 (Psi1189) in 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. N1-methylation is independent on acp-modification at the N3-position of U1191. Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 (RPS19A/RPS19B) during the formation of pre-ribosomes.
Present with 5110 molecules/cell in log phase SD medium.
Putative zinc aminopeptidase which may be involved in ribosome biogenesis.
Component of the GINS complex which is a heterotetramer of SLD5, PSF1, PSF2 and PSF3.
Present with 2205 molecules/cell in log phase SD medium.
Belongs to the Clp1 family. NOL9/GRC3 subfamily.
Cell cycle-regulated with a peak of transcription at the G1/S boundary.
Polynucleotide 5'-kinase involved in rRNA processing. Required for the efficient termination by RNA polymerase I and the processing of the IST2 pre-rRNA internal transcribed spacer localized between the 5.8S and 25S rRNAs. May act by maintaining the phosphorylated status of the downstream RNT1 cleavage product, which in turn allows the torpedo activity of RAT1 to efficiently terminate Pol I transcription. In vitro, displays polynucleotide kinase activity on both single- and double-stranded RNA and on single-stranded DNA alone, but not double-stranded DNA alone.
Acts on phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol 1,4,5,-trisphosphate (PubMed:8194527, PubMed:8248783). PIK1 is part of a nuclear phosphoinositide cycle and could control cytokinesis through the actin cytoskeleton (PubMed:8194527). Involved in the response to mating pheromone (PubMed:8248783).
Belongs to the PI3/PI4-kinase family. Type III PI4K subfamily.
Acts as essential component of the kinetochore MIND complex, which is required for the spindle checkpoint and kinetochore integrity. MIND plays a role in establishing a bipolar spindle-kinetochore interaction by joining kinetochore subunits contacting DNA to those contacting microtubules. NNF1 is required for a number of nuclear functions. Cells depleted of NNF11 or containing a temperature-sensitive NNF1 mutation have elongated microtubules and become bi- and multinucleate. They also have a fragmented nucleolus and accumulate poly(A)+ RNA inside the nucleus.
Component of the MIND kinetochore complex, which is composed of at least MTW1, NNF1, NSL1 and DSN1.
Marked reduction in binding of the eIF-3 core complex to 40S ribosomes.
Present with 17900 molecules/cell in log phase SD medium.
Probable component of the eukaryotic translation initiation factor 3 (eIF-3) complex. Is not part of the eIF-3 core complex, with which it is associated in substochiometric amounts.
The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. CDC26 is required to tether the essential subunits APC9, CDC27 and CDC16 to the complex.
Was originally thought to be a suppressor of CDC26.
Functions together with the other V-type ATPase assembly factors in the endoplasmic reticulum to efficiently assemble the V-type ATPase membrane sector V(0).
Interacts with CBF5, NAF1 and NHP2. The interaction with NAF1 and SHQ1 does not occur when NAF1 is associated with the chromatin.
Involved in the early biogenesis steps of box H/ACA snoRNP assembly.
Present with 101000 molecules/cell in log phase SD medium.
Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis- Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events. COG3 is also involved in actin cytoskeleton organization.
Present with 4140 molecules/cell in log phase SD medium.
Interacts with PEX7; The interaction with PEX7 stabilizes PEX18 (PubMed:12167700, PubMed:11590152, PubMed:9864360, PubMed:11606420). Interacts with PEX13 (PubMed:12167700).
Involved in peroxisome biogenesis and the import of peroxisomal matrix proteins that contain the peroxisomal targeting sequence PTS2 (PubMed:12167700, PubMed:15456864, PubMed:9864360). Required for peroxisomal targeting of PEX7 and growth on oleate (PubMed:12167700, PubMed:15456864, PubMed:9864360).
Ubiquitinated in a UBC4/UBC5 dependent manner.
Plays an important role in the regulation of rRNA transcription. Binds near or at the enhancer region of rRNA repeating units. May have DNA polymerase activity, but it is not required for in vivo function.
Stimulated by PCNA and inhibited by aphidicolin.
Was originally thought to belong to the DNA polymerase type-B family based on conserved motifs (PubMed:12093911). Has later been shown to be unrelated to B class DNA polymerases. The observation of a low level of polymerase activity in vitro, which is not required for its essential cellular function, may require further validation (PubMed:12695662).
Catalyzes the deamination of L-threo-3-hydroxyaspartate to oxaloacetate and ammonia. Shows a high specificity towards L-threo-3-hydroxyaspartate as other 3-hydroxyaminoacids, i.e. D,L-erythro- and D-threo-3-hydroxyaspartate, D-threonine, L-threonine, D,L-allothreonine, D-serine, and L-serine, are not substrates for this enzyme. Exhibits no detectable serine racemase activity. Is responsible for the 3-hydroxyaspartate resistance of S.cerevisiae, and thus may be involved in the detoxification of naturally occurring 3-hydroxyaspartate.
Cells lacking this gene grow as well as the wild-type parent strain on SD medium, but fail to grow on hydroxyaspartate-containing agar plate.
Is strongly inhibited by hydroxylamine and EDTA in vitro.
Requires a divalent metal cation such as Mn(2+), Mg(2+), or Ca(2+).
Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain VTC4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation (PubMed:19390046). The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen (PubMed:25315834, PubMed:19390046). PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase (PubMed:25315834). VTC1 contributes only 3 transmembrane domains to the complex (Probable). The VTC complex also plays a role in vacuolar membrane fusion (PubMed:10480897, PubMed:11102525, PubMed:11823419, PubMed:12584253). Required for SEC18/NSF activity in SNARE priming, membrane binding of LMA1 and V(0) trans-complex formation (PubMed:11823419).
Present with 12074 molecules/cell in log phase SD medium.
Belongs to the Mediator complex subunit 22 family.
Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. SRB6/MED22 interacts directly with SRB4/MED17.
Present with 2181 molecules/cell in log phase SD medium.
Belongs to the eukaryotic ribosomal protein eL42 family.
In wild-type cells, 78% of L42 is monomethylated at both Lys-40 and Lys-55, and 22% are a mixture of species with either residue monomethylated.
Present with 13600 molecules/cell in log phase SD medium.
Present with 4846 molecules/cell in log phase SD medium.
Belongs to the mitochondrion-specific ribosomal protein mS35 family.
Present with 10600 molecules/cell in log phase SD medium.
Putative glucokinase involved in phosphorylation of aldohexoses and glucose uptake (By similarity). Involved in sporulation. Required for the full activation of the early meiotic inducer IME1.
Repressed by glucose through the MIG1 and MIG2 repressors.
Copper chaperone for apo superoxide dismutase 1 (SOD1). Binds copper ions and delivers them specifically to apo-SOD1.
Homodimer, and heterodimer with apo-SOD1. Zinc-binding at His-16 of CCS1 and 'Glu-43' of apo-SOD1 is required for this heterodimerization.
May play a role in polarity establishment and bud formation. The MSB1 gene may be functionally redundant.
Belongs to the actin-binding proteins ADF family. GMF subfamily.
Activated by it's association with the proteasome.
Associates with the regulatory particle (RP) of the proteasome.
Belongs to the peptidase C19 family. USP14/UBP6 subfamily.
Predominant proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Has proteasome-inhibitory activity and delays the degradation of ubiquitinated proteins to provide a time window allowing gradual deubiquitination of the substrate. Stabilizes the association of HUL5 with proteasomes and works in opposition to polyubiquitin elongation activity of HUL5.
Present with 6770 molecules/cell in log phase SD medium.
The N-terminal ubiquitin-like domain is required for proteasome association and UBP6 activation at the proteasome.
Involved in G-protein mediated signal transduction and in the regulation of polarized cell growth in pheromone-induced cells.
Component of the fork protection complex (FPC) consisting of TOF1 and CSM3. Interacts with WSS1 and ESC4.
Forms a fork protection complex (FPC) with CSM3 and which is required for chromosome segregation during meiosis and DNA damage repair. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors and protects stalled replication forks against the fork-releasing activity of RRM3 helicase.
Controls the cellular levels and subcellular distribution of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Does not utilize phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), nor phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P). Plays an essential role in a TGN (trans Golgi network)-to-early endosome pathway. Involved in endocytosis and acts as a negative regulator of the Slm pathway which modulates polarized actin assembly and growth.
IRS4 and TAX4 are both positive regulator of INP51 activity and phosphatidylinositol 4,5-bisphosphate turnover.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane. The K chain binds the dimeric form by interacting with the G and E chains.
Belongs to the dihydrofolate reductase family.
Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
Belongs to the gluconokinase GntK/GntV family.
Component of the nascent polypeptide-associated complex (NAC), a dynamic component of the ribosomal exit tunnel, protecting the emerging polypeptides from interaction with other cytoplasmic proteins to ensure appropriate nascent protein targeting. The NAC complex also promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane and blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum. EGD2 may also be involved in transcription regulation.
Part of the nascent polypeptide-associated complex (NAC), consisting of EGD2 and either EGD1 or BTT1. NAC associates with ribosomes via EGD1 or BTT1, and with the CCR4-NOT complex.
Present with 38016 molecules/cell in log phase SD medium.
The UBA domain is required for the stability of EGD1.
Ubiquitinated by the NOT4 E3 ligase and the UBC4 E2 ubiquitin conjugation enzyme.
May play a role in the regulation of DNA replication and cell cycle control.
Composed of a globular head region and a rod-like C-terminal coiled coil domain. The rodlike tail sequence is highly repetitive, composed of a heptapeptide repeat pattern characteristic of alpha-helical coiled coils. May form filamentous structures in the cell.
Homodimer. Dimerizes by parallel association of the tails, resulting in an elongated structure with two globular head domains side by side, and a long rod-like tail structure.
Required for protein transport from the ER to the Golgi complex.
Component of eisosomes, large cytoplasmic protein assemblies that localize to specialized domains termed MCCs on the plasma membrane.
Important for the biogenesis of eisosomes, large cytoplasmic protein assemblies that localize to specialized domains on the plasma membrane to cluster specific proteins at sites of membrane invaginations. Required for efficient incorporation of the eisosome component PIL1 into eisosomes.
Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by the guanine nucleotide-exchange factor (GEF) TRAPP complex, and inactivated by GTPase-activating protein (GAP) GYP3.
Interacts with YIF1, YIP3, YIP4 and YIP5. Interacts with the GEF SEC2. Interacts with TRS130.
Present with 4298 molecules/cell in log phase SD medium.
Required for protein transport through the secretory pathway. Probably involved in regulation of secretory vesicle formation at the trans-Golgi compartment. Mediates the proper polarized localization of SEC2, a GEF for SEC4, but does not alter the exchange activity of SEC2 on SEC4. Plays a role in autophagy.
Belongs to the cyclin family. PHO80 subfamily.
Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Negatively regulates the expression of phosphate-starvation-responsive genes under phosphate-rich conditions. The PHO80-PHO85 cyclin-CDK holoenzyme phosphorylates and inactivates the transcription factor PHO4, by preventing its association with the transcription factor PHO2 and the nuclear import receptor PSE1, and by promoting association with the nuclear export receptor MSN5, excluding PHO4 from the nucleus. PHO80-PHO85 phosphorylates and inactivates protein kinase RIM15 by retaining it in the cytoplasm, antagonizing RIM15-induced entry into stationary phase. PHO80-PHO85 also phosphorylates and inactivates the calcineurin-responsive transcription factor CRZ1, linking PHO85 to calcium signaling.
Forms a cyclin-CDK complex with PHO85. PHO80-PHO85 forms a stable complex with its inhibitor PHO81 under both high- and low-phosphate conditions, but PHO81 only inhibits the kinase upon phosphate starvation. Interacts with transcription factor PHO4.
Inhibited by the CDK inhibitor (CKI) PHO81 in response to phosphate starvation.
Phosphorylation of Ser-267 by PHO85 is required to form an active cyclin-kinase complex and for function.
Acts as an osmosensitive calcium-permeable cation channel (By similarity). Required for spore wall assembly and ascus formation.
Expressed in anaerobic conditions. Down-regulated by heme and the ROX1 and REO1 transcription factors in aerobic conditions.
Homodimer. Interacts with DYS1 and LIA1.
Lys-51 undergoes hypusination, a unique post-translational modification that consists in the addition of a butylamino group from spermidine to lysine side chain, leading to the formation of the unusual amino acid hypusine. eIF-5As are the only known proteins to undergo this modification, which is essential for their function.
Present with 14200 molecules/cell in log phase SD medium.
There are two genes for eIF-5A in yeast.
Was originally thought to be a translation initiation factor but further analysis (PubMed:19424157 and PubMed:19338753) clearly suggests that it is involved in translation elongation and not translation initiation.
mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Critical for the efficient synthesis of peptide bonds between consecutive proline residues. Can resolve ribosomal stalling caused by consecutive prolines during translation (By similarity). Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Essential for polarized growth, a process necessary for G1/S transition. May mediate large range of effects of the polyamine spermidine in the cell (By similarity).
Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Produced by alternative initiation at Met-41 of isoform 1. Major isoform.
Belongs to the class-II aminoacyl-tRNA synthetase family. Alax-L subfamily.
Conflicting data shows that it is not able to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala) in trans (PubMed:14663147). Another paper shows that this protein can edit mischarged Ser-tRNA(Ala) but not Gly-tRNA(Ala) in trans (PubMed:20010690). Experiments are not well detailed in either paper.
May function in trans to edit the amino acid moiety from incorrectly charged tRNA(Ala).
Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity (PubMed:11875065, PubMed:12684511). The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. GRX1 is less active as an oxidoreductase than GRX2 (PubMed:9571241, PubMed:18992757, PubMed:20417731).
In response to heat shock and osmotic stress.
ATP-dependent chaperone which uses the energy provided by ATP hydrolysis to generate mechanical force to disassemble protein complexes (PubMed:12006565, PubMed:17646390, PubMed:23185031, PubMed:24371142). Plays an essential role in the cytoplasmic maturation steps of pre-60S ribosomal particles by promoting the release of shuttling protein RLP24 from the pre-ribosomal particles (PubMed:17646390, PubMed:23185031, PubMed:24371142). This step facilitates the subsequent release of other shuttling proteins such as NOG1 and allows the transition of the pre-ribosomal particles to later maturation forms that bind REI1 (PubMed:17646390, PubMed:23185031, PubMed:24371142). Essential for viability (PubMed:8109176, PubMed:24371142).
Belongs to the AAA ATPase family. AFG2 subfamily.
Homohexamer; ATP binding induces oligomerization (PubMed:12006565, PubMed:23185031). Forms a ring-shaped particle of about 12 nm diameter, that displays 6-fold radial symmetry (PubMed:12006565). Associates with cytoplasmic pre-60S ribosomal particles containing ARX1, ALB1, RLP24 and NOG1 (PubMed:17646390). Binds to pre-60S ribosomal particles soon after their export from the nucleus and is released before REI1 and LSG1 are incorporated into the particles (PubMed:17646390). Hexameric form interacts with RLP24 (via C-terminal); the interaction recruits AFG2 to pre-60S ribosomal particles and promotes AFG2 ATPase activity and RLP24 release from pre-60S ribosomal particles (PubMed:23185031, PubMed:24371142). Interacts (via N-terminus) with nucleoporin NUP116 (via N-terminus); the interaction is required for RLP24 release from pre-60S ribosomal particles (PubMed:23185031).
The first ATP-binding region binds ATP with low affinity whereas the second ATP-binding region binds ATP with high affinity (PubMed:12006565). ATP hydrolysis mediated by the second ATP binding region releases RLP24 from pre-60S ribosomal particles whereas the ATP hydrolysis mediated by the first ATP binding region is subsequently required for RLP24 dissociation from AFG2, probably by disassembling AFG2 into monomers (PubMed:23185031, PubMed:24371142).
The hexamer is activated by RLP24 during pre-60S ribosomal particle maturation; RLP24 activates ATPase activity of both ATP-binding regions and increases cooperativity between AFG2 subunits (PubMed:23185031). The second ATP-binding region is inhibited by diazaborine; the inhibition requires prior ATP binding specifically to the second ATP-binding region (PubMed:24371142).
Component of the Smc5-Smc6 complex which consists of KRE29, MMS21, NSE1, NSE3, NSE4, NSE5, SMC5 and SMC6. Interacts with KRE29.
Catalyzes the synthesis of activated sulfate.
Although this protein has evidently no mitochondrial targeting pre-sequence, it is efficiently transported into mitochondria.
Belongs to the bacterial ribosomal protein bL17 family.
Homodimer; disulfide-linked, upon oxidation (PubMed:8041739). Interacts with YAP1 via transient disulfide linkages (PubMed:19106090).
Present with 378000 molecules/cell in log phase SD medium.
The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRX1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events (PubMed:2895105, PubMed:7961686, PubMed:10681558, PubMed:15210711, PubMed:19106090). Protects the cell against the oxidative stress caused by nascent-protein misfolding and aggregation (PubMed:24424024). Relays hydrogen peroxide as a signal to the transcription factor YAP1 by inducing the formation of intramolecular disulfide bonds in YAP1, which causes its nuclear accumulation and activation (PubMed:15706081, PubMed:19106090). Can act alternatively as peroxidase and molecular chaperone. Oxidative stress and heat shock exposure cause a reversible shift of the protein structure from low MW species to high MW complexes, triggering a peroxidase-to-chaperone functional switch. The chaperone function of the protein enhances resistance to heat shock (PubMed:15163410).
Required for the biogenesis of cytochrome c oxidase. Probably for its assembly into an active holoenzyme.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily.
Present with 9960 molecules/cell in log phase SD medium.
ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5'-splice site duplex to permit an effective competition for the 5'-splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5'-splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/U5 snRNP, facilitating the first covalent step of splicing.
Belongs to the DEAD box helicase family. DDX23/PRP28 subfamily.
Component of the U5 snRNP complex, composed of at least BRR2, PRP8, PRP28, DIB1, LIN1, SMB1, SMD1, SMD2, SMD3, SME1, SMX2, SMX3, and SNU114, associated with the U5 snRNA.
Serine/threonine-protein kinase which may phosphorylate the same targets substrates as PKH1 and PKH2, 2 upstream activators of PKC1.
Required for bud-site selection and cell separation. Also involved in nucleolar processing of pre-18S ribosomal RNA.
Belongs to the V-ATPase G subunit family.
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:7775427). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:7775427).
Subject to complex allosteric regulation. The enzyme can assume an active R-state, or an inactive T-state. Intermediate conformations may exist. AMP acts as allosteric inhibitor. AMP binding affects the turnover of bound substrate and not the affinity for substrate (By similarity).
The Pro/N-degron targets the protein for proteasomal degradation when cells are shifted to glucose-containing growth medium.
Ubiquitinated (PubMed:22645139). Targeted for proteasomal degradation when cells are shifted to glucose-containing growth medium (PubMed:12686616, PubMed:18508925, PubMed:22645139, PubMed:28126757).
Activator of the gluconeogenic enzymes FBP1 and PCK1 genes.
Could be the target of the SNF1/CAT1 - SNF4/CAT3 kinase complex.
May be involved in the preferential repair of active genes.
In carbon, ammonium, phosphate and sulfate starvation conditions.
Involved in the curing of prion [URE3]. Nuclear localization of this protein may suggest a role in transcription regulation, so it might exert an effect on [URE3] through known prion-curing chaperones or BTN2.
Belongs to the AB hydrolase superfamily. AB hydrolase 2 family.
Hydrolyzes fatty acids from S-acylated cysteine residues in proteins with a strong preference for palmitoylated G-alpha proteins over other acyl substrates. Mediates the deacylation of G-alpha proteins such as GPA1 in vivo, but has weak or no activity toward palmitoylated Ras proteins. Has weak lysophospholipase activity in vitro; however such activity may not exist in vivo.
May be used by cells under conditions in which the level of glycolytic flux is very low.
Not activated by fructose-1,6-bisphosphate.
Belongs to the bacterial ribosomal protein bS6 family.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NUP120 is part of the heptameric 0.5 MDa autoassembling NUP84 NPC subcomplex (NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1).
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP120 is involved in nuclear poly(A)+ RNA and pre-ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization.
Component of the monopolin complex composed of at least CSM1, LRS4 and MAM1. The complex associates with the kinetochore during late pachytene.
Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis.
Phosphorylated by CDC5. This phosphorylation is required for the location to the kinetochores during late pachytene.
Potential transcriptional regulator that is required to activate expression of a number of early meiotic genes including HOP1.
Acetylates spermine and probably also other polyamines such as putrescine or spermidine. May regulate the levels of polyamines on chromosomal DNA, which would modify chromatin structure and affect transcription or replication. Also able to acetylate arylalkylamines such as tryptamine and serotonin in vitro.
Belongs to the acetyltransferase family. AANAT subfamily.
Present with 8680 molecules/cell in log phase SD medium.
Functions as part of ribonuclease MRP (RNase MRP), which is involved in rRNA processing in mitochondria.
Belongs to the mediator complex subunit 11 family.
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex (PIC) with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. The essential MED11/22 heterodimer specifically functions in promoting stable PIC formation.
Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. MED11 forms a heterodimer with SRB6/MED22. The MED11/22 heterodimer binds to and stabilizes the central head subunit SRB4/MED17. Interacts with TFIIH subunit RAD3.
Belongs to the eukaryotic ribosomal protein eS8 family. Ribosome biogenesis protein NSA2 subfamily.
Component of the pre-66S ribosomal particle. Interacts with NOP7 and RRP1. Interacts with RSA4 (via WD repeats) (PubMed:25404745).
Involved in the biogenesis of the 60S ribosomal subunit. May play a part in the quality control of pre-60S particles. Under normal, rapid growth conditions, high levels of NSA2 would allow the progression of pre-60S particles through the ITS2 processing.
Present with 8660 molecules/cell in log phase SD medium.
To yeast killer toxin KHS and to YGL262w.
Belongs to the phosphatidylethanolamine-binding protein family.
Present with 6230 molecules/cell in log phase SD medium.
Belongs to the eukaryotic ribosomal protein P1/P2 family.
Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). The 5 acidic ribosomal P-proteins form the stalk structure of the 60S subunit. They are organized as a pentameric complex in which uL10/P0 interacts with 2 heterodimers, P1A-P2B and P1B-P2A (PubMed:16573688, PubMed:11431471).
The 4 small acidic ribosomal P-proteins from yeast can be classified into two couples of similar but not identical sequences. Each couple (P1A/P1B and P2A/P2B) is distinctly related to one of the two acidic ribosomal P-proteins P1/P2 present in multicellular organisms.
Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.
Interacts with the fatty acid elongation system components ELO3 and TSC13.
Present with 41900 molecules/cell in log phase SD medium.
Mannosyltransferase that transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage. Required for the attachment of the third mannose residue of O-linked saccharides.
Belongs to the eukaryotic ribosomal protein eL13 family.
Present with 54200 molecules/cell in log phase SD medium.
Component of a RSP5 ubiquitin ligase complex which specifies polyubiquitination and intracellular trafficking of the general amino acid permease GAP1 as well as other permeases such as PMA1. The RSP5-BUL1/2 complex is also necessary for the heat-shock element (HSE)-mediated gene expression, nitrogen starvation GLN3-dependent transcription and pressure-induced differential regulation of the 2 tryptophan permeases TAT1 and TAT2.
Component of the RSP5-BUL1/2 ubiquitin ligase complex composed of at least RSP5 and BUL1 or BUL2.
The PY-motif is required for the interaction with RSP5 ubiquitin-ligase and the HSE-mediated gene expression.
Component of the PAN1 actin cytoskeleton-regulatory complex composed of at least END3, PAN1, and SLA1. Interacts with SCD5, SLA2 and YAP1802. Interacts directly with PAN1; the interaction with PAN1 is prevented by PAN1 phosphorylation by PKR1.
Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization. END3 regulates PAN1 function by preventing phosphorylation of PAN1 by PKR1 and is also involved in the correct localization of SLA1 to the cell cortex, in the bipolar budding of diploid cells and the correct distribution of chitin at the cell surface.
Component of the fork protection complex (FPC) consisting of TOF1 and CSM3.
Forms a fork protection complex (FPC) with TOF1 which is required for chromosome segregation during meiosis and DNA damage repair. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors and protects stalled replication forks against the fork-releasing activity of RRM3 helicase.
Belongs to the glutamate--cysteine ligase type 3 family.
Catalyzes the ATP-dependent condensation of cysteine and glutamate to form the dipeptide gamma-glutamylcysteine (gamma-GC), the first and rate-limiting step in the production of glutathione (GSH).
GSS(-) is a potent inhibitor of RDL1, since the presence of the sulfur dioxygenase strongly increases the RDL1 catalytic activity (PubMed:24981631).
Present with 7470 molecules/cell in log phase SD medium.
Thiosulfate:glutathione sulfurtransferase (TST) required to produce S-sulfanylglutathione (GSS(-)), a central intermediate in hydrogen sulfide metabolism (PubMed:24981631). Provides the link between the first step in H(2)S metabolism performed by the sulfide:quinone oxidoreductase (SQOR) which catalyzes the conversion of H(2)S to thiosulfate, and the sulfur dioxygenase (SDO) which uses GSS(-) as substrate (PubMed:24981631). The thermodynamic coupling of the irreversible SDO and reversible TST reactions provides a model for the physiologically relevant reaction with thiosulfate as the sulfane donor (PubMed:24981631).
The eukaryotic translation initiation factor 3 (eIF-3) core complex is composed of TIF32, PRT1, NIP1, TIF34 and TIF35. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a multifactor complex (MFC) that may bind to the 40S ribosome.
Belongs to the metallothionein superfamily. Type 12 family.
Contains 1 metal-binding domain: 6 to 8 copper ions are chelated within a single copper-thiolate cluster and are coordinated via cysteinyl thiolate bridges to 10 cysteine ligands. 6 copper ions are trigonally coordinated, whereas the other 2 are only digonally coordinated.
Protects the cell against copper toxicity by tightly chelating copper ions. May also act as a depository for copper designated for the effective transfer into the apo forms of copper proteins.
There are 2 copies for copper thionein in yeast. The 2 identical copies CUP1-1 and CUP1-2 are arranged in tandem.
Belongs to the isocitrate and isopropylmalate dehydrogenases family.
Binds 1 Mg(2+) or Mn(2+) ion per subunit.
May function in the production of NADPH for fatty acid and sterol synthesis.
Present with 2620 molecules/cell in log phase SD medium.
Component of the ASH1 mRNP composed of at least PUF6, SHE2, SHE3, SHE1 and the ASH1 mRNA. Interacts with SHE2 and FUN12.
Present with 21500 molecules/cell in log phase SD medium.
RNA-binding protein involved in post-transcriptional regulation. Component of the ASH1 mRNP which transports the ASH1 mRNA to the distal tip of the bud, where the ASH1 protein is translated and targeted to the daughter cell nucleus. Binds to the ASH1 3'-UTR containing the PUF consensus UUGU segment and represses its translation. This silencing of ASH1 mRNA is critical for asymmetric seggregation of ASH1 to the daughter cell nucleus.
phosphorylation by CK2 relieves translational repression activity.
Belongs to the FAD-binding oxidoreductase/transferase type 4 family.
Catalyzes the reversible oxidation of (R)-2-hydroxyglutarate to 2-oxoglutarate coupled to reduction of pyruvate to (R)-lactate. Can also use oxaloacetate as electron acceptor instead of pyruvate producing (R)-malate (PubMed:26774271). In addition to its enzymatic role it could play an important role in the yeast cell morphology (PubMed:10509019).
Expression is induced by mild heat-stress on a non-fermentable carbon source (PubMed:14561723). Expression is also induced upon entry into stationary phase and upon nitrogen deprivation (PubMed:11102521). Expression is repressed by inosine and choline in an OPI1-dependent manner (PubMed:12871953).
Plays a role in haploid invasive growth under conditions of nutrient insufficiency, suggesting that the function of the MEMO1 family in cell motility/invasion is conserved across species.
Belongs to the V-ATPase C subunit family.
Present with 21114 molecules/cell in log phase SD medium.
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:10781598, PubMed:11777935, PubMed:1730668, PubMed:8416931). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:8416931). Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity (PubMed:15792803). Reversibly leaves the enzyme after glucose depletion, causing the catalytic subcomplex V1 to detach from the V0 section (PubMed:15792803).
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and VOA1) (PubMed:25971514). Interacts directly with VMA4 (PubMed:15751969).
Component of the monopolin complex composed of at least CSM1, LRS4 and MAM1. The complex associates with the kinetochore. Interacts with CDC46, CDC47, GIC1, GIC2, MCM3 and NUR1.
Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis. Also plays a mitotic role in DNA replication.
Binds specifically G4 quadruplex (these are four-stranded right-handed helices, stabilized by guanine base quartets) and purine motif triplex (characterized by a third, antiparallel purine-rich DNA strand located within the major groove of a homopurine stretch of duplex DNA) nucleic acid structures. These structures may be present at telomeres or in rRNAs. Acts with CDC13 to control telomere length homeostasis. Involved in the control of the apoptosis-like cell death.
Interacts with CDC13. Associates with mature 80S ribosomes. Associates with the telomere-proximal Y' element.
Present with 46842 molecules/cell in log phase SD medium.
Mitochondrial amino-acid transporter that mediates transport of serine into mitochondria.
Present with 9290 molecules/cell in log phase SD medium.
Component of ATP-dependent clamp loader (RFC and RFC-like) complexes for DNA clamps, such as the POL30/PCNA homotrimer and the checkpoint clamp DDC1:MEC3:RAD17 complex. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA. Component of the replication factor C (RFC or activator 1) complex which loads POL30/PCNA and acts during elongation of primed DNA templates by DNA polymerase delta and epsilon. RFC has an essential but redundant activity in sister chromatid cohesion establishment. Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. Component of the RFC-like RAD24-RFC complex which loads the checkpoint clamp DDC1:MEC3:RAD17 complex and is involved in DNA repair pathways. Component of the RFC-like ELG1-RFC complex which appears to have a role in DNA replication, replication fork re-start, recombination and repair. RFC3 supplies a catalytic site to the ATP site of RFC4.
Replication factor C (RFC) is a heteropentamer of subunits RFC1, RFC2, RFC3, RFC4 and RFC5 and forms a complex with POL30/PCNA in the presence of ATP. Component of the RAD24-RFC complex which consists of RAD14, RFC2, RFC3, RFC4 and RFC5 and associates with the checkpoint clamp DDC1:MEC3:RAD17 complex. Component of the ELG1-RFC complex which consists of ELG1, RFC2, RFC3, RFC4 and RFC5. Component of the CTF18-RFC complex, which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. RFC3 interacts with ECO1 and POL30/PCNA.
Inhibitory regulator of the Ras-cyclic AMP pathway in S.cerevisiae. Stimulates the GTPase activity of Ras proteins.
With ARG80, ARG82 and MCM1, coordinates the expression of arginine anabolic and catabolic genes in response to arginine.
Invasive growth defect with elongated cell morphology.
Present with 4050 molecules/cell in log phase SD medium.
Required for viability of cells lacking mtDNA.
Catalyzes the covalent attachment of ubiquitin to other proteins (PubMed:17550898). Mediates the selective degradation of short-lived and abnormal proteins (PubMed:17550898). Mediates ubiquitination of PEX5 (PubMed:17550898).
Defective activation of the ribosome quality control (RQC) pathway.
Component of the mitochondrial large ribosomal subunit (mt-LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. Unlike bacterial L5, uL5m does not bind zinc.
Belongs to the Mediator complex subunit 17 family.
Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. The head module may also interact with the TFIIF complex. SRB4/MED17 interacts directly with MED6, MED11, ROX3/MED19, SRB2/MED20 and SRB6/MED22. Interacts directly with the activator GAL4.
The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Positively regulates FAB1 kinase activity. Major activator of FAB1 during hyperosmotic shock and can elevate levels of PtdIns(3,5)P2 in the absence of VAC14 and FIG4. Directly involved in vacuolar membrane scission. Required for normal vacuole acidification, inheritance and morphology.
This is 1 of 2 proteins that can stabilize the ATPase-inhibitor complex, which normally dissociates when externally added ATP has been consumed.
Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
Component of complex II composed of four subunits: a flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a large and a small subunit.
Present with 9540 molecules/cell in log phase SD medium.
Subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDH1 and SDH2 form the catalytic dimer. Electrons flow from succinate to the FAD bound to SDH1, and sequentially through the iron-sulfur clusters bound to SDH2 and enter the membrane dimer formed by SDH3 and SDH4.
Present with 26300 molecules/cell in log phase SD medium.
Required for TORC1 to properly control gene expression and chronological life span. Plays an essential role in initiation of the G0 program by preventing the degradation of specific nutrient-regulated mRNAs via the 5'-3' mRNA decay pathway.
Produced by +1 ribosomal frameshifting between codon Leu-431 and Gly-432 of the YDR261W-A ORF.
Involved in cytokinesis by recruiting INN1 to the bud neck. Cooperates with INN1 to stimulate the synthesis of the primary septum (PS) by CHS2.
By nutrient, osmotic, oxidative and heat stress. Up-regulated during the diauxic shift.
Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP) or tri-methyl guanosine nucleoside monophosphate (m3(2,2,7)GMP), respectively. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to (m(7)GMP) and m3(2,2,7)GMP, respectively (PubMed:22985415). May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCS1 to m7GMP (PubMed:14523240). Binds to m7GpppG and strongly to m7GDP. May also regulate the 5'->3' exoribonucleolytic mRNA decay pathway in a cap-independent manner. Negatively regulates trehalase activity.
Homodimer. Forms heterodimer with DCS2; the interaction inhibits the DCS1 scavenger decapping activity during post-diauxic growth.
Phosphorylated. Phosphorylation occurs upon glucose deprivation.
The C-terminal histidine triad (HIT) motif and the N-terminal domain are required for the decapping activity.
The hydrolytic product 7-methylguanosine diphosphate (m7GDP) efficiently inhibits the decapping scavenger activity and acts as a competitive inhibitor in vitro.
Interacts with the HSP70 family members SSA1, SSA4, and SSB1. These interactions are strongly reduced by ADP and ATP.
Present with 3346 molecules/cell in log phase SD medium.
Stimulator of ATPase activity of molecular chaperones of the HSP70 family (principally of the SSA class). Stimulation is important for HSP70-substrate complex dissociation after folding of newly synthesized or refolded proteins. SNL1 is probably involved in nuclear pore biogenesis and in particular the folding or refolding of misfolded NUP116, GLE2 and NIC96.
Co-chaperone that binds to the molecular chaperones Hsp90 (HSC82 and HSP82) and Hsp70 (SSA1). Stimulates SSA1 ATPase activity, but not Hsp90 ATPase activity. Involved in only a subset of Hsp90 functions.
Monomer. Component of Hsp70 and Hsp90 chaperone complexes. Interacts (via TPR repeats) with HSC82 and HSP82 (via C-terminal MEEVD pentapeptide). Interacts with CPR7, SSA1 and SPI1.
Structure-specific DNA-binding protein with a preference for cruciform structures. Also binds single-stranded DNA (ssDNA). Functions together with SGS1 and TOP3 to maintain genome integrity. Essential for proper meiotic cell division. Required for normal S-phase progression and DNA damage response. Required for resistance to the DNA-damaging agent methyl methanesulfonate (MMS).
Belongs to the UbiA prenyltransferase family.
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate.
Decreases nucleosomal density (PubMed:25406467, PubMed:19683497). Increases HTA1 RNA level; simultaneous disruption RTT109 alleviates the effect (PubMed:22156209, PubMed:19683497).
Histones H3 and H4 chaperone involved in the nucleosome formation and heterochromatin silencing. Required for the deposition of H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role in the transcriptional regulation of the cell-cycle dependent histone genes by directly recruiting the SWI/SNF and RSC chromatin remodeling complexes to the histone genes in a cell cycle dependent manner. In cooperation with HIR and ASF1, creates a repressive structure at the core histone gene promoter and contributes to their repression outside of S phase. Involved in regulation of Ty1 transposition.
Homodimers (via the N-terminal domain) (PubMed:22307274). Interacts with the SWI/SNF complex (PubMed:21698254). Interacts with the RSC complex (PubMed:21698254). Interacts with the HIR complex (PubMed:21698254, PubMed:19683497). Interacts with the CAF-1 complex (PubMed:19683497). Interacts with RLF2 (PubMed:16157874). Interacts with SIR4 (PubMed:17410207). Interacts with YTA7 (PubMed:22156209). Interacts with CAC2 (PubMed:19683497). Interacts with HPC2 (PubMed:19683497). Interacts with HIR2 (PubMed:19683497). Interacts with MSI1 (PubMed:19683497). Interacts with HIR1 (PubMed:19683497). Interacts with histone H3 (PubMed:16157874, PubMed:20007951, PubMed:20188666, PubMed:21444721, PubMed:22307274). Interacts with histone H4 (PubMed:16157874, PubMed:20007951, PubMed:21444721, PubMed:22307274).
Present with 11100 molecules/cell in log phase SD medium.
The N-ter domain (residues 1-67) homodimerizes and interacts with H3-H4 independently of acetylation while the double pleckstrin-homology (PH) domain (residues 68-301) binds the 'Lys-56'-containing region of H3.
Present with 3360 molecules/cell in log phase SD medium.
Belongs to the proteasome subunit p55 family.
Acts as an osmosensitive calcium-permeable cation channel.
Forms part of complex II containing four subunits: a flavoprotein (FP), an iron-sulfur protein (IP) and a cytochrome b composed of two integral membrane proteins.
Membrane-anchoring mono-heme cytochrome b subunit of succinate dehydrogenase (SDH) that is involved in system II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDH3 and SDH4 form the membrane dimer that anchors the catalytic dimer formed by SDH1 and SDH2 to the matrix surface of the mitochondrial inner membrane. Electrons originating from the catalytic dimer enter the membrane dimer for ubiquinone reduction.
The heme is bound between the two transmembrane subunits.
Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxin TSA1. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and as thioltransferase.
Forms a transient disulfide bond with TSA1 during the reduction of cysteine sulfinic acid (-SO2H).
Component of the monopolin complex composed of at least CSM1, LRS4 and MAM1. The complex associates with the kinetochore.
Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis. Involved in rDNA silencing.
Belongs to the peptidase C56 family. HSP31-like subfamily.
Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals. Involved in protection against reactive oxygen species (ROS) (By similarity). Important for viability in stationary phase. May negatively regulate TORC1 in response to nutrient limitation (PubMed:24706893).
Induced during entry into stationary phase.
Results in higher sensitivity to oxidative stress, reduced thermotolerance, accumulation of higher levels of reactive oxygen species, and reduced chronological life span.
Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and also probably that of HMP to HMP-P.
In the C-terminal section; belongs to the thiaminase-2 family.
In the N-terminal section; belongs to the ThiD family.
Involved in the sorting of ubiquitinated cargo proteins at the multivesicular body (MVB).
Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2)) required for protein glycosylation.
Present with 3550 molecules/cell in log phase SD medium.
Adapter protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit APL4 and beta-type subunit APL2), a medium adaptin (mu-type subunit APM1) and a small adaptin (sigma-type subunit APS1) (PubMed:10564262). AP-1 interacts with clathrin (PubMed:10564262). Also a component of the AP-1R complex composed of at least APM2, APL4 and APS1 (PubMed:26658609).
Adaptins are components of the adapter complexes which link clathrin to receptors in coated vesicles (PubMed:10564262). Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration (PubMed:10564262). The AP-1 complex interacts directly with clathrin (PubMed:10564262). Component of the AP-1-related (AP-1R) complex, an adapter protein complex that mediates sorting of cargo SNARE SNC1 (PubMed:26658609). In contrast to the APM1-containing AP-1 complex, AP-1R is incapable of sorting CHS3 (PubMed:26658609).
Present with 4850 molecules/cell in log phase SD medium.
Acts as a positive activator of the GCN2 protein kinase activity in response to low amino acid, carbon, or purine availability (PubMed:8497269, PubMed:24333428. PubMed:10733573). Component of the GCN1-GCN20 complex that forms a complex with GCN2 on translating ribosomes; during this process, GCN1 seems to act as a chaperone to facilitate delivery of uncharged tRNAs that enter the A site of ribosomes to the tRNA-binding domain of GCN2, and hence stimulating GCN2 kinase activity (PubMed:7621831, PubMed:9234705, PubMed:15722345). Participates in the repression of global protein synthesis and in gene-specific mRNA translation activation, such as the transcriptional activator GCN4, by promoting the GCN2-mediated phosphorylation of eukaryotic translation initiation factor 2 (eIF-2-alpha/SUI2) on 'Ser-52', and hence allowing GCN4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:8497269, PubMed:10801780, PubMed:11350982, PubMed:15722345).
Inhibits GCN4 derepression in glucose, amino acid, or purine-starved cells.
Interacts (via N- and C-terminus) with GCN2 (via N-terminal RWD domain); this interaction stimulates GCN2 kinase activity in a GCN20-dependent manner in response to amino acid starvation (PubMed:10775272, PubMed:11101534, PubMed:10801780, PubMed:11350982, PubMed:15126500, PubMed:15722345, PubMed:21849502). Interacts (via C-terminus) with GCN20 (via N-terminus); this interaction stimulates GCN2 kinase activity in response to amino acid starvation (PubMed:7621831, PubMed:9234705, PubMed:11101534). The GCN1-GCN20 complex interacts with GCN2 on translating ribosomes in amino acid-starved cells; GCN1 may bind near the ribosomal A-site and promotes the transfer of uncharged tRNAs from the A-site to the tRNA-binding domain in GCN2 for its subsequent kinase activation, and hence allowing GCN4 translational activation and derepression of amino acid biosynthetic genes (PubMed:7621831, PubMed:9234705, PubMed:10775272, PubMed:11101534). Interacts (via C-terminus) with YIH1 (via N-terminus); this interaction reduces the GCN1-GCN20 complex formation and prevents the interaction of GCN1 with GCN2 and GCN2 kinase activation in amino acid-starved cells (PubMed:15126500, PubMed:21239490, PubMed:22404850). Interacts with GIR2; this interaction prevents the interaction of GCN1 with GCN2 and GCN2 kinase activation in amino acid-starved cells (PubMed:19448108). Interacts (via middle region) with RPS10A and RPS10B; these interactions are direct and promote GCN2 kinase activation (PubMed:25437641). Associates (via N-terminus) with ribosomes; this association is stimulated in a ATP- and GCN20-dependent manner and is necessary to activate GCN2 kinase activity (PubMed:7621831, PubMed:9234705, PubMed:11101534, PubMed:15722345, PubMed:19448108, PubMed:21849502, PubMed:22888004, PubMed:25437641).
The EF3-like region is necessary and sufficient for interaction with GCN20 (PubMed:9234705).
Catalytic subunit in the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.
Inhibited by Ras, probably via the interaction between RAS2 and ERI1.
Was originally thought to be involved in transcription.
Involved in cytochrome c oxidase assembly or stability.
The twin Cx9C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system and the subsequent transfer of disulfide bonds by dithiol/disulfide exchange reactions to the newly imported protein.
No growth on non-fermentable carbon sources like glycerol and lactate and sensitivity to calcofluor white.
Probable transcription factor involved in the stress response.
Involved in chromosome segregation during sporulation.
Proteolytically removes the C-terminal three residues of farnesylated A-factor mating pheromone. Also acts to cleave the N-terminal extension of the pheromone. Does not act on Ras.
Constituent of COPII-coated endoplasmic reticulum-derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. Possesses a C-terminal dilysine motif that interacts with COPI coat subunits. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum.
Present with 51700 molecules/cell in log phase SD medium.
Belongs to the flavin monoamine oxidase family.
Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance.
In contrast to some bacterial and mammalian enzymes, MGT1 is not induced by alkylating agents.
Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. Prefers double-stranded DNA over single-stranded DNA as substrate.
Present with 150 molecules/cell in log phase YPD medium, but not detectable in stationary phase cells.
This enzyme catalyzes only one turnover and therefore is not strictly catalytic. According to one definition, an enzyme is a biocatalyst that acts repeatedly and over many reaction cycles.
Binds 1 divalent metal cation per subunit.
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. KAE1 likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Required for normal transcription at a number of loci in yeast.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Forms a heterodimer with the catalytic subunit TRM8.
Present with 5910 molecules/cell in log phase SD medium.
Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
Component of the TIM23 complex, at least composed of TIM23, TIM17, TIM50 and TIM21. Interacts directly with TIM23. Interacts with preproteins in transit.
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Required to direct preproteins in transit and direct them to the channel protein TIM23, and possibly facilitates transfer of the translocating proteins from the TOM complex to the TIM23 complex. Does not act as a structural subunit of the TIM23 complex but plays a dynamic role in protein import. Has no phosphatase activity.
The FCP1 homology domain does not contain the canonical D-x-D-x-[TV] active site, suggesting that it probably does not display phosphatase activity.
The mitochondrial intermembrane region is required for generation but not stabilization of the TIM23 complex.
Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. SPT3 interacts directly with TBP (TATA-binding protein). Component of the SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9.
Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SPT3 is required for recruitment of TATA-binding protein (TBP) to SAGA-dependent promoters. During SAGA-mediated transcriptional inhibition, SPT3 and SPT8 prevent binding of TBP to the TATA box. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. SPT factors 3, 7 and 8 are required for the initiation of Ty transcription from the delta promoter. SPT3 regulates Ty1 as well as the mating factor genes.
Present with 33200 molecules/cell in log phase SD medium.
Component of the HOPS complex which is composed of PEP5, VPS16, PEP3, VPS33, VPS39 and VPS41. HOPS associates with phosphoinositides and the PX domain of VAM7. Interacts with IVY1 and VAM7.
Essential for vacuolar biogenesis, maturation and function. Involved in the sorting of vacuolar proteins from the Golgi apparatus and their targeting to the vacuole. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion.
Homolog of SDH4, but seems not to be a stoichiometric subunit of either the succinate dehydrogenase (SDH) complex or the mitochondrial inner membrane translocase TIM22 complex.
High-affinity transport of valine and tyrosine. Low-affinity transport of tryptophan. Can also transport L-cysteine.
Required for sporulation where it is believed to have a role in meiotic nuclear division.
Belongs to the carnosine N-methyltransferase family.
N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His).
By exposition to pheromone (A-factor) secreted by the opposite mating type cells (type A).
Cell surface glycoprotein promoting cell-cell contact to facilitate mating. S.cerevisiae A and alpha cells express the complementary cell surface glycoproteins A-agglutinin and alpha-, respectively, which interact with one another to promote cellular aggregation during mating.
N-glycosylated, and O-glycosylated by both PMT1 and PMT2.
Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid (PubMed:22633490). Involved in coenzyme Q (CoQ) biosynthesis, catalyzing the last step in the tyrosine to 4-hydroxybenzoate (4-HB) pathway. Oxidizes 4-hydroxybenzaldehyde (4-Hbz) to 4-HB, the aromatic precursor for coenzyme Q (PubMed:27693056, PubMed:27669165).
Belongs to the DNA mismatch repair MutL/HexB family.
Heterodimer of MLH1 and MLH3, called MutLbeta, which is involved in correction of a specific subset of IDLs when associated with MutSbeta. Forms a ternary complex with a SGS1-TOP3 heterodimer during meiosis.
Involved in DNA mismatch repair (MMR), correcting insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of the MutLbeta heterodimer, which probably forms a ternary complex with the MutSbeta heterodimer that initially recognizes the DNA mismatches. This complex is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in promoting meiotic crossing-over and is involved in maintaining the genetic stability of simple sequence repeats by correction of frameshift intermediates.
Belongs to the adenylate kinase family. AK2 subfamily.
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Present with 123000 molecules/cell in log phase SD medium.
The phenotype of disruption mutants is pet, showing that complementation by another adenylate kinase isozyme occurs only under fermentative conditions. The disruption completely destroys the activity in mitochondria, whereas in the cytoplasmic fraction about 10% is retained.
Expressed periodically during cell division with a peak during M phase.
May be involved in protein-linked oligosaccharide phosphorylation since the deletion reduces the negative charge of the cell surface. Involved in the resistance to EDTA, cadmium chloride, cycloheximide, 6-dimethylaminopurine, methyl caffeate, beta-chloro-L-alanine, caffeine and cerulenin.
Present with 295 molecules/cell in log phase SD medium.
May be required for the activity of an ISWI chromatin-remodeling complex.
Abnormal mRNA processing; 3' termini are cleaved but transcripts lack full-length poly(A) tails (PubMed:9819425). Decreases HO mRNA translation (PubMed:15082763).
Interacts (via C-terminus) with MKT1 (via C-terminus) (PubMed:15082763). Interacts with FIR1, IGO1, LSM12, PBP4 and PAB1 (PubMed:15121841, PubMed:16702403, PubMed:20471941, PubMed:9819425).
Involved in pre-mRNA polyadenylation (PubMed:15121841, PubMed:9819425). May act to repress the ability of PAB1 to negatively regulate polyadenylation (PubMed:9819425). Negative regulator of poly(A) nuclease (PAN) activity (PubMed:15121841). Promotes mating-type switching in mother cells by positively regulating HO mRNA translation (PubMed:15082763). Localizes MKT1 to polysomes (PubMed:15082763).
Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of at least PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. Interacts with the CTD domain of RPB1/RNA polymerase II; the interaction is enhanced upon phosphorylation of the RPB1 CTD domain. Interacts with PCF11.
RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. May be involved in poly(A)-site recognition. May be involved in the association of the CPF, CPFIA and RNA polymerase II complexes.
Has phosphatase activity in vitro. Involved in the response to sodium and lithium ion stress (but not to potassium or sorbitol stress) by inducing transcription of the sodium pump ENA1/PMR2. Acts through a calcineurin-independent pathway and is functionally redundant with PSR2. Also involved in the general stress response; acts together with WHI2 to activate stress response element (STRE)-mediated gene expression, possibly through dephosphorylation of MSN2.
Present with 5620 molecules/cell in log phase SD medium.
Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint.
Present with 97100 molecules/cell in log phase SD medium.
Component of the mitochondrial large ribosomal subunit (mt-LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. uL23m forms the wall of the exit tunnel (PubMed:2060626, PubMed:9151978, PubMed:24675956). Interacts with the C-terminus of OXA1 (PubMed:14657017).
Present with 2200 molecules/cell in log phase SD medium.
Cystine/H(+) symporter that mediates export of cystine, the oxidized dimer of cysteine, from vacuoles/endodomes.
Inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin.
Not essential for mitotic growth but is necessary for normal morphogenesis. Involved in the organization and/or function of the actin cytoskeleton.
Interacts with SKP1. Component of the probable SCF(YDR131C) complex containing CDC53, SKP1, RBX1 and YDR131C.
Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family.
Sodium-phosphate symporter. Active in early growth phase.
The gene for PHO89 is only transcribed under conditions of phosphate limitation.
E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (PubMed:18644345, PubMed:19687296, PubMed:22471590, PubMed:35768507). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (PubMed:35768507). PEX10 also regulates PEX5 recycling by acting as a E3 ubiquitin-protein ligase (PubMed:18644345, PubMed:15283676, PubMed:35768507). When PEX5 recycling is compromised, PEX10 catalyzes polyubiquitination of PEX5 during its passage through the retrotranslocation channel, leading to its degradation (PubMed:35768507).
The E3 ubiquitin-protein ligase activity is stimulated by PEX12.
Component of the 18S U1 snRNP particle, a subcomplex of the spliceosome. Interacts with the nuclear cap-binding complex CBC1-CBC2 (yCBC). Directly contacts intronic sequences of substrate pre-RNA.
Present with 361 molecules/cell in log phase SD medium.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Kinesin II subfamily.
Interacts (via its ubiquitin-like domain) with CDC48 (via N-terminus). Associates with the 26S proteasome. Specifically interacts with the regulatory particle (RP) subunit RPN2. Exposure to arsenite, a known inducer of protein misfolding resulting in accumulation of polyubiquitinated conjugates, enhances the association with the proteoasome. Binds to ubiquitinated proteins conjugated to a 4 or more molecule ubiquitin chain. Binding to ubiquitinated proteins is zinc-dependent.
Promotes efficient arsenite-induced clearance of stress granules (SGs) (PubMed:29804830). May have a role in the ubiquitin-proteasome system (UPS) protecting cells from metalloid-induced proteotoxicity (PubMed:24121501, PubMed:24297164).
Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Beta adaptin is a subunit of the plasma membrane adaptor.
Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit APL3 and beta-type subunit APL1), a medium chain (mu-type subunit APM4) and a small adaptin (sigma-type subunit APS2). Interacts with APS2.
Catalytic component of the DSC E3 ubiquitin ligase complexes that tag proteins present in Golgi, endosome and vacuole membranes and function in protein homeostasis under non-stress conditions and support a role in protein quality control (PubMed:25078903, PubMed:29355480). Mediates ubiquitination of vacuolar proteins such as CPS1, PPN1, PEP12 and other proteins containing exposed hydrophilic residues within their transmembrane domains, leading to their sorting into internal vesicles in late endosomes (PubMed:11788821). Targets also the unpalmitoylated endosomal SNARE TLG1 to the MVB pathway (PubMed:15973437).
Component of the DSC E3 ligase complexes composed of at least TUL1, DSC2, DSC3, UBX3, CDC48 as well as VLD1 for the vacuole-localized complex or GLD1 for the Golgi/endosome-localized complex (PubMed:25078903, PubMed:29355480). Interacts with UBC4 (PubMed:11788821).
Belongs to the metallophosphoesterase superfamily.
Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family.
Probable transporter involved in ethionine resistance. Overproduction leads to accumulation of S-adenosylmethionine.
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.
Phosphorylated at multiple sites in response to pheromone.
Serine/threonine protein kinase required for cell-type-specific transcription and signal transduction in yeast. It is thought that it is phosphorylated by the ste11 protein kinase and that it can phosphorylate the FUS3 and or KSS1 kinases.
Involved in the transport of siderophore ferrichrome and so has a role in iron homeostasis.
Non-catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. May be required to embody the molecular ruler of the complex.
Present with 531 molecules/cell in log phase SD medium.
tRNA splicing endonuclease is a heterotetramer composed of SEN2, SEN15, SEN34 and SEN54. Interacts directly with SEN2.
By PDR1 through its PDRE-like promoter element.
Defective sporulation accompanied by the appearance of pseudohyphal-like projections.
Phosphorylated during meiosis. During meiosis, exists in both unphosphorylated and phosphorylated forms with the highest degree of phosphorylation occurring in mid-meiosis.
Catalyzes the covalent attachment of ubiquitin to other proteins (PubMed:1869573) (By similarity). Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium (PubMed:9737955, PubMed:10811607, PubMed:12686616). Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:9737955, PubMed:10811607, PubMed:12686616, PubMed:28126757).
Belongs to the steroid 5-alpha reductase family. Polyprenol reductase subfamily.
Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism.
Suppression of filamentatous growth, defects in cell polarity, and cellular elongation, due to defects in N-glycosylation.
Involved in regulating the activity of the plasma membrane proton pump PMA1.
The KEN and D (destructive) boxes are required for the cell cycle-controlled ALK1 degradation by the anaphase promoting complex (APC) pathway.
Heterodimer (PubMed:6389537, PubMed:3029058). The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an mRNA 5'-triphosphate monophosphatase (PubMed:6389537, PubMed:3029058).
Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-diphosphate terminus of RNA via a covalent enzyme-GMP reaction intermediate.
Interacts directly with SPO21/MPC70, NUD1, SPO74 and SPC42. Probable component of a spindle pole body (SPB) complex composed of ADY3, SSP1, DON1, MPC54, SPO21/MPC70, NUD1 and CNM67.
Involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation.
Meiosis-specific. Expressed during meiosis II, from 3 to 9 hours after induction of sporulation. Not expressed during mitosis.
Homomultimer. Interacts with YPT7 and VPS33.
May be required for vacuolar fusion. Overexpression leads to fragmentation of vacuoles, missorting of the vacuolar enzyme carboxypeptidase Y (CPY) to the exterior of the cell and accumulation of multivesicular bodies inside the cell.
Belongs to the NADPH-dependent diflavin oxidoreductase NDOR1 family.
In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
In the N-terminal section; belongs to the flavodoxin family.
Interacts with DRE2; as part of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery.
NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery (PubMed:20802492). Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of DRE2, another key component of the CIA machinery (PubMed:20802492, PubMed:21902732). In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins (PubMed:20802492). Positively controls H(2)O(2)-induced cell death (PubMed:19194512).
5-fold reduced production of the first heme precursor 5-aminolevulinic acid (ALA) and 2-fold reduction in total heme. In combination with a disruption of HEM25 or an inactivated HEM1, abrogates mitochondrial respiration.
ATP-dependent unfoldase that stimulates the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase (HEM1), thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis. Up-regulates heme biosynthesis.
Homohexamer that forms a ring structure; this hexamerization requires ATP binding (By similarity). Interacts with HEM1 (PubMed:25957689).
Present with 10900 molecules/cell in log phase SD medium.
Component of the SEA complex composed of at least IML1/SEA1, RTC1/SEA2, MTC5/SEA3, NPR2, NPR3, SEA4, SEC13 and SEH1. Forms a heterodimer with NPR2.
Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis. Mediates inactivation of the TORC1 complex in response to amino acid starvation. Required for meiotic nuclear division.
Phosphorylated by TORC1 in nutrient-replete conditions and during mechanical stress.
Protein kinase that is part of growth control pathway which is at least partially redundant with the cAMP pathway. Regulates both BCY1 phosphorylation and MPK1 activity (PubMed:20702584). Regulates ribosome biogenesis, translation initiation, and entry into stationary phase in a TORC1-dependent manner (PubMed:17560372).
Sensitive to high hydrostatic pressure (mechanical stress); simultaneous disruption of RRD1 exacerbates the effect.
Present with 3990 molecules/cell in log phase SD medium.
May be involved in splicing since overexpression antagonizes the suppression of splicing defects by SPP382 mutants.
Present with 1440 molecules/cell in log phase SD medium.
Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently per subunit.
By L-lactate. Induced during respiratory adaptation.
Catalyzes the oxidation of (S)-lactate (L-lactate) to pyruvate with subsequent transfer of electrons to cytochrome c (PubMed:11914072). Is involved in the utilization of (S)-lactate as a sole source of carbon for growth (PubMed:3004948). Can also use ferricyanide as an electron acceptor in vitro (PubMed:4593578, PubMed:3004948).
Consists of two discrete domains, an N-terminal cytochrome b domain from residues 81 to 179 and a C-terminal flavin-binding domain from residues 180 to 566. In addition there is an extended C-terminal tail (PubMed:2329585, PubMed:11914072). The cytochrome b domain is required for efficient cytochrome c reduction (PubMed:11914072).
In the C-terminal section; belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.
In the N-terminal section; belongs to the cytochrome b5 family.
Inactivation of this gene leads to a deficiency in L-lactate dehydrogenase activity and consequently to the inability to use L-lactate as a sole source of carbon.
Present with 12388 molecules/cell in log phase SD medium.
The N-terminal domain mediates interaction with FAB1 and VAC7 while the C-terminal domain mediates interaction with FIG4.
The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Regulates the synthesis of PtdIns(3,5)P2 by positive activation of FAB1 and by controlling FIG4 localization. Required for FIG4-mediated turnover of PtdIns(3,5)P2 after hyperosmotic shock. Essential for the control of trafficking of some proteins to the vacuole lumen via the multivesicular body (MVB), and for maintenance of vacuole size and acidity.
Present with 184 molecules/cell in log phase SD medium.
Involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. Required to localize MPC54 to all four spindle pole bodies, and localize DON1 and SPO14 to four prospore membranes.
Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. Transcription elongation is promoted by the repression of transcription initiation from cryptic sites. Also acts in establishing transcription initiation complexes and promotes SPT15/TBP-binding to a TATA box. Together with replication factor-A protein (RPA), FACT may play a role in nucleosome deposition during DNA replication.
Forms a stable heterodimer with SPT16. The SPT16-POB3 dimer weakly associates with multiple molecules of NHP6 (NHP6A or NHP6B) to form the FACT (yFACT or SNP) complex. The FACT complex interacts with the CK2 (casein kinase II) complex subunits CKA1, CKA2, CKB1 and CKB2 and the components of the transcription machinery CHD1, CTR9, PAF1 and CDC73. The FACT complex interacts with the PAF1 complex. SPT16 interacts with SAS3 and POL1. Interacts directly with RFA1.
In contrast to the orthologous protein in animals and plants, this protein does not contain a HMG box DNA-binding domain. This function may instead be provided by the HMG box of the associated NHP6A/NHP6B proteins in the FACT complex of yeast.
Present with 22400 molecules/cell in log phase SD medium.
Belongs to the cytidine and deoxycytidylate deaminase family. ADAT2 subfamily.
Deaminates adenosine-34 to inosine in many tRNAs.
Interacts with SKP1. Component of the probable SCF(HRT3) complex containing CDC53, SKP1, RBX1 and HRT3.
CTDK-I consists of three subunits, CTK1, CTK2 and CTK3 (also called alpha, beta and gamma). Interacts directly with the CTK2 and CTK3 subunits, this interaction is required for kinase activity. Interacts with RNA polymerase I. Interacts with SNF1, but only at low glucose concentrations. Interacts with translating ribosomes.
Catalytic subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. CTDK-I phosphorylates 'Ser-5' if the CTD substrate is not phosphorylated at 'Ser-5', but will phosphorylate 'Ser-2' of a CTD substrate if 'Ser-5' is already phosphorylated. CTDK-I is also more reactive toward substrates that are prephosphorylated at 'Ser-2' or 'Ser-5' compared with an unphosphorylated CTD substrate, therefore efficiently creating doubly phosphorylated CTD repeats. Involved in RNA polymerase II transcriptional elongation, and through PTI1, pre-mRNA 3'-end processing. Participates in both positive and negative regulation of CTD phosphorylation. Required for DNA damage induced transcription, including the expression of the RNR genes, and reprogramming of gene expression upon amino acid starvation. Required for SET2 mediated H3K36 methylation. Also regulates H3K4 methylation. Controls the maintenance of suppressive chromatin in the coding regions of genes by both promoting H3K36 methylation, which leads to histone deacetylation, and catalyzing phosphorylation of the CTD required to localize H3K4 chromatin modification specifically to the 5' ends of genes, thereby creating a boundary for H3K4 methylation that prevents a mark associated with transcriptional initiation from spreading into the bodies of genes. Involved in RNA polymerase I transcription. Involved in telomere maintenance. Acts together with SNF1 to induce GSY2 transcription in response to glucose limitation. Involved in the adaptation to alternative carbon sources, including galactose, glycerol and ethanol, but not raffinose. Required for the integrity of the rDNA locus. Functions in translation elongation by enhancing decoding fidelity. Needed for translational accuracy by phosphorylating RPS2.
Null mutants are viable, but grow more slowly than wild-type cells at 30 degrees Celsius. They are cold-sensitive, failing to grow at 12 degrees Celsius. They display flocculent growth in liquid media and they show abnormal cell morphologies, for example, a significant fraction of the cells are greatly enlarged. Deletion mutant has increased phosphorylation of 'Ser-5' of the CTD repeat during logarithmic growth. Deletion eliminates transient increase in CTD 'Ser-2' phosphorylation observed during diauxic shift. Deletion mutant is synthetically lethal when combined with deletion of DST1 or ELP genes. Deletion mutants are modestly sensitive to the uracil analog 6-azauracil (6AU), which inhibits elongation by depleting nucleotide pools. Deletion mutant is sensitive to the DNA synthesis inhibitor hydroxyurea (HU) and UV irradiation. 'Ser-2' phosphorylation within the CTD repeats is not increased in deletion mutants upon treatment with DNA-damaging agents.
Phosphorylated on Thr-338 by CAK1. Phosphorylation is essential for the elevated CTD Ser-2 phosphorylation and required to activate transcription of stationary-phase genes during the diauxic shift.
Interacts with the guanyl-nucleotide exchange factor SEC2. Interacts with SRO7, YIF1, YIP3, YIP4 and YIP5.
Involved in exocytosis. Maybe by regulating the binding and fusion of secretory vesicles with the cell surface. The GTP-bound form of SEC4 may interact with an effector, thereby stimulating its activity and leading to exocytotic fusion. SEC4 may be an upstream activator of the 19.5S SEC8/SEC15 particle. SEC4 probably interacts directly with SEC8; it could serve as the attachment site for the SEC8/SEC15 particle.
Serine hydrolase involved in the detoxification of formaldehyde.
Activity increases just before cells entry in the stationary phase.
Allosteric activation by glucose-6-phosphate, and phosphorylation by a cAMP-dependent kinase.
Belongs to the glycosyltransferase 3 family.
Synthesized in response to growth limitation.
Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. Is believed to regulate the synthesis of glycogen.
Catalyzes the rate-limiting reaction in the mitochondrial fatty acid synthesis (FAS) type II pathway. Responsible for the production of the mitochondrial malonyl-CoA, used for the biosynthesis of the cofactor lipoic acid. This protein carries three functions: biotin carboxyl carrier protein, biotin carboxylase, and carboxyltransferase.
The reading frame from which this protein is translated has no Met initiation codon near to the 5'-end. However, it is not a pseudogene. It has been shown (PubMed:14761959) that at least 72 residues upstream of the first in-frame start codon (Met-151) are required for function and proper subcellular location. May be translated by means of alternative initiation codon usage, programmed translational frame shifting, or mRNA editing.
Involved in cell morphogenesis. Binds to F-actin and stabilizes the actin filaments.
The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity.
Component of the heterotrimeric Sec61 complex, which is composed of SEC61, SBH1 and SSS1. Presumably three to four Sec61 heterotrimers assemble into an oligomeric ring with a central aqueous pore. In cotranslational ER import, the pore diameter varies from 9-15 A in a ribosome-free resting state to 40-60 A in a functional state when associated with the ribosome. The Sec61 complex is part of a channel-forming translocon complex whose composition seem to change dependent upon different functional states. During post-translational ER import the Sec61 complex associates with the Sec62/63 complex to form the Sec complex. SEC61 interacts with STT3, OST1, OST2, OST4, SWP1 and WBP1 components of the OT complex.
Part of the Sec61 complex, which is the major component of a channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). The functional states of the translocon complex include co- and post-translational ER import, cotranslational membrane protein integration and retrograde transport of misfolded proteins out of the ER. In the cotranslational pathway, ribosomes synthesizing presecretory proteins are targeted to the translocon by the cytosolic signal recognition particle (SRP) and its ER-localized receptor. The association of the Sec61 complex with the ribosome is mediated by the 28S rRNA of the large ribosomal subunit. SRP-independent post-translational translocation requires the association of additional factors, such as the Sec62/63 complex and KAR2. In an initial step, the signal sequence seems to bind simultaneously to SEC61 and SEC62. A cycle of assembly and disassembly of Sec62/63 complex from SEC61 may govern the activity of the translocon. SEC61 mediates the association with the ribosome.
Present with 24800 molecules/cell in log phase SD medium.
Belongs to the peptidase S8 family. Furin subfamily.
Processing of precursors of alpha-factors and killer toxin.
By maltose and maltotriose (PubMed:10618490, PubMed:12210897, PubMed:8594329). Repressed by glucose (PubMed:10618490, PubMed:12210897, PubMed:8594329).
High-affinity uptake of alpha-glucosides such as maltose, turanose, isomaltose, alpha-methylglucoside, maltotriose, palatinose, trehalose, melezitose and glucose. Acts with the concomitant transport of protons into the cell (symport system).
Belongs to the 5'-3' exonuclease family. XRN2/RAT1 subfamily.
Inhibited by nucleoside 3', 5'-bisphosphates.
Possesses 5'->3' exoribonuclease activity. Required for the processing of nuclear mRNA, rRNA and small nucleolar RNA (snoRNA) precursors. May promote termination of transcription by RNA polymerase II via the recruitment of 3'-end processing factors to the poly(A) site and by the degradation of nascent RNA downstream of the poly(A) site.
Component of the SRB8-11 complex which consists of SRB8, SSN2/SRB9, SSN3/SRB10 and SSN8/SRB11. The SRB8-11 complex associates with the Mediator complex. The SSN3/SRB10 and SSN8/SRB11 kinase-cyclin pair also associate with the RNA polymerase II holoenzyme. Interacts with TUP1.
Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The SRB8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II RPB1 at serines 2 and 5. The SSN3/SRB10 and SSN8/SRB11 kinase-cyclin pair may also positively and negatively regulate numerous transcriptional activators in response to changes in nutritional and physiological conditions. Phosphorylates GCN4, promoting its ubiquitin-mediated degradation, and MSN2, promoting its nuclear exclusion. Phosphorylates STE12, thereby promoting its degradation and inhibition of filamentous growth. Phosphorylates GAL4, and this phosphorylation is required for efficient galactose-inducible transcription. Also phosphorylates BDF1 and the TAF2 subunit of the TFIID complex.
Protein level and kinase activity are reduced during nitrogen starvation.
Belongs to the protease inhibitor I9 family.
Present with 5300 molecules/cell in log phase SD medium.
Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of at least PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. Interacts with FIP1, PFS2, RNA14 and YTH1.
Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Has endonuclease activity.
Present with 17400 molecules/cell in log phase SD medium.
Interacts with RNA polymerase II subunits RPB2 and RPB3. Interacts with the R2TP complex. Interacts with the nuclear pore complex subunits NUP100 and NUP116.
Required for the cytoplasmic assembly and the nuclear import of RNA polymerase II. May facilitate the starting interaction between RNA polymerase II subunits RPB2 and RPB3 and the subsequent interaction of the resulting complex with subunit RPB1. May also participate in the transport of RNA polymerase II through the nuclear pore complex.
Interacts with YAP1. Forms a peroxide stress induced complex with YAP1 in the cytoplasm. Systematic proteome-wide 2-hybrid interaction studies suggest that YAP1, HYR1/GPX3, and YBP1 all interact with the nuclear pore complex subunit NUP116, which is involved in nucleocytoplasmic transport.
Involved in oxidative stress response and redox homeostasis. Required for hydrogen peroxide-induced oxidation and nuclear localization (activation) of YAP1. Functions probably in concert with HYP1/GPX3, the actual YAP1 modifying enzyme. YBP1 is not required for HYP1/GPX3-independent, diamide-induced oxidation of YAP1.
YBP1 encoded by the widely used laboratory strain W303-1a is only partially functional, probably due to four amino acid substitutions.
Guanine-nucleotide exchange factor for ARF3 required for localization of ARF3 to the bud neck and tip and involved in actin patch polarization.
Component of the YIP1-YIF1 complex, composed of at least YIF1, YIP1 and YOS1. The complex interacts with the ER to Golgi SNAREs BOS1 and SEC22. Interacts with the prenylated form of the Rab GTPases YPT1 and YPT31. Interacts with the YIP1 family members YIP4 and YIP5. Interacts with SNX3, YIP3 and YOP1.
Required for fusion of ER-derived vesicles with the Golgi during ER-to-Golgi protein transport, probably by mediating correct membrane localization of YPT1.
Acyltransferase required to remodel newly synthesized phospholipid cardiolipin (1',3'-bis-[1,2-diacyl-sn-glycero-3-phospho]-glycerol or CL), a key component of the mitochondrial inner membrane, with tissue specific acyl chains necessary for adequate mitochondrial function (PubMed:14651618, PubMed:28202545, PubMed:29091407). Its role in cellular physiology is to improve mitochondrial performance (By similarity). CL is critical for the coassembly of lipids and proteins in mitochondrial membranes, for instance, remodeling of the acyl groups of CL in the mitochondrial inner membrane affects the assembly and stability of respiratory chain complex IV and its supercomplex forms (PubMed:16135531). Catalyzes the transacylacion between phospholipids and lysophospholipids, with the highest rate being between phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) and CL. Catalyzes both 1-acyl-sn-glycero-3-phosphocholine (lysophosphatidylcholine or LPC) reacylation and PC-CL transacylation, that means, it exchanges acyl groups between CL and PC by a combination of forward and reverse transacylations. Also catalyzes transacylations between other phospholipids such as phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) and CL, between PC and PE, and between PC and phosphatidate (1,2-diacyl-sn-glycero-3-phosphate or PA), although at lower rate. Not regiospecific, it transfers acyl groups into any of the sn-1 and sn-2 positions of the monolysocardiolipin (MLCL), which is an important prerequisite for uniformity and symmetry in CL acyl distribution. Cannot transacylate dilysocardiolipin (DLCL), thus, the role of MLCL is limited to that of an acyl acceptor (By similarity). CoA-independent, it can reshuffle molecular species within a single phospholipid class (PubMed:15588229). Redistributes fatty acids between MLCL, CL, and other lipids, which prolongs the half-life of CL. Its action is completely reversible, which allows for cyclic changes, such as fission and fusion or bending and flattening of the membrane. Hence, by contributing to the flexibility of the lipid composition, it plays an important role in the dynamics of mitochondria membranes. Essential for the final stage of spermatogenesis, spermatid individualization (By similarity). Required for the initiation of mitophagy (By similarity).
Present with 1340 molecules/cell in log phase SD medium (PubMed:14562106). The enzyme was named after a masochistic character Tafazzi, once popular on Italian television, apparently due to the difficulty encountered for its identification and characterization (By similarity).
High-affinity S-methylmethionine (SMM) permease, required for utilization of S-methylmethionine as a sulfur source.
By treatment with 8-methoxypsoralen and UVA irradiation.
Component of the mitotic checkpoint complex (MCC) which consists of MAD2, MAD3, BUB3 and CDC20. Part of complex consisting of MAD1, BUB1 and BUB3 after activation of spindle checkpoint. Interacts with MAD1, MAD2 and CDC20.
Required for cell cycle arrest in response to loss of microtubule function. Component of the spindle assembly checkpoint which is a feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. Component of the mitotic checkpoint complex (MCC) which inhibits the ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) by preventing its activation by CDC20. The formation of a MAD1-BUB1-BUB3 complex seems to be required for the spindle checkpoint mechanism.
Present with 5700 molecules/cell in log phase SD medium.
Component of the GPI transamidase complex. Required for a terminal step of GPI anchor attachment onto proteins. Affects endocytosis.
Forms a complex with CDC91, GPI17, GPI16 and GPI8.
Component of the RAVE complex composed of RAV1, RAV2 and CBF3D/SKP1. Within the complex, it interacts directly with RAV1 and CBF3D. Interacts with the V-ATPase V1 subunits VMA1, VMA2 and VMA8.
Component of the RAVE complex, which is required for stable assembly of the vacuolar ATPase complex V-ATPase under many conditions. May be required for transport between the early endosome and the late endosome/prevacuolar compartment (PVC).
Present with 13200 molecules/cell in log phase SD medium.
Belongs to the eukaryotic RPC4/POLR3D RNA polymerase subunit family.
Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. Interacts with RPC37/RPC5. RPC53/RPC4, RPC37/RPC5 and RPC11/RPC10 probably form a Pol III subcomplex.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Essential for tRNA synthesis. The RPC53/RPC4-RPC37/RPC5 subcomplex is required for terminator recognition and reinitiation.
Present with 998 molecules/cell in log phase SD medium.
Eukaryotic pyruvate dehydrogenase (PDH) complexes are organized as a core consisting of the oligomeric dihydrolipoamide acetyl-transferase (E2), around which are arranged multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and protein X (E3BP) bound by non-covalent bonds.
The E2 component contains covalently-bound lipoyl cofactors and it participates in the generation of acetyl groups from hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to coenzyme A.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
Catalytic component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is the essential ATPase of the complex. It is a DNA translocase capable of nucleosome remodeling. Required for full expression of early meiotic genes. Essential for mitotic growth and repression of CHA1 expression. Also involved in G2 phase control.
Interacts directly with SFH1, CSE4, histones H3, H4 and H2B, and via its N-terminus, with RSC8. Interacts with LDB7, NPL6 and RTT102. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin.
Interacts with EMP47 in the endoplasmic reticulum membrane in order to be transported to the Golgi apparatus. Interacts with the coatomer proteins COP1, SEC21 and SEC23.
Involved in the secretion of glycoproteins and in nucleus architecture and gene silencing.
Present with 2550 molecules/cell in log phase SD medium.
High-affinity transporter for external inorganic phosphate. Is not an essential protein, since a constitutive, low affinity pI transporter exists in yeast.
Present with 335000 molecules/cell in log phase SD medium.
Under the control of phosphate. It is derepressed by phosphate starvation.
Belongs to the CWC complex (or CEF1-associated complex), a spliceosome subcomplex composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with ISY1. Interacts with PRP19.
Involved in the first step of pre-mRNA splicing. Required for cell growth and cell cycle control. Plays a role in the levels of the U1, U4, U5 and U6 snRNAs and the maintenance of the U4/U6 snRNA complex. May provide the link between the 'nineteen complex' NTC spliceosome protein complex and the spliceosome through the U6 snRNA. Associates predominantly with U6 snRNAs in assembled active spliceosomes. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycle. Binds also to U1, U4, U5 and U6 snRNAs and to pre-mRNAs, in vitro. Is not required for the Prp2-mediated remodeling of the activated spliceosome.
The C-terminal RRM domain and the zinc finger motif are necessary for RNA-binding.
Phosphorylated by PKH1 and PKH2. Phosphorylation is stimulated by sphingolipid long chain bases (LCBs).
Present with 104485 molecules/cell in log phase SD medium.
Together with PIL1, main component of eisosomes, structures at the cell periphery underneath the plasma membrane that mark the site of endocytosis. Negative regulator of cell wall integrity (CWI) in unstressed cells, probably by inhibiting protein kinase PKH1/PHK2 activity and regulating their downstream CWI pathways PKC1-MAP kinase pathway and protein kinase YPK1 pathway. Activity may be regulated by the transient increase of sphingolipid long chain bases (LCBs) during heat stress.
Belongs to the glycosyl hydrolase 15 family.
In the 2nd section; belongs to the EPSP synthase family.
In the 3rd section; belongs to the shikimate kinase family.
In the 4th section; belongs to the type-I 3-dehydroquinase family.
In the C-terminal section; belongs to the shikimate dehydrogenase family.
In the N-terminal section; belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.
Involved in the regulation of the iron regulon in response to decreased mitochondrial iron-sulfur cluster synthesis. May be involved in mitochondrial organization and biogenesis.
Catalyzes the ATP-dependent translocation of sphingoid long-chain bases (LCBs) from the cytoplasmic site toward the extracytoplasmic side of the membrane (flip-flop). Involved in the establishment of the functional lipid asymmetry of the plasma membrane. Regulates intracellular levels of LCBs, sphingolipid precursors that are growth inhibitory at increased levels.
In response to loss of mitochondrial DNA in a transcription factor PDR3-dependent manner. Induced in response to altered glycerophospholipid asymmetry of the plasma membrane in a transcription factor PDR1-dependent manner.
Belongs to the OMP decarboxylase family.
Belongs to the fatty acid desaturase type 1 family.
Expected to bind 2 Fe(2+) ions per subunit.
Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed:1978720, PubMed:7947684). Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:1978720, PubMed:2674136). Required for the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (PubMed:1978720, PubMed:7947684, PubMed:16443825). Regulates fatty acid desaturation, that is, the ratio of unsaturated versus saturated fatty acyl chains, by competing with the acyltransferase STC1 for the common substrate C16:0-CoA. SCT1 sequesters C16:0-CoA into lipids, thereby shielding it from desaturation by OLE1 (PubMed:22323296).
The histidine box domains are involved in binding the catalytic metal ions.
Supplies CDP-diacylglycerol, which may play an important role as both a precursor to phosphoinositide biosynthesis in the plasma membrane and as a negative effector of phosphatidylinositol 4-kinase activity, thereby exerting an effect on cell proliferation via a lipid-dependent signal transduction cascade.
Belongs to the cytochrome c oxidase subunit 5A family.
Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of 12 subunits. The complex is composed of a catalytic core of 3 subunits COX1, COX2 and COX3, encoded in the mitochondrial DNA, and 9 supernumerary subunits COX4, COX5A (or COX5B), COX6, COX7, COX8, COX9, COX12, COX13 and COX26, which are encoded in the nuclear genome (PubMed:7851399, PubMed:30598556, PubMed:30598554). The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a dimer of ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), resulting in 2 different assemblies (supercomplexes III(2)IV and III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556, PubMed:30598554). COX26 interacts with COX1, COX2, COX6 and COX9 (PubMed:30598554).
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix (Probable). COX6 may stabilize the region of CIV at the interface with CIII, supporting a role in formation or stability of the CIII(2)IV(2) SC (PubMed:30598554).
By heat stress. Expressed at a higher level in respiring cells than in fermenting cells (at protein level).
Has 2 AAA ATPase type nucleotide-binding domains (NBDs) per monomer. NBD1 is primarily responsible for ATP hydrolysis. NBD2 is crucial for oligomerization.
Homohexamer, forming a ring with a central pore. The hexamer is stabilized by high protein concentrations and by ADP or ATP. Oligomerization influences ATP hydrolysis activity.
Required, in concert with mitochondrial Hsp70 (SSC1), for the dissociation, resolubilization and refolding of aggregates of damaged proteins in the mitochondrial matrix after heat stress. May extract proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by the Hsp70 chaperone system. Required for resumption of mitochondrial respiratory function, DNA synthesis and morphology after heat stress. Its main role may be maintaining the molecular chaperone SSC1 in a soluble and functional state. Also required for the efficient degradation of proteins by matrix protease PIM1, independent on its protein remodeling activity.
Probable transcriptional activator involved in uracil catabolism.
Loss of QRI7 leads to the formation of mitochondria with abnormal morphology and no DNA.
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance.
Involved in G1/S and or S phase progression. Interacts with CDC28.
Maximally expressed just before cell cycle start.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NUP53 interacts with MAD1-MAD2. During mitosis NUP53 changes its binding partner within the NPC from NUP170 to NIC96, exposing a high affinity binding site for the karyopherin PSE1, and retaining it in the NPC, while MAD2 is released. It forms a subcomplex with ASM4 and NDC1.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP53 may play an important role in cell cycle regulation by inhibiting PSE1 transport functions during mitosis and sequestration of MAD1-MAD2 in a cell cycle-dependent manner. It also seems to play an important role in de novo NPC assembly by associating with nuclear membranes and driving their proliferation.
There are 3 tandem-duplicated genes coding for this protein in S.cerevisiae (YLR156W, YLR159W and YLR161W). Additionally, a fourth copy has been disrupted by a Ty1 retrotransposon, which led to the prediction of the 2 dubious ORFs YLR157W-D and YLR157W-E.
Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Substrate specificity requires an N-terminal glycine in the nascent polypeptide substrates. Uncharged amino acids are preferred at position 2 while neutral residues are favored at positions 3 and 4. Ser is present at position 5 in almost all known N-myristoyl proteins and Lys is commonly encountered at postion 6.
Has an ordered Bi-Bi kinetic mechanism, with myristoyl-CoA binding taking place prior to peptide binding and CoA release occurring before acylated peptide release. Cooperative interactions between the acyl-CoA and peptide binding sites of NMT contribute to its extraordinary chain-length specificity.
Inhibited by diethylpyrocarbonate. Competitively inhibited by S-(2-oxo)pentadecyl-CoA, a non hydrolysable myristoyl-CoA analog, and by SC-58272, a peptidomimetic derived from the N-terminal sequence of a natural substrate.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. Interacts through its FG repeats with nuclear transport receptors. Binds to the nuclear basket of the NPC through NUP60. Interacts with KAP122.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). As one of the FG repeat nucleoporins NUP1 is involved in interactions with and guidance of nuclear transport receptors such as SRP1-KAP95 (importin alpha and beta) through the NPC. Like the closely related NUP2 it also plays an important role in disassembling and recycling SRP1-KAP95 to the cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1-KAP95-cargo complex in the nucleus, NUP1 binds through its C-terminus to KAP95, thus accelerating the release of KAP95 and, indirectly, of the nuclear localization signal (NLS)-containing cargo from the SRP1-KAP95-cargo complex.
Regulatory subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-glucose in a two step process. May stabilize the trehalose synthase complex.
The trehalose synthase complex is composed of the two catalytic subunits TPS1 and TPS2 and at least one of the two regulatory subunits TPS3 or TSL1.
Repressed by glucose but is activated in the presence of non-fermentable carbon sources or salt stress. The latter transcriptional activation of NSF1 is partially dependent on the SNF1 signaling pathway.
Transcription factor that participates in the transcriptional activation of glucose-repressed genes during exponential growth in non-fermentable carbon conditions. Also involved in salt-stress response.
Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization. Required for the bipolar budding of diploid cells and the correct distribution of chitin at the cell surface.
Forms homooligomers. Component of the PAN1 actin cytoskeleton-regulatory complex composed of at least END3, PAN1, and SLA1. Interacts directly with END3, and with ENT1, SCD5, SLA2, YAP1801 and YAP1802.
Phosphorylated by PRK1 on threonine residues in the L-x-x-Q-x-T-G motif of repeats 1-6 to 1-15 (PubMed:9885245, PubMed:11739778, PubMed:17978096). Phosphorylated by ARK1 (PubMed:17978096).
Was originally thought to be a subunit of PAB-dependent poly(A)-specific ribonuclease.
Present with 7720 molecules/cell in log phase SD medium.
tRNA (uracil-O(2)-)-methyltransferase, which catalyzes the formation of O(2)-methyluracil at position 44 (Um44) in tRNA(Ser).
Belongs to the alpha-ketoglutarate dehydrogenase family.
Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA.
Interacts with snoRNA U3. Interacts with MPP10, UTP21 and UTP25. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.
Present with 9570 molecules/cell in log phase SD medium.
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
During the reaction, ATP is used to activate the C2 atom of U34 by adenylation. After this, the persulfide sulfur on the catalytic cysteine is transferred to the C2 atom of the wobble base (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards the activated C2 atom on U34. Subsequently, a transient disulfide bond is formed between the two active site cysteine residues (By similarity).
Was originally thought to be a 5-methylaminomethyl-2-methyltransferase involved in tRNA modification.
Belongs to the cytochrome c oxidase subunit 3 family.
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix (Probable). COX3 is a catalytic core subunit (PubMed:30598554).
In contrast to the other two peroxiredoxins, HYR1/GPX3 expression is constitutive, not stress-induced.
Involved in oxidative stress response and redox homeostasis. Functions as a sensor and transducer of hydroperoxide stress. In response to hydroperoxide stress it oxidizes (activates) the transcription activator YAP1, which is involved in transcription activation of genes of the oxidative stress response pathway. May also play a direct role in hydroperoxide scavenging, being the most active of three closely related S.cerevisiae peroxiredoxins (GPX1, GPX2, and HYR1/GPX3) with respect to peroxide and lipid hydroperoxide reduction. The three enzymes are not required for the glutaredoxin-mediated antioxidant function. In the presence of peroxides, HYR1/GPX3 is directly oxidized at Cys-36 to form a cysteine sulfenic acid (-SOH). Cys-36-SOH then forms either an intramolecular disulfide bond (Cys-36 with Cys-82) or a transient, intermolecular disulfide bond with 'Cys-598' of YAP1, which is further resolved into a YAP1 intramolecular disulfide bond ('Cys-303' with 'Cys-598'), which causes its nuclear accumulation and activation, and a reduced Cys-36 in HYR1/GPX3.
Present with 8000 molecules/cell in log phase SD medium.
Sensitive to hydrogen peroxide and tert-butyl hydroperoxide (t-BHP).
Was originally thought to be a glutathione peroxidase (PubMed:10480913) or a phospholipid hydroperoxide glutathione peroxidase (PubMed:11445588), but functions as an atypical 2-Cys peroxiredoxin using thioredoxin as reducing power instead (PubMed:12437921).
Associates with TFIID-IIA (DA complex) to form TFIID-IIA-IIB (DAB-complex) which is then recognized by polymerase II.
General factor that plays a major role in the activation of eukaryotic genes transcribed by RNA polymerase II.
Acts as a catalytic component of the translation initiation factor 2B (eIF2-B or GCD complex), which catalyzes the exchange of eukaryotic initiation factor 2 (eIF-2)-bound GDP for GTP and is regulated by phosphorylated eIF-2. It activates the synthesis of GCN4 in yeast under amino acid starvation conditions by suppressing the inhibitory effects of multiple AUG codons present in the leader of GCN4 mRNA. It may promote either repression or activation of GCN4 expression depending on amino acid availability. GCD6 and GCD7 repress GCN4 expression at the translational level by ensuring that ribosomes which have translated UORF1 will reinitiate at UORF2, -3, or -4 and thus fail to reach the GCN4 start site.
Translation initiation factor 2B (eIF2-B) is composed of five different subunits; alpha (GCN3), beta (GCD7), gamma (GCD1), delta (GCD2) and epsilon (GCD6). A catalytic subcomplex comprising GCD1 and GCD6 interacts with both, phosphorylated and non-phosphorylated eIF-2 and has exchange activity in vitro. GCD6 interacts with SUI3.
CLN1 and CLN2 mRNAs fluctuate periodically in the cell cycle, peaking in G1 phase.
Essential for the control of the cell cycle at the G1/S (start) transition. Interacts with the CDC28 protein kinase to form MPF.
Expression is GCR1-dependent. Promoter is also bound by the RAP1 transcription factor.
May be involved in ribosome biogenesis. Has also been proposed to play a role in calcium homeostasis (PubMed:23569283).
Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM5 family.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that trimethylates elongation factor 1-alpha (TEF1 and TEF2) at 'Lys-79' (PubMed:25446118). Required for replication of Brome mosaic virus (BMV) (PubMed:14671320).
Was originally thought to be an N(6)-adenine-specific DNA methyltransferase based on primary sequence and predicted secondary structure.
Possible glycosyltransferase involved in N-linked glycosylation. Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage.
Present with 23000 molecules/cell in log phase SD medium.
Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced stress responses (PubMed:32780017).
Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes formed of CUL1, SKP1/HRT1, RBX1 and a variable F-box domain-containing protein as substrate-specific adapter. Component of the SCF(CDC4) complex containing CDC4. Component of the SCF(MET30) complex containing MET30. Component of the SCF(GRR1) complex containig GRR1. Component of the probable SCF(DIA2) complex containing DIA2. Component of the probable SCF(YDR131C) complex containing YDR131C. Component of the probable SCF(YDR306C) complex containing YDR306C. Component of the probable SCF(YLR224W) complex containing YLR224W. Component of the probable SCF(YJL149W) complex containing YJL149W. Component of the probable SCF(YNL311C) complex containing YNL311C. Component of the probable SCF(MDM30) complex containing MDM30. Component of the probable SCF(UFO1) complex containing UFO1. Component of the probable SCF(HRT3) complex containing HRT3. Component of the probable SCF(YBR280C) complex containing YBR280C. Component of the probable SCF(YBR352W) complex containing YBR352W. Interacts with DCN1, YBR280C, YLR224W and YLR352W. The unneddylated form interacts with LAG2/CAND1 and the interaction mediates the exchange of the F-box substrate-specific subunit.
Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The SCF complex associates with CDC34 as the E2 ubiquitin-conjugating enzyme. The functional specificity of the SCF complex depends on the type of F-box protein. SCF(CDC4) controls the G1-to-S phase transition; it directs ubiquitination of the phosphorylated CDK inhibitor SIC1 and of CDC6. SCF(CDC4) directs ubiquitination of GCN4. SCF(GRR1) directs ubiquitination of phosphorylated CLN1, CLN2 and GIC2. SCF(MET30) directs ubiquitination of MET4. SCF(DIA2) is specifically involved in the pheromone induced degradation of phosphorylated TEC1. SCF(MDM30) seems to direct ubiquitination of FZ01. Involved in the regulation of methionine biosynthesis genes.
Neddylated; enhancing the ubiquitin-ligase activity.
Involved in the early step of endocytosis.
Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Probably plays a role in structure.
Belongs to the SMC family. SMC6 subfamily.
Component of the Smc5-Smc6 complex which consists of KRE29, MMS21, NSE1, NSE3, NSE4, NSE5, SMC5 and SMC6.
The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC5, forming a V-shaped heterodimer.
Binds to ribosomes (PubMed:9670014, PubMed:1394434, PubMed:27917864). Binds close to the ribosomal tunnel exit via contacts with both ribosomal proteins RPL35, RPL39 and RPL19, and rRNA (PubMed:27882919). Directly interacts with nascent polypeptides. This interaction is dependent on the ribosome-associated complex (RAC) (PubMed:11929994, PubMed:23332755). Interacts with SSE1 (PubMed:16219770, PubMed:16221677, PubMed:23332755). Interacts with FES1 (PubMed:17132105). Interacts with NAP1 (PubMed:18086883).
Expression decreases after heat shock or during growth to stationary phase (PubMed:6761581, PubMed:2651414). Degraded during heat shock treatment (at protein level) (PubMed:7646503). Up-regulated upon carbon upshift and down-regulated upon amino acid limitation in an HSF1-dependent manner (PubMed:10322015).
Present with 170000 molecules/cell in log phase SD medium.
Belongs to the universal ribosomal protein uL16 family.
Belongs to the indoleamine 2,3-dioxygenase family.
Catalyzes the first step in tryptophan catabolism in order to supply de novo nicotinamide adenine dinucleotide (NAD(+)) via the kynurenine pathway. Plays a role in the cellular response to telomere uncapping.
Expression is mediated by the AFT2, HCM1, and SUM1 transcription factors. Up-regulated in absence of NPT1.
Transporter required for vacuolar uptake of histidine, arginine and lysine and to a lesser extent tyrosine.
Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family.
Belongs to the cyclophilin-type PPIase family.
Inhibited by the immunosuppressant drug cyclosporin A and by SDZ NIM811, a PPIase inhibitor.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. This isozyme is required for growth on lactate at high temperature.
In response to low temperature (By cold-shock).
Involved in pre-rRNA processing (PubMed:1644811). Specifically binds nuclear localization sequences (PubMed:1706724). Candidate for a receptor at the nucleus that may be involved in both RNA and protein transport (Probable). Binds telomeric sequences of the type (TG[1-3])n in vitro (PubMed:7800479).
Methylated by HMT1, forming asymmetric dimethylarginines (DMA) within a domain referred to as an RGG box, made up of repeated Gly-Gly dipeptides interspersed with Arg and aromatic residues.
Present with 77400 molecules/cell in log phase SD medium.
Functions in the late secretory pathway. Required for the generation of secretory vesicles as well as for actin polarization and polarized growth.
Involved in the early part of the secretory pathway.
Component of the UAF (upstream activation factor) complex which consists of UAF30, RRN5, RRN9, RRN10, and histones H3 and H4. Interacts with SPT15 and RRN7.
Secreted protein required for efficient export of lipids such as acetylated sterols. Acts in detoxification of hydrophobic compounds.
The SCP domain is necessary and sufficient for lipid export and sterol-binding.
Adaptor protein complex 3 (AP-3) is a heterotetramer composed of 2 large adaptins (APL5 and APL6), a medium adaptin (APM3) and a small adaptin (APS3).
Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole. Required for the transport via the ALP pathway, which directs the transport of the cargo proteins PHO8 and VAM3 to the vacuole.
Belongs to the PPP phosphatase family. PP-2A subfamily.
Exact function not known, phosphatase 2A performs an essential cellular function.
Inactivated in a complex with phosphatase methylesterase PPE1 (PP2Ai). Interacts with phosphatase 2A activator RRD2, which can reactivate PP2Ai by dissociating the catalytic subunit from the complex. Forms a ternary complex with RRD2-TAP42.
Reversibly methyl esterified on Leu-369 by leucine carboxyl methyltransferase 1 (PPM1) and protein phosphatase methylesterase 1 (PPE1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization.
Belongs to the pterin-4-alpha-carbinolamine dehydratase family.
Overexpression confers resistance to the antimicrobial peptide MiAMP1.
Belongs to the glycosyltransferase 32 family.
Exhibits a reduction in the synthesis of mannosylated sphingolipids.
Involved in the synthesis of mannosyl phosphorylinositol ceramide (PubMed:12954640). Catalyzes the addition of mannosyl to phosphorylinositol ceramide (PubMed:12954640).
Belongs to the ribonucleoside diphosphate reductase small chain family.
Heterotetramer of two large (R1) and two small (R2) subunits. S.cerevisiae has two different R1 subunits (RNR1 and RNR3) and two different R2 subunits (RNR2 and RNR4). The functional form of the small subunits is a RNR2-RNR4 heterodimer, where RNR2 provides the iron-radical center and RNR4 is required for proper folding of RNR2 and assembly with the large subunits. Under normal growth conditions, the active form of the large subunits is a homodimer of the constitutively expressed RNR1. In damaged cells or cells arrested for DNA synthesis, the reductase consists of multiple species because of the association of the small subunits (RNR2-RNR4) with either the RNR1 homodimer or a heterodimer of RNR1 and the damage-inducible RNR3. Interacts with DIF1.
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. RNR2 provides the diiron-tyrosyl radical center.
Interacts with DID2. Interacts with VPS4 (via MIT domain); the interaction prevents VPS4 oligomerization, competes with the binding of VTA1 to VSP4 and diminishes the ATPase activity of VSP4.
Involved in a late step in sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins are targeted into the vacuole after fusion of the endosome with the vacuole. Regulates the recruitment of VPS4 to the ESCRT-III complex, probably in conjunction with DID2, and VPS4 catalyzes the disassembly of the ESCRT-III complex.
Present with 4760 molecules/cell in log phase SD medium.
Required for normal growth rate on galactose and mannose.
Belongs to the eukaryotic RPB4 RNA polymerase subunit family.
Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. RPB4 and RPB7 form a dissociable subcomplex associated with the 10-subunit Pol II core complex. In exponentially proliferating cells, only approximately 20 % of the Pol II complexes contain the RPB4-RPB7 subcomplex. In starving cells, that enter stationary phase, RPB4-RPB7 is associated with Pol II in a stoechiometric manner. The RPB4-RPB7 subcomplex probably associates with TFG1. Interacts with LSM2 and PAT1.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB4 is part of a subcomplex with RPB7 that binds to a pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The RPB4-RPB7 subcomplex binds single-stranded DNA and RNA. The RPB4-RPB7 subcomplex is necessary for promoter-directed transcription initiation but is not required for recruitment of Pol II to active preinitiation complexes and seems to be dispensable for transcription elongation and termination. The RPB4-RPB7 subcomplex recruits FCP1 to Pol II. Involved in DNA repair of damage in the transcribed strand. RPB4 is dispensable under optimal growth conditions, but becomes essential during heat or cold shock and under nutrient depletion. Suppresses the RBP9-mediated transcription-coupled repair (TCR) subpathway of nucleotide excision repair (NER) but facilitates the RAD26-mediated TCR subpathway. Under stress conditions only, involved in mRNA export to the cytoplasm. Involved in mRNA decay. Promotes or enhances the deadenylation process of specific mRNAs and may recruit PAT1 and the LSM1-7 complex to these mRNAs, thus stimulating their decapping and further decay.
Component of the transcription/export (TREX) complex, which is at least is formed of SUB2, TEX1 and YRA1 and the THO complex composed of HPR1, MFT1, THO2 and THP1. Interacts with RDS3 and YRA2.
RNA-binding RNA annealing protein. May have a role in pre-mRNA metabolism. Component the TREX complex, which operates in coupling transcription elongation to mRNA export.
GTPase-activating protein (GAP) for CDC42 and/or RHO1. Negative regulator of the pheromone-response pathway through the STE20 protein kinase; acts at a step between the G-protein and the MAP kinase module. Dominant suppressor of bud emergence defect caused by deletion of IPL2/BEM2. Involved in the control of polarized cell growth and proper bud site selection.
Component of the proteasome. ECM29 binds to both proteasome 19S and 20S particles.
Stabilizes the proteasome holoenzyme, probably by tethering the 20S proteolytic core particle and the 19S regulatory particle. The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Belongs to the thymidylate kinase family.
Catalyzes the conversion of dTMP to dTDP.
This protein is coded in group-II intron 2 of OXI3 (COX1).
Acts in conjunction with the alpha-factor receptor to promote morphogenesis and adaptation.
Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SMT3 to its mature form and deconjugation of SMT3 from targeted proteins. Has an essential role in the G2/M phase of the cell cycle.
Transcription activator required for the expression of genes involved in the catabolism of aromatic amino acids such as the aromatic aminotransferase II ARO9 and the phenylpyruvate decarboxylase ARO10.
Belongs to the NTC complex (or PRP19-associated complex), composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2, and PRP19. The NTC complex associates with the spliceosome after the release of the U1 and U4 snRNAs and forms the CWC spliceosome subcomplex (or CEF1-associated complex) reminiscent of a late-stage spliceosome composed also of the U2, U5 and U6 snRNAs and at least BUD13, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8, PRP9, PRP11, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNU114, SPP2, RSE1 and YJU2. Interacts with CEF1, CLF1, ISY1, PRP46, and SYF1.
Involved in pre-mRNA splicing. As a component of the NTC complex, associates to the spliceosome to mediate conformational rearrangement or to stabilize the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation.
Belongs to the uroporphyrinogen-III synthase family.
Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the fourth step in the heme biosynthetic pathway.
Was originally thought to be involved in mitochondrial import.
Interacts with the AAA ATPase VPS4; regulates OSH6 membrane association. VPS4 is required for membrane dissociation of OSH6.
Lipid transport protein (LTP) involved in non-vesicular transfer of lipids between membranes. Functions in phosphoinositide-coupled directional transport of various lipids by carrying the lipid molecule in a hydrophobic pocket and transferring it between membranes through the cytosol. Involved in maintenance of intracellular sterol distribution and homeostasis (PubMed:15173322, PubMed:16156791, PubMed:23934110, PubMed:26206936). Catalyzes the lipid countertransport between the endoplasmic reticulum (ER) and the plasma membrane (PM). Specifically exchanges phosphatidylserine (PS) with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the PM in exchange for PI4P, which is delivered to the ER-localized PI4P phosphatase SAC1 for degradation. Thus, by maintaining a PI4P gradient at the ER/PM interface, SAC1 drives PS transport (PubMed:23934110, PubMed:26206936). Binds phosphatidylserine and PI4P in a mutually exclusive manner (PubMed:26206936). Also binds phosphatidic acid (PA) (PubMed:16156791).
Belongs to the dihydroxyacetone kinase (DAK) family.
Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde.
Forms a complex with the cullin-RING ligase (CRL) RTT101(MMS1-MMS22). Interacts with MMS22 and RTT101. Interacts with histone H2A; requires H2A to be phosphorylated (gamma-H2A). Interacts with RAD55.
Required for resumption of chromosome replication after DNA damage, specifically in S phase. Is recruited to chromatin in the presence of RTT109 and RTT101 in response to stalled replication forks and acts as a scaffold during DNA repair.
May function in the second step of pre-mRNA splicing. Regulatory protein involved in replication and mitotic spindle formation and/or maintenance. Required for initiation and completion of S-phase and for initiation and completion of DNA replication. Might be required for the maintenance of microtubules. Essential only at elevated temperatures.
Belongs to the RecA family. DMC1 subfamily.
Double stacked ring-shaped homooctamer (By similarity). Forms a ternary complex with MEI5 and SAE3. Interacts with RDH54.
Expressed 2.5 hours after induction of meiosis.
Required for meiotic recombination, synaptonemal complex formation and cell cycle progression. Recruited to meiosis recombination hotspots by MEI5 and SAE3.
Accumulates DPCs and exhibits gross chromosomal rearrangements.
Belongs to the peptidase M3 family. WSS1-like metalloprotease (WLM) subfamily.
Binds to DNA. Interacts with CDC48 and SMT3. Interacts with PSY2 and TOF1.
Metalloendopeptidase that acts selectively on DNA-binding proteins. DNA is needed to bring the protease and substrates together to enable proteolysis. Involved in the repair of toxic DNA-protein cross-links (DPCs) such as covalently trapped topoisomerase 1 (TOP1) adducts on DNA lesions or DPCs induced by reactive compounds such as formaldehyde. Involved in DNA damage response and processing of stalled or collapsed replication forks by removing the covalently trapped TOP1 from chromatin. DPC proteolysis enables the repair of the lesions via downstream DNA repair pathways. May be recruited to DPCs via the SUMOylation of substrate proteins at damaged DNA sites.
The SHP box and the VCP-interaction motif (VIM) are important both together for binding to CDC48. The 2 SUMO interaction motifs (SIM) are each important for binding to SMT3(SUMO).
Was initially reported to be a SUMO-dependent isopeptidase (PubMed:20516210), but this activity could not be confirmed (PubMed:24998930).
3-keto-steroid reductase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:10535978, PubMed:12119386, PubMed:12842197, PubMed:15995173). ERG27 is a catalytic component of the C-4 demethylation complex that catalyze the reduction of the keto group on the C-3 (PubMed:10535978). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672).
Belongs to the short-chain dehydrogenases/reductases (SDR) family. ERG27 subfamily.
Facilitates the association of ERG7 with lipid particles preventing its digestion in the endoplasmic reticulum and the lipid particles.
Heterotetramer of ERG25, ERG26, ERG27 and ERG28. ERG28 acts as a scaffold to tether ERG27 and other 4,4-demethylation-related enzymes, forming a demethylation enzyme complex, in the endoplasmic reticulum. Interacts with ERG25 and ERG28. Also interacts with ERG7, but only in lipid particles.
Interacts with DNF3; interaction is required for proper expression and endoplasmic reticulum (ER) export of either partner.
Potential non-catalytic subunit for a heteromeric phospholipid translocase (PLT) CRF1-DNF3, implicated in the translocation of phospholipids from the outer to the inner leaflet of membrane bilayers. Shares an essential function for cell growth with PLTs CDC50-DRS2 and LEM3-DNF1/2. May be involved in transport from early endosomes to the trans-Golgi network (TGN).
Present with 4510 molecules/cell in log phase SD medium.
It is uncertain whether Met-1 or Met-10 is the initiator.
Sequentially activated during the process of meiosis and spore formation.
Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.
Interacts with PCNA (POL30). Three molecules of RAD27 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma.
Present with 6120 molecules/cell in log phase SD medium.
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).
Contains two cysteine rich domains (CRD), referred to as the N- and C-terminal CRD's, n-CRD (Cys-303, Cys-310 and Cys-315) and c-CRD (Cys-598, Cys-620 and Cys-629), respectively. Cys-315 is not conserved in orthologs in other yeast species. A nuclear export signal is embedded in the c-CRD, with which the nuclear export protein CRM1/exportin 1 interacts only in the absence of disulfide bonds (or otherwise oxidized cysteines) within the c-CRD or between the c-CRD and the n-CRD.
Depending on the oxidative stress inducing agent, YAP1 can undergo two distinct conformational changes, both involving disulfide bond formation, and both masking the nuclear export signal, thus abolishing nuclear export by CRM1/exportin 1. The disulfide stress-inducing agent diamide leads to the formation of one of three possible disulfide bonds in the c-CRD. Peroxide stress induces the formation of the HYR1/GPX3- and YBP1-dependent interdomain disulfide bond between Cys-303 and Cys-598 (causing nuclear localization of YAP1), and the possibly stabilizing bond between Cys-310 and Cys-629 (required for full activity of YAP1).
Interacts independent of oxidation state in the cytoplasm with the karyopherin PSE1/KAP121 (and less strongly with KAP123). The reduced form of YAP1 interacts in the nucleus with the nuclear export protein CRM1, and in the cytoplasm with YBP1 and the peroxiredoxin HYR1/GPX3/ORP1. Interacts with RBG1.
Transcription activator involved in oxidative stress response and redox homeostasis. Regulates the transcription of genes encoding antioxidant enzymes and components of the cellular thiol-reducing pathways, including the thioredoxin system (TRX2, TRR1), the glutaredoxin system (GSH1, GLR1), superoxide dismutase (SOD1, SOD2), glutathione peroxidase (GPX2), and thiol-specific peroxidases (TSA1, AHP1). The induction of some of these genes requires the cooperative action of both, YAP1 and SKN7. Preferentially binds to promoters with the core binding site 5'-TTA[CG]TAA-3'. Activity of the transcription factor is controlled through oxidation of specific cysteine residues resulting in the alteration of its subcellular location. Oxidative stress (as well as carbon stress, but not increased temperature, acidic pH, or ionic stress) induces nuclear accumulation and as a result YAP1 transcriptional activity. Activation by hydrogen peroxide or thiol-reactive chemicals elicit distinct adaptive gene responses. Nuclear export is restored when disulfide bonds are reduced by thioredoxin (TRX2), whose expression is controlled by YAP1, providing a mechanism for negative autoregulation. When overexpressed, YAP1 confers pleiotropic drug-resistance and increases cellular tolerance to cadmium, iron chelators and zinc.
YAP1 expression is at least partially regulated at the level of translation. A small upstream open reading frame (uORF) retains the 40S ribosomal subunit. By leaky scanning it then proceeds and reinitiates at the functional YAP1 ORF.
Activity is strongly promoted by Co(2+), Ni(2+) and Mn(2+) (PubMed:27322068). Activity is inhibited by EDTA (PubMed:27322068).
Belongs to the damage-control phosphatase family. Sugar phosphate phosphatase III subfamily.
Expression is up-regulated in response to treatment with the DNA-damaging agent methyl methanesulfonate (MMS).
Leads to the accumulation of fructose-1-phosphate (PubMed:27322068). Leads to increased DNA damage or decreased repair (PubMed:18085829).
Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (PubMed:27322068). Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism (PubMed:27322068).
Phosphatase activity is strongly promoted by several divalent cations but it is suggested that Mn(2+) and possibly Ni(2+) represent biologically relevant metal ion cofactors for damage-control phosphatases.
Subfamily III proteins have a conserved RTxK motif about 40-50 residues from the C-terminus; the threonine may be replaced by serine or cysteine.
Interacts with XRS2 and associates with DNA double-strand breaks.
Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Recruited by the MRX-complex to sites of DNA lesions immediately after damage to initiate non-homologous end-joining (NHEJ). Subsequently displaced by the RPA complex in a reaction probably involving the SAE2 protein. Phosphorylates MRE11 and XRS2, 2 subunits of the MRX-complex. The phosphorylation of MRE11 is a feedback response from the checkpoint signaling pathway. Phosphorylates RAD9, CHK1 and RAD53, leading to the activation of the CHK1 and RAD23 kinases involved in the DNA damage response cascade. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of DNA damage, also involved in the regulation of DNA damage response mechanism. Phosphorylates also SLX4 and RTT107 which are involved in genome stability. Required for the control of telomere length and genome stability.
Belongs to the mitochondrion-specific ribosomal protein mL61 family.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (PubMed:24675956, PubMed:25609543). mL61 is not essential in cells grown at 30 degree Celsius but is required for mitochondrial translation in cells grown at 18 degree Celsius.
Acts as an E3 ligase mediating SUMO/Smt3 attachment to septins and PCNA. May be involved in chromosome maintenance.
The SAP domain is required for nuclear targeting.
The SP-RING-type zinc finger mediates interaction with UBC9 and CDC3 and is required for E3 activity.
During endoplasmic reticulum (ER) stress or when cellular ceramide levels increase, induces contacts between the ER and medial-Golgi complex to facilitate non-vesicular transport of ceramides from the ER to the Golgi complex where they are converted to complex sphingolipids, preventing toxic ceramide accumulation.
Cell membrane polyamine/proton antiporter, involved in the detoxification of excess polyamines in the cytoplasm. Recognizes spermidine, spermine and the antimalarial drug quinidine, but not quinine, chloroquine and mefloquine.
Present with 21400 molecules/cell in log phase SD medium.
Decreases haze protective activity in white wine.
Expression is induced in both high and low pH environments.
Secreted protein that may be involved in cell wall organization and biosynthesis.
Present with 93700 molecules/cell in log phase SD medium.
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Belongs to the GatB/GatE family. GatB subfamily.
Subunit of the heterotrimeric GatFAB amidotransferase (AdT) complex, composed of A (HER2), B (PET112) and F (YGR102C) subunits.
This protein may be expected to contain an N-terminal transit peptide but none has been predicted.
Assembly factor that plays a role in the assembly of the respiratory chain supercomplexes (SCs) composed of ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV). Involved in the recruitment of COX13 and RCF2 into cytochrome c oxidase. May also be required for late-stage assembly of the COX12 and COX13 subunits (PubMed:22342701, PubMed:22405070, PubMed:22310663). Required for the generation and maintenance of a normal proton motive force (PMF) across the inner mitochondrial membrane (IMM) by preventing proton leakage through an inactive population of CIV that accumulates when RCF1 and/or RCF2 proteins are absent (PubMed:30683696, PubMed:31591265).
Associates with a subpopulation of the cytochrome bc1-cytochrome c oxidase supercomplexes (PubMed:19750512, PubMed:22342701, PubMed:22405070, PubMed:22310663). Associates in substoichiometric amounts with complex IV (PubMed:22310663). Interacts with COX3 (PubMed:22310663).
Increases frequency of mitochondrial genome loss. Promotes reactive oxygen species (ROS) generation.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YOR142W-A ORF.
Component of the peroxisomal translocation machinery with PEX13 and PEX14. Interacts indirectly with the PTS1 receptor (PAS10/PEX5) and directly binds to PEX14. Required for import of both PTS1 and PTS2 proteins.
Forms a heterotrimeric complex with RPL5 and RPL11A or RPL11B. Interaction of this complex with KAP104 allows the nuclear import of the heterotrimer.
Nuclear import adapter that specifically recruits the two functionally and topologically linked ribosomal proteins RPL5 and RPL11 (encoded by RPL11A and RPL11B). Guarantees that this cargo pair remains bound together from the time of synthesis in the cytoplasm until delivery to the nascent 5S rRNA in the nucleus.
Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. The action of SPO11 is important in setting off a regulatory chain of events encompassing 5' to 3' resection. When there are no SPO11-DSBs, resection of a site specific VDE-DSB takes place but it is faster than in wild-type meiosis and increases the risk of uncovering flanking homology.
Plays a role in the maintenance of mitochondrial DNA.
Present with 168000 molecules/cell in log phase SD medium.
Belongs to the phospholipid scramblase family.
Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Required for the entry in S phase and for cell division.
Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5; loaded onto DNA, forms a head-head double hexamer. Interacts with MCM10.
Probable serine/threonine protein kinase which may function redundantly with MPK1-independent branch of the PCK1 pathway that is presumed to be required for the tolerance to high temperatures and staurosporine.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.
Probably involved in copper transport and in the regulation of cellular copper level. Retrieves copper from the metallochaperone ATX1 and incorporates it into trans-Golgi vesicles.
Glucose transport is thought to be mediated by two kinetically distinct systems, a glucose-repressible high-affinity system and a constitutive low-affinity system.
Present with 37200 molecules/cell in log phase SD medium.
Repressed at high glucose concentrations.
Cleavage of the transit peptide by mitochondrial processing protease (MPP) produces a long integral membrane form of MGM1 (l-MGM1). Further processing by the rhomboid protease PCP1 produces a short peripheral membrane form of MGM1 (s-MGM1). Both isoforms are required for full activity.
Deletion of MGM1 causes the mitochondria to fragment and aggregate, and subsequently to lose their mitochondrial DNA and become respiration deficient.
Dynamin-related GTPase required for mitochondrial fusion. Coordinates interaction between the inner and outer mitochondrial membrane to promote the formation of the double membrane.
Homooligomer. Associates with FZO1 through interaction with the intermembrane space domain of UGO1 which binds FZO1 through its cytoplasmic domain.
Catalyzes the final step in the CDP-ethanolamine route leading to phosphatidylethanolamine (PE). Can also catalyze the formation of phosphatidylcholine (PC) from CDP-choline, but does not substantially contribute to PC biosynthesis. Preferentially uses CDP-dimethylethanolamine and CDP-propanolamine as aminoalcohol substrates. Shows highest activity toward di-unsaturated diacylglycerol species as lipid substrates. The CDP-ethanolamine pathway may play a role in maintaining the proper PE species distribution.
Repressed by inositol. Repression is dependent on the presence of CPT1.
Requires a divalent cation activator, and is inhibited by CMP. Activated by phospholipids, especially phosphatidylcholine.
This is one of two catalases in S.cerevisiae; the other is catalase T, which is the cytoplasmic form.
Regulates the activity of glycogen synthase. It is most probably a regulatory subunit for protein phosphatase type 1.
Cells are impaired in growth on synthetic complete medium with acetate as a carbon source due to defects in mitochondrial [4Fe-4S] cluster formation.
Homodimer; in absence of BOL3, probably bridged by an iron-sulfure cluster (PubMed:27532773). Interacts with BOL3 (PubMed:27532773). Interacts with apo-target proteins, such as ACO1, LYS4, ACO2 and SDH2 (PubMed:27532773).
Involved in iron homeostasis within the mitochondrion where it is involved in the assembly of iron-sulfur proteins (PubMed:10468587, PubMed:27532773). Together with BOL3, required during the last step of iron-sulfur protein assembly when the iron-sulfur cluster is inserted into the target protein (PubMed:27532773). Required for protecting iron sulfur clusters from oxidative damage (PubMed:27532773).
Present with 11300 molecules/cell in log phase SD medium.
The CxxC motif may bind a [4Fe-4S] cluster.
Highly specific phosphatase involved in the metabolism of ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of tRNA splicing. Removes ADP-ribose from glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose.
Causes severe growth phenotype and leads to reduced biogenesis of mitochondrial proteins and abnormal mitochondrial morphology (PubMed:22467864). Compromises import of multispan mitochondrial outer membrane (MOM) proteins (PubMed:22467864).
Component of the MIM complex containing at least MIM1 and MIM2 (PubMed:22467864). Interacts with MIM1; interaction is direct (PubMed:22467864).
Component of the MIM complex required for outer membrane protein import (PubMed:22467864). Involved in import of the subset of proteins with multiple alpha-helical transmembrane segments, including UGO1, TOM20 and FZO1 (PubMed:22467864).
Belongs to the glycosyl hydrolase 5 (cellulase A) family.
Belongs to the phosphatase 2A regulatory subunit A family.
Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure.
PP2A exists in several trimeric forms, all of which consist of a core composed of a catalytic subunit associated with a 65 kDa regulatory subunit (PR65) (subunit A). The core complex associates with a third, variable subunit (subunit B), which confers distinct properties to the holoenzyme.
Phosphatase 2A affects a variety of biological processes in the cell such as transcription, cell cycle progression and cellular morphogenesis, and provides an initial identification of critical substrates for this phosphatase. The regulatory subunit may direct the catalytic subunit to distinct, albeit overlapping, subsets of substrates.
Interacts with SSC1; binds to the nucleotide-free state as well as to the ADP- or ATP-bound state of SSC1.
Involved in protein import into mitochondria. Acts as a Hsp70-specific chaperone that prevents self-aggregation of the matrix Hsp70 chaperones SSC1 (mtHSP70) and SSQ1, thereby maintaining their function in mitochondrial protein import and Fe/S protein biosynthesis. May act together with PAM18 as co-chaperone to facilitate recognition and folding of imported proteins by SSC1 in the mitochondrial matrix.
Decrease in plasma membrane electron transport.
Cofactor for the uncoating of clathrin-coated vesicles (CCVs) by Hsp70-type chaperones (SSA1/2/3 and SSB1/2). Coat disassembly is important for fusion of vesicles with target membranes and for recycling components of clathrin coats to the cytoplasm for further rounds of vesicle formation. Binds to assembled clathrin and recruits the ATP-activated chaperone to CCVs. Stimulates the ATPase activity of the clathrin-associated Hsp70-type chaperone SSA1, which then disrupts clathrin-clathrin interactions, leading to release of the clathrin coat. In addition, prevents unproductive clathrin assembly in the cell. Also required for cortical endoplasmic reticulum inheritance.
Interacts with the clathrin light and heavy chains CLC1 and CHC1, respectively. Binds to clathrin with its N-terminal domain containing 3 clathrin-binding (CB) motifs. Association with clathrin is transient. Binds to polyubiquitin and ubiquitinated proteins.
The TPR repeats and the J domain are required for interaction with Hsp70-type chaperones. The J domain is responsible for stimulating the ATPase activity of the chaperone.
Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain.
Belongs to the dienelactone hydrolase family.
E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (PubMed:19687296, PubMed:22471590, PubMed:35768507). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (PubMed:35768507). PEX2 also regulates peroxisome organization by acting as a E3 ubiquitin-protein ligase (PubMed:35768507). PEX2 ubiquitinates PEX5 during its passage through the retrotranslocation channel: catalyzes monoubiquitination of PEX5 at 'Cys-6', a modification that acts as a signal for PEX5 extraction into the cytosol (PubMed:35768507).
Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate (PubMed:9521740). Essential for growth under anaerobic conditions (PubMed:12062417).
Transiently phosphorylated on a His residue during the reaction cycle (By similarity). Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production (PubMed:9521740). Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release (By similarity).
Component of the dynactin complex composed of at least ARP1, JNM1, NIP100 and ARP10. Dynactin comprises a short rod of the ARP1 filament attached to ARP10 at its pointed-end and probably associated with the capping protein at its barbed-end. The rod is implicated in dynein cargo binding. A sidearm formed by NIP100 projects from the ARP1 filament and is implicated in motor binding (By similarity).
Motor-binding component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding (By similarity). The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint.
Belongs to the carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family.
Catalyzes the hydrolysis of the amide bond in N-(4-oxoglutarate)-L-cysteinylglycine (deaminated glutathione), a metabolite repair reaction to dispose of the harmful deaminated glutathione (PubMed:28373563). Possesses amidase activity toward deaminated ophthalmate in vitro (PubMed:28373563).
Induced during anaerobic growth and completely repressed during aerobic growth.
Expressed during meiosis and ascospore formation. First expressed at the beginning of meiosis I, and is highly expressed prior meiosis II.
Interacts with itself. Interacts with CDC11 and SPR3; probably to form a ring at the bud neck.
May be involved in phosphatase regulation and/or generation of precursor metabolites and energy.
Component of the nuclear complex (NPC) (PubMed:24152732). NPC constitutes the exclusive means of nucleocytoplasmic transport (PubMed:24152732). NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope (PubMed:24152732). Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof (PubMed:24152732). Interacts with NUP60 and NIC96, which tether it to the nuclear pore complex. Component of the spindle pole body core in which it interacts directly with SPC110, SPC42 and SPC29. Also interacts with YKU70 (HDF1) and MLP1.
Together with the closely related MLP1, involved in the structural and functional organization of perinuclear chromatin (PubMed:10638763). MLP1/MLP2 associate with the nuclear pore complex and form filamentous structures along the nuclear periphery (PubMed:10085285, PubMed:24152732, PubMed:10617624). Has a role in the localization of Esc1 to nucleolar regions (PubMed:24152732). Together with MLP1, mediates tethering of the some telomeres to the nuclear periphery, probably mediated by YKU70/YKU80 (HDF1/HDF2) heterodimer and show perinuclear location dependent silencing (PubMed:11862215). MLP1 and MLP2 are involved in telomere length regulation but not silencing or telomere anchoring (PubMed:12490156). Plays a role in the incorporation of components into the spindle pole body (PubMed:10617624, PubMed:14718167, PubMed:16027220). Involved in double-strand break repair, probably also mediated by the YKU70/YKU80 (HDF1/HDF2) heterodimer (PubMed:10638763, PubMed:14718167, PubMed:16027220).
Expression is induced by the KAR4 transcription factor.
May be involved in the regulation of dNTP production. Induces the SOS system when expressed in E.coli, therefore, it may play a role in DNA metabolism and/or in genome stability.
Related to oxidoreductases, but misses the conserved Thr active site. Therefore it may not have any oxidoreductase activity.
Suppresses the lethality of LCD1 and RAD53 mutations. Leads to resistance to the chemicals that inhibit nucleotide metabolism and increases dNTP levels in the presence of hydroxyurea.
Expressed very quickly after G1 release, just prior to initiation of DNA replication.
Negative regulator of GDH1, the activator protein that regulates the ubiquitin ligase activity and substrate specificity of the anaphase promoting complex/cyclosome (APC/C), and which is required for exit from mitosis, cytokinesis and formation of prereplicative complexes in G1.
Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 10 subunits. The complex is composed of 3 respiratory subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10 (PubMed:10873857, PubMed:11880631, PubMed:18390544, PubMed:30598554). The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a monomer or a dimer of cytochrome c oxidase (complex IV, CIV), resulting in 2 different assemblies (supercomplexes III(2)IV and III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556, PubMed:30598554).
Does not seem to have protease activity as it lacks the zinc-binding site.
Present with 35700 molecules/cell in log phase SD medium.
Responsible for the proteolytic maturation of the alpha-factor precursor.
Interacts with FLO8 and MSS11, both morphogenetic transcription factors binding directly to the FLO11 promoter.
Transcriptional regulator with a general role in all morphogenetically distinct forms of filamentous growth, namely haploid invasive growth, biofilm formation, and diploid pseudohyphal growth. May control FLO11 gene expression as part of a promoter-bound complex with FLO8 and MSS1.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC7 subfamily.
Serine/threonine-protein kinase. Needed for the initiation of DNA synthesis during mitosis as well as for synaptonemal complex formation and commitment to recombination during meiosis. Required for HTA1-HTB1 locus transcription repression.
Catalyzes the attachment of lysine to tRNA(Lys) in the mitochondrion.
Belongs to the TRAFAC class YlqF/YawG GTPase family. GEP3 subfamily.
Interacts genetically with prohibitins and thus may be involved in the mitochondrial lipid metabolism.
Deletion causes an increase in metal sensitivity at 15 mM manganese, but does not affect invertase glycosylation. Deletion shows increased sensitivity to external iron, which is suppressed by MRS3 or MRS4 overexpression requiring oxygen but not respiration, and exacerbated by ectopic expression of the iron transporter FET4. Deletion also results in decreased vacuolar iron content and decreased iron stores, which affect cytosolic iron levels and cell growth. Deletion together with MRS3 and MRS4 restores cellular and mitochondrial iron homeostasis to near normal level, corrects the MRS3 and MRS4 double deletion phenotype (which shows increased resistance to cobalt but decreased resistance to copper and cadmium), and has near normal levels of aconitase activity. When overexpressed, maintains respiratory function in a YFH1 deletion mutant regardless of extracellular iron concentration, activates the iron-dependent transcription factor AFT1 resulting in an increase in iron uptake, cytosolic iron accumulation and a change in copper metabolism. Overexpression prevents excessive mitochondrial iron accumulation by limiting mitochondrial iron uptake and results in increased expression of the high affinity iron transport system composed of FET3 and FTR1. Overexpression also suppresses the rapamycin-resistant phenotype of PMR1 deletion mutant.
Down-regulated under iron starvation by TIS11. Transcriptionally up-regulated by YAP5 in response to increased cytosolic iron.
Has a role in both calcium and manganese homeostasis. Involved in the transfer of iron and Mn(2+) from the cytosol to the vacuole for storage of these metals.
Interacts with GYP5 and RVS167. Is part of SEC4-containing complexes.
Probable GTPase-activating protein which stimulates the GTP hydrolysis rate by GYP5 of YPT1 and SEC4. Involved in ER to Golgi trafficking and polarized exocytosis.
Component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs) (PubMed:21708174, PubMed:9843512, PubMed:9848653, PubMed:21131909). The protein component of the H/ACA snoRNP contains CBF5, GAR1, NHP2 and NOP10 (PubMed:21708174, PubMed:9843512, PubMed:9848653, PubMed:21131909). The complex contains a stable core composed of CBF5 and NOP10, to which GAR1 and NHP2 subsequently bind (PubMed:21708174, PubMed:9843512, PubMed:9848653, PubMed:21131909). Interacts with SHQ1 (PubMed:12228251). Interacts with NAF1 (PubMed:12515383).
Non-catalytic component of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP), which catalyzes pseudouridylation of rRNA and is required for ribosome biogenesis (PubMed:9843512, PubMed:9848653). This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1 (PubMed:9843512, PubMed:9848653). Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs (PubMed:9843512, PubMed:9848653). The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs (PubMed:21131909). The H/ACA snoRNP complex mediates pseudouridylation at position 93 in U2 snRNA (PubMed:21131909). Essential for growth (PubMed:9843512). Directly binds H/ACA snoRNAs (PubMed:11433018).
Essential for the formation and/or stabilization of microtubules. Binds to microtubules in vitro.
Component of the ceramide synthase complex composed of at least LAC1, LAG1 and LIP1.
Component of the ceramide synthase complex required for synthesis of ceramides.
Contains seven CCCH Zn fingers that bind to A-rich RNAs and fingers 5 to 7 are critical for these function (PubMed:12496292, PubMed:22560733, PubMed:28180315). Binding A(11)G RNA induces dimerization of Zn fingers 5-7 mediated by the spatial arrangement of the fingers promoting each RNA chain binding two protein chains (PubMed:28180315).
Essential protein that binds to polyadenylated RNA and single-stranded DNA (PubMed:8474438). It may be involved not only in RNA processing but also in transcription regulation. Associates directly with nascent RNA polymerase II transcripts and remain associated during subsequent nuclear RNA processing reactions (Probable). Involved in mRNA poly(A) tail length control and nuclear export (PubMed:11927564, PubMed:11779864). Functions in surveillance and the packaging leading to generation of export-competent mRNPs. Controls both mRNP compaction that facilitates movement through nuclear pore complexes and the length of transcript poly(A) tails (PubMed:19840948, PubMed:22560733).
Present with 9670 molecules/cell in log phase SD medium.
The N-terminal domain is required for nuclear export of both poly(A) RNA and NAB2.
The RGG domain is important for NAB2 import.
In the C-terminal section; belongs to the NAGSA dehydrogenase family.
In the N-terminal section; belongs to the acetylglutamate kinase family.
The kinase activity is inhibited by arginine.
The protein precursor is cleaved into the two biologically active enzymes, the kinase and the reductase.
Involved in uptake of biotin with the concomitant entry of protons.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Erg6/SMT family.
Present with 53800 molecules/cell in log phase SD medium.
Sterol 24-C-methyltransferase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:6363386). ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol (PubMed:6363386). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672).
Associated with nucleolar and cytoplasmic pre-60S particles. Directly interacts with RLP24.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. NOG subfamily.
Present with 28000 molecules/cell in log phase SD medium.
Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Silenced copy of A1 at HMR.
There is no sequence for the expressed copy of A1 in strain S288c, because this strain is of mating type alpha. A sequence for the expressed copy of A1 can be found in other strains (AC P0CY10).
Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Together with GET1, acts as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. The GET complex cooperates with the HDEL receptor ERD2 to mediate the ATP-dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER. Involved in DNA replication and DNA damage response and also in cell wall function.
Essential for the establishment and maintenance of sister chromatid cohesion at centromere proximal and distal regions during S phase. Also required for chromosomal condensation.
Belongs to the actin family. ARP2 subfamily.
Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament (By similarity).
Affects the glycerophosphocholine metabolism but not the glycerophosphoinositol metabolism (PubMed:16141200).
Glycerophosphocholine glycerophosphodiesterase responsible for the hydrolysis of intracellular glycerophosphocholine into glycerol-phosphate and choline (PubMed:16141200, PubMed:16172116). The choline is used for phosphatidyl-choline synthesis. Required for utilization of glycerophosphocholine as phosphate source (PubMed:16141200). May also use glycerophosphoinositol as substrate in vivo (PubMed:16172116).
Belongs to the eukaryotic ribosomal protein eS26 family.
Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). eS26 interacts with eS1 forming part of the mRNA exit tunnel (PubMed:9559554, PubMed:22096102). eS26 interacts with TSR2 (PubMed:10688190, PubMed:12837249).
Inhibited by fructose 6-P, activated by glycerol 3-P.
Monofunctional, high-specificity fructose-2,6-bisphosphatase, which releases phosphate from the 2-position of fructose 2,6-bisphosphate. Has no detectable 6-phosphofructo-2-kinase activity.
Belongs to the Mediator complex subunit 20 family.
Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. MED1 interacts directly with MED4 and MED7. SRB2/MED20 interacts directly with SRB4/MED17 and SRB5/MED18.
Dosage-dependent suppressor of Ty-induced promoter mutations. May exert its suppression effect through protein-protein interactions since does not present any of the motifs generally found in transcriptional activators or DNA binding proteins.
Belongs to the ATF1 alcohol acetyltransferase family.
Expression is repressed both by aeration and by unsaturated fatty acids (PubMed:9055409, PubMed:9675816). Also repressed by heat and ethanol stress (PubMed:14654433). Rapid induction by glucose depends on the cAMP/PKA signaling pathway (PubMed:14654433). Long-term expression requires both carbon and nitrogen sources (PubMed:14654433). The activation of transcription is dependent on RAP1, and the ROX1-TUP1p-SSN6 hypoxic repressor complex is responsible for repression by oxygen (PubMed:10487921). The putative ROX1-binding sequence in the ATF1 promoter is 5'-CCTATTGTTTT-3' and the RAP1-binding sequence is 5'-AACCCAACAAA-3' (PubMed:10487921).
Found to be inhibited by cadmium, copper, zinc and mercurium divalent cations and sulfhydryl reagents (PubMed:7764365). Inhibited by the addition of unsaturated fatty acids to the culture (PubMed:7764365).
Major alcohol O-acetyltransferase that uses acetyl-CoA to synthesize acetate esters from various alcohols, producing ethyl acetate, isoamyl acetate, isobutyl acetate, butyl acetate, hexyl acetate, heptyl acetate and octyl acetate (PubMed:7764365, PubMed:9758847, PubMed:10653746, PubMed:12937998, PubMed:16845703, PubMed:18597084, PubMed:17891501, PubMed:25306884, PubMed:28160314). The alcohol acyltransferase activity is promiscuous with regard to alcohol but relatively specific for acetyl-CoA since ATF1 does not use any other acyl-CoAs (C3, C4, C5, C6, C8, C10, C12) (PubMed:28160314). Acts also as an efficient thioesterase in vitro with specificity towards medium-chain-length acyl-CoAs (PubMed:28160314). In natural environments, the production of aromatic volatile metabolites promotes dispersal through insect vectors (PubMed:25310977).
Reduces levels of isoamyl acetate production during fermentation to about 16% of those produced by the wild-type strain and causes a 40% reduction of ethyl acetate formation (PubMed:12957907).
Segments of the N- and C-terminal domains (residues 24-41 and 508-525, respectively) are predicted to be amphipathic helices and are essential for endoplasmic reticulum and lipid dropplet association (PubMed:25093817).
Understanding the biochemistry of the volatile esters is of considerable importance in industrial agriculture, winemaking and brewing. ATF1 could profoundly affect the flavor profiles of wines and distillates deficient in aroma, thereby paving the way for the production of products maintaining a fruitier character for longer periods after bottling (PubMed:10653746, PubMed:16845703, PubMed:18597084, PubMed:25306884, PubMed:28176138). The most important acetate esters from the perspective of fermented foods and beverages are probably ethyl acetate (fruity, solvent aroma), isobutyl acetate (sweet, fruit), isoamyl acetate (banana) and 2-phenylethyl acetate (rose). In addition, the enzymes responsible for ester synthesis are targets for the metabolic engineering of cellular factories intended to produce insect pheromones for use in pest control, but also for the production of fragrances, industrial solvents, fine chemicals, pharmaceuticals and renewable biofuels (PubMed:25281839, PubMed:24609358, PubMed:26205521, PubMed:26801935).
Belongs to the type 2 lipid phosphate phosphatase family.
Dihydrosphingosine 1-phosphate phosphatase required for efficient ceramide synthesis from exogenous sphingoid bases (PubMed:10477278, PubMed:10563329, PubMed:10856228, PubMed:9353337, PubMed:9419344). Involved in endocytosis and calcium-mediated signaling (PubMed:10856228).
Belongs to the ZIP transporter (TC 2.A.5) family. KE4/Catsup subfamily.
Zinc transporter whose role depends on the zinc status of the cells. It helps to balance zinc levels between the cytosol and the secretory pathway. It transports zinc into the secretory pathway in a zinc-adequate environment and in a high zinc medium. In high zinc medium, transport of zinc into the secretory pathway is a way to eliminate zinc from the cytosol. Under low cytosolic zinc conditions, it removes zinc from the secretory pathway and acts as zinc importer that helps to alleviate ER stress.
Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family.
Pyridoxal 5'-phosphate (PLP)-binding protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5'-phosphate (PLP), the active form of vitamin B6.
Component of the mitochondrial outer membrane sorting assembly machinery (SAM or TOB) complex, which at least consists of SAM35, SAM37 and SAM50 (PubMed:14570913, PubMed:14685243, PubMed:15590639). Associates with the mitochondrial contact site and cristae organizing system (MICOS) complex (also known as MINOS or MitOS complex) (By similarity).
Its C-terminal part seems to contain many membrane-spanning sided beta-sheets, that have the potential to adopt a transmembrane beta-barrel type structure.
Interacts with SKP1 and CDC53. Component of the probable SCF(YBR352W) complex containing CDC53, SKP1, RBX1 and YBR352W.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Present with 164000 molecules/cell in log phase SD medium.
Component of the origin recognition complex (ORC) composed of at least ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. Interacts with MCM10 and TAH11.
Belongs to the TPT transporter family. SLC35C subfamily.
Belongs to the nucleoporin Nup85 family.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NUP85 is part of the heptameric 0.5 MDa autoassembling NUP84 NPC subcomplex (NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1). NUP85 also interacts directly with the GLFG repeats of NUP116 and directly or indirectly with the mRNA transport factor MTR2.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP85 is involved in nuclear poly(A)+ RNA and pre-ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization.
Belongs to the bacterial ribosomal protein bL32 family.
Component of the mitochondrial large ribosomal subunit (mt-LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. bL32m has a zinc binding site.
Interacts with H3K4me3 and to a lesser extent with H3K4me2. Component of the RPD3C(L) complex composed of at least ASH1, CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6.
Protein required for cold tolerance (PubMed:25725023). Plays a role in the regulation of phosphate uptake (PubMed:25725023).
By copper deprivation and repressed by copper excess.
Abolishes acetylation of histone H3 'Lys-56'; simultaneous disruption of GCN5 also abolishes acetylation of histone H3 'Lys-9' and 'Lys-27' (PubMed:21256037). Decreases acetylation of histone H3 'Lys-9' and 'Lys-23' (PubMed:19172748). Decreases HTA1 RNA level; simultaneous disruption of HIR1 or RTT106 alleviates the effect (PubMed:19683497). Increases sensitivity to methyl methane sulfonate, hydroxyurea, and camptothecin (genotoxic stress) (PubMed:18568037, PubMed:18719104).
Forms a complex composed of two RTT109 subunits and one VPS75 homodimer; each RTT109 subunit interacts predominantly with VPS75 instead of interacting with the other RTT109 subunit (PubMed:21256037, PubMed:20560668, PubMed:17320445, PubMed:31387991, PubMed:18719104). Interacts with VPS75; the interaction is direct (PubMed:31387991, PubMed:20560668, PubMed:17369253, PubMed:17690098, PubMed:17320445, PubMed:17272723, PubMed:18723682, PubMed:18719104, PubMed:21256037). Interacts (via C-terminus) with ASF1; the interaction is direct (PubMed:29300933, PubMed:31387991, PubMed:17690098, PubMed:17320445). Interacts with histone H3/H4 heterodimers via histone H3 (PubMed:21454705, PubMed:19172748).
Histone chaperone-dependent acetylase that modifies 'Lys-9', 'Lys-14', 'Lys-23', 'Lys-27', and 'Lys-56' on histone H3 (H3K9Ac, H3K14Ac and H3K23Ac, H3K27Ac, and H3K56Ac) to promote nucleosome assembly, genomic stability, DNA repair and transcriptional regulation during mitotic S-phase (PubMed:31194870, PubMed:17046836, PubMed:17369253, PubMed:17320445, PubMed:17272723, PubMed:18723682, PubMed:20560668, PubMed:21256037, PubMed:29300933, PubMed:19172748, PubMed:19683497). Its residue selectivity is influenced by the acetylation status of histone H3, and also the presence of histone chaperone ASF1 that shifts selectivity to 'Lys-56' when H3K14Ac is already present (PubMed:31194870). H3K56 acetylation weakens the interaction between the histone core and the surrounding DNA in the nucleosomal particle and drives chromatin disassembly (PubMed:18577595). Autoacetylates (PubMed:18568037, PubMed:18707894, PubMed:18719104). Independently of acetyltransferase activity, stimulates histone deposition by VPS75 (PubMed:19172748). Involved in regulation of Ty1 transposition (PubMed:11779788).
FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation in the endoplasmic reticulum lumen in parallel to ERO1.
Homodimer. Interacts with the substrate protein PDI1, forming transient intermolecular disulfide bridges.
Belongs to the nucleotide-sugar transporter family. SLC35B subfamily.
Sugar transporter that specifically mediates the transport of UDP-N-acetylglucosamine (UDP-GlcNAc) and is required for cell wall chitin synthesis.
Essential regulatory protein in yeast whose DNA-binding sites are found at three types of chromosomal elements: promoters, silencers, and telomeres. RAP1 is also involved in the regulation of telomere structure, where its binding sites are found within the terminal poly[C(1-3)A] sequences. The opposite regulatory functions of RAP1 are not intrinsic to its binding sites but, instead, result from interactions with different factors at promoters and silencers. RAP1 associates with SIR3 and SIR4 proteins to form a DNA-binding complex that initiates the repression at the HM loci and telomeres. May also target the binding of RIF1 and RIF2 to silencers and telomeres. Forms with GCR1 a transcriptional activation complex that is required for expression of glycolytic and ribosomal gene.
Present with 4390 molecules/cell in log phase SD medium.
RIF1, SIR3 and SIR4 associate with RAP1 C-terminus in vivo. Interacts with a GCR1 homodimer.
Seems to be degraded by the proteasome upon its formation.
Short-lived chaperone present in the precursor form of the 20S proteasome and absent in the mature complex. Required for the correct assembly and enzymatic activation of the proteasome. Also prevents premature processing of the PRE2 propeptide.
Important role in G1 events required for bud emergence and septin organization. Coordinates cell growth and cell division at G2/M, essential for efficient cytokinesis and for regulation of SWE1.
Component of the heptameric LSM2-LSM8 complex that forms a seven-membered ring structure with a doughnut shape; an RNA strand can pass through the hole in the center of the ring structure. The LSm subunits are arranged in the order LSM8, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. LSM2-LSM8 associates with PAT1 and XRN1. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 snRNP, spliceosomal U4/U6.U5 snRNP, and free U6 snRNP). It binds directly to the U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. It probably also is involved in degradation of nuclear pre-mRNA by targeting them for decapping. LSM2-LSM8 probably is involved in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM2 is required for processing of pre-tRNAs, pre-rRNAs and U3 snoRNA.
Belongs to the argininosuccinate synthase family. Type 1 subfamily.
Catalyzes the eighth step in arginine biosynthesis. Also has a catabolic function as the first enzyme of citrulline utilization as nitrogen source via arginine and the reactions involved in the arginase pathway.
Present with 20700 molecules/cell in log phase SD medium.
Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling.
Present with 4240 molecules/cell in log phase SD medium.
Component I catalyzes the formation of anthranilate using ammonia rather than glutamine, whereas component II provides glutamine amidotransferase activity.
Tetramer of two components I and two components II.
Yeast component II C-terminal half also has indole-3-glycerol phosphate synthase activity.
Belongs to the amino acid-polyamine-organocation (APC) superfamily. Amino acid/choline transporter (ACT) (TC 2.A.3.4) family.
Inhibition of activity by intracellular choline.
Belongs to the eukaryotic-type primase small subunit family.
DNA polymerase alpha:primase is a four subunit enzyme complex, which is assembled throughout the cell cycle, and consists of the two DNA polymerase subunits A POL1 and B POL12, and the DNA primase large PRI2 and small PRI1 subunits.
DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. In a complex with DNA polymerase alpha (DNA polymerase alpha:primase) constitutes a replicative polymerase. Both primase components participate in formation of the active center, but the ATP-binding site is exclusively located on p48.
Present with 197 molecules/cell in log phase SD medium.
The bound zinc ion is not a cofactor. It is bound to a zinc knuckle motif that may be involved in sequence recognition and the binding of ssDNA (By similarity).
Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits (PubMed:11805306, PubMed:12914699, PubMed:16341226). Interacts with DEF1; the interaction is direct and serves to bridge RPB1 to the Elongin complex in a DNA-damaged dependent manner (PubMed:23993092). Interacts with the Elongin subunit ELA1 (PubMed:23993092). Interacts with the Elongin subunit ELC1 (PubMed:23993092). Interacts with ASK10 (PubMed:14555478). Interacts with ESS1 (PubMed:10531363). Interacts with RTT103 (PubMed:15565157). Interacts with SHE2 (PubMed:20713510).
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. During a transcription cycle, Pol II, general transcription factors and the Mediator complex assemble as the preinitiation complex (PIC) at the promoter. 11-15 base pairs of DNA surrounding the transcription start site are melted and the single-stranded DNA template strand of the promoter is positioned deeply within the central active site cleft of Pol II to form the open complex. After synthesis of about 30 bases of RNA, Pol II releases its contacts with the core promoter and the rest of the transcription machinery (promoter clearance) and enters the stage of transcription elongation in which it moves on the template as the transcript elongates. Pol II appears to oscillate between inactive and active conformations at each step of nucleotide addition. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Pol II is composed of mobile elements that move relative to each other. The core element with the central large cleft comprises RPB3, RBP10, RPB11, RPB12 and regions of RPB1 and RPB2 forming the active center. The clamp element (portions of RPB1, RPB2 and RPB3) is connected to the core through a set of flexible switches and moves to open and close the cleft. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. In elongating Pol II, the lid loop (RPB1) appears to act as a wedge to drive apart the DNA and RNA strands at the upstream end of the transcription bubble and guide the RNA strand toward the RNA exit groove located near the base of the largely unstructured CTD domain of RPB1. The rudder loop (RPB1) interacts with single-stranded DNA after separation from the RNA strand, likely preventing reassociation with the exiting RNA. The cleft is surrounded by jaws: an upper jaw formed by portions of RBP1, RPB2 and RPB9, and a lower jaw, formed by RPB5 and portions of RBP1. The jaws are thought to grab the incoming DNA template, mainly by RPB5 direct contacts to DNA.
Following transcription stress, the elongating form of RNA polymerase II (RNA pol IIo) is polyubiquitinated via 'Lys-63'-linkages on Lys-1246 by the RSP5-UBA1-UBC5 complex at DNA damage sites without leading to degradation: ubiquitination promotes RNA pol IIo backtracking to allow access by the transcription-coupled nucleotide excision repair (TC-NER) machinery (PubMed:32142654, PubMed:15166235, PubMed:15960978, PubMed:19920177). Subsequent DEF1-dependent polyubiquitination by the elongin complex via 'Lys-48'-linkages may lead to proteasome-mediated degradation; presumably at stalled RNA pol II where TC-NER has failed, to halt global transcription and enable 'last resort' DNA repair pathways (PubMed:15166235, PubMed:32142654, PubMed:11859374, PubMed:19920177).
Mutagenesis experiments demonstrate that the minimum viable CTD contains eight consensus Y-S-P-T-S-P-[A-S-N-G] heptapeptide repeats. Identical and simultaneous substitutions in a number of consecutive repeats are lethal: 'Ser-2' -> 'Ala-2' (14 repeats), 'Ser-5' -> 'Ala-5' (15 repeats), '2-Ser-Pro-Thr-Ser-5'-> '2-Ala-Pro-Thr-Ala-5' (10 repeats), 'Ser-2'-> 'Glu-2' (15 repeats), 'Ser-5' -> 'Glu-5' (12 repeats), '2-Ser-Pro-3' -> '2-Pro-Ser-3' (15 repeats) and 'Tyr-1' -> 'Phe-1' (12 repeats).
The C-terminal domain (CTD) serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing.
The binding of ribonucleoside triphosphate to the RNA polymerase II transcribing complex probably involves a two-step mechanism. The initial binding seems to occur at the entry (E) site and involves a magnesium ion temporarily coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits. The ribonucleoside triphosphate is transferred by a rotation to the nucleotide addition (A) site for pairing with the template DNA. The catalytic A site involves three conserved aspartate residues of the RNA Pol II largest subunit which permanently coordinate a second magnesium ion.
The tandem 7 residues repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat. The phosphorylated form of Pol II appears to carry, on average, one phosphate per repeat. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphatases, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed. Phosphorylation at 'Ser-5' occurs in promoter-proximal regions in early elongation. Phosphorylation at 'Ser-2' predominates in regions more distal to the promoter and triggers binding of the 3' RNA processing machinery. CTD kinases include KIN28 (as part of the TFKII complex, a subcomplex of the TFIIH holo complex), SSN3/SRB10 (as part of the SRB8-11 complex, a module of the Mediator complex), CTK1 (as part of CTD kinase), and probably BUR1 (as part of the BUR1-BUR2 kinase complex). Phosphatases include FCP1 and SSU72.
Component of the SCF(UCC1) E3 ubiquitin-protein ligase complex composed of CDC53, SKP1, RBX1 and UCC1 (PubMed:11283612, PubMed:14747994). Interacts with CIT2 (PubMed:25982115).
Expression is down-regulated by the presence of C2-compounds such as acetate.
Leads to poor ubiquitination of CIT2 and accumulation of citrate in the cells.
Substrate recognition component of the SKP1-CUL1-F-box protein E3 ubiquitin-protein ligase complex SCF(UCC1) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:10582239, PubMed:25982115). The SCF(UCC1) complex acts as a metabolic switch for the glyoxylate cycle and regulates the level of CIT2 protein to maintain citrate homeostasis (PubMed:25982115).
Component of the MIM complex containing at least MIM1 and MIM2 (PubMed:15608614, PubMed:18187149, PubMed:21825073, PubMed:22467864). Interacts with MIM2; interaction is direct (PubMed:22467864). Interacts with TOM70 (PubMed:21825073).
Component of the MIM complex required for mitochondrial outer membrane protein import (PubMed:22467864). The MIM complex cooperates with the receptor TOM70 in binding of precursor proteins and promotes their insertion and assembly into the outer membrane (PubMed:21825073). Involved in import of the subset of proteins with multiple alpha-helical transmembrane segments, including UGO1 (PubMed:21825073, PubMed:21825074). Required for the assembly of the TOM (translocase of outer membrane) receptor complex, which is responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins (PubMed:15242642, PubMed:15326197, PubMed:15608614). Required specifically for assembly of TOM40, TOM20, and TOM70, but not TOM22 (PubMed:17974559, PubMed:18187149).
Leads to reduced levels of TOM complex but retains the respiratory chain.
Regulator in phosphate metabolism and acts as a derepressor of another central regulator PHO5. Binds to the upstream activator sequence (UAS) of PHO5. It also binds to the TRP4, HIS4, and CYC1 promoters.
Transport of FAD from the cytosol to the mitochondrial matrix.
Belongs to the mitochondrion-specific ribosomal protein mS42 family.
Component of the mitochondrial small ribosomal subunit (mt-SSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. mS42 forms a dimer with mS43, building a large protuberance adjacent to the mRNA channel exit in the mt-SSU body.
Interacts with MYO2 and VAC8. Interacts with ATG18.
Vacuole-specific MYO2 receptor required for vacuole inheritance. Binds simultaneously to MYO2 and to VAC8, a vacuolar membrane protein, forming a transport complex which moves the attached vacuole membrane along actin cables into the bud. Once the vacuole arrives in the bud, VAC17 is degraded, depositing the vacuole in its correct location.
Required for the accumulation of subunits 1 and 2 of cytochrome c oxidase complex. Thought to play a role in either mitochondrial copper transport or insertion of copper into the active site of COX.
Binds to specific AU-rich elements (ARE) in the 3'-untranslated region of target mRNAs and promotes their degradation. In response to iron deficiency, promotes the decay of many mRNAs encoding proteins involved in iron-dependent pathways. Negatively regulates primarily iron-dependent mitochondrial processes including respiration and amino acid biosynthesis.
By transcription factors AFT1 and AFT2 in response to iron deficiency.
DNA-binding transcription factor that specifically binds heat shock promoter elements (HSE) and activates transcription.
Exhibits temperature-dependent phosphorylation that activates the transcriptional capacity.
Homotrimer (PubMed:8175654). Homotrimerization increases the affinity of HSF1 to DNA (PubMed:8175654).
C-22 sterol desaturase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:8635732, PubMed:8543054). ERG5 converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain (PubMed:8635732, PubMed:8543054). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672).
Present with 24700 molecules/cell in log phase SD medium.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. KIN82 subfamily.
Down-regulated by YKP1 phosphorylation. This effect is counteracted in the presence of mannosyl-inositolphosphorylceramide (MIPC).
Flippase activator that phosphorylates DNF1 and DNF2 and which is involved in the generation of phospholipid asymmetry in membranes by the inward translocation of phospholipids and in the retrieval pathway from early endosomes to the trans-Golgi network (TGN). Phosphorylates also the N-terminal half of YPK1. Involved in pheromone-response.
The N-terminal non-catalytic domain is phosphorylated by YPK1.
Belongs to the HAD-like hydrolase superfamily. DOG/GPP family.
Phosphatase that is active on 2-deoxy-D-glucose 6-phosphate (2-DOG-6P), but not very active on fructose-1-P.
Rescues temperature-sensitivity of MPT5 deletion. Partially suppresses the hydroxyurea (HU) sensitivity of MPT5 deletion.
Belongs to the WD repeat WDR3/UTP12 family.
Involved in nucleolar processing of pre-18S ribosomal RNA.
Present with 9620 molecules/cell in log phase SD medium.
Interacts with SDH1 within the SDH catalytic dimer.
Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit SDH1 of the SDH catalytic dimer. It is unclear whether it participates in the chemistry of FAD attachment (enzymatic function) or acts as a chaperone that maintains SDH1 in a conformation that is susceptible to autocatalytic FAD attachment (PubMed:19628817). Does not bind FAD or FADH(2) in vitro (PubMed:23062074). Involved in sporulation (PubMed:12432101). Required for the full activation of the early meiotic inducer IME1 (PubMed:12586695).
Respiratory deficient phenotype: viable on glucose medium, but is inviable on non-fermentable carbon sources such as glycerol. Cells lack SDH activity due to a complete loss of FAD cofactor attachment of SDH1.
Endocytosed alpha-factor accumulates in late endosomes.
Interacts with IVY1 (PubMed:12553664). Interacts with YIF1, YIP4 and YIP5 (PubMed:11943201). Interacts with the HOPS complex (PubMed:10944212, PubMed:19386605). Interacts with the class C-Vps complex (PubMed:11062257). Interacts with VPS35 (PubMed:22593205). Interacts with VPS39 (PubMed:25026035). Interacts with the GDP dissociation inhibitor GDI1 (PubMed:11118206, PubMed:11785952).
Rab activation is generally mediated by a guanine exchange factor (GEF), while inactivation through hydrolysis of bound GTP is catalyzed by a GTPase activating protein (GAP). YPT7 is activated by GEFs MON1-CCZ1 complex (MC1) and VAM6/VPS39, and inactivated by GAPs GYP7 and GYP1.
Ypt/Rab-type GTPases are key regulators of membrane trafficking and intracellular vesicular transport. They act as molecular switches that convert between GTP-bound and GDP-bound states, and regulate virtually all steps of membrane traffic from the formation of the transport vesicle at the donor membrane to its fusion at the target membrane. In the GDP-bound state, Ypt proteins are predominantly cytosolic, solubilized through the interaction with a GDP dissociation inhibitor (GDI). In the GTP-bound state, the proteins are membrane bound and interact with specific effector proteins that select cargo, promote vesicle movement, or verify the correct site of fusion (Probable). YPT7 is involved in regulation of vesicular protein transport in exo- and endocytosis (PubMed:8308065). Involved in homotypic vacuole fusion, the last step in the vacuole inheritance process, by interacting in its GTP-bound state on the donor membrane with the large multiprotein tethering complex termed HOPS on the acceptor membrane (PubMed:7489715, PubMed:11118206, PubMed:10725336, PubMed:10944212, PubMed:11210571, PubMed:19386605). Involved in the regulation of transport steps from late endosomes to the vacuole, mediated by interaction in its GTP-bound state on the donor membrane with the large multiprotein tethering complex termed class C-Vps complex on the acceptor membrane (PubMed:8308065, PubMed:11062257, PubMed:21062894). Involved in retromer assembly and cargo export, recognizing the cargo selection complex (CSC). GTP-bound YPT7 recruits CSC to vacuolar membranes via retromer subunit VPS35 (PubMed:22593205). Interacts with the HOPS complex subunit VPS39 independent of the HOPS complex at mitochondria-vacuole contact sites (vCLAMPs), providing a physical and metabolic interconnection between the endocytic pathway and mitochondria (PubMed:25026035).
Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complex SAGA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3, and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.
In TFIID, TAF9 heterodimerizes with TAF6, forming ultimately an octamer consisting of a TAF6/TAF9 heterotetramer core flanked by TAF4/TAF12 dimers on either side, similar to the histone H2A/H2B/H3/H4 octamer. The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14. Component of the 1.8 MDa SAGA complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9.
Activated by a E1 ligase composed of AOS1 and UBA2.
Belongs to the ubiquitin family. SUMO subfamily.
Not known; suppressor of MIF2 mutations.
May be involved in thiaminediphosphate transport across the mitochondrial membrane.
Belongs to the Mediator complex subunit 21 family.
Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. SRB7/MED21 interacts directly with MED4, MED6, MED7 and NUT2/MED10.
Present with 1391 molecules/cell in log phase SD medium.
Belongs to the pseudouridine synthase TruB family.
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs (PubMed:9358157). Also catalyzes pseudouridylation of mRNAs with the consensus sequence 5'-GGUUCRA-3' (PubMed:25219674).
Has a role in promoting intracellular calcium ion sequestration via the exchange of calcium ions for hydrogen ions across the vacuolar membrane. Involved also in manganese ion homeostasis via its uptake into the vacuole.
By osmotic, ionic and heat stress, and by water-deficiency.
Autoubiquitinated at Cys-89; undergoes 'Lys-48'-linked polyubiquitination, which leads to proteasome-dependent protein degradation. Degradation is autoregulated when its levels exceed that of its binding partner CUE1.
Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains, and of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). Involved in resistance to cadmium poisoning.
Forms a heterodimer with CUE1. Interacts with SSM4/DOA10 and HDR1. Interacts with UFD4.
This protein is required for high-affinity potassium transport.
Activates YPK1 by phosphorylating of a threonine residue.
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PDPK1 subfamily.
The PIF-pocket is a small lobe in the catalytic domain required by the enzyme for the binding to the hydrophobic motif of its substrates. It is an allosteric regulatory site that can accommodate small compounds acting as allosteric inhibitors.
Interacts with PCF11, RAI1, RAT1, RPO21 and RBP2.
Involved in transcription termination by RNA polymerase II and in regulation of Ty1 transposition.
Transporter required for vacuolar uptake of basic amino acids.
Leads to inefficient mitochondrial sequestration and degradation, as well as to defective reticulophagy and pexophagy (PubMed:29305265).
Regulatory component of the NEM1-SPO7 complex which acts as a phosphatase and dephosphorylates the phosphatidic acid phosphohydrolase PAH1 (PubMed:15889145). Essential for the formation of a spherical nucleus and meiotic division (PubMed:9822591). The NEM1-SPOo7 protein phosphatase is required for efficient mitophagy under prolonged respiration, as well as for reticulophagy and pexophagy (PubMed:29305265).
Present with 51100 molecules/cell in log phase SD medium.
Specifically expressed during sporulation.
Involved in regulation of actin cytoskeleton organization and endocytosis.
Present with 1551 molecules/cell in log phase SD medium.
In vitro, can complement a SDH1 disruption and leads to less than 15% of wild-type SDH reductase activity probably due to its lower expression level (compared to SDH1).
Probable minor catalytic subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Probably forms a catalytic dimer with SDH2. Electrons flow from succinate to the FAD bound to the catalytic subunit, and sequentially through the iron-sulfur clusters bound to SDH2 and enter the membrane dimer formed by SDH3 and SDH4.
Interacts according to large scale protein interaction studies with BZZ1, SRB4 and SUA7.
TY1 element enhancer binding protein. Binds to the DNA sequence 5'-TCGGTGGTATTATTCCGA-3'.
Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP (By similarity).
Expression is very low in the presence of fermentable carbon sources, but is induced, in contrast to PDC5, by ethanol.
Minor of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-keto-acids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids derived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate), valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate), isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins. The expression level of this protein in the presence of fermentable carbon sources is so low that it cannot compensate for the other two pyruvate decarboxylases to sustain fermentation.
Present with 1525 molecules/cell in log phase SD medium.
Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domains.
Interacts with TCB2 via its C-terminal domain.
May play a role in membrane trafficking.
The C-terminal C2 domain shows Ca(2+)-dependent phospholipid binding. It binds to phosphatidylserine, phosphatidylinositol and various phosphoinositides. The other C2 domains do not retain all 5 conserved Asp residues found in calcium-binding C2 domains.
Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Involved in phosphate regulation and polyphosphate accumulation. Required for resistance to salt stress, cell wall integrity, vacuole morphogenesis, and telomere maintenance.
Belongs to the cytidylyltransferase family.
Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis.
Belongs to the multicopper oxidase family.
Could be an iron transport multicopper oxidase, which is required for Fe(2+) high affinity uptake. May be required to oxidize Fe(2+) and release it from the transporter. Essential component of copper-dependent iron transport (By similarity). Involved in meiotic prophase and synaptonemal complex (SC) assembly.
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Tyr residues of target mitochondrial proteins (AMPylation) (PubMed:30270044). Involved in redox homeostasis by regulating the cellular response to oxidative stress (PubMed:30270044). Regulates protein S-glutathionylation levels possibly by AMPylation of deglutathionylation enzymes such as glutaredoxins (PubMed:30270044).
Forms probably one or more intrachain disulfide bridges.
Induced in absence of non-fermentable carbon sources including glycerol, lactate, and acetate (at protein level) (PubMed:30270044). Expression is regulated by zinc levels (PubMed:17938904).
Reduced growth and survival in presence of oxygen reactive species.
Interacts with TCB1 and TCB3 via its C-terminal domain.
The C2 domains show Ca(2+)-independent phospholipid binding. None of the C2 domains retains all 5 conserved Asp residues found in calcium-binding C2 domains.
Plays a role in regulating basal-level expression of CUP1. Activates EGT2 transcription in the absence of SWI5.
Belongs to the Mediator complex subunit 9 family.
Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. CSE2/MED9 interacts directly with MED4.
Catalyzes the attachment of leucine to tRNA(Leu) in the mitochondrion.
PubMed:3034607 authors identified this protein as the gene product of the NAM2 gene, which is capable of compensating for mutations in mRNA maturase encoded by the fourth intron of the mitochondrial cytochrome b gene.
Belongs to the GHMP kinase family. Homoserine kinase subfamily.
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate in the threonine biosynthesis pathway.
Present with 92600 molecules/cell in log phase SD medium.
Adenine nucleotide transporter involved in the uniport of ATP and adenine nucleotide hetero-exchange transport between the cytosol and the peroxisomal lumen. This transport is accompanied by a proton transport from the peroxisomal lumen to the cytosol. Transport of ATP into the peroxisome is required for beta-oxidation of medium-chain fatty acids. Required for growth on medium-chain fatty acids, pH gradient formation in peroxisomes and for normal peroxisome proliferation.
Induced by oleic acid, through its ORE-like (oleate responsive element) promoter element and the PIP2-OAF1 transcription factors.
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site (By similarity).
Forms a ternary complex with DMC1 and MEI5.
Belongs to the universal ribosomal protein uL30 family.
Identified in a Set3C complex with SET3, HST1, SNT1, SIF2, CPR1 and HOS4/YIL112W.
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). It is apparently involved in transcriptional activation.
Belongs to the ATPase delta chain family.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Present with 32400 molecules/cell in log phase SD medium.
Acts antagonistically to MID2 in signaling cell wall stress to the PKC1-MPK1 cell integrity pathway.
Phosphorylation of Ser-25 is induced 2-fold in response to mating pheromone.
Extensively modified; probably through addition of O-linked mannose residues.
Involved in a late stage of cell wall 1,6-beta-glucan synthesis and assembly. Has a structural, rather than enzymic, function within cell wall 1,6-beta-glucan assembly and architecture, possibly by being involved in covalently cross-linking 1,6-beta-glucans to other cell wall components such as 1,3-beta-glucan, chitin and certain mannoproteins. Acts as the plasma membrane receptor for the yeast K1 viral toxin.
By growth with glucose as a carbon source.
Mitochondrial IDP1 may regulate flux through the tricarboxylic acid cycle and respiration. Its probably critical function is the production of NADPH.
The enzyme is subject to end product inhibition by NADPH and 2-oxoglutarate.
Inhibitor of the cyclin-dependent kinase CDC28. Necessary for cell cycle arrest. Involved in pheromone response. Contributes to mating efficiency. Required for oriented polarization of yeast cells in response to mating pheromones.
Some mutants appear to be defective in mating because they are unable to locate the mating partner.
There is evidence to suggest that the N-terminal part may be sufficient for cell cycle arrest and the C-terminal may be necessary for some step in mating.
Thought to be phosphorylated by MAP kinase FUS3. Thought to enhance the binding of FAR1 to G1-specific cyclin-dependent kinase (CDK) complexes.
Component of the synapsis initiation complex (SIC) necessary for the synaptonemal complex assembly. Stabilizes the ZIP2 component to the chromosomes. The SIC complex loads onto chromosomes and nucleates ZIP1 polymerization, a molecular zipper that acts to bring homologous chromosomes in close apposition, which is required for meiotic crossover. May also be involved in double strand break repair.
Component of the synapsis initiation complex composed of at least ZIP2, ZIP3, MSH4 and MSH5. Interacts also with ZIP1, MRE11, RAD51 and RAD53.
Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
Catalyzes the reversible stereospecific interconversion of fumarate to L-malate (PubMed:3040736, PubMed:11585823, PubMed:1587456, PubMed:20231875). In mitochondrion, catalyzes the hydration of fumarate to L-malate in the tricarboxylic acid (TCA) cycle to facilitate a transition step in the production of energy in the form of NADH (PubMed:1587456, PubMed:20231875). In cytoplasm and nucleus, involved in DNA repair in response to DNA damage: following DNA double-strand breaks (DSBs), translocates from the cytosol to the nucleus and promotes DNA repair by catalyzing the dehydration of L-malate to fumarate (PubMed:20231875).
Cells accumulate extracellular fumarate.
Present with 6920 molecules/cell in log phase SD medium.
There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors.
With ARG81, ARG82 and MCM1, coordinates the expression of arginine anabolic and catabolic genes in response to arginine.
Belongs to the CWC complex (or CEF1-associated complex), a spliceosome subcomplex composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2.
CCL1 and KIN28 form the TFIIK complex, a component of the TFIIH holo complex. Component of a complex consisting of KIN28, CCL1 and TFB3. Interacts with TFB3. Also interacts with HNT1 and HOG1.
Catalytic component of the TFIIK complex (KIN28-CCL1 dimer) which is the protein kinase component of transcription factor IIH (TFIIH) and phosphorylates the C-terminal domain of RNA polymerase II during transition from transcription to elongation after preinitiation complex (PIC) formation, thereby positively regulating transcription. TFIIH (or factor B) is essential for both basal and activated transcription, and is involved in nucleotide excision repair (NER) of damaged DNA. TFIIH has DNA-dependent ATPase activity and is essential for polymerase II transcription in vitro. Essential for cell proliferation.
Phosphorylation of Thr-162 regulates the affinity of interaction between CCL1, KIN28 and TFB3. Thr-162 phosphorylation does not vary through the cell cycle and is necessary for full kinase activity.
Present with 4400 molecules/cell in log phase SD medium.
Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Dispensable for growth and sporulation on solid acetate and oleate media, but is essential for these processes to occur on petroselineate.
By oleate. Transcription is regulated by the transcription factors PIP2, OAF1 and ADR1. Weakly induced during sporulation in diploid cells.
Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (By similarity). Binds one iron-sulfur cluster per dimer. The iron-sulfur cluster is bound between subunits, and is complexed by a bound glutathione and a cysteine residue from each subunit (Probable).
Present with 7800 molecules/cell in log phase SD medium.
MSL5, MUD2 and PRP40 interact to form the commitment complex 2 (CC2), a precursor of mature spliceosomes.
Present with 4170 molecules/cell in log phase SD medium.
Splicing factor that contacts pre-mRNA directly and is a component of the pre-mRNA-U1 snRNP complex (commitment complex 2) that forms during early spliceosome assembly in yeast extracts.
Required for sporulation. Required for meiotic nuclear division.
Belongs to the eukaryotic/archaeal RNase P protein component 2 family.
TAF11 heterodimerizes with TAF13, but they do not seem to form a heterotetramer like TAF6/TAF9. The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors (one copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14), ranging in size from 17 to 150 kDa.
Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA.
Present with 8430 molecules/cell in log phase SD medium.
Required, directly or indirectly, for TATA-binding protein function at particular promoters. May promote a functional interaction between SPT3 and TATA-binding protein. Functions as a component of the transcription regulatory histone acetylation (HAT) complex SAGA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs).
The Pro-rich region of rgm1 attached to a heterologous DNA binding domain is able to repress the expression of the target gene.
Under the control of the inducible GAL10 promoter.
Up-regulates the transcription of the genes for ATP-binding cassette (ABC) transporters YOR1 and PDR15, for major facilitator superfamily transporter AZR1, for pleiotropic drug resistance SNG1, for alpha-glucosidase YJL216C and for YLL056C.
Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. Connects the central plaque of the SPB with the half-bridge. Required for proper localization of CDC5 at the SPB and for proper M-phase progression.
Homodimer. Interacts with KAR1, MPS2 and SPC29.
The C-ter coiled-coil domain is sufficient for localization and homodimerization.
Expression is induced in response to DNA replication stress.
Involved in bleomycin tolerance with links to DNA repair and/or proteasome function.
Leads to sensitivity to bleomycin (Ref.7). Bleomycin sensnsitivity is even increased when CUB1 deletion is combined with proteasome mutants including PRE9 or UMP1 disruptions (Ref.7). Suppresses the copper tolerance induced by the proteasome subunit PRE9 disuption (Ref.7). Leads to synthetic sickness with deletion of RAD6 on media containing bleomycin, but not hydroxyurea (HU) (Ref.7).
Belongs to the bacterial ribosomal protein bL35 family.
Belongs to the type II pantothenate kinase family.
Plays a role in the physiological regulation of the intracellular CoA concentration.
Regulated by feedback inhibition by malonyl-CoA.
Component of the HOPS complex which is composed of PEP5, VPS16, PEP3, VPS33, VPS39 and VPS41. HOPS associates with phosphoinositides and the PX domain of VAM7. Interacts with PEP5, PEP7 and VAM7.
Required for vacuolar biogenesis and for trafficking of hydrolase precursors to the vacuole. Mediates transport at the vacuolar membrane where it may be responsible for tethering transport vesicles on the target membranes. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion.
Belongs to the eukaryotic/archaeal RNase P protein component 1 family.
Required for 5.8S rRNA and tRNA processing; associated with RNase MRP and RNase P.
Required for the methylation of the wobble bases at position 34 in tRNA. Appears to have a role in stress-response.
Required for the retention of luminal endoplasmic reticulum proteins. Determines the specificity of the luminal ER protein retention system. Also required for normal vesicular traffic through the Golgi. This receptor strongly recognizes H-D-E-L and weakly recognizes D-D-E-L and K-D-E-L.
Heterodimer of MLH1 and PMS1, called MutLalpha, which is the major MMR MutL activity correcting base-base mismatches as well as IDLs. The heterodimer binds double strand DNA independently of a mismatch with positive cooperativity and has more than one DNA binding site. Forms a ternary complex with either the MSH2-MSH6 (MutSalpha) or the MSH2-MSH3 heterodimer (MutSbeta), which recognize and bind to mismatch DNA. Ternary complex formation is promoted by ATP binding.
Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of the MutLalpha heterodimer that forms a ternary complex with the MutS heterodimers, which initially recognize the DNA mismatches. This complex is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in maintaining the genetic stability of simple sequence repeats and in the repair of heteroduplex sites present in meiotic recombination intermediates.
Involved in transcriptional activation. Catalytic component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Belongs to the MICOS complex subunit Mic12 family.
Constituent of pre-60S ribosomal particles. Required for large subunit rRNA maturation, in particular processing of the 27S pre-rRNA at the A3 and B1 sites to yield 5.8S and 25S rRNA.
Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA and the nucleoplasmic transit of the pre-60S ribosomal subunits (PubMed:11313466, PubMed:14759368, PubMed:15528184, PubMed:26619264). Regulates pre-60S association of the critical remodeling factor MDN1 (PubMed:26619264).
Component of the RIX1 complex, composed of IPI1, RIX1/IPI2 and IPI3 in a 1:2:2 stoichiometry. The complex interacts (via RIX1) with MDN1 (via its hexameric AAA ATPase ring) and the pre-60S ribosome particles (PubMed:14690591, PubMed:14759368, PubMed:15260980, PubMed:15528184, PubMed:26619264). Interacts with NUG1 (PubMed:11583615). Interacts with IPI3 (PubMed:14690591).
Plays an important role in cell growth. Required to keep the uninucleated state. May be involved in the organization of the cytoskeleton which affects microtubule functions. Most likely RHO3 and RHO4 of S.cerevisiae regulate partially overlapping but different pathways.
Component of the heterotetrameric kinetochore subcomplex COMA, which consists of AME1, CTF19, MCM21 and OKP1 (PubMed:14633972). The COMA subcomplex is part of a larger constitutive centromere-associated network (CCAN) (also known as central kinetochore CTF19 complex in yeast), which is composed of at least AME1, CHL4, CNN1, CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1 (PubMed:12408861, PubMed:22561346). COMA binds the centromeric nucleosome-binding protein MIF2, and to the outer kinetochore MIND subcomplex, probably via AME1. AME1 interacts directly with OKP1 and an NKP1-NKP2 dimer (By similarity).
Present with 6580 molecules/cell in log phase SD medium.
Unknown; suppressor of the transcriptional defect of HPR1 by overexpression.
Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.
Mediates dephosphorylation of MAPK substrates such as SLT2, acquiring enhanced catalytic activity under oxidative conditions.
Autoacetylation at Lys-262 is required for proper function.
Catalytic component of the NuA4 histone acetyltransferase (HAT), a multiprotein complex involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z (PubMed:9520405, PubMed:12379856, PubMed:10082517, PubMed:10835360, PubMed:10911987, PubMed:12353039, PubMed:15045029, PubMed:15175650, PubMed:15494307, PubMed:15923609, PubMed:16543223, PubMed:18245364, PubMed:9858608). Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, histone H2B to form H2BK16ac, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac (PubMed:10082517, PubMed:10835360, PubMed:10911987, PubMed:12353039, PubMed:15045029, PubMed:15175650, PubMed:15494307, PubMed:15923609, PubMed:18245364, PubMed:9858608). Acetylation of histones gives a specific tag for epigenetic transcription initiation and elongation (PubMed:16543223, PubMed:19822662). Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination (PubMed:10082517, PubMed:10835360, PubMed:10911987, PubMed:12353039, PubMed:15045029, PubMed:15175650, PubMed:15494307, PubMed:15923609, PubMed:18245364, PubMed:9858608). Involved in cell cycle progression (PubMed:10082517, PubMed:10835360, PubMed:10911987, PubMed:12353039, PubMed:15045029, PubMed:15175650, PubMed:15494307, PubMed:15923609, PubMed:18245364, PubMed:9858608). Recruitment to promoters depends on H3K4me (PubMed:10082517, PubMed:10835360, PubMed:10911987, PubMed:12353039, PubMed:15045029, PubMed:15175650, PubMed:15494307, PubMed:15923609, PubMed:18245364, PubMed:9858608). Also acetylates non-histone proteins, such as ATG3 and PAH1 (PubMed:22539722, PubMed:29765047). Regulates autophagy by acetylating ATG3, controlling interaction the interaction between ATG3 and ATG8 and ATG8 lipidation (PubMed:22539722). Acts as a regulator of fatty-acid-induced triacylglycerol synthesis by catalyzing acetylation of PAH1, thereby promoting the synthesis of diacylglycerol (PubMed:29765047). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively (PubMed:31699900). Catalyzes histone crotonylation (PubMed:31699900).
Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, SWC4, TRA1, VID21, YAF9 and YNG2. The complex interacts with histones H4 (HHF1 and HHF2), H3 (HHT1 and HHT2) and H2A (HTA1 and HTA2).
The ESA1-RPD3 motif is common to ESA1 and RPD3 and is required for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone deacetylase (HDAC) activity.
The catalytic mechanisms is still under debate. Cys-304 was proposed to function as a nucleophile that forms a covalent intermediate with acetyl-CoA during the reaction (PubMed:12368900), and indeed the residue can be acetylated (in vitro) (PubMed:12368900 and PubMed:17223684). Depending on the assay system, mutation of Cys-304 leads to reduced or undetectable activity, indicating that is plays an important role. Still, mutation of Cys-304 has only a minor effect on the catalytic activity of the NuA4 histone acetyltransferase (HAT) complex (PubMed:17223684), making it unlikely that this residue functions as the catalytic nucleophile.
Promotes the exchange of Ras-bound GDP by GTP. This protein positively controls the level of cellular cAMP at start, the stage at which the yeast cell division cycle is triggered.
Ty1-GR2 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Component of the heterotetrameric kinetochore subcomplex COMA, which consists of AME1, CTF19, MCM21 and OKP1 (PubMed:14633972). The COMA subcomplex is part of a larger constitutive centromere-associated network (CCAN) (also known as central kinetochore CTF19 complex in yeast), which is composed of at least AME1, CHL4, CNN1, CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1 (PubMed:12408861, PubMed:22561346). COMA binds the centromeric nucleosome-binding protein MIF2, and to the outer kinetochore MIND subcomplex. OKP1 interacts directly with AME1, with an NKP1-NKP2 dimer, and with CTF19-MCM21 (PubMed:29046335).
Present with 2688 molecules/cell in log phase SD medium.
Component of the TOM (translocase of outer membrane) receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. TOM7 is involved in assembly and stability of the TOM complex.
Forms part of the preprotein translocase complex of the outer mitochondrial membrane (TOM complex) which consists of at least 7 different proteins (TOM5, TOM6, TOM7, TOM20, TOM22, TOM40 and TOM70).
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.
Homodimer. Oligomerizes to a tetramer in the presence of its substrates UTP and ATP.
Present with 57600 molecules/cell in log phase SD medium.
Belongs to the DASH complex ASK1 family.
Present with 2836 molecules/cell in log phase SD medium.
Interacts with BRO1, RFU1 and VPS32. Associates with the 26S proteasome.
Present with 428 molecules/cell in log phase SD medium.
RFU1 is an inhibitor of deubiquitination activity.
Residues 1-208 are essential for the localization to the late endosome and constitute a late endosome localization (LEL) domain.
Ubiquitin thioesterase that acts at the late endosome/prevacuolar compartment to recover ubiquitin from ubiquitinated membrane proteins en route to the vacuole. Removes also ubiquitin from soluble proteins targeted to proteasomes. Is essential to maintain a normal level of free ubiquitin. Involved in the ammonium-induced down-regulation of the GAP1 permease and the UME3 destruction in response to oxidative stress. Has a role in the RAD9 checkpoint response to TOP1 poisons. Required for promoting coordination of DNA replication and avoids DNA overreplication.
Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of at least PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. Interacts with YSH1/BRR5, FIP1 and RNA14.
Integral and essential component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. May bridge the CPF and CFIA complexes.
Present with 7810 molecules/cell in log phase SD medium.
Exclusively expressed between the end of mitosis and early G1; inactivated before cells pass start.
Seems to be involved in the correct timing of cell separation after cytokinesis, as separation of mutant daughter cells is delayed. Could either be an enzyme necessary for glucans-degradation of the cell wall at the neck region between mother and daughter cells or a regulatory protein controlling this metabolic step.
Interacts with RPP0 (PubMed:15286401). Interacts with APM2 (PubMed:26658609).
Probable lipase that recruits the AP-1-related (AP-1R) complex to membranes via interaction with APM2 (PubMed:26658609). The AP-1R complex is an adapter protein complex that mediates of cargo protein SNC1 sorting in clathrin-coated vesicles (PubMed:26658609).
Belongs to the eukaryotic ribosomal protein eL6 family.
Present with 37100 molecules/cell in log phase SD medium.
Probable RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase that regulates RNA polymerase II transcription. May have functional redundancy with RTR1.
Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.
Flavin-dependent enoate reductase that catalyzes the chemo- and stereoslective hydrogenation of electron-poor alkenes. The enzyme is reduced by NADPH, and oxygen, quinones, and alpha,beta-unsaturated aldehydes and ketones can act as electron acceptors to complete catalytic turnover. The physiological oxidant remains elusive (By similarity). Has an antioxidant activity, reducing reactive oxygen species (ROS) levels when overexpressed. Formation of OYE2-OYE3 heterodimers contribute to the induction of programmed cell death upon oxidative stress (PubMed:17897954).
Present with 15100 molecules/cell in log phase SD medium.
Mitochondrial and nuclear transcriptional activator required for respiratory growth.
Forms a one-to-one complex with ATPase to inhibit the enzyme activity completely.
Forms a NOT protein complex that comprises NOT1, NOT2, NOT3, NOT4 and NOT5. Subunit of the 1.0 MDa CCR4-NOT core complex that contains CCR4, CAF1, NOT1, NOT2, NOT3, NOT4, NOT5, CAF40 and CAF130. In the complex interacts with CCR4, POP2, NOT2, NOT4 and NOT5. The core complex probably is part of a less characterized 1.9 MDa CCR4-NOT complex.
Present with 4300 molecules/cell in log phase SD medium.
Belongs to the cyclophilin-type PPIase family. PPIase A subfamily.
Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.
Interacts with a complex composed of SIN3 and RPD3. Identified in the Set3C complex with HOS2, HST1, SNT1, SIF2, HOS4/YIL112W and SET3.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in histone deacetylase complexes, suggesting a function in chromatin. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degradation (Vid) vesicles. Regulates the meiotic gene program via the Set3C histone deacetylase complex to promote efficient sporulation, and the prolyl-isomerase activity is required for this function.
Present with 86000 molecules/cell in log phase SD medium.
Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events.
Component of a fungal signal recognition particle (SRP) complex that consists of a 7SL RNA molecule (scR1) and at least six protein subunits: SRP72, SRP68, SRP54, SEC65, SRP21 and SRP14 (PubMed:7925282). At least SRP14, SRP21, SRP68 and SRP72 are proposed to get assembled together with scR1 RNA as a pre-SRP complex in the nucleolus which is exported to the cytoplasm. SRP14 binds RNA as a homodimer (PubMed:7925282).
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:7925282, PubMed:10573124). The SRP complex is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences (PubMed:10573124). It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the arrest of nascent chain elongation during membrane targeting (PubMed:10573124). SRP14 binds scR1 RNA to form the probable Alu domain of SRP responsible for elongation arrest (PubMed:10573124).
Homodimer (By similarity). Interacts with FRA2.
Involved in the regulation of the iron regulon in responss to decreased mitochondrial iron-sulfur cluster synthesis.
Present with 3237 molecules/cell in log phase SD medium.
As part of the CRL3 E3 ubiquitin ligase complex; polyubiquitylates monoubiquitylated RNA polymerase II subunit RPO21 to trigger its proteolysis; plays a role in global genomic repair (PubMed:19920177). Prevents degradation of interacting proteins like PCL6 by the proteasome (PubMed:11864988).
Heterodimer with ELA1 (PubMed:10430890, PubMed:10753924, PubMed:10998253, PubMed:11545595, PubMed:23993092). Component of a CRL3 E3 ubiquitin ligase complex consisting of the cullin CUL3, the linker protein ELC1, the substrate receptor ELA1, and the RING protein HRT1 (PubMed:19920177). Interacts with CIN5 (PubMed:10760578). Interacts with PCL6 (PubMed:10760578). Interacts with SNF4 (PubMed:10760578). Interacts with the large RNA polymerase II subunit RPO21 in a manner dependent on DEF1 (PubMed:23993092). Interacts with DEF1 (PubMed:23993092). Interacts with RAD7 (PubMed:19920177). Interacts with RAD16 (PubMed:19920177).
In contrast to other members of the family it does not integrate a functional E3 ubiquitin complex.
Belongs to the ubiquitin-activating E1 family.
Heterodimer of UBA2 and AOS1. The complex binds SMT3.
The dimeric enzyme acts as a SMT3 E1 ligase. It mediates ATP-dependent activation of SMT3 and formation of a thioester with a conserved cysteine residue on AOS1.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
G-protein that, in its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be recycled before binding another molecule of aminoacyl-tRNA. Required for mitochondrial protein biosynthesis and maintenance of mitochondrial DNA.
Present with 58527 molecules/cell in log phase SD medium.
The precursor is processed in two steps involving mitochondrial intermediate peptidase (MIP) and mitochondrial processing peptidase (MPP).
Ap4A phosphorylase catalyzes the phosphorolytic degradation of bis(5'-adenosyl) tetraphosphate (Ap4A) into ADP and ATP. Can also use other Np4N' nucleotides (where N and N' stand for A,C,G or U) as substrates, but prefers A-containing substrates. Cannot catalyze the reverse reaction. Additionally, this enzyme can also catalyze the phosphorolytic degradation of adenosine 5'-phosphosulfate (AMPS) into ADP and sulfate, the reversible exchange reaction between inorganic phosphate and the beta-phosphate of a nucleoside diphosphate (NDP), and the synthesis of Ap4A from AMPS plus ATP.
Belongs to the ATP adenylyltransferase family.
Inactivation of both APA1 and APA2 promotes a great increase in the cellular concentration of bis(5'-nuceleosidyl) tetraphosphate nucleotides.
Multidrug resistance transporter involved in resistance and adaptation to quinidine and ketoconazole.
Belongs to the casein kinase 2 subunit beta family.
Regulatory subunit of casein kinase II/CK2 (By similarity). As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (By similarity).
Tetramer composed of an alpha subunit, an alpha' subunit, one beta subunit and one beta' subunit (PubMed:12242279). Interacts with FACT subunits POB3 and SPT16 (PubMed:12242279). interacts with YTA7 (PubMed:22156209).
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YNL054W-A ORF.
Has a role in the formation of the multivesicular body (MVB). Required for the sorting of lipids to form intralumenal vesicles and for fluid-phase transport to the vacuole. Required for sorting the plasma membrane proteins STE2 and STE3 into the MVB. Acts a cofactor of VSP4, promotes the oligomerization of VPS4 and stimulates its ATPase activity by 6- to 8-fold.
Homodimer (in cytoplasm). Interacts with VPS4; the interaction requires the dimeric structure of VTA1; 6 homodimers of VTA1 appear to associate with the dodecameric VSP4 complex; the interaction is ADP-dependent. Interacts with SNF7; the interaction requires DID2. Interacts with DID2. Interacts with VPS60; the interaction occurs at he endosomal membrane.
May be involved in the secretion of hexose transporters from the endoplasmic reticulum. Involved in secretion of GAL2 and HXT1.
Associated with nucleolar and cytoplasmic pre-60S particles (PubMed:12808088). At the end of biogenesis it dissociates from cytoplasmic pre-60S particles and is likely to be exchanged for its ribosomal homolog, RPL24 (PubMed:12808088, PubMed:23185031). Interacts (via C-terminus) with AFG2 (hexameric form); the interaction is direct, recruits AFG2 to pre-60S ribosomal particles and promotes AFG2 ATPase activity and RLP24 release from pre-60S ribosomal particles (PubMed:23185031). Interacts with NOG1; the interaction is direct (PubMed:12808088).
Involved in the biogenesis of the 60S ribosomal subunit (PubMed:12808088, PubMed:23185031). Ensures the docking of NOG1 to pre-60S ribosomal particles (PubMed:12808088). Activates and recruits ATPase AFG2 to cytoplasmic pre-60S ribosomal particles (PubMed:23185031).
Belongs to the WD repeat NOL10/ENP2 family.
May be involved in rRNA-processing and ribosome biosynthesis.
ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA. May also have a gene-specific regulatory function since it affects nuclear fusion by regulating KAR4 expression and contributes with KEM1 to ISP-1 sensitivity.
Belongs to the DEAD box helicase family. DDX52/ROK1 subfamily.
Interacts with the U3 snoRNA and is associated with the 90S and 40S pre-ribosomes. This association requires the presence of RRP5. Interacts also with OSH3.
Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity.
Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5; loaded onto DNA, forms a head-head double hexamer. Interacts with CSM1 and MCM10.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IID subfamily.
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of sodium or lithiums ions to allow salt tolerance.
Interacts with NOC2. Forms a nucleolar complex with NOC2 that binds to 90S and 66S pre-ribosomes.
Present with 15000 molecules/cell in log phase SD medium.
Belongs to the protein prenyltransferase subunit beta family.
Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X where X is Ser, Ala, Met, Cys, or Gln. Required for the membrane localization of proteins such as a-factor, Ras proteins and other membrane proteins containing the C-terminal CAAX motif (PubMed:3533274, PubMed:2124698, PubMed:1860864, PubMed:1763050, PubMed:8424764, PubMed:8527442, PubMed:17142567). The beta subunit is responsible for isoprenoid and peptide-binding (PubMed:7878044, PubMed:8995312, PubMed:9380709, PubMed:9545274, PubMed:12667062).
Heterodimer of an alpha (RAM2) and a beta (RAM1) subunit.
By acetate, acetaldehyde and ethanol. Subject to glucose catabolite repression. Inactivated and degraded after addition of glucose (at protein level).
Catalyzes the production of acetyl-CoA. Provides the acetyl-CoA source for histone acetylation in the nucleus. 'Aerobic' isozyme of acetyl-coenzyme A synthetase, which supports growth on nonfermentable carbon sources such as glycerol and ethanol. May be required for assimilation of ethanol and acetate.
It is uncertain whether Met-1 or Met-25 is the initiator.
Plays a role in mitochondrial biogenesis and protein folding.
Present with 7570 molecules/cell in log phase SD medium.
Belongs to the Cu-Zn superoxide dismutase family.
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Homodimer in holo form. In apo form, heterodimer with CCS1. Zinc-binding at 'His-16' of CCS1 and Glu-43 of apo-SOD1 is required for this heterodimerization.
Present with 519000 molecules/cell in log phase SD medium.
Associates with the pre-60S ribosomal particle (PubMed:16702403, PubMed:18658244, PubMed:19737519). Interacts (via WD repeats) with uL18 (RPL5) (PubMed:25404745). Interacts (via UBL domain) with MDN1 (via VWFA/MIDAS domain) (PubMed:19737519, PubMed:20542003). Interacts (via WD repeats) with NSA2 (PubMed:25404745).
Involved in ribosome biogenesis. Required for processing and efficient intra-nuclear transport of pre-60S ribosomal subunits. Interacts with the AAA-ATPase Midasin (MDN1/REA1), which is essential for the ATP-dependent dissociation of a group of nonribosomal factors from the pre-60S particle.
May be involved in protein sorting and cell wall formation.
Involved in sporulation and affects the sphingolipid composition of the plasma membrane.
Belongs to the universal ribosomal protein uL4 family.
Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). uL4 is associated with the polypeptide exit tunnel (PubMed:9559554, PubMed:22096102). uL4 interacts with its chaperone ACL4 and the nuclear import receptor KAP104 (PubMed:25936803).
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). uL4 participates in the regulation of the accumulation of its own mRNA (PubMed:2065661).
The eukaryote-specific C-terminal extension harbors a nuclear import signal and delivers the ACL4-uL4/RPL4 complex to the pre-ribosome, triggering uL4 release from ACL4 and incorporation into the 60S ribosomal subunit.
Belongs to the formin homology family. BNI1 subfamily.
Each FH2 dimer contains binding sites for 4 actin molecules.
Homodimer, and possibly also homotetramer. Interacts with PFY1 via the FH1 domain and with actin via the FH2 domain.
Required for the assembly of F-actin structures, such as actin cables and stress fibers. Nucleates actin filaments. Binds to the barbed end of the actin filament and acts as leaky capper, slowing both polymerization and depolymerization. Protects the growing actin fiber from tight capping proteins and so increases the time of elongation and the total amount of F-actin. May organize microtubules by mediating spindle positioning and movement in the budding process. Potential target of the RHO family members.
The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity).
Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of COQ3, COQ4, COQ6, COQ7 and COQ9 polypeptides.
GTP-binding protein involved in termination of M phase. May play a role in triggering the degradation of G2 cyclin to inactivate M-phase promoting factor at the termination of mitosis. Acts upstream of CDC15 kinase and may be required to activate the CDC15 protein kinase pathway.
Interacts with CDC15 and AMN1. AMN1 and CDC15 compete for association with TEM1.
Additional regions of lower homology to the repeat consensus (always starting with proline) are found in both flanking domains of the tandem repeats.
Controls nuclear migration. NUM1 specifically controls the interaction of the bud neck cytoskeleton with the pre-divisional G2 nucleus. Functions in dynein-anchoring. During late anaphase forms dynein-interacting cortical microtubule capture sites at both cellular poles. This leads to dynein-dependent sliding of the microtubules in the bud.
Interacts with PAC11 when DYN1 is present, and TUB3.
Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is required for transcription of ribosomal protein genes and genes involved in the integrity of the cell wall, and also for proper metaphase progression. Together with HTL1, LDB7, NPL6, RSC30 components, defines a fungal-specific module within the RSC complex that plays a role in many cellular functions including the maintenance of cell wall integrity.
Forms a heteromer with RSC30. Interacts with LDB7 and NPL6. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin. Component of a fungal-specific module (HTL1-LDB7-NPL6-RSC3-RSC30) within the RSC complex.
The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Major enzyme required for hyperosmotic shock-induced turnover of PtdIns(3,5)P2 and requires VAC14 for this function. In vivo, mediates turnover of PtdIns(3,5)P2 at the vacuole membrane necessary for vacuolar size control. In vitro, catalyzes the removal of phosphate from the fifth hydroxyl of the myo-inositol ring of phosphatidylinositol 3,5-bisphosphate.
Component of the spliceosome where it is associated with snRNP U1.
Involved in nuclear mRNA splicing. The principal role of the U1A is to help fold or maintain U1 RNA in an active configuration. It is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP.
Rnase which modulates cell survival under stress conditions. Released from the vacuole to the cytoplasm during stress to promote tRNA and rRNA cleavage and to activate separately a downstream pathway that promotes cell death. Involved in cell size, vacuolar morphology and growth at high temperatures and high salt concentration.
Up-regulated by heat shock and osmotic stress.
Present with 967 molecules/cell in log phase SD medium.
Involved in the biogenesis of rRNA. Required for the formation of 18S and 5.8S rRNA.
Present with 8860 molecules/cell in log phase SD medium.
Belongs to the U1 small nuclear ribonucleoprotein C family.
Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. YHC1/U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region.
U1 snRNP is composed of the 7 core Sm proteins SMB1, SMD1, SMD2, SMD3, SME1, SMX3 and SMX2 (Sm proteins B, D1, D2, D3, E, F and G, respectively) that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP, and at least 10 U1 snRNP-specific proteins SNP1/U1-70K, MUD1/U1-A, YHC1/U1-C, LUC7, NAM8, PRP39, PRP40, PRP42, SNU56 and SNU71. YHC1/U1-C interacts with U1 snRNA and the 5' splice-site region of the pre-mRNA.
Catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. Postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Decreases VPS13 levels at endosomal membranes and nuclear envelope-vacuole contact sites.
Interacts (via PxP motif) with VPS13 (via SHR-BD domain) (PubMed:30018089). Interacts with RBD2 (PubMed:15263065). Interacts with YIF1 (PubMed:15263065). Interacts with YIP1 (PubMed:15263065). Interacts with YIP4 (PubMed:15263065).
Recruits the lipid transfer protein VPS13 to endosomal and vacuolar membranes.
The PX domain binds phosphatidylinositol 3-phosphate (PtdIns(3)P) which is necessary for peripheral membrane localization.
Microtubule-associated force-producing protein that participates mitochondrial fission. Fission of mitochondria occurs in many cell types and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission. Functions antagonistically with FZO1.
The GTPase domain modulates a rate-limiting step in mitochondrial membrane fission.
Component of the origin recognition complex (ORC) composed of at least ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. Interacts with ORC6.
Associates with the MCM2-7 complex. Interacts with MCM2, ORC1, ORC2 and ORC6.
DNA replication licensing factor, required for pre-replication complex assembly. Faithful duplication of the genetic material requires 'once per cell cycle' DNA replication initiation and elongation. Central to this control is the tightly regulated formation of prereplicative complexes (preRCs) at future origins of DNA replication. Required for the recruitment of the MCM2-7 helicase complex to the replication origins.
Belongs to the methyltransferase TRM13 family.
tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His).
Involved in the regulation of anaerobiotic glycerol metabolism.
Present with 247000 molecules/cell in log phase SD medium.
Required for normal transcription at a number of loci in yeast. Affects transcription at Ty1 elements, at PHO5, STE6 and ADH2.
Plays an important role in nitrogen catabolite repression. Down-regulates the expression of many genes involved in nitrogen utilization by inhibiting the GATA transcriptional activators GLN3 and GAT1. Under good nitrogen conditions, binds to the phosphorylated forms of GLN3 and GAT1 and sequesters them in the cytoplasm, preventing transcription of genes expressed upon nitrogen limitation. Is also an atypical glutaredoxin without a catalytical cysteine residue. Has glutathione peroxidase and thiol:disulfide oxidoreductase activities in both native and fibrillar form. Also shows insulin disulfide reductase and dehydroascorbic acid reductase (DHAR) activities.
[URE3] is the prion form of URE2. [URE3] is the result of a conformational change of the cellular URE2 protein that becomes self-propagating and infectious. This conformational change generates a form of URE2 that assembles into amyloid fibrils. [URE3]-aggregates sequester soluble URE2, which then fails to retain GLN3 in the cytoplasm, resulting in GLN3 activation and consequently derepression of genes that are required for utilization of poor nirogen sources (PubMed:7909170). [URE3] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [URE3] propagation (PubMed:11073991).
Belongs to the HFCD (homooligomeric flavin containing Cys decarboxylase) superfamily.
Component of the phosphopantothenoylcysteine decarboxylase (PPCDC) involved in the coenzyme A synthesis. Acts as an inhibitory subunit of protein phosphatase PPZ1, which is involved in many cellular processes such as G1-S transition or salt tolerance. Also modulates the expression of the ENA1 ATPase.
Interacts with the C-terminal domain of PPZ1. Component of the phosphopantothenoylcysteine decarboxylase (PPCDC) complex, a heterotrimer composed of CAB3, SIS2 and VHS3.
Component of the SPT4-SPT5 complex. Interacts with RNA polymerase II. Interacts with SHE2.
It is phosphorylated in a PKA-dependent manner in vitro.
The C-terminal repeats are critical for activity.
The SPT4-SPT5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene.
An adapter protein that specifically links the 26S proteasome to its substrate CDC4 which is one of the substrate recognition subunits of the SCF E3 ubiquitin ligase complex. Required for turnover of cell cycle regulatory proteins CDC4 and GRR1. Required for synthesis and nuclear export of 60S ribosomal subunits. Required for vegetative growth.
Interacts with CDC4, PRE4, PRE6, RPT1 and SCL1 as part of the fully assembled 26S proteasome. Interacts with pre-ribosomal particles constituent NOP7.
Present with 45900 molecules/cell in log phase SD medium.
Belongs to the nucleoporin Nup133 family.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NUP133 is part of the heptameric 0.5 MDa autoassembling NUP84 NPC subcomplex (NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1).
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP133 is involved in nuclear poly(A)+ RNA, tRNA and pre-ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization.
Usually mRNA binding pumilio repeats come in 8 copies. In the 8-fold symmetry of the NPC the 8 repeats may be provided by eight copies of NUP133.
Component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs) (PubMed:9843512, PubMed:21131909). The protein component of the H/ACA snoRNP contains CBF5, GAR1, NHP2 and NOP10 (PubMed:9843512, PubMed:21131909). The complex contains a stable core composed of CBF5 and NOP10, to which GAR1 and NHP2 subsequently bind (PubMed:9843512).
Non-catalytic component of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP), which catalyzes pseudouridylation of rRNA and is required for ribosome biogenesis (PubMed:9843512). This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1 (PubMed:9843512). Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs (PubMed:9843512). The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs (PubMed:21131909). The H/ACA snoRNP complex mediates pseudouridylation at position 93 in U2 snRNA (PubMed:21131909). Essential for growth (PubMed:9843512).
Belongs to the NAD(P)-dependent epimerase/dehydratase family. Dihydroflavonol-4-reductase subfamily.
Belongs to the universal ribosomal protein uS7 family.
Positively regulated by signaling through MPK1 in response to cell wall perturbation. Expression is also regulated by the SWI5 transcription factor.
The PIR1/2/3 repeats are required for covalent linkage to the cell wall (By similarity). Their number varies among different strains of S.cerevisiae.
Belongs to the TAF9 family. CENP-S/MHF1 subfamily.
The MHF histone-fold complex is a heterotetramer of 2 MHF1-MHF2 heterodimers. Together with MPH1/FANCM, forms the FANCM-MHF complex. Component of the inner kinetochore constitutive centromere-associated network (CCAN) (also known as central kinetochore CTF19 complex in yeast), which is composed of at least AME1, CHL4, CNN1, CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1 (Probable).
dsDNA-binding component of a FANCM-MHF complex involved in DNA damage repair and genome maintenance (PubMed:20347428). FANCM-MHF promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork (By similarity). Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly (PubMed:22561346).
Present with 211 molecules/cell in log phase SD medium.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YOL103W-A ORF.
Belongs to the lariat debranching enzyme family.
Cleaves the 2'-5' phosphodiester linkage at the branch point of lariat intron pre-mRNAs after splicing and converts them into linear molecules that are subsequently degraded. It thereby facilitates ribonucleotide turnover. It also participates in Ty1 retrovirus-like transposition via an RNA lariat intermediate in cDNA synthesis.
Acts as a central regulator in the cell wall integrity signaling pathway, which is regulated by the cell cycle and in response to various types of cell wall stress. Integrates signals from different cell surface sensors, and activates a set of effectors, regulating processes including beta-glucan synthesis at the site of wall remodeling, gene expression related to cell wall biogenesis, organization of the actin cytoskeleton, and protein- and secretory vesicle-targeting to the growth site. Activates the protein kinase C (PKC1) MAP kinase cascade, the beta-1,3-glucan synthase (FKS1), the formin BNI1, the exocyst component SEC3 and the transcription factor SKN7.
Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by the guanine nucleotide-exchange factors (GEFs) ROM1, ROM2 and TUS1, and inactivated by GTPase-activating proteins (GAPs) BAG7, BEM2, LRG1, and SAC7, and the Rho GDP-dissociation inhibitor RDI1. The different GAPs regulate RHO1 in a target-specific manner.
Interacts with BEM4; the interaction is direct (PubMed:8754839, PubMed:8754840). Interacts with SEC3; the interaction is direct (PubMed:11283608). Interacts with the GAP BAG7 (PubMed:11591390, PubMed:12207708). Interacts with the GAP LRG1 (PubMed:11447600). Interacts with the GAP SAC7 (PubMed:11447600, PubMed:9038344). Interacts with the GAP RDI1 (PubMed:9242378). Interacts with the 1,3-beta-glucan synthase component FKS1 (PubMed:8602515). Interacts with the protein kinase PKC1 (PubMed:8621575, PubMed:8846785). Interacts with the G protein beta subunit STE4 (PubMed:12660244). Interacts with SKN7 (PubMed:9535835). Interacts with TUS1 (PubMed:11839800). Interacts with BNI1 (PubMed:8947028).
Catalyzes the first step in a degradation pathway of oxalate to CO(2) to protect the cell against the harmful effects of oxalate derived from endogenous processes or an environmental sources.
Decreases recovery from exposure to oxalate, to oxalate-secreting microbes, and to oxidative stress.
Present with 8770 molecules/cell in log phase SD medium.
Belongs to the iron-containing alcohol dehydrogenase family.
Induced by transcription factor ZAP1 in response to zinc deficiency.
Reduces acetaldehyde to ethanol during glucose fermentation. Specific for ethanol. Shows drastically reduced activity towards primary alcohols from 4 carbon atoms upward. Isomers of aliphatic alcohol, as well as secondary alcohols and glycerol are not used at all.
While ADH4 is expressed at only low levels in laboratory strains, it is often highly expressed in brewing strains.
Zinc. May bind iron when zinc levels are limiting.
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity).
In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9. Component of the ADA/GCN5 complex that consists of HFI1/ADA1, ADA2, ADA3, SPT20/ADA5 and GCN5 and is probably a subcomplex of SAGA. Component of the 0.8 MDa ADA complex, which at least consists of ADA2, ADA3, AHC1 and GCN5.
Transcription regulator. Could inhibit GAL4 DNA-binding or its ability to activate transcription. Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA, SLIK and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. ADA preferentially acetylates nucleosomal histones H3 (at 'Lys-14' and 'Lys-18') and H2B.
Belongs to the bacterial ribosomal protein bS18 family.
Leads to the appearance of giant lipid droplets and an excessive accumulation of non-polar lipids and phospholipids upon growth on medium containing oleic acid as a sole carbon source.
Serine hydrolase required for the maintenance of steady state level of non-polar and polar lipids of lipid droplets and thus plays a role in maintaining the lipids homeostasis (PubMed:21478434). Exhibits both esterase and triacylglycerol lipase activity (PubMed:21478434).
Interacts with the phosphatase PP2A-like catalytic subunits PPG1, PPH3 and SIT4. Forms a ternary complex with SIT4-TAP42.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for TAP42-associated PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex. Involved in the regulation of cell cycle progression, mitotic spindle formation, bud morphogenesis and DNA repair.
Sensitive to high hydrostatic pressure (mechanical stress); simultaneous disruption of SCH9 exacerbates the effect.
Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
Cells lacking this gene accumulate a 6-hydroxy-2,4,5-triaminopyrimidine derivative.
Belongs to the eukaryotic ribosomal protein eL22 family.
Present with 60400 molecules/cell in log phase SD medium.
Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
Involved in the activation of the plasma membrane proton-ATPase (PMA1) by glucose.
Dihydrosphingosine 1-phosphate phosphatase required for efficient ceramide synthesis from exogenous sphingoid bases (PubMed:10477278, PubMed:10563329, PubMed:10856228, PubMed:11278643, PubMed:11967828, PubMed:12493772, PubMed:12684378, PubMed:12786943, PubMed:9195906, PubMed:9353337, PubMed:9419344, PubMed:25345524). Involved in endocytosis and calcium-mediated signaling (PubMed:10856228, PubMed:11278643).
Binds to intron-containing transcripts and is involved in quality control for the export of spliced mRNAs from the nucleus (PubMed:14769921, PubMed:24452287). Binds to pre-mRNAs until splicing is completed or until faulty mRNAs are degraded. On correctly spliced mRNAs, GBP2 and HRB1 recruit MEX67 to allow nuclear export. On faulty mRNAs, GBP2 and HRB1 associate with the TRAMP complex that guides those pre-mRNAs to the exosome for degradation (PubMed:24452287). Binds single-stranded telomeric sequences of the type (TG[1-3])n in vitro (PubMed:7800479). Influences the localization of RAP1 in the nuclei (PubMed:7777547). Involved in modulating telomere length (PubMed:12519786).
RRM 1 and RRM 2 recognize preferentially RNAs containing the core motif GGUG. The atypical C-terminal RRM domain (RRM 3) does not interact with RNA/DNA, but is crucial for interaction with the THO/TREX complex.
Produced by +1 ribosomal frameshifting between codon Leu-431 and Gly-432 of the YCL020W ORF.
Catalyzes the NAD(+)-dependent cleavage of saccharopine to L-lysine and 2-oxoglutarate, the final step in the alpha-aminoadipate (AAA) pathway for lysine biosynthesis.
Induced by alpha-aminoadipate semialdehyde in a LYS14-dependent manner. Repressed by lysine.
Inhibited by p-chloromercuribenzoate and iodoacetate by modification of the active site cysteine residue. Inhibited by diethyl pyrocarbonate by modification of histidine residues. Inhibited by pyridoxal 5'-phosphate by modification of an essential lysine residue.
Present with 111934 molecules/cell in log phase SD medium.
PubMed:10077615 shows data confirming the peroxisomal localization of the protein, however this study was later retracted as the images were additionally used in other articles for other proteins.
May be involved in transcription regulation.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). uS4 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835).
Present with 63300 molecules/cell in log phase SD medium.
Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration.
Present with 23600 molecules/cell in log phase SD medium.
This permease has a broad specificity towards purines, and also transport cytosine and 5-methylcytosine but neither uracil nor thymine.
Required for vacuolar protein sorting; may be required for the consumption of transport vesicles containing vacuolar protein precursors. May bind a Rab GTPase such as VPS21.
The CUE domain (Coupling of ubiquitin conjugation to ER degradation) is monoubiquitin-binding and is required for intramolecular ubiquitination.
According to PubMed:9200603, it contains a transmembrane domain and may be responsible to anchor the complex into membranes, however, PubMed:12925762 showed that it is peripherically associated with membranes, and is probably not a transmembrane protein.
Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. This subunit may anchor the endonuclease complex to the nuclear membrane. Probably carries the active site for 5'-splice site cleavage.
Heterotetramer composed of SEN2, SEN15, SEN34 and SEN54. Interacts directly with SEN54.
Belongs to the heme-copper respiratory oxidase family.
Binds 2 heme A groups non-covalently per subunit.
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix (Probable). COX1 is a catalytic core subunit containing heme A and the active site BNC with heme A3 and the copper atom CU(B) (PubMed:30598554).
Magnesium and/or manganese. Specific for polynucleotide RNA in the presence of magnesium, but becomes specific for nucleotide triphosphates in the presence of manganese.
Probably involved in an RNA processing event other than mRNA capping. Releases gamma-phosphate from the 5'-end of RNA to produce a diphosphate terminus.
Belongs to the creA/MIG C2H2-type zinc-finger protein family.
Involved in glucose repression of the SUC2 gene.
ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Specifically involved in the ATP-dependent splicing of the bl1 intron of COB. Also required for efficient mitochondrial translation.
Lipid transport protein (LTP) involved in non-vesicular transfer of lipids between membranes. Functions in phosphoinositide-coupled directional transport of various lipids by carrying the lipid molecule in a hydrophobic pocket and transferring it between membranes through the cytosol. Involved in maintenance of intracellular sterol distribution and homeostasis. Plays a role in ergosterol synthesis (PubMed:15173322, PubMed:11238399, PubMed:16408938, PubMed:20008566). Binds and transports sterol (PubMed:20008566). May be involved in ergosterol transport from the plasma membrane (PM) to the ER (PubMed:16585271).
Component of the SPC105 complex composed of at least SPC105 and KRE28. The SPC105 complex interacts with the MIND and NDC80 complexes at the centromere.
Forms a kinetochore complex with SPC105 which is required for kinetochore binding by a discrete subset of kMAPs (BIM1, BIK1 and SLK19) and motors (CIN8, KAR3). Involved in kinetochore-microtubule binding and the spindle assembly checkpoint.
mRNA-binding protein which stimulates mRNA decapping by DCP1 and DCP2.
Ty1-BL is a highly expressed element. Induced under amino acid starvation conditions by GCN4.
Redundant with SPS2 for the organization of the beta-glucan layer of the spore wall.
E3 ubiquitin-protein ligase component of the GID complex (PubMed:12686616, PubMed:18508925). Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium (PubMed:9737955, PubMed:18508925). Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:9737955, PubMed:12686616, PubMed:18508925, PubMed:28126757).
Identified in the GID complex. In the absence of glucose, the complex contains VID30/GID1, the E3 ubiquitin-ligase RMD5/GID2, VID28/GID5, GID7, GID8, and FYV10/GID9. When cells are shifted to glucose-containing medium, VID24/GID4 is induced and becomes part of the complex (PubMed:22645139). Interacts with FYV10/GID9; the interaction is direct (PubMed:22044534). Within the GID complex, interacts directly with GID8, FYV10/GID9 and VID28/GID5 (PubMed:22645139).
Belongs to the NAD(P)-dependent epimerase/dehydratase family.
Highly induced under sulfur starvation conditions.
Belongs to the glycosyltransferase 22 family. PIGB subfamily.
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI during GPI precursor assembly.
Acts as a positive activator of the GCN2 protein kinase activity in response to in response to low amino acid, carbon, or purine availability (PubMed:7621831, PubMed:10733573). Component of the GCN1-GCN20 complex that forms a complex with GCN2 on translating ribosomes; during this process, GCN20 helps GCN1 to act as a chaperone to facilitate delivery of uncharged tRNAs that enter the A site of ribosomes to the tRNA-binding domain of GCN2, and hence stimulating GCN2 kinase activity (PubMed:7621831, PubMed:9234705, PubMed:10775272, PubMed:15722345). Participates in gene-specific mRNA translation activation, such as the transcriptional activator GCN4, by promoting the GCN2-mediated phosphorylation of eukaryotic translation initiation factor 2 (eIF-2-alpha/SUI2) on 'Ser-52', and hence allowing GCN4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:15722345).
Inhibits GCN4 derepression in amino acid or purine-starved cells (PubMed:10733573). Attenuates GCN4 derepression in glucose-starved cells (PubMed:10733573).
Interacts (via N-terminus) with GCN1 (via C-terminus); this interaction stimulates GCN2 kinase activity in response to amino acid starvation (PubMed:7621831, PubMed:9234705, PubMed:11101534, PubMed:15722345). The GCN1-GCN20 complex interacts with GCN2 on translating ribosomes in amino acid-starved cells; this association stimulates GCN2 kinase activation by uncharged tRNAs, and hence allowing GCN4 translational activation and derepression of amino acid biosynthetic genes (PubMed:7621831, PubMed:9234705, PubMed:10775272, PubMed:11101534). Associates with ribosomes (PubMed:7621831, PubMed:9234705, PubMed:15722345).
Present with 158000 molecules/cell in log phase SD medium.
Component of the U3 small nucleolar ribonucleoprotein. Required for the early cleavages at sites A0, A1 and A2 of the pre-ribosomal RNA. Participates in ribosome biogenesis.
Homodimer (PubMed:7812714, PubMed:9402066). Interacts (via PTS2-type peroxisomal targeting signal region) with PEX7; leading to its translocation into peroxisomes (PubMed:23812376).
Responsible for the thiolytic cleavage of straight chain 3-keto fatty acyl-CoAs (3-oxoacyl-CoAs).
The PTS2-type peroxisomal targeting signal, which mediates interaction with PEX7 and localization to peroxisomes, is cleaved following import into peroxisomes.
Heterodimers with GPN2 or GPN3 (PubMed:23324351, PubMed:23267056). Binds to RNA polymerase II (RNAPII) in a GTP-dependent manner (PubMed:20855544, PubMed:21844196). Interacts with nuclear pore protein NUP133 and nuclear export factor CRM1 (PubMed:21844196). Interacts with PCL1 (PubMed:15082539).
Phosphorylated by the cyclin-CDK PCL1-PHO85.
Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII) (PubMed:20855544, PubMed:21844196). May act at an RNAP assembly step prior to nuclear import (PubMed:23267056). Promotes sister chromatid separation during anaphase (PubMed:21532343).
Present with 49500 molecules/cell in log phase SD medium.
Impairs the efficient localization of TUS1 to the bud neck at late anaphase.
Regulator of RHO1 signaling that acts as a cofactor required for the efficient localization of the TUS1 GTP exchange factor (GEF) for RHO1 to the bud neck during all phases of cytokinesis (PubMed:22344253). RHO1 is a key, essential hub protein in the cell wall integrity (CWI) pathway in which activated RHO1-GTP binds directly to and activates multiple different downstream effectors required for cell wall synthesis and actin assembly during cytokinesis (Probable).
Present with 20400 molecules/cell in log phase SD medium.
Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:15769872, PubMed:18755837, PubMed:31309145, PubMed:25569479). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:29332244). Functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin) (PubMed:12424236). May also be involved in sensitivity to Pichia inositovora toxin (PubMed:13680368). ELP1/IKI3 binds to tRNA, mediating interaction of the elongator complex with tRNA (PubMed:24750273). Independently, may be involved in polarized exocytosis (PubMed:15780940).
Homodimer; dimerization promotes ELP1/IKI3 stability and elongator complex formation (PubMed:26261306). Component of the elongator complex which consists of ELP1/IKI3, ELP2, ELP3, ELP4, ELP5/IKI1 and ELP6 (PubMed:11435442, PubMed:11689709, PubMed:27974378, PubMed:27872205, PubMed:26261306). The elongator complex is composed of two copies of the Elp123 subcomplex (composed of ELP1/IKI3, ELP2 and ELP3) and two copies of the Elp456 subcomplex (composed of ELP4, ELP5/IKI1 and ELP6) (PubMed:27974378, PubMed:27872205, PubMed:25960406). The Elp123 subcomplex forms a two-lobed scaffold, which binds the Elp456 subcomplex asymmetrically (PubMed:27974378, PubMed:27872205). In the complex, ELP1/IKI3 interacts with ELP2 (PubMed:12139626). In each lobe, ELP2 is tightly sandwiched between ELP1/IKI3 and ELP3 (PubMed:31309145). The Elp123 subcomplex binds tRNA through ELP1/IKI3 and ELP3 and can bind 2 tRNAs simultaneously (PubMed:31309145). tRNA-binding induces conformational rearrangements which precisely position the targeted anticodon base in the active site (PubMed:31309145). The Elp456 subcomplex binds tRNA and has ATPase activity (PubMed:22343726). ELP1/IKI3 interacts with HRR25 and KTI12 (PubMed:25569479). Interacts with KTI11/DPH3 (PubMed:27694803).
Loss of mcm5U (5-methoxycarbonylmethyl uridine) and ncm5U (5-carbamoylmethyl uridine) from tRNA.
Phosphorylation promotes the tRNA modification function of the elongator complex.
Involved in microtubule organization by the microtubule organizing center, the spindle pole body (SPB). Probably part of the microtubule attachment site at the SPB.
Belongs to the RNase H2 subunit B family. Highly divergent.
Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.
The RNase 2 complex is a heterotrimer composed of the catalytic subunit RNH201 and of the non-catalytic subunits RNH202 and RNH203.
Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:15769872). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:29332244). It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin) (PubMed:11296232). May also be involved in sensitivity to Pichia inositovora toxin.
Component of the elongator complex, which consists of ELP1/IKI3, ELP2, ELP3, ELP4, ELP5/IKI1 and ELP6 (PubMed:11435442, PubMed:11390369, PubMed:11689709, PubMed:27974378, PubMed:27872205). The elongator complex is composed of two copies of the Elp123 subcomplex (composed of ELP1/IKI3, ELP2 and ELP3) and two copies of the Elp456 subcomplex (composed of ELP4, ELP5/IKI1 and ELP6) (PubMed:27974378, PubMed:27872205). The Elp123 subcomplex forms a two-lobed scaffold, which binds the Elp456 subcomplex asymmetrically (PubMed:27974378, PubMed:27872205). In each lobe, ELP2 is tightly sandwiched between ELP1/IKI3 and ELP3 (PubMed:31309145). The Elp123 subcomplex binds tRNA through ELP1/IKI3 and ELP3 and can bind 2 tRNAs simultaneously (PubMed:31309145). tRNA-binding by the Elp123 subcomplex induces conformational rearrangements which precisely position the targeted anticodon base in the active site (PubMed:31309145). The Elp456 subcomplex binds tRNA and has ATPase activity (PubMed:22556426, PubMed:22343726). Interacts with KTI11/DPH3 (PubMed:18627462).
Can regulate translation through binding to eIF4E. Competes with eIF4G and p20 for binding to eIF4E in vivo and inhibits cap-dependent translation in vitro. Plays a role in cell growth and is implicated in the TOR signaling cascade. Functions independently of eIF4E to maintain genetic stability and to attenuate GCN4 translation upon TOR inactivation.
Present with 3240 molecules/cell in log phase SD medium.
Heterodimer of YKU70/HDF1 and YKU80/HDF2. Interacts with SIR4.
Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.
By iron depletion. Expressed at a very low level.
Proton/glutathione antiporter that imports glutathione from the vacuole and exports it through the plasma membrane. Involved in resistance to oxidative stress and modulation of the PKA pathway.
N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.
Vacuolar class C ABC transporter which regulates the translocation of phosphatidylcholine to the vacuole lumen, the release of lumenal calcium stores, and acts as a negative regulator of vacuole fusion. Exhibits ATP-dependent bile acid transport.
Allantoin metabolism-specific malate synthase involved in the recycling the glyoxylate generated during allantoin degradation by the ureidoglycollate (UG) hydrolase reaction.
Diminishes the ureidoglycollate hydrolase activity by 3 to 4 fold.
Expression is insensitive to carbon catabolite repression, but highly sensitive to nitrogen catabolite repression (PubMed:8462696). Its expression is induced by allophanate or oxalurate (PubMed:3915539).
Involved in sphingolipid trafficking. May recycle sphingolipids between cellular membranous compartments.
Belongs to the BI1 family. LFG subfamily.
Links the unfolded protein response and programmed cell death and mediates mitochondrial-dependent apoptosis (PubMed:21673659, PubMed:21673967). Induces cell death and disruption of the mitochondrial transmembrane potential via the mitochondrial phosphate carrier MIR1 (PubMed:21673659). Dispensible for starvation-induced autophagy (PubMed:21926971).
No effect on autophagy during nitrogen starvation.
Component of the Golgi/endosome-localized DSC E3 ligase complex composed of at least TUL1, DSC2, DSC3, UBX3, CDC48 and GLD1.
Component of the Golgi/endosome-localized DSC E3 ubiquitin ligase complex involved in the targeting of the DSC complex to the Golgi apparatus and endosome membranes via the AP3 pathway to ubiquinate Golgi/endosome membrane proteins (PubMed:29355480). Competes with VLD1 to determine the subcellular localizations of the DSC complex (PubMed:29355480). May be required for cell cycle progression (PubMed:12829295).
Expression is regulated by the metabolic and meiotic transcriptional regulator UME6.
Homodimer that binds non-covalently to a protein complex in the inner mitochondrial membrane.
Involved in energy production. Its activity is stimulated by uncouplers of ATP synthesis.
Ty1-ML1 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Acts on phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol 1,4,5,-trisphosphate. STT4 functions in PKC1 protein kinase pathway.
Component of the mitochondrial outer membrane sorting assembly machinery (SAM or TOB) complex, which at least consists of SAM35, SAM37 and SAM50.
Essential component of the mitochondrial outer membrane sorting assembly machinery (SAM or TOB) complex, which is required for the sorting of proteins with complicated topology, such as beta-barrel proteins, to the mitochondrial outer membrane after import by the TOM complex.
Not known. Binds to the sorting sequence of cytochrome b2.
Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by a SNO isoform. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
Defects cause some sensibility to 6-azauracil, an inhibitor of purine and pyrimidine biosynthetic enzymes, and methylene blue, a producer of singlet oxygen. These effects are probably due to the inability to synthesize pyridoxal 5'-phosphate.
Homohexamer (PubMed:19523954). Interacts with AIM18 (PubMed:12271461).
Shows increased synthesis after entry into stationary phase.
Present with 74700 molecules/cell in log phase SD medium.
Belongs to the ureidoglycolate lyase family.
Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as secondary nitrogen source when primary sources are limiting.
Subject to nitrogen catabolite repression.
This enzyme was also named ureidoglycolate hydrolase in the literature. However, this is the recommended name of another enzyme (EC 3.5.1.116) acting on ureidoglycolate. To make the distinction between ammonia- or urea-releasing activities from ureidoglycolate, the use of this ambiguous name is deprecated.
Belongs to the protease inhibitor I34 family.
Specific and potent inhibitor for yeast aspartic protease A (yscA). The proteinase acts as a folding template stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity.
Involved in resistance to carboplatin and cisplatin. Is probably involved in a pathway contributing to genomic integrity.
Induced at low temperature and during anaerobic growth and completely repressed during aerobic growth. Induced at an early stage of fermentation and remains almost constant throughout the entire fermentation process.
Involved in recycling plasma membrane proteins internalized by endocytosis. Required for recycling of the v-SNARE SNC1.
Present with 2700 molecules/cell in log phase SD medium.
Belongs to the Nudix hydrolase family. DIPP subfamily.
May eliminate potentially toxic dinucleoside polyphosphates during sporulation. Most active against diadenosine 5',5'''-P1,P6-hexaphosphate (Ap6A). Can also hydrolyze diadenosine 5',5'''-P1,P5-pentaphosphate (Ap5A), adenosine 5'-pentaphosphate, and adenosine 5'-tetraphosphate are also substrates, but not diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) or other dinucleotides, mononucleotides, nucleotide sugars, or nucleotide alcohols. Also cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate).
Present with 3340 molecules/cell in log phase SD medium.
Belongs to the PPP phosphatase family. PP-Z subfamily.
Essential for the maintenance of cell size and integrity in response to osmotic stress.
Present with 189 molecules/cell in log phase SD medium.
Exhibits an absence of G1 checkpoint in response to linoleic acid hydroperoxide (LoaOOH) treatment. Rescues the temperature sensitivity of CDC13-1 mutant.
Required for replication of Brome mosaic virus (BMV).
Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio.
Acts as a chaperone for the L4 ribosomal subunit encoded by RPL4A and PRPL4B, required for hierarchical ribosome assembly. Shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.
Involved in pseudohyphal differentiation.
Belongs to the mitochondrion-specific ribosomal protein mS33 family.
In the N-terminal section; belongs to the heme-copper respiratory oxidase family.
Mitochondrial DNA endonuclease involved in intron homing. It introduces a specific double-strand break at the junction of the two exons a4-a5 of the COX1 gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Recognizes with limited specificity and cleaves the sequence 5'-TTTGGTCACCCTGAAGTA-3'. The protein may acquire mRNA maturase activity, like the closely related bI4, through a single amino acid substitution Glu-362 to Lys or when present together with a mutant form of the imported mitochondrial leucyl-tRNA synthetase NAM2.
Residues 299 to 556 are sufficient for endonuclease and intron homing activity.
The mature protein may arise from proteolytic cleavage of an in-frame translation of COX1 exons 1 to 4 plus intron 4, containing the aI4 open reading frame. Cleavage would take place close to the Met-299 resulting in an active endonuclease of about 30 kDa.
It requires NPR (nitrogen permease reactivator protein) for its full activity.
Required for high-affinity, high-specificity GABA transport. Also transports putrescine.
Catalyzes the incorporation of an ammonium ion into alpha-ketoglutarate to form L-glutamate, the major route of assimilation of ammonia into an organic form in yeast.
Present with 77500 molecules/cell in log phase SD medium.
Involved in proper sorting of the v-SNARE protein SNC1.
The PX domain binds to phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the punctate structures.
High-affinity low glucose sensor that is part of the sensor/receptor-repressor (SSR) glucose-signaling pathway, which detects extracellular glucose and induces expression of glucose transporters that bring glucose into the cell (PubMed:8901598, PubMed:9564039). The transporter-like sensor generates an intracellular signal in the presence of low levels of glucose to promote low glucose-induced expression of HXT2 (PubMed:9564039). Binding of glucose to the SNF3 transmembrane domain activates a downstream signaling cascade, leading to phosphorylation of the RGT1 corepressors MTH1 and STD1, targeting them for SCF(Grr1)-dependent ubiquitination and degradation. Depletion of the corepressors robs RGT1 of its ability to repress expression of HXT genes, leading to accumulation of glucose transporters in the plasma membrane (By similarity). SNF3 is involved as well in the transport of mannose and fructose (PubMed:20014043). Even though SNF3 is similar to glucose transporters, it appears to be unable to transport glucose (PubMed:9564039).
Phosphorylated in the C-terminal tail on Yck consensus sites in a yeast casein kinases YCK1 and YCK2 (Yck)-dependent manner. This phosphorylation is required for interaction with HXT corepressors MTH1 and STD1 and ultimately HXT expression.
The C-terminal cytoplasmic domain seems to be important for SNF3 regulatory function.
Belongs to the alpha-IPM synthase/homocitrate synthase family. Homocitrate synthase LYS20/LYS21 subfamily.
Catalyzes the aldol-type condensation of 2-oxoglutarate with acetyl-CoA to yield homocitrate. Carries out the first step of the alpha-aminoadipate (AAA) lysine biosynthesis pathway.
Present with 21900 molecules/cell in log phase SD medium.
Component of the Smc5-Smc6 complex which consists of KRE29, MMS21, NSE1, NSE3, NSE4, NSE5, SMC5 and SMC6. Interacts with NSE4. Interacts with NSE1.
Belongs to the helicase family. PIF1 subfamily.
Cell cycle-regulated. The nuclear isoform is present in very low amounts in G1 phase cells, but increases as cells progress through S phase, with a peak in late S/G2. The mitochondrial isoform follows a similar, but less pronounced induction pattern. The nuclear isoform is prone to APC/C-dependent degradation in G1, whereas the mitochondrial isoform is not.
DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Appears to move along DNA in single nucleotide or base pair steps, powered by hydrolysis of 1 molecule of ATP. Processes at an unwinding rate of about 75 bp/s. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Involved in the maintenance of ribosomal (rDNA). Required for efficient fork arrest at the replication fork barrier within rDNA. Involved in the maintenance of mitochondrial (mtDNA). Required to maintain mtDNA under conditions that introduce dsDNA breaks in mtDNA, either preventing or repairing dsDNA breaks. May inhibit replication progression to allow time for repair. May have a general role in chromosomal replication by affecting Okazaki fragment maturation. May have a role in conjunction with DNA2 helicase/nuclease in 5'-flap extension during Okazaki fragment processing.
Mg(2+). To a lesser extent, can also use Mn(2+).
Monomer in solution. DNA binding induces dimerization. Associates with mitochondrial and telomeric DNA. Binding to mtDNA is non-specific and the protein seems to coat the entire mtDNA molecule. Binds to the telomerase RNA TLC1. Interacts with the mitochondrial single-strand DNA-binding protein RIM1.
Phosphorylated. Undergoes RAD53-dependent phosphorylation in response to loss of mtDNA.
Produced by alternative initiation at Met-40 of isoform Mitochondrial.
Positive regulator of proteins involved in permeability. PDR1 and PDR3 jointly control the transcription level of both SNQ2 and PDR5.
the 9aaTAD motif (residues 1054 to 1062) is a transactivation domain present in a large number of yeast and animal transcription factors.
Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1).
Homodimer and heterodimer with PAM16/TIM16. Homodimerization may not be relevant in vivo, while heterodimerization is essential for activity regulation of mtHSP70. Component of the PAM complex, at least composed of mtHsp70, MGE1, TIM44, PAM16, PAM17 and PAM18/TIM14. Interacts directly with mtHsp70. Interacts directly with TIM17 subunit of the TIM23 complex.
The J domain is essential for co-chaperone activity and mediates the heterodimerization with the J-like domain of PAM16.
Catalyzes the covalent attachment of ubiquitin to other proteins. In association with the E3 enzyme BRE1 and LGE1, it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In association with the E3 enzyme RAD18, it catalyzes the monoubiquitination of POL30 'Lys-164', involved in postreplication repair of UV-damaged DNA. The RAD6/UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine. In association with the E3 enzyme UBR1, is involved in N-end rule-dependent protein degradation. Also involved in sporulation.
Forms a heterodimer complexes with the E3 enzymes BRE1, RAD18 and UBR1. Interacts also with UBR2, RTF1, PAF1 and the RNA polymerase II hyperphosphorylated form. The interaction with RNA polymerase II is BRE1- and PAF1-dependent.
The acidic-tail domain of UBC2 mediates interaction with UBR1 and UBR2, and thus is important for polyubiquitination of histones. This domain is also important for sporulation.
Up-regulated by UV radiations and during meiosis.
Forms homooligomers. Associates with ribosomal complexes.
Trans-acting factors of the ribosome biogenesis process.
Methylated by RKM1 at 2 different sites, but it is unclear which are the 2 methylated residues among Lys-40, Lys-106 and/or Lys-110.
Monomer. Part of the heterodimeric LMA1 complex together with the proteinase inhibitor PBI2. Most of the thioredoxin of yeast is in this complex rather than the well-studied monomer. LMA1 binds to the ATPase SEC18.
Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl-hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism.
Present with 8579 molecules/cell in log phase SD medium.
Reversible disulfide bond formation between Cys-30 and Cys-33, reverted by thioredoxin reductase TRR1 using NADPH as hydrogen donor.
Yeast has two cytoplasmic thioredoxins, TRX1 and TRX2, and one mitochondrial, TRX3.
Plays a specific role in mating-type regulation of yeast, by acting post-translationally to control the stability or activity of the SIR4 proteins.
Belongs to the eukaryotic ribosomal protein eS28 family.
Present with 94500 molecules/cell in log phase SD medium.
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Polyphosphatase (polyPase) involved in the degradation of inorganic polyphosphates (polyP) that is able to degrade a range of chains from three to several hundreds of residues in a highly processive manner.
Catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with adenine.
Displays only the t(6)A but not the ct(6)A modification in tRNAs. Unable to sustain respiratory growth under non-fermenting conditions.
ct(6)A is involved in promoting decoding efficiency. It is an unstable modification that can be easily hydrolyzed and converted to t(6)A during nucleoside preparation by conventional methods (PubMed:23242255).
Component of the global genome repair (GGR) complex which promotes global genome nucleotide excision repair (GG-NER) which removes DNA damage from nontranscribing DNA. Involved in differential repair of DNA after UV damage. Will repair preferentially the MAT-alpha locus compared with the HML-alpha locus.
Required for high-affinity proline transport. May be responsible for proline recognition and probably also for proline translocation across the plasma membrane. Also functions as non-specific GABA permease. Can also transport alanine and glycine.
Lipid raft-associated protein involved in the targeting of PMA1 from Golgi to the plasma membrane (Probable). May induce clustering of PMA1, which facilitates partition of PMA1 into lipid rafts after leaving the ER its and transport to the cell surface (By similarity).
May be involved in the degradation process of some misfolded endoplasmic reticulum (ER) luminal proteins. Its precise role is however unclear and its inability to complement der1 mutations, suggests either that it is not involved in degradation process of misfolded proteins, or that it participates in the destruction of specific misfolded ER luminal proteins.
Involved in respiratory growth and required for cell survival in the absence of prohibitins or GEM1.
Mg(2+) is required for catalysis and for stabilizing the dimer.
Present with 76700 molecules/cell in log phase SD medium.
Belongs to the apolipoprotein O/MICOS complex subunit Mic27 family. Yeast Mic26 subfamily.
Moderate changes in the mitochondrial morphology.
Present with 5220 molecules/cell in log phase SD medium.
First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.
Heterodimer (PubMed:6389537, PubMed:3029058). The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an mRNA 5'-triphosphate monophosphatase (PubMed:6389537, PubMed:3029058, PubMed:12788946).
Present with 3900 molecules/cell in log phase SD medium.
Belongs to the protein disulfide isomerase family.
Protein disulfide isomerase of ER lumen required for formation of disulfide bonds in secretory and cell-surface proteins and which unscrambles non-native disulfide bonds. Forms a complex with MNL1 to process unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2, promoting degradation in unfolded protein response.
The protein kinase domain is predicted to be catalytically inactive.
Required for the expression of the mitochondrial gene for cytochrome c oxidase subunit III (COX3).
Involved in modulation of rDNA transcription.
Catalyzes the reversible hydration of cis-homoaconitate to (2R,3S)-homoisocitrate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.
Component of the Golgi-associated retrograde protein (GARP) complex, also called VFT (VPS fifty-three) complex, composed of VPS51, VPS52, VPS53 and VPS54. Interacts also with YPT6, TLG1, RBL2, SEC10, SEC15, EXO84 and ARL1.
Involved in retrograde transport from early and late endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1 to the Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles. Seems also to be involved in protein transport from Golgi to the plasma membrane and is required for the integrity of the actin cytoskeleton.
RNA helicase component of the SKI complex involved in 3'-mRNA degradation pathway. Represses dsRNA virus propagation by specifically blocking translation of viral mRNAs, perhaps recognizing the absence of CAP or poly(A). Essential for cell growth only in the presence of M1 replicon.
Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Plays a role in the assembly of the exocyst.
The exocyst complex is composed of SEC3, SEC5, SEC6, SEC8, SEC10, SEC15, EXO70 and EXO84. Interacts with RHO3.
Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole. Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment oflate-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. The DID4/VPS2-VPS24 subcomplex is required for the VPS4-dependent dissociation of ESCRT-III.
Core component of the ESCRT-III complex (endosomal sorting required for transport complex III). ESCRT-III appears to be sequentially assembled as a flat lattice on the endosome membrane and forms a transient 450 kDa complex that contains DID4, oligomerized SNF7, VPS20 and VPS24. SNF7 oligomerization into a membrane-associated filament is nucleated by association of SNF7 with VPS20; the process is terminated through association of VPS24, possibly by capping the SNF7 filament. VPS24 subsequently associates with DID4/VPS2. Interacts with the VPS4. Interacts with DID2.
Component of the elongator complex which consists of ELP1/IKI3, ELP2, ELP3, ELP4, ELP5/IKI1 and ELP6 (PubMed:11435442, PubMed:11390369, PubMed:11689709, PubMed:27974378, PubMed:27872205). The elongator complex is composed of two copies of the Elp123 subcomplex (composed of ELP1/IKI3, ELP2 and ELP3) and two copies of the Elp456 subcomplex (composed of ELP4, ELP5/IKI1 and ELP6) (PubMed:27974378, PubMed:27872205). The Elp123 subcomplex forms a two-lobed scaffold, which binds the Elp456 subcomplex asymmetrically (PubMed:27974378, PubMed:27872205). In each lobe, ELP2 is tightly sandwiched between ELP1/IKI3 and ELP3 (PubMed:31309145). The Elp123 subcomplex binds tRNA through ELP1/IKI3 and ELP3 and can bind 2 tRNAs simultaneously (PubMed:31309145). tRNA-binding by the Elp123 subcomplex induces conformational rearrangements which precisely position the targeted anticodon base in the active site (PubMed:31309145). The Elp456 subcomplex binds tRNA and has ATPase activity (PubMed:22556426, PubMed:22343726).
Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:15769872, PubMed:18755837). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:29332244). It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin) (PubMed:11296232). May also be involved in sensitivity to Pichia inositovora toxin (PubMed:13680368).
Belongs to the anthranilate synthase component I family.
Belongs to the WD repeat MET30/SCONB/SCON-2 family.
Homomultimer (PubMed:14660673). Interacts with CDC53 and SKP1/CBF3D to form the E3 ubiquitin ligase complex SCF(Met30) (PubMed:14660673, PubMed:9499404, PubMed:9716410, PubMed:33443148). Interacts with MET4 (PubMed:10637232, PubMed:15883825, PubMed:8524217).
Substrate-recognition component of the SCF(Met30) complex, an E3 ubiquitin ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:9716410, PubMed:10637232, PubMed:14660673). Negatively regulates sulfur amino acids biosynthesis genes expression (PubMed:8524217, PubMed:15689486, PubMed:15870262). Controls cell cycle function (being required for the G1/S transition and M-phase but not the S-phase), sulfur metabolism, and methionine biosynthesis as part of the SCF(Met30) complex (PubMed:8524217, PubMed:15689486, PubMed:15870262). Required for the efficient binding of CDC45 and MCM proteins to origins of replication (PubMed:8524217, PubMed:15689486, PubMed:15870262). Required for efficient expression of G1 cyclins (PubMed:15870262). The SCF(Met30) complex catalyzes ubiquitination and degradation of the Cdk-inhibitory kinase SWE1 (PubMed:9716410). Involved in the S-adenosylmethionine (AdoMet)-mediated inhibition of the transcription function of MET4 (PubMed:8524217, PubMed:10637232). The SCF(Met30) complex mediates ubiquitination and subsequent degradation of MET4 and the cellular response to cadmium (PubMed:10637232). The SCF(Met30) complex acts as an inhibitor of autophagy by promoting ubiquitination and degradation of ATG9 in normal conditions (PubMed:33443148).
Transcriptional activation requires MET4 as well as MET31 and MET32. Regulated by intracellular AdoMet levels. L-methionine regulates the abundance of MET30. The amount of MET30 regulates the activity of the E3 ubiquitin ligase complex SCF(Met30).
Catalytic component of the inositol phosphorylceramide synthase which catalyzes the addition of a phosphorylinositol group onto ceramide to form inositol phosphorylceramide, an essential step in sphingolipid biosynthesis.
Component of the inositol phosphorylceramide synthase complex composed of at least AUR1 and KEI1.
Inhibited by aureobasidin A (AbA), khafrefungin and rustmicin.
Binds 2 Zn(2+) ions per subunit. The average amount of Zn(2+) bound at physiological metal concentrations will be lower than stoichiometric.
Homododecamer. The precursor form of aminopeptidase 1 (prApe1) assembles into dodecamers and further aggregates into higher multimers (the Ape1 complex) in the cytoplasm. The Ape1 complex is disaggregated in the vacuolar lumen, but mature aminopeptidase 1 (mApe1) retains its dodecameric form. Dodecamer assembly in the cytoplasm is essential for formation of an enzymatically active complex. If cytoplasmic homododecamerization of prApe1 is disturbed in mutants, homododecamers of mApe1 will form in the vacuole, but they are enzymatically inactive. Interacts with ATG19.
It is unsure whether this protein is glycosylated or not. PubMed:5147 has shown that a preparation of aminopeptidase 1 contains about 12% of conjugated carbohydrate, while PubMed:1400574 could not identify any glycosylation, which is in agreement with the fact that aminopeptidase 1 does not transit through the secretory pathway.
Resident vacuolar enzyme that catalyzes the removal of amino acids from the N-terminus of peptides and proteins. Also acts as the major cargo protein of the cytoplasm-to-vacuole targeting (Cvt) pathway. The precursor form of aminopeptidase 1 (prApe1) assembles into dodecamers and the propeptide mediates the aggregation of dodecamers into higher multimers. The multimers are then recognized via the propeptide by their receptor ATG19, and ATG19 further interacts with ATG11, which tethers the APE1-ATG19 complex to the pre-autophagosomal structure (PAS). The cargo-receptor complex (also Cvt complex) is selectively enwrapped by a double-membrane structure termed the Cvt vesicle under vegetative growth conditions and by a similar but larger double-membrane structure termed the autophagosome under nitrogen starvation conditions. The Cvt vesicle or the autophagosome fuses with the vacuolar membrane and release its content in the vacuolar lumen. In the vacuole, prApe1 is processed into mature aminopeptidase 1 (mApe1).
Strongly and specifically activated by Cl(-) and Br(-), which act as positive allosteric effectors. Inactivated by metal-chelating agents.
Synthesized in a precursor form (prApe1) that has an amino-terminal propeptide. The N-terminal extension of the 61 kDa precursor is proteolytically processed in two sequential steps. The first step involves proteinase A (PrA/PEP4) and produces a 55 kDa unstable intermediate (iAPI). The second step involves proteinase B (PrB/PRB1) and converts iAPI into the 50 kDa stable, mature enzyme (mApe1).
Belongs to the Mediator complex subunit 7 family.
Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. MED7 interacts directly with MED1, MED4 and SRB7/MED21.
Present with 7598 molecules/cell in log phase SD medium.
Present with 5920 molecules/cell in log phase SD medium.
Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
Transcriptional repressor involved in regulation of glucose repression. Binds to UAS-1 in the STA1 promoter.
Interacts with translation release factors eRF1 (SUP45) and eRF3 (SUP35) in vitro.
Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family.
Modulates the efficiency of translation termination, resulting in the readthrough of all three types of nonsense codons UAA, UAG and UGA.
Regulator of type 1 phosphatases which maintains protein phosphatase activity under strict control. Regulates the nuclear localization of type 1 phosphatase GLC7 and SDS22, and is involved in the regulation of mRNA 3'-end processing. May also regulate the activity of type 1 phosphatase PPZ1.
Was originally (PubMed:14506263) thought to be an inhibitor of type 1 phosphatases using in vitro experiments, but further in vivo experiments (PubMed:18172024) showed that it was rather an activator of these phosphatases.
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CHEK2 subfamily.
Controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints. Phosphorylates proteins on serine, threonine, and tyrosine. Prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. Seems to be involved in the phosphorylation of RPH1.
FHA domains are phosphothreonine recognition modules, FHA 1 strongly selects for Asp at position +3 relative to phosphothreonine, whereas FHA 2 selects for Ile in this position.
Interacts with EAP1 and MSL5 (via the GYP domain).
Belongs to the universal ribosomal protein uL18 family.
Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). uL18 forms a heterotrimeric complex with SYO1 and uL5 (RPL11A/RPL11B). Interaction of this complex with KAP104 allows the nuclear import of the heterotrimer (PubMed:23118189).
Abolishes localization of RTT106 to the HTA1-HTB1 promoter.
Component of the HIR complex, composed of HIR1, HIR2, HIR3 and HPC2 (PubMed:16264190, PubMed:16303565, PubMed:9001207). This complex may consist of one copy of HIR1 and HIR3 and two copies of HIR2 and HPC2 (PubMed:16264190). The HIR complex interacts with ASF1 (PubMed:11412995, PubMed:16303565). Interacts with SNF2 (PubMed:10445029). Interacts with SNF5 (PubMed:10445029). Interacts with SWI3 (PubMed:10445029). Interacts with RTT106 (PubMed:19683497).
Component of the HIR complex, which cooperates with ASF1 to promote replication-independent chromatin assembly. The HIR complex is also required for the periodic repression of three of the four histone gene loci during the cell cycle as well as for autogenous regulation of the HTA1-HTB1 locus by H2A and H2B. DNA-binding by the HIR complex may repress transcription by inhibiting nucleosome remodeling by the SWI/SNF complex. The HIR complex may also be required for transcriptional silencing of centromeric, telomeric and mating-type loci in the absence of CAF-1.
Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity (PubMed:11875065, PubMed:12684511). The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. GRX2 is more active as an oxidoreductase than GRX1 (PubMed:9571241, PubMed:18992757, PubMed:20417731). Responsible for the S-glutathionylation of DHBP synthase (PubMed:21565288).
In response to exposure to reactive oxygen species (ROS) and upon entry into stationary phase.
It is unclear whether the long polypeptide observed in mitochondria represents the immature form of the protein before cleavage of the transit peptide and release of the short form into the cytoplasm or whether two mature isoforms exists.
Present with 31400 molecules/cell in log phase SD medium.
Necessary for protein synthesis in mitochondria. Functions as a ribosome recycling factor in mitochondria.
Belongs to the mitochondrion-specific ribosomal protein mS46 family.
Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.
In eukaryotes this enzyme is synthesized by two pathway-specific (arginine and pyrimidine) under separate control.
Interacts with TMA22. Associates with ribosomal complexes.
Component of the SAS complex, a multiprotein complex that acetylates 'Lys-16' of histone H4 and 'Lys-14' of histone H3. The SAS complex is however unable to acetylate nucleosomal histones. The complex is involved in transcriptional silencing at telomeres and at HML locus. Also involved in rDNA silencing. In the complex, SAS4 is essential for histone acetyltransferase (HAT) activity of the complex.
Interacts with ASF1. Component of the SAS complex, at least composed of SAS2, SAS4 and SAS5. These three proteins constitute the core of the complex and are sufficient to acetylate histones.
Present with 800 molecules/cell in log phase SD medium.
Involved in selective mitochondria autophagy (mitophagy).
The N-terminus is dedicated to mating-type repression.
Together with SLM1, effector of the TORC2- and calcineurin-signaling pathways. Phosphorylated and activated by TORC2 under favorable growth conditions. Mediates actin polarization via inhibition of calcineurin-dependent transcription. Upon nutrient limitation or environmental stress, gets dephosphorylated by calcineurin, inhibiting interaction with TORC2, thereby antagonizing TORC2 signaling and mediating calcineurin-dependent actin depolarization. Also functions in heat-induced, calcineurin-mediated uracil permease (FUR4) endocytosis.
Interacts the PTS1-receptor docking protein PEX14 (PubMed:27678487). Interacts with malate synthases MLSL1 and MLS2 (PubMed:27678487). Interacts with TLG1 (PubMed:11283351).
Leads to a clear mislocalization of both MLS1 and MLS2 to the cytosol.
Peroxisomal import receptor that mediates the peroxisomal import of both malate synthases MLS1 and MLS2 in oleate-grown cells (PubMed:27678487, PubMed:27663510). Recognizes the C-terminal peroxisomal targeting signal PTS1 sequence SKL of MLS1 and MLS2, probably via its TPR domains (PubMed:27678487). Interacts with the PTS1-receptor docking protein PEX14 but not with peroxins PEX1, PEX3 through to PEX8, PEX10, PEX11, PEX12, PEX13, PEX15, PEX17, PEX18, PEX19 and PEX21 (PubMed:27678487).
The TPR repeats are involved in the interaction with the C-terminal peroxisomal targeting signal PTS1 of MLS1 and MLS2.
The WxxxF motif is involved in the interaction with the PTS1-receptor docking protein PEX14.
Belongs to the DPH1/DPH2 family. DPH1 subfamily.
Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (PubMed:15485916, PubMed:24422557, PubMed:27694803, PubMed:31463593, PubMed:34154323). In association with DPH2, transfers a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising KTI11/DPH3 and a NADH-dependent reductase, predominantly CBR1 (PubMed:15485916, PubMed:31463593, PubMed:34154323, PubMed:24422557, PubMed:27694803).
Component of the 2-(3-amino-3-carboxypropyl)histidine synthase complex composed of DPH1, DPH2, KTI11/DPH3 and a NADH-dependent reductase, predominantly CBR1 (PubMed:15485916, PubMed:18627462, PubMed:23645155, PubMed:24422557, PubMed:27694803, PubMed:31463593). Interacts with DPH2; the interaction is direct (PubMed:15485916, PubMed:23645155, PubMed:31463593). Interacts with KTI11/DPH3 (PubMed:12940988, PubMed:18627462, PubMed:23645155, PubMed:27694803).
Increases translational -1 frameshifting (PubMed:18627462). Abolishes the formation of the 2-(3-amino-3-carboxypropyl)histidine synthase complex (PubMed:18627462). Resistance to sordarin and zymocin (PubMed:18627462).
Present with 2526 molecules/cell in log phase SD medium.
Component of the oligosaccharyltransferase (OST) complex, which appears to exist in two assemblies comprising OST1, OST2, OST4, OST5, STT3, SWP1, WPB1, and either OST3 or OST6 (PubMed:8175708, PubMed:16297388, PubMed:16096345, PubMed:15886282, PubMed:9405463, PubMed:29301962). OST assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains OST1 and OST5, subcomplex 2 contains STT3, OST3, and OST4, and subcomplex 3 contains OST2, WBP1, and SWP1 (PubMed:29301962).
Belongs to the carnitine/choline acetyltransferase family.
By ethanol and by acetate. Repressed by glucose, and to a lesser extent, by galactose. Derepressed by glycerol.
Involved in the transfer of acetyl-CoA into mitochondria. May also be involved in the metabolism of acetate and of ethanol.
Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization.
Component of the PAN1 actin cytoskeleton-regulatory complex. Interacts with ABP1, KRE6, LAS17, LSB5, RSP5, RVS167, VPS1 and YSC84.
Dimer or multimer. Interacts with MRE11.
Endonuclease that cooperates with the MRX complex in processing meiotic and mitotic double-strand breaks by allowing the endonucleolytic removal of SPO11 from the break sites and ensuring both resection and intrachromosomal association of the broken ends. Required for proper recovery from checkpoint-mediated cell cycle arrest after DNA damage. MRX complex and SAE2 remove a small oligonucleotide(s) from the DNA ends to form an early intermediate which is rapidly processed by EXO1 and/or SGS1 to generate extensive tracts of single-stranded DNA that serve as substrate for RAD51. Plays a transitional role in the dissociation of MRE11 from, and the recruitment of RAD52 to, repair foci. Ensures that both ends of a DSB participate in a recombination event and impairs the formation of palindromic structures in the genome. With TEL1, promotes microhomology-mediated end joining (MMEJ) but inhibits non-homologous end joining (NHEJ), likely by regulating MRE11-dependent ssDNA accumulation at DNA break. SAE2 and MRX are particularly important for removal of hairpins, bulky adducts and other irregular end structures. Facilitates telomere length reequilibration and subsequent checkpoint switch off. Involved in homing efficiency of VMA1 intein VDE and in repair of transposon excision sites.
Phosphorylated forms accumulate periodically during the unperturbed cell cycle and in response to DNA damage in G2. Phosphorylated by MEC1 and TEL1. Mutagenesis experiments showed that several of the 5 residues located in canonical (S/T)Q motifs, which are favored for phosphorylation by ATM/ATR kinases (Ser-73, Thr-90, Ser-249, Thr-279 and Ser-289) may be phosphorylated. Phosphorylated at Ser-267 by CDC28 which is required to initiate meiotic DSB resection by allowing SPO11 removal from DSB ends.
Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and involved in the inositol cycle of calcium signaling.
Regulator of phospholipase D (SPO14) which is required for SPO14 catalytic activity in mitotic cells. Essential to buffer the toxic effects of C16:0 platelet activating factor.
Although strongly related to the PI3/PI4-kinase family, it lacks the typical motifs that constitute the catalytic site of PI3/PI4-kinase proteins, suggesting that it may lack such activity.
Belongs to the PI3/PI4-kinase family. TRA1 subfamily.
Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7,TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9. Also identified in the NuA4 complex with ESA1. Identified in the Ada.spt complex with ADA3 and SPT7.
Essential component of histone acetyltransferase (HAT) complexes, which serves as a target for activators during recruitment of HAT complexes. Essential for vegetative growth. Functions as a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.
The C-terminal domain (2233-2836) is essential for its ability to interact with activators.
Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability.
Belongs to the alkaline phosphatase family.
Phosphatase with broad substrate specificity. A truncated (soluble) version of the protein is responsible for the production of (E,E)-farnesol from (E,E)-farnesyl diphosphate. Acts as a fructose-2,6-bisphosphate 6-phosphatase (PubMed:1848184).
Involved in nucleotide excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents.
Protein phosphatase that shows typical type 2C protein phosphatase (PP2C) activity (PubMed:17002782). Catalyzes the dephosphorylation and concomitant reactivation of the E1 alpha subunit (PDA1) of the pyruvate dehydrogenase complex (PubMed:18180296). Required for efficient mitophagy in stationary phase cells (PubMed:17166847).
3,4-epoxy-l-butenyl diphosphate and 3-(fluoromethyl)-3-butenyl diphosphate (FIPP) act as specific active site-directed inhibitors of IP Pisomerase.
Belongs to the IPP isomerase type 1 family.
Isopentenyl-diphosphate delta-isomerase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (PubMed:2223785, PubMed:2681212, PubMed:7908830). IDI1 catalyzes the 1,3-allylic rearrangement of isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP) (PubMed:2223785, PubMed:2681212, PubMed:7908830). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD1/ERG19 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (PubMed:32679672).
Present with 25500 molecules/cell in log phase SD medium.
DNA-binding protein that induces severe bending of DNA. Required for DNA-binding by the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. Also augments the fidelity of transcription by RNA polymerase III independently of any role in the FACT complex. Required for transcriptional initiation fidelity of some but not all tRNA genes. Seems to be functionally redundant with NHP6B.
Weakly associates with the stable SPT16-POB3 heterodimer to form the FACT (yFACT or SNP) complex, which is associated with nucleosomes. Multiple molecules of NHP6 (NHP6A and/or NHP6B) are required to recruit the SPT16-POB3 heterodimer to DNA.
Catalytic component of the NEM1-SPO7 complex which acts as a phosphatase and dephosphorylates the phosphatidic acid phosphohydrolase PAH1 (PubMed:15889145). Essential for the formation of a spherical nucleus and meiotic division (PubMed:9822591). The NEM1-SPOo7 protein phosphatase is required for efficient mitophagy under prolonged respiration, as well as for reticulophagy and pexophagy (PubMed:29305265).
Interacts with the target of rapamycin complex 2 (TORC2) subunit TSC11 and the TORC2 effectors SLM1 and SLM2.
Belongs to the ATP-dependent DNA ligase family.
Cdc9 is included within the category of so-called 'start genes', encoding proteins which are required in early G1, when the cell is faced with the option of initiating a further cell cycle.
DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. The mitochondrial form is required for mitochondrial DNA maintenance but is non-essential while the nuclear form is essential for cell viability.
Produced by alternative initiation at Met-24 of isoform Mitochondrial.
Belongs to the CND3 (condensin subunit 3) family.
Component of the inner kinetochore constitutive centromere-associated network (CCAN) (also known as central kinetochore CTF19 complex in yeast), which is composed of at least AME1, CHL4, CNN1, CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1 (PubMed:14633972, PubMed:22561346). Interacts with outer kinetochore MIND complex subunit NNF1 (PubMed:14633972). Interacts with outer kinetochore Ndc80 complex subunits SPC24 and SPC25 (PubMed:22561346, PubMed:23334295).
Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly (PubMed:22561346). CNN1 is important for the recruitment of the outer kinetochore Ndc80 complex (PubMed:23334295).
Phosphorylation of the C-ter by MPS1 kinase regulates interaction with the outer kinetochore Ndc80 complex.
Belongs to the peptidase M16 family. UQCRC1/QCR1 subfamily.
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 10 subunits. The complex is composed of 3 respiratory subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10 (PubMed:10873857, PubMed:11880631, PubMed:18390544, PubMed:30598554). The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a monomer or a dimer of cytochrome c oxidase (complex IV, CIV), resulting in 2 different assemblies (supercomplexes III(2)IV and III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556, PubMed:30598554). COR1 interacts with COX5A at the CIII-CIV interface (PubMed:30598556, PubMed:30598554).
Component of a SNARE complex consisting of SED5, GOS1, YKT6 and SFT1.
Vesicle SNARE required for retrograde transport within the Golgi complex.
DIG1 and DIG2 are negative regulators of the filamentation and pheromone induced mating program. DIG1 and DIG2 inhibit the transcriptional activity of STE12 by direct protein-protein interaction. DIG1 colocalizes to promoters with STE12 and redistributes with it during induction of filamentation (by butanol) or mating (by pheromone) to program specific genes, but binding of DIG1 to STE12 is reduced by pheromone treatment.
Forms a complex with DIG2, STE12 and either FUS3 or KSS1. The interaction of FUS3 with STE12 depends on the presence of both DIG1 and DIG2. STE12 is lost from FUS3/DIG1/DIG2 complex after pheromone treatment. DIG1 and DIG2 have also been reported to interact with CLN1 and CLN2.
Phosphorylated by FUS3 and KSS1, in a pheromone-stimulated manner. Phosphorylation reduces the affinity for STE12.
Present with 5000 molecules/cell in log phase SD medium (5480 according to TAP-tag study).
Dual substrate-specific glycerol-3-phosphate/dihydroxyacetone phosphate sn-1 acyltransferase, catalyzing the first and committed reaction in the de novo synthesis of glycerophospholipids and triacylglycerols (TAGs). Can use both Gly-3-P and dihydroxyacetone phosphate with similar efficiencies and has a broad fatty acyl-CoA specificity profile. Transfers a fatty acid from fatty acyl-CoA to the sn-1 position of glycerol-3-phosphate to produce lysophosphatidic acid (LysoPA). These lipids not only are precursors of glycerolipids, but also are dynamic components of signal transduction systems that control cell physiology.
Phosphorylatied at a conserved motif involving Ser-664, Ser-668 and Ser-671. This phosphorylation plays a critical role for efficient TAG mobilization. Phosphorylation deficiency at this motif increases the enzyme activity and consequently induces de novo formation of phosphatidic acid.
Belongs to the eukaryotic/archaeal RNase P protein component 4 family.
Component of nuclear RNase P. RNase P consists of an RNA moiety and at least 9 protein subunits including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RPP1 and RPR2, many of which are shared with the RNase MPR complex.
Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Translational activator of cytochrome b. The cytochrome b (coB) leader RNA may represent the target sequence for CBS1 and/ or CBS2.
Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen.
Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole. Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Required for the oligomerization of SNF7 into a membrane-associated filament. The VPS20-SNF7 subcomplex is responsible for the membrane association of the ESCRT-III complex. Also required for the RIM101 repressor proteolytic activation.
Core component of the ESCRT-III complex (endosomal sorting required for transport complex III). ESCRT-III appears to be sequentially assembled as a flat lattice on the endosome membrane and forms a transient 450 kDa complex that contains DID4, oligomerized SNF7, VPS20 and VPS24. SNF7 oligomerization into a membrane-associated filament is nucleated by association of SNF7 with VPS20; the process is terminated through association of VPS24, possibly by capping the SNF7 filament. VPS24 subsequently associates with DID4/VPS2. Interacts with the VPS4. Interacts with VPS25; the interaction mediates the association with the ESCRT-II complex.
Binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NUP49 is part of the NUP57 subcomplex (NIC96, NSP1, NUP49, NUP57) interacting with NUP57. Interacts through its FG repeats with karyopherins.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP49 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, and pre-ribosome transport.
Required for normal growth in the presence of linoleic acid hydroperoxide (LoaOOH).
Cells fail to arrest in G1, cells remain budded and a significant fraction has a G2 DNA content. In such conditions, deletion mutants have a disorganized actin cytoskeleton and actin accumulates in one or two intensely staining clumps per cell. Deletion mutants also show defects in ion homeostasis and cell integrity. They fail to grow on medium containing 1.0 M NaCl, 5 mM caffeine or when incubated at 37 degrees Celsius. The caffeine and temperature sensitivity are rescued by supplementing the growth medium with 1.0 M sorbitol.
Involved in the Ran-GTPase system for nuclear protein import and poly(A)+ mRNA export.
Belongs to the eukaryotic ribosomal protein eS17 family.
Present with 30900 molecules/cell in log phase SD medium.
Leads to hypersensitivity to arsenic (PubMed:9234670). Impairs the arsenic-dependent induction of arsenate reductase ARR2, arsenite transporter ARR3 and vacuolar transporter YCF1 (PubMed:11527213, PubMed:15147884).
Phosphorylation by HOG1 promotes nuclear localization in the presence of arsenic.
Transcription activator required for resistance to arsenic compounds and for a regulated expression of ACR2, ACR3 and YCF1.
Transcriptional activity is controled by regulated degradation by the ubiquitin-proteasome pathway in absence of arsenic (PubMed:17200139). Arsenic-exposure results in stabilization and increased transcriptional activity (PubMed:15147884, PubMed:17200139).
ATP-NADH kinase with a low phosphorylation activity of both NADH and NAD(+) to produce NADP and NADPH by using ATP. UTR1 is responsible for essentially all of the NAD/NADH kinase activity resident in the cytoplasm, whereas POS5 is responsible for all mitochondrial NAD/NADH kinase activity and consequent mitochondrial genome maintenance. YEF1 can substitute for UTR1 when overexpressed.
Belongs to the Nudix hydrolase family. NudF subfamily.
Binds 3 Mg(2+) ions per subunit. Can also accept Mn(2+) ions.
By amino acid starvation. It has a GCN4-dependent and a GCN4-independent (basal) expression.
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The glutaminase domain produces the ammonia necessary for the cyclase domain to produce IGP and AICAR from PRFAR. The ammonia is channeled to the active site of the cyclase domain.
In the C-terminal section; belongs to the HisA/HisF family.
Present with 11800 molecules/cell in log phase SD medium.
Acts as a receptor for reticulophagy and nucleophagy. Directs autophagic sequestration of double-membrane vesicles derived from the nuclear envelope and perinuclear endoplasmic reticulum (pnER) into autophagosomes. Is not required for the cytoplasm-to-vacuole targeting pathway, mitophagy, pexophagy, and non-selective autophagy.
Expression is increased by rapamycin, which mimics nitrogen starvation by inactivating the TORC1 complex.
Partially blocks reticulophagy, and the double ATG39/ATG40 knockout almost completely blocks this pathway. Leads to abnormal morphology in the nucleus/pnER, when exposed to prolonged nitrogen starvation.
Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, which is a biosynthetic precursor of chitin and also supplies the amino sugars for N-linked oligosaccharides of glycoproteins (PubMed:8174553). Also has phosphoglucomutase activity (PubMed:8119301).
Present with 14700 molecules/cell in log phase SD medium.
Results in undivided strings of cells and growth arrest after approximately 5 division cycles.
Glucose-induced phosphorylation regulates the DNA-binding activity. Hyperphosphorylation in cells growing on high levels of glucose does prevents DNA-binding and dephosphorylation restores DNA-binding ability.
Glucose-responsive transcription factor that regulates expression of several glucose transporter (HXT) genes in response to glucose. In the absence of glucose, it functions as a transcriptional repressor, whereas high concentrations of glucose cause it to function as a transcriptional activator. In cells growing on low levels of glucose, has a neutral role, neither repressing nor activating transcription. Binds the consensus binding site sequence 5'-CGGANNA-3', of which multiple copies are present in all HXT promoters regulated by RGT1.
Cell wall protein that plays a role in adaptation and resistance to cell wall stress.
Induced by transcription factors MSN2 and MSN4 in stationary phase and by transcription factors MSN2, MSN4 and HAA1 upon weak-acid stress. Up-regulated by low pH.
By allophanate or its non-metabolized analog oxalurate. Repressed in the presence of readily used nitrogen sources.
Hydrolysis of urea to ammonia and CO(2).
Belongs to the auxin efflux carrier (TC 2.A.69) family.
Both IUM domains are necessary for efficient binding to ubiquitin.
Component of the ESCRT-0 complex composed of HSE1 and VPS27 (PubMed:12055639, PubMed:14581452, PubMed:15086794). Interacts with ENT3 and ENT5, the ESCRT-I subunits VPS23 and VPS28 and with the COPIb subunits SEC27, SEC28 and SEC33 (PubMed:12900393, PubMed:15107463, PubMed:17101773). May form a complex composed of VPS27, HSE1 and DOA1 (PubMed:18508771). Interacts with DOA1 (PubMed:18508771). Interacts with ubiquitin (PubMed:11988742, PubMed:12750381, PubMed:14581452).
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane (PubMed:3062374, PubMed:1493335, PubMed:9265642, PubMed:11416128, PubMed:12055639, PubMed:11872141, PubMed:12900393, PubMed:14581452, PubMed:15166140, PubMed:15107463, PubMed:15086794, PubMed:17135292, PubMed:18508771). Controls exit from the prevacuolar compartment (PVC) in both the forward direction to the vacuole and the return to the Golgi (PubMed:11208109, PubMed:8649377, PubMed:9015300). Allows VPS10 to return to the (trans-Golgi network) TGN from the PVC (PubMed:8649377). Might also function as an alternate adapter in the COPIb clathrin-like coat (PubMed:17101773).
The FYVE domain is involved in the binding to phosphatidylinositol 3-phosphate (PtdIns(3)P) which is required for the association to endosomal membranes.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.
Forms a stable complex with CAR1 in the presence of ornithine and arginine. In this complex CAR1 retains activity, but ARG3 activity is inhibited.
Interacts with RRT2. Interacts with TRM7; for 2'-O-methylation of position 34 in substrate tRNAs.
Involved in regulation of Ty1 transposition. Also plays a role in the regulation of the retromer complex and is required for the recycling from endosomes of plasma membrane proteins like CAN1 and MUP1. Required together with TRM7 for the methylation of the 2'-O-ribose of nucleotides at position 34 of the tRNA anticodon loop of tRNA(Phe) and tRNA(Leu(UAA)).
Present with 3450 molecules/cell in log phase SD medium.
Component of the NC2 (negative cofactor 2) complex composed of BUR6 and NCB2. The NC2 complex associates with SPT15/TBP. Interacts with SPT15/TBP.
Component of the NC2 complex which represses RNA polymerase II transcription through binding to SPT15/TBP and thereby inhibiting the assembly of the preinitiation complex. The NC2 complex may also mediate transcriptional activation from TATA-driven promoters through association with SPT15/TBP.
Activates the CHA1 gene for L-serine dehydratase. Binds to the DNA sequence 5'-GVGGARAYRTRATTCCRC-3'.
Component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair.
Insertion mutation in SMT4 confers temperature and benomyl sensitivity; high copy suppressor of a temperature sensitive mutation in MIF2.
Component of the SEA complex composed of at least IML1/SEA1, RTC1/SEA2, MTC5/SEA3, NPR2, NPR3, SEA4, SEC13 and SEH1. Interacts with ribosomes.
Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis. May be involved in a process influencing telomere capping.
Iron transport multicopper oxidase, which is required for Fe(2+) high affinity uptake. May be required to oxidize Fe(2+) and release it from the transporter. Essential component of copper-dependent iron transport.
Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription.
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Monoubiquitinated by the RAD6/UBC2-BRE1 complex to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and H3K79me formation. H2BK123ub1 also modulates the formation of double-strand breaks during meiosis and is a prerequisite for DNA-damage checkpoint activation. Deubiquitination is performed by UBP8 in presence of SGF11.
Phosphorylated by STE20 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation. H2BS10ph is also formed after H(2)O(2) treatment, and is a step leading to apoptosis.
Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su or H2BK17su, occurs preferentially near the telomeres and represses gene transcription.
To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H2BK6ac = acetylated Lys-7; H2BK6su = sumoylated Lys-7; H2BK7ac = acetylated Lys-8; H2BK7su = sumoylated Lys-8; H2BS10ph = phosphorylated Ser-11; H2BK11ac = acetylated Lys-12; H2BK16ac = acetylated Lys-17; H2BK16su = sumoylated Lys-17; H2BK17su = sumoylated Lys-18; H2BK123ub1 = monoubiquitinated Lys-124.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (PubMed:25609543, PubMed:28154081). uS3m is essential for mitochondrial protein synthesis and required for the maturation of small ribosomal subunits (PubMed:7770043).
Activated by calcium (PubMed:22320399). Activated by protein kinase A (PKA)-mediated phosphorylation (PubMed:22320399).
Hydrolyzes intracellular trehalose to glucose (PubMed:22320399, PubMed:29087344) (Probable). The disaccharide trehalose serves as a storage carbohydrate that is mobilized during nutrient stress (Probable). Regulates the level of trehalose as a protectant for cell integrity during heat stress (PubMed:7883049, PubMed:7730323).
Increases cellular trehalase level during thermal stress (PubMed:7730323). Increases sensitivity to heat shock (PubMed:7730323, PubMed:7883049). Decreases growth on the non-fermentable carbon source glycerol; simultaneous knockout of ATH1 exacerbates the effect (PubMed:7883049).
Induced during thermal stress (at protein level) (PubMed:7883049, PubMed:9276477). Induced by oxidative stress (hydrogen peroxide, sodium arsenite) (at protein level) (PubMed:9276477). Induced by copper stress (at protein level) (PubMed:9276477). Induced by protein synthesis inhibitor (cycloheximide) (PubMed:9276477).
Monomer (PubMed:22320399, PubMed:29087344). Interacts with BMH1 dimers; the interaction is direct and activates NTH1 (PubMed:29087344, PubMed:22320399). Interacts with BMH2 (PubMed:22320399).
Phosphorylated by protein kinase A (PKA); phosphorylation at Ser-60 and Ser-83 is required for activation by the 14-3-3 proteins BMH1 and BMH2.
Present with 1840 molecules/cell in log phase SD medium.
Heterodimer of YKU70/HDF1 and YKU80/HDF2.
Belongs to the universal ribosomal protein uS10 family.
Homodimer via the leucine-zipper domain. Forms a complex with a GCR1 homodimer.
Transcriptional activator required for the expression of glycolytic genes. Enhances the CT box-dependent transcriptional activation of a RAP1-GCR1 complex. Required for GCR1 phosphorylation.
Involved in resistance to ionizing radiation.
Present with 2290 molecules/cell in log phase SD medium.
Proton-conducting pore forming of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:9030535). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:9030535).
Increases cellular chitin level (PubMed:17142567). Increases chitin chain length (PubMed:17142567).
Present with 11000 wall-bound molecules/cell in log phase YPD medium.
Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall biosynthesis and morphogenesis.
Present with 780 molecules/cell in log phase SD medium.
Probable serine/threonine protein kinase involved in the G1-S transition.
Interacts with DRS2. Might function as an essential subunit for this protein.
Belongs to the eukaryotic/archaeal RNase P protein component 3 family.
Exhibits lumenal vesicles within vacuoles suggestive of vacuole fusion/fission defects. Leads to internal accumulation of precursor CPY.
Probable dehydrogenase required for replication of Brome mosaic virus. Involved in vacuolar processing and morphology.
Forms a complex composed of CDC48, NPL4, UFD1, DOA1, SHP1 and deubiquitinase OTU1 (PubMed:16427015). Interacts with CDC48 (PubMed:15258615).
Involved in CDC48-dependent protein degradation through the ubiquitin/proteasome pathway. Direct or indirect positive regulator of GLC7 activity.
Present with 3200 molecules/cell in log phase SD medium.
Component of the heterotrimeric CDC48-NPL4-UFD1 ATPase complex (PubMed:16873066). The CDC48-NPL4-UFD1 ATPase complex interacts with the HRD1 ubiquitin ligase complex composed of the E3 ligase HRD1, its cofactors HRD3, USA1 and DER1, substrate recruiting factor YOS9 and CDC48-binding protein UBX2 (PubMed:16873066). Interaction between the complexes is mediated by interaction between CDC48-NPL4-UFD1 complex member CDC48 and HRD1 complex member UBX2 (PubMed:16873066). Forms a complex composed of CDC48, NPL4, UFD1, DOA1, SHP1 and deubiquitinase OTU1 (PubMed:16427015). Interacts with CDC48, UFD1 and VMS1 (PubMed:11598205, PubMed:11733065, PubMed:11739805, PubMed:21070972, PubMed:31249135).
Substrate-recruiting cofactor of the CDC48-NPL4-UFD1 segregase (PubMed:31249135). Assists CDC48 in the dislocation of misfolded, polyubiquitinated ERAD substrates that are subsequently delivered to the proteasome for degradation (PubMed:11739805, PubMed:11740563, PubMed:11847109). Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus (PubMed:8930904, PubMed:11733065). Required for the proteasome-dependent processing/activation of MGA2 and SPT23 transcription factors leading to the subsequent expression of OLE1 (PubMed:11733065). Regulates ubiquitin-mediated mitochondria protein degradation (PubMed:31249135). Involved in spindle disassembly probably by promoting the degradation of spindle assemby factors ASE1 and CDC5 at the end of mitosis (PubMed:14636562).
With IRS4, acts as a positive regulator of INP51 activity and phosphatidylinositol 4,5-bisphosphate turnover. Negatively regulates signaling through the cell integrity pathway, including the MAP kinase SLT2.
Abolishes localization of HIR1 and RTT106 to the HTA1-HTB1 promoter.
Component of the HIR complex, composed of HIR1, HIR2, HIR3 and HPC2 (PubMed:16264190, PubMed:16303565). This complex may consist of one copy of HIR1 and HIR3 and two copies of HIR2 and HPC2 (PubMed:16264190). The HIR complex interacts with ASF1 (PubMed:16303565). Interacts with RTT106 (PubMed:19683497).
Component of the HIR complex, which functions as a histone chaperone that cooperates with ASF1 to promote replication-independent chromatin assembly. The HIR complex is also required for the periodic repression of three of the four histone gene loci during cell cycle as well as for autogenous regulation of the HTA1-HTB1 locus by H2A and H2B. DNA-binding by the HIR complex may repress transcription by inhibiting nucleosome remodeling by the SWI/SNF complex. The HIR complex may also be required for transcriptional silencing of centromeric, telomeric and mating-type loci in the absence of CAF-1.
Belongs to the glycosyl hydrolase 16 family. CRR1 subfamily.
Expression is increased in low copper conditions, probably through the transcription regulation by the copper regulon transcription factor MAC1.
Spore specific glycosidase involved in spore wall assembly during sporulation. May be involved in copper import.
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
The alpha and beta chains are autoproteolytically processed from a single precursor protein within the mitochondrion.
Present with 38400 molecules/cell in log phase SD medium.
Heterohexamer; composed of 3 copies of TIM9 and 3 copies of TIM10, named soluble 70 kDa complex. Associates directly with the TIM12 component of the TIM22 complex, whose core is composed of TIM18, TIM22 and TIM54. Interacts with the transmembrane regions of multi-pass transmembrane proteins in transit.
Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. Compared to TIM9, it may function as a substrate sensor.
The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIM10 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane.
Component of the RQT (ribosome quality control trigger) complex, composed of SLH1, CUE3, and RQT4 (PubMed:28757607, PubMed:32203490). Interacts with SLH1 (PubMed:28757607). Interacts with CUE3 (PubMed:28757607, PubMed:28223409). Interacts with HEL2 (PubMed:28757607). Associates with translating ribosomes (PubMed:28757607, PubMed:28223409).
Defective activation of the ribosome quality control (RQC) pathway (PubMed:28757607). Mildly defective ribosome stalling induced by RNA arrest sequences (PubMed:28223409). Sensitive to anisomycin (stalls ribosomes in the rotated state) (PubMed:28757607).
Functions as part of the RQC trigger (RQT) complex that activates the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation.
Component of a cullin-RING ligase (CRL)-like complex composed of at least the cullin RTT101, a linker protein MMS1, and the potential substrate receptor ESC2. Interacts with RTT101 and MMS1. Interacts with SIR2.
May be a substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-ESC2). Involved in HMR and telomere silencing via the recruitment or stabilizing of the SIR (silent information regulators) complex.
The 2 SUMO-like regions, although related to ubiquitin domains lack the conserved acceptor Gly residue in position 456.
Required for efficient mating. Involved in the production of alpha-factor, the KAR9 and TUB1 location to the shmoo tip and nuclear migration into pheromone-induced shmoos.
Belongs to the protein prenyltransferase subunit alpha family.
Essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. If X is Ser, Ala, Met, Cys, or Gln, then the protein is farnesylated, if X is Leu or Phe, then the protein is geranylgeranylated. The alpha subunit wraps partly around the beta subunit forming part of the active site. The beta subunit is responsible for isoprenoid and peptide-binding.
Farnesyltransferase and geranyl-geranyltransferase share a common alpha subunit (RAM2) (Probable). Protein farnesyltransferase is a heterodimer of alpha subunit RAM2 and beta subunit RAM1 (PubMed:1763050). Protein geranyl-geranyltransferase type-1 is a heterodimer of alpha subunit RAM2 and beta subunit CDC43 (PubMed:1400380, PubMed:9174352).
Belongs to the SOS response-associated peptidase family.
Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites. Recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross-link with DNA: forms a stable thiazolidine linkage between a ring-opened abasic site and the alpha-amino and sulfhydryl substituents of its N-terminal catalytic cysteine residue (By similarity). Acts as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (By similarity).
Component of the SPOTS complex that acts as a negative regulator of sphingolipid synthesis. Acts by inhibiting serine palmitoyltransferases (LCB1 and LCB2) activity.
Component of the SPOTS complex, at least composed of LCB1/2 (LCB1 and/or LCB2), ORM1/2 (ORM1 and/or ORM2), SAC1 and TSC3.
Phosphorylated in case of disruption of sphingolipid synthesis. Phosphorylation regulates inhibitory activity of serine palmitoyltransferases (LCB1 and LCB2).
Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity.
Belongs to the peptidase M24 family. SPT16 subfamily.
Forms a stable heterodimer with POB3 (PubMed:9832518, PubMed:9705338, PubMed:10413469). The SPT16-POB3 dimer weakly associates with multiple molecules of NHP6 (NHP6A or NHP6B) to form the FACT (yFACT or SNP) complex (PubMed:11432837, PubMed:11313475, PubMed:12952948). The FACT complex interacts with the CK2 (casein kinase II) complex subunits CKA1, CKA2, CKB1 and CKB2 and the components of the transcription machinery CHD1, CTR9, PAF1 and CDC73 (PubMed:12682017, PubMed:12242279). The FACT complex interacts with the PAF1 complex (PubMed:11927560). Interacts with POL1 (PubMed:9199353). Interacts with SAS3 (PubMed:10817755). Interacts with YTA7 (PubMed:22156209).
Present with 18500 molecules/cell in log phase SD medium.
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Required for cell growth, osmoresistance and expression of GPD1.
The target of rapamycin complex 2 (TORC2) is composed of at least AVO1, AVO2, BIT61, LST8, TOR2 and TSC11. TORC2 likely forms a homodimer. Contrary to TORC1, TORC2 does not bind to and is not sensitive to FKBP-rapamycin. AVO2 is peripherally associated to AVO1 and TSC11.
Implicated in secretion, nuclear segregation and in maintenance of cell size.
Present with 33400 molecules/cell in log phase SD medium.
Three regions of the protein are predicted to form a coiled-coil. It may adopt a rod-shaped rather than a globular configuration.
Forms homodimers in the absence, and homotetramers in the presence of acetyl-CoA.
N-acetyltransferase that acetylates histone H3 at 'Lys-14' and histone H4 at 'Lys-5' and 'Lys-12'. Also acetylates polyamines like putrescine, spermidine and spermine, and certain other small basic proteins like nuclear HMG proteins.
GTPase-activating protein (GAP) for RHO1 and RHO2. Involved in the control of cellular morphogenesis. Required for proper bud site selection and bud emergence.
Part of the multisubunit TRAPP (transport protein particle) III complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33 and TRS85.
Specific subunit of the TRAPP III complex that acts as an autophagy-specific guanine nucleotide exchange factor (GEF) for YPT1. TRS85 directs the TRAPP III complex to the phagophore assembly site (PAS) that is involved in autophagosome formation. Required for membrane expansion during autophagy and the CVT pathway. Required for sporulation. Has a role late in meiosis following DNA replication.
Belongs to the ubiquitin conjugation factor E4 family.
E4 ubiquitin chain-elongation enzyme specifically involved in polyubiquitin chain assembly. Binds to CDC48 and elongates mono- and diubiquitinated ERAD substrates presented by the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex to a chain length of 4 to 6 ubiquitin moieties. Delivers these polyubiquitinated substrates to RAD23 and DSK2, which target them to the proteasome. Has E3 ubiquitin-protein ligase activity, accepting ubiquitin from its cognate E2 ubiquitin-conjugating enzyme UBC4. Enhances ubiquitination at 'Lys-48', but not at 'Lys-29' of the Ub moiety. Promotes ubiquitin chain elongation at 'Lys-48' on the DOA10 substrate PEX29. Also involved in the proteolytic processing of the ER-bound transcription factor SPT23.
Interacts with CDC48. Interacts with the ubiquitin-like domain of RAD23 and DSK2. Interacts with PEX29.
The U-box domain is required for the ubiquitin protein ligase activity.
Involved in DNA double-strand break (DSB) repair and recombination. Promotes the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase.
Part of a complex that includes RAD51, RAD52 and RAD59. Interacts with SAW1.
Produced by alternative initiation at Met-5 of isoform 1.
Produced by alternative initiation at Met-7 of isoform 1.
Belongs to the archaeal/bacterial/fungal opsin family.
Present with 182000 molecules/cell in log phase SD medium.
Belongs to the FKBP-type PPIase family. FKBP2 subfamily.
Inhibited by both FK506 and rapamycin. Binds FK506 with 15-fold lower affinity than FKB1.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. FKBP-13 may play a role in protein trafficking in the ER.
Present with 5400 molecules/cell in log phase SD medium.
This protein is a negative regulator for the gene expression of the lactose/galactose metabolic genes. It binds to GAL4 and so blocks transcriptional activation by it, in the absence of an inducing sugar.
May play a role in transcription regulation.
Present with 1332 molecules/cell in log phase SD medium.
'ZDS' means 'zillion different screens' as both ZDS1 and ZDS2 have been found by a wide variety of genetic screens.
Has a role in establishing cell polarity. Together with cAMP-dependent protein kinase regulatory subunit BCY1, provides a negative feedback control on the cell wall integrity-signaling pathway by acting as a negative regulator of MAP kinase SLT2/MPK1. In heat-stressed cells appears to play a role in localizing BCY1 to the cytoplasm. Seems to interact with, and down-regulate, CDC42. Also acts as a suppressor of PKC1. May act as an integration point for distinct signaling pathways helping to maintain a balance among these different pathways.
Interacts with BCY1, DBP5, GFD1 and SKG6.
When associated with DBP5, GFD1 and nucleoporins at the cytosolic fibrils of the nuclear pore complex, is required for mRNA export form the nucleus.
Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). uL1 forms part of the L1 stalk (PubMed:9559554, PubMed:22096102).
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. uL1 forms part of the L1 stalk, a mobile element that plays a role in evacuating the exit-site tRNA.
Present with 116000 molecules/cell in log phase SD medium.
Present with 265000 molecules/cell in log phase SD medium.
Required for the function of coenzyme Q in the respiratory chain. May serve as a chaperone or may be involved in the transport of Q6 from its site of synthesis to the catalytic sites of the respiratory complexes.
Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.
Produced by alternative initiation at Met-10 of isoform Mitochondrial.
Produced by alternative initiation at Met-18 of isoform Mitochondrial.
This enzyme carries out synthesis of the tRNA CCA terminus without the direction of a template using the multiple accepting and donating subsites within its active site.
Component of the GINS complex which is a heterotetramer of SLD5, PSF1, PSF2 and PSF3. Interacts with PSF2.
Present with 1431 molecules/cell in log phase SD medium.
Required for DNA replication. Functions as part of the GINS complex which plays an essential role in the initiation of DNA replication by binding to DNA replication origins and facilitating the assembly of the DNA replication machinery. Required for the chromatin binding of CDC45.
Golgi membrane protein involved in vesicular trafficking.
Present with 4540 molecules/cell in log phase SD medium.
Phosphorylated by the cyclin-CDK PCL10-PHO85. Phosphorylation causes inactivation of enzyme.
Component of the THO complex, which is composed of HPR1, MFT1, THO2 and THP2. Together with SUB2, TEX1 and YRA1, THO forms the transcription/export (TREX) complex. THO associates with DNA and RNA in vitro.
Component the THO subcomplex of the TREX complex, which operates in coupling transcription elongation to mRNA export. The THO complex is recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymerase II elongation complex by preventing formation of DNA:RNA hybrids behind the elongating polymerase. It functions in cotranscriptional formation of an export-competent messenger ribonucleoprotein particle (mRNP) by facilitating the loading of ATP-dependent RNA helicase SUB2 and the mRNA export factor YRA1 along the nascent mRNA.
HPR1 is not required for sporulation, and is not essential for DNA repair. It is probably not a DNA topoisomerase.
Component of the small ribosomal subunit, ribosomal RNA processing complex (SSU RRP complex). Interacts with NOB1.
Required for small ribosomal subunit (SSU) synthesis. Has a role in the processing of early nucleolar and late cytoplasmic pre-RNA species. Recruits DIM1 to nucleolar pre-RNAs. Indirectly required for cleavage at the A2 site of the 20S pre-rRNA, forming 18S rRNA, and at A1 and A2 sites of other pre-rRNAs.
Component of the 0.8 MDa ADA complex, which at least consists of ADA2, ADA3, AHC1 and GCN5.
Functions as component of the transcription regulatory histone acetylation (HAT) complex ADA. ADA preferentially acetylates nucleosomal histones H3 (at 'Lys-14' and 'Lys-18') and H2B. AHC1 is required for the overall structural integrity of the ADA complex.
Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.
Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor. Molecular oxygen can replace fumarate in vitro. Does not use oxaloacetate or NAD or NADP as electron acceptors.
Present with 264000 molecules/cell in log phase SD medium.
The activity is independent of the presence of oxygen.
Component of the CTF18-RFC complex, which consists of CTF18, CTF8, DSCC1, RFC2, RFC3, RFC4 and RFC5.
Essential for the fidelity of chromosome transmission. Required for the DNA replication block checkpoint. Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA.
The target of rapamycin complex 2 (TORC2) is composed of at least AVO1, AVO2, BIT61, LST8, TOR2 and TSC11. TORC2 likely forms a homodimer. Contrary to TORC1, TORC2 does not bind to and is not sensitive to FKBP-rapamycin.
Present with 36600 molecules/cell in log phase SD medium.
Component of the signal peptidase complex (SPC) composed of a catalytic subunit SEC11 and three accessory subunits SPC1, SPC2 and SPC3 (PubMed:8910564, PubMed:9148931). The complex induces a local thinning of the ER membrane which is used to measure the length of the signal peptide (SP) h-region of protein substrates (By similarity). This ensures the selectivity of the complex towards h-regions shorter than 18-20 amino acids (By similarity). SPC associates with the translocon complex (PubMed:10921929). Interacts with SBH1 and SEB2/SBH2 (PubMed:10921929).
Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (PubMed:8910564, PubMed:10921929). Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site (PubMed:8910564, PubMed:10921929).
Important for signal peptidase activity and cell viability at high temperatures.
Component of the 90S pre-ribosome. Component of the pre-40S ribosome.
RNA-binding nucleolar protein required for pre-rRNA processing. Component of the 90S pre-ribosome involved in production of 18S rRNA and assembly of small ribosomal subunit. Component of the pre-40S ribosome required for release from the nucleolus.
Present with 9100 molecules/cell in log phase SD medium.
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of mitochondrial acyl-carrier-protein.
Catalyzes the covalent attachment of ubiquitin to other proteins. Essential for peroxisome biogenesis (By similarity) (PubMed:17550898, PubMed:18644345). Required for UBC4-independent ubiquitination of PEX5 (PubMed:17550898, PubMed:18644345).
By the HOG1 MAPK, cell wall perturbations, and nitrogen stress. Expression is controlled by the MSS11 pseudohyphal growth transcription factor.
Contributes to the wild-type cellular response to nitrogen stress through signaling pathways that regulate the expression of genes involved in amino acid biosynthesis. Required for wild-type filamentous growth, cell growth, and cell-cell adhesion.
Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, TRA1 and YNG2.
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair.
Glyoxylate reductase that reversibly reduces glyoxylate to glycolate, or alternatively hydroxypyruvate to D-glycerate, using either NADPH or NADH as a cosubstrate (PubMed:17173333). Does not act as a hydroxyisocaproate dehydrogenase even though it also has minor activity on alpha-ketoisocaproate (PubMed:17173333).
Leads to higher biomass concentration after diauxic shift.
N-glycosylation may be involved in the sorting process for misfolded STE2 protein.
Receptor for the peptide pheromone alpha factor, the mating factor of yeast.
Belongs to the F-actin-capping protein alpha subunit family.
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
Component of the CTF18-RFC complex, which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5.
Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA.
Interacts with the target of rapamycin complex 1 (TORC1) in a rapamycin-dependent manner. Interacts with MRS6.
It is uncertain whether Met-1 or Met-6 is the initiator.
Phosphorylated by TORC1 kinase at multiple sites. Phosphorylation regulates nuclear localization and RP promoter binding.
Transcription factor that regulates ribosomal protein (RP) and ribosome biogenesis (Ribi) gene expression in response to nutrients and stress. Promotes RP gene expression under optimal growth conditions. Leaves the nucleus upon environmental challenges, resulting in a down-regulation of RP gene transcription. The effect of the environmental cues on SFP1 localization is mediated through the TOR pathway. Also regulates the expression of genes involved in the G2/M transition during the mitotic cell cycle and the DNA-damage response. Required for carbon-source modulation of cell size.
[ISP+] is the prion form of SFP1. [ISP+] is the result of a conformational change of the cellular SFP1 protein that becomes self-propagating and infectious. This conformational change generates a form of SFP1 that assembles into amyloid fibrils. [ISP+]-aggregates accumulate in the nucleus, and results in significantly larger cell size and increased drug resistance (PubMed:20498075). [ISP+] can be cured by GdnHCl (PubMed:11805042). It is speculated that prion properties of transcription factors may generate an optimized phenotypic heterogeneity that buffers yeast populations against diverse environmental insults (PubMed:20498075).
Component of the GINS complex which is a heterotetramer composed of SLD5, PSF1, PSF2 and PSF3. Interacts with PSF2.
Required for DNA replication. Functions as part of the GINS complex which plays an essential role in the initiation of DNA replication by binding to DNA replication origins and facilitating the assembly of the DNA replication machinery.
Present with 6840 molecules/cell in log phase SD medium.
Required for the synthesis of yeast cytochrome oxidase.
CKII-mediated phosphorylation of Ser-45 and Ser-46 regulates its function in the production of PA.
CTP-dependent diacylglycerol kinase that catalyzes the phosphorylation of diacylglycerol (DAG) to phosphatidate (PA). Controls phosphatidate levels at the nuclear envelope. Counteracts the activity of PA phosphatase PAH1/SMP2, controlling the levels of PA and DAG for the synthesis of triacylglycerol and membrane phospholipids (PubMed:18458075, PubMed:27834677). May be involved in vesicle trafficking between the endoplasmic reticulum and the Golgi apparatus (PubMed:11481671). Required to convert triacylglycerol-derived DAG to PA for phospholipid synthesis during growth resumption from stationary phase in the absence of de novo fatty acid synthesis (PubMed:21071438). Involved in the resistance to nickel chloride and nalidixic acid (PubMed:10407277).
Inhibited by N-ethylmaleimide, dCTP, and sphingoid bases including sphinganine, sphingosine and phytosphingosine. DAG pyrophosphate, cardiolipin, CDP-DAG, and lyso-PA inhibited activity by 23-66%. Also inhibited by Ca(2+) concentrations of more than 1 mM, by addition of EDTA or EGTA at 5 mM, and by 5 mM Mn(2+) and Zn(2+). Stimulated by major membrane phospholipids including phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, phosphatidylserine, phosphatidylglycerol, and phosphatidate. Also stimulated to a maximum by addition of TritonX-100 at a concentration of 1 mM, followed by an apparent inhibition of activity at concentrations above 1 mM.
Rescues the lethality of dephosphorylated PAH1/SMP2. Overexpression causes the appearance of phosphatidate-enriched membranes around the nucleus, leading to expansion of the nuclear membrane without proliferation of the cortical endoplasmic reticulum membrane. Deletion restores normal nuclear structure in PAH1/SMP2 deleted cells and returns the level of INO1 mRNA to normal. Deletion does not affect the abnormal levels of phosphatidylinositol and major neutral lipid triacylglycerol seen in the PAH1/SMP2 deletion mutant.
Belongs to the folylpolyglutamate synthase family.
Glutamate-adding enzyme which catalyzes the binding of the first glutamyl side chain to dihydropteroate. Leads to the de nove synthesis of tetrahydrofolate.
Required for the maintenance of the bipolar budding pattern. Involved in selecting bud sites at both the distal and proximal poles of daughter cells as well as near previously used division sites on mother cells.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. GLE2 interacts with the NUP82 subcomplex via NUP116. It also interacts with NUP42.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically important for nuclear mRNA export.
Regulates exocytosis by functioning as a GAP for SEC4. Also required for efficient polarization of the actin patches.
The exocyst complex is composed of SEC3, SEC5, SEC6, SEC8, SEC10, SEC15, EXO70 and EXO84. Interacts with SEC4.
Homooligomer. Interacts with PEX11, PEX25 and PEX27.
In concert with the three peroxisome divisional factors, PEX11, PEX25 and PEX27, controls peroxisome morphology and abundance under conditions of peroxisome proliferation. Maintains mature peroxisomes in actively dividing cells.
Forms DNA polymerase zeta with REV3 (PubMed:8658138). Interacts with REV1 (PubMed:18242152).
Required for DNA damage induced mutagenesis. Involved in DNA repair, mitochondrial DNA repair and translesion synthesis. Has a role in the bypass of abasic (AP) sites.
Interacts with HAP1. Component of the HMC including HAP1, SRO9 and YDJ1.
May overlap in function with tropomyosin and may be involved in organization of actin filaments. Acts as a multicopy suppressor of RHO3 mutation. RNA-binding protein which may modulate mRNA translation. Involved in heme regulation of HAP1, as a component of the high-molecular-weight complex (HMC).
Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Involved in regulation of various organellar membrane contact sites (PubMed:26119743). May be involved in sterol transfer between intracellular membranes (PubMed:26001273). Selectively transports sterols between membranes in vitro. Involved in stress-dependent formation of sterol-enriched vacuolar membrane domains (PubMed:25987606).
Serine/threonine-protein kinase involved in the control of sugar metabolism and translation. Phosphorylates UGP1, which is required for normal glycogen and beta-(1,6)-glucan synthesis. This phosphorylation shifts glucose partitioning toward cell wall glucan synthesis at the expense of glycogen synthesis.
Present with 4990 molecules/cell in log phase SD medium.
Required for 60S ribosomal subunit synthesis. Probably involved in the processing of 27S rRNA to produce mature 25S rRNA.
TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity.
TFIIA is a heterodimer composed of the large TOA1 and a small TOA2 subunits. Interacts with TBP. Interacts with TAF11. Interacts with KAP122.
Activates endogenous medium-chain (MCFA) and long-chain fatty acids (LCFA) by esterification of the fatty acids into metabolically active CoA-thioesters for subsequent degradation or incorporation into phospholipids (PubMed:8206942). Preferentially acts on C9:0-C13:0 fatty acids although C7:0-C17:0 fatty acids are tolerated (PubMed:8206942). Is the main if not exclusive MCFA (octanoate, decanoate and laureate) acyl-CoA ligase. Required for efficient MCFA beta-oxidation inside peroxisomes. Facilitates the transport of MCFAs into peroxisomes by passive diffusion, by decreasing the intraorganellar MCFA concentration (PubMed:8670886). Also esterifies LCFAs in the peroxisome matrix. The LCFAs are actively transported into peroxisomes by a PXA1-PXA2 heterodimeric transporter in the peroxisomal membrane (PubMed:22493507).
Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression (PubMed:25683707). Involved in mitochondrial lipid homeostasis (PubMed:23781023).
Metal-independent, broad-range acid phosphatase. Involved, either directly or indirectly, in the bidirectional transport of sterols between the endoplasmic reticulum and the plasma membrane.
Belongs to the eukaryotic ribosomal protein eS30 family.
Present with 37600 molecules/cell in log phase SD medium.
Component of the mitochondrial inner membrane i-AAA protease supercomplex composed of MGR1, MGR3 and YME1. With MGR1, forms a subcomplex that binds to YME1 and to substrates to facilitate proteolysis.
Component of the mitochondrial inner membrane i-AAA protease supercomplex, which degrades misfolded mitochondrial proteins. Together with MGR1, functions in an adapter complex that targets substrates to the i-AAA protease for degradation. Required for growth of cells lacking the mitochondrial genome.
Forms a NOT protein complex that comprises NOT1, NOT2, NOT3, NOT4 and NOT5. Subunit of the 1.0 MDa CCR4-NOT core complex that contains CCR4, CAF1, NOT1, NOT2, NOT3, NOT4, NOT5, CAF40 and CAF130. In the complex interacts with NOT1 and NOT2. The core complex probably is part of a less characterized 1.9 MDa CCR4-NOT complex.
Belongs to the peptidase M67A family. CSN5 subfamily.
Catalytic component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes (By similarity). The CSN complex is involved in the regulation of the mating pheromone response.
Component of a COP9 signalosome-like (CSN) complex, composed of at least RRI1/CSN5, CSN9, RRI2/CSN10, PCI8/CSN11, CSN12 and CSI1. Within this complex it probably interacts directly with CSN12. Also interacts with RPN5.
The JAMM motif is essential for the protease activity of the CSN complex resulting in deneddylation of cullins. It constitutes the catalytic center of the complex (By similarity).
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. May lack catalytic activity.
Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Functions at the internalization step of the clathrin-mediated endocytosis (CME) as an early-acting scaffold protein. Requires clathrin adapter proteins, ENT1/2 and YAP1801/2, for normal spatiotemporal dynamics and viability. Binds to biological membranes in a ubiquitin-dependent manner.
Interacts (via UBA domain) with monoubiquitin and ENT1 (via asparagine-proline-phenylalanine tripeptide motif called NPF). Interacts with PAL1 and SYP1.
Random budding pattern and morphological defects. Defects in fluid-phase endocytosis and defective internalization of the pheromone alpha-factor and uracil permease. Deletion has only a small impact on actin cytoskeleton organization. Deletion shows synthetic growth defects with thermosensitive mutants of PAN1, END3 and RSP5.
Interacts with MUD2 and PRP40. The proline-rich sequence of this protein interacts with the GYF domains of SMY2 and SYH1.
Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. 2 commitment complexes, CC1 and CC2, have been defined. CC1 is a basal complex dependent only on the 5'-splice site. CC2 is a complex of lower mobility and is dependent on a branchpoint as well as a 5'-splice site region. This protein is involved in CC2 formation where it binds to the snRNP U1-associated protein PRP40, bridging the U1 snRNP-associated 5'-splice site and the MSL5-associated branch point 3' intron splice site. Involved in nuclear retention of pre-mRNA.
Interacts with RIF1 and RAP1 C-terminus.
Involved in transcriptional silencing and telomere length regulation. Its role in telomere length regulation results from either a block in elongation or promoting degradation of the telomere ends. Loss of RIF1 function results in derepression of an HMR silencer, whose ARS consensus element has been deleted, and in the elongation of telomeres. RAP1 may target the binding of RIF1 to silencers and telomeres.
Required for the retention of luminal endoplasmic reticulum proteins, affects glycoprotein processing in the Golgi apparatus.
Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen. Defective copy causes severe glycosylation defect and abnormal retention of soluble endoplasmic reticulum proteins. Involved in vanadate sensitivity.
Present with 31900 molecules/cell in log phase SD medium.
Transporter involved in the uptake of sterol.
Essential for respiratory growth and required for mitochondrial protein synthesis. Required for vacuolar acidification.
Lacks 3 iron-binding residues conserved in all other R2 subunits.
Present with 88884 molecules/cell in log phase SD medium.
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. RNR4 is required for proper folding of RNR2 and assembly with the large subunits.
Component of the ER-mitochondria encounter structure (ERMES) or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34.
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria (PubMed:11907266, PubMed:14981098). Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria (PubMed:27469264). MDM34 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10 (By similarity) (PubMed:19556461).
Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex containing the F-box protein MDM30. Ubiquitination is important for mitochondrial integrity.
Component of the COMPASS (Set1C) complex which consists of SET1(2), BRE2(2), SPP1(2), SDC1(1), SHG1(1), SWD1(1), SWD2(1), and SWD3(1). Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. Component of the APT complex, which is a subcomplex of CPF, and is composed of PTI1, SYC1, SSU72, GLC7, REF2, PTA1 and SWD2.
Involved in mediating RNA polymerase II termination. Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation.
Belongs to the squalene monooxygenase family.
Inhibited by the allylamine antimycotic drugs.
Present with 65400 molecules/cell in log phase SD medium.
Squalene epoxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:1743514, PubMed:8358382, PubMed:9450962). ERG1 catalyzes the epoxidation of squalene into 2,3-epoxysqualene (PubMed:1743514, PubMed:8358382, PubMed:9450962). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672).
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids.
Fusel oils are important flavor and aroma compounds in yeast-fermented products contributing to the quality of beverages and food. In low concentration they are generally desirable, whereas high concentrations may spoil the product. By adjusting growth conditions and substrate their production is sought to be influenced.
One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-acids). In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids derived from leucine (4-methyl-2-oxopentanoate, also alpha-keto-isocaproate) and isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), whereas transaminated valine, transaminated aromatic amino acids, and pyruvate are no substrates. In analogy to the pyruvate decarboxylases the enzyme may in a side-reaction catalyze condensation (or carboligation) reactions leading to the formation of 2-hydroxy ketone, collectively called acyloins. The enzyme is also positively regulating the thiamine metabolism by a molecular mechanism that may involve thiamine concentration sensing and signal transmission.
While genetic evidence suggests this enzyme is involved in leucine and isoleucine catabolism (PubMed:9341119, PubMed:10753893), no decarboxylase enzymatic activity could be detected in cell extracts of S.cerevisiae strains expressing the individual gene (PubMed:22904058).
Essential for the organization of the actin cytoskeleton, fluid phase endocytosis and vesicle trafficking, together with LSB5.
Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (By similarity). Phosphorylates YTA7 during S-phase to promote transcription of histones (PubMed:22156209).
Tetramer composed of an alpha chain, an alpha', one beta chain and one beta' chain (PubMed:12242279). Interacts with FACT subunits POB3 and SPT16 (PubMed:12242279). Interacts with NAP1 (PubMed:18086883). Interacts with YTA7 (PubMed:22156209).
Present with 3570 molecules/cell in log phase SD medium.
Pyrophosphorylated by 5-diphosphoinositol pentakisphosphate (5-IP7) (PubMed:17873058). Serine pyrophosphorylation is achieved by Mg(2+)-dependent, but enzyme independent transfer of a beta-phosphate from a inositol pyrophosphate to a pre-phosphorylated serine residue (PubMed:17873058).
Belongs to the eukaryotic ribosomal protein eS25 family.
It is presumed that the precursor part of S25 is engaged in assembling of the small subunit, thus being essential in ribosome maturation.
Present with 162000 molecules/cell in log phase SD medium.
Heterodimer with ALG14 to form a functional enzyme.
Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway.
Present with 22600 molecules/cell in log phase SD medium.
Involved in the second step of GPI biosynthesis. De-N-acetylation of N-acetylglucosaminyl-phosphatidylinositol.
Component of the ER-mitochondria encounter structure (ERMES) or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34 (PubMed:13679517, PubMed:17410204, PubMed:19556461). A MMM1 homodimer associates with one molecule of MDM12 on each side in a pairwise head-to-tail manner, and the SMP-LTD domains of MMM1 and MDM12 generate a continuous hydrophobic tunnel for phospholipid trafficking (PubMed:28479252, PubMed:29078410). Interacts with PUF3 (By similarity) (PubMed:17210948).
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria (PubMed:19556461, PubMed:22250200). Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria (PubMed:19556461, PubMed:27469264). MDM12 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids (By similarity) (PubMed:17410204).
Produced by +1 ribosomal frameshifting between codon Leu-431 and Gly-432 of the YDR210W-A ORF.
Belongs to the WD repeat G protein beta family. Ribosomal protein RACK1 subfamily.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). Located at the head of the 40S ribosomal subunit in the vicinity of the mRNA exit channel, RACK1 serves as a scaffold protein that can recruit other proteins to the ribosome. Involved in induction of the ribosome quality control (RQC) pathway; a pathway that degrades nascent peptide chains during problematic translation (PubMed:28223409). Involved in the negative regulation of translation of a specific subset of proteins (PubMed:15340087).
Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). RACK1 is located at the head of the SSU in the vicinity of the mRNA exit channel (PubMed:15340087, PubMed:15334071, PubMed:22096102). RACK1 interacts with the mRNA-binding protein SCP16 (PubMed:15012629). RACK1 also exists simultaneously as a homodimer in a cytosolic non-ribosome-bound form (PubMed:21704636).
Present with 333112 molecules/cell in log phase SD medium.
Component of the ISW1A complex, which at least consists of ISW1 and IOC3.
Functions as component of the ISW1A complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW1A complex represses gene expression at initiation through specific positioning of a promoter proximal dinucleosome.
Present with 337000 molecules/cell in log phase SD medium.
Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis.
The chaperone activity is regulated by ATP-induced allosteric coupling of the nucleotide-binding (NBD) and substrate-binding (SBD) domains. In the ADP-bound and nucleotide-free (apo) states, the two domains have little interaction. In contrast, in the ATP-bound state the two domains are tightly coupled, which results in drastically accelerated kinetics in both binding and release of polypeptide substrates. J domain-containing co-chaperones stimulate the ATPase activity and are required for efficient substrate recognition.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.
Required for assembly of the mitotic spindle.
Component of a microsomal membrane bound medium-chain fatty acid elongation system, which extends medium-chain-length fatty acids to long-chain fatty acids. Component of elongase I, which extends 12-16-carbon fatty acyl-CoAs such as lauroyl-CoA to 14-18-carbon fatty acids by incorporation of malonyl-CoA.
Induced in wild-type cells supplemented with 14:0 fatty acids and repressed when cells are supplied with 16- and 18-carbon fatty acids.
The C-terminal di-lysine motif may confer endoplasmic reticulum localization.
The HxxHH motif is essential for ELOp function in vivo and 3-keto acyl-CoA synthase activity in vitro.
Specific cargo receptor protein for the plasma membrane ATPase PMA1 that acts with PSG1 to promote the transport and maturation of PMA1 (PubMed:28727280). EXP1 and PSG1 probably act sequentially to promote PMA1 sorting between the ER and the Golgi, with EXP1 promoting PMA1 export from the ER to the Golgi while PSG1 has a role in PMA1 maturation or quality control in the Golgi (PubMed:28727280).
By oxygen at the level of transcription. Expression drops rapidly when the oxygen concentration falls below 0.5 uM O(2).
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of ubiquinol-cytochrome c oxidoreductase. Cytochrome c then transfers this electron to the dinuclear copper A center (CU(A)) of the COX2 subunit of cytochrome oxidase, the final protein carrier in the mitochondrial electron-transport chain. Isoform 1 (CYC1) is the predominant cytochrome c during aerobic/normoxic growth.
Methylation may enhance its transport into mitochondria. Methylation occurs in fungi, plants, and some protozoa, but not in animals. The precise role of methylation at Lys-79 is unknown, but it seems to preclude pro-apoptotic activity, possibly by lowering affinity for APAF1.
Belongs to the PDK/BCKDK protein kinase family.
Inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the E1 alpha subunit (PDA1), thus contributing to the regulation of glucose metabolism.
Component of the nuclear pore complex (NPC) (PubMed:11689687). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NUP82 is part of the NUP82 subcomplex. This subcomplex is the base for interactions with NUP116 and GLE2, with NUP42 and GLE1 and with DYN2.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved as part of the NUP82-NUP159-NSP1 subcomplex in nuclear mRNA and pre-ribosome export by acting as a linker tethering nucleoporins that are directly involved in nuclear transport to the NPC via its coiled-coil domain.
Present with 9470 molecules/cell in log phase SD medium.
Belongs to the activator 1 small subunits family. CTF18 subfamily.
Component of the CTF18-RFC complex, which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. CTF18 interacts with ECO1.
Belongs to the WD repeat IPI3/WDR18 family.
Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA.
Component of the RIX1 complex, composed of IPI1, RIX1/IPI2 and IPI3 in a 1:2:2 stoichiometry. The complex interacts (via RIX1) with MDN1 (via its hexameric AAA ATPase ring) and the pre-60S ribosome particles. Interacts with RIX1.
The coiled-coil motif forms a homodimeric contact and facilitates RIX1 complex oligomerization.
Yeast contains two L-asparaginase isoenzymes: cytoplasmic L-asparaginase I, and cell wall L-asparaginase II.
Dioxygenase that catalyzes the alpha-oxidation of 2-hydroxy fatty acids in an iron-dependent manner (PubMed:30530523). Involved in metabolism of phytosphingosine and is required for proper endoplasmic reticulum stress response (PubMed:25345524, PubMed:30530523).
Exhibits a defect in the metabolism that converts phytosphingosine to glycerophospholipids (PubMed:25345524). Leads to sensitivity to tunicamycin (PubMed:30530523).
Present with 5570 molecules/cell in log phase SD medium.
Required for normal formation of eisosomes, large cytoplasmic protein assemblies that localize to specialized domains on plasma membrane and mark the site of endocytosis.
Acts as essential component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events. Possesses ATPase activity.
Involved in metal homeostasis and more specially in manganese sensitivity.
Involved in rRNA processing. Required growth at elevated temperatures, resistance to hydroxyurea and for cell cycle progression.
Expression is regulated by the KAR4 transcription factor and reduced after pheromone induction.
Involved in morphogenesis. May be involved in cell wall organization and biogenesis.
Belongs to the Mediator complex subunit 10 family.
Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. NUT2/MED10 interacts directly with SRB7/MED21.
Present with 1472 molecules/cell in log phase SD medium.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.
Belongs to the enhancer of polycomb family.
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Involved in gene silencing by neighboring heterochromatin, blockage of the silencing spreading along the chromosome, and required for cell cycle progression through G2/M.
Elongator complex-associated factor that is not a structural subunit but rather transiently contacts the complex. Regulates elongator complex gamma-toxin target (TOT) activity, resulting in G1 block by Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin), probably through regulation of the ELP1/IKI3 subunit phosphorylation state. Required for an early step in synthesis of 5-methoxycarbonylmethyl (mcm5) and 5-carbamoylmethyl (ncm5) groups present on uridines at the wobble position in tRNA.
Phosphorylation of Ser-152 and Ser-160 is induced 2-fold in response to mating pheromone.
Present with 602000 molecules/cell in log phase SD medium.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YLR157C-A ORF.
Impairs growth on oleate as well as on the non-fermentable carbon sources ethanol and acetate (PubMed:27392156). Leads to increased level in threonine, serine, valine, isoleucine and histidine; as well as a reduction in citrulline, tyrosine and phenylalanine (PubMed:27392156).
Probably involved in peroxisome formation or maintenance as well as in amino acid metabolism.
Involved in a signal transduction pathway that play a role in yeast cell morphogenesis and cell growth. This pathway seems to start by SMP3; then involve the kinase PKC1 that may act on the BCK1 kinase that then phosphorylates MKK1 and MKK2 which themselves phosphorylate the MPK1 kinase.
Component of the RPD3C(L) complex composed of at least ASH1, CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6. Interacts with RIM11, MCK1 and IME1.
Component of the RPD3C(L) histone deacetylase complex (HDAC) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Binds to the URS1 site (5'-AGCCGCCGA-3') and recruits the RPD3 histone deacetylase complex to the promoters to negatively regulate the expression of many genes including CAR1 (arginase), several required for sporulation, mating type switching, inositol metabolism, and oxidative carbon metabolism. Recruits also the ISW2 chromatin remodeling complex to promoters in a second gene repression pathway. Associates with the master regulator of meiosis IME1 in order to activate the expression of meiosis genes. Has both a positive and negative role in regulating phospholipid biosynthesis.
Efficient DNA binding requires dimerization with another bHLH protein.
Transcriptional activator of phospholipid synthetic genes (such as INO1, CHO1/PSS, CHO2/PEM1, OPI3/PEM2, etc.).
Hyperphosphorylated in response to DNA damage by MEC1.
Involved in normal G2/M phase transition of the mitotic cell cycle. In association with RAD53, also involved in checkpoint control in response to DNA damage.
Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Has a role in cell integrity and polarized cell growth together with the other PCL1/PCL2 cyclin family members.
Belongs to the acireductone dioxygenase (ARD) family.
Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4-methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate.
Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site (By similarity). Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway (PubMed:15938715, PubMed:18625006). Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway (By similarity).
Required for processing of 5.8S rRNA (short form) at site A3 and for 5'- and 3'-processing of pre-tRNA.
Phosphorylated by the plasma membrane-anchored casein kinase YCK1. Phosphorylation at its C-terminus reduces its RNA-binding capacity.
Present with 15600 molecules/cell in log phase SD medium.
RNA-binding protein involved in the correct localization of transcripts in the cell. RNA localization is a widespread mechanism for achieving localized protein synthesis. Required for the asymmetric localization to the daughter cell nucleus of the ASH1 transcript, coding for a specific repressor of transcription. Overexpression inhibits translation of the ASH1 transcript. Involved in the stability of transcripts such as the MTL1 mRNA. Involved in structural and functional organization of telomeric chromatin and regulates silencing at the HMR locus.
By mating pheromone. Expression is directly controlled by STE12 as cells respond to mating pheromone.
Required for nuclear membrane fusion during karyogamy.
Has phosphatidylinositol transfer activity. Involved in the regulation of the phospholipid composition of plasma- and endomembranes. Altering plasma membrane composition may provide a possible mechanism for multidrug resistance. Involved in the regulation of sterol biosynthesis. Contributes to efficient phospholipase D1 activation in the regulation of phospholipid turnover. Regulates the release of fatty acids from lipid droplets (PubMed:24403601).
Homodimer (PubMed:23519406). Apo-SFH3 forms a dimer through the hydrophobic interaction of gating helices. Binding of phosphatidylinositol leads to dissociation of the dimer into monomers in a reversible manner (PubMed:23603387).
Present with 15361 molecules/cell in log phase SD medium.
Involved in transcription-coupled repair nucleotide excision repair (NER) of UV-induced DNA lesions.
Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.
Ref.3 sequence was originally thought to originate from Mycobacterium phlei.
Involved in pre-mRNA splicing. May be involved in endoplasmic reticulum-associated protein degradation (ERAD) and required for growth at low and high temperatures.
This is a truncated version of an UPF0507 family protein. Strain S288c has a frameshift in position 286, which disrupts the gene coding for this protein and produces two ORFs YML003W and YML002W. A contiguous sequence for a S.cerevisiae UPF0507 family protein can be found in strain YJM789 (AC A6ZM60).
Component of a COP9 signalosome-like (CSN) complex, composed of RRI1/CSN5, CSN9, RRI2/CSN10, PCI8/CSN11, CSN12 and CSI1. In the complex, it probably interacts directly with CSN9 and CSN12. Interacts also with RPN5.
Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes The CSN complex is involved in the regulation of the mating pheromone response.
Present in a pentameric cis-SNARE complex composed of the v-SNAREs NYV1, VTI1 and YKT6, and the t-SNAREs VAM3 and VAM7 on vacuolar membranes. Interacts in trans with the cognate t-SNARE VAM3 during the docking step of homotypic vacuolar fusion. Interacts with the vacuolar transporter chaperone (VTC) complex and the vacuolar Ca(2+)-ATPase PMC1.
Present with 1885 molecules/cell in log phase SD medium.
Vacuolar v-SNARE required for docking. Only involved in homotypic vacuole fusion. Required for Ca(2+) efflux from the vacuolar lumen, a required signal for subsequent membrane fusion events, by inhibiting vacuolar Ca(2+)-ATPase PMC1 and promoting Ca(2+) release when forming trans-SNARE assemblies during the docking step.
Component of the SCF(DIA2) complex containing CDC53, SKP1, RBX1 and DIA2. Interacts with SKP1.
F-box protein component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins (By similarity). The SCF(DIA2) complex is specifically involved in the pheromone induced degradation of phosphorylated TEC1. The SCF(DIA2) complex binds to DNA replication origins. Involved in DNA replication, genome stability, and the control of cell cycle, probably through its association to replication origins to facilitate the ubiquitination of another origin-binding protein. Required for invasive growth and growth under alkaline conditions.
Activates the ARF proteins by exchanging bound GDP for free GTP. Plays a role in maintaining mitochondrial morphology, and in the turnover of mitochondria through mitophagy (PubMed:25190516).
Interacts with GMH1. Interacts (via N-terminal region) with SEC21 (via C-terminus).
The SEC7 domain is sufficient for stimulation of nucleotide exchange on myristoylated yeast ARF2.
Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase (PubMed:12446688, PubMed:28821616). May participate in merging the COX1 and COX2 assembly lines (PubMed:28821616).
Required for meiosis I segmentation (PubMed:2123556). Probably acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage (PubMed:25533956).
Expression increases in late G1 phase compared to other phases of the cell cycle.
Homohexamer (By similarity). Interacts with RAD51; RAD51-ssDNA filaments do not interact autonomously with dsDNA but do so robustly in the presence of RAD54 (PubMed:9590697, PubMed:31492866).
Plays an essential role in homologous recombination (HR) which is a major pathway for repairing DNA double-strand breaks (DSBs), single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication forks (PubMed:12453424). Acts as a molecular motor during the homology search and guides RAD51 ssDNA along a donor dsDNA thereby changing the homology search from the diffusion-based mechanism to a motor-guided mechanism (PubMed:32502392). Also plays an essential role in RAD51-mediated synaptic complex formation which consists of three strands encased in a protein filament formed once homology is recognized (PubMed:31492866). Once DNA strand exchange occured, dissociates RAD51 from nucleoprotein filaments formed on dsDNA (PubMed:12453424).
Belongs to the peptidase S26 family. IMP2 subfamily.
Catalytic component of the mitochondrial inner membrane peptidase (IMP) complex. IMP catalyzes the removal of signal peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. The two catalytic IMP subunits seem to have non-overlapping substrate specificities. IMP2 substrates include nuclear encoded CYB2, mitochondrially encoded COX2 and cytochrome c1. Required for the stability of IMP1.
Can also be processed to start at Phe-54.
Cleaves proteins C-terminally to mono- and paired-basic residues. Required for cell wall integrity.
Positively regulated in response to cell wall perturbation.
Displays increased sensitivity to some cell wall disrupting agents including sodium dodecyl sulfate (SDS) and calcofluor white (CFW).
RNA-binding protein that associates with mRNAs encoding cell wall proteins.
In the N-terminal section; belongs to the FGAMS family.
Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (By similarity).
Present with 40800 molecules/cell in log phase SD medium.
Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Serves a receptor for nuclear localization signals. Mediates the nuclear import of TATA-binding protein (TBP) and of histones H2A and H2B.
Present with 19700 molecules/cell in log phase SD medium.
Responsible, together with PTC2, for the dephosphorylation of the cyclin-dependent protein kinase CDC28.
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids. Required for protein transport from Golgi to vacuoles.
Component of the Asi complex, which contains ASI1, ASI2 and ASI3 (PubMed:25236469). Interacts directly with ASI3 (PubMed:17085444).
E3 ubiquitin-protein ligase which transfers ubiquitin to substrates promoting their degradation. Part of the nuclear inner membrane (INM)-specific branch of the ER-associated degradation (ERAD) pathway, required for the elimination of misfolded proteins in the INM, a specialized ER subdomain. Required for ERG11 degradation (PubMed:25236469). Negative regulator of SPS-sensor signaling. Together with ASI2 and ASI3, prevents the unprocessed precursor forms of STP1 and STP2 that escape cytoplasmic anchoring from inducing SPS-sensor-regulated genes in the absence of inducing signals (PubMed:16735580, PubMed:17085444). Controls amino acid permease (AAP) gene expression in response to amino acid availability, a process mediated by the transcription factors STP1 and STP1 (PubMed:11454748).
Glycosylation is not required for ASI1 function.
Potassium-activated aldehyde dehydrogenase involved in acetate formation during anaerobic growth on glucose.
Present with 22200 molecules/cell in log phase SD medium.
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1), a complex that is involved in endosomal cargo sorting.
Constituent of COPII-coated endoplasmic reticulum-derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. The C-terminal Phe-Tyr motif is required for exit from the endoplasmic reticulum. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum.
Ty1-GR1 is a highly expressed element. Induced under amino acid starvation conditions by GCN4.
Belongs to the spermidine/spermine synthase family.
Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1.
Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB.
Glucanases possibly play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme hydrolyzes both 1,3-beta- and 1,6-beta-linkages and even has beta-glucosidase activity. It could also function biosynthetically as a transglycosylase.
Involved in mitochondrial fragmentation during programmed cell death in response to high levels of alpha-factor mating pheromone or the drug amiodarone (PubMed:15657396, PubMed:18800175). May be involved in sterol transfer between intracellular membranes (PubMed:26001273).
Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro).
Inhibited by 3-(4-benzyloxyphenyl)-2-(R)-amino-1-propanethiol (thioamine) and N-hydroxy-N-(2-(S)-amino-3-(4-benzyloxyphenyl)propyl)-5-carboxypen-tanamide (hydroxamic acid). The aminopeptidase activity is stimulated by LTA(4).
Interacts with DCD53 and SKP1. Component of the SCF(CDC4) complex containing CDC53, SKP1, RBX1 and CDC4. CDC34. Interacts with CDC6 and CIC1. Interacts with SIC1; the interaction involves a SIC1 double phosphorylated motif (degron). Homodimerizes; the dimerization increases SIC1 ubiquitination in vitro.
Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and binds to phosphorylated target proteins. Directs ubiquitination of the phosphorylated CDK inhibitor SIC1. Involved in the degradation of CDC6 together with CDC34/UBC3 and CDC53, and in restricting the degradation of FAR1 to the nucleus. Is essential for initiation of DNA replication and separation of the spindle pole bodies to form the poles of the mitotic spindle. It also plays a role in bud development, fusion of zygotic nuclei after conjugation and various aspects of sporulation. Required for HTA1-HTB1 locus transcription activation. Required for G1/S and G2/M transition.
Transcriptional repressor of multidrug resistance genes, such as PDR5. Required for growth on non-fermentable carbon sources like lactate or glycerol.
Belongs to the amino acid-polyamine-organocation (APC) superfamily.
Required for polyamine transport. Transports putrescine effectively and spermidine less effectively.
Broad substrate range permease which transports asparagine and glutamine with intermediate specificity. Also transports Ala, Cys, Gly, Ile, Leu, Met, Phe, Ser, Thr, Tyr and Val. Important for the utilization of amino acids as a nitrogen source.
Induced by transcription factors DAL81 and STP1, which are activated by a signal initiated by the plasma membrane SPS (SSY1-PTR3-SSY5) amino acid sensor system in response to external amino acid levels.
Present with 21100 molecules/cell in log phase SD medium.
Centromeric protein that plays a central role in the incorporation and maintenance of histone H3-like variant CENPA at centromeres.
HIR1, HIR2 and HIR3 are repressors of histone gene transcription. They are required for the periodic repression of three of the four histone gene loci during cell cycle as well as for autogenous regulation of the HTA1-HTB1 locus by H2A and H2B. Also has a role in nucleosome assembly.
Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis.
Homodimer (PubMed:6381051). Interacts with MCX1 (PubMed:25957689).
In combination with a disruption of MCX1, abrogates mitochondrial respiration.
Cleaves proteins C-terminally to mono- and paired-basic residues (By similarity). Required for cell wall integrity.
Present with 17600 molecules/cell in log phase SD medium.
Stimulates 40S and 60S ribosome biogenesis.
ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs. Required for the maintenance of dsRNA killer plasmid.
Belongs to the DEAD box helicase family. DDX24/MAK5 subfamily.
Identified in the GID complex. In the absence of glucose, the complex contains VID30/GID1, the E3 ubiquitin-ligase RMD5/GID2, VID28/GID5, GID7, GID8, and FYV10/GID9. When cells are shifted to glucose-containing medium, VID24/GID4 is induced and becomes part of the complex (PubMed:22645139). Within the complex, VID30/GID1 interacts directly (via LisH domain) with GID8, and (via CTLH domain) with GID7 (PubMed:22645139).
Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium (PubMed:9737955, PubMed:12686616). Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:9737955, PubMed:12686616, PubMed:22645139, PubMed:28126757).
Catalyzes the addition of a phosphorylinositol group onto mannosyl phosphorylinositol ceramide (MIPC) to form mannosyl diphosphorylinositol ceramide (M(IP)2C), the major sphingolipid in membranes of S.cerevisiae.
Fails to accumulate M(IP)2C and instead accumulates increased amounts of the precursor mannose-inositol-P-ceramide.
Component of the SPS-sensor system, which regulates the expression of several amino acid-metabolizing enzymes and amino acid- and peptide-permeases in response to extracellular amino acid levels by controlling the activity of two transcription factors, STP1 and STP2.
Homodimer. Component of the plasma membrane SPS (SSY1-PTR3-SSY5) amino acid sensor complex. Interacts directly with SSY1 and SSY5.
Hyperphosphorylated in response to extracellular amino acids and dependent on the amino acid sensor component SSY1. Phosphorylation is positively regulated by casein kinases YCK1 and YCK2, and negatively regulated by phosphatase PP2A regulatory subunit RTS1.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.
Catalyzes the formation of 5-methyl-uridine at position 54 (m5U54) in all tRNA. May also have a role in tRNA stabilization or maturation.
Cloning artifact which fused this protein with RHO4.
It is uncertain whether Met-1, Met-38, Met-71, Met-77 or Met-82 is the initiator.
Was originally thought to be an endo-exonuclease.
Homodimer (PubMed:29087344). Interacts with NTH1 (via N-terminus when phosphorylated by PKA); the interaction is direct and activates NTH1 (PubMed:29087344, PubMed:22320399). Interacts with FIN1 (PubMed:12551942).
Component of the heterotrimeric CDC48-NPL4-UFD1 ATPase complex (PubMed:16873066). The CDC48-NPL4-UFD1 ATPase complex interacts with the HRD1 ubiquitin ligase complex composed of the E3 ligase HRD1, its cofactors HRD3, USA1 and DER1, substrate recruiting factor YOS9 and CDC48-binding protein UBX2 (PubMed:16873066). Interaction between the complexes is mediated by interaction between CDC48-NPL4-UFD1 complex member CDC48 and HRD1 complex member UBX2 (PubMed:16873066). Forms a complex composed of CDC48, NPL4, UFD1, DOA1, SHP1 and deubiquitinase OTU1 (PubMed:16427015). Interacts with NPL4, CDC48 and UBX2 (PubMed:11733065, PubMed:11598205, PubMed:16873066).
Functions at a post-ubiquitation step in the ubiquitin fusion degradation (UFD) pathway. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway. Required for the proteasome-dependent processing/activation of MGA2 and SPT23 transcription factors leading to the subsequent expression of OLE1. Has an additional role in the turnover of OLE1 where it targets ubiquitinated OLE1 and other proteins to the ERAD.
Present with 3530 molecules/cell in log phase SD medium.
Serine/threonine protein kinase required for spore wall development.
Homohexamer and homotetramer. Interacts with TOM40 preferentially in an unfolded, unphosphorylated form.
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (PubMed:5793714). Required for repair of UV radiation- and etoposide-induced DNA damage (PubMed:18983998).
It is uncertain whether Met-1 or Met-13 is the initiator.
Belongs to the V-ATPase F subunit family.
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:7929071). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:7929071).
Belongs to the methyltransferase superfamily. METTL18 family.
Loss of Protein-histidine methylation (PubMed:24865971). Impaired early rRNA processing, resulting in a deficiency of 60S subunits and translation initiation defects (PubMed:24865971). A haploid deletion mutant leads to hypersensitivity to echinocandin-like antifungal lipopeptide caspofungin, a 1,3-beta-glucan synthase inhibitor. Deletion confers sensitivity to the synthetic tripeptide arsenical 4-(N-(S-glutathionylacetyl)amino) phenylarsenoxide (GSAO) (PubMed:15166135).
Protein-histidine N-methyltransferase that mediates methylation of RPL3 at 'His-243' (PubMed:20864530, PubMed:24865971). Methylates ribosome-associated RPL3, but not free RPL3, thereby regulating 60S subunit assembly (PubMed:24865971, PubMed:26826131). In addition to RPL3, mediates His methylation of other proteins (PubMed:26826131).
Belongs to the glycosyltransferase 2 family.
Endoplasmic reticulum membrane-bound UDP-glucose:dolichyl-phosphate glucosyltransferase involved in protein N-linked glycosylation.
Leads to a loss of UDP-glucose:dolichyl-phosphate glucosyltransferase activity and a concomitant underglycosylation of carboxypeptidase Y.
Present with 5800 molecules/cell in log phase SD medium.
Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 or PEX21 receptors (PubMed:8858167, PubMed:20154681). The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (PubMed:20154681). Mechanistically, PEX5 (or PEX21) receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix (PubMed:20154681).
Interacts (via SH3 domain) with PEX14 (via SH3-binding motif); forming the PEX13-PEX14 docking complex.
Present with 7900 molecules/cell in log phase SD medium.
Belongs to the DNA polymerase type-X family.
Interacts with DNL4 subunit of the DNL4-LIF1 complex.
Repair polymerase. Involved in gap-filling in DNA nonhomologous end joining (NHEJ) required for double-strand break repair. Seems to conduct DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. Preferentially acts upon short gaps formed by the alignment of linear duplexes with complementary single-strand ends. Required for filling gaps that need removal of a 5'- or 3'-terminal mismatch, however lacks nuclease activities.
Stimulated by the interaction with the DNL4-LIF1 complex.
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:7925282). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER (By similarity). The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER (By similarity). Binds the signal recognition particle RNA (7SL RNA), SRP72 binds to this complex subsequently (By similarity). The SRP complex possibly participates in the elongation arrest function (PubMed:7925282).
Heterodimer with SRP72 (By similarity). SRP68-SRP72 heterodimer formation is stabilized by the presence of 7SL RNA (By similarity). Component of a fungal signal recognition particle (SRP) complex that consists of a 7SL RNA molecule (scR1) and at least six protein subunits: SRP72, SRP68, SRP54, SEC65, SRP21 and SRP14 (PubMed:7925282, PubMed:11352936).
Induced during anaerobic growth. Induced by cold shock.
Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate (Probable). Has also an unrelated function in expression of mitochondrial respiration (PubMed:12595523).
Present with 5460 molecules/cell in log phase SD medium.
S-glutathionylation of Cys-56 is reversible and dependent on the cytoplasmic isoform of glutaredoxin-2.
Copper chaperone for cytochrome c oxidase (COX). Binds two copper ions and deliver them to the Cu(A) site of COX.
Component of the HOPS complex which is composed of PEP5, VPS16, PEP3, VPS33, VPS39 and VPS41. HOPS associates with phosphoinositides and the PX domain of VAM7. Interacts with VAM7.
Essential for vacuolar protein sorting. Required for vacuole biogenesis, stability and to maintain vacuole morphology. Required for growth at elevated temperatures. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion.
Activated by Ca(2+) which induces self-processing and is required for the activity of the mature enzyme.
Cysteine protease that cleaves specifically after arginine or lysine residues (PubMed:22761449). Mediates cell death (apoptosis) triggered by oxygen stress, salt stress or chronological aging. Regulated cell death can prevent a release of toxic cellular components, thus avoiding necrotic collapse of the colony, and can also provide nutrients for healthy cells. Therefore, regulated cell death in yeast colonies can be as important for their development as are apoptosis and related processes that occur within metazoa. Promotes the removal of insoluble protein aggregates during normal growth.
Proteolytic cleavage of the propeptide appears to occur after Arg-72 and/or Lys-86; it is not clear how the processing takes place (PubMed:11983181, PubMed:22761449). Proteolytic cleavage after Lys-331 generates a large (p20) and a small (p10) subunits (PubMed:22761449). The small subunit may be further cleaved to give rise to a shorter product starting at Gly-335 (PubMed:22761449).
PubMed:19174511 reported that MCA1 may have a prion form, dubbed [MCA]. However, the same authors have later not been able to reproduce these results and retracted the paper.
The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain. It targets the protein to insoluble protein aggregates.
Activated by tyrosine and threonine phosphorylation.
Dually phosphorylated on Thr-207 and Tyr-209, which activates the enzyme.
Required for spore wall assembly. Required for proper deposition of the two outer layers of the spore wall, the chitosan and dityrosine layers. Negatively regulates GSC2, an alternate catalytic subunit of the 1,3-beta-glucan synthase (GS). Participates in a developmentally regulated signal transduction pathway that coordinates cytodifferentiation events with the transcriptional program.
DNA-binding protein that specifically binds the regulatory region of middle sporulation genes (MSE). Required for the repression of middle sporulation genes during vegetative growth. Represses expression via the recruitment of histone deacetylase HST1.
Interacts with RFM1. This interaction is required to recruit HST1.
Expression in mammalian cells increases survival under conditions inducing apoptosis.
Present with 45200 molecules/cell in log phase SD medium.
Required for survival in response to oxidative stress. Involved in the diauxic shift.
Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with CLF1, PRP22 and PRP46. Interacts with SPP382.
Involved in pre-mRNA splicing. Associated with the spliceosome throughout the splicing reactions, until after the second catalytic step.
Involved in peroxisomal proliferation. Promotes peroxisome division and biogenesis.
Expression is controlled by the transcription factor YRR1.
Required for normal localization of actin patches. Involved in tolerance to sodium ions and hydrogen peroxide.
Belongs to the sulfate adenylyltransferase family.
Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
Expression depends on the formation of the MET4-MET28-MET31 and MET4-MET28-MET32 complexes on its 5' upstream region.
The oligomerization domain is distantly related to APS kinases, but it is not functional and does not bind APS. It is required for oligomerization of the enzyme, although the oligomerization state has no effect on the catalytic activity of the enzyme.
Guanine nucleotide-exchange factor (GEF) required for the formation or budding of transport vesicles from the ER. This function involves the cytoplasmic domain of the protein, which is thought to interact with the small GTP-binding protein SAR1. Required for autophagy.
In the process of transport, SEC12 itself may migrate to the Golgi apparatus and function in subsequent transport events.
Belongs to the non-repetitive/WGA-negative nucleoporin family.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. During mitosis NUP53 changes its binding partner within the NPC from NUP170 to NIC96, exposing a high affinity binding site for the karyopherin PSE1, and retaining it in the NPC.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP170 probably plays an important role in NPC assembly and organization. In addition it is required for chromosome transmission fidelity.
The transcription activation by RCS1 and AST2 depends on the mitochondrial iron-sulfur protein biosynthesis pathway.
Transcription factor required for iron homeostasis and resistance to oxidative stress. With RCS1, activates the gene expression in response to low-iron conditions, also called iron regulon.
Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Required for S phase execution.
Present with 8800 molecules/cell in log phase SD medium.
Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
By allophanate or its non-metabolized analog oxalurate. Sensitive to nitrogen catabolite repression.
Probable protein kinase required for meiotic recombination.
Belongs to the AB hydrolase superfamily. Monoacylglycerol lipase family.
Converts monoacylglycerides (MAG) to free fatty acids and glycerol (PubMed:20554061). Has a strong preference for monounsaturated monoglycerides (PubMed:26869448). Required for efficient degradation of MAG, short-lived intermediates of glycerolipid metabolism which may also function as lipid signaling molecules. Controls inactivation of the signaling lipid N-palmitoylethanolamine (PEA) (PubMed:19529773). Involved in fatty acid ethyl ester (FAEE) catabolism. FAEEs are non-oxidative metabolites of ethanol that are transiently incorporated into lipid droplets (LDs). Their mobilization by LD-resident FAEE hydrolases facilitates a controlled metabolism of these potentially toxic lipid metabolites (PubMed:27036938).
Association between GAL11 and GAL4 may serve to expedite phosphorylation of GAL4.
Binds DNA as a homodimer. Interacts directly with the mediator subunits GAL11/MED15 and SRB4/MED17.
This protein is a positive regulator for the gene expression of the galactose-induced genes such as GAL1, GAL2, GAL7, GAL10, and MEL1 which code for the enzymes used to convert galactose to glucose. It recognizes a 17 base pair sequence in (5'-CGGRNNRCYNYNCNCCG-3') the upstream activating sequence (UAS-G) of these genes.
the 9aaTAD motif (residues 862 to 870) is a transactivation domain present in a large number of yeast and animal transcription factors.
Present with 1280 molecules/cell in log phase SD medium.
Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
Present with 6000 molecules/cell in log phase SD medium.
GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
Present with 25000 molecules/cell in log phase SD medium.
Allosterically regulated by several compounds including AMP, NAD(+), and citrate.
Octamer of two non-identical subunits IDH1 and IDH2.
Performs an essential role in the oxidative function of the citric acid cycle. Also binds RNA; specifically to the 5'-untranslated leaders of mitochondrial mRNAs.
Plays an important role in the degradation of heme under conditions of iron deprivation.
Present with 107000 molecules/cell in log phase SD medium.
Was originally thought to be MFT1, the mitochondrial fusion target protein.
Present with 131 molecules/cell in log phase SD medium.
Inactivated in a complex with phosphatase methylesterase PPE1 (PP2Ai). Interacts with phosphatase 2A activator RRD2, which can reactivate PP2Ai by dissociating the catalytic subunit from the complex. Interacts with TAP42.
Reversibly methyl esterified on Leu-377 by leucine carboxyl methyltransferase 1 (PPM1) and protein phosphatase methylesterase 1 (PPE1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization.
Involved in a late nucleoplasmic step of 60S ribosomal subunit assembly.
Mediates extracellular nucleotide derived phosphate hydrolysis along with NPP1 and PHO5.
Has a role in a late stage of multivesicular body (MVB) formation. Can stimulate VPS4 ATPase activity via VTA1.
Interacts with VTA1; the interaction occurs at he endosomal membrane.
Component of the nucleoplasmic and cytoplasmic pre-60S ribosomal particles. Interacts directly with ARX1.
Present with 4780 molecules/cell in log phase SD medium.
With ARX1, involved in proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Accompanies the pre-60S particles to the cytoplasm.
Belongs to the PPP phosphatase family. PP-1 subfamily.
Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation.
Involved in control of glycogen metabolism, meiosis, translation, chromosome segregation, cell polarity and G2/M cell cycle progression. PP1 may act in opposition to the IPL1 protein kinase in regulating chromosome segregation by dephosphorylating H3S10ph. The BUD14-GLC7 complex is necessary to regulate microtubule dynamics at the cortex and may function as a specific activator of the dynein complex.
Probably complexed with regulatory or targeting subunits (PubMed:12819204). Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1 (PubMed:12819204). Component of the APT complex, which is a subcomplex of CPF, and is composed of PTI1, SYC1, SSU72, GLC7, REF2, PTA1 and SWD2 (PubMed:12819204). Interacts with BUD14 (PubMed:12477789, PubMed:16107882). Interacts with YPI1 (PubMed:14690591). Interacts with SCD5 (via KKVRF motif) (PubMed:12356757).
Belongs to the STE12 transcription factor family.
Binds to the DNA sequence mediating pheromone induction (called the pheromone response element = PRE) which is found in the upstream control region of several a-, alpha- and haploid-specific genes. Involved in mating of haploids and in pseudohyphae formation in diploids.
Interacts with mating-type protein ALPHA1.
Phosphorylated by the STE7, STE11 and STE20 kinases.
The DNA-binding domain seems to be involved in the suppression of pseudohyphae formation under nitrogen-rich conditions and in haploids. This region is also involved in the regulation of budding pattern of haploids.
Transcription factor that represses the expression of HEM13, COX5B, ANB1, CYC7 or AAC3 (hypoxic function). Binds to the DNA sequence 5'-RRRTAACAAGAG-3'.
Belongs to the DNA mismatch repair MutS family. MSH3 subfamily.
Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS beta, which binds to DNA mismatches thereby initiating DNA repair. MSH3 provides substrate-binding and substrate specificity to the complex. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. Acts mainly to repair insertion-deletion loops (IDLs) from 2 to 13 nucleotides in size, but can also repair base-base and single insertion-deletion mismatches that occur during replication. After mismatch binding, forms a ternary complex with either the MutL alpha or MutL beta heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. MutS beta also has a role in regulation of heteroduplex formation during mitotic and meiotic recombination. MutS beta binds to DNA flap structures predicted to form during recombination, and is required for 3' non-homologous tail removal (NHTR). MutS beta-binding alters the DNA conformation of its substrate at the ds/ssDNA junction and may facilitate its recognition and/or cleavage by the downstream nucleotide excision repair (NER) RAD1-RAD10 endonuclease. ATP binding and hydrolysis play a pivotal role in MMR and NHTR.
Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a ternary complex with either MutL alpha (MLH1-PMS1) or MutL beta (MLH1-MLH3). MutS beta interacts with proliferating cell nuclear antigen (PCNA/POL30). Interacts with SAW1.
Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) and 5-bromodeoxyuridine 5'-triphosphate (BrdUTP) to their respective monophosphate derivatives. Xanthosine 5'-triphosphate (XTP) is also a potential substrate. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Catalytic component of the ISW2 complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW2 complex is involved in coordinating transcriptional repression and in inheritance of telomeric silencing. It is involved in repression of MAT a-specific genes, INO1, and early meiotic genes during mitotic growth dependent upon transcription factor UME6 and in a parallel pathway to the RPD3-SIN3 histone deacetylase complex.
Component of the ISW2 complex, which at least consists of ISW2, ITC1, DLS1 and DPB4. May form a stable subcomplex with ITC1.
Belongs to the LAGLIDADG endonuclease family.
Endonuclease aI5 beta (group I intron) is encoded within an intron of the mitochondrial COX1 gene. Splicing from COX1 requires PET54, MRS1, SUV3 and MSS18. Translational initiation codon is predicted to be ATA rather than ATG.
Mitochondrial DNA endonuclease involved in intron homing.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family.
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports the calcium to the vacuole and participates in the control of the cytosolic free calcium.
ATP-dependent chaperone which probably uses the energy provided by ATP hydrolysis to generate mechanical force to unfold substrate proteins, disassemble protein complexes, and disaggregate protein aggregates (PubMed:21454554, PubMed:31445887). By recruiting and promoting the degradation of ubiquitinated proteins, plays a role in the ubiquitin fusion degradation (UFD) pathway (PubMed:16428438). Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway which mediates the cytoplasmic elimination of misfolded proteins exported from the ER (PubMed:11813000, PubMed:11740563, PubMed:11847109, PubMed:21148305). Required for the proteasome-dependent processing/activation of MGA2 and SPT23 transcription factors leading to the subsequent expression of OLE1 (PubMed:11847109, PubMed:11733065). Has an additional role in the turnover of OLE1 where it targets ubiquitinated OLE1 and other proteins to the ERAD (PubMed:11847109). Regulates ubiquitin-mediated mitochondria protein degradation (PubMed:21070972, PubMed:27044889). Involved in spindle disassembly probably by promoting the degradation of spindle assembly factors ASE1 and CDC5 at the end of mitosis (PubMed:14636562). Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation (PubMed:23178123, PubMed:24261871). CDC48 may provide the mechanical force that dislodges the polyubiquitinated nascent peptides from the exit channel (PubMed:23178123, PubMed:24261871). Required for ribophagy, a process which relocalizes ribosomal particles into the vacuole for degradation in response to starvation (PubMed:20508643). Component of the DSC E3 ubiquitin ligase complexes that tag proteins present in Golgi, endosome and vacuole membranes and function in protein homeostasis under non-stress conditions and support a role in protein quality control (PubMed:29355480). Substrate initially binds through the attached polyubiquitin chain to UDF1/NPL4 and then moves through the pore of the ATPase rings and is thereby unfolded (PubMed:31249135, PubMed:31249134). Acts on a broad range of even well-folded proteins via ubiquitin-binding and unfolding to initiate substrate processing (PubMed:31249135). Involved in degradation of mislocalized tail-anchored transmembrane proteins extracted from the mitochondrion outer membrane by MSP1 and ubiquitinated by DOA10 (PubMed:31445887).
Component of the heterotrimeric CDC48-NPL4-UFD1 ATPase complex (PubMed:16873066). The CDC48-NPL4-UFD1 ATPase complex interacts with the HRD1 ubiquitin ligase complex composed of the E3 ligase HRD1, its cofactors HRD3, USA1 and DER1, substrate recruiting factor YOS9 and CDC48-binding protein UBX2 (PubMed:16873066). Interaction between the complexes is mediated by interaction between CDC48-NPL4-UFD1 complex member CDC48 and HRD1 complex member UBX2 (PubMed:16873066). Forms a complex composed of CDC48, NPL4, UFD1, UFD2 and SHP1 (PubMed:16427015). Forms a complex composed of CDC48, NPL4, UFD1, DOA1, SHP1 and deubiquitinase OTU1; within the complex interacts with DOA1/UFD3 and OTU1 to prevent multiubiquitination of substrates (PubMed:16427015). Interacts with UFD2, to add further ubiquitin moieties; the interaction with UFD2 is prevented by DOA1/UFD3 (PubMed:16427015). Forms a complex composed of CDC48, DOA1, deubiquitinase UBP3 and probably BRE5; within the complex interacts with DOA1 and UBP3 (PubMed:20508643). Interacts (via C-terminus) with DOA1 (via PUL domain); the interaction is direct (PubMed:16428438, PubMed:19805280, PubMed:27044889). Interacts with NPL4 (PubMed:11733065, PubMed:11598205, PubMed:31249134). Interacts with SHP1/UBX1, UBX2, UBX3, UBX4, UBX5, UBX6 and UBX7 (PubMed:15258615, PubMed:31249134). Interacts with VMS1; the interaction recruits CDC48 to the mitochondria in response to mitochondrial stress (PubMed:21070972, PubMed:21148305). Component of the ribosome quality control complex (RQC), composed of the E3 ubiquitin ligase RKR1/LTN1, RQC1 and RQC2, as well as CDC48 and its ubiquitin-binding cofactors (PubMed:23178123, PubMed:23479637). RQC forms a stable complex with 60S ribosomal subunits (PubMed:23178123, PubMed:23479637). Interacts with ASE1 and CDC5; the interaction is likely to result in their degradation (PubMed:14636562). Component of the DSCc E3 ligase complexes composed of at least TUL1, DSC2, DSC3, UBX3, CDC48 as well as VLD1 for the vacuole-localized complex or GLD1 for the Golgi/endosome-localized complex (PubMed:29355480).
Present with 78400 molecules/cell in log phase SD medium.
The first ATP-binding region has low ATPase activity (By similarity). The second ATP-binding region is responsible for ATPase activity (By similarity). ATP binding to the first ATP-binding region induces intrinsic activity of the second ATP-binding region (PubMed:21454554). While ATP binding to the first ATP-binding region appears to prevent ATP hydrolysis by the second ATP-binding region, ADP-binding to first region promotes the coordinate and cooperative ATPase cycle of the second ATP-binding region (By similarity). ATP binding to the first ATP-binding region induces a conformational change, promoting the rotation of the first ATP-binding region relative to the second ATP-binding region in the hexamer (By similarity).
Glucanases possibly play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase.
Present with 45000 molecules/cell in log phase SD medium.
This protein strongly binds to glucan and chitin.
May function as a positive regulator for mannosylphosphate transferase. Is required to mediate mannosylphosphate transfer in both the core and outer chain portions of N-linked oligosaccharides.
Essential for the assembly of the mitochondrial F1-F0 complex. May interact with the alpha and/or beta subunits of F1-ATPase.
Belongs to the MID2 like cell wall stress sensor family.
Involved in cell integrity signaling during vegetative growth at elevated temperature. Acts positively on the PKC1-MAPK pathway. Cell membrane sensor of oxidative stress in the cell integrity pathway upstream of PKC1. Required to transmit the oxidative signal to SLT2 and to restore the correct actin organization following oxidative stress. Multicopy suppressor of 1,3-beta-glucan synthase (GS) mutation. Also suppresses RGD1 null mutations.
Able to autophosphorylate in cis in vitro. This activity may not be relevant in vivo and only reflects in vitro conditions. Probably does not act as a protein kinase as it is unable to act in trans (PubMed:27499294).
Adopts an atypical protein kinase-like fold: while it adopts a core fold similar to that of well-characterized protein kinase-like domains. The KxGQ motif completely occludes the typical substrate binding pocket. Nucleotide-binding opens the substrate binding pocket and flips the active site from inside the hydrophobic core into a catalytically competent, solvent-exposed posture.
Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration (PubMed:27499294). Affects the molecular organization and function of COQ3, possibly through kinase activity towards COQ3, COQ5 and/or COQ7 (PubMed:11279158, PubMed:15063807, PubMed:1648478, PubMed:18801050, PubMed:19002377, PubMed:21296186, PubMed:9210471, PubMed:9266513, PubMed:25498144). Its substrate specificity is unclear: does not show any protein kinase activity (PubMed:27499294). Probably acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway, as suggested by its ability to bind coenzyme Q lipid intermediates (By similarity).
Decreases COQ3 O-methyltransferase activity.
Forms homopolymers. Predominantly associated with a complex of about 500 kDa.
Was originally (PubMed:1648478) isolated as a multicopy suppressor of a yeast strain harboring a mutation in a cytochrome b translational activator (cbs2-223). But more recently it has been shown (PubMed:15063807) that a tRNA(Trp) gene located downstream of COQ8 mediates suppression of the cbs2-223 mutation. The inability of COQ8 to suppress the cbs2-223 allele in multicopy indicates it may not be a chaperone as previously reported.
Involved in DNA double-strand break repair (DSBR). Possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity. Also involved in meiotic DSB processing.
Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Belongs to the ALG10 glucosyltransferase family.
Present with 3920 molecules/cell in log phase SD medium.
Fungal signal recognition particle (SRP) complex consists of a 7S RNA molecule (scR1) and at least six protein subunits: SRP72, SRP68, SRP54, SEC65, SRP21 and SRP14.
Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the arrest of nascent chain elongation during membrane targeting. SEC65 is required for SRP integrity.
Component of the DOA10 ubiquitin ligase complex which contains E3 ligase SSM4/DOA10 and CDC48-binding protein UBX2/SEL1. The DOA10 complex interacts with the heterotrimeric CDC48-NPL4-UFD1 ATPase complex which is recruited by UBX2/SEL1 via its interaction with CDC48. Interacts with its associated ubiquitin conjugating enzymes UBC6 and UBC7 with its membrane anchor CUE1. Interacts with PEX29.
E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC6 and UBC7 E2 ligases, and transfers it to substrates promoting their degradation (PubMed:11641273, PubMed:16179952, PubMed:16437165, PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468). Mediates the degradation of a broad range of substrates, including endoplasmic reticulum membrane proteins (ERQC), soluble nuclear proteins and soluble cytoplasmic proteins (CytoQC) (PubMed:11641273, PubMed:16179952, PubMed:16437165, PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468). Component of the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains (PubMed:16873066). ERAD-C substrates are ubiquitinated through DOA10 in conjunction with the E2 ubiquitin-conjugating enzymes UBC6 and UBC7-CUE1 (PubMed:11641273, PubMed:16179952, PubMed:16437165, PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468). Ubiquitinated substrates are then removed to the cytosol via the action of the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex and targeted to the proteasome (PubMed:11641273, PubMed:16179952, PubMed:16437165, PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468). Also recognizes the N-terminally acetylated residue of proteins as degradation signal (degron) (PubMed:20110468). N-terminally acetylated target proteins include MATALPHA2, TBF1, SLK19, YMR090W, HIS3, HSP104, UBP6 and ARO8 (PubMed:20110468). Catalyzes ubiquitination of mislocalized tail-anchored proteins that are extracted from the mitochondrion membrane by MSP1: following extraction, mistargeted proteins are transferred to the endoplasmic reticulum, where they are ubiquitinated by DOA10 and degraded by the proteasome (PubMed:31445887).
The RING-CH-type zinc finger domain is required for E3 ligase activity.
Belongs to the ETF beta-subunit/FixA family.
Displays higher growth rate and higher sensitivity to superoxide and heat stress, on nonfermentable carbon sources. Leads to decreased intracellular oxidation upon heat shock. Under conditions of mitochondrial perturbation by antimycin A, displays increased peroxisomal proliferation.
Heterodimer of an alpha and a beta subunit (By similarity). Interacts with YFH1.
The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).
Associates with the hexameric DNA polymerase alpha.
DNA polymerase alpha-associated DNA helicase which may be involved in DNA replication.
Expression peaks in S-phase (at the RNA level).
Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly (PubMed:16936140, PubMed:16678113, PubMed:16407267, PubMed:16039596, PubMed:15891116, PubMed:16303565, PubMed:15766286, PubMed:15542829, PubMed:15175160, PubMed:15452122, PubMed:15071494, PubMed:11856374, PubMed:11404324, PubMed:11331602, PubMed:11172707, PubMed:14680630). Facilitates histone deposition through both replication-dependent and replication-independent chromatin assembly pathways (PubMed:14585955, PubMed:16678113, PubMed:15632066). Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with the HIR complex to promote replication-independent chromatin assembly, which may occur during transcription and DNA repair (PubMed:16501045, PubMed:16582440, PubMed:16141196, PubMed:16143623, PubMed:16020781, PubMed:15821127, PubMed:16303565, PubMed:15542840, PubMed:12093919, PubMed:11756556, PubMed:11404324, PubMed:11731480, PubMed:11731479, PubMed:11412995, PubMed:10591219). May be required for the maintenance of a subset of replication elongation factors, including DNA polymerase epsilon, the RFC complex and PCNA, at stalled replication forks (PubMed:15901673, PubMed:11412995). Also required for RTT109-dependent acetylation of histone H3 on 'Lys-9' and 'Lys-56' (PubMed:17320445, PubMed:17107956, PubMed:17046836, PubMed:16815704, PubMed:16627621, PubMed:15840725, PubMed:21256037). Promotion of RTT109-mediated histone H3 'Lys-56' acetylation is dependent on interactions with histone H3 pre-acetylated on 'Lys-14' (PubMed:31194870).
Interacts with histone H3/H4 heterodimers via both histone H3 and histone H4 (PubMed:11172707, PubMed:11412995, PubMed:11856374, PubMed:11756556, PubMed:12626510, PubMed:16303565, PubMed:15840725, PubMed:16582440, PubMed:14680630, PubMed:17081973, PubMed:31387991, PubMed:29300933, PubMed:27036862). Binds with higher affinity to H3/H4 heterodimers where histone H3 has been pre-acetylated on 'Lys-14' (PubMed:31194870). Interacts with RAD53 and this may impair interaction with histones and chromatin assembly; the interaction is reduced upon activation of DNA damage or replication checkpoints which in turn promotes histone binding and chromatin assembly (PubMed:11331602, PubMed:12851493, PubMed:12917350, PubMed:16303565, PubMed:16020781, PubMed:14680630). Interacts with the CAC2 subunit of chromatin assembly factor 1 (CAF-1) (PubMed:11756556). Interacts with the HIR1, HIR2, HIR3 and HPC2 subunits of the HIR complex (PubMed:11404324, PubMed:11412995, PubMed:16303565). Interacts with the RFC1, RFC2, RFC3, RFC4 and RFC5 subunits of the replication factor C (RF-C/RFC) complex; which may recruit this protein to DNA (PubMed:15901673). Interacts with the SAS2, SAS4 and SAS5 subunits of the SAS/SAS-I complex (PubMed:11731479, PubMed:11731480). Interacts with the BDF1, BDF2, SPT15, TAF1 and TAF7 subunits of the TFIID complex (PubMed:12093919). Interacts with RTT109 and VPS75; the interaction with RTT109 is direct (PubMed:29300933, PubMed:31387991, PubMed:17320445).
Tube-forming lipid transport protein which binds to phosphatidylinositols and affects phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P2) distribution.
Assembly factor that plays a role in the assembly of the respiratory chain supercomplexes (SCs) composed of ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV). May be required for late-stage assembly of the COX12 and COX13 subunits (PubMed:22342701, PubMed:22310663). Required for the generation and maintenance of a normal proton motive force (PMF) across the inner mitochondrial membrane (IMM) by preventing proton leakage through an inactive population of CIV that accumulates when RCF1 and/or RCF2 proteins are absent (PubMed:30683696, PubMed:31591265).
Associates with a subpopulation of the cytochrome bc1-cytochrome c oxidase supercomplexes (PubMed:19750512, PubMed:22342701, PubMed:22310663). Associates in substoichiometric amounts with complex IV (PubMed:22310663). Interacts with COX3 (PubMed:22310663).
General activator of RNA polymerase III transcription.
TFIIIB comprises the TATA-binding protein (TBP), the B-related factor (BRF) and the B'' component (BDP1). Interacts with TFC4.
Causes conditional lethality. Strains bearing this mutation do not grow at temperatures exceeding 30 degrees Celsius.
GTPase activator for the nuclear Ras-related regulatory protein GSP1 (Ran), converting it to the putatively inactive GDP-bound state.
Present with 52200 molecules/cell in log phase SD medium.
Causes only a modest decline in CLB2 cluster genes expression, but this expression is abolished when both FKH1 and FKH2 are deleted (PubMed:10959837). Leads to a defect in silencing HMRa (PubMed:10747051). Causes a form of yeast pseudohyphal growth, when FKH2 is also deleted (PubMed:10747051). Affects cell-cycle progression and CLB2 mRNA expression (PubMed:10747051). Leads to defect in pre-mRNA 3' end formation during transcription of targeted genes (PubMed:12702877).
Interacts (via FHA domain) with ECM30, GLN3, URE2, MPH1 AND FDO1 (PubMed:27257873). Interacts with the origin recognition complex (ORC) composed of ORC1 to ORC6 (PubMed:22265405).
The phosphothreonine-binding FHA domain is required for the interaction with MPH1 and controlling recombination donor preference during mating-type switching.
Transcription factor that regulates the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle (PubMed:10959837, PubMed:10894548, PubMed:10894549, PubMed:11562353, PubMed:12702877, PubMed:17283050, PubMed:24504085). The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20 as well as SWI5 and ACE2, transcription factors required for the subsequent temporal wave of cell cycle regulated gene expression in the M/G1 phase interval (PubMed:10959837, PubMed:10894548, PubMed:11562353). Involved in HMRa silencing (PubMed:10747051). FKH1 and FKH2 associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing (PubMed:12702877). Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation (PubMed:22438832). FKH1 and FKH2 function also in controlling yeast cell morphology by preventing preudohyphal growth (PubMed:10747051, PubMed:10894548). Acts as a rate-limiting replication origin activator via its interactin with the origin recognition complex (ORC) (PubMed:22265405, PubMed:26728715). Plays a transcription-independent role in recombination donor preference during mating-type switching through binding to the recombination enhancer (RE), a 700-bp cis-acting element that controls recombination along the left arm of chromosome III (PubMed:12183363, PubMed:16809780, PubMed:22496671, PubMed:27257873).
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. PCC1 functions as a dimerization module for the complex. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Component of the transcription complex MCB-binding factor (MBF) composed of SWI6 and MBP1. Component of the transcription complex SCB-binding factor (SBF) composed of SWI6 and SWI4. Interacts with MSA1 and STB1.
Phosphorylated by CDC28 and dephosphorylated by CDC14.
Activated by phytosphingosine (PHS), a sphingoid long chain base. Activated by PKH1 phosphorylation.
Autophosphorylated. Autophosphorylation is stimulated by PHS. Phosphorylated by PKH1. PHS stimulates phosphorylation by PKH1. The N-terminal half is phosphorylated by FPK1.
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.
Plays an essential role in the proliferation of yeast cells. Involved in a signaling pathway, required for optimal cell wall integrity, that acts in parallel with the PKC1-SLT2-dependent pathway. Downstream kinase in the sphingolipid-mediated signaling pathway. Its phosphorylation is regulated by the intracellular sphingolipid concentration. Cooperates with SLI1 in mediating resistance to the sphingolipid biosynthesis inhibitor drug myriocin (ISP-1). Its kinase activity is essential for the resistance. Required for both receptor-mediated and fluid-phase endocytosis, but is not necessary for receptor phosphorylation or ubiquitination. Necessary for the internalization of plasma membrane proteins carrying different types of internalization signals. Acts downstream of the PKH kinases to control endocytosis by phosphorylating components of the endocytic machinery. Phosphorylation of residue Thr-504 in the activation loop is essential for activity. phosphorylates and down-regulates flippase activator FPK1.
Catalyzes the phosphorylation of the sphingoid long chain bases dihydrosphingosine (DHS or sphinganine) and phytosphingosine (PHS) to form dihydrosphingosine 1-phosphate (DHS-1P) and phytosphingosine 1-phosphate (PHS-1P) respectively (PubMed:9677363, PubMed:11102354, PubMed:11795842, PubMed:16141212, PubMed:25345524). Involved in the biosynthesis of sphingolipids and ceramides (PubMed:12493772). Required with LCB3 for an effective incorporation of DHS into ceramides through a phosphorylation-dephosphorylation cycle. Involved in heat-induced transient cell cycle arrest (PubMed:11056159). Accumulation of phosphorylated sphingoid long chain bases (LCBPs) stimulates calcium influx and activates calcineurin signaling (PubMed:11278643). Involved in heat-stress resistance (PubMed:11967828).
Completely abolishes the conversion of phytosphingosin to glycerophospholipid.
Palmitoylated by palmitoyltransferase AKR1; this anchors the protein to the plasma membrane.
Phosphorylated by the cyclin-CDKs PCL1-PHO85 and PCL2-PHO85. Phosphorylation is a prerequisite to ubiquitination. The phosphorylation level depends on sterol composition and may also be involved in subcellular location (PubMed:16141212).
Ubiquitinated. The ubiquitination leads to degradation in the vacuole.
Belongs to the TRAFAC class translation factor GTPase superfamily. Bms1-like GTPase family. TSR1 subfamily.
Required for 40S ribosomal subunit synthesis. Required for normal export of the pre-40S particles from the nucleus to the cytoplasm. Its subcellular location and association with pre-40S subunitshifts from mixed cytoplasm/nucleus to all nuclear in RPS19 disruptions, suggesting it acts after the ribosomal protein.
Formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of transfer RNAs; at positions 34 and 36 of intron-containing precursor tRNA(Ile) and at position 35 in the intron-containing tRNA(Tyr) (PubMed:9671058, PubMed:10356324, PubMed:25219674). Catalyzes pseudouridylation at position 44 in U2 snRNA (PubMed:25219674). Also catalyzes pseudouridylation of mRNAs (PubMed:25219674, PubMed:31477916).
Present with 8130 molecules/cell in log phase SD medium.
Identified in the Set3C complex with HOS2, HST1, SNT1, SIF2, CPR1 and HOS4/YIL112W.
Transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. Required for both gene activation and repression. Part of the Set3C complex, which is required to repress early/middle sporulation genes during meiosis. Required for the transcriptional activation of genes with high activity.
Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 snRNP, U4/U6.U5 snRNP, and free U6 snRNP). It binds directly to the U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. It probably also is involved in degradation of nuclear pre-mRNA by targeting them for decapping. LSM3 binds specifically to the 3'-terminal U-tract of U6 snRNA. LSM2-LSM8 probably is involved in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM3, probably in a complex that contains LSM2-LSM7 but not LSM1 or LSM8, associates with the precursor of the RNA component of RNase P (pre-P RNA) and may be involved in maturing pre-P RNA. LSM3 is required for processing of pre-tRNAs, pre-rRNAs and U3 snoRNA.
Component of the heptameric LSM1-LSM7 complex that forms a seven-membered ring structure with a doughnut shape. The LSm subunits are arranged in the order LSM1, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. Except for LSM1, where a C-terminal helix crosses the ring structure to form additional interactions with LSM3 and LSM6, each subunit interacts only with its two neighboring subunits. The LSM1-LSM7 complex interacts with PAT1; within the complex PAT1 has direct interactions with LSM2 and LSM3. Component of the heptameric LSM2-LSM8 complex that forms a seven-membered ring structure with a doughnut shape; an RNA strand can pass through the hole in the center of the ring structure. The LSm subunits are arranged in the order LSM8, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. LSM2-LSM8 associates with PAT1 and XRN1. A complex comprising LSM2-LSM7 without LSM1 or LSM8 may exist. Likewise, LSM2 and LSM3 can assemble into a doughnut structure that binds PAT1 (in vitro). Besides, LSM3 can form a homooctameric ring (in vitro). Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
Exoribonuclease involved in ribosome biosynthesis. Involved in the processing of ITS1, the internal transcribed spacer localized between the 18S and 5.8S rRNAs.
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. FDH subfamily.
Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms (PubMed:9178506, PubMed:12144528, PubMed:11921099). Has a role in the detoxification of exogenous formate in non-methylotrophic organisms (PubMed:11921099).
Has a temperature-sensitive growth defect in glucose-rich medium, with slower growth and smaller colonies at 37 degrees Celsius but not 30 degrees Celsius; the phenotype is suppressed by overexpression of YHM2.
Specific binding to the autonomously replicating sequence 1 (ARS1). Interaction with regulatory regions: probably involved in compacting the mitochondrial genome. It might play a positive role in gene expression and replication.
May be associated with hnRNA within the nucleus and remains associated during nucleocytoplasmic mRNA transport, once the proteins are in the cytoplasm, disassembly of PUB1-RNA complexes may occur prior to PAB1 binding and formation of a translationally competent RNP complex. Binds to polyadenylated RNA; prefers to bind poly(rU); binds to T-rich single-stranded DNA.
Present with 49600 molecules/cell in log phase SD medium.
Component of the TTT complex composed of TEL2, TTI1 and TTI2. Interacts with TTI1 and TTI2.
Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins (By similarity). Required for telomere length regulation and telomere position effect. Regulates telomere length and participates in gene silencing at subtelomeric regions. Binds to telomeric DNA repeats.
Present with 638 molecules/cell in log phase SD medium.
Involved in the assembly of mitochondrial and cytoplasmic iron-sulfur proteins. Probably involved in the binding of an intermediate of Fe/S cluster assembly.
The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. APC1 interacts directly with MND2.
Catalyzes the attachment of methionine to tRNA(Met) in the mitochondrion.
Acyl-CoA synthetase required for both the import of long chain fatty acids (LCFAs) (C14-C18) and the activation very long chain fatty acids (VLCFAs) (C20-C26) by esterification of the fatty acids into metabolically active CoA-thioesters for subsequent degradation or incorporation into phospholipids (PubMed:9079682, PubMed:11330068, PubMed:9988704, PubMed:12052836, PubMed:12601005). The transport and fatty acyl-CoA synthetase activities are genetically separable and are thus independent activities (PubMed:12052836). Esterifies VLCFAs in the peroxisome matrix. The VLCFAs are actively transported into peroxisomes by a PXA1-PXA2 heterodimeric transporter in the peroxisomal membrane (PubMed:22493507).
Interacts with fatty acyl-CoA synthetases FAA1 and FAA4.
Essential for the assembly of ubiquinol-cytochrome c reductase. It has a direct effect on the correct occurrence of the Rieske protein, core 4, core 5 and apocytochrome b.
Component of the TFIIIC complex composed of TFC1, TFC3, TFC4, TFC6, TFC7 and TFC8. The subunits are organized in two globular domains, tauA and tauB, connected by a proteolysis-sensitive and flexible linker. Interacts with TFC1, TFC3, TFC6, TFIIIB subunits BRF1 and BDP1, and with RNA polymerase III subunit RPC10.
TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and similar genes. TFC4 is the TFIIIB-assembling subunit of TFIIIC and essential for viability.
Component of the outer cell wall layer. Required for stability of the cell wall and for optimal growth. Required for resistance against several antifungal and cell wall-perturbing agents.
Covalently linked to beta-1,3-glucan of the inner cell wall layer via an alkali-sensitive ester linkage between the gamma-carboxyl group of glutamic acid, arising from Gln-74 within the PIR1/2/3 repeat, and hydroxyl groups of glucoses of beta-1,3-glucan chains.
Extensively O-mannosylated. Also N-glycosylated.
Positively regulated by signaling through MPK1 in response to cell wall perturbation.
The PIR1/2/3 repeat is required for the covalent linkage to the cell wall.
Cell cycle-regulated. Expression peaks during S/G2 phase.
Has a partially redundant function to WHI3, a dosage-dependent modulator of cell size.
Channel protein that mediates glycerol entry under ethanol stimulation (PubMed:12832087). Does not seem to mediate glycerol uptake under standard conditions (PubMed:12832087).
Decreases the gylcerol uptake in presence of ethanol.
Belongs to the mitochondrion-specific ribosomal protein mL53 family.
Required for a novel path of interorganelle communication between mitochondria, peroxisomes and the nucleus, thereby maintaining a functional metabolic interaction between the tricarboxylic acid and glyoxylate cycles. Transcription factor that regulates CIT2 gene expression. Binds to two identical sites oriented as inverted repeats 28 bp apart in a regulatory upstream activation sequence element (UASR) in the CIT2 promoter. The core binding site is 5'-GGTCAC-3'.
PP2A exists in several trimeric forms, all of which consist of a core composed of a catalytic subunit associated with a 65 kDa (PR65) (Subunit A) and a 55 kDa (PR55) (Subunit B) regulatory subunit. Interacts with YND1; this interaction mediates adenovirus E4orf4 (early region 4 open reading frame 4) induced toxicity and is disrupted by adenovirus E4orf4, which remains associated with both CDC55 and YND1.
Present with 8600 molecules/cell in log phase SD medium.
Belongs to the eukaryotic-type primase large subunit family.
DNA polymerase alpha:primase is a four subunit enzyme complex, which is assembled throughout the cell cycle, and consists of the two DNA polymerase subunits A POL1 and B POL12, and the DNA primase large PRI2 and small PRI1 subunits (PubMed:3061469). Interacts with MCM10 (PubMed:16675460).
Fluctuates in amount during the cell cycle.
Belongs to the type IB topoisomerase family.
In yeast, topoisomerase I seems to be dispensable. This is thought to be due to the abundant presence of topoisomerase II that can substitute for the relaxing activity of topoisomerase I.
Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity).
Increases frequency of mitochondrial genome loss and leads to synthetic letality with a prohibitin complex subunit PHB1 deletant.
Present with 1835 molecules/cell in log phase SD medium.
Forms 200-350 kDa oligomeric complexes independent on heme binding.
Required for the assembly of yeast cytochrome oxidase. Involved in the biosynthesis of heme A and the initial step in this pathway, the hydroxylation of heme O, is thought to be catalyzed by a three-component mono-oxygenase consisting of COX15, ferredoxin YAH1 and ferredoxin reductase ARH1.
Autophosphorylated. Phosphorylation by PKA strongly inhibits kinase activity. Phosphorylation by cyclin-CDK PHO80-PHO85 under favorable growth condition causes inactivation of RIM15 by promoting its export to the cytoplasm.
Interacts with the cyclin-dependent kinase (CDK) PHO85 and IGO1.
Kinase activity is inhibited by phosphorylation by cAMP-dependent protein kinase (PKA).
Protein kinase that positively regulates proper entry into stationary phase of cells under nutrient starvation conditions. Involved in glycogen and trehalose accumulation, derepression of stress-induced genes, induction of thermotolerance and starvation resistance, and proper G1 cell cycle arrest. Also involved in the activation of a meiotic genes activation pathway. Phosphorylates IGO1 and IGO2, both involved in the TORC1 control of gene expression and chronological life span.
Present with 530 molecules/cell in log phase SD medium.
TEC1 is involved in the activation of TY1 and TY1-mediated gene expression. It is not involved in mating or sporulation processes.
Belongs to the mitochondrion-specific ribosomal protein mS29 family.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. mS29 binds GTP and is probably an active GTPase. GTP hydrolysis may be linked to subunit association (PubMed:25609543, PubMed:28154081). mS29 also has an extraribosomal function, being required for maintenance of mitochondrial DNA (PubMed:11017876).
Essential for the assembly of the mitochondrial F1-F0 complex.
Mutations in ATP10 induce a loss of rutamycin sensitivity of mitochondrial ATPase.
Required for survival at high temperature during stationary phase.
Belongs to the DEAD box helicase family. DDX48/FAL1 subfamily.
Component of the glycine decarboxylase complex (GDC), which is composed of four proteins: P, T, L and H.
Induced by glycine and repressed by the C1 metabolic end products.
The glycine cleavage system (glycine decarboxylase complex) catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (By similarity).
Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Its predominant cargo substrate seems to be ribosomal proteins (PubMed:9321403). Required for import of the ribosomal assembly factor NMD3 (PubMed:12612077). May be involved in nuclear transport of YAP1 (PubMed:11274141). Mediates the nuclear import of histones H3 and H4 (PubMed:11694505). Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins. The complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:11423015). At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo (PubMed:9321403). The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:11423015).
Interacts with Ran (GSP1); interacts specifically with the GTP-bound form of Ran (GTP-Ran), protecting it from GTP hydrolysis and nucleotide exchange (PubMed:9321403). Interacts with RPL25; this interaction is dissociated by binding to Ran-GTP (PubMed:9321403). Interacts with YAP1 (PubMed:11274141). Interacts with histones H3 and H4; via their NLS (PubMed:11694505).
By the unfolded protein response pathway. Accumulation of unfolded proteins in the ER leads to activation of IRE1, which initiates splicing of the untranslated HAC1 precursor mRNA to produce the mature form.
Not translated. The unspliced HAC1 mRNA is stable, located in the cytoplasm, and is associated with polyribosomes, yet does not produce protein. Translational attenuation is due to basepairing of the intron with the 5'-UTR of the mRNA.
Transcriptional activator involved in the unfolded protein response (UPR) pathway. Recognizes and binds to the UPR element (UPRE) in the promoter of UPR-regulated genes such as KAR2, PDI1, EUG1 and FKB2. Increases the synthesis of endoplasmic reticulum-resident proteins required for protein folding as well as components of the secretory pathway.
ATP-dependent RNA helicase required for 60S ribosomal subunit synthesis. Involved in efficient pre-rRNA processing, predominantly at site A3, which is necessary for the normal formation of 25S and 5.8S rRNAs.
Present with 38900 molecules/cell in log phase SD medium.
Present with 3080 molecules/cell in log phase SD medium.
The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Interacts with the mitochondrial 54S large ribosomal subunit.
Required for mitochondrial protein synthesis. May be involved in mitochondrial ribosome biogenesis.
Forms a homotrimer with a solvated central pore, which is connected laterally to the cytosol through the cavity within each protomer (By similarity). Acts as a lipid scramblase that uses its central pore to function: the central pore opens laterally to accommodate lipid headgroups, thereby enabling lipid flipping and redistribution of lipids added to the outer leaflet of ATG9-containing vesicles, thereby enabling growth into autophagosomes (By similarity).
Homotrimer; forms a homotrimer with a central pore that forms a path between the two membrane leaflets (PubMed:33106658). Interacts with ATG23 and ATG27 to form a cycling complex for trafficking to the PAS (PubMed:14504273, PubMed:17178909, PubMed:27050455). Interacts (via N-terminus) with ATG11, required for recruitment of ATG9 to the PAS for the Cvt pathway during nutrient-rich conditions (PubMed:17178909, PubMed:17192412, PubMed:19371383, PubMed:31356628). Interacts (via N-terminus) with ATG17; required for recruitment to the PAS during autophagy and starved conditions (PubMed:19371383). Interacts with ATG2 and ATG18; required for the retrieval of ATG9 from the PAS to the cytoplasmic pool (PubMed:11382760, PubMed:14723849, PubMed:24905091, PubMed:24440502). Interacts with ATG41 (PubMed:26565778). Interacts with the conserved oligomeric Golgi (COG) complex subunits COG3 and COG4 (PubMed:20065092). Interacts with TRS85 (PubMed:23129774).
Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation (PubMed:7593182, PubMed:8224160, PubMed:8663607, PubMed:10735854, PubMed:14504273, PubMed:24440502, PubMed:27050455, PubMed:33106658, PubMed:33439214). Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome (PubMed:10662773, PubMed:11689437, PubMed:17329962, PubMed:17426440, PubMed:18829864, PubMed:22826123, PubMed:24905091, PubMed:33439214). Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion (PubMed:33106658, PubMed:32883836, PubMed:33439214). Required for mitophagy (PubMed:18818209). Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress (PubMed:17132049). Recruits vesicle-tethering proteins TRS85 and YPT1 to the autophagosome formation site (PubMed:23129774). Recruits also ATG23 and ATG8 to the PAS (PubMed:14504273).
Phosphorylated by ATG1; phosphorylation is required for autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation (PubMed:24440502). Phosphorylation by ATG1 regulates ATG18 interaction and preautophagosome elongation (PubMed:24905091). Phosphorylation at Ser-122 is required for selective autophagy by regulating anterograde trafficking and interaction with ATG23 and ATG27 (PubMed:27050455, PubMed:33443148). Phosphorylation at Ser-122 prevents ubiquitination by the SCF(MET30) complex (PubMed:33443148).
Ubiquitinated by the SCF(MET30) complex in normal conditions, leading to its degradation by the proteasome, thereby preventing inappropriate induction of autophagy (PubMed:33443148). Ubiquitination by the SCF(MET30) complex is prevented by phosphorylation at Ser-122 (PubMed:33443148).
By the macrolide rapamycin in a TOR-dependent manner.
Protein kinase that functions as regulator in the pheromone-induced mating pathway downstream of mitogen-activated protein kinase (MAPK) FUS3. Diminishes transcriptional induction of genes in response to pheromone signaling.
Involved in mitochondrial distribution and morphology. Mediates the import of UPS1, UPS2 and UPS3, 3 atypical mitochondrial intermembrane space (IMS) proteins lacking the two major IMS-targeting signals, into the intermembrane space. The UPS1:MDM35 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space (PubMed:26071602, PubMed:26071601, PubMed:26235513). Phosphatidic acid import is required for cardiolipin (CL) synthesis in the mitochondrial inner membrane (PubMed:26071602).
Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily.
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). Redundant to LEU4, responsible of about 20% of alpha-IPMS activity. Involved in leucine synthesis.
Present with 28800 molecules/cell in log phase SD medium.
Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. APC5 directly interacts with MND2 and SWM1.
Interacts with YCK1 (PubMed:14755054). Interacts with MTH1 and STD1 (PubMed:27630263).
Low-affinity high glucose sensor that is part of the sensor/receptor-repressor (SSR) glucose-signaling pathway, which detects extracellular glucose and induces expression of glucose transporters that bring glucose into the cell (PubMed:9564039, PubMed:14755054, PubMed:27630263). The transporter-like sensor generates an intracellular signal in the presence of high levels of glucose to promote high glucose-induced expression of HXT1 (PubMed:9564039). Binding of glucose to the RGT2 transmembrane domain activates a downstream signaling cascade, leading to phosphorylation of the RGT1 corepressors MTH1 and STD1, targeting them for SCF(Grr1)-dependent ubiquitination and degradation. Depletion of the corepressors robs RGT1 of its ability to repress expression of HXT genes, leading to accumulation of glucose transporters in the plasma membrane (PubMed:8901598, PubMed:27630263). Even though RGT2 is similar to glucose transporters, it appears to be unable to transport glucose (PubMed:9564039).
Catalyzes the transfer of a phosphate group to glutamate to form glutamate 5-phosphate which rapidly cyclizes to 5-oxoproline.
Expressed at elevated levels early in meiosis. Expression depends on IME1.
Positive regulator of sporulation-specific genes and of sporulation. Required for premeiotic DNA synthesis and meiotic chromosomal segregation. May act in a nutritional signaling pathway.
Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication.
Facilitates protein transport into the nucleus. Interacts with various nucleoporins and with Ran-GDP. Could be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import. In vitro, the NTF2-Ran-GDP association, in the presence of GTP, triggers dissociation of the karyopherin alpha-beta complex, allowing nuclear translocation of karyopherin alpha and the NLS substrate.
Homodimer via the leucine-zipper domain. Forms a complex with a GCR2 homodimer. Interacts with RAP1.
Phosphorylated in a GCR2-dependent manner.
Transcriptional activator required for the expression of glycolytic and ribosomal genes. Forms a transcriptional activation complex with RAP1, RAP1 providing the specific DNA-binding function and GCR1 providing the activation function. Can also bind itself to DNA to a core 5'-CTTCC-3' sequence (CT box). CT box-binding is not essential, but enhances the activation function of the RAP1-GCR1 complex in promoters that contain both DNA signals (only glycolytic genes). CT box-dependent transcriptional activation requires GCR2.
Amino acid sensor component of the SPS-sensor system, which regulates the expression of several amino acid-metabolizing enzymes and amino acid- and peptide-permeases in response to extracellular amino acid levels by controlling the activity of two transcription factors, STP1 and STP2. Amino-acid permease homolog that seems to interact directly with the extracellular signaling molecules, but has no amino acid transporter activity. May recruit casein kinases YCK1 and YCK2 to hyperphosphorylate and activate downstream component PTR3 in response to amino acid stimulus.
Component of the plasma membrane SPS (SSY1-PTR3-SSY5) amino acid sensor complex. Interacts directly with PTR3 and SSY5. Interacts with YCK1.
Binds DNA as a homodimer. Interacts with SRO9 and YDJ1. In the absence of heme, binds to at least four cellular proteins, including YDJ1 and SRO9, forming a high-molecular-weight complex (HMC) which results in repression of its activity and dictates its DNA-binding specificity (By similarity).
Heme is an effector molecule for CYP1/HAP1. The HRM repeat region mediates heme induction by masking the DNA-binding domain in the absence of inducer (By similarity).
Regulation of oxygen dependent gene expression. It modulates the expression of Iso-1 (CYP1) and Iso-2 (CYP3) cytochrome c. In response to heme, promotes transcription of genes encoding functions required for respiration, controlling oxidative damage and repression of anaerobic genes. Binds to the sequence 5'-CGGNNNTNNCGG-3' (By similarity). Is non-functional in terms of iso-1 cytochrome c expression in strain S288c and its derivatives.
The sequence for strain S288c and its derivatives differs from other strain backgrounds due to the insertion of a defective Ty1 element in the C-terminus. This acts as a null allele in terms of iso-1 cytochrome c expression and beta-galactosidase activity. Also, the expression levels of ergosterol-related genes and ergosterol content are decreased in laboratory strain X2180 caused by the defective Ty1 insertion. The sequence of a wild-type allele can be found in other strain backgrounds (AC P0CS82).
Involved in HMR and telomere silencing via the recruitment or stabilizing of the SIR (silent information regulators) complex.
Belongs to the tRNA-aminoacylation cofactor ARC1 family.
Binds to tRNA and functions as a cofactor for the methionyl-tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS). Forms a complex with MetRS and GluRS and increases their affinity for cognate tRNAs due to the presence of a tRNA binding domain in its middle and C-terminal part. Binds specifically G4 quadruplex nucleic acid structures (these are four-stranded right-handed helices, stabilized by guanine base quartets). Also required for cytoplasmic confinement of the synthetases and tRNA.
Component of a yeast aminoacyl-tRNA synthase (aaRS) complex formed by methionyl-tRNA synthase MES1, glutamyl-tRNA synthase GUS1 and the tRNA aminoacylation cofactor ARC1 in a stoichiometric complex. Interacts (via N-ter) with MES1 (via N-ter) and GUS1 (via N-ter). Can also form a stable binary complex with either MES1 or GUS1 that is functional in terms of aminoacylation.
Present with 57700 molecules/cell in log phase SD medium.
Belongs to the eukaryotic RPC7 RNA polymerase subunit family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. C31 is involved in the formation of the initiation complex.
The acidic domain is essential for its function.
Probable transcription factor that activates the genes for FRE1, FRE2 and FET3 in response to iron deprivation (PubMed:7720713, PubMed:9200812). Also required for the expression of LSO1 (PubMed:26450372). Iron could interact directly with AFT1 and inhibits its activity (PubMed:7720713).
Two-fold reduction in expression of LSO1.
Expression is regulated by SKN7, SLN1, and CDC4.
Mannosyltransferase involved in outer chain elongation of asparagine-linked oligosaccharides of the type Man(9)GlcNAc(2). Adds the first alpha-1,6-mannose to the Man(8)GlcNAc(2) and Man(9)GlcNAc(2), but not Man(5)GlcNAc(2), endoplasmic reticulum intermediates. Represents the first enzymatic event required for synthesis of outer chain mannose linkages on yeast secretory proteins. Has also the potential to transfer a second alpha-1,6-mannose to the Man(8)GlcNAc(2) core oligosaccharide.
Present with 9490 molecules/cell in log phase SD medium.
Stops growing at the early stage of bud formation and rapidly loses viability at the non-permissive temperature. Exhibits a defect in the initiation of the mannose outer chain. Leads to accumulation of free forms of oligosaccharides (fOSs).
The conserved DXD motif is involved in enzyme activity.
Abolishes CHS3 localization to the bud neck and plasma membrane, with increased protein localization to the trans-Golgi cisternae.
Belongs to the mitochondrion-specific ribosomal protein mS44 family.
Present with 16000 molecules/cell in log phase SD medium.
Binds DNA as a dimer. Associates with MET4 to form a heteromeric complex which also includes MET28.
Required for chromosome stability and methionine prototrophy. It is involved in chromosomal segregation. Binds to a highly conserved DNA sequence (5'-RTCACRTG-3'), called CDEI, found in centromeres and in several promoters. DNA-binding activity is enhanced by MET28. Required as an auxiliary factor for transcriptional activation of sulfur metabolism together with MET4 and MET28.
Present with 33700 molecules/cell in log phase SD medium.
Component of the 1.8 MDa SAGA complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9. Component of the ADA/GCN5 complex, that consists of HFI1/ADA1, ADA2, ADA3, SPT20/ADA5 and GCN5 and is probably a subcomplex of SAGA.
Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. HFI1/ADA1 and SPT20/ADA5 may recruit TATA binding protein (TBP) and possibly other basal factors to bind to the TATA box.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. BUB1 subfamily.
Involved in cell cycle checkpoint enforcement. The formation of a MAD1-BUB1-BUB3 complex seems to be required for the spindle checkpoint mechanism. Catalyzes the phosphorylation of BUB3 and its autophosphorylation. Associates with centromere (CEN) DNA via interaction with SKP1. The association with SKP1 is required for the mitotic delay induced by kinetochore tension defects, but not for the arrest induced by spindle depolymerization or kinetochore assembly defects.
Part of complex consisting of MAD1, BUB1 and BUB3 after activation of spindle checkpoint.
The glycine cleavage system (glycine decarboxylase complex) catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Interacts with AFR1, AKR1, activated CDC42, calmodulin (CMD1), myosin MYO1 and its light chain MLC1, BUD4, INN1, SEC3 and TEM1.
Required for the assembly and the contraction of the actomyosin ring at the bud neck during cytokinesis. Seems to be involved in additional tasks during cell division like axial bud-site selection and targeted secretion by recruiting the spatial landmark BUD4, the septin CDC12 and the secretion landmark SEC3 to the bud neck. May be regulated by calcium ions.
The IQ domains provide the interaction surface for the myosin light chain MLC1.
The Ras-GAP domain is required for contraction of the actomyosin ring and is needed for the interaction with TEM1. It probably does not stimulate GTPase activity.
The calponin homology (CH) domain binds to actin filaments and is required for their recruitment to the bud neck.
Alpha-1,2-specific exomannosidase involved in endoplasmic reticulum-associated degradation (ERAD). Delivers misfolded glycoproteins to proteasomes. Forms a complex with PDI1 to process unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2, promoting degradation in unfolded protein response.
Belongs to the glycosyl hydrolase 47 family.
Required for mitochondrial cristae morphogenesis and MGM1-processing. Controls the stability of mitochondrial phosphatidylethanolamine (PE). With UPS1, controls the level of cardiolipin in mitochondria. Cardiolipin is a unique phospholipid with four fatty acid chains and is present mainly in the mitochondrial inner membrane where it stabilizes the electron transport chain supercomplex between complexes III and IV through direct interaction of their subunits.
Belongs to the LDH/MDH superfamily. MDH type 1 family.
Yeast contains at least 3 malate dehydrogenase isoenzymes: a mitochondrial (MDH1), a cytoplasmic (MDH2) and a peroxisomal (MDH3).
Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.
By formaldehyde, ethanol and methyl methanesulphonate.
Oxidizes long-chain alcohols and, in the presence of glutathione, is able to oxidize formaldehyde (PubMed:8483449). Is responsible for yeast resistance to formaldehyde (PubMed:8483449).
Requires GSH for oxidation of formaldehyde or of methylglyoxal, while oxidation of long-chain alcohols is independent of GSH and enzyme activity improves with chain length.
Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals (PubMed:24302734). Involved in protection against reactive oxygen species (ROS) (PubMed:17395014). Important for viability in stationary phase. May negatively regulate TORC1 in response to nutrient limitation (PubMed:24706893).
Cys-138 is easily oxidized to sulfinic acid.
Up-regulated 10- to 30-fold during entry into stationary phase, by hydrogen peroxide or diamide stress, by heat stress, and by growth in the presence of the proline analog azetidine-2-carboxylic acid.
Belongs to the phosphatidylethanolamine-binding protein family. Mitochondrion-specific ribosomal protein mL38 subfamily.
Required for vacuolar fusion. Involved in the early steps of the fusion pathway.
Flavin-dependent oxidation of thiol-containing compounds. Probably required for the correct folding of disulfide-bonded proteins.
Involved in protection from oxidative damage.
Up-regulated by heat and oxidative stress.
Accumulates diphthine, the last intermediate in the diphthamide biosynthesis pathway. Increases the interaction of DPH5 with elongation factor 2.
Catalyzes the demethylation of diphthine methyl ester to form diphthine, an intermediate in diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EFT1 and EFT2). Also plays a role in the regulation of the retromer complex and is required for the recycling from endosomes of plasma membrane proteins like CAN1 and MUP1. Identified in a screen for mutants with decreased levels of rDNA transcription.
Was originally (PubMed:19965467) thought to be required for the first step of diphthamide biosynthesis but further studies (PubMed:22188241, PubMed:23468660) clearly suggest that it is involved in the third step of diphthamide biosynthesis.
Activated by the amino acid-induced proteolytic removal of an N-terminal inhibitory domain by serine protease SSY5, an intrinsic component of the SPS-sensor. Processing requires at least 2 components of the SCF(GRR1) ubiquitin ligase complex, namely the F-box protein GRR1 and the E2 enzyme CDC34, but does not depend on the proteasome. Processing is negatively regulated by the protein phosphatase 2A regulatory subunit RTS1.
Interacts (via Region II) with SSY5; protease component of the SPS-sensor.
Phosphorylated by casein kinase I. Phosphorylation is not dependent on the extracellular amino acid levels, but is a prerequisite for proteolytic processing.
The N-terminal inhibitory domain contains conserved sequence elements important for cytoplasmic retention (Region I) and proteolytic processing (Region II) of the protein. Region I is also required for ASI1/2/3-mediated negative regulation of transcription.
Transcription factor involved in the regulation of gene expression in response to extracellular amino acid levels. Synthesized as latent cytoplasmic precursor, which, upon a signal initiated by the plasma membrane SPS (SSY1-PTR3-SSY5) amino acid sensor system, becomes proteolytically activated and relocates to the nucleus, where it induces the expression of SPS-sensor-regulated genes, including the amino-acid permeases AGP1, BAP2, BAP3 and GNP1. Binding to promoters is facilitated by DAL81. Involved in the repression of genes subject to nitrogen catabolite repression and genes involved in stress response. Negatively regulated by inner nuclear membrane proteins ASI1, ASI2 and ASI3, which prevent unprocessed precursor forms that escape cytoplasmic anchoring from inducing SPS-sensor-regulated genes. May be involved in pre-tRNA splicing.
Was originally thought to be an amino-acid permease.
Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Not involved in the GTP-dependent ribosomal translocation step during translation elongation (By similarity). Required for respiratory growth and essential for mitochondrial genome maintenance.
Present with 1733 molecules/cell in log phase SD medium.
Results in loss of mitochondrial DNA. Causes a significant slow growth phenotype under normal growth conditions (glucose) and a reduced chronological life-span (CLS). Growth on a non-fermentable carbon source (gylcerol) is absent.
High-affinity S-adenosylmethionine permease, required for utilization of S-adenosylmethionine as a sulfur source.
Calcium-dependent mitochondrial solute carrier.
Strain S288c has a frameshift in position 403, which disrupts the gene coding for this protein and produces the non-functional allele sal1-1. A full-length functional allele can be found in strain CG379 (AC P0CI40).
Present with 67600 molecules/cell in log phase SD medium.
Putative transcription factor that seems to be involved in the sporulation process. Suppresses the lethal phenotype of RPM2 deletion.
Belongs to the phosphoenolpyruvate carboxykinase (ATP) family.
Essential for mitotic growth. Mediates organelle inheritance.
Belongs to the pseudouridine synthase RluA family.
Catalyzes the formation of pseudouridine at position 31 in the psi GC loop of tRNAS.
Phosphorylated by CDC5. CDC5 phosphorylation is necessary for cleavage by ESP1 and subsequent removal from chromosome arms.
Replaces the SCC1 mitosis-specific cohesin to ensure sister chromatid cohesion during meiosis (PubMed:10412984, PubMed:10691741, PubMed:11081626, PubMed:11163190, PubMed:12101124, PubMed:12663816, PubMed:12665553, PubMed:12717442, PubMed:15062096, PubMed:15120066, PubMed:15819623, PubMed:16027219, PubMed:9784122). Is cleaved by ESP1 shortly before the first meiotic division, and dissociates from chromatin, allowing sister chromatids to segregate (PubMed:11081626). Is protected from cleavage by SPO13 (PubMed:15620644). Promotes localization of the LINC complex subunit MPS3 on nuclear envelope in mitotic cells (PubMed:30417519).
Activator protein that regulates the ubiquitin ligase activity and substrate specificity of the anaphase promoting complex/cyclosome (APC/C). During telophase and in the subsequent G1 phase of the cell cycle, recognizes and binds proteins containing a destruction box (D-box) and an additional degradation signal termed the KEN box including ASE1, CDC20, the B-type cyclins CLB2 and CLB3, the polo-like kinase CDC5 and HSL1, and recruits them in a C-box-dependent manner to the APC/C for ubiquitination and subsequent proteolysis. Required for exit from mitosis, cytokinesis and formation of prereplicative complexes in G1. Probably is the target of a BUB2-dependent spindle checkpoint pathway.
Associates with the APC/C complex. Interacts with CLB2, CLB3, CDC5, HSL1, MSN5 and PSE1.
Phosphorylated at multiple sites by CDC28, probably in its CLB5 bound form, in S, G2 and M phase of the cell cycle, thereby blocking the association of CDH1 to the APC/C and promoting nuclear export of CDH1 by MSN5. Dephosphorylated and activated by CDC14 in late anaphase, which may be necessary for PSE1-dependent nuclear localization.
Adds the first glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Man(9)GlcNAc(2)-PP-Dol.
Belongs to the ALG6/ALG8 glucosyltransferase family.
Although highly homologous to the 2 other thiaminase-2 family members THI20 and THI21 in yeast, no hydroxymethylpyrimidine phosphate kinase activity could be demonstrated for this protein.
Is not required for thiamine biosynthesis.
Induced in response to cell wall damage.
Mediates the nuclear localization of RNR2 and RNR4, 2 subunits of the ribonucleotide reductase.
Phosphorylated by DUN1 in response to DNA damage which leads to its degradation.
Phosphatase involved in the regulation of protein synthesis. Affects translational accuracy.
Chaperone required for the assembly of ubiquinol-cytochrome c reductase of the mitochondrial respiratory chain.
Essential for the control of the cell cycle at the G1/S (start) transition. CLN3 may be an upstream activator of the G1 cyclins which directly catalyze start.
Expression is decreased during transition to slow growing or stationary phases.
Involved in the remodeling of the cell wall during the various phases of yeast culture development and under various environmental conditions and plays a role in septation.
Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.
Catalyzes oxidation of cytoplasmic one-carbon units for purine biosynthesis.
Present with 16200 molecules/cell in log phase SD medium.
Belongs to the GHMP kinase family. Mevalonate kinase subfamily.
Phosphomevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (PubMed:1846667). ERG8 converts 5-phosphomevalonate to 5-diphosphomevalonate (PubMed:1846667). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD1/ERG19 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (PubMed:32679672).
Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from SEC61 may govern the activity of the translocon. SEC63 may affect SEC1-polypeptide interactions by increasing the affinity of targeting pathways for SEC61 and/or by modifying SEC61 to allow more efficient polypeptide interaction. May also be involved in SRP-dependent cotranslational translocation. Is essential for cell growth and for germination.
Component of the heterotetrameric Sec62/63complex composed of SEC62, SEC63, SEC66 and SEC72. The Sec62/63 complex associates with the Sec61 complex to form the Sec complex. SEC63 interacts in its phosphorylated form with SEC62. May physically associate with KAR2 in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis. Part of a complex consisting of KAR2, SEC63, SEC66 and SEC72.
By DNA-damaging agent methyl methanesulphonate (MMS) (at protein level).
Involved in the synthesis of (1->6)- and (1->3)-beta-D-glucan polymers of the yeast cell wall in vivo. It is required for full activity of beta-glucan synthase in vitro. May be involved in the maturation and transport of cell wall proteins (CWP) to the cell wall. May act as a transglucosidase and contribute to the construction of a protein-bound glucan-structure that acts as an acceptor site for the addition of (1->6)-beta-D-glucan at the cell surface.
The cytoplasmic domain interacts with the actin patch assembly proteins LAS17 and SLA1. Interacts with KEG1.
Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type II sub-subfamily.
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (PubMed:7890740, PubMed:7890739, PubMed:24366873). Phosphatidylethanolamine produced by PSD2 is insufficient to completely provide the PtdEtn pool required by mitochondria under respiratory conditions (PubMed:11294902). PSD2 is also involved in the PtdSer transport step to the site of PtdEtn synthesis on the Golgi/endosome membranes (PubMed:24366873). Required for normal heavy metal resistance (PubMed:20016005).
Decreases induction of mitophagy in stationary phase following growth on a respiratory carbon source.
Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit (By similarity). Interacts with pstB2/PDR17 (PubMed:20016005, PubMed:24366873). This interaction may be a means to structurally tether the donor membrane (ER) harboring PstB2/PDR17 to acceptor membranes (Golgi/endosomes) harboring PSD2 during PtdSer transport to the site of PtdEtn synthesis (PubMed:24366873).
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
The C2 domains have an essential, but non-catalytic function (Probable) (PubMed:24366873). Both C2-1 and C2-2 facilitate interaction with PstB2/PDR17 and are required for lipid transport function (PubMed:24366873).
Catalyzes the cleavage of 5-oxo-L-proline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.
Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA) (PubMed:10333520). It is the only aminotransferase known to utilize SAM as an amino donor (PubMed:10333520).
Component of the oligosaccharyltransferase (OST) complex, which appears to exist in two assemblies comprising OST1, OST2, OST4, OST5, STT3, SWP1, WPB1, and either OST3 or OST6 (PubMed:10358084, PubMed:16297388, PubMed:16096345, PubMed:15886282). OST assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains OST1 and OST5, subcomplex 2 contains STT3, OST3, and OST4, and subcomplex 3 contains OST2, WBP1, and SWP1 (By similarity).
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (PubMed:11580295). Can participate in redox reactions and is able to catalyze dithiol-disulfide exchange reactions with other proteins, albeit with relatively low efficiency. May form transient disulfide bonds with nascent polypeptides in the endoplasmic reticulum and thereby promote efficient glycosylation (PubMed:19549845).
Part of the multisubunit TRAPP (transport protein particle) II complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33, TRS65, TRS120 and TRS130. Interacts directly with TRS120 and TRS130.
Specific subunit of the TRAPP II complex, a highly conserved vesicle tethering complex that functions in the late Golgi as a guanine nucleotide exchanger (GEF) for the Golgi YPT1 GTPase. TRS65 plays a role in the YPT GEF activity of TRAPP II in concert with the two other TRAPP II-specific subunits TRS120 and TRS130. Involved in cell wall (1-->6)-beta-glucan synthesis.
Mitochondrial DNA endonuclease involved in intron homing. It introduces a specific double-strand break in the DNA of the 21S rRNA gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Specifically recognizes and cleaves the sequence 5'-TAGGGATAACAGGGTAAT-3'.
Calcium-binding protein that is required for polar bud growth and cell wall abscission. Can also bind zinc ions.
Activated by fructose 6-phosphate. Inorganic phosphate inhibits the synthase activity in the complex, but activates the synthase activity in the free monomeric form.
Belongs to the glycosyltransferase 20 family.
Either partial repression by glucose or induction by galactose. Induced by heat shock.
Synthase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process. Can function independently of the complex.
Catalyzes the reversible transfer of the terminal phosphoryl group of ATP to the acceptor molecule GMP. Essential for recycling GMP and indirectly, cGMP.
Present with 20500 molecules/cell in log phase SD medium.
FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space (IMS). Forms a redox cycle with MIA40 that involves a disulfide relay system. Important for maintaining the cysteine residues in MIA40 in an oxidized state. Reduced ERV1 is reoxidized by cytochrome c. Required for the maturation of cytoplasmic, but not of mitochondrial Fe/S proteins.
Homodimer. Interacts with MIA40, forming transient intermolecular disulfide bridges.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Probable component of the endoplasmic reticulum-associated degradation (ERAD) pathway that acts upstream of HRD3 and USA1.
May act in the sexual differentiation pathway.
Present with 96655 molecules/cell in log phase SD medium.
Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the 19S regulatory complex (RC). During the base subcomplex assembly is part of a NAS2:RPT4:RPT5 module; NAS2 is released during the further base assembly process.
Belongs to the proteasome subunit p27 family.
Part of a transient complex containing NAS2, RPT4 and RPT5 formed during the assembly of the 26S proteasome.
Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 2 subfamily.
Tetramer of two alpha and two beta subunits.
Was originally erroneously assigned as an alpha subunit.
Ethanolamine-phosphate cytidylyltransferase which catalyzes the second step of phosphatidylethanolamine biosynthesis. Involved in the maintenance of plasma membrane and required for proper sporulation.
Present with 4700 molecules/cell in log phase SD medium.
Belongs to the metallo-dependent hydrolases superfamily.
Involved in nonsense-mediated decay of mRNAs containing premature stop codons. It interacts, via its C-terminus, with NAM7/UPF1. Could be involved in determining the efficiency of translational termination or reinitiation or factors involved in the initial assembly of an initiation- and termination-competent mRNP.
Acts as an activator of both rRNA/tRNA and protein methyltransferases. Together with methyltransferase MTQ2, required for the methylation of eRF1 on 'Gln-182'. Together with methyltransferase TRM11, required for the formation of 2-methylguanosine at position 10 (m2G10) in tRNA. Together with methyltransferase BUD23, required for the formation of 7-methylguanine at position 1575 (m7G1575) in 18S rRNA. Involved in biogenesis of both 40S and 60S ribosomal subunits.
Heterodimer of MTQ2-TRM112, forming the eRF1 methyltransferase. TRM112 is necessary for the solubility and activity of the catalytic subunit MTQ2. Interacts with TRM11; required for full tRNA methyltransferase activity. Interacts with BUD23; required for full rRNA methyltransferase activity. Interacts with RCM1, NOP2, TRM9 and LYS9.
Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1. Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with PRP40 and SNP1. Interacts (via SCwid domain) with CWC21. Interacts (via SCwid domain) with SNU114 (via N-terminus). Interacts (via RNase H homology domain and MPN domain) with BRR2; this modulates BRR2 ATPase and helicase activity. Interacts (via RNase H homology domain) with AAR2. AAR2 and BRR2 compete for PRP8 binding, and during U5 snRNP maturation BRR2 displaces the initially bound AAR2. Is associated with snRNP U5, together with SNU114 and BRR2.
Contains a region with structural similarity to RNase H, but lacks RNase H activity.
Contains a region with structural similarity to reverse transcripase, presenting the classical thumb, fingers and palm architecture, but lacks enzyme activity, since the essential metal-binding residues are not conserved.
Contains a region with structural similarity to type-2 restriction endonucleases, but the residues that would bind catalytic metal ions in endonucleases are instead involved in hydrogen bonds that stabilize a highly conserved loop.
Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for association of BRR2 with the spliceosomal U5 snRNP, and the subsequent assembly of the U4/U6-U5 tri-snRNP complex. Functions as scaffold that positions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that splicing can occur. Interacts with both the 5' and the 3' splice site, as well as the branch region. Has a role in branch site-3' splice site selection. Associates with the branch site-3' splice 3'-exon region. Also has a role in cell cycle.
The MPN (JAB/Mov34) domain has structural similarity with deubiquitinating enzymes, but lacks the residues that would bind the catalytic metal ion.
Forms a complex composed of CDC48, NPL4, UFD1, DOA1, SHP1 and deubiquitinase OTU1; within the complex interacts with CDC48 (PubMed:16427015). Interacts (via PUL domain) with CDC48 (via C-terminus); the interaction is direct (PubMed:8890162, PubMed:16427015, PubMed:16428438, PubMed:27044889, PubMed:19805280, PubMed:20508643). Forms a complex composed of CDC48, DOA1, deubiquitinase UBP3 and probably BRE5; within the complex interacts with CDC48 and UBP3 (PubMed:20508643). May form a complex composed of VPS27, HSE1 and DOA1 (PubMed:18508771). Interacts with HSE1 (via SH3 domain) (PubMed:18508771). Interacts (via WD repeats and PFU domain) with ubiquitin; the interaction is direct (PubMed:15096053, PubMed:16427015, PubMed:16428438, PubMed:21070969). Interacts with ubiquitinated FZO1 but not unmodified FZO1; the interaction recruits FZO1 to CDC48 and promotes FZO1 proteasomal degradation (PubMed:27044889).
Severely reduces cell growth in response to misfolded protein, translation inhibition-induced, heat or mitochondrial oxidative stresses but not in response to ER stress (PubMed:16427015, PubMed:18508771, PubMed:16428438, PubMed:27044889).
The PFU domain mediates interaction with ubiquitin.
The PUL domain is composed of 6 armadillo-like repeats and mediates the interaction with CDC48 C-terminus.
The WD repeats mediate interaction with ubiquitin.
Ubiquitin-binding protein involved in protein ubiquitination, sorting and degradation (PubMed:2111732, PubMed:8890162, PubMed:19805280, PubMed:18508771, PubMed:20508643, PubMed:27044889). Acts as a ubiquitinated substrate-recruiting adapter for chaperone ATPase CDC48 by binding mono- or polyubiquitin chains (PubMed:15096053, PubMed:16427015, PubMed:16428438, PubMed:27044889). Depending on the context, promotes or prevents proteasomal degradation of ubiquitinated proteins (PubMed:2111732, PubMed:8890162, PubMed:19805280, PubMed:27044889). Involved in the ubiquitin fusion degradation (UFD) pathway by promoting the degradation of ubiquitinated proteins (PubMed:2111732, PubMed:8890162, PubMed:19805280, PubMed:27044889). Involved in the mitochondria-associated degradation pathway (MAD) by promoting the degradation of several ubiquitinated membrane proteins (PubMed:27044889). By competing with UFD2 to bind CDC48, prevents the multi-ubiquitination and subsequent degradation of UFD2-dependent substrates (PubMed:16427015). Required for ribophagy, a process which relocalizes ribosomal particles into the vacuole for degradation in response to starvation (PubMed:20508643). Involved in the ubiquitin-mediated sorting of membrane proteins into multivesicular bodies (MVBs) (PubMed:18508771). In addition, plays an essential role in maintaining cellular ubiquitin levels (PubMed:7615550, PubMed:16427015, PubMed:16428438, PubMed:18508771, PubMed:19805280). May affect indirectly the degradation of ubiquitinylated proteins by regulating cellular ubiquitin levels (PubMed:7615550, PubMed:23525333).
Expression is regulated by various nitrogen sources.
Belongs to the glycosyl hydrolase 16 family. CRH1 subfamily.
Positively regulated by cell integrity signaling through MPK1 in response to cell wall perturbation. Induced by heat stress.
Present with 44000 wall-bound molecules/cell in log phase YPD medium.
Probable glycosidase that plays a role in cell wall architecture. Required for the transfer of chitin to 1,6-beta-glucan in the cell wall.
Based on current literature, utilization of para-aminobenzoic acid (pABA) involving C4-deamination seems not to occur in bacteria, plants and mammals where only C5 hydroxylation of HHB has been shown, even if human COQ6 is able to perform the deamination reaction in the absence of COQ9.
FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-hexaprenyl-4-hydroxybenzoic acid (HHB) to 3-hexaprenyl-4,5-dihydroxybenzoic acid (DHHB). The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via ferredoxin (YAH1) and ferredoxin reductase (ARH1) to COQ6 (PubMed:21944752). Can also convert 3-hexaprenyl-4-aminobenzoic acid (HAB), a COQ2-prenylated pABA, to DHHB in a two step process. HAB is first hydroxylated at C5 to yield 3-hexaprenyl-4-amino-5-hydroxybenzoic acid (HHAB) which is further deaminated at C4 by COQ6 to produce DHHB (PubMed:26260787).
Belongs to the fluoride exporter Fluc/FEX family.
Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
Highly sensible to fluoride, but not to other halide salts. The growth of a double deletion of both FEX1 and FEX2 is inhibited at almost a 1000-fold lower fluoride concentration than in the wild-type. Has increased intracellular fluoride concentrations.
Present with 220 molecules/cell in the plasma membrane.
Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy (PubMed:10995454, PubMed:11086004, PubMed:15743910, PubMed:17295840, PubMed:18077553, PubMed:18287526, PubMed:19805182, PubMed:19995911, PubMed:20647741, PubMed:20855505, PubMed:22447937, PubMed:22778255, PubMed:22782902, PubMed:22885598, PubMed:8224160, PubMed:21468027). Required for autophosphorylation of ATG1 at 'Thr-226' and its dimerization (PubMed:20439775, PubMed:17699586, PubMed:21712380). May also be involved in the regulation of autophagy through SNF1 (PubMed:11486014). Involved in ATG9 and ATG23 cycling through the pre-autophagosomal structure (PubMed:14723849, PubMed:17426440). Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation (PubMed:10837477). Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy (PubMed:10837477). Finally, ATG13 is also required for glycogen storage during stationary phase (PubMed:11486014).
Belongs to the ATG13 family. Fungi subfamily.
Hypophosphorylated form interacts with ATG1 to form the ATG1-ATG13 kinase complex (PubMed:10995454, PubMed:15743910, PubMed:15901835, PubMed:18829864, PubMed:20439775, PubMed:20953146, PubMed:21712380, PubMed:22778255, PubMed:22885598). The ATG1-ATG13 complex interacts with the ATG17-ATG29-ATG31 complex through direct interaction with ATG17 (PubMed:23219485, PubMed:15743910, PubMed:15901835, PubMed:19755117, PubMed:19805182). Interacts with VAC8 (PubMed:10837477).
Phosphorylated; hyperphosphorylated by the TORC1 kinase complex to repress the induction of autophagy in nutrient-replete conditions (PubMed:10995454, PubMed:19995911, PubMed:19805182, PubMed:22447937, PubMed:22727621, PubMed:29698392). Starvation and TOR inactivation results in ATG13 partial dephosphorylation leading to ATG1-binding (PubMed:10995454). Rephosphorylated by ATG1 during prolonged nitrogen starvation (PubMed:21490424). Also phosphorylated by PKA (PubMed:17699586, PubMed:19805182, PubMed:21078689). PKA phosphorylation regulates the association of ATG13 with the PAS (PubMed:21900499). Within this regulatory network, mitochondrial respiratory deficiency suppresses autophagic flux (PubMed:21468027). Hyperphosphorylation in rich medium is impaired in the absence of VAC8 (PubMed:10837477). Dephosphorylation is dependent on FAR11 (PubMed:22782902).
Component of the M-Pol II complex composed of ANP1, MNN9, MNN10, MNN11 and HOC1.
The M-Pol II complex possesses alpha-1,6-mannosyltransferase activity and is probably involved in the elongation of the mannan backbone of N-linked glycans on cell wall and periplasmic proteins.
Interacts with PEX6 (PubMed:12808025). Interacts with PEX19; targets PEX15 to the peroxisome (PubMed:16763195).
Peroxisomal docking factor that anchors PEX1 and PEX6 to peroxisome membranes (PubMed:12808025, PubMed:9405362, PubMed:16007078). PEX26 is therefore required for the formation of the PEX1-PEX6 AAA ATPase complex, a complex that mediates the extraction of the PEX5 receptor from peroxisomal membrane (PubMed:12808025, PubMed:9405362).
Belongs to the AP endonuclease 2 family.
DNA repair enzyme that cleaves apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA. APN1 accounts for > 97% of both apurinic/apyrimidinic (AP) endonuclease and DNA 3'-repair diesterase activities.
Seems to act in the pleiotropic control of cell division. May participate in chromosome segregation events.
Strongly interacts with CBF2/NDC10. Also interacts with CBF3D/SKP1.
Acyltransferase with lysophosphatidic acid acyltransferase (LPAAT) activity. Fatty acyl substrates include 18:0-acyl-CoA, 16:0-acyl-CoA, 17:0-acyl-CoA and 14:0-acyl-CoA (PubMed:20694142). Responsible for the acyl-CoA-dependent introduction of saturated very long chain fatty acids (VLCFAs) into phosphatidylinositol, transferring saturated FAs with 18 to 26 carbon atoms (PubMed:27462707). Responsible for the incorporation of stearate into phosphatidylinositol (PubMed:19796168, PubMed:26711260). Overexpression has an effect on chromosome stability (PubMed:10454593). Regulates phosphorylation and expression of glycerol-3-phosphate acyltransferase SCT1 (PubMed:22323296).
Phosphoinositides (PIPs) with stearic acyl chains are strongly disturbed. Induces disturbances in intracellular trafficking, alterations in the budding pattern and defects in actin cytoskeleton organization.
Belongs to the alkylbase DNA glycosidase AlkA family.
Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine or 7-methyladenine from the damaged DNA polymer formed by alkylation lesions.
E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H2B to form H2BK123ub1 in association with the E2 enzyme RAD6/UBC2. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. It thereby plays a central role in histone code and gene regulation. Also modulates the formation of double-strand breaks during meiosis.
Forms a complex with the E2 enzyme RAD6/UBC2. May interact with LGE1.
Ty1-DR1 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Belongs to the universal ribosomal protein uS12 family.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (PubMed:25609543, PubMed:28154081). uS12m is required for respiratory growth (PubMed:11780787).
Component of the mitochondrial small ribosomal subunit (mt-SSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. uS12m forms part of the decoding center of the mt-SSU.
Involved in sporulation. Essential for completion of the nuclear division.
Guanine-nucleotide-releasing protein that acts on SEC4. Might play a general role in vesicular transport.
Interacts with the serine palmitoyltransferase complex LCB1-LCB2. Component of the SPOTS complex, at least composed of LCB1/2 (LCB1 and/or LCB2), ORM1/2 (ORM1 and/or ORM2), SAC1 and TSC3.
Stimulates the activity of serine palmitoyltransferase (SPT).
Affects the meiotic recombination and the formation of viable spores.
Component of the U1 small nuclear ribonucleoprotein complex (U1 snRNP) involved in the initiation of meiotic recombination (PubMed:1603056, PubMed:7625279). Involved in the formation of DSBs at recombination hot-spots through meiosis-specific splicing of REC107 pre-mRNA (PubMed:7625279, PubMed:9112441, PubMed:21788335). Collaborates with MER1 to promote splicing of essential meiotic mRNAs REC10, AMA1, MER3, HFM1, SPO22 and PCH2 (PubMed:10983980, PubMed:21208980, PubMed:21788335). NAM8 interacts with the pre-mRNA downstream of the 5' splice site, in a region of non-conserved sequence and is required for efficient splicing of uncapped RNA precursor (PubMed:10072385).
Component of the U1 small nuclear ribonucleoprotein complex (U1 snRNP).
The RNA binding domains RRM2 and RRM3 are required for NAM8 meiotic function (PubMed:21788335, PubMed:21208980). Within the U1 snRNP complex, the RRM2 domain of NAM8 is positioned to bind to the intronic region immediately down-stream of nucleotide +13 (PubMed:31485080).
Syntaxin required for targeting and fusion of Golgi-derived retrograde transport vesicles with the ER.
In response to cytotoxic stress but not genotoxic stress.
Involved in nucleolar integrity and required for processing of the pre-rRNA for the 60S ribosome subunit.
Associates with the mitochondrial ribosomes.
Involved in mitochondrial potassium homeostasis through the mitochondrial K(+)/H(+) exchange regulation.
Induced by amino acid and purine starvation in a GCN4 dependent manner.
Component of the YIP1-YIF1 complex, composed of at least YIF1, YIP1 and YOS1. The complex interacts with the ER to Golgi SNAREs BOS1 and SEC22. Interacts with the YIP1 family members YIP4 and YIP5, and with the Rab GTPases SEC4, YPT1, YPT6, YPT7, YPT10, YPT11, YPT31, YPT32 and YPT52. Interacts with BTN2 and SNX3.
Required for fusion of ER-derived vesicles with the Golgi during ER-to-Golgi protein transport. May be involved in proper membrane localization of Rab GTPases.
Associated with pre-ribosomal particles. Interacts with DBP9 and RSA3. Together with NOP8, URB1, URB2 and RSA3, forms an RNA-independent complex, which is required during early maturation of nascent 60S ribosomal subunits.
Belongs to the DEAD box helicase family. DDX51/DBP6 subfamily.
Belongs to the bacterial ribosomal protein bS16 family.
Catalytic subunit of serine palmitoyltransferase (SPT), which catalyzes the committed step in the synthesis of sphingolipids, the condensation of serine with palmitoyl CoA to form the long chain base 3-ketosphinganine.
LCB1 and LCB2 encode essential subunits of the enzyme and form a heterodimer. Component of the SPOTS complex, at least composed of LCB1/2 (LCB1 and/or LCB2), ORM1/2 (ORM1 and/or ORM2), SAC1 and TSC3. Interacts with LCB1 and TSC3.
Present with 54500 molecules/cell in log phase SD medium.
Belongs to the eukaryotic ribosomal protein eL27 family.
Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 33 subfamily.
Homodimer. Interacts with ALG2 and ALG11.
Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER.
Component of the retromer complex which consists of VPS29, VPS26, VPS35, VPS5 and VPS17. Component of a retromer subcomplex consisting of VPS5 and VPS17.
Phosphorylated on one or more serine residues.
Plays a role in vesicular protein sorting. Required for the sorting and delivery of a subset of soluble vacuolar hydrolases. Required for retention of late Golgi membrane proteins and vacuolar biogenesis. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. The VPS5-VPS17 subcomplex may assemble onto the membrane to promote vesicle formation.
Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIM8-TIM13 complex is non essential and only mediates the import of few proteins under precise conditions while the predominant TIM9-TIM10 70 kDa complex is crucial and mediates the import of much more proteins. Strictly required for import of TIM23 in some conditions, when a low membrane potential exists in the mitochondria.
The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIM13 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane.
By cell wall stress and the YRR1 transcription factor.
Involved in the export of PMA1, possibly through the monitoring or assisting of PMA1 folding and acquisition of competence to enter vesicles.
Phosphorylated at tyrosine and dephosphorylated by the phosphotyrosine-specific phosphoprotein phosphatase PTP1.
Proline isomerase that belongs to an abundant class of enzymes that catalyze the cis-trans isomerization of X-Pro peptide bonds and can accelerate the refolding of proline-containing polypeptides (PubMed:7925954, PubMed:8051210, PubMed:7525596). Specifically binds nuclear localization sequences (PubMed:7925954). May be involved in the assembly or folding of ribosomal proteins (PubMed:8051210).
Required for microtubule stability. Interacts with CIN4.
Belongs to the phage and mitochondrial RNA polymerase family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
General activator of RNA polymerase III transcription. Interacts with TBP. Binds to Pol III subunit C34 and to the TAU135 component of TFIIIC.
Present with 4330 molecules/cell in log phase SD medium.
TFIIIB comprises the TATA-binding protein (TBP), the B-related factor (BRF) and the B' component (TFC5).
Component of the RIX1 complex, composed of IPI1, RIX1/IPI2 and IPI3 in a 1:2:2 stoichiometry. The complex interacts (via RIX1) with MDN1 (via its hexameric AAA ATPase ring) and the pre-60S ribosome particles.
Has a partially redundant function to ECM33 in cell wall integrity. May be involved in a repair mechanism activated in response to cell wall damage.
Mannoprotein called haze protective factor from wine that is able to prevent visible wine protein haze formation. This mannoprotein showed haze-protective activity against wine proteins and BSA when either was heated in white wine.
Positively regulated by cell integrity signaling through MPK1 in response to cell wall perturbation. Induction is dependent on transcription factor RLM1.
Cargo-receptor protein involved in the cytoplasm to vacuole transport (Cvt) and in autophagy. Recognizes cargo proteins, such as AMS1 and delivers them to the pre-autophagosomal structure for eventual engulfment by the autophagosome and targeting to the vacuole.
Seems to activate its own expression and that of the repressor ROX1 which in turn represses YAP6 expression.
Transcription activator involved in the regulation of genes expressed in response to environmental changes and metabolic requirements. According to genome-wide promoter binding and gene expression studies it regulates, among others, genes involved in ribosome biogenesis, protein synthesis, carbohydrate metabolism, and carbohydrate transport. It may also be involved in pleiotropic drug resistance. When overexpressed, it confers resistance to cisplatin, methylmethanosulfonate, and mitomycin C, and increases cellular tolerance to sodium and lithium.
Belongs to the eukaryotic ribosomal protein eL30 family.
Present with 59300 molecules/cell in log phase SD medium.
Required for high-affinity tryptophan transport. Also transports cysteine, phenyalanine and tyrosine.
Could be the product of a pseudogene. Almost identical to BUD5 N-terminal.
Belongs to the protein kinase superfamily. PAN3 family.
Contains a pseudokinase domain. The protein kinase domain is predicted to be catalytically inactive because some of the residues important for catalytic activity are substituted and it lacks the equivalent of the binding site for a peptide substrate (PubMed:24880344). However, it has retained an ATP-binding site and ATP-binding is required for mRNA degradation, stimulating the activity of the PAN2 nuclease in vitro. The nucleotide-binding site is juxtaposed to the RNase active site of PAN2 in the complex and may actually bind nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active site of the deadenylase and thus increasing the efficiency with which this distributive enzyme degrades oligo(A) RNAs (By similarity).
Homodimer. Forms a heterotrimer with a catalytic subunit PAN2 to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts (via PAM-2 motif) with poly(A)-binding protein PAB1 (via PABC domain), conferring substrate specificity of the enzyme complex.
Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping by DCP1-DCP2 and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails, trimming the tails from their synthesized length to the slightly shorter, apparently messenger-specific length found on newly exported mRNAs. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and with PAB1. PAN cooperates with protein kinase DUN1 in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress.
The N-terminal zinc finger binds to poly(A) RNA.
The pseudokinase domain, the coiled-coil (CC), and C-terminal knob domain (CK) form a structural unit (PKC) that forms an extensive high-affinity interaction surface for PAN2.
Divalent metal cations. Has optimal activity with Mg(2+).
Has both endo- and exonuclease activities. Incises double-stranded DNA without obvious specificity via its endonuclease activity and excises the DNA from the 3'-to 5'-end by its exonuclease activity. May have a role in apoptosis.
Belongs to the eukaryotic release factor 1 family. Pelota subfamily.
Involved in protein translation. Together with HBS1, may function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs. The complex formed by DOM34 and HBS1 has ribonuclease activity towards double-stranded RNA substrates, but does not cleave single-stranded RNA. Acts as endonuclease; has no exonuclease activity. Increases the affinity of HBS1 for GTP, but nor for GDP. Promotes G1 progression and differentiation and is involved in mitotic and meiotic cell divisions.
The N-terminal domain has the RNA-binding Sm fold (PubMed:18180287). It harbors the endoribonuclease activity (PubMed:17889667).
By transcription factor HCM1 during S phase.
Interacts with the heterodimeric transcription factors SBF (SWI4-SWI6 cell-cycle box binding factor) and MBF (MluI cell-cycle box binding factor), each composed of the transcriptional coactivator SWI6 and a sequence-specific DNA-binding protein SWI4 or MBP1, respectively.
Phosphorylation by the cyclin-dependent kinase (CDK) CDC28 controls both subcellular location and association of WHI5 with SBF.
Transcriptional repressor that negatively regulates G1-specific, SBF- and MBF-dependent transcription. Binds via SBF to promoters of G1-specific genes to repress transcription in early G1. During G1, phosphorylated by cyclin-CDK CLN3-CDC28 and progressively hyperphosphorylated by CDK associated with other G1-cyclins, which leads to dissociation of WHI5 from SBF, activating SBF-dependent transcription in late G1. Elimination of CDK activity at the end of mitosis by the mitotic exit network (MEN) allows WHI5 to reassociate with SBF to again repress G1/S transcription.
Binds to nucleoporin FxFG but not GLFG repeat regions. Ran-GTP can disrupt the karyopherin heterodimer by binding to the beta subunit and releases both subunits from the docking site.
Forms a complex with an importin beta subunit. In the nucleus, interacts with NUP2 which accelerate release of NLSs, NUP2 is subsequently displaced by CSE1:RanGTP which mediates re-export and recycling. Interacts with HEH2, SHE2, and STS1.
Functions in nuclear protein import as an adapter protein for importin beta nuclear receptors (PubMed:10913188). Binds specifically and directly to substrates containing either a simple or bipartite NLS motif (PubMed:10745017). Promotes docking of import substrates to the nuclear envelope (PubMed:8521485). Together with importin beta KAP95, mediates nuclear import of transcription factor GCN4 (PubMed:14648200). Together with tethering factor STS1, targets the proteasome to the nucleus (PubMed:10913188, PubMed:21075847).
Present with 2790 molecules/cell in log phase SD medium.
The NLS binding sites are mainly involved in recognition of simple or bipartite NLS motifs. Structurally located within in a helical surface groove they contain several conserved Trp and Asn residues of the corresponding third helices (H3) of ARM repeats which mainly contribute to binding.
Expressed during late S phase and G2 phases.
May be regulated by MCM1. Regulated by SWI4-SWI6 heterodimer. Down-regulated by nonfermentable carbon source.
Transcriptional repressor required to restrict transcription of ECB-dependent genes to the G1/M phase by repressing their transcription during S late phase. Genes that contain a ECB (early cell box) element in their transcription regulatory region are transcribed only during G1/M phases. Binds the IMEI regulatory region in vitro, its relevance in vivo is however unclear.
Belongs to the acetyltransferase family. GNA1 subfamily.
Component of the ceramide synthase complex that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward hexacosanoyl-CoA (C26:0-CoA) (PubMed:15692566, PubMed:11694577). N-acylates sphinganine and phytosphingosine bases to form dihydroceramides and phytoceramides, respectively (PubMed:15692566, PubMed:11694577). Redundant with LAG1. Facilitates ER-to-Golgi transport of GPI-anchored proteins.
Composed of the ceramide synthase complex composed of at least LAC1, LAG1 and LIP1.
Expression is controlled by PDR1 and PDR3 which bind its propmoter PDRE element, and by ROX1 and CBF1.
Belongs to the DASH complex SPC19 family.
Hyperaccumulates ribose 1-phosphate and upstream purines upon glucose-induced purine nucleoside recycling.
Major phosphoribomutase that converts ribose 1-phosphate to ribose 5-phosphate. Involved in ribose salvage via the pentose phosphate pathway.
Present with 4960 molecules/cell in log phase SD medium.
Transports C5-C7 oxodicarboxylates across the inner membranes of mitochondria. Can transport 2-oxoadipate, 2-oxoglutarate, adipate, glutarate, 2-oxopimelate, oxaloacetate, citrate and malate. The main physiological role is probably to supply 2-oxoadipate and 2-oxoglutarate from the mitochondrial matrix to the cytosol where they are used in the biosynthesis of lysine and glutamate, respectively, and in lysine catabolism.
Present with 30500 molecules/cell in log phase SD medium.
Forms a ternary complex with RSP5 and RUP1 (PubMed:15933713). Interacts with RSP5 (PubMed:19920177). Interacts with FZO1 (PubMed:23317502).
Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety in natural or engineered linear fusion proteins, irrespective of their size or the presence of an N-terminal extension to ubiquitin (PubMed:15933713). Hydrolyzes polyubiquitinated 'Lys-63' polyubiquitin chains in RPO21, producing mono-ubiquitinated RNA polymerase II (PubMed:19920177). Removes ubiquitin chains that initiate proteolysis of FZO1 and inhibit mitochondrial fusion (PubMed:23317502).
Increases the amount of polyubiquitinated RNA polymerase II subunit RPO21.
Present with 2420 molecules/cell in log phase SD medium.
Binds 2 heme b groups non-covalently per subunit.
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 10 subunits. The complex is composed of 3 respiratory subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10 (PubMed:10873857, PubMed:11880631, PubMed:8031140, PubMed:30598554). The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a monomer or a dimer of cytochrome c oxidase (complex IV, CIV), resulting in 2 different assemblies (supercomplexes III(2)IV and III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556, PubMed:30598554).
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (Probable). Cytochrome b is a catalytic core subunit containing 2 b-type hemes BL and BH topographically segregated in the quinone reduction (Qi) and quinol oxidation (Q0) sites on opposite sides of the membrane (PubMed:18390544).
Heme 1 (or BL or b562) is low-potential and absorbs at about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs at about 566 nm.
Involved in spore wall maturation. Catalyzes a two step reaction that leads to the LL-dityrosine containing precursor of the spore wall.
Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (PubMed:12359722). This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (PubMed:29301962).
Component of the oligosaccharyltransferase (OST) complex, which appears to exist in two assemblies comprising OST1, OST2, OST4, OST5, STT3, SWP1, WPB1, and either OST3 or OST6 (PubMed:10677492, PubMed:16297388, PubMed:16096345, PubMed:15831493, PubMed:15886282, PubMed:9405463, PubMed:9435788, PubMed:29301962). OST assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains OST1 and OST5, subcomplex 2 contains STT3, OST3, and OST4, and subcomplex 3 contains OST2, WBP1, and SWP1 (PubMed:29301962). Interacts with SEC61 (PubMed:15831493).
Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.
Belongs to the steroid 5-alpha reductase family.
Catalyzes the last of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme reduces the trans-2,3-enoyl-CoA fatty acid intermediate to an acyl-CoA that can be further elongated by entering a new cycle of elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. VLCFAs serve for instance as precursors for ceramide and sphingolipids. Required for normal biogenesis of piecemeal microautophagy of the nucleus (PMN) bleps and vesicles during nutrient stress.
Interacts with the fatty acid elongation system components ELO2 and ELO3. Interacts with NVJ1.
Belongs to the NmrA-type oxidoreductase family.
Component of multiple cullin-RING ligases (CRLs) composed of 4 subunits: the RING protein HRT1, the cullin RTT101, a linker protein MMS1, and one of many alternative substrate receptors belonging to a protein family described as DCAF (DDB1- and CUL4-associated factor). Component of a RTT101(MMS1-MMS22) complex with the substrate receptor MMS22. This complex further interacts with RTT107 and CTF4 to form RTT101-MMS1-MMS22-RTT107 and RTT101-MMS1-MMS22-CTF4 complexes respectively. Component of a RTT101(MSS1-CRT10) complex with the substrate receptor CRT10. Component of a RTT101(MSS1-ESC2) complex with the potential substrate receptor ESC2. Component of a RTT101(MSS1-ORC5) complex with the potential substrate receptor ORC5. Interacts (via C-ter) with HRT1; required for ubiquitin-ligase activity. Interacts (via N-ter) with MMS1.
Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes (CRLs), which mediate the ubiquitination of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The CRL associates with CDC34 as the E2 ubiquitin-conjugating enzyme. The functional specificity of the CRL depends on the type of the associated substrate receptor protein. RTT101(MMS1-MMS22) promotes fork progression through damaged DNA or natural pause sites by stabilizing replication proteins like the replication fork-pausing complex (FPC) and leading-strand polymerase at stalled replication forks. RTT101(MMS1-MMS22) ubiquitinates the acetylated histones H3K56ac-H4 at lysine residues H3K121, H3K122 and H3K125. Ubiquitination is required for efficient histone deposition during replication-coupled nucleosome assembly, probably by facilitating the transfer of H3-H4 from ASF1 to other chaperones involved in histone deposition. RTT101(MMS1-CRT10) may regulate nucleotide synthesis through transcriptional regulation of ribonucleotide reductase. RTT101(MMS1) is also involved in the non-functional rRNA decay (NRD) of 25S rRNA through the selective, ubiquitination-dependent degradation of nonfunctional ribosomal particles. Ubiquitinates the FACT (facilitates chromatin transcription) complex subunit SPT16 in an MMS1-independent manner. Involved in regulation of Ty1 transposition and protects the genome from Ty1 integration upstream of tRNA genes.
Neddylated. HRT1-binding is necessary for RUB1/NEDD8 modification of RTT101. The modification enhances ubiquitin-ligase activity.
Essential for life in oxygen, but nonessential under anaerobic conditions. Required for biogenesis of the large ribosomal subunit and initiation of translation in oxygen (PubMed:23318452). The complex LTO1:YAE1 functions as a target specific adapter that recruits apo-RLI1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery (PubMed:26182403).
Forms a complex with YAE1; the complex bridges the interaction between the CIA complex and RLI1 (PubMed:23318452). Associates with the CIA complex (via its C-terminal tryptophan) (PubMed:26182403).
Present with 322000 molecules/cell in log phase SD medium.
Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro/Leu-Ala/Ser (NPA).
Channel protein for glycerol. Has a role in both glycerol influx and efflux. Plays a role in osmoregulation: under osmotic stress the channel is apparently closed to allow accumulation of glycerol in the cell under hyperosmotic conditions.
Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2.
The DPH-type metal-binding (MB) domain can bind either zinc or iron ions.
Belongs to the mitochondrion-specific ribosomal protein mL58 family.
Present with 350 molecules/cell in log phase SD medium.
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). Required for HMG2-induced ER-remodeling.
Belongs to the amidase family. GatA subfamily.
Component of the checkpoint clamp complex composed of DDC1, MEC3 and RAD17. The interaction with MEC3 is performed in a RAD17-dependent manner. The checkpoint clamp complex loads onto DNA. Interacts with the DNA polymerase zeta subunit REV7. Forms also a heterotrimer with 2 RAD17 subunits. Interacts with SET1.
Phosphorylation at Ser-230 by cAMP-dependent protein kinase A does not affect DNA binding but appears to prevent transcription of ADH2 during glucose repression.
Required for transcriptional activation of glucose-repressible alcohol dehydrogenase (ADH2).
Homodimer. Interacts with DOP1, ARL1 and NEO1.
Required for traffic between late Golgi and early endosomes. Required for endocytosis and maintenance of vacuolar structure.
Belongs to the helicase family. HRQ1 subfamily.
Forms heptamer rings (PubMed:24440721). Interacts with RAD4 (PubMed:24682993).
Helicase with 3'-5' helicase activity involved in genome stability (PubMed:23456718, PubMed:24440721, PubMed:24700328). Functions in the RAD4-dependent nucleotide excision repair (NER) pathway and plays a critical role in DNA interstrand cross-link repair (PubMed:24440721, PubMed:24682993). Unwinds relatively long duplex DNA up to 120-bp and requires a long 3'-tail of at least 70 nucleotides for efficient unwinding of duplex DNA (PubMed:23026052). Activity is significantly stimulated by a preexisting fork structure (PubMed:24682993). Shows both processive helicase and DNA strand annealing activities (PubMed:24682993). Affects telomere length by a non-catalytic mechanism, probably through inhibiting telomerase by competing with it for ssDNA binding (PubMed:24440721).
Leads to increased mitotic recombination and spontaneous mutation, as well as to sensitivity to 4-nitroquinoline 1-oxide and cisplatin (PubMed:23456718). Causes also hypersensitivity to DNA interstrand cross-links (ICLs) and telomere addition to DNA breaks (PubMed:24440721).
Belongs to the dynein light intermediate chain DYN3 family.
Component of the cytoplasmic dynein which acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play an important role in the proper orientation of the mitotic spindle into the budding daughter cell yeast. Probably required for normal progression of the cell cycle.
The dynein complex consists of at least two heavy chains and a number of intermediate and light chains. Interacts with DYN1.
Inhibited by inositol hexakisphosphate and benzene tri-, tetra- and hexacarboxylates.
Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also Catalyzes the reaction of EC 5.4.2.4 (synthase), but with a reduced activity.
Present with 172000 molecules/cell in log phase SD medium.
Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis.
By heat shock, high osmolarity, oxidative stress, DNA damage and glucose starvation.
Transcriptional repressor which binds to the consensus sequence 5'-GCCTCGA[G/A]G[C/A]-3'. Represses CLN1 transcription.
Belongs to the MICOS complex subunit Mic19 family.
Belongs to the HMG-CoA reductase family.
HMG-CoA reductase; part of the first module of ergosterol biosynthesis pathway constitutes by the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (PubMed:3065625, PubMed:3526336). HMG1 and HMG2 catalyze the reduction of hydroxymethylglutaryl-CoA (HMG-CoA) to mevalonate that is the rate-limiting step within the first mosule (PubMed:3526336). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthase ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases HMG1 and HMG2 which are derived from a single ancestral HMGR gene by gene duplication (PubMed:32679672).
The sterol-sensing domain (SSD) is required for sterol pathway signals to stimulate hmg2 ER-associated degradation and detects both geranylgeranyl pyrophosphate and a secondary oxysterol signal.
When both HMG1 and HMG2 are deleted, cells are unable to undergo spore germination and vegetative growth.
Present with 2440 molecules/cell in log phase SD medium.
Required for mitochondrial iron-sulfur proteins biosynthesis.
Required for initiation of translation of the COX1 coding region. Also involved in the stability of the intron containing transcript of COX1.
Belongs to the class I-like SAM-binding methyltransferase superfamily. METTL21 family. EFM6 subfamily.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 1-alpha (TEF1 and TEF2) at 'Lys-390'.
Interacts with HRR25. May interact with SEC72.
Present with 15400 molecules/cell in log phase SD medium.
Although initial characterizations described PCA1 as a copper-transporting ATPase, subsequent experiments have demonstrated that PCA1 is capable of high affinity copper ion binding, but not active copper ion transport.
Cadmium transporting P-type ATPase which plays a critical role in cadmium resistance by extruding intracellular cadmium. Capable of high affinity copper ion binding, but not active copper ion transport. May play a role in copper resistance by chelating and sequestering copper ions.
In the absence of cadmium, is ubiquitinated and targeted for degradation before reaching the plasma membrane. This allows a rapid and specific cellular response to cadmium.
Strain S288C, as well as other laboratory cadmium-sensitive strains, contain a natural Gly-970-Arg mutation which eliminates cadmium transport function. Loss of cadmium resistance provides a fitness advantage under cadmium-free conditions.
Binds human HTN3/histatin-5, a peptide from saliva, and mediates its fungicidal activity. Interacts with polyadenylate-binding protein PAB1 and Hsp70 chaperone SSA1 on translating ribosomes. Interacts with NAP1.
May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A functional difference between SSA1 and SSA2 proteins is expected. SSA1 can participate in the ATP-dependent disassembly of clathrin-coated vesicles.
Present with 269000 molecules/cell in log phase SD medium.
Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is involved in transcriptional regulation. Heterodimer of ARP7 and ARP9 functions with HMG box proteins to facilitate proper chromatin architecture. Heterodimer formation is necessary for assembly into RSC complex. Part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Forms a heterodimer with ARP9. Interacts with NPL6. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin. Component of the SWI/SNF global transcription activator complex. The 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29.
Catalytic subunit of mitochondrial acetolactate synthase, which catalyzes the first of a series of common steps in the biosynthesis of the branched-chain amino acids. Catalyzes the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate (AL) or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate (AHB). The first product is the precursor for valine and leucine biosynthesis, while the second leads to isoleucine.
Contains 1 molecule of FAD per monomer. The role of this cofactor is not clear considering that the reaction does not involve redox chemistry.
Homodimer. The acetolactate synthase complex contains the catalytic subunit ILV2 and the regulatory small subunit ILV6.
The regulatory subunit ILV6 stimulates enzymatic activity seven- to tenfold and confers sensitivity to inhibition by valine and activation by ATP.
Belongs to the protoporphyrinogen/coproporphyrinogen oxidase family. Protoporphyrinogen oxidase subfamily.
Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Displays sensitivity to DNA damaging agents.
Can heterodimerize with RLM1. Interacts with HOG1.
Transcription factor that controls part of the HOG1-mediated osmostress responses. Binds to the DNA sequence 5'-ACTACTA[TA](4)TAG-3'. Does not appear to function in the MPK1 pathway.
During S phase of the cell cycle. Expression is cell cycle regulated by HCM1.
Phosphorylation of Thr-319 by CDC28 is required for the interaction with FKH2 and recruitment to promoters.
Present with 779 molecules/cell in log phase SD medium.
Transcription activator involved in G2/M transcription through its association with FKH2.
Involved in the uptake of inorganic phosphate.
Activates the ARF proteins by exchanging bound GDP for free GTP. Plays a role in maintaining mitochondrial morphology (PubMed:25190516).
Involved in regulation of meiotic recombination and repair of DNA damage. Inhibits RAD51-mediated recombination when the meiotic recombination machinery is impaired.
Converts protoheme IX and farnesyl diphosphate to heme O.
Farnesyl pyrophosphate and geranyl pyrophosphate inhibit mevalonate kinase by binding competitively at the ATP-binding site.
Mevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (PubMed:1645230). ERG12 converts mevalonate into 5-phosphomevalonate (PubMed:1645230). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD1/ERG19 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (PubMed:32679672).
Trans-acting regulatory protein that activates transcription of the CUP1 gene (metallothionein) in response to copper ions. Binds to the CUP1 UAS sequence 5'-GCTTCTTTTCCGCTGA-3'. Binds DNA only in presence of copper or silver. Copper seems to alter the conformation of the protein.
Ergosteryl beta-glucosidase involved in the ergosteryl beta-glucoside (EG) catabolic pathway and vacuole formation via hydrolysis of EG to generate glucose (PubMed:26116408). Is also able to hydrolyze cholesteryl beta-glucoside and sitosteryl beta-glucoside to generate glucose; and C6-7-nitro-2,1,3-benzoxadiazole (NBD)-GlcCer to generate C6-NBD-ceramide (Cer) (PubMed:26116408).
Resulted in the accumulation of ergosteryl beta-glucoside (EG) and fragmentation of vacuoles.
Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Responsible for the N-terminal methylation of the ribosomal proteins RPL12A, RPL12B, RPS25A and RPS25B.
Belongs to the methyltransferase superfamily. NTM1 family.
Defects in both translation efficiency and fidelity.
Belongs to the Mediator complex subunit 4 family.
Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. MED4 interacts directly with MED1, MED7 and SRB7/MED21.
Present with 1617 molecules/cell in log phase SD medium.
E3 ubiquitin-protein ligase which functions in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, 2 E2 ubiquitin conjugating enzymes. Involved in nutritional control of the cell cycle. Required for proper spindle positioning, likely regulating septin ring deposition at the bud neck.
UBC4-dependent autoubiquitination occurs at Lys-211, Lys-258, Lys-288, Lys-310, Lys-333, Lys-343, Lys-346, Lys-366, Lys-406, Lys-412 and Lys-423. UBC4-dependent autoubiquitination is responsible for DMA2 turnover. UBC13/MMS2-dependent autoubiquitination occurs at Lys-258, Lys-310, Lys-346 and Lys-366. Lys-211, Lys-256, Lys-288, Lys-310, Lys-343, Lys-258, Lys-366 and Lys-412 are also ubiquitinated in trans by DMA1 E3 ligase in association with UBC4.
There are two plasma membrane ATPases in yeast. This is the minor isoform.
Component of a SNARE complex consisting of SED5, BOS1, BET1 and SEC22 or YKT6. Interacts with SEC24.
Belongs to the peptidase M28 family. M28E subfamily.
May play a role in endocytic and/or exocytic pathways.
Required for the proteolytic cleavage of the transcription factor RIM101 in response to alkaline ambient pH (By similarity). Required for growth at alkaline pH.
Cell wall stress sensor. Involved in activation of a response that includes both stress-related increased chitin synthesis and the MPK1 mitogen-activated protein kinase cell integrity pathway. High-copy activator of the SKN7 transcription factor. Required during induction of MPK1 tyrosine phosphorylation under a variety of stress conditions. Required for PKC pathway activation under low pH conditions. Required for cell integrity signaling during pheromone-induced morphogenesis. Activates ROM1 or ROM2 catalyzed guanine nucleotide exchange toward RHO1 in cell wall integrity signaling.
Acyl-CoA-independent ceramide synthase that catalyzes the conversion of dihydroceramide and also phytoceramide to dihydrosphingosine or phytosphingosine. Prefers dihydroceramide. Very low reverse hydrolysis activity, catalyzing synthesis of dihydroceramide from fatty acid and dihydrosphingosine. Is not responsible for the breakdown of unsaturated ceramide. May play a role in heat stress response.
Belongs to the alkaline ceramidase family.
Glutathione peroxidase-like protein that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress (PubMed:10480913, PubMed:11445588). Has peroxidase activity using thioredoxin or glutathione as a reducing power (PubMed:20572871, PubMed:22659048). Involved in peroxisome formation (PubMed:22659048).
Impairs growth and peroxisome formation in oleic acid medium.
Was originally thought to be a glutathione peroxidase (PubMed:10480913) or a phospholipid hydroperoxide glutathione peroxidase (PubMed:11445588), but functions as an atypical 2-Cys peroxiredoxin using both glutathione and thioredoxin almost equally as reducing power instead (PubMed:20572871).
Required for mother cell-specific ho expression. Might be required for the transport of factors (such as ASH1) that promote HO repression from the mother cell into its bud.
Belongs to the peptidase M28 family. M28A subfamily.
Present with 4740 molecules/cell in log phase SD medium.
Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione (PubMed:11050082, PubMed:8824231). Can use gamma-glutamylcysteine as a substrate (PubMed:8824231).
Identified in the GID complex. In the absence of glucose, the complex contains VID30/GID1, the E3 ubiquitin-ligase RMD5/GID2, VID28/GID5, GID7, GID8, and FYV10/GID9. When cells are shifted to glucose-containing medium, VID24/GID4 is induced and becomes part of the complex (PubMed:22645139). Within the GID complex, interacts directly with VID30/GID1, RMD5/GID2 and FYV10/GID9 (PubMed:22645139).
Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium (PubMed:12686616). Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:12686616). Required also for cell cycle progression. Positively controls G1 and the timing of START (PubMed:15590836).
Essential for meiotic chromosome segregation. MER1 and MER2 proteins must interact directly or indirectly. MER1 might be responsible for regulating the MER2 gene and/or gene product. MER2 is not required for mitosis and mitotic DNA repair mechanisms. Component of the MER2-MEI4-REC114 complex which seems to be required for meiotic double-strand break (DSB) formation.
Interacts with MEI4, REC114 and XRS2. Component of the MER2-MEI4-REC114 complex.
Phosphorylated during meiotic prophase. Dephosphorylation seems to be dependent on DSB formation.
Required for sorting and processing of soluble vacuolar proteins, integrity of vacuolar morphology, efficient segregation of vacuolar material into the bud during the cell cycle, acidification of the vacuolar lumen, and assembly of the vacuolar H(+)-ATPase.
Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is involved in meiotic sporulation through regulating IME2 expression.
Although no clear MSS51 ortholog is encoded in mammalian genomes, the mammalian MSS51/ZMYND17 protein of unknown function is significantly similar.
Has a dual role in the assembly of cytochrome oxidase subunit 1 (COX1). It has a regulative function on COX1 synthesis, acting as a translational activator specific for the COX1 mRNA, and it also binds to newly synthesized COX1 protein. Together with COX14, may act as a chaperone that binds efficiently unassembled COX1 and prevents it from unproductive aggregation. When bound to COX1, MSS51 is unable to interact with the COX1 mRNA and translation is halted. This may be a feedback control that ensures that COX1 is only produced as long as potentially harmful assembly intermediates are not accumulating.
Present with 18600 molecules/cell in log phase SD medium.
Homodimer (PubMed:31015336). Interacts with SLX5 (PubMed:31015336).
Prevents ub-hotspot formation and exacerbates heat sensitivity of cells deficient in Rpd3L histone deacetylase complex members (PubMed:31015336). Leads to the up-regulation of the expression of the Rpd3S complex subunit RCO1 of the Rpd3S complex and down-regulation of HSP12 and SIR2 (PubMed:31015336).
Sumoylated at Lys-231 and subsequently ubiquitinated by the SUMO-targeted ubiquitin ligase (STUbL) complex SLX5/SLX8.
The coiled-coil motif is required for homodimerization.
Transcription factor-like protein that binds to specific DNA motifs called ub-HS-motif associated with several locations where proteins other than histone H2B are ubiquitinated (ub-hotspots) (PubMed:31015336). Ubiquitination at these sites depends on the SUMO-targeted ubiquitin ligase (STUbL) complex SLX5/SLX8 and protein turnover on the CDC48 segregase (PubMed:31015336). UBC9, SIZ1, or SIZ2 sumoylate DNA-bound EUC1 to stabilize its DNA-binding (PubMed:31015336). Sumoylated EUC1 acts a cofactor required for the recruitment of the SLX5/SLX8 STUbL complex via specific contacts between EUC1 and SLX5, as well as an additional SUMO-mediated interaction (PubMed:31015336). SLX5/SLX8 then ubiquitinates EUC1 and presumably other targets at ub-hotspots, and the CDC48/UFD1/NPL4 complex, together with UBX4 and UBX5, removes Lys-48-linked ubiquitinated proteins from chromatin. Ubiquitinated proteins could be either degraded by the proteasome or recycled by deubiquitination (PubMed:31015336). EUC1 itself does not seem to underlie extensive turnover, as it is a very stable protein (PubMed:31015336). EUC1 is able to act as a transcription factor, but its function at ub-hotspots does not seem to depend on this ability (PubMed:31015336). EUC1-mediated ub-hotspots are crucial during stress responses when gene expression control is impaired (PubMed:31015336).
Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to proteins having the C-terminal -XCC or -XCXC, where both cysteines may become modified. Acts on YPT1 and SEC4.
Belongs to the class I-like SAM-binding methyltransferase superfamily. BUD23/WBSCR22 family.
Interacts with TRM112. Interacts with ECM16.
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of guanine 1575 (m7G1575) in 18S rRNA. Requires the methyltransferase adapter protein TRM112 for full rRNA methyltransferase activity. Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity. Required for efficient cleavage of the primary 35S precursor rRNA at site A2. Involved in positioning the proximal bud pole signal.
Belongs to the DNA polymerase type-Y family.
Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents. Involved in mitochondrial DNA mutagenesis.
Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA (PubMed:10523634, PubMed:9315678, PubMed:9472021, PubMed:9848653). This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1 (PubMed:10523634, PubMed:9315678, PubMed:9472021, PubMed:9848653). Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs and play a central role in ribosomal RNA processing (PubMed:10523634, PubMed:9315678, PubMed:9472021, PubMed:9848653). The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs (PubMed:21131909, PubMed:25219674). Catalyzes pseudouridylation at position 93 in U2 snRNA (PubMed:21131909). Also catalyzes pseudouridylation of mRNAs; H/ACA-type snoRNAs probably guide pseudouridylation of mRNAs (PubMed:25219674). It is a centromeric DNA-CBF3-binding factor which is involved in mitotic chromosome segregation (PubMed:8336724). Essential for cell growth (PubMed:8336724).
Component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs) (PubMed:9472021, PubMed:9848653, PubMed:15388873, PubMed:21131909). The protein component of the H/ACA snoRNP contains CBF5, GAR1, NHP2 and NOP10 (PubMed:9472021, PubMed:9848653, PubMed:15388873). The complex contains a stable core composed of CBF5 and NOP10, to which GAR1 and NHP2 subsequently bind (PubMed:9472021, PubMed:9848653, PubMed:15388873). Also interacts with NAF1 and SHQ1, which may be required for assembly of H/ACA snoRNP complexes. May also associate with the CBF3 110 kDa subunit (CBF2). Interacts with the trimethylguanosine synthase (TGS1) and with NOP53.
Present with 33600 molecules/cell in log phase SD medium.
ATP-dependent kinase whose specificity is not yet known.
Transports zinc from storage in the vacuole to the cytoplasm.
Belongs to the TALE/CUP9 homeobox family.
Probable DNA-binding protein which plays a role in protecting yeast cells against copper toxicity. May regulate the expression of important copper homeostatic genes.
Interacts with the Hsp70 chaperones SSA1 and SSB1.
Involved in protein translation, propagation of [PSI+] prions, and polyamine tolerance. Functions as a nucleotide exchange factor (NEF), which accelerates the release of ADP, for the cytosolic Hsp70 chaperone SSA1 and the ribosome-associated Hsp70 chaperone SSB1. Required for fully efficient Hsp70-mediated folding of proteins.
Present with 13100 molecules/cell in log phase SD medium.
CAD1/YAP2 expression is at least partially regulated at the level of mRNA stability. Two small upstream open reading frames (uORF) in its mRNA cause increased RNA decay. The translation initiation factor eIF2 counteracts this effect by causing reinitiation at the functional initiation site, thus suppressing RNA decay.
Contains a C-terminal cysteine rich domain (c-CRD), but lacks the N-terminal CRD (n-CRD) found in its paralog YAP1. It probably also contains embedded in the c-CRD a nuclear export signal, with which the nuclear export protein CRM1/exportin 1 may interact in the absence of inter- or intramolecular disulfide bonds (or otherwise oxidized/modified cysteines) within the c-CRD.
Depending on the oxidative stress inducing agent, CAD1/YAP2 can undergo two distinct conformational changes, both through oxidation of cysteine residues, and both masking the nuclear export signal, thus abolishing nuclear export by CRM1/exportin 1. Peroxide stress induces the formation of possible intramolecular disulfide bonds as well as intermolcular disulfide within a homodimer. Cadmium may bind directly to specific cysteine residues (Cys-391 and either Cys-356 or Cys-387) in the c-CRD.
Homodimer; disulfide-linked, upon oxidation (Probable). Interacts in the nucleus with the nuclear export protein CRM1 (PubMed:17187783). Interacts with RCK1 (PubMed:15341652).
Hypersensitive to the cytotoxic metal cadmium.
Transcription activator involved in oxidative stress response and cadmium resistance. Regulates the transcription of genes overrepresented for the function of stabilizing proteins including the inducible Hsp90-family protein HSP82. Preferentially binds to promoters with the core binding site 5'-TTA[CG]TAA-3'. Activity of the transcription factor is controlled through oxidation of specific cysteine residues resulting in the alteration of its subcellular location. Activation by alkyl hydroperoxides or cadmium induces nuclear accumulation and as a result CAD1/YAP2 transcriptional activity.
Component of the phosphopantothenoylcysteine decarboxylase (PPCDC) complex, a heterotrimer composed of CAB3, HAL3 and VHS3.
Component of the phosphopantothenoylcysteine decarboxylase (PPCDC) involved in the coenzyme A synthesis.
Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. Fusion between endosomes and the vacuole will then target the cargo proteins to the vacuolar lumen. Acts as an adapter that recruits the DOA4 deubiquitinase to the endosomes, leading to deubiquitination of cargo proteins prior to the lumenal sequestration. Its association to the endosomes depends on SNF7 and its dissociation requires VPS4. Interacts functionally with the Pkc1p-mitogen-activated protein kinase pathway.
Present with 10200 molecules/cell in log phase SD medium.
The BRO1 domain may be involved in the binding to SNF7.
The coiled-coil domain is essential for MVB sorting.
Belongs to the group II decarboxylase family. Sphingosine-1-phosphate lyase subfamily.
Leads to the accumulation of endogenous phosphorylated sphingoid bases, and exhibits unregulated proliferation upon approach to stationary phase (PubMed:10329480). Causes a reduction in total C15 and C17 phosphatidylcholine levels (PubMed:25345524).
Sphingosine-1-phosphate lyase that cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine (PubMed:20696404, PubMed:25345524, PubMed:9334171). Prefers C-16 dihydrosphingosine-l-phosphate (DHS-P) as a substrate. Regulates intracellular levels of sphingolipid long-chain base phosphates (LCBPs) (PubMed:11795842). Plays a role in the regulation of global responses to nutrient deprivation in yeast (PubMed:10329480).
Catalyzes the attachment of asparagine to tRNA(Asn) in the mitochondrion.
Belongs to the RSC7/SWP82 family. SWP82 subfamily.
Interacts with SWI3 and SNF12. Component of the SWI/SNF global transcription activator complex. The 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29.
May act as a cytoplasmic retention protein with a role in regulating nuclear transport. Binds nuclear localization sequences in vitro. Needed to adapt efficiently to ethanol, either as sole carbon source or as cell stressor. Involved in ethanol-dependent transcriptional activation of several genes and ethanol-induced protein turnover of some proteins.
Required for efficient assembly of cytochrome c oxidase in the mitochondrial inner membrane. Seems to be involved in the SHY1-mediated step of cytochrome c oxidase maturation. May aid in stabilizing an early COX1 intermediate containing the nuclear subunits COX5A and COX6.
Was originally thought to be involved in mitochondrial protein import.
Interacts with PRP11. Associates with the U2 snRNA.
U2 snRNP protein which helps to refold U2 into a structure favorable for its binding to SF3b and SF3a prior to spliceosome assembly. Mediates functional interactions between U2 RNA and PRP5. Enforces ATP dependence during formation of the prespliceosome by brokering an interaction between PRP5 and the U2 snRNP that depends on correct U2 RNA structure.
May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi. May be involved in invertase secretion.
Required for localization and recycling of the CPY sorting receptor (VPS10) to the late-Golgi compartment. Involved in the retention of proteins to the late-Golgi. Plays an integral role in the complex vacuolar protein sorting process.
Abnormal punctate localization of TOR1 (PubMed:32801125). Sensitive to high hydrostatic pressure (PubMed:32801125). Resistance to tunicamycin (endoplasmic reticulum stressor) administered together with FK506 (calcineurin inhibitor) (PubMed:26510498). Sensitive to rapamycin (TORC1 signaling-inhibitor) (PubMed:28993463). Simultaneous disruption of GTR1 results in abnormal localization of TOR1 and PIB2 to vacuoles and abnormal activation of TORC1 in nitrogen-replete conditions (glutamine or leucine nitrogen source) (PubMed:28993463).
Belongs to the GTR/RAG GTP-binding protein family.
GTPase involved in activation of the TORC1 signaling pathway, which promotes growth and represses autophagy in nutrient-rich conditions (PubMed:26510498, PubMed:15989961, PubMed:32801125, PubMed:28993463). Also required for TORC1 inactivation during nitrogen starvation (PubMed:28993463). Required for intracellular sorting of GAP1 out of the endosome (PubMed:16732272). Involved in the regulation of microautophagy (PubMed:15989961).
Heterodimer; with GTR1 (PubMed:21816923). Component of the GSE complex composed of GTR1, GTR2, SLM4, MEH1 and LTV1 (PubMed:16732272). Component of the EGO complex, at least composed of GTR2, SLM4 and MEH1 (PubMed:15989961). Interacts with GTR1; the interaction is direct (PubMed:21816923).
Belongs to the small GTPase superfamily. SAR1 family.
COPII is composed of at least 5 proteins: the SEC23/24 complex, the SEC13/31 complex and SAR1. Interacts with EMP24.
Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SAR1 controls the coat assembly in a stepwise manner. Activated SAR1-GTP by SEC12 binds to membranes first and recruits the SEC23/24 complex. These SEC23/24-SAR1 prebudding intermediates are then collected by the SEC13/31 complex as subunits polymerize to form coated transport vesicles. Conversion to SAR1-GDP triggers coat release and recycles COPII subunits.
Interacts (via myosin motor domain) with SHE4; this interaction is important for proper localization and may regulate the interaction of the motor domain with actin. Interacts (via SH3 domain) with VRP1; this interaction is required for localization to sites of polarized growth and may regulate the interaction of the tail domain with actin. Interacts (via SH3 domain) with PAN1; this interaction is important for late stages of endocytopsis. Interacts (via SH3 domain) with BBC1 and LAS17. Interacts (via C-terminal acidic tail) with ARC19 and ARC40; ARC19 and ARC40 are Arp2/3 complex subunits. Interacts with BZZ1, PKH1, PKH2, YPK1 and YPK2.
Phosphorylation of the TEDS site (Ser-357) is required for the polarization of the actin cytoskeleton and for ligand-induced, but not for constitutive internalization of STE2. Phosphorylation probably activates the myosin-I ATPase activity. Ser-357 is phosphorylated by YPK2 in vitro.
Interacts with PAN1 and the clathrin heavy and light chains CHC1 and CLC1.
Involved in endocytosis and clathrin cage assembly.
Mutants are deficient in mitochondrial protein synthesis.
Binds preferentially to the U4/U6 hybrid snRNAs. Can stimulate the annealing of U4 and U6. Could participate in both the formation and disassembly of the U4/U6 hybrid during splicing.
Stabilizes the HMG-CoA reductase HMG2 by preventing its HRD1-dependent degradation. Binds directly to the sterol-sensing domain (SSD)-containing transmembrane region of HMG2, promoting its folding to protect it from degradation.
Expression is increased in response to DNA replication stress (PubMed:22842922). Expression is regulated by ZAP1 during zinc-deficiency via changes in transcription start sites (PubMed:31692084). Expression is also down-regulated during unfolded protein response (UPR) (PubMed:32475637, PubMed:33184379).
Homodimer (By similarity). Interacts with KIN28 (PubMed:10958787).
Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2 (PubMed:11805111). Plays a role in the regulation of kinase KIN28 function (PubMed:10958787). Essential for growth on galactose media at elevated temperatures (PubMed:11805111).
It is uncertain whether Met-1 or Met-15 is the initiator.
Component of the PAF1 complex which consists of at least CDC73, CTR9, LEO1, PAF1 and RTF1. Interacts with SPT6. Interacts with FACT subunits POB3 and SPT16.
The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2. In complex with PAF1, required for normal CLN1 and CLN2 G1 cyclin expression in late G1. Also has a role in chromosome segregation where it appears to be involved in microtubule placement.
Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events. COG2 is required for ER to Golgi vesicle docking. Not essential for viability.
Component of the conserved oligomeric Golgi (COG or Sec34/Sec35) complex which consists of eight different proteins COG1-COG8. The COG complex interacts with the Rab GTPase YPT1, the Glogi SNAREs GOS1, SEC22, SED5, VTI1 and YKT6 and the COPI coatomer subunit gamma SEC21.
Abolishes canavanine sensitivity (PubMed:3327612). Extends replicative lifespan and leads to distinct changes in transcriptional and translational profiles, including translational activation of the GCN4 transcription factor (PubMed:28228255).
High-affinity permease for arginine (PubMed:8436127, PubMed:9231419, PubMed:10654085, PubMed:11746604).
Phosphorylated probably at multiple sites (PubMed:9544242).
Activated by GTP. Subject to allosteric product inhibition by CTP. Inhibited by p-chloromercuriphenylsulfonic acid, N-ethylmaleimide and cyclopentenylcytosine (CPEC).
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Plays an important role in the regulation of phospholipid synthesis.
Belongs to the Mediator complex subunit 16 family.
Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. Interacts with HOG1.
Acetylated by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex, and/or by GCN5, a component of the SAGA complex, to form H2A.ZK3Ac, H2A.ZK8Ac, H2A.ZK10Ac and H2A.ZK14Ac once deposited into chromatin (PubMed:16543223). Acetylation is required for function at telomeres (PubMed:16543222). H2A.ZK14Ac is acetylated at the promoters of active genes (PubMed:16543223).
In contrast to H2A1 and H2A2, appears to be weakly or not sumoylated.
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers (Probable). The octamer wraps approximately 147 bp of DNA. H2A or its variant H2A.Z forms a heterodimer with H2B. H2A.Z associates with the VPS72/SWC2 subunit of the SWR1 chromatin remodeling complex. Interacts also with RBP1/DNA-directed RNA polymerase II largest subunit (PubMed:11509669). Interacts with NAP1 (PubMed:14645854, PubMed:14690608, PubMed:15045029, PubMed:16299513, PubMed:18086883). Interacts with MPS3 (PubMed:21518795).
To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H2A.ZK3ac = acetylated Lys-4; H2A.ZK8ac = acetylated Lys-9; H2A.ZK10ac = acetylated Lys-11; H2A.ZK14ac = acetylated Lys-15.
Variant histone H2A which can replace H2A in some nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. This variant is enriched at promoters, it may keep them in a repressed state until the appropriate activation signal is received (PubMed:11000274, PubMed:11081628, PubMed:11090616, PubMed:11509669, PubMed:12628191, PubMed:14645854, PubMed:14690608, PubMed:15045029, PubMed:16239142, PubMed:16344463, PubMed:16543223). Near telomeres, it may counteract gene silencing caused by the spread of heterochromatin proteins (PubMed:16543222). Required for the RNA polymerase II and SPT15/TBP recruitment to the target genes (PubMed:11509669). Involved in chromosome stability (PubMed:15353583). Required to target MPS3 to the inner membrane of the nuclear envelope (PubMed:21518795).
Regulator of the mitotic function of yeast type 1 protein phosphatase.
May negatively regulate the SNF1 kinase by promoting the interaction of the REG1/GLC7 phosphatase complex with the kinase. Deletion of SIP5 promotes resistance to artimisin, which is probably an indirect effect of an action on the electron transport chain.
Component of the nuclear pore complex (NPC) (PubMed:10684247). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NUP42 interacts with the NUP82 subcomplex. It interacts directly with GLE1, and through its FG repeats with GFD1, the heterodimeric mRNA transport factor MEX67/MTR2, and the karyopherin CRM1.
Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. FG repeat types and their physico-chemical environment change across the NPC from the nucleoplasmic to the cytoplasmic side: SXFG/PXFG repeats are especially abundant in NUPs on the cytoplasmic side.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP42 is specifically important for nuclear protein and mRNA export.
High-affinity permease for basic amino acids.
ATG19 is important for yeast autolysis which is the source of several molecules responsible for the quality of wines aged in contact with yeast cells.
Cargo-receptor protein involved in the cytoplasm to vacuole transport (Cvt) and in autophagy. Recognizes cargo proteins, such as APE4, LAP3, LAP4 and AMS1 and delivers them to the pre-autophagosomal structure for eventual engulfment by the autophagosome and targeting to the vacuole. Involved in the organization of the preautophagosomal structure (PAS). ATG19 association with cargo protein is required to localize ATG11 to the PAS. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates, and is essential for the survival of cells subjected to severe ER stress. Also plays a role in regulation of filamentous growth.
Interacts with the vacuolar aminopeptidase 1 (LAP4) precursor and mature forms. Also interacts with AMS1, APE4, ATG8 ATG11, and UBP3.
Polyubiquitinated at Lys-213 and Lys-216. Deubiquitination by UBP3 is required for full activity of ATG19.
The C-terminal WXXL motif is crucial for ATG8-binding and Cvt pathway.
The coiled coil domain is required for the interaction with LAP4.
Regulator of the mitochondrial protein import machinery that is localized in the mitochondrial intermembrane space (IMS) and facilitates the transport of proteins from the cytosol into the mitochondrial matrix (PubMed:32826315). Not essential for mitochondrial protein import but induced and required when mitochondrial import is compromised (PubMed:32826315). Stimulates or stabilizes the translocation into the mitochondria of proteins such as OXA1, ATP1 and COX12 (PubMed:32826315).
The Cx14C/Cx13C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system and the subsequent transfer of disulfide bonds by dithiol/disulfide exchange reactions to the newly imported protein.
Up-regulated by RPN4 transcription factor upon mitochondrial protein-induced stress conditions such as the accumulation in the cytosol of non-imported mitochondrial precursors.
Involved in surveillance of pre-rRNAs and pre-mRNAs, and the degradation of cryptic non-coding RNAs (ncRNA) derived from intergenic regions and the ribosomal DNA spacer heterochromatin. Binds RNA.
Lethal in combination with the absence of either RRP6 or its cofactor RRP47. Weak but detectable stabilization of unspliced pre-mRNAs, and stronger stabilization is detected for mRNAs with defects in 3' cleavage and polyadenylation.
Required for loading and maintenance of stable association of CDC45 with chromatin during initiation and elongation of DNA replication. Also involved in temporal regulation of origin firing. Required for the association of PSF1 with origins.
Binds 1 [4Fe-4S] cluster (PubMed:16420352). The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (PubMed:16420352). The cluster is required for structural integrity of the elongator complex, while it is not required for catalytic activity (PubMed:18986986).
Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:15769872, PubMed:17018299, PubMed:18755837, PubMed:21912530, PubMed:31309145). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). The complex functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin) (PubMed:11296232). May also be involved in sensitivity to Pichia inositovora toxin (PubMed:13680368). Independently, ELP3 may be involved in polarized exocytosis (PubMed:15780940).
Component of the elongator complex which consists of ELP1/IKI3, ELP2, ELP3, ELP4, ELP5/IKI1 and ELP6 (PubMed:10445034, PubMed:11435442, PubMed:11689709, PubMed:18986986, PubMed:27974378, PubMed:27872205). The elongator complex is composed of two copies of the Elp123 subcomplex (composed of ELP1/IKI3, ELP2 and ELP3) and two copies of the Elp456 subcomplex (composed of ELP4, ELP5/IKI1 and ELP6) (PubMed:27974378, PubMed:27872205). The Elp123 subcomplex forms a two-lobed scaffold, which binds the Elp456 subcomplex asymmetrically (PubMed:27974378, PubMed:27872205, PubMed:25960406). In each lobe, ELP2 is tightly sandwiched between ELP1/IKI3 and ELP3 (PubMed:31309145). The Elp123 subcomplex binds tRNA through ELP1/IKI3 and ELP3 and can bind 2 tRNAs simultaneously (PubMed:31309145). tRNA-binding induces conformational rearrangements which precisely position the targeted anticodon base in the active site (PubMed:31309145). ELP3 interacts with KTI11/DPH3 (PubMed:18986986, PubMed:27694803). ELP3 interacts with KTI12 (PubMed:15772087). The Elp456 subcomplex binds tRNA and has ATPase activity (PubMed:22343726).
Sensitive to caffeine and thermal stress (PubMed:18627462). Resistance to zymocin (PubMed:27694803, PubMed:18627462).
The elongator complex was originally thought to play a role in transcription elongation. Was reported to display histone acetyltransferase activity and to acetylate histone H3 preferentially at 'Lys-14', and H4 preferentially at 'Lys-8' (PubMed:10445034, PubMed:11904415, PubMed:15138274). However, it was later shown that the effect on histone acetylation and chromatin regulation is indirect and that the elongator complex is primarily involved in tRNA modification (PubMed:17018299, PubMed:18986986, PubMed:21912530).
Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Together with cyclin PCL7, controls glycogen phosphorylase and glycogen synthase activities in response to nutrient availablility. The PCL6-PHO85 cyclin-CDK holoenzyme has GLC8 kinase activity and phosphorylates and inactivates the phosphatase PP1-2 inhibitor GLC8, causing activation of PP1-2, which then dephosphorylates and activates glycogen phosphorylase. PCL6-PHO85 also phosphorylates YJL084C.
Forms a cyclin-CDK complex with PHO85. Interacts with the substrate protein YJL084C. Interacts with elongin-C, which stabilizes PCL6. Interacts with the CDK inhibitor (CKI) PHO81.
ATP-binding RNA helicase involved in 40S ribosomal subunit biogenesis and is required for the normal formation of 18S rRNAs through pre-rRNA processing at A0, A1 and A2 sites. Required for vegetative growth.
Belongs to the DEAD box helicase family. DDX49/DBP8 subfamily.
Functions as a component of the DNA-binding general transcription factor complex TFIID and the regulatory transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.
In TFIID, TAF6 heterodimerizes with TAF9, forming ultimately an octamer consisting of a TAF6/TAF9 heterotetramer core flanked by TAF4/TAF12 dimers on either side, similar to the histone H2A/H2B/H3/H4 octamer. The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14. Component of the 1.8 MDa SAGA complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9.
Present with 6506 (+/-1290) molecules/cell in log phase SD medium.
Could be an ATP-dependent permease. Confers hyper-resistance to the mutagens 4-nitroquinoline-N-oxide (4-NQO) and triaziquone, as well as to the chemicals sulphomethuron methyl phenanthroline when present in multiple copies. Exhibits nucleoside triphosphatase activity.
Encoded by the antisense strand of the FYV5 gene.
Transcriptional repressor which negatively regulates transcription of FYV5 by binding to the promoter on the sense strand.
Lyase that catalyzes the covalent linking of the heme group to the cytochrome C apoprotein to produce the mature functional cytochrome.
Required for processing of 5.8S rRNA (short form) at site A3 and for 5' and 3' processing of pre-tRNA.
Leads to elevated levels of Ty1 retrotransposition and Ty1 cDNA.
Abolishes methenyltetrahydrofolate synthase activity and leads to accumulation of folinic acid. Leads to a striking methionine deficiency when combined with ADE16 and ADE17, 2 isoenzymes involved in the purine synthesis.
Belongs to the 5-formyltetrahydrofolate cyclo-ligase family.
Only enzyme known to utilize 5-formyltetrahydrofolate (folinic acid) as substrate. Contributes to tetrahydrofolate metabolism in an alternative way of folate biosynthesis. May regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids.
DNA helicase which participates in several chromatin remodeling complexes, including the SWR1 and the INO80 complexes. The SWR1 complex mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. The INO80 complex remodels chromatin by shifting nucleosomes. Its ability to induce transcription of some phosphate-responsive genes is modulated by inositol polyphosphates. The INO80 complex is involved in DNA repair by associating to 'Ser-129' phosphorylated H2A histones as a response to DNA damage. RVB1 recruits ARP5 to the INO80 complex. During transcription may recruit SPT15/TBP to the TATA-boxes of involved genes. Required for box C/D and box H/ACA snoRNA accumulation and involved in pre-rRNA processing.
Probably forms a homohexamer. Interacts with RVB2 and may form heterododecamers with RVB2. Component of the SWR1 chromatin remodeling complex composed of at least ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4, SWC5, SWC7 and SWR1, and perhaps BDF1. Component of the chromatin-remodeling INO80 complex, at least composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3, IES4, IES6, ACT1, IES2, IES5 and INO80. Component of the R2TP complex composed of at least RVB1, RVB2, TAH1 and PIH1. Interacts with SPT15/TBP and HSP90.
Required for Fe(2+) ion low affinity uptake.
Identified in the Set3C complex with HOS2, SIF2, SNT1, CPR1, HOS4/YIL112W and SET3. Its presence is however not essential for meiotic repression by the Set3C complex. Interacts with SUM1 and RFM1. The interaction with SUM1 is mediated by RFM1.
NAD-dependent histone deacetylase involved in telomeric silencing. Histone deacetylase proteins act via the formation of large multiprotein complexes that are responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Restores silencing at HMR in SIR2 mutants when overexpressed. Required to repress middle sporulation genes during vegetative growth. Acts as a sensor of NAD(+) levels and regulator of NAD(+) biosynthesis. Regulates the gene expression of de novo NAD(+) biosynthesis genes.
Belongs to the ubiquitin-conjugating enzyme family. UEV subfamily.
Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of STP22, VPS28, SRN2 and MVB12 in a 1:1:1:1 stoichiometry. Interacts with HSE1 and VPS27. Interacts with MVB12 and SRN2.
Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association to the ESCRT-0 complex. Required for vacuolar targeting of temperature-sensitive plasma membrane proteins STE2 and CAN1.
The UEV domain is required for the interaction of the complex with ubiquitin.
Involved in chromosome segregation during meiosis. Involved in meiotic telomere clustering (bouquet formation) and telomere-led rapid prophase movements.
Rapidly induced by a shift to glucose-containing medium.
Substrate-recognition component of the GID complex, a multisubunit ubiquitin ligase that targets enzymes involved in gluconeogenesis for proteasomal degradation when cells are shifted to glucose-containing medium (PubMed:12686616, PubMed:18508925, PubMed:28126757). Specific for substrates with an N-terminal Pro (Pro/N-degron), including FBP1, ICL1 and MDH2 (PubMed:28126757). Has high affinity for the N-terminal sequence Pro-Thr-Leu-Val, and can bind peptides with an N-terminal sequence of the type Pro-[Gly,Ala,Ser,Thr,Asp,Asn,Tyr,His]-[Ala,Val,Leu,Ile,Lys,Arg]-[Val,Cys,Pro,Leu,Ile,Trp] (PubMed:28126757). Required for vacuolar degradation of FBP1 when cells are shifted to glucose-containing medium, probably by targeting FBP1-containing vesicles to the vacuole, but is not required for FBP1 sequestration in cytoplasmic vesicles (PubMed:9508768).
Substrate-recognition component of the GID ubiquitin ligase complex; interacts with proteins that have an N-terminal Pro/N-degron, including FBP1, ICL1 and MDH2 (PubMed:28126757). Identified in the GID complex, but only when cells are shifted to glucose-containing medium. In the absence of glucose, the complex contains VID30/GID1, the E3 ubiquitin-ligase RMD5/GID2, VID28/GID5, GID7, GID8, and FYV10/GID9. When cells are shifted to glucose-containing medium, VID24/GID4 is recruited to the complex via interaction with VID28/GID5 (PubMed:22645139).
To yeast YGR066c and S.pombe SpAC3H1.14.
Ubiquitinated by the GID complex, leading to subsequent proteasomal degradation.
Component of the high-osmolarity glycerol (HOG) pathway involved in mating response and osmotolerance. May act as a membrane anchor for the STE50/STE11 complex.
Interacts with SDH1 in its FAD-bound form.
Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Binds to the flavoprotein subunit SDH1 in its FAD-bound form, blocking the generation of excess reactive oxigen species (ROS) and facilitating its assembly with the iron-sulfur protein subunit SDH2 into the SDH catalytic dimer.
Component of the 90S pre-ribosomal particle.
Plays an important role in the synthesis of 18S rRNA but is not required for the 5.8S and 25S pathway. Is necessary for the cleavage at site A2. Is required for efficient association of RPS27 with the pre-ribosomal particle.
Identified in the GID complex. In the absence of glucose, the complex contains VID30/GID1, the E3 ubiquitin-ligase RMD5/GID2, VID28/GID5, GID7, GID8, and FYV10/GID9. When cells are shifted to glucose-containing medium, VID24/GID4 is induced and becomes part of the complex (PubMed:22645139). Within the GID complex, interacts with VID30/GID1; the interaction is direct (PubMed:22645139).
Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions such as folding and glycosylation of secretory proteins in the ER lumen.
Activated by C-terminal proteolytic cleavage. At neutral to alkaline ambient pH, the signaling protease (probably RIM13) cleaves RIM101, removing a C-terminal 8 kDa peptide to yield the active form.
Binds to DNA. Interacts with RIM20, which probably binds to the two YPX[LI] motifs and is required for proteolytic processing.
Present with 1822 molecules/cell in log phase SD medium.
Transcription factor that mediates regulation of both acid- and alkaline-expressed genes in response to ambient pH. At alkaline ambient pH, activates transcription of alkaline-expressed genes (including RIM101 itself), mainly by repressing transcriptional repressors of those genes, and represses transcription of acid-expressed genes. Required for meiosis, sporulation and invasive growth.
Belongs to the Dus family. Dus3 subfamily.
Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs (PubMed:12003496, PubMed:14970222). Specifically modifies U47 in cytoplasmic tRNAs (PubMed:14970222). Catalyzes the synthesis of dihydrouridine in some mRNAs, thereby affecting their translation (By similarity).
Has a dual role in the assembly of mitochondrial ATPase. Acts as a protease that removes the N-terminal 10 residues of mitochondrial ATPase CF(0) subunit 6 (ATP6) at the intermembrane space side. Also involved in the correct assembly of the membrane-embedded ATPase CF(0) particle, probably mediating association of ATP6 with the subunit 9 ring.
Belongs to the mannitol dehydrogenase family.
Catalyzes the NAD(H)-dependent interconversion of D-fructose and D-mannitol in the mannitol metabolic pathway.
Rescues temperature-sensitivity of MPT5 deletion.
There are two genes for this mannitol dehydrogenase in yeast, DSF1 and YNR073C.
Required for mRNA nuclear export. Involved in the nuclear pore complex (NPC) distribution and nuclear envelope morphology.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second largest subunit. A single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity).
In response to both anaerobic and osmotic stress. Expression seems to be under the control of YIG1.
Major isoform of glycerol-1-phosphate phosphohydrolase involved in glycerol biosynthesis. Plays a role in osmoadaptation and required for adaptation to anaerobic conditions.
Present with 193000 molecules/cell in log phase SD medium.
In zinc-depleted conditions and has increased expression in NAP1 deletion mutants.
Deletion HUR1 has been reported to cause increased sensitivity to hydroxyurea (PubMed:12615994). However, HUR1 partially overlaps with PMR1 and a later analysis revealed that deletion of PMR1 but not HUR1 affected resistance to hydroxyurea (PubMed:18069899).
No increased sensitivity to hydroxyurea.
Mitochondrial DNA endonuclease involved in intron homing. It introduces a specific double-strand break in the DNA of the COX1 gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Recognizes with high specificity and cleaves the sequence 5'-GGTTTTGGTAACTATTTATTAC-3'.
Strain Capensis / YB4237 has two stop codons in position 276 and 407, which disrupt the gene coding for this protein. Consequently, the corresponding intron containing its coding sequence is not mobile.
The mature protein may arise from proteolytic cleavage of an in-frame translation of some COX1 exons plus the intron containing the aI3 open reading frame.
Belongs to the prephenate/arogenate dehydrogenase family.
Presence of Phe represses the TYR1 gene expression.
The IMP cyclohydrolase activity resides in the N-terminal region.
MRS4 suppresses a mitochondrial splice defect in the first intron of the COB gene. It may act as a carrier, exerting its suppressor activity via modulation of solute concentrations in the mitochondrion (possibly of cations). Not essential.
Component of the GIN4 complex composed of at least BNI5, CDC3, CDC10, CDC11, CDC12, GIN4, NAP1 and SHS1. Interacts directly with CDC11 and CDC12.
Expression peaks during S phase of the cell cycle.
Required for normal septin function and cytokinesis.
Belongs to the glycosyl hydrolase 38 family.
Composed of isoforms with three constituent polypeptides described as [(107 kDa)-n (73 kDa)-(6-n) (31 kDa)-(6-n)], where n is 0-6. The 73 kDa and the 31 kDa polypeptides may be proteolytic derivatives of the 107 kDa polypeptide in the vacuole. Oligomerizes in the cytoplasm and retains its oligomeric form during import into the vacuole.
Degrades free oligosaccharides in the vacuole.
It is not specific for the 1,2-alpha-mannosidic linkage.
With MSL1, acts as a negative regulator of salt tolerance.
Desensitization to alpha-factor pheromone. Is involved in regulating the signaling pathway for responding to mating pheromone.
Present with 5980 molecules/cell in log phase SD medium.
The fungal-differentiation regulator (Fungal-DR) domain is only found in fungal regulator of G-protein signaling (RGS) proteins that regulate differentiation pathways. It is required for function (By similarity).
Acts as an allosteric regulator of polarized exocytosis by promoting the targeted fusion of vesicles with the plasma membrane. Involved in maintenance of ion homeostasis in cells exposed to NaCl stress. May be involved in the targeting of the myosin proteins to their intrinsic pathways. Multicopy suppressor of RHO3. May also participate in the maintenance of cell polarity and bud growth.
Belongs to the DEAD box helicase family. DDX31/DBP7 subfamily.
Belongs to the choline/ethanolamine kinase family.
Catalyzes the committed step in the synthesis of phosphatidylcholine by the CDP-choline pathway (PubMed:2536698, PubMed:9506987, PubMed:10329685). Also exhibits ethanolamine kinase activity but it is a poor substrate at 14% efficiency compared with choline (PubMed:2536698, PubMed:9506987).
Non-catalytic subunit of the NatB N-terminal acetyltransferase, which catalyzes acetylation of the amino-terminal methionine residues of all proteins beginning with Met-Asp or Met-Glu and of some proteins beginning with Met-Asn or Met-Met. NatB acetylates TPM1 protein and regulates tropomyocin-actin interactions. MDM20 is required for mitochondrial inheritance during budding and together with TPM1, is essential for the integrity and assembly of actin cables. Genetically interacts with CIN8.
Able to suppress the functional loss of YPT1. May form a channel. Protein SLY41 is not essential for cell viability. The SLY41 gene is a multicopy suppressor.
Involved in cation homeostasis and in the regulation of the cation stress signaling cascades. Also involved in bipolar budding.
Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. Seems to be implicated in the regulation of the expression of the ADH2 gene.
Could be the product of a pseudogene. YPL277C and YPL278C correspond to the N- and C-terminal regions of the uncharacterized protein YOR389W, respectively.
GTPase-activating protein (GAP) that stimulates specifically the intrinsic GTPase activity of Ypt/Rab-type GTPases YPT1 and YPT7 (PubMed:11359917, PubMed:19386605). Functions on the Golgi as a negative regulator of YPT1 (PubMed:11359917). Functions on the vacuole as a negative regulator of YPT7 (PubMed:11118206, PubMed:19386605). It is also active on SEC4 and YPT51 (PubMed:10508155). Provides a catalytic arginine (arginine finger) and glutamine (glutamine finger) in trans to accelerate the GTP hydrolysis rate of the substrate GTPase (Probable) (PubMed:16855591).
Probable transporter that confers resistance to short-chain monocarboxylic acids and quinidine.
Demethylates proteins that have been reversibly carboxymethylated. Demethylates the phosphatase PP2A catalytic subunits PPH21 and PPH22. Forms inactive complexes (PP2Ai) with phosphatase PP2A-like catalytic subunits. Involved in the regulation of cell cycle progression at START.
Interacts with and inactivates the phosphatase PP2A-like catalytic subunits PPG1, PPH21, PPH22, PPH3 and SIT4.
Was originally thought to be a mitochondrial ribosomal protein (PubMed:9151978), but has not been identified in the structure of the yeast mitoribosome (PubMed:28154081).
Required for the vacuolar uptake of large neutral amino acids including tyrosine, glutamine, asparagine, isoleucine and leucine. Requires ATP for function.
Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle. Required for growth on ethanol or acetate, but dispensable when fermentable carbon sources are available. Acts also on 2-methylisocitrate.
Impairs growth when acetate or ethanol are the sole carbon source. Leads to reduced chronological lifespan.
Phosphorylated and inactivated after addition of glucose to the cell culture (repressing conditions).
Phosphorylated in response to elevated glucose levels, leading first to reversible inactivation of the enzyme (short-term inactivation), and at a later stage to proteolytic degradation of the protein (long-term inactivation).
Repressed by glucose and induced by ethanol via the transcriptional activator CAT8. The promoter sequence located between -397 and -388 contains an upstream activating sequence (UAS)element whereas the sequence located between -261 and -242 contains an upstream repressing sequence (URS) element.
Yeast isocitrate lyase is the only eukaryotic member of this family that is located in the cytoplasm, instead of being targeted to the peroxisome or the glyoxysome.
Required for efficient progression through S phase and possibly for the normal progression through meiosis. Interacts with CDC28.
In the C-terminal section; belongs to the aldose epimerase family.
In the N-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family.
Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose (By similarity).
Positive nitrogen regulatory protein. Required for the activation of transcription of a number of genes (including the allantoin pathway genes) in response to the replacement of glutamine by glutamate as source of nitrogen. Binds the nitrogen upstream activation sequence of GLN1, the gene encoding glutamine synthetase. URE2 may catalytically inactivate GLN3 in response to an increase in the intracellular concentration of glutamine.
Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family.
Responsible for methylating the 5'-cap structure of mRNAs.
Each trimer binds three substrate molecules. The ligands are bound between subunits, and for each substrate molecule, residues from adjacent subunits contribute to the binding interactions.
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:2139027, PubMed:18055462). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:2139027, PubMed:18055462).
PI-SceI is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates 'homing', a genetic event that converts a VMA1 allele lacking VDE into one that contains it.
Present with 199895 molecules/cell in log phase SD medium.
This protein undergoes a protein self splicing that involves a post-translational excision of the VDE intervening region (intein) followed by peptide ligation.
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and VOA1) (PubMed:25971514, PubMed:18055462, PubMed:27295975). Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase (PubMed:11283612).
Present with 41 molecules/cell in log phase SD medium.
KAR1 is required for function of both intranuclear and extranuclear microtubules. KAR1 helps localize CDC31 to the spindle pole body (SPB), CDC31 then initiates SPB duplication via interaction with a downstream effector.
Regulates the copper-dependent mineralization of copper sulfide complexes on the cell surface in cells cultured in medium containing copper salts.
Catalytic component of the RPD3 histone deacetylase complexes RPD3C(L) and RPD3C(S) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. SIN3 has also a RPD3 independent function required for normal longevity.
Component of the RPD3C(L) complex composed of at least ASH1, CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6. Component of the RPD3C(S) complex composed of at least EAF3, RCO1, RPD3, SIN3, and UME1. Interacts with ESS1 and STB1.
Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 or PEX21 receptors (PubMed:9094717, PubMed:20154681). The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (PubMed:20154681). Mechanistically, PEX5 (or PEX21) receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix (PubMed:20154681).
Interacts with PEX13 (via SH3 domain); forming the PEX13-PEX14 docking complex (PubMed:10087260, PubMed:20154681, PubMed:12453410). Interacts with PEX5 (via WxxxF/Y motifs) (PubMed:9094717, PubMed:20154681). Interacts with PEX7 (PubMed:9094717). Interacts with PEX9 (PubMed:27678487).
Abnormal localization of the peripheral membrane protein PIB2 to the vacuolar membrane (PubMed:29698392, PubMed:26510498). Decreases activation of TORC1 in response to glutamine (PubMed:28483912).
Autophosphorylated. Might also be phosphorylated by VPS15.
Component of the autophagy-specific VPS34 PI3-kinase complex I composed of VPS15, VPS30, VPS34, ATG14 and ATG38, and of the VPS34 PI3-kinase complex II composed of VPS15, VPS30, VPS34 and VPS38. Interacts directly with ATG38.
Phosphatidylinositol 3-kinase activity is directly dependent on VPS15 protein kinase activity.
Phosphatidylinositol 3-kinase required for cytoplasm to vacuole transport (Cvt) and autophagy as a part of the autophagy-specific VPS34 PI3-kinase complex I. This complex is essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Its activation by VPS15 may lead to the phosphorylation of phosphatidylinositol in the sorting compartment membrane. Finally, it might also be involved in ethanol tolerance and cell wall integrity.
Active in zinc-limited cells and repressed in replete cells. Zinc controls ZAP1 DNA binding activity.
Contains 2 activation domains, embedded within larger zinc-responsive domains (ZRDs), designated AD1 and AD2, which are regulated independently by zinc. AD1 plays the primary role in zinc-responsive gene regulation, whereas AD2 is required for maximal expression of only a few target genes (PubMed:21177862). AD2 recruits coactivators less effectively than AD1 and is therefore only functional on some promoters (PubMed:22950018). AD2 is also important for ZAP1 activity under heat stress conditions (PubMed:21177862).
Contains 2 zinc-responsive domains ZRD(AD1) and ZRD(AD2). Zinc binding to residues in ZRD(AD1) and ZRD(AD2) represses the activation function of AD1 and AD2, respectively.
Induced by zinc. Regulates transcription of its own promoter in response to zinc through a positive autoregulatory mechanism.
Transcription regulator controlling zinc-responsive gene expression. Binds to zinc-responsive elements (ZREs) (consensus sequence 5'-ACCYYNAAGGT-3') in the promoter of target genes (PubMed:9786867). Recruits SWI/SNF, SAGA, and Mediator complexes as coactivators in a zinc-responsive manner (PubMed:22950018). Involved in zinc ion homeostasis by zinc-responsive transcriptional regulation of the zinc uptake system genes ZTR1 and ZTR2 (PubMed:9271382). Positively regulates ETR1 expression, affecting mitochondrial function (PubMed:26711224).
Uses 4 of its 7 zinc finger domains to contact the ZRE. 2 of these (ZF4 and ZF7) dominate the interaction by contacting the essential ACC--GGT ends, while the other 2 (ZF5 and ZF6) contact the 5 basepair central ZRE sequence. 2 zinc finger domains (ZF1 and ZF2) do not contact DNA, and a third ZF3 may be more important for interfinger protein-protein interactions (PubMed:12549926). ZF1 and ZF2 bind zinc in vitro but less stably than zinc fingers involved in DNA binding. ZF1 and ZF2 are critical for zinc regulation of activation domain 2 (AD2) and play a role in zinc sensing and consequent regulation of ZAP1 activity (PubMed:14517251). ZF1-ZF2 interactions stabilize the beta-beta-alpha folded repressed state of the ZF2 activation domain in the presence of cellular zinc excess (PubMed:16720702, PubMed:16483601). DNA binding is inhibited by zinc (PubMed:21799889).
Regulatory subunit of the vacuolar transporter chaperone (VTC) complex (PubMed:27587415). The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain VTC4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation (Probable). The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen (Probable). PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase (Probable). VTC5 interacts with the VTC complex to increase the rate of polyP production (PubMed:27587415).
The VTC core complex is an integral membrane heterooligomer composed of the catalytic subunit VTC4 and the accessory subunits VTC1, VTC2 and VTC3. The complex exists in 2 different sub-complexes: VTC1-VTC2-VCT4 and VCT1-VTC3-VTC4. The VCT1-VTC3-VTC4 subcomplex is mostly found on the vacuolar membrane. The VTC1-VTC2-VCT4 subcomplex is observed in the cell periphery, probably ER and nuclear envelope, but localizes to the vacuole under phosphate starvation. Each subunit contains 3 transmembrane helices. VTC1 is a small membrane protein without hydrophilic domain. VTC2, VTC3 and VTC4 are related and have 2 hydrophilic domains that face the cytosol, an N-terminal SPX domain and the central core domain. The central core in VTC4 is the catalytic domain, with the essential catalytic lysine replaced by isoleucine and leucine in VTC2 and VTC3, respectively. The core complex associates with the regulatory subunit VTC5.
Component of the ASTRA chromatin-remodeling machinery complex composed of at least ASA1, RVB1, RVB2, TRA1, TEL2, TT1 and TTI2.
Decreases the level of CSE4/CENP-A at centromeres (PubMed:32079723). Decreases internucleosome spacing at protein-coding genes (PubMed:25406467). Decreases localization of RNA polymerase II to the histone HTA1-HTB1 gene locus during the G1/S transition (PubMed:22156209). Decreases HTA1 RNA level (PubMed:19683497). Heterochromatin spreading downstream of the silent mating-type locus HMR (PubMed:16079223). Decreases cell population growth; simultaneous disruption of proteins required for maintaining centromere and kinetochore function, including CLH4 and CBF1, enhances the growth defect (PubMed:32079723).
Functions as an ATP-dependent nucleosome disassembly factor that helps evict canonical histone H3 from the 5'-end of genes upon their induction (PubMed:25406467). Also contributes to kinetochore assembly by cooperating with SCM3 to load the histone H3 variant CSE4/CENP-A at centromeres (PubMed:32079723). Provides a chromatin boundary function at the 5'-end of genes that restricts access by RTT106 and thus prevents ectopic spreading of repressive chromatin into coding regions (PubMed:19683497, PubMed:25406467, PubMed:22156209). Also prevents heterochromatin spreading downstream of the silent mating-type locus HMR, this function is independent of the tRNA boundary element (PubMed:16079223). Contributes to appropriate cell cycle regulation of histone gene expression by recruiting RNA polymerase II to histone genes, and subsequent CDK1- and casein kinase II-dependent eviction from chromatin is required to promote transcriptional elongation (PubMed:22156209).
Interacts with CSE4/CENP-A (PubMed:32079723). Interacts with SCM3 (PubMed:32079723). Interacts with SPT16 (PubMed:22156209). Interacts with POB3 (PubMed:22156209). Interacts with the casein kinase II complex subunits CKA1, CKA2, CKB1 and CKB2 (PubMed:22156209). Interacts with RNA polymerase II (PubMed:22156209). Interacts (via Bromo domain) with histone H3 (PubMed:16079223). Interacts (via Bromo domain) with histone H4 (PubMed:16079223).
Phosphorylated by CDK1 and casein kinase II during S-phase, which leads to its eviction from histone gene promoters and promotes histone gene transcription.
Component of the exocyst complex composed of SEC3, SEC5, SEC6, SEC8, SEC10, SEC15, EXO70 and EXO84. Interacts also with SNP1.
Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Plays a role in both the assembly of the exocyst and the polarization of this complex to specific sites of the plasma membrane for exocytosis and to the budding site. Also involved in assembly of the spliceosome.
Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). uL6 lines the binding pocket for eukaryotic elongation factor 2 (eEF2) (PubMed:9559554, PubMed:22096102).
Present with 52400 molecules/cell in log phase SD medium.
Present with 1127 molecules/cell in log phase SD medium.
Regulatory light chain for the class II conventional myosin MYO1. May play a role in the disassembly of the MYO1 ring at the bud neck at the end of its contraction during cytokinesis.
Interacts directly with MPC54, NUD1 and SPC42. Interacts with ADY3. Interacts with ADY4. Probable component of a SPB complex composed of ADY3, SSP1, DON1, MPC54, SPO21/MPC70, NUD1 and CNM67.
Involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. May provide a meiosis-specific scaffold for the assembly of other proteins on spindle pole bodies (SPBs), and may be a limiting component for SPB formation.
Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. TAF7 is responsible for the recruitment of BDF1 to TATA element containing promoters.
TAF7 interacts with BDF1. The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14.
Acts as an inhibitor of cullin neddylation and SCF complex assembly in vitro (PubMed:19942853). However in vivo experiments in other organisms strongly suggest that it acts as an essential regulator of SCF complex assembly.
Assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor (By similarity). Involved in the aging process. Longevity-assurance protein.
Interacts with unneddylated cullin CDC53.
Preferentially expressed in young cells.
Transports pantothenate into the cell. Also involved in the catabolite repression-mediated regulation of ergosterol biosynthesis and in fenpropimorph resistance.
Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.
Rhizoxin, an antibiotic that exhibits potent anti-mitotic activity against most eukaryotic cells except for yeasts, binds to beta tubulin.
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers (PubMed:28013290). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Associates with the nuclear pore complex (NPC). Interacts with GSP1, LOS1, MSN5, NUP116 and TEF2.
Component of the nuclear tRNA export machinery that my collect tRNA from the nuclear tRNA export receptors of the aminoacylation-dependent export and may deliver aminoacylated tRNAs to the translation machinery pathway at the nuclear pore complex.
Plays a role in sequence-specific regulation of nuclear pre-mRNA abundance.
Mediates the hydrolysis of steryl esters (SE) (PubMed:10515935, PubMed:14640980, PubMed:15713625). Preferentially hydrolyzes ergosteryl and zymosteryl esters (PubMed:19111628). Required for mobilization of SEs from lipid particles/droplets, thereby playing a central role in lipid metabolism and sterol homeostasis. Sterol intermediates stored in SE and set free by SE hydrolases are recycled to the sterol biosynthetic pathway and converted to the final product, ergosterol, in the endoplasmic reticulum. Has also weak lipase activity toward triglycerides at neutral pH, however, the physiological relevance of this activity is unclear (PubMed:15922657, PubMed:19111628, PubMed:28866104).
NAD-dependent histone deacetylase, which contributes together with HST3 to histone H3 'Lys-56' deacetylation, regulation of telomeric silencing, proper cell cycle progression, DNA damage control, DNA recombination, and genomic maintenance.
Belongs to the V-ATPase D subunit family.
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:7797485, PubMed:7831318). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:7797485, PubMed:7831318).
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and VOA1) (PubMed:25971514, PubMed:27295975). Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase (PubMed:11283612).
Belongs to the cytochrome c oxidase VIIc family.
Necessary for the targeting of ARL3 to the Golgi. Involved in protein trafficking. May serve as a receptor for acetylated ARL3.
Acts a component of the CCAT-binding factor, which is a transcriptional activator and binds to the upstream activation site (UAS2) of the CYC1 gene and other genes involved in mitochondrial electron transport and activates their expression. Recognizes the sequence 5'-CCAAT-3'. HAP4 encodes a regulatory subunit of the DNA-bound complex and seems to provide the principal transcriptional activation domains. Does not bind DNA directly, but augments the binding of HAP2 and HAP3.
Component of the CCAT-binding factor (CBF or HAP complex II), which consists of one copy each of HAP2, HAP3, HAP4 and HAP5. The assembly of the HAP2-HAP3-HAP5 heteromer (HAP complex I) occurs in a one-step pathway and its binding to DNA is a prerequisite for the association of HAP4.
Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA polymerase subunit family.
DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, RBP10 is part of the core element with the central large cleft.
Catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Present with 7430 molecules/cell in log phase SD medium.
Catalyzes the Claisen rearrangement of chorismate to prephenate (PubMed:2646272, PubMed:2187528, PubMed:10894726, PubMed:31498992, PubMed:9642265, PubMed:10428795). Acts at the first branch point in the aromatic amino acid pathway where it steers biosynthesis towards phenylalanine and tyrosine, and away from tryptophan (Probable).
Each dimer has two allosteric binding sites that can bind the regulatory effectors tryptophan or tyrosine (PubMed:31498992, PubMed:2187528, PubMed:10428795, PubMed:9642265). Can bind either one tryptophan or one tyrosine, two tryptophan or two tyrosine or one tryptophan and one tyrosine, which differentially affect the catalytic activity (PubMed:31498992). Activated by tryptophan and subject to feedback inhibition by tyrosine (PubMed:10428795, PubMed:31498992, PubMed:2646272, PubMed:2187528). In the presence of both tryptophan and tyrosine, the enzyme is in the activated state (PubMed:2646272, PubMed:31498992).
Not affected by altering tryptophan or tyrosine levels.
Binds to the catalytic subunit of the cyclin dependent kinase (CDC28) and is essential for its biological function.
Forms a stable but non-covalent complex with the CDC28 protein and with a cyclin.
Present with 8780 molecules/cell in log phase SD medium.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily.
Expressed periodically during the cell cycle, with a peak in late G1. Transcriptional repression requires ZDS1. Protein accumulation is also periodic, peaking during S/G2 and declining prior to and during nuclear division of the unperturbed cell cycle. Stabilized during a checkpoint response in G2. Induced during meiosis. Induced by ethanol (at protein level).
Interacts with CLB2-CDC28. Partial hyperphosphorylation of SWE1 by CLB2-CDC28 stabilizes the ternary complex of SWE1 and CLB2-CDC28 and stimulates kinase activity of SWE1 in a positive feedback loop, maintaining CLB2-CDC28 in the tyrosine-phosphorylated state. Fully hyperphosphorylated SWE1 dissociates from CLB2-CDC28. Interacts with HSL7, KCC4 and MET30.
Phosphorylated progressively by CLA4, CLB2-CDC28 and CDC5. CLA4-dependent phosphorylation occurs in late S phase, followed by phosphorylation by CLB2-CDC28 in early G2, when the levels of mitotic CLB2 increases. This phosphorylation is critical for triggering subsequent SWE1-CDC5 interaction and CDC5-dependent phosphorylation. The resulting cumulative hyperphosphorylation down-regulates SWE1 by targeting it for ubiquitin-mediated degradation. This stepwise phosphorylation is thought to be a mechanism to integrate the different checkpoint requirements before entry into mitosis.
Protein kinase that acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylating and inhibiting the mitosis-promoting cyclin B-bound CDC28 at 'Tyr-19'. SWE1-mediated inhibition of CDC28 acts in a cell size or morphogenesis checkpoint to delay mitosis in response to defects in growth, actin organization or bud formation. Inhibits the activity of B-type cyclins in replication initiation strongly for CLB2, moderately for CLB3 and CLB4, and there is no apparent inhibition for CLB5 and CLB6, correlating with the normal expression timing of those cyclins. Hyperphosphorylation and degradation of SWE1 when all checkpoint requirement are met releases CLB2-CDC28 from inhibition and allows for progression through the cell cycle. SWE1-dependent CDC28 phosphorylation is also required for pachytene arrest upon activation of the recombination checkpoint during meiosis. Also involved in the regulation of nitrogen starvation- and short chain alcohol-induced filamentous growth, or filamentous differentiation in response to slowed DNA synthesis. Can act both on serines and on tyrosines.
Ubiquitinated by the SCF(MET30) complex, leading to its degradation by the proteasome.
Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family. Adenine deaminase type 2 subfamily.
Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism. Also exhibits a low activity towards N(6)-substituted adenines that are commonly known as the plant hormones cytokinins.
Probably ubiquitinated when cells enter quiescence in response to nutrient limitation, since it is specifically degraded via a process requiring the F-box protein SAF1 and components of the SKP1-Cullin-F-box complex.
Reduced when grown in a poor nitrogen source medium and strongly down-regulated when cells enter quiescence under nutrient-limiting conditions.
Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole. Probably acts as a peripherally associated component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruits late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Regulates the membrane association of VPS4. Can stimulate VPS4 ATPase activity directly or via VTA1.
Self-associates. Interacts with VPS4 and VTA1. Interacts with IST1.
This isozyme preferentially catalyzes the conversion of ethanol to acetaldehyde. Acts on a variety of primary unbranched aliphatic alcohols.
Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. Catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) in the methionine salvage pathway primarily using branched chain amino acids (leucine, isoleucine, and valine) as well as lysine and proline as the amino donors. Involved in cell cycle regulation.
Down-regulated in the presence of repressive nitrogen sources (glutamine) and derepressed in secondary non-repressive nitrogen sources such as GABA. Highly expressed on cultures with isoleucine, leucine and valine as sole nitrogen source (catabolic conditions).
Highly expressed during stationary phase, down-regulated during logarithmic phase of growth.
Present with 25900 molecules/cell in log phase SD medium.
Involved in lipid metabolism and lipid droplet (LD) morphology, number, and size (PubMed:18093937, PubMed:18250201). Facilitates initiation of LD formation, and ensures that vectorial budding of LDs from the ER is directed towards the cytoplasm (PubMed:25540432).
Produces supersized LDs that are up to 50 times the volume of those in wild-type cells.
Belongs to the glycosyl hydrolase 31 family.
Catalytic subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins.
Inhibited by glucose, maltose and nigerose, and by the antibiotic deoxynojirimycin.
Belongs to the NTC complex (or PRP19-associated complex), composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2, and PRP19. The NTC complex associates with the spliceosome after the release of the U1 and U4 snRNAs and forms the CWC spliceosome subcomplex (or CEF1-associated complex) reminiscent of a late-stage spliceosome composed also of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8, PRP9, PRP11, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNU114, SPP2, RSE1 and YJU2. Interacts with CEF1, CLF1 and SYF1.
Involved in pre-mRNA splicing and cell cycle control. As a component of the NTC complex (or PRP19-associated complex), associates to the spliceosome to mediate conformational rearrangement or to stabilize the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation. The cell cycle arrest of SYF2 defective cells may be due to the inefficient splicing of TUB1.
A combined deletion of the LDS proteins RRT8, LDS1 and LDS2 fails to incorporate dityrosine and another yet uncharacterized component in the outer spore wall.
GABA-dependent positive regulation of genes required for catabolism of GABA (UGA4, UGA1, and UGA2).
UGA3 proteins associate in oligomers, at least in the presence of inducer.
In contrast with other calnexin, yeast CNE1 does not seem to bind calcium.
Interacts with newly synthesized monoglucosylated glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins.
Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.
Mainly expressed in the early logarithmic phase.
Ty1-JR2 is a highly expressed element. Induced under amino acid starvation conditions by GCN4.
Interacts directly with ADY3. Probable component of a spindle pole body (SPB) complex composed of ADY3, SSP1, DON1, MPC54, SPO21/MPC70, NUD1 and CNM67.
Involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. May be required for the formation of ADY3 and DON1-containing protein coats at the leading edge of the PSMs during meiosis II.
Meiosis-specific. Expressed from 3 to 9 hours after induction of sporulation. Not expressed during mitosis.
Belongs to the Mediator complex subunit 1 family.
Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. MED1 interacts directly with MED4 and MED7.
Present with 4675 molecules/cell in log phase SD medium.
Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily.
Transcriptional modulator with roles in meiotic regulation and silencing.
Increases cellular tolerance to 2-deoxy-glucose.
Forms a heterodimer with IML3 (PubMed:12589047, PubMed:24075991). CHL4-IML3 is part of a larger constitutive centromere-associated network (CCAN) (also known as central kinetochore CTF19 complex in yeast), which is composed of at least AME1, CHL4, CNN1, CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1 (PubMed:12408861, PubMed:22561346). Interacts with CHL4 and CTF19 (PubMed:12589047).
Involved in pre-rRNA processing. Required for the final stage of 3'-end maturation of 5.8S rRNA at site E.
ATP-dependent 5'->3' DNA/RNA helicase required for the expression and maturation of diverse classes of non-protein-coding RNAs like precursor tRNAs, rRNAs and small nuclear (snRNA) and nucleolar (snoRNA) RNAs. Directs RNA polymerase II transcription termination on snoRNAs as well as on several short protein-coding genes. May also play a role in transcription-coupled nucleotide excision repair.
Interacts with RAD2, RNT1 and RPB1. Binds to multiple snoRNAs.
Belongs to the bacterial ribosomal protein bS1 family.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. bS1m functionally interacts with the 5'-UTR of mitochondrial mRNAs.
Component of the septin complex which consists of CDC3, CDC10, CDC11, CDC12 and probably SHS1 and rearranges to a cortical collar of highly ordered filaments at the mother-bud-neck. A complex formed by CDC3, CDC10, CDC11 and CDC12 is capable of forming long filaments in vitro and the components seem to be present in a 2:2:2:2 arrangement in vivo. The filaments are proposed to be formed by the end-to-end polymerization of CDC3-CDC12-CDC11 complexes with CDC10 serving as a bridge to bundle the polymers into paired filaments. Component of the GIN4 complex composed of at least BNI5, CDC3, CDC10, CDC11, CDC12, GIN4, NAP1 and SHS1. Self-associates. Interacts with CDC11 and SPA2.
Phosphorylated by GIN4 and CLA4. Phosphorylation state is essential for septin ring dynamics during telophase.
Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring approximate 15 min before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation.
Sumoylated during mitosis on the mother cell side of the bud neck. Sumoylation probably plays a central role in regulating septin ring disassembly during the cell cycle.
Component of the RNA polymerase I (Pol I) and RNA polymerase III (Pol III) complexes. Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA. Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. Directly interacts with the RPC40 subunit.
DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common core component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively.
Catalyzes the attachment of serine to tRNA(Ser) (PubMed:3031581). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) (Probable).
Homodimer; the tRNA molecule probably binds across the dimer (PubMed:3031581). Interacts with ABP140; interaction is required for the tRNA N(3)-methylcytidine methyltransferase activity of ABP140 (PubMed:28003514).
Causes increased leaky scanning through AUG codons, +1 frameshifting, and read-through of stop codons. Also causes progressive telomere shortening.
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Likely catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. Required for normal translation, by ensuring translation fidelity at the level of codon recognition, appropriate translation initiation selection and maintenance of reading frame. Also involved in telomere replication. Binds to single-stranded telomeric (ssTG) DNA and positively regulates telomere length.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family.
Loses mitochondrial DNA with high frequency.
S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methyluridine at position 2791 (Um2791) in the 21S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.
Present with 21600 molecules/cell in log phase SD medium.
The SUI1 domain may be involved in RNA binding.
Belongs to the NUP186/NUP192/NUP205 family.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NUP192 interacts with NIC96.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP192 is located to the NPC core at the nuclear membrane and is essential for de novo assembly of NPCs.
Belongs to the small GTPase superfamily. Rheb family.
Involved in the regulation of arginine and lysine uptake. Acts through the CAN1 permease.
Can suppress the synthetic lethality of the hal3 sit4 double mutation when overexpressed, suggesting that it is involved in the G1-S transition.
By replication arrest and DNA damage. Repressed by CYC8, RFX1 and TUP1.
Involved in the MEC1-mediated checkpoint response to DNA damage and replication arrest.
Belongs to the JHDM1 histone demethylase family.
Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Does not demethylate H3 'Lys-4' nor 'Lys-79'.
The JmjC domain mediates the demethylation activity.
Belongs to the glycosyl hydrolase 16 family.
Required for heat stress-instigated phosphorylation of BCY1 which is involved in cell wall integrity signaling. Regulates activity of MSN2, a transcription factor that binds to the stress-response element (STRE). Probably promotes formation of a complex between MSN2 and DNA. Regulates the stability of ROG1.
Interacts with the acetylglutamate kinase chain of AGR5,6.
N-acetylglutamate synthase involved in arginine biosynthesis.
Present with 34906 molecules/cell in log phase SD medium.
May be involved in positioning the proximal bud pole signal.
Belongs to the trichothecene 3-O-acetyltransferase family.
Trichothecene 3-O-acetyltransferase involved in self-protection against trichothecenes, mycotoxins acting as eukaryotic protein synthesis inhibitors. Its existence is surprising in a non-trichothecene producer organism which needs no self-protection again endogenic trichothecenes. The persistence of this non-essential gene may be due to a selective advantage that it may confer, like a resistance to exogenic trichothecenes.
Present with 391 molecules/cell in log phase SD medium.
Required for meiotic chromosome synapsis and cell cycle progression. May act as a molecular zipper to bring homologous chromosomes in close apposition. ZIP1 may encode the transverse filaments of the synaptonemal complex.
Belongs to the cytochrome c oxidase IV family.
By low oxygen levels (hypoxia) at the level of transcription. Repressed by ROX1 in the presence of oxygen (PubMed:2546055). Not expressed until the oxygen concentration is below 0.5 uM O(2) (PubMed:9169434).
Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of 12 subunits. The complex is composed of a catalytic core of 3 subunits COX1, COX2 and COX3, encoded in the mitochondrial DNA, and 9 supernumerary subunits COX4, COX5A (or COX5B), COX6, COX7, COX8, COX9, COX12, COX13 and COX26, which are encoded in the nuclear genome (PubMed:2986105). COX5A is the predominant subunit V during aerobic/normoxic growth, it gets replaced by COX5B under anaerobic/hypoxic conditions (PubMed:2546055). The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a dimer of ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), resulting in 2 different assemblies (supercomplexes III(2)IV and III(2)IV(2)) (By similarity).
The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2. Important for TATA site selection by TBP. Directly or indirectly regulates the DNA-binding properties of SPT15, the TATA box-binding protein, and the relative activities of different TATA elements.
Alkaline ceramidase that hydrolyzes phytoceramide and also dihydroceramide into phytosphingosine or dihydrosphingosine. Prefers phytoceramide. Has also reverse activity as acyl-CoA-independent ceramide synthase, catalyzing synthesis of phytoceramide and dihydroceramide from palmitic acid and phytosphingosine or dihydrosphingosine. Is not responsible for the breakdown of unsaturated ceramide (PubMed:10702247, PubMed:10900202, PubMed:11694577, PubMed:24866405). Preferentially uses very long chain fatty acids (C-24 and C-26) in vivo compared to C-16 in vitro (PubMed:24866405).
Polarity-determining protein which forms a conjugate with the ubiquitin-like modifier HUB1. Involved in bud site selection and cellular morphogenesis during conjugation. Required for survival during stationary phase.
Interacts with CNM67, SPO21/MPC70 and NUD1.
Involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. May be required to stabilize the outer plaque of the spindle pole body (SPB).
Binds to both phosphatidylinositol (PI) and phosphatidylinositol 3,5-bisphosphate (PIP2).
Lipase which is essential for lysis of subvacuolar cytoplasm to vacuole targeted bodies and intravacuolar autophagic bodies. Involved in the lysis of intravacuolar multivesicular body (MVB) vesicles. The intravacuolar membrane disintegration by ATG15 is critical to life span extension.
Belongs to the beta-class carbonic anhydrase family.
Catalyzes the reversible hydration of CO(2) to H(2)CO(3). The main role may be to provide inorganic carbon for the bicarbonate-dependent carboxylation reactions catalyzed by pyruvate carboxylase, acetyl-CoA carboxylase and carbamoyl-phosphate synthetase. Involved in protection against oxidative damage. Encodes a substrate for the non-classical protein export pathway for proteins that lack a cleavable signal sequence.
Transcription and activity down-regulated at elevated CO(2) concentrations.
Serine/threonine protein kinase involved in the regulation of exocytosis. Induces phosphorylation of SEC9 and its release from the plasma membrane to the cytosol.
Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. Interacts with RPC53/RPC4. RPC53/RPC4, RPC37/RPC5 and RPC11/RPC10 probably form a Pol III subcomplex.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. The RPC53/RPC4-RPC37/RPC5 subcomplex is required for terminator recognition and reinitiation.
Protein transport. Probably involved in vesicular traffic (By similarity). Specifically binds guanine nucleotides.
Via its C-terminal end interacts with the Rab GDP dissociation inhibitor (RabGDI). Interacts with YIF1, YIP3, YIP4 and YIP5.
Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration. Binds copper. May be involved in copper trafficking and distribution to mitochondrial COX and SOD1.
Activated by phosphorylation by SSK2 or SSK22. Ser/Thr phosphorylation is also necessary for SHO1-mediated activation.
Alternative way of activation involves binding the proline-rich motif to the SH3 domain of SHO1.
Interacts with NBP2, PTC1, SHO1 and STE11.
Kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Seems to phosphorylate HOG1 on a tyrosine residue.
Impairs growth in culture media with D-xylulose as the sole carbon source.
Xylulose kinase necessary for growth in culture media with D-xylulose as the solecarbon source.
By pheromone. Expression is controlled by the STE12 transcription factor that binds to pheromone-response cis-elements (PREs) in the promoter of target genes.
Required for the fusion of nuclear envelopes during mating, ensuring proper karyogamy. Plays a role in the initiation of outer nuclear envelope fusion.
Was originally shown to be localized in the inner nuclear membrane by using a truncated protein (PubMed:12514182). Was used as an inner nuclear membrane marker (PubMed:17996101, PubMed:18660802 and PubMed:19369416). However, more recent studies showed that it is localized in the nuclear outer membrane, which is consistent with a function in the initiation of nuclear fusion (PubMed:19297527 and PubMed:19570912).
Belongs to the ABC transporter superfamily. Alpha-factor sex pheromone exporter (TC 3.A.1.206) family.
STE6 is required in yeast MATA cells for production of A-factor pheromone. STE6 is involved in the transport of the farnesyl-derivation of the A-factor pheromone.
Associates with the SIT4 phosphatase in a cell cycle dependent manner. May be directly or indirectly involved in SIT4-dependent functions in budding and in normal G1 cyclin expression.
Present with 11200 molecules/cell in log phase SD medium.
Belongs to the glycosyl hydrolase 63 family.
Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor highly specifically (PubMed:9363442). Seems to play a role in beta-1,6-glucan synthesis (PubMed:8576053).
Displays phenotypes characteristic of cell wall defects such as hypersensitivity to calcofluor white and resistance to K1 killer toxin, and results in a 50% reduction of cell wall beta-1,6-glucan level (PubMed:9363442). Abolishes glucosidase I activity (PubMed:9363442).
Miglitol is an effective inhibitor at 1 mM.
Deletion results in antifungal drug fluconazole-resistant phenotype.
Belongs to the V-ATPase E subunit family.
Homodimer (PubMed:8626613). V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and VOA1) (PubMed:2145285, PubMed:8416931, PubMed:25971514, PubMed:18055462, PubMed:27295975). Interacts with VMA5; the interaction is direct (PubMed:15751969). Interacts with VMA10; the interaction is direct (PubMed:15751969). Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase (PubMed:11283612).
Present with 16134 molecules/cell in log phase SD medium.
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:8416931). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:8416931, PubMed:2145285).
Exhibits cold sensitivity, a significant increase in cells with fragmented vacuoles, internal accumulation of precursor CPY, increased glycogen accumulation, and displays elongated buds.
Involved in vacuolar processing and morphology.
Component of the precatalytic spliceosomal complex B. Interacts with PRP19.
Component of the spliceosome involved in mRNA processing.
Essential protein. Required for biogenesis of the 60S ribosomal subunit.
Belongs to the WD repeat MDV1/CAF4 family.
Interacts with DNM1, FIS1 and MDV1, components of the mitochondrial fission machinery. Interacts via its WD repeats with DNM1. Interacts with CCR4 and NOT1, components of the CCR4-NOT complex. It is however not a component of the 1.0 MDa CCR4-NOT core complex, but appears to be part of a less characterized, 1.9 MDa CCR4-NOT complex. Interacts with DBF2, another likely component of the 1.9 MDa complex. Interacts with SRB9 and SRB10, components of the SRB8-11 complex.
Involved in mitochondrial fission. Has a partially redundant function to MDV1 in acting as an adapter protein, binding to FIS1 on the mitochondrial outer membrane and recruiting the dynamin-like GTPase DNM1 to form mitochondrial fission complexes. Plays a key role in determining the polarized localization of those DNM1 clusters that are not immediately involved in the mitochondrial fission process.
Belongs to the enoyl-CoA hydratase/isomerase family.
By oleate, through the binding of the OAF1-PIP2 transcriptional activator complex to its promoter ORE element. Expression is also induced during ammonia pulses in yeast colonies, at the beginning of detectable ammonia production.
Peroxisomal di-isomerase that is involved in fatty acid metabolism enzyme by converting 3,5-dienoyl-CoAs to the corresponding 2,4-dienoyl-CoAs (PubMed:10381339, PubMed:10455114). Required for ECI1 to be locazed to the peroxisome (PubMed:10381339, PubMed:11302517).
Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Is not a genuine component of the 26S proteasome, but an auxiliary factor that interacts with the proteasomal ATPase of 19S regulatory particle (RP). Acts as a chaperone which regulates the highly structured assembly of the 19S regulatory particle. Involved in the substrate specificity of the 26S proteasome and is especially involved in the degradation of ubiquitinated GCN4. May contribute to the stability of the 26S proteasome in some stress conditions.
Associates with the 19S proteasome regulatory particle (RP). Interacts directly with RPT5 and RPT6.
Belongs to the WD repeat PAAF1/RPN14 family.
Transport into the cell of 7-keto 8-aminopelargonic acid.
Catalyzes the phosphorylation of the sphingoid long chain bases dihydrosphingosine (DHS or sphinganine) and phytosphingosine (PHS) to form dihydrosphingosine 1-phosphate (DHS-1P) and phytosphingosine 1-phosphate (PHS-1P) respectively (PubMed:9677363, PubMed:11102354, PubMed:12493772, PubMed:25345524). Redundant to LCB4, is only responsible for few percent of the total activity (PubMed:9677363). Involved in the biosynthesis of sphingolipids and ceramides (PubMed:9677363, PubMed:25345524). Involved in heat-induced transient cell cycle arrest (PubMed:11056159). Accumulation of phosphorylated sphingoid long chain bases (LCBPs) stimulates calcium influx and activates calcineurin signaling (PubMed:11102354, PubMed:11278643). Involved in heat-stress resistance (PubMed:11056159).
Component of the ESCRT-II complex, which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs (PubMed:12194858, PubMed:15469844, PubMed:15329733). The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation (PubMed:12194858). The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex (PubMed:12194858). Involved in the trafficking of the plasma membrane ATPase (PubMed:12194858). Its ability to bind ubiquitin plays a central role in endosomal sorting of ubiquitinated cargo proteins by the ESCRT complexes (PubMed:15029239).
Component of the endosomal sorting required for transport complex II (ESCRT-II), which consists of 2 copies of VPS25, 1 copy of SNF8, and 1 copy of VPS36 (PubMed:15329733, PubMed:15469844). The ESCRT-II complex interacts directly with the VPS20 subunit of the ESCRT-III complex (PubMed:12194858). Binds ubiquitin (PubMed:15029239).
The second RanBP2-type zinc-finger is functional and binds ubiquitin.
Catalyzes the ATP-dependent ligation of glycine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (Gly-AMP) (PubMed:23816885). Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis (By similarity).
GRS1, which appears to be a duplication of GRS2, is necessary and sufficient for both mitochondrial and cytoplasmic glycyl-tRNA synthetase activities, suggesting that GRS2 may not be essential.
Homodimer. Part of the 350 kDa complex which is at least composed of ATG5, ATG12 and ATG16. Several units of each may be present in this complex. Interacts directly with ATG12.
Stabilizes the ATG5-ATG12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS). Recruits also ATG3 to the PAS. Involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress.
Expression is under the control of the ADR1, CAT8, and GCN4 transcription factors. Also induced by external ammonia and in rho(0) cells.
Transporter protein required for ammonia export. Induced in rho(0) cells, probably to eliminate the excess ammonia that arises because of a potential defect in ammonia assimilation in those cells.
Expression is regulated by the ACE2 and SWI5 transcription factors.
Interacts with CBF2, GIS1, NAP1, PRM8, REI1, SHS1 and SMT3.
May be involved in a mitotic signaling network. Binds sumoylated proteins and may stabilize SUMO chains.
Could be the product of a pseudogene. This is the C-terminal part of an allantoate permease subfamily member protein. Strain S288c has a stop codon in position 170, which disrupts the gene coding for this protein and produces two ORFs YOL163W and YOL162W.
With TMN2 and TMN3, plays a critical role in the late stages of a nutrient-controlled pathway notably regulating FLO11 gene expression. Acts downstream of RAS2 and TOR. Essential for cell adhesion and filamentous growth. May play a role as effector of cellular copper homeostasis.
Present with 23100 molecules/cell in log phase SD medium.
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
RNA-binding protein involved in post-transcriptional regulation through transcript degradation of SRE (SMG-recognition elements) bearing mRNAs.
The SAM domain is essential for RNA-binding.
Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes. Regulates also the sphingolipid metabolism. Required for growth during anaerobiosis and sterol uptake.
Abolishes CHS3 localization to the bud neck with increased protein localization to the ER membrane.
Chaperone required for the export of the chitin synthase CHS3 from the endoplasmic reticulum.
Activated by phytosphingosine (PHS), a sphingoid long chain base. Activated by PKH2 phosphorylation. Kinase activity is regulated by TOR2 via direct phosphorylation of Ser-641 and Thr-659.
Autophosphorylated (By similarity). Phosphorylated by PKH2 and TOR2.
May act as a downstream kinase in the sphingolipid-mediated signaling pathway. Plays an essential role in the proliferation of yeast cells. Involved in a signaling pathway, required for optimal cell wall integrity, that acts in parallel with the PKC1-SLT2-dependent pathway. A substrate of TOR complex 2 (TORC2) and required for TORC2 to regulate spatial aspects of cell growth. Phosphorylation of residue Thr-501 is indispensable for function.
Interacts with ABD1, RBP1, SPT5 and SPT6.
Transcription factor involved in RNA polymerase II transcription regulation. May function in both SPT15/TBP post-recruitment and recruitment steps of transcription.
Component of the HRD1 ubiquitin ligase complex which contains the E3 ligase HRD1, its cofactors HRD3, USA1 and DER1, substrate recruiting factor YOS9 and CDC48-binding protein UBX2 (PubMed:16873066). Within the complex, interacts directly with HRD1 (via N-terminus) and DER1 (via C-terminus) and indirectly with HRD3 (PubMed:20005842, PubMed:19898607, PubMed:21074049, PubMed:32327568). In ERAD-L, HRD3 and YOS9 jointly bind misfolded glycoproteins in the endoplasmic reticulum (ER) lumen (PubMed:32327568). Movement of ERAD-L substrates through the ER membrane is facilitated by HRD1 and DER1 which have lateral gates facing each other and which distort the membrane region between the lateral gates, making it much thinner than a normal phospholipid bilayer (PubMed:32327568). Substrates insert into the membrane as a hairpin loop with one strand interacting with DER1 and the other with HRD1 (PubMed:32327568). The HRD1 complex interacts with the heterotrimeric CDC48-NPL4-UFD1 ATPase complex which is recruited by UBX2 via its interaction with CDC48 and which moves ubiquitinated substrates to the cytosol for targeting to the proteasome (PubMed:16873066).
Impaired degradation of proteins with misfolded lumenal domains such as CPY*, a mutant, misfolded form of carboxypeptidase Y which is a known ERAD-L substrate. Impaired degradation of proteins with misfolded intramembrane domains. Impaired trans-ubiquitination and degradation of the HRD1 ligase. Degradation of proteins with misfolded cytosolic domains is not affected. Interaction of substrate with HRD1 is reduced; in USA1 and YOS9 double mutants this interaction is completely abolished.
Scaffold protein of the endoplasmic reticulum-associated degradation (ERAD) (also known as endoplasmic reticulum quality control, ERQC) pathway involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). Has multiple functions in ERAD including recruitment of DER1 to the HRD1 ubiquitin ligase, and regulation of HRD1 activity. Involved in oligomerization of HRD1 and in HRD1 autoubiquitination and degradation.
The ubiquitin-like domain is required for HRD1 trans-ubiquitination and degradation. Reported to be involved in ERAD-M but not ERAD-L function (PubMed:20005842). However, a contradictory report states that it is not required for either ERAD-L or ERAD-M function (PubMed:19940128). Reported to be required for HRD1 oligomer formation (PubMed:19940128). However, a contradictory report does not observe any defects in oligomerization following deletion of the domain (PubMed:21074049).
Cell polarity defects; delocalized actin patches and abnormal budding (PubMed:8754840). Cell lysis at high temperature (PubMed:8754840).
Interacts with CDC42; the interaction is direct (PubMed:8754839). Interacts with RHO1; the interaction is direct (PubMed:8754839, PubMed:8754840). Interacts with RHO2 (PubMed:8754839). Interacts with RHO4 (PubMed:8754839). Interacts with CDC11 (PubMed:12665577).
Present with 6330 molecules/cell in log phase SD medium.
Probably acts as a GEF (guanine nucleotide exchange factor) for the Rho family of small GTP-binding proteins (G proteins) that stimulates the dissociation of GDP to enable subsequent binding of GTP (By similarity). May also chaperone the processing and/or trafficking of small GTPases independently of GEF activity (By similarity). Involved in the control of polarized cell growth via CDC42-mediated signaling (PubMed:8754839). Involved in the control of cell-wall organization via RHO1-mediated signaling (PubMed:8754839, PubMed:8754840). May also function via RHO2 and RHO4 (PubMed:8754839).
Belongs to the activator 1 large subunit family.
Component of the ATP-dependent clamp loader RFC complex for the POL30/PCNA homotrimer DNA clamp. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA. Replication factor C (RFC or activator 1) complex acts during elongation of primed DNA templates by DNA polymerase delta and epsilon. RFC has an essential but redundant activity in sister chromatid cohesion establishment.
Replication factor C (RFC) is a heteropentamer of subunits RFC1, RFC2, RFC3, RFC4 and RFC5 and forms a complex with POL30/PCNA in the presence of ATP. Interacts with ECO1 and POL30/PCNA.
Component of the 90S pre-ribosomes. Interacts directly with DBP8.
Involved in the small subunit (SSU) processome assembly and function, and in the 18S rRNA synthesis. Required for the early cleavages at sites A0, A1 and A2. Stimulates DBP8 RNA helicase ATPase activity.
Increased accumulation of copper, cadmium and cobalt ions and enhanced sensitivity to the toxic effects of copper and cadmium. Exhibits no additional sensitivity to manganese. SMF1 fails to enter the vacuole and is stabilized. Reverses the aerobic defects of yeast strains lacking superoxide dismutase (SOD). Concomitant deletion of SMF1 completely abolishes the ability of BSD2 deletion to suppress SOD deficiency and reverses the increased sensitivity to cadmium and copper. However cobalt ion hyperaccumulation is not suppressed.
Present with 3070 molecules/cell in log phase SD medium.
Required for homeostasis of heavy metal ions such as cadmium, cobalt and copper. Controls metal ion transport and prevents metal hyperaccumulation by negatively regulating the SMF1 and SMF2 metal transport systems. Under manganese-replete conditions facilitates trafficking of SMF1 and SMF2 metal transporters to the vacuole where they are degraded.
Interacts with the internal control region (ICR) of approximately 50 bases within the 5S RNA genes, is required for correct transcription of these genes by RNA polymerase III. Also binds the transcribed 5S RNA's.
Acts a component of the CCAT-binding factor, which is a transcriptional activator and binds to the upstream activation site (UAS2) of the CYC1 gene and other genes involved in mitochondrial electron transport and activates their expression. Recognizes the sequence 5'-CCAAT-3'. HAP2 has primarily a structural role in the HAP complexes I and II.
Belongs to the NFYA/HAP2 subunit family.
Deletion of the gene leads to brefeldin A-sensitivity.
May be involved in intracellular vesicle transport.
RNA-binding protein involved in post-transcriptional regulation. Negatively regulates expression of COX17 by binding to the 3'-UTR of COX17 mRNA. Promotes decay of COX17 mRNA by enhancing its rate of deadenylation and subsequent turnover. Predominantly binds to mRNAs encoding mitochondrial proteins and localizes them to the vicinity of mitochondria for translation. Regulates mitochondrial biogenesis, motility and morphology.
By diamide and 1-chloro-2,4-dinitrobenzene (CDNB) in a transcriptional factors YAP1 and/or MSN2/4-dependent manner.
Null mutants display increased sensitivity to cadmium in the absence of GTT1 and GTT2. Null mutants also show growth defects on oleic acid-based medium, indicative of abnormal peroxisomal functions and altered expression of genes related to sulfur amino acid metabolism, and have low levels of reduced glutathione.
Required for growth under high-pressure and low-temperature conditions.
Sensitivity to 6-azauracil (6AU) and mycophenolic acid (MPA).
E3 ubiquitin-protein ligase which functions in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, 2 E2 ubiquitin conjugating enzymes (PubMed:18202552). Involved in nutritional control of the cell cycle (PubMed:15319434). Targets the G1 cyclin PCL1 for destruction (PubMed:23264631). Required for proper spindle positioning, likely regulating septin ring deposition at the bud neck (PubMed:15146058).
Interacts with CDC123 (PubMed:15319434). Interacts with PCL1 (PubMed:23264631).
Protein levels are regulated by nutrient status, being high under good nutrient conditions.
UBC4-dependent autoubiquitination occurs at Lys-150, Lys-204, Lys-217, Lys-237, Lys-240, Lys-260, Lys-300, Lys-306, Lys-313 and Lys-317. UBC4-dependent autoubiquitination is responsible for DMA2 turnover. UBC13/MMS2-dependent autoubiquitination occurs at Lys-237 and Lys-306. Lys-204 and Lys-306 are also ubiquitinated in trans by DMA2 E3 ligase in association with UBC4.
DNA polymerase delta (DNA polymerase III) participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair.
DNA polymerase delta is a heterotrimer of POL3, POL32 and HYS2. POL32 can form homodimers.
Required for autophagic breakdown of peroxisomes, called pexophagy, through linking peroxisomes to the autophagy apparatus. Involved in regulation of the glyoxylate cycle.
Ty1-OR is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Ty1-PR2 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Belongs to the cyclic nucleotide phosphodiesterase family.
Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Controls the level of cAMP in yeast cells, together with the low-affinity cAMP phosphodiesterase (PDE1).
Derepression of silent mating type loci when overexpressed.
Present with 1910 molecules/cell in log phase SD medium.
Identified in the Set3C complex with HOS2, HST1, SNT1, SIF2, CPR1 and SET3.
Unknown. Component of the Set3C complex, which is required to repress early/middle sporulation genes during meiosis.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. Binds to NUP1 and NUP2 forming the nuclear basket and the distal ring. The interaction with NUP2 is GSP1-GTP-dependent. Interacts through its FG repeats with karyopherins, such as KAP123 and KAP95-SRP1 (KAP60). Also interacts with GSP1-GTP and SRM1 (PRP20), where NUP60 reduces SRM1 activity, thus inhibiting GSP1 guanine nucleotide dissociation.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm).
tRNA backbone modifying enzyme that mediates initiator/ elongator tRNA discrimination. This enzyme modifies exclusively the initiator tRNA in position 64 using 5'-phosphoribosyl-1'-pyrophosphate as the modification donor. Recognize the stem-loop IV region that is unique in eukaryotic cytoplasmic initiator tRNAs.
Component of a COP9 signalosome-like (CSN) complex, composed of at least RRI1/CSN5, CSN9, RRI2/CSN10, PCI8/CSN11, CSN12 and CSI1. In the complex, it probably interacts directly with CSN12 and CSI1. Interacts also with RPN5.
Component of the COP9 signalosome (CSN) complex that acts as a regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes. The CSN complex is involved in the regulation of the mating pheromone response.
Belongs to the bacterial ribosomal protein bL19 family.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (PubMed:25609543, PubMed:24675956). bL19m is essential for respiration (PubMed:8771712).
Belongs to the mitochondrion-specific ribosomal protein mS26 family.
Could be the product of a pseudogene unlikely to encode a functional protein. This is a truncated version of a flocculin protein family member. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set.
Monomer. Part of the heterodimeric LMA1 complex together with the proteinase inhibitor PBI2. LMA1 binds to the ATPase SEC18.
Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl-hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism. Through its capacity to inactivate the stress response transcription factor YAP1 and its regulator the hydroperoxide stress sensor HYR1, it is involved in feedback regulation of stress response gene expression upon oxidative stress.
Present with 17237 molecules/cell in log phase SD medium.
Reversible disulfide bond formation between Cys-31 and Cys-34, reverted by thioredoxin reductase TRR1 using NADPH as hydrogen donor.
Strongly induced by hydrogen peroxide and diamide stress in a YAP1- and SKN7-dependent manner. Also induced by reducing stress by DTT.
By the presence of non-fermentable carbon sources and oxidative stress.
Decreased growth in non-fermentable sugar mediums (PubMed:23940037, PubMed:28076776). This is caused by a decrease in COQ6 levels, which results in a severe decrease in complex II, NADH-coenzyme Q dehydrogenase to complex III, and complex II to complex III activities in the electron transport chain (PubMed:23940037). Impaired antioxidant defenses (PubMed:23940037). Decreased phosphorylation of CAT5/COQ7 (PubMed:23940037). Increased phosphorylation of CIT1 and decreased citrate synthase activity (PubMed:28076776).
Protein phosphatase which positively regulates biosynthesis of the ubiquinone, coenzyme Q (PubMed:12220683, PubMed:23940037, PubMed:28076776, PubMed:30267671). Dephosphorylates and activates the ubiquinone biosynthesis protein CAT5/COQ7 (PubMed:23940037, PubMed:30267671). Also dephosphorylates CIT1 on 'Ser-462', which leads to its activation (PubMed:28076776).
There are conflicting reports on the effect the deletion of PTC7 causes in cells (PubMed:23940037, PubMed:28076776). In one report, deletion of PTC7 causes decreases in COQ6 levels, and mitochondrial defects observed are thought to be caused by disruption of the COQ6 pathway (PubMed:23940037). In another report, deletion of PTC7 causes no change in COQ6 levels and mitochondrial defects observed in mutants are not thought to be caused by changes in the COQ6 pathway (PubMed:28076776).
Component of the nucleoplasmic and cytoplasmic pre-60S ribosomal particles. Interacts directly with REI1.
Present with 45100 molecules/cell in log phase SD medium.
Probable metalloprotease involved in proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Accompanies the pre-60S particles to the cytoplasm.
Belongs to the HAD-like hydrolase superfamily. MasA/MtnC family.
Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Glutathione-dependent oxidoreductase with lower activity compared to the other members of the glutaredoxin family. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase.
Strongly induced by the exposure to arsenic which causes glutathione depletion.
Interacts with UTP25. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.
Involved in nucleolar processing of pre-18S ribosomal RNA. Required for efficient pre-rRNA cleavage at sites A0, A1 and A2, and biosynthesis of 18S rRNA.
The WD domains are required for nucleolar localization and U3 small nucleolar RNAs binding.
By osmotic stress and by methylglyoxal in a HOG pathway-dependent manner.
Catalyzes the production and accumulation of glycerol during hyperosmotic stress conditions. Glycerol acts as a osmoregulator that prevents loss of water and turgor of the cells.
Present with 807 molecules/cell in log phase SD medium.
Was originally thought to be GUT2, the FAD-dependent glycerol-3-phosphate dehydrogenase.
Component of the autophagy-specific VPS34 PI3-kinase complex I composed of VPS15, VPS30, VPS34, ATG14 and ATG38; and of the VPS34 PI3-kinase complex II composed of VPS15, VPS30, VPS34 and VPS38.
Required for cytoplasm to vacuole transport (Cvt), autophagy, nucleophagy, and mitophagy, as a part of the autophagy-specific VPS34 PI3-kinase complex I. This complex is essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Also plays a role in regulation of filamentous growth.
The C-terminal domain called the BARA domain is dispensable for the construction of both VPS34 PI3-kinase complexes, but is specifically required for autophagy through the targeting of complex I to the pre-autophagosomal structure.
General aromatic amino acid transaminase involved in several otherwise unrelated metabolic pathways. Responsible for phenylalanine and tyrosine biosynthesis. Active with glutamate, phenylalanine, tyrosine and tryptophan as amino donors and with phenylpyruvate, hydroxyphenylpyruvate, 2-oxoglutarate and pyruvate as amino acceptors. Also active with methionine, alpha-aminoadipate and leucine as amino donors when phenylpyruvate is the amino acceptor and in the reverse reactions with the corresponding oxo acids and phenylalanine as amino donor. Catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) in the methionine salvage pathway primarily using aromatic amino acids (tyrosine, phenylalanine and tryptophan) as the amino donors. Catalyzes the formation of alpha-aminoadipate from alpha-ketoadipate in the lysine biosyntheic pathway.
Activated by the amino acid-induced proteolytic removal of an N-terminal inhibitory domain by serine protease SSY5, an intrinsic component of the SPS-sensor. Processing requires at least 2 components of the SCF(GRR1) ubiquitin ligase complex, namely the F-box protein GRR1 and the E2 enzyme CDC34, but does not depend on the proteasome. Processing is negatively regulated by the protein phosphatase 2A regulatory subunit RTS1 (By similarity).
The N-terminal inhibitory domain contains conserved sequence elements important for cytoplasmic retention (Region I) and proteolytic processing (Region II) of the protein (By similarity). Region I is also required for ASI1/2/3-mediated negative regulation of transcription.
Transcription factor involved in the regulation of gene expression in response to extracellular amino acid levels. Synthesized as latent cytoplasmic precursor, which, upon a signal initiated by the plasma membrane SPS (SSY1-PTR3-SSY5) amino acid sensor system, becomes proteolytically activated and relocates to the nucleus, where it induces the expression of SPS-sensor-regulated genes, including the amino-acid permeases BAP2 and BAP3. Binding to promoters is facilitated by DAL81 (By similarity). Involved in the repression of genes subject to nitrogen catabolite repression and genes involved in stress response. Negatively regulated by inner nuclear membrane proteins ASI1, ASI2 and ASI3, which prevent unprocessed precursor forms that escape cytoplasmic anchoring from inducing SPS-sensor-regulated genes.
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Has a role in the secretory pathway.
Component of the spliceosome where it interacts with CUS1, HSH49, HSH155, IST3 and RSE1. Also interacts with YRA1.
Required for pre-mRNA splicing. Involved in regulation of drug sensitivity and may play a role in multidrug resistance.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). uS19 is involved in the nuclear export of the small ribosomal subunit precursor. Has a role in the late stage of the assembly of pre-40S particles within the nucleus and controls their export to the cytoplasm (PubMed:15167894).
Present with 21200 molecules/cell in log phase SD medium.
Present with 5171 molecules/cell in log phase SD medium.
Interacts with polyadenylate-binding protein PAB1.
Present with 20300 molecules/cell in log phase SD medium.
Required for nuclear migration during mitosis. It is required for the normal initiation of translation. Might mediate the dissociation of a specific protein complex of the translation machinery. Essential for viability.
Induced during anaerobic growth and by cold shock and heat shock.
Present with 35600 molecules/cell in log phase SD medium.
Seems to have esterase activity. Prefers ester of fatty acids from 4 to 16 carbon atoms.
Belongs to the mitochondrion-specific ribosomal protein mL40 family.
Component of the MIS complex, a complex that mediates N6-methyladenosine (m6A) methylation on some mRNAs during meiosis and is required for sporulation. In the complex, mediates the entry of the MIS complex in nucleolus, where methylation takes place.
Component of the MIS complex, composed of SLZ1, MUM2 and IME4.
During sporulation. Expression is activated by IME1 during meiosis.
Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding proteins, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation.
Expression is induced by the AFT2 iron homeostasis transcription factor, as well as by 8-methoxypsoralen and UVA radiation.
May form a homodimer or a heterodimer with a related family member. Interacts with OLA1, TMA17, and UBR1.
Amidase that catalyzes the last step of diphthamide biosynthesis using ammonium and ATP. Diphthamide biosynthesis consists in the conversion of an L-histidine residue in the translation elongation factor eEF-2 (EFT1 or EFT2) to diphthamide.
In the C-terminal section; belongs to the RutC family.
In the N-terminal section; belongs to the Diphthine--ammonia ligase family.
Interacts with elongation factor 2 (eEF-2; EFT1 or EFT2).
Functions as an activator subunit for the CBK1 protein kinase. Part of the regulation of ACE2 activity and cellular morphogenesis (RAM) signaling network. Required for coordinating polarized cell growth during interphase with the onset of mitosis. Required for mother/daughter cell separation after cytokinesis. Also has a role in the prevention of nuclear export of ACE2 from the daughter cell nucleus after mitotic exit. It coordinates ACE2-dependent transcription with mitotic exit network activation.
Interacts with protein kinase CBK1 to form the RAM CBK1-MOB2 kinase complex.
Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation (PubMed:23178123). RQC1 is essential for the recruitment of CDC48 to ribosomal subunits (PubMed:23479637).
Component of the ribosome quality control complex (RQC), composed of the E3 ubiquitin ligase RKR1/LTN1, RQC1 and RQC2, as well as CDC48 and its ubiquitin-binding cofactors. RQC forms a stable complex with 60S ribosomal subunits (PubMed:23178123, PubMed:23479637).
Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
Binds to the immunosuppressant drug FK506 and also mediates the sensitivity to rapamycin (PubMed:1996117). Rapamycin disrupts interaction with FAP1.
Interacts with HMO1. Interacts with FAP1.
Present with 1643 molecules/cell in log phase SD medium.
Ubiquitin-like protein modifier that can be covalently attached to lysine residues of target proteins. Activated by the dimeric UBA3-ULA1 E1 enzyme and conjugated by the E2 UBC12 to substrate proteins. RUB1-conjugated (neddylated) substrate proteins include the cullins CDC53, RTT101 and CUL3, and the modification enhances the ubiquitin-ligase activity of the corresponding cullin-RING-based E3 ubiquitin-protein ligase complexes (CRLs).
Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system. Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP (PubMed:18662542, PubMed:1989885, PubMed:24816100). The RSP5-UBA1-UBC5 ubiquitin ligase complex ubiquitinates RPO21 forming 'Lys-63'-linked polyubiquitin chains (PubMed:19920177).
Monomer. Binds simultaneously two ubiquitin chains (PubMed:24816100). Component of the RSP5-UBA1-UBC5 ubiquitin ligase complex composed of E3 RSP5, E1 UBA1 and E2 UBC5 (Probable).
There are two active sites within the E1 molecule, allowing it to accommodate two ubiquitin moieties at a time, with a new ubiquitin forming an adenylate intermediate as the previous one is transferred to the thiol site.
SNC1 and SNC2 are vesicle-targeting proteins essential for normal secretory traffic between the Golgi and the plasma membrane. They may also be involved in vesicle fusion.
Necessary for efficient spore formation.
TAF3 heterodimerizes with TAF10. The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Present with 6820 molecules/cell in log phase SD medium.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport (PubMed:10891509). NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof (PubMed:10891509). NUP116 interacts with the NUP82 subcomplex and GLE2 (PubMed:10801828, PubMed:9463388, PubMed:10891509). Through its FG repeats it interacts with numerous karyopherins including KAP95, PSE1 (GSP1-GDP dependent), MEX67, and to homomeric RNA (PubMed:9891088, PubMed:10952996, PubMed:11104765, PubMed:12372823). Interacts with CEX1 (PubMed:17203074). Interacts (via N-terminus) with AFG2 (via N-terminus) (PubMed:23185031).
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). Plays an important role in several nuclear export and import pathways including poly(A)+ RNA, tRNA, pre-ribosome, and protein transport. By binding ATPase AFG2, promotes AFG2-mediated release of shuttling protein RLP24 from pre-60S ribosomal particles (PubMed:23185031).
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YDR365W-A ORF.
Belongs to the protein kinase superfamily. BUD32 family.
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators. Important for bud site selection.
Present with 3020 molecules/cell in log phase SD medium.
This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event (PubMed:12023889). BUD32 has protein kinase activity in vitro, but in the context of the EKC/KEOPS complex, the catalytic subunit KAE1 switches the activity of BUD32 from kinase into ATPase (By similarity).
Ty1-PR3 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Multidrug resistance transporter involved in resistance and adaptation to quinidine and to the herbicide barban (4-chloro-2-butynyl [3-chlorophenyl] carbamate).
Contains one Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif essential for phosphatidate phosphatase activity.
Mg(2+)-dependent phosphatidate (PA) phosphatase which catalyzes the dephosphorylation of PA to yield diacylglycerol. May play a role in vesicular trafficking through its PAP activity at cortical actin patches (PubMed:23071111, PubMed:23335564). Can also utilize diacylglycerol pyrophosphate and lyso-PA as substrates with specificity constants 4- and 7-fold lower, respectively, when compared with PA (PubMed:23335564).
Monomer (PubMed:23335564). Interacts with ABP1 (PubMed:14737190).
Present with 2289 molecules/cell in log phase SD medium.
To yeast low affinity methionine permease (MUP3).
Belongs to the lysophospholipase family.
Sequentially removes both fatty acyl groups from diacylglycerophospholipids and therefore has both phospholipase A and lysophospholipase activities. However, it does not display transacylase activity. Substrate preference is phosphatidylserine > phosphatidylinositol > phosphatidylcholine > phosphatidylethanolamine (PubMed:10231538, PubMed:10497163). The substrate specificity is pH- and ion-dependent. In contrast with activities observed at optimum pH 3.5, the order of substrate preference at pH 5.5 is phosphatidylserine = phosphatidylethanolamine > phosphatidylcholine > phosphatidylinositol (PubMed:15588231).
Component of the GSH degradosomal complex composed of at least DUG1, DUG2 and DUG3.
Component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond.
Belongs to the ribonucleoside diphosphate reductase large chain family.
Heterotetramer of two large (R1) and two small (R2) subunits. S.cerevisiae has two different R1 subunits (RNR1 and RNR3) and two different R2 subunits (RNR2 and RNR4). The functional form of the small subunits is a RNR2-RNR4 heterodimer, where RNR2 provides the iron-radical center and RNR4 is required for proper folding of RNR2 and assembly with the large subunits. Under normal growth conditions, the active form of the large subunits is a homodimer of the constitutively expressed RNR1. In damaged cells or cells arrested for DNA synthesis, the reductase consists of multiple species because of the association of the small subunits (RNR2-RNR4) with either the RNR1 homodimer or a heterodimer of RNR1 and the damage-inducible RNR3.
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Two distinct regulatory sites have been defined: the specificity site, which controls substrate specificity, and the activity site which regulates overall catalytic activity. A substrate-binding catalytic site, located on R1, is formed only in the presence of the second subunit R2 (By similarity).
Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the large subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site (By similarity).
In association with GSP1, required for nuclear export of both pre-40S and pre-60S ribosomal subunits. Required for the late maturation of the 18S and 5.8S rRNA of the pre-40S ribosomes and for maturation of the 25S and 5.8S rRNA of the pre-60S ribosomes.
Long-term depletion of PKH2 in a PKH1 null mutant (Pkh depletion) induces programmed cell death. This is mediated by the lack of Pkh-dependent activation of the PKC1 downstream signaling cascade and results in accumulation of reactive oxigen species (ROS) and DNA fragmentation.
Serine/threonine-protein kinase which is part sphingolipid-mediated signaling pathway that is required for the internalization step of endocytosis by regulating eisosome assembly and organization, and modulating the organization of the plasma membrane. Phosphorylates and activates PKC1. Activates YPK1 and YPK2, 2 components of signaling cascade required for maintenance of cell wall integrity. Required for stress-induced P-body assembly and regulates global mRNA decay at the deadenylation step.
Sphingoid base activates kinase activity.
Belongs to the acetyltransferase family. ARD1 subfamily.
Catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover.
Component of the N-terminal acetyltransferase A (NatA) complex, which is composed of ARD1, NAT1 and NAT5. Can self-associate.
Interacts with MDM32. Participates in a complex of about 600 kDa.
Involved in the organization of the mitochondrial membranes and the global structure of the mitochondria. Also required for mitochondrial distribution and mobility as well as for the maintenance of mitochondrial DNA nucleoids structures.
Enters the endoplasmic reticulum as an inactive zymogen and is modified by four N-linked core oligosaccharides, giving rise to a precursor known as P1 (67 kDa). As P1 transits through the Golgi, extension of its core oligosaccharides leads to the Golgi-modified P2 precursor (69 kDa). P2 is sorted away from secretory proteins at or beyond a late Golgi compartment and is subsequently delivered to the vacuole via a prevacuolar endosome-like compartment. Upon arrival in the vacuole, the N-terminal prosegment of P2 is cleaved by vacuolar proteases to yield the enzymatically active mature vacuolar form of CPY (61 kDa).
Leads to vacuolar defects as well as defects in the terminal steps of autophagy, when ATG42 is also deleted (PubMed:29514932). The PCR1/ATG42 double deletion abrogates also the production of phytochelatin and the degradation of glutathione-S-conjugates (PubMed:17408619, PubMed:19897216).
Present with 44000 molecules/cell in log phase SD medium.
The four high mannose core N-glycans found in mature CPY are Man(11-15)GlcNAc(2) at Asn-124, Man(8-12)GlcNAc(2) at Asn-198, Man(9-14)GlcNAc(2) at Asn-279 and phosphorylated Man(12-17)GlcNAc(2) as well as Man(11-16)GlcNAc(2) at Asn-479.
Vacuolar serine-type carboxypeptidase involved in degradation of small peptides (PubMed:8679540). Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (PubMed:8679540). Also plays a role in breakdown of the autophagic body and the autophagosome-dependent protein synthesis (PubMed:29514932). Plays a key role in phytochelatin (PC) synthesis from glutathione (GSH) by cleaving the Gly from GSH and form the PC-peptides of the structure (gamma-Glu-Cys)2-Gly (PubMed:17408619). Also involved in resistance to xenobiotics via the degradation of glutathione-S-conjugates (PubMed:19897216).
Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. Is also involved in ribosome biogenesis. Associates with pre-60S subunits in the nucleus and is involved in its nuclear export. Cytoplasmic release of TIF6 from 60S subunits and nuclear relocalization is promoted by the GTPase RIA1/EFL1 and by SDO1. Also required for pre-rRNA processing.
Monomer. Associates with the 60S ribosomal subunit.
Phosphorylation at Ser-174 and Ser-175 promotes nuclear export.
Transcription factor that regulates expression of both nuclear and mitochondrial genes, and more specifically those required for glycerol-based growth and respiration.
Belongs to the GTP cyclohydrolase II family.
Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Present with 102130 molecules/cell in log phase SD medium.
Subunit of the eukaryotic elongation factor 1 complex (eEF1). Probably plays a role in anchoring the complex to other cellular components (By similarity).
The eukaryotic elongation factor 1 complex (eEF1) is probably a heterohexamer. Two trimeric complexes, each composed of eEF1A (TEF1 or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or TEF4), are probably dimerized via the eF1Bgamma subunits. The eEF1B subcomplex with the GEF activity is formed of eEF1Balpha and eEF1Bgamma. TEF4 interacts with EFB1 (By similarity).
The glycine cleavage system (glycine decarboxylase complex) catalyzes the degradation of glycine.
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix (Probable). Treatments with Lantrunculin A, the microbial peptide Chondramide or the microbial metabolite Chivazole F inhibit actin polymerization (PubMed:28796488). Each actin can bind to 4 others. Interacts with YIH1 (via C-terminus); this interaction occurs in a GCN1-independent manner (PubMed:15126500, PubMed:21239490). Component of the INO80 complex. Component of the SWR1 complex. Component of the NuA4 complex.
Acts on mitochondrial thioredoxin 3. Implicated in the defense against oxidative stress.
Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. SEH1 is part of the heptameric 0.5 MDa autoassembling NUP84 NPC subcomplex (NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1). Component of the SEA complex composed of at least IML1/SEA1, RTC1/SEA2, MTC5/SEA3, NPR2, NPR3, SEA4, SEC13 and SEH1.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Involved in nuclear poly(A)+ RNA export and NPC biogenesis. It is also required for normal nuclear morphology. Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis.
Interacts with AAH1, SKP1 and CDC53. Component of the SCF(SAF1) complex containing CDC53, SKP1, HRT1 and SAF1.
Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Targets AAH1 adenine deaminase for proteasome-dependent degradation upon entry into quiescence. Targets also URA7.
Required for 27S rRNA processing to 25S and 5.8S.
Essential for cell cycle arrest at the G2 stage following DNA damage by X-irradiation or inactivation of DNA ligase.
Present with 400 molecules/cell in log phase SD medium.
Present with 4870 molecules/cell in log phase SD medium.
Phospholipid scramblase that transports phosphatidylserine (PS) and phosphatidylethalonamine (PE) bidirectionally from one leaflet to the other of the phospholipid bilayer to at least partially collapse the membrane asymmetry established by NEO1 and other flippases (PubMed:27811238, PubMed:28057802). Functions in the trafficking pathway from endosomes to the trans-Golgi network (TGN) (PubMed:28057802).
Suppresses the growth defects caused by mutations of flippases including NEO1, DRS2, DNF1, DNF2 and DNF3, as well as of the DRS2 regulator CDC50.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YDR098C-A ORF.
Aspartic protease (PubMed:21266539). Appears to act as negative regulator of constitutive exocytosis (PubMed:10330187, PubMed:12051757). May act at the level of secretory vesicle docking and fusion as a competitive inhibitor of SNARE assembly (PubMed:12925750). Acts as a linker between the 19S proteasome and polyubiquitinated proteins like the HO endonuclease and UFO1 via UBA domain interactions with ubiquitin for their subsequent degradation (PubMed:17144915, PubMed:16478980). Required for S-phase checkpoint control (PubMed:11238935, PubMed:17144915).
Forms homodimers. Interacts with RAD23. These interactions are mediated by the UBA domain. Is also able to bind ubiquitin and polyubiquitinated proteins. Interacts with the SNAREs SNC1, SNC2, SSO1, TLG1 and TLG2. Binding to SSO1 is promoted by the phosphorylation of 'Ser-49' of SSO1 by TKP1.
Inhibited by the proteinase inhibitors indinavir, lopinavir, nelfinavir, isovaleryl pepstatin, ritonavir, saquinavir and tipranavir.
Belongs to the lcsJ thioesterase family.
Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Involved in both the HOG and the PKC MAP kinase signaling cascade necessary for adaptation to stress conditions due to high osmolarity or cell wall perturbation.
Forms a complex with Hsp90. Interacts with CDC28, CAK1 HOG1, SLT2 and STE11.
Phosphorylation at Ser-14 is required for the interactions with HOG1 and SLT2 MAP kinases and is crucial for adaptation to stress conditions due to high osmolarity or cell wall perturbation.
Forms cell-cycle specific filaments between the spindle pole bodies of dividing yeast cells.
Homooligomer; in vitro, FIN1 self-assembles into 10 nm diameter filaments. Interacts with the 14-3-3 proteins BMH1 and BMH2, and the protein phosphatase 1 complex catalytic subunit GLC7.
Overexpression is lethal in haploids and causes very poor growth in diploids.
Phosphorylated by CDC28. Phosphorylation is required for BMH1 and BMH2 interaction. Dephosphorylation by GLC7 depends on the presence of BMH1 and BMH2.
Strong overexpression results in the accumulation of filamentous structures resembling the neurofibrillary tangles found in cells of patients with Alzheimer disease.
The coiled coil domain is essential for dimerization.
Belongs to the peptidase C19 family. PAN2 subfamily.
Binds 2 metal cations per subunit in the catalytic exonuclease domain.
Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping by DCP1-DCP2 and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails, trimming the tails from their synthesized length to the slightly shorter, apparently messenger-specific length found on newly exported mRNAs. PAN cooperates with protein kinase DUN1 in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress.
Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex.
Forms a heterotrimer with an asymmetric homodimer of the regulatory subunit PAN3 to form the poly(A)-nuclease (PAN) deadenylation complex.
Positively regulated by the regulatory subunit PAN3. Negatively regulated by PAB1-binding protein PBP1. Inhibited under stress conditions. Inhibition of deadenylation under stress increases mRNA stability, which may be a mechanism to retain the majority of the cytoplasmic pool of mRNAs for later reuse and recovery from stress.
The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with PAN3.
Component of the NTR complex (NTC-related complex), composed of NTR1, NTR2 and PRP43. Interacts with CLF1, NTR1 and PRP43.
Core component of the ESCRT-III complex (endosomal sorting required for transport complex III). ESCRT-III appears to be sequentially assembled as a flat lattice on the endosome membrane and forms a transient 450 kDa complex that contains DID4, oligomerized SNF7, VPS20 and VPS24. SNF7 oligomerization into a membrane-associated filament is nucleated by association of SNF7 with VPS20; the process is terminated through association of VPS24, possibly by capping the SNF7 filament. VPS24 subsequently associates with DID4/VPS2.
Required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Can directly stimulate VPS4 ATPase activity. The DID4/VPS2-VPS24 subcomplex is required for the VPS4-dependent dissociation of ESCRT-III.
Homohexamer. Binds to nucleic acids. Binds single-stranded DNA and RNA with higher affinity than double-stranded DNA.
Inhibited by E64, a specific inhibitor of cysteine proteases, N-ethylmaleimide, iodacetamide, and mercury and zinc ions.
Produced by alternative initiation at Met-30 of isoform Mitochondrial.
The N-terminus of isoform Cytoplasmic is blocked.
The normal physiological role of the enzyme is unknown, but it is not essential for the viability of yeast cells. Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity. Acts as a repressor in the GAL4 regulatory system, but this does not require either the peptidase or nucleic acid-binding activities.
Required for the establishment of the bipolar budding pattern. Involved in selecting bud sites at both the distal and proximal poles of daughter cells as well as near previously used division sites on mother cells. Has a role in the localization of BUD8, the distal bipolar budding landmark, and of BUD9, the proximal pole landmark.
DNA-binding protein that is probably part of the rDNA transcription apparatus. Acts synergetically with the RPA49 subunit of RNA polymerase I during rDNA transcription. May participate in mutagenesis control.
Interacts with FPR1. Interacts with an unidentified DNA helicase. Associates with rDNA.
Present with 19000 molecules/cell in log phase SD medium.
Inactivated in a complex with phosphatase methylesterase PPE1 (PP2Ai). Interacts with phosphatase 2A activator RRD1, which can reactivate PP2Ai by dissociating the catalytic subunit from the complex. Interacts with TAP42.
Reversibly methyl esterified on Leu-368 by leucine carboxyl methyltransferase 1 (PPM1) and protein phosphatase methylesterase 1 (PPE1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization.
Belongs to the GcvT family. CAF17 subfamily.
Required for lysine and glutamate prototrophy and mitochondrial genome maintenance. Has a role in the maturation of mitochondrial aconitase-type and radical-SAM Fe/S proteins biotin synthase and lipoic acid synthase.
Component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs) (PubMed:9556561, PubMed:9843512, PubMed:21131909). The protein component of the H/ACA snoRNP contains CBF5, GAR1, NHP2 and NOP10 (PubMed:9556561, PubMed:9843512, PubMed:21131909). The complex contains a stable core composed of CBF5 and NOP10, to which GAR1 and NHP2 subsequently bind. Interacts with snoRNAs (PubMed:9556561, PubMed:9843512).
Non-catalytic component of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP), which catalyzes pseudouridylation of rRNA and is required for ribosome biogenesis (PubMed:9303321, PubMed:9843512). This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1 (PubMed:9303321, PubMed:9843512). Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs (PubMed:9843512). The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs (PubMed:21131909). The H/ACA snoRNP complex mediates pseudouridylation at position 93 in U2 snRNA (PubMed:21131909). Essential for growth (PubMed:9303321).
Alcohol acetyltransferase that catalyzes the synthesis of ethyl acetate from ethanol and acetyl-CoA (PubMed:28356220). Can also function as a thioesterase by hydrolyzing acetyl-CoA in the absence of ethanol, as well as esterase hydrolyzing ethyl acetate (By similarity).
Reduces ethyl acetate production by at least 50%.
S.cerevisiae produces only trace amounts of ethyl acetate. These traces help S.cerevisiae disseminate in the environment by attracting fruit flies. However, as ethyl acetate is a key flavor compound and the most abundant ester in wine and beer, ethyl acetate-producting genes such as ethanol acetyltransferase are relevant for the fermented foods and beverages industry.
ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M (PubMed:10931920). May have a role in changing DNA topology to allow the loading of proteins involved in maintaining sister chromatid cohesion in the vicinity of the centromeres (PubMed:15020404, PubMed:14742714). Has a specific role in chromosome segregation during meiosis II (PubMed:15226378).
Belongs to the DEAD box helicase family. DEAH subfamily. DDX11/CHL1 sub-subfamily.
Belongs to the peroxidase family. Cytochrome c peroxidase subfamily.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Forms a one-to-one complex with cytochrome c.
Present with 6730 molecules/cell in log phase SD medium.
Involved in nucleotide excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Along with RAD10 forms an endonuclease that specifically degrades single-stranded DNA.
Has a role in the initiation of DNA replication. Required at S-phase checkpoint. Also required for the proper activation of RAD53 in response to DNA damage and replication blocks.
Phosphorylated by CDC28 at the onset of S-phase. This phosphorylation, specifically phosphorylation of Thr-84 promotes interaction with DPB11 leading to DNA replication. Dephosphorylated by CDC14.
Involved in the processing and trafficking of GAS1 and PHO8 glycosylated proteins.
Homodimer; may form higher order oligomers (PubMed:23993092). Interacts with the large RNA polymerase II subunit RPO21; the interaction is direct and serves to bridge RPO21 to the Elongin complex in a manner dependent on transcription stress (PubMed:15166235, PubMed:23993092). Interacts with RAD26 (PubMed:11859374). Interacts (via CUE domain) with the Elongin complex subunit ELA1 (via C-terminus); the interaction is direct (PubMed:23993092).
Proteolytically cleaved by the proteasome in response to transcription stress; the resulting N-terminal form constitutes the activated nuclear form and the C-terminal portion is degraded.
Recruits the ubiquitination machinery to RNA polymerase II for polyubiquitination, removal and degradation, when the transcription-coupled repair (TCR) factor RAD26 fails to efficiently displace stalled RNA polymerase II (PubMed:11859374, PubMed:15166235, PubMed:15960978). Also involved in telomere length regulation (PubMed:15863512). Binds DNA (PubMed:15863512).
The C-terminal part appears to promote nuclear export.
Ubiquitinated at Lys-281 or Lys-288, and at Lys-328 or Lys-329. in a manner dependent on RSP5; ubiquitination accelerates its proteolytic processing by the proteasome.
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Belongs to the MsrA Met sulfoxide reductase family.
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. Also able to reduce dimethyl sulfoxide (DMSO) as well, with DMS as the product.
A divalent cation Ca(2+), Mg(2+) or Mn(2+).
Activity is inhibited both by interaction with VMA13 and by V-ATPase acidification of the lumen. The activity of VMA13 is not required for YND1 inhibition.
Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates. Has equal high activity toward ADP/ATP, GDP/GTP, and UDP/UTP and approximately 50% less toward CDP/CTP and thiamine pyrophosphate. Has no activity toward GMP. Required for Golgi glycosylation and cell wall integrity. Together with CDC55, required for adenovirus E4orf4 (early region 4 open reading frame 4) induced toxicity, the apyrase activity is not required for this function. Plays a role in sphingolipid synthesis.
Cells are partially resistant to E4orf4 and can partially suppress the spindle checkpoint defect in CDC55 deletion mutant. Does not suppress the rapamycin-resistance of CDC55 deletion mutant. YND1 and CDC55 double mutant is fully resistant to E4orf4. Deletion mutant suppresses the synthetic lethality of triple mutants, where UPC2 and ECM22 are knocked out along with either HAP1, ERG6 or ERG28.
Interacts with activator subunit VMA13 of vacuolar H(+)-ATPase. Interacts with CDC55; this interaction is disrupted by adenovirus E4orf4, which remains associated with both YND1 and CDC55.
Belongs to the glycosyltransferase 4 family.
Catalyzes the initial step in the synthesis of dolichol-P-P-oligosaccharides.
Transcriptional activator of glycolytic gene expression, such as enolase genes (ENO1 and ENO2), glyceraldehyde-3-phosphate dehydrogenase gene (TDH), phosphoglycerate kinase (PGK1), phosphoglycerate mutase (PGM1), pyruvate kinase (PYK1) and triosephosphate isomerase (TPI1) genes. Binds DNA on E-box motifs: 5'-CANNTG-3'.
Belongs to the F-actin-capping protein beta subunit family.
Shows evidence of translation. May be a new protein-coding gene that originated de novo from non-coding sequences, e.g. transcripts of unknown function that escape exonucleolytic degradation (stable unannotated transcripts or SUTs) and associate with ribosomes.
Involved in the targeting of ARL1 to the Golgi. Can bind and hydrolyze GTP.
Adds the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(1)Man(9)GlcNAc(2)-PP-Dol.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.
Protein kinase required for the cell cycle where it is involved in mitotic exit. A component of the fear (CDC14 early anaphase release) network which promotes CDC14 release from the nucleolus during early anaphase. Phosphorylates SCC1/MCD1 and NET1.
Lipid particle-localized triacylglycerol (TAG) lipase. The lipid droplet/particle is a lipid storage compartment which serves as a depot of energy and building blocks for membrane lipid biosynthesis. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs, releasing and supplying specific fatty acids to the appropriate metabolic pathways (PubMed:10515935, PubMed:12682047, PubMed:16267052). Also catalyzes the acylation of lysophosphatidic acid (LPA). Important for efficient sporulation, but rather through its acyltransferase than lipase activity (PubMed:20016004).
Loses its lipolytic activity in cells lacking nonpolar lipids.
The C-terminal wHLH region seems to mediate telomere-specific function.
Not known. Seems to be able to provoque the non-Mendelian trait [PIN(+)] which is required for the de novo appearance of the [PSI(+)] prion.
As accessory component of the DNA polymerase epsilon (DNA polymerase II) participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair.
GTPase activating protein for GPA2. Negatively down-regulates glucose-induced cAMP signaling via GPA2.
Essential for the synthesis of pyruvate decarboxylase. May be important for a high basal level of PDC gene expression or play a positive role in the autoregulation control of PDC1 and PDC5.
Present with 572 molecules/cell in log phase SD medium.
Belongs to the reverse transcriptase family. Telomerase subfamily.
Catalytic subunit of the telomerase holoenzyme complex composed minimally of EST2 and the telomerase RNA template component.
Deletion causes telomere shortening and senescence.
Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Belongs to the carbon-nitrogen hydrolase superfamily. Nitrilase family.
Could be the product of a pseudogene. NIT1/YIL164C seems to be the N-terminal part of a putative nitrilase-like protein formed of NIT1/YIL164C and YIL165C.
Transcription factor which regulates nonfermentable carbon utilization (By similarity). Binds specifically to 5'-CGGN(8)CGG-3' and 5'-CGGN(9)CGG-3' sequences in the promoter region.
Present with 238000 molecules/cell in log phase SD medium.
Has been originally identified as involved in pre-tRNA splicing since its deletion accumulates pre-tRNAs (PubMed:7363329, PubMed:3031485). However, further studies have shown that it is actually a nuclear pore protein involved in transport of pre-tRNAs and mature tRNAs (PubMed:9774653).
Interacts with CEX1, GSP1, GSP2, NSP1, NUP2 and UTP8.
tRNA nucleus export receptor which facilitates tRNA translocation across the nuclear pore complex. Preferentially interacts with tRNAs with mature 5'- and 3'-termini and does not distinguish between intron-containing and spliced tRNAs. In the nucleus binds to tRNA and to the Ran-GTPases GSP1 or GSP2 in their active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP cause release of the tRNA from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
Required to stabilize the cell wall in the absence of multiple GPI-anchored mannoproteins.
Drug export permease. Multi-copy suppressor of loss-of-function mutation of GAL11. Involved specifically in transcription of GAL4-dependent genes. Can link GAL4 with the basal transcription machinery if GAL11 is missing. Confers resistance to 10-N-nonyl acridine orange (NAO) and in general to cationic dyes.
CBS1 protein devoid of mitochondrial targeting sequences can enter mitochondria in vivo, possibly due to a bypass of the mitochondrial import system.
The in vitro imported CBS1 protein is functional and soluble indicating that the N-terminal part of CBS1 confers some binding to mitochondrial membranes.
mRNA-specific translational activator of cytochrome b. The cytochrome b (COB) leader RNA may represent the target sequence for CBS1 and CBS2, tethering the COB mRNA to the inner mitochondrial membrane, where cotranslational insertion of cytochrome b into the membrane can occur.
DNA-binding transcriptional repressor involved in response to toxic agents such as ribonucleotide reductase inhibitor, hydroxyurea (HU).
Phosphorylated during genotoxic stress. DNA damage induces phosphorylation by SNF1 or the MEC1 pathway and leads to its inactivation, which allows induction of damage response genes.
Present with 13900 molecules/cell in log phase SD medium.
Inhibited by acetylsalicylic acid (aspirin).
Interacts with the C-terminus of SAC1, thereby sequestering it to the endoplasmic reticulum in exponentially growing cells. Under nutrient limitation conditions, this interaction is rapidly abolished.
Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins.
Interacts with the response regulatory domains of SLN1 and SSK1.
Phosphorelay intermediate protein that is part of the branched SLN1-YPD1-SKN7/SSK1 two-component regulatory system, which controls activity of the HOG1 pathway and gene expression in response to changes in the osmolarity of the extracellular environment. Catalyzes the phosphoryl group transfer from the membrane-bound osmosensing histidine kinase SLN1 to two distinct response regulator proteins, SSK1 in the cytoplasm, and transcription factor SKN7 in the nucleus.
The phosphorelay mechanism involves the sequential transfer of a phosphate group from 'His-576' (H1) to 'Asp-1144' (D1) of SLN1, then to His-64 (H2) of YPD1 and finally to 'Asp-554' (D2) of SSK1 or 'Asp-427' (D2) of SKN7.
Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1. Interaction with PRP8 is important for recruitment to the U4/U6-U5 tri-snRNP complex. Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2.
Contains two helicase domains. The N-terminal helicase domain has catalytic activity by itself, contrary to the C-terminal helicase domain that may have a regulatory role and enhance the activity of the first helicase domain.
RNA helicase that plays an essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes. Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome.
Belongs to the glucose-6-phosphate dehydrogenase family.
Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis (By similarity).
Shows growth defects in acetate-supplemented medium; the phenotype is enhanced by addition of hydrogen peroxide (increased oxidative stress) and/or double knockout of ZWF1 and YHM2 (PubMed:20371607). Decreases the cytosolic NADPH/NADP(+) ratio; this effect is enhanced in the presence of hydrogen peroxide (PubMed:20371607). Ribitol-5P absent from cell (PubMed:30240188). Decreases cellular levels of ribose-5P and ribulose-5P (PubMed:30240188). Decreases cytosolic levels of citrate and oxoglutarate in the presence of hydrogen peroxide (PubMed:20371607). Double knockouts of ZWF1 and YHM2 show an increased mitochondrial NADPH/NADP(+) ratio in the presence of hydrogen peroxide (PubMed:20371607). Reactive oxygen species (ROS) levels are moderately increased following hydrogen peroxide treatment; in double knockouts of YHM2 and ZWF1 there is a larger increase (PubMed:20371607).
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate (By similarity). Plays a role in the physiological regulation of the intracellular CoA concentration.
Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family.
DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. RNA polymerases are composed of mobile elements that move relative to each other. In Pol II, RPB6 is part of the clamp element and together with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds.
Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3. Interacts with snoRNA U3. Interacts with EBP2, FAF1, MPP10, RPS16A and RRP14.
Interacts with SKP1. Component of the probable SCF(GRR1) complex containing CDC53, SKP1, RBX1 and GRR1.
Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and directs ubiquitination of phosphorylated CLN1, CLN2 and GIC2. Probably constitutes the primary response element required for the generation or interpretation of the signal that induces glucose repression.
Probable membrane-bound O-acyltransferase (By similarity). Together with GUP1, has an influence on the chemical composition of the yeast extracellular matrix (yECM) in yeast multicellular aggregates, such as biofilms and colonies (PubMed:25589358).
Was originaly thought to be involved in active uptake of glycerol driven by electrogenic proton symport (PubMed:10931309), but has later been shown to be an acyltransferase and that effects on glycerol transport may be indirect (PubMed:15381122).
Farnesyl pyrophosphate synthase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (PubMed:8096487). ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (PubMed:8096487). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD1/ERG19 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (PubMed:32679672).
Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Potential transcription factor; suppressor for a mitochondrial RNA polymerase mutant.
Required for assembly of the mitotic spindle. Interacts with spindle microtubules to produce an outwardly directed force acting upon the poles. Following spindle assembly, CIN8 and KIP1 apparently act to oppose a force that draws separated poles back together. This force seems to be mediate by KAR3.
Confers sensitivity to calcofluor white, and prevents growth on non-fermentable carbon sources such as glycerol or lactate (PubMed:11353088, PubMed:24998441). Sensitizes cells to oxidative stress (PubMed:24998441). Leads to a decrease in peroxisome abundance when oleate was used as a sole carbon source (PubMed:24998441).
Transcriptional activator required for growth on non-fermentable carbon sources and that regulates genes involved in fatty acid utilization (PubMed:11353088, PubMed:24998441). Acts as a direct activator that binds the promoters of oleate utilizing genes, encoded key enzymes in beta-oxidation and NADPH regeneration (POX1, FOX2,POT1 and IDP2), the glyoxylate shunt (MLS1 and ICL1), and gluconeogenesis (PCK1 and FBP1) (PubMed:24998441). Regulates also the abundance of peroxisomes that are vital for fatty acid oxidation (PubMed:24998441).
Zinc cluster transcription factor involved in resistance to cycloheximide.
May be an RNA-binding protein involved in control of an RNA processing pathway that influences the regulation of cell growth in early log phase. Can bind to RNA and single-stranded DNA but not double-stranded DNA.
Belongs to the universal ribosomal protein uL2 family.
Component of the mitochondrial large ribosomal subunit (mt-LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. uL2m has a Na/K ligand binding site.
Homooligomers. Interacts with EMP46 in the endoplasmic reticulum membrane. Interacts with the coatomer proteins COP1, SEC21 and SEC23.
Involved in the secretion of glycoproteins and in nucleus architecture and gene silencing. Required for the endoplasmic reticulum exit of EMP46.
Belongs to the DASH complex DAD2 family.
Belongs to the replication factor A protein 2 family.
Binds to single-stranded sequences participating in DNA replication in addition to those mediating transcriptional repression (URS1) and activation (CAR1). Stimulates the activity of a cognate strand exchange protein (SEP1). It cooperates with T-AG and DNA topoisomerase I to unwind template DNA containing the simian virus 40 origin of DNA replication.
Heterotrimer of 69, 36, and 13 kDa chains. The DNA-binding activity may reside exclusively on the 69 kDa subunit. Interacts with MCM10.
Phosphorylated in a cell cycle-dependent manner with phosphorylation increasing at the entry in S phase and dephosphorylation occurring at mitosis.
Interacts in a SNARE-pin with the SNAREs TLG2 (Qa), VTI1 (Qb), and SNC1 or SNC2 (R). Interacts with VPS51 of the VFT (or GARP) complex.
Palmitoylated by SWF1, which prevents its recognition and ubiquitination by TUL1 and its subsequent degradation.
Phosphorylated at Thr-31 by TPK1 and dephosphorylated by SIT4.
SNARE protein (of Qc type) involved in membrane fusion probably in retrograde traffic of cytosolic double-membrane vesicles derived from both, early and possibly late endosomes/PVC (prevacuolar compartment) back to the trans-Golgi network (TGN or late Golgi). It has been reported to function both as a (target membrane) t-SNARE and as a (vesicle) v-SNARE. Upon vesicle tethering to the target membrane, which requires additional proteins, a SNARE-pin is formed. This is a very stable 4 parallel alpha-helical coil bundle consisting of 4 SNARE domains (usually one of each type: Qa, Qb, Qc, and R), of which at least one is anchored in the opposite membrane. The formation of the SNARE-pin is believed to bring the two membranes in close proximity and to provide the energy to drive membrane fusion. Through its interaction with the VFT (or GARP) complex, it may also contribute to vesicle recognition specificity and tethering. Regulation of SNARE-pin formation also seems to depend on the phosphorylation state of the protein, phosphorylation by TPK1 causing inhibition and dephosphorylation by SIT4 activation.
Present with 22900 molecules/cell in log phase SD medium.
Involved in the cellular supply of leucine from externally offered leucine-containing dipeptide substrates.
Homodimer and homotetramer. Interacts with LOC1, MYO4, PUF6, SHE3 and with RNA pol II subunits RPO21, SPT4 and SPT5.
RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Recruits the MYO4-SHE3 complex to the ASH1 mRNA. Recruits also LOC1 and PUF6 to ASH1 mRNA, which are required for translational repression of this mRNA.
Performs an essential function in the repair of oxidatively damaged mtDNA that is required for the maintenance of the mitochondrial genome. Binds to DNA.
Associates with 60S pre-ribosomal particles.
Essential for cell growth. Plays a role in assembly of 60S pre-ribosomal particles in the nucleolus. Also required for replication of the M1 double-stranded RNA of the L-A virus. This latter function may reflect an enhanced requirement for free 60S ribosomal particles for the translation of viral mRNAs which lack poly-A tails.
Tetramer composed of an alpha subunit, an alpha' subunit, one beta subunit and one beta' subunit (PubMed:12242279). Interacts with FACT subunits POB3 and SPT16 (PubMed:12242279). Interaction with YTA7 (PubMed:22156209).
Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts (via C-terminus) with GEA1 (via N-terminal region) and KEI1 (via C-terminal region).
Present with 77900 molecules/cell in log phase SD medium.
Belongs to the actin family. ARP10 subfamily.
Pointed-end-associated component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding (By similarity). The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. May regulate the association of the dynactin complex with the plasma membrane.
Self-associates. Component of the dynactin complex composed of at least ARP1, JNM1, NIP100 and ARP10. Dynactin comprises a short rod of the ARP1 filament attached to ARP10 at its pointed-end and probably associated with the capping protein at its barbed-end. The rod is implicated in dynein cargo binding. A sidearm formed by NIP100 projects from the ARP1 filament and is implicated in motor binding (By similarity). Interacts with ARP1 and JNM1.
Belongs to the eukaryotic initiation factor 4E family.
Component of the eIF4F complex, which composition varies with external and internal environmental conditions. It is composed of at least eIF4A (TIF1/TIF2), eIF4E (TIF45) and eIF4G (TIF4631 or TIF4632) (By similarity). Interacts with PAT1 in a RNA-dependent manner. eIF4E is also known to interact with other partners.
Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures.
Component of the nascent polypeptide-associated complex (NAC), a dynamic component of the ribosomal exit tunnel, protecting the emerging polypeptides from interaction with other cytoplasmic proteins to ensure appropriate nascent protein targeting. The NAC complex also promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane and blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum EGD1 may act as a transcription factor that exert a negative effect on the expression of several genes that are transcribed by RNA polymerase II. Can enhance DNA binding of the GAL4 protein activator.
Present with 18000 molecules/cell in log phase SD medium.
Permease for leucine, valine and isoleucine. Also transports cysteine, methionine, phenyalanine, tyrosine and tryptophan.
Component of the phosphopantothenoylcysteine decarboxylase (PPCDC) involved in the coenzyme A synthesis. Acts as an inhibitory subunit of protein phosphatase PPZ1, which is involved in many cellular processes such as G1-S transition or salt tolerance.
Cleaves A-5'-PPP-5'A to yield AMP and ADP. Can cleave all dinucleoside polyphosphates, provided the phosphate chain contains at least 3 phosphates and that 1 of the 2 bases composing the nucleotide is a purine. Is most effective on dinucleoside triphosphates. Negatively regulates intracellular dinucleoside polyphosphate levels, which elevate following heat shock.
Divalent metal cations. Mn(2+) is the preferred ion.
Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I together with a subset of U3 proteins required for transcription (t-UTPs). Involved in ribosome biosynthesis.
Belongs to the DASH complex DUO1 family.
Required for nuclear migration to the bud neck during cell division. Targets cytoplasmic dynein to microtubule plus ends thereby promoting dynein-mediated microtubule sliding along the bud cortex and consequently the movement of the mitotic spindle to the bud neck.
Active efflux of weakly charged organic compounds of 90 cubic Angstroms to 300 cubic Angstroms surface volume. Confers resistance to numerous chemicals including cycloheximide, sulfomethuron methyl, steroids, antiseptics, antibiotics, anticancer, herbicides, mycotoxins, insecticides, ionophores, alkaloids, flavonoids, phenothiazines, organotin compounds, carbazoles, lysosomotropic aminoesters, detergents, rhodamines and other fluorophores, azoles and other antifungals. Exhibits nucleoside triphosphatase activity.
Expressed during exponential growth. Transcription is transiently activated within 40 min after induction by benomyl and other toxic chemicals. Multidrug resistance and PDR5 mRNA level are activated by the transcription regulators PDR1, PDR3, YAP1, YAP2, STB5 and by the mitochondrial rho zero mutation. Mutations or deletion in the PDR1 or PDR3 transcription factors strongly activate PDR5 mRNA and PDR5 translation. The transcription regulator RDR1 represses PDR5 expression.
FK506, isonitrile, enniatin, RU49953, kitasatospora E420, staurosporine CGP42700, prenyl-flavonoids, D-octapeptides were found to be inhibitors in vivo. Vanadate and oligomycin were found to be inhibitors in vitro.
Full-sized PDR5 orthologs are found only in fungi and plants. Their topology and substrate specificity are distinct from mammalian MDR transporters.
Present with 42000 molecules/cell in log phase SD medium in log phase SD medium.
Strains lacking PDR5 are used for toxicity tests. Strains overexpressing PDR5 are used for screening antifungal sensitizers.
The N-terminal ABC transporter domain (positions 161 to 410) contains degenerated Walker A and B ATP-binding motifs, suggesting that it may be less efficient in ATP binding or not functional at all. This is a distinctive feature of the PDR subfamily.
The unusual length of the two extracellular loops at positions 686 to 774 and 1408 to 1476 is another specific feature of the PDR subfamily which may have an important role for function.
This protein has been 'adopted' by Andre Goffeau from the Catholic University of Louvain (Belgium). The above-mentioned scientist has agreed to help us to curate information available on this protein. We are grateful to that person for committing precious time to help producing annotation useful to the whole community. However, that person is not responsible for any errors or omissions in this UniProtKB/Swiss-Prot entry. If you have found something wrong or missing in this entry you should submit an update report to: help@uniprot.org.
Ubiquitinylation mediates endocytosis and vacuolar degradation. Phosphorylation by casein kinase I stabilizes the protein half-life.
Farnesylated by RAM1-RAM2, which is required for targeting RAS1 to the cytoplasmic site of the endoplasmic reticulum, where proteolytic processing of the C-terminus by RCE1 and methylation of the resulting carboxyl group by STE14 occurs.
Palmitoylated by the ERF2-SHR5 complex, which is required for proper plasma membrane localization of RAS1.
It is found only in a mating type cells.
This protein called 'barrier activity' is excreted by yeast cells mating type a. It is probably a protease that cleaves alpha-factor and thus acts as an antagonist of this mating pheromone and establishes optimal pheromone concentration for conjugation.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Involved in Pol III transcription reinitiation and RNA cleavage during transcription termination.
Component of the 1.8 MDa SAGA complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9.
Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. SPT7 is transcriptional activator of TY elements and other genes.
Shuttles copper to the transport ATPase CCC2. Protects against oxygen toxicity.
Belongs to the pyridoxine kinase family.
Required for synthesis of pyridoxal-5-phosphate from vitamin B6 (By similarity). Important for bud site selection.
Causes increased sensitivity to hypertonic growth medium.
Irreversibly catalyzes the reduction of fumarate to succinate. Together with the second isozyme of soluble fumarate reductase (FRD1), essential for anaerobic growth. Involved in maintaining redox balance during oxygen deficiency conditions. Reduction of fumarate is the main source of succinate during fermentation, and under anaerobic conditions, the formation of succinate is strictly required for the reoxidation of FADH(2).
Dephosphorylates a number of phosphatidylinositols (PIs) like phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), but also phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Controls the cellular levels and subcellular distribution of phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-bisphosphate. Plays an essential role in a TGN (trans Golgi network)-to-early endosome pathway. Involved in clathrin-mediated protein sorting at the TGN.
The 5-phosphatase domain (residues 568 to 856) selectively removes the phosphate group at the 5' position of inositol of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2).
The C-terminal proline-rich domain is required for the function and associates with clathrin heavy chain CHC1.
GTPase involved in activation of the TORC1 signaling pathway, which promotes growth and represses autophagy in nutrient-rich conditions (PubMed:26510498, PubMed:32801125, PubMed:28993463). Also required for TORC1 inactivation during nitrogen starvation (PubMed:28993463). Required for intracellular sorting of GAP1 out of the endosome (PubMed:16732272). Functionally associated with the inorganic phosphate transporter PHO84, and may be involved in regulating its function or localization (PubMed:1620108).
Heterodimer; with GTR2 (PubMed:21816923). Component of the GSE complex composed of GTR1, GTR2, SLM4, MEH1 and LTV1 (PubMed:16732272). Interacts with GTR2; the interaction is direct (PubMed:21816923). Interacts with TOR1 (PubMed:29698392).
Sensitive to rapamycin (TORC1 signaling-inhibitor) (PubMed:28993463). Decreases and delays activation of TORC1 signaling in nitrogen-replete conditions (glutamine nitrogen source) (PubMed:29698392). Abnormal punctate localization of PIB2 and TOR1 in nitrogen-replete conditions (glutamine nitrogen source) (PubMed:29698392, PubMed:32801125, PubMed:28993463). Increases cellular levels of glutamine and alanine during high hydrostatic pressure (mechanical stress) (PubMed:32801125). Sensitive to high hydrostatic pressure (PubMed:32801125). Resistance to tunicamycin (endoplasmic reticulum stressor) administered together with FK506 (calcineurin inhibitor) (PubMed:26510498). Normal localization of KOG1 and TOR1 to the vacuolar membrane (PubMed:28483912). Simultaneous disruption of PIB2 results in TOR1 mislocalization and loss of TORC1 activity and viability (PubMed:29698392).
Component of the allantoate transport system.
Phosphatidylinositol 3-kinase homolog, component of both TORC1 and TORC2. TORC1 regulates multiple cellular processes to control cell growth in response to environmental signals. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls ribosome biogenesis via control of rRNA, ribosomal protein and tRNA gene expression, and rRNA processing. TORC1 positively controls protein biosynthesis by regulation of mRNA stability, translation initiation factor activity, and high-affinity amino acid permeases that serve to provide amino acids for use by the translation machinery. TORC1 also promotes growth by sequestering a number of nutrient and general stress-responsive transcription factors in the cytoplasm. TORC1 negatively controls macroautophagy, a process to recycle surplus cytoplasmic mass under nutrient starvation conditions. TORC1 controls many of these processes via TIP41-TAP42-mediated inhibition of the type 2A-related phosphatases PP2A and SIT4 (PubMed:10198052, PubMed:10329624, PubMed:10604478, PubMed:11741537, PubMed:15620355, PubMed:7606777, PubMed:8741837, PubMed:9539725, PubMed:9843498). In nutrient-rich conditions, responsible for the phosphorylation of AGC S6 kinase (S6K) YPK3, activating YPK3 kinase activity and promoting phosphorylation of ribosomal protein S6 (PubMed:25767889). Phosphorylates kinase SCH9 at 6 amino acids in the C-terminus, activating SCH9 kinase activity to properly regulate ribosome biogenesis, translation initiation, and entry into stationary phase (PubMed:17560372). TORC2 regulates cell cycle-dependent polarization of the actin-cytoskeleton, cell wall integrity, and receptor endocytosis. TORC2 controls polarity of the actin cytoskeleton, which is required for orienting the secretory pathway toward discrete growth sites, via the RHO1/PKC1/MAPK cell integrity pathway by activating the RHO1 guanine nucleotide exchange factor ROM2. TORC2 phosphorylates the AGC kinase YPK2, an upstream effector of the cell integrity pathway. TORC2 negatively regulates calcineurin-dependent stress signaling via phosphorylation of its effector SLM1-SLM2 (PubMed:14593073, PubMed:15372071, PubMed:16055732, PubMed:16959779, PubMed:8846782, PubMed:8943012).
The target of rapamycin complex 1 (TORC1) is composed of at least KOG1, LST8, TCO89 and either TOR1 (TORC1-A) or TOR2 (TORC1-B) (PubMed:12408816, PubMed:12631735). TORC1 binds to and is inhibited by FKBP-rapamycin (PubMed:12408816). Interacts with PIB2; following activation of PIB2 by glutamine (PubMed:29698392). The target of rapamycin complex 2 (TORC2) is composed of at least AVO1, AVO2, BIT61, LST8, TOR2 and TSC11 (PubMed:12408816, PubMed:12631735, PubMed:16002396, PubMed:16959779). TORC2 likely forms a homodimer (PubMed:16002396). Contrary to TORC1, TORC2 does not bind to and is not sensitive to FKBP-rapamycin (PubMed:12408816). Interacts with SLM1 and SLM2 (PubMed:15689497, PubMed:16959779).
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication. SWM1 is required for APC/C activity in meiosis.
The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. SWM1 interacts directly with CDC23 and APC5, and is required to tether APC9, CDC16, CDC26 and CDC27 to the complex.
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly. Required for cell wall integrity.
Component of the CBC complex, which binds co-transcriptionally to the 5'-cap of pre-mRNAs and is involved in maturation, export and degradation of nuclear mRNAs. The CBC complex is required for efficient pre-mRNA splicing through efficient commitment complex and spliceosome formation. Together with NPL3, the CBC complex is required for export of mRNAs out of the nucleus. The CBC complex is also involved in nuclear mRNA degradation, probably by directing the mRNAs to the sites of degradation. Affects replication of the positive-strand RNA virus BMV.
Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Component of the spindle pole body (SPB) required for the proper execution of spindle pole body (SPB) duplication.
Component of the SPC110 complex containing at least CMD1, SPC29, SPC42 and SCP110. Interacts with SPC110.
This protein has three functional calcium-binding sites.
Accessory factor for DNA replication. It plays a role in accurately duplicating the genome in vivo.
Calcium-dependent mitochondrial aspartate and glutamate carrier. Transport of glutamate in mitochondria is required for mitochondrial transamination reactions and ornithine synthesis. Plays also a role in malate-aspartate NADH shuttle, which is critical for growth on acetate and fatty acids.
Golgi membrane protein involved in vesicular trafficking and spindle migration.
The VTT domain was previously called the SNARE-assoc domain. As there is no evidence that this domain associates with SNARE proteins, it was renamed as VMP1, TMEM41, and TVP38 (VTT) domain.
Putative serine/threonine-protein kinase.
GTPase-activating protein for RHO1. Must be involved in the normal assembly or function or both of actin. Plays an essential role only at low temperatures.
Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Encoded from partially processed COB mRNA that terminates with the in-frame coding sequence of the second intron.
The variant in strain Capensis / YB4237 has additional DNA endonuclease (I-ScaI) activity promoting intron homing, which makes intron 2 of the COB gene highly mobile (PubMed:8670880). Introduction of 2 (Ala-355 and His-382) of its 4 variant residues into other strains is sufficient for acquisition of endonuclease activity of the corresponding mRNA maturases and for induction of intron mobility (PubMed:8670880).
This protein is responsible for splicing and maturation of cytochrome b mRNA. Specifically, it may be responsible for the splicing specificity of the second intron.
Binds to actin. Interacts with ABP1, GYL1, GYP5, PCL2 and YBR108W.
Component of a cytoskeletal structure that is required for the formation of endocytic vesicles at the plasma membrane level. Could be implicated in cytoskeletal reorganization in response to environmental stresses and could act in the budding site selection mechanism.
Phosphorylated redundantly by cyclin-dependent kinase PHO85 in association with PCL1,2-type cyclins or by MAP kinase FUS3. Phosphorylation inhibits interaction with complexes involved in actin cytoskeleton function.
Belongs to the aromatic-ring hydroxylase family. KMO subfamily.
Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid.
Deletion of BNA4 suppresses the toxicity of a mutant HD/HTT fragment.
This protein binds preferentially and cooperatively to single-stranded DNA (ssDNS). Involved in mitochondrial DNA replication. Stimulates PIF1 helicase activity.
Forms a stable complex with ATG17 and ATG31. Interacts directly with ATG31. The ATG17-ATG29-ATG31 complex interacts with the ATG1-ATG13 complex. Note=The interaction with the ATG1-ATG13 complex is induced by starvation.
Plays a role in autophagy. Functions at the preautophagosomal structure (PAS) in order to form normal autophagosomes under starvation conditions. Also plays a role in mitophagy and regulation of filamentous growth.
Required for growth on non-fermentable carbon sources.
Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Present with 6348 molecules/cell in log phase SD medium.
Present with 43100 molecules/cell in log phase SD medium.
Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment. Required for correct localization of SEC12, SEC71 and SEC63 in the endoplasmic reticulum.
Belongs to the EF-1-beta/EF-1-delta family.
Catalytic subunit of the guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) of the eukaryotic elongation factor 1 complex (eEF1). Stimulates the exchange of GDP for GTP on elongation factor 1A (eEF1A), probably by displacing GDP from the nucleotide binding pocket in eEF1A. The 30-fold higher concentration of GTP compared to GDP in cells favors the formation of eEF1A-GTP, which rapidly forms a ternary complex with aminoacyl-tRNA that in turn displaces eEF1B from the complex.
S-thiolated in response to oxidative stress, probably inhibiting the protein and causing a reduction in protein synthesis.
The C-terminus (pos. 119-205) exhibits guanine nucleotide exchange activity.
The eukaryotic elongation factor 1 complex (eEF1) is probably a heterohexamer. Two trimeric complexes, each composed of eEF1A (TEF1 or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or TEF4), are probably dimerized via the eF1Bgamma subunits. eEF1Balpha interacts directly with eEF1A. eEF1Balpha and eEF1Bgamma form the eEF1B subcomplex with the GEF activity.
Belongs to the cytochrome c oxidase subunit 6A family.
Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of 12 subunits. The complex is composed of a catalytic core of 3 subunits COX1, COX2 and COX3, encoded in the mitochondrial DNA, and 9 supernumerary subunits COX4, COX5A (or COX5B), COX6, COX7, COX8, COX9, COX12, COX13 and COX26, which are encoded in the nuclear genome (PubMed:7851399, PubMed:30598556, PubMed:30598554). The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a dimer of ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), resulting in 2 different assemblies (supercomplexes III(2)IV and III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556, PubMed:30598554). COX13 interacts with COX1 and COX3 on the intermembrane space (IMS) and COX4 on the matrix side (PubMed:30598554).
CTDK-I consists of three subunits, CTK1, CTK2 and CTK3 (also called alpha, beta and gamma). Interacts with CTK1. Heterodimerization with CTK3 is required to protect this subunit from degradation.
Cyclin subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. CTDK-I phosphorylates 'Ser-5' if the CTD substrate is not phosphorylated at 'Ser-5', but will phosphorylate 'Ser-2' of a CTD substrate if 'Ser-5' is already phosphorylated. CTDK-I is also more reactive toward substrates that are prephosphorylated at 'Ser-2' or 'Ser-5' compared with an unphosphorylated CTD substrate, therefore efficiently creating doubly phosphorylated CTD repeats. Involved in RNA polymerase II transcriptional elongation, and as part of the CTDK-I complex, pre-mRNA 3'-end processing and SET2 mediated H3K36 methylation. Together with CTK3, required for CTK1 CTD kinase activation. Required for DNA damage induced transcription. Involved in the adaptation to alternative carbon sources, including galactose, glycerol and ethanol, but not raffinose. Required for the integrity of the rDNA locus.
Phosphorylated. Ubiquitinated. Phosphorylation and ubiquitination lead to degradation in growth-related way by the ubiquitin-proteasome pathway. Neither phosphorylation nor degradation requires association with CTK1.
Binds to specific AU-rich elements (ARE) in the 3'-untranslated region of target mRNAs and promotes their degradation. In response to iron deficiency, promotes the decay of many mRNAs encoding proteins involved in iron-dependent pathways. Recruits the DHH1 helicase to the SDH4 mRNA and promotes SDH4 mRNA decay. Also destabilizes target mRNA by modulating 3'-end processing, creating extended transcripts that are prone for degradation.
Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes.
In the transfer reaction, the free carboxyl group of lipoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
Forms a NOT protein complex that comprises NOT1, NOT2, NOT3, NOT4 and NOT5. Subunit of the 1.0 MDa CCR4-NOT core complex that contains CCR4, CAF1, NOT1, NOT2, NOT3, NOT4, NOT5, CAF40 and CAF130. In the complex interacts with NOT1. The core complex probably is part of a less characterized 1.9 MDa CCR4-NOT complex.
DNA-binding protein that recognizes oligo(A).oligo(T) tracts (A.T DNA). Can bind to any 11 bp sequence in which 10 bases conform to an uninterrupted oligo(A).oligo(T) tract.
Present with 9970 molecules/cell in log phase SD medium.
Pyruvate dehydrogenase (E1) is a tetramer of 2 alpha and 2 beta subunits. Eukaryotic pyruvate dehydrogenase (PDH) complexes are organized as a core consisting of the oligomeric dihydrolipoamide acetyl-transferase (E2), around which are arranged multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and protein X (E3BP) bound by non-covalent bonds.
Putative guanine nucleotide-exchange factor (GEF) involved in the formation or budding of transport vesicles from the ER. Positive regulator of SAR1 probably through inhibition of the GTPase activation by SEC23.
Required for spore wall assembly and ascus formation.
Forms a complex with CSN12 that is recruited to transcribed genes and required for transcription elongation. May also be involved in pre-mRNA splicing.
Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM4 family.
Defects at both very early and later stages of endocytic transport in cells.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono- and dimethylates elongation factor 1-alpha (TEF1 and TEF2) at 'Lys-316'. May play a role in intracellular transport.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YPR158W-A ORF.
Present with 89800 molecules/cell in log phase SD medium.
By the zinc-responsive transcription factor ZAP1.
Binds DNA as monomer. The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14. Interacts with TFC8.
General transcription factor that functions at the core of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). eS19 is required for proper maturation of the small (40S) ribosomal subunit. Binds to 40S pre-ribosomal particles, probably required after association of NOC4 but before association of ENP1, TSR1 and RIO2 with 20/21S pre-rRNA (PubMed:16159874).
Disruption of a single RPS19 gene reduces cell growth; a double disruption is lethal. Depletion experiments show the proteins are required for correct maturation of precursor rRNA to generate the 18S small rRNA. A specific site between the 18S and 5.8S precursors (site A2 in ETS1) is not cleaved in disruption mutants. Partially assembled ribosomes are retained in the nucleolus rather than being exported to the cytoplasm. All effects are exacerbated in the double disruption. Increases association of NOC4 with 20/21S pre-rRNA, decreases association of ENP1, TSR1 and RIO2 with 20/21S pre-rRNA.
Required for proper maturation of the small (40S) ribosomal subunit. Binds to 40s pre-ribosomal particles, probably required after association of NOC4 but before association of ENP1, TSR1 and RIO2 with 20/21S pre-rRNA.
Involved in ribosome biogenesis. Seems to be required for restructuring nucleoplasmic 60S pre-ribosomal particles to make them competent for nuclear export.
Component of the adapter complexes which link clathrin to receptors in coated vesicles (PubMed:10564262). Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration (PubMed:10564262). AP19 is probably a subunit of the Golgi membrane adapter (PubMed:10564262). Component of the AP-1-related (AP-1R) complex, an adapter protein complex that mediates sorting of cargo SNARE SNC1 (PubMed:26658609). In contrast to the APM1-containing AP-1 complex, AP-1R is incapable of sorting CHS3 (PubMed:26658609).
Present with 6370 molecules/cell in log phase SD medium.
Ty1-DR3 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Involved in the control of meiosis. Represses the transcription of the IME1 gene thereby inhibiting cells from entering meiosis. But also activates the CLN2 gene thus promoting mitosis.
Interacts with PEP12, VTI1 and the SNC SNARE complex proteins.
t-SNARE which may play a role in determining the specificity of membrane fusion, protein transport and vesicle trafficking within the Golgi/endosomal and plasma membrane/endosomal systems.
Component of the eIF4F complex, which interacts with the mRNA cap structure and serves as an initial point of assembly for the translation apparatus. Stimulates translation by interaction with polyadenylate-binding protein PAB1, bringing the 5'- and 3'-ends of the mRNA in proximity. The formation of this circular mRNP structure appears to be critical for the synergistic effects of the cap and the poly(A) tail in facilitating translation initiation, recycling of ribosomes, and mRNA stability. TIF4631 is probably essential when TIF4632 is missing.
In the C-terminal section; belongs to the histidinol dehydrogenase family.
Present with 47500 molecules/cell in log phase SD medium.
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
The eukaryotic translation initiation factor 3 (eIF-3) core complex is composed of TIF32, PRT1, NIP1, TIF34 and TIF35. A subcomplex of TIF32, NIP1 and PRT1 mediates the interaction with eIF-1, TIF5/eIF-5 and HCR1. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a multifactor complex (MFC) that may bind to the 40S ribosome.
Promotes cell fusion during zygote formation.
Forms a chaperone-bound H2A.Z-H2B complex that acts as a source for SWR1 complex-dependent H2A to H2A.Z histone replacement in chromatin.
Forms a heterotrimer with H2A.Z-H2B, stabilizing the association of the histone dimer. Also, with a lower affinity, forms a heterotrimer with H2A-H2B.
Open reading frame that exhibits genomic organization compatible with a translational readthrough-dependent mode of expression. The sequence can give a readthrough frequency of 9% when cloned in a plasmid with reporter genes. When the initial stop codon is bypassed, translation will go on to the second stop codon 321 bp downstream.
This protein has no orthologs in any species other than the S.cerevisiae lineage. It may be the result of de novo origination of a protein-coding gene.
Component of the heterotetrameric kinetochore subcomplex COMA, which consists of AME1, CTF19, MCM21 and OKP1 (PubMed:10323865, PubMed:14633972). The COMA subcomplex is part of a larger constitutive centromere-associated network (CCAN) (also known as central kinetochore CTF19 complex in yeast), which is composed of at least AME1, CHL4, CNN1, CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1 (PubMed:12408861, PubMed:22561346). COMA binds the centromeric nucleosome-binding protein MIF2, and to the outer kinetochore MIND subcomplex (By similarity).
Transferable epigenetic modifier which forms a prion responsible for the non-Mendelian trait [PIN+]. The native function of the soluble protein is unknown.
[PIN+], also known as [RNQ+], is the prion form of RNQ1 (PubMed:10678178). [PIN+] is the result of a conformational change of the cellular RNQ1 protein that becomes self-propagating and infectious. This conformational change generates a form of RNQ1 that assembles into amyloid fibrils (PubMed:17097676). [PIN+] promotes de novo [PSI+] formation upon SUP35 overproduction (cross-seeding) (PubMed:11511345). [PIN+] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [PIN+] propagation (PubMed:10678178).
Interacts with FZO1 through its cytoplasmic domain and with MGM1 through its mitochondrial intermembrane space domain.
Required for mitochondrial fusion as well as normal mitochondrial morphology by bridging the essential interaction between FZO1 and MGM1. May coordinate fusion of inner and outer membranes during mitochondrial fusion.
Constitutively active kinase, specifically and sequentially phosphorylates serine/arginine (SR)-type shuttling mRNA binding proteins in their RS dipeptide repeats.
Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
Present with 133000 molecules/cell in log phase SD medium.
Binds DNA with a high specificity in complex with an MCM1 dimer. Interacts with STE12.
Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Silenced copy of ALPHA1 at HML.
Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Transcriptional coactivator that, in alpha-cells, binds cooperatively with MCM1 and STE12 to a DNA sequence termed the QP' element, to activate the transcription of alpha-specific genes.
Repressed in a/alpha diploid cells by A1/ALPHA2.
May play a role in mediating the heat shock response of some HSP70 genes. It is required for optimal growth of yeast cells at both low and high temperature.
Part of a larger complex that includes HSP70, HSP90, and immunophilins.
Abolishes CHS3 localization to the bud neck and plasma membrane, with increased protein localization to intracellular vesicles.
Component of the CHS5/6 complex which mediates export of specific cargo proteins, including chitin synthase CHS3. Also involved in targeting FUS1 to sites of polarized growth.
Forms an active dehydrodolichyl diphosphate synthase complex with either SRT1 or RER2.
With SRT1 or RER2, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER).
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YBL005W-A ORF.
Belongs to the cyclophilin-type PPIase family. CWC27 subfamily.
PPIases accelerate the folding of proteins. Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in pre-mRNA splicing (PubMed:11884590).
Lack of GOT1 is lethal in a strain lacking SFT2.
Nonessential protein required for the fusion of ER-derived transport vesicles with the Golgi complex. Can be replaced by SFT2.
Function prior to stable branch point recognition by the U1 snRNP particle to facilitate or stabilize the U1 snRNP/5'-splice site interaction. Has a direct role in the assembly or function of a catalytically active spliceosome.
Present with 4460 molecules/cell in log phase SD medium.
Growth rate is increased in lithium chloride (PubMed:33256608). Calcofluor White sensitivity is background dependent (PubMed:9335584, PubMed:33256608).
Inactive carboxypeptidase that may play a role in cell wall organization and biogenesis.
Lacks the conserved Glu residue in position 391 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates.
Catalyzes the conversion of uridine into UMP and cytidine into CMP in the pyrimidine salvage pathway.
Belongs to the glycosyltransferase 34 family.
Required for synthesis of full-length mannan chains.
May be required for cell cycle progression.
Belongs to the Mediator complex subunit 15 family.
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. It has an important role in the negative regulation of Ty transcription.
Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules (PubMed:17192271). The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16 (PubMed:17192271). The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins (PubMed:17192271). GAL11/MED15 interacts with the activator GAL4; the interaction is direct (PubMed:11478912). GAL11/MED15 interacts (via multiple regions) with the activator GCN4; the interaction is direct (PubMed:19940160).
Sensitive to amino acid starvation (PubMed:19940160). Normal GCN4 protein level during amino acid starvation (PubMed:19940160).
Belongs to the phosphoglycerate mutase family. SHB17 subfamily.
Expression is correlated with levels of ribosomal proteins, thus periodic SHB17 expression coincides with the peak demand for ribose phosphate that occurs during ribosome synthesis.
Sedoheptulose 1,7-bisphosphatase involved in riboneogenesis. Dephosphorylates sedoheptulose 1,7-bisphosphate (SBP), which is converted via the non-oxidative pentose phosphate pathway to ribose-5-phosphate. Has a fructose 1,6-bisphosphatase activity in vitro, but this is probably not biologically relevant, since deletion does not affect fructose 1,6-biphosphate (FBP) levels.
Leads to altered expression of 79 genes, including genes related to transcription, genes involving cell rescue and defense, and genes involved in cell cycle and DNA processing.
Probable transcription factor involved in the regulation of the transcription of genes involved in cell rescue and defense, as well as cell cycle and DNA processing.
Present with 443000 molecules/cell in log phase SD medium.
Belongs to the eukaryotic/archaeal PrmC-related family.
Heterodimer of MTQ2-TRM112. MTQ2 is the catalytic subunit carrying the catalytic and the S-adenosyl L-methionine binding sites.
Methylates eRF1 on 'Gln-182' using S-adenosyl L-methionine as methyl donor. eRF1 needs to be complexed to eRF3 in its GTP-bound form to be efficiently methylated.
Binds to the BEM1 protein. Involved in bud formation.
RNA-binding protein involved in post-transcriptional regulation. Negatively regulates expression of COX17 by binding to the 3'-UTR of COX17 mRNA. Promotes decay of COX17 mRNA by enhancing its rate of deadenylation and subsequent turnover. Predominantly binds to mRNAs encoding membrane-associated proteins with roles in transmembrane transport and vesicular trafficking.
Component of the cell wall. May play a role in the formation of a tightly packed outer mannan layer, which protects the inner glucan.
Extensively O-glycosylated; glycans consist probably of single mannose residues. N-glycosylated.
By stress such as heat shock or increased salt concentration. Up-regulated by all stress conditions tested. Also expressed in unstressed cells.
Forms oligomeric complexes. Interacts with itself.
Required for processing of the 20S pre-rRNA at site D to generate mature 18S rRNA.
Involved in glucose repression of the SUC, GAL and MAL genes as well as of the CAT8 gene. Binds to two sites in the upstream region of SUC2.
Positive effector of glycogen accumulation. May be involved in nutrient-sensing.
Present with 77000 molecules/cell in log phase SD medium.
Associates with pre-60S ribosomal particles; released from the pre-60S particle very early in the cytoplasm.
Belongs to the ZNF593/BUD20 C2H2-type zinc-finger protein family.
Involved in pre-60S ribosomal particles maturation by promoting the nuclear export of the 60S ribosome (PubMed:23045392). Involved in positioning the proximal bud pole signal (PubMed:11452010).
Present with 5630 molecules/cell in log phase SD medium.
Plays a role in the regulation of membrane potential. Could mediate a proton leak.
DEAD-box RNA helicase-like protein required for pre-18S rRNA processing, specifically at sites A0, A1, and A2.
Interacts with snoRNA U3. Interacts with MPP10, NOP19, RRP9, UTP8 and UTP18. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Interacts with the ANK repeats of SWI6. The interaction with SWI6 is required for function. Interacts with SIN3.
Involved in the regulation and timing of MBF-dependent transcription in late G1 of the cell cycle.
Phosphorylated by CDC28 in a cell cycle-dependent manner, inhibiting the interaction with SWI6.
Interacts directly with RSC8. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin. Component of a fungal-specific module (HTL1-LDB7-NPL6-RSC3-RSC30) within the RSC complex.
Required for cell cycle progression through G2/M transition at temperatures higher than 33 degrees Celsius. Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. When associated with the RSC complex, may act coordinately with PKC1 to regulate G2/M transition. Together with LDB7, NPL6, RSC3, RSC30 components, defines a fungal-specific module within the RSC complex that plays a role in many cellular functions including the maintenance of cell wall integrity.
Probable tRNA acetyltransferase required for the formation of the modified nucleoside N(4)-acetylcytidine in serine and leucine tRNAs. Binds RNA.
Component of the ESCRT-0 complex composed of HSE1 and VPS27 (PubMed:12055639). Interacts with the ESCRT-I subunit VPS23, the UBP7 deubiquitinase and the E3 ligase RSP5 (PubMed:17079730, PubMed:15086794). May form a complex composed of VPS27, HSE1 and DOA1 (PubMed:18508771). Interacts (via SH3 domain) with DOA1 (PubMed:18508771).
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane.
Serine/threonine protein kinase involved in a signal transduction pathway that plays a role in yeast cell morphogenesis and cell growth. This pathway seems to start by SMP3; then involves the kinase PKC1 that may act on the BCK1 kinase that then phosphorylates MKK1 and MKK2 which themselves phosphorylate the MPK1 kinase.
Requires a bound zinc ion for normal folding and solubility.
Ap4A phosphorylase catalyzes the phosphorolytic degradation of bis(5'-adenosyl) tetraphosphate (Ap4A) into ADP and ATP. Can also use other Np4N' nucleotides (where N and N' stand for A,C,G or U) as substrates with equal efficiency. Cannot catalyze the reverse reaction. Additionally, this enzyme can also catalyze the phosphorolytic degradation of adenosine 5'-phosphosulfate (AMPS) into ADP and sulfate, the reversible exchange reaction between inorganic phosphate and the beta-phosphate of a nucleoside diphosphate (NDP), and the synthesis of Ap4A from AMPS plus ATP.
Belongs to the polyadenylate-binding protein type-1 family.
Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation. In the nucleus, interacts with the nuclear cleavage factor IA (CFIA), which is required for both mRNA cleavage and polyadenylation. Is also required for efficient mRNA export to the cytoplasm. Acts in concert with a poly(A)-specific nuclease (PAN) to affect poly(A) tail shortening, which may occur concomitantly with either nucleocytoplasmic mRNA transport or translational initiation. Regulates PAN activity via interaction with the stimulator PAN3 or the inhibitor PBP1. In the cytoplasm, affects both translation and mRNA decay. Stimulates translation by interaction with translation initiation factor eIF4G, a subunit of the cap-binding complex eIF4F, bringing the 5'- and 3'-ends of the mRNA in proximity. The formation of this circular mRNP structure appears to be critical for the synergistic effects of the cap and the poly(A) tail in facilitating translation initiation, recycling of ribosomes, and mRNA stability. Also regulates translation termination by recruiting eukaryotic release factor 3 (eRF3). Interaction with eRF3 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening, probably mediated by PAN. Loss of PAB1 from the mRNP after deadenylation triggers mRNA degradation. Inhibits the major cytoplasmic mRNA deadenylase CCR4-NOT complex. Is also associated peripherally with COPI vesicles through its interaction with ARF1, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA.
Binds to poly(A) mRNA to form a periodic structure with a packing density of one molecule per 25 adenylate residues. Interacts with the nuclear export factor CRM1 and with the importin SXM1. Interacts with RNA15, a component of the cleavage factor IA (CFIA) complex. Interacts with translation initiation factor eIF4G (TIF4631 or TIF4632) and release factor eRF3 (SUP35). Interacts with the PAB-dependent poly(A)-nuclease (PAN) complex regulatory subunit PAN3. Interacts with ARF1, DCP1, PBP1, the Hsp70 chaperone SSA1, and TPA1. Interacts with PAT1 in an RNA-dependent manner.
Present with 198000 molecules/cell in log phase SD medium.
RNA recognition motifs (RRMs) 1 and 2 bind specifically to the poly(A) tail, whereas RRMs 3 and 4 bind non-specifically to polypyrimidine RNAs and may serve to bind to a different part of the messenger or to other RNAs. RRM 2 also mediates interaction with eIF-4G.
Involved in the biosynthesis of (1->6)-beta-D-glucan polymers of the cell wall. Required for viability. Involved in maintaining chromosome stability.
Belongs to the class-I DAHP synthase family.
Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
Involved in secretion. Component of the secretory vesicle docking complex.
Present with 3630 molecules/cell in log phase SD medium.
In contrast to Ty3-1 (Ty3-G), Ty3-2 (Ty3-I) is a transpositionally inactive element. The Ty3-2 ORF is truncated by the deletion of a single nucleotide, which causes a frameshift mutation when compared with Ty3-1.
Nucleocapsid protein p11 (NC) forms the nucleocore that coats the retro-elements dimeric RNA. Binds these RNAs through its zinc fingers (By similarity). Promotes primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty3 RNA and initiation of reverse transcription (By similarity).
Produced by +1 ribosomal frameshifting between codon Ala-285 and Val-286 of the YIL082W ORF.
Positive regulator of multiple nitrogen catabolic genes.
Involved in non-homologous end joining (NHEJ). Facilitates the transport of LIF1 into the nucleus, where it can interact with DNA ligase DNL4 to repair double-strand breaks (DSB). Mediates mating-type regulation of NHEJ. Prevents chromosome circularisation by NHEJ in absence of telomerase.
Interacts with the small Tim proteins TIM8, TIM9, TIM10, TIM12, and TIM13.
Required for the assembly or recycling of the small Tim proteins in the mitochondrial intermembrane, thereby participating in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Probably acts by facilitating the formation of disulfide bonds in small Tim proteins.
Interacts with STH1 and SWI3. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin. Probable additional component of the SWI/SNF global transcription activator complex. The 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29.
Probable component of the chromatin structure-remodeling complex (RSC) which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. Probable component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. DIS3 has both 3'-5' exonuclease and endonuclease activities. The exonuclease activity of DIS3 is down-regulated upon association with Exo-9 possibly involving a conformational change in the catalytic domain and threading of the RNA substrate through the complex central channel. Structured substrates can be degraded if they have a 3' single-stranded extension sufficiently long (such as 35 nt poly(A)) to span the proposed complex inner RNA-binding path and to reach the exonuclease site provided by DIS3. Plays a role in mitotic control.
Component of the RNA exosome complex. The catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits DIS3 and RRP6 in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits and peripheral S1 domain-containing components CSL4, RRP4 and RRP40 located on the top of the ring structure. DIS3 associates at the respective bottom side with Exo-9. Interacts with GSP1.
It was originally thought that there are multiple subunits in the exosome that have exonuclease activity but it was later shown (PubMed:17173052 and PubMed:17174896) that only this DIS3/RRP44 subunit of the exosome core has this activity.
Mn(2+) doesn't support the hydrolytic activity. Activity is KCl or NaCl dependent and activity is slightly increased in the presence of reducing agents such as DTT or beta-mercaptoethanol and doesn't vary notably between pH 6.8 and 8.8.
Involved in aerobic respiration where it is required for assembly of respiratory chain enzyme complexes III and IV. Also has a role in mitochondrial gene expression. May be part of a mitochondrial membrane-associated RNA-shuttling system, delivering NAM1-associated transcripts to the translation machinery.
Glycerol-1-phosphate phosphohydrolase involved in glycerol biosynthesis. Plays a role in osmoadaptation.
Essential component of both TORC1 and TORC2. TORC1 regulates multiple cellular processes to control cell growth in response to environmental signals. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls ribosome biogenesis via control of rRNA, ribosomal protein and tRNA gene expression, and rRNA processing. TORC1 positively controls protein biosynthesis by regulation of mRNA stability, translation initiation factor activity, and high-affinity amino acid permeases that serve to provide amino acids for use by the translation machinery. TORC1 also promotes growth by sequestering a number of nutrient and general stress-responsive transcription factors in the cytoplasm. TORC1 negatively controls macroautophagy, a process to recycle surplus cytoplasmic mass under nutrient starvation conditions. LST8 is involved in the negative regulation of transcription factors GLN3 and RTG1-RTG3, limiting the synthesis of alpha-ketoglutarate, glutamate and glutamine. LST8 is required for targeting of amino acid permeases (AAPs) to the plasma membrane. TORC2 regulates cell cycle-dependent polarization of the actin-cytoskeleton, cell wall integrity, and receptor endocytosis. TORC2 controls polarity of the actin cytoskeleton, which is required for orienting the secretory pathway toward discrete growth sites, via the RHO1/PKC1/MAPK cell integrity pathway. LST8 is involved in maintenance of cell wall integrity. LST8 modulates TOR2 kinase activity.
The target of rapamycin complex 1 (TORC1) is composed of at least KOG1, LST8, TCO89 and either TOR1 (TORC1-A) or TOR2 (TORC1-B) (PubMed:12408816, PubMed:12631735, PubMed:12719473). TORC1 binds to and is inhibited by FKBP-rapamycin (PubMed:12408816). Interacts with PIB2; following activation of PIB2 by glutamine or cysteine and as part of the TORC1 complex (PubMed:29698392). The target of rapamycin complex 2 (TORC2) is composed of at least AVO1, AVO2, BIT61, LST8, TOR2 and TSC11 (PubMed:12408816, PubMed:12631735, PubMed:12719473). TORC2 likely forms a homodimer (PubMed:16002396). Contrary to TORC1, TORC2 does not bind to and is not sensitive to FKBP-rapamycin (PubMed:12408816). LST8 binds to the C-terminal kinase domain in TOR2 (PubMed:16002396).
Required for mitochondrial morphology. With UPS1 and UPS2, controls phospholipid metabolism in the mitochondrial intermembrane space.
Belongs to the DNA polymerase alpha subunit B family.
DNA polymerase alpha:primase is a four subunit enzyme complex, which is assembled throughout the cell cycle, and consists of the two DNA polymerase subunits A POL1 and B POL12, and the DNA primase large PRI2 and small PRI1 subunits (PubMed:3061469). Subunit B POL12 binds to subunit A POL1 (PubMed:19494830).
Non-catalytic component of DNA polymerase alpha, which in a complex with DNA primase (DNA polymerase alpha:primase) constitutes a replicative polymerase. POL12 may play an essential role at the early stage of chromosomal DNA replication by coupling DNA polymerase alpha to the cellular replication machinery (By similarity). Interacts with MCM10.
Belongs to the FNT transporter (TC 2.A.44) family.
Involved in sporulation. Required for the full activation of the early meiotic inducer IME1.
Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily.
Impairs cytosolic iron-sulfur (Fe-S) cluster assembly and decreases cytosolic tRNA thiolation.
Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins (PubMed:10406803, PubMed:31040179, PubMed:25006243). Hydrolyzes ATP (PubMed:25006243, PubMed:24604199). Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound (PubMed:24604199, PubMed:25006243, PubMed:31040179).
Component of the TFIIIC complex composed of TFC1, TFC3, TFC4, TFC6, TFC7 and TFC8. The subunits are organized in two globular domains, tauA and tauB, connected by a proteolysis-sensitive and flexible linker.
TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and similar genes.
Belongs to the methyltransferase superfamily. Fibrillarin family.
Component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles that contain SNU13, NOP1, SIK1/NOP56 and NOP58, plus a guide RNA. Interacts with snoRNA U3. Interacts with MPP10, NOP58, SIK1 and SOF1. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.
S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA (PubMed:2686980, PubMed:1825809, PubMed:12215523). Site specificity is provided by a guide RNA that base pairs with the substrate (PubMed:2686980, PubMed:1825809). Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA (PubMed:2686980, PubMed:1825809). Involved in the biogenesis of the 18S rRNA (PubMed:2686980, PubMed:1825809). Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ105me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (PubMed:24352239).
Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis. Required for methionine synthesis and maintenance of intact mitochondrial DNA. Involved in telomere maintenance.
Methionine auxotroph. Undetectable levels of folylpolyglutamate synthase activity. Increased rate of loss of mitochondrial DNA. Respiration-deficient. MET7 and FOL3 double mutant cells are not viable even in the presence of methionine and folinic acid. MET7, FOL3 and TUP1 triple disruption mutant is able to germinate on YPGA medium containing thymidylate and to grow although poorly on synthetic medium containing methionine, adenine and thymidylate. Adenine and thymidine auxotroph when grown in the presence of sulfanilamide. Becomes petite under normal growth conditions but can be maintained with a grande phenotype if the strain is TUP1 and all media are supplemented with dTMP. MET7 and GLY1 double mutant is auxotrophic for glycine when grown on glucose but prototrophic when grown on glycerol. MET7 and SER1 double mutant cannot use glycine to suppress serine auxotrophy. MET7 and SHM2 double mutant is nonviable.
Belongs to the fungal cytochrome c oxidase subunit 26 family.
Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of 12 subunits. The complex is composed of a catalytic core of 3 subunits COX1, COX2 and COX3, encoded in the mitochondrial DNA, and 9 supernumerary subunits COX4, COX5A (or COX5B), COX6, COX7, COX8, COX9, COX12, COX13 and COX26, which are encoded in the nuclear genome. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a dimer of ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), resulting in 2 different assemblies (supercomplexes III(2)IV and III(2)IV(2)).
Homodimer (PubMed:22262864). Component of the HRD1 ubiquitin ligase complex which contains the E3 ligase HRD1, its cofactors HRD3, USA1 and DER1, substrate recruiting factor YOS9 and CDC48-binding protein UBX2 (PubMed:16873065, PubMed:16873066). Within the complex, interacts (via N-terminus) with HRD3 (PubMed:22262864). In ERAD-L, HRD3 and YOS9 jointly bind misfolded glycoproteins in the endoplasmic reticulum (ER) lumen (PubMed:32327568). Movement of ERAD-L substrates through the ER membrane is facilitated by HRD1 and DER1 which have lateral gates facing each other and which distort the membrane region between the lateral gates, making it much thinner than a normal phospholipid bilayer (PubMed:32327568). Substrates insert into the membrane as a hairpin loop with one strand interacting with DER1 and the other with HRD1 (PubMed:32327568). The HRD1 complex interacts with the heterotrimeric CDC48-NPL4-UFD1 ATPase complex which is recruited by UBX2 via its interaction with CDC48 and which moves ubiquitinated substrates to the cytosol for targeting to the proteasome (PubMed:16873065, PubMed:16873066). Interacts with KAR2 and EMP47 (PubMed:16873065). Interacts with misfolded ER lumenal proteins like PCR1 (PubMed:16168370, PubMed:16168371, PubMed:16168372). Interacts with the GPI-anchored proteins GAS1 and MKC7 (PubMed:12077121).
Interaction of substrate with HRD1 is reduced; in YOS9 and USA1 double mutants this interaction is completely abolished. Interaction of substrate (either glycosylated or non-glycosylated) with HRD3 is not affected.
Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. The recognition of targets is N-glycan specific. Functions in recruiting misfolded protein substrates in conjunction with HRD3 (PubMed:32327568).
The MRH (mannose 6-phosphate receptor homology) domain is required for the ERAD-L activity.
Produced by +1 ribosomal frameshifting between codon Leu-363 and Gly-364 of the YJL114W ORF.
Component of the TOM (translocase of outer membrane) receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. TOM5 is involved in insertion of preproteins into the TOM40 translocation pore.
Involved in the final stage of protein secretion.
Deletion causes a vacuolar protein sorting defect.
Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration. May be involved in copper trafficking and distribution to mitochondrial COX and SOD1.
Present with 31600 molecules/cell in log phase SD medium.
Component of the ISW1B complex, which at least consists of ISW1, IOC2 and IOC4.
Functions as component of the ISW1B complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW1B complex acts within coding regions to control the amount of RNA polymerase II released into productive elongation and to coordinate elongation with termination and pre-mRNA processing.
Belongs to the proteasome subunit S5A family.
The 26S proteasome is composed of a core protease, known as the 20S proteasome, capped at one or both ends by the 19S regulatory complex (RC) (PubMed:12504901, PubMed:8887631, PubMed:22927375). The RC is composed of at least 18 different subunits in two subcomplexes, the base and the lid, which form the portions proximal and distal to the 20S proteolytic core, respectively (PubMed:22927375).
Ubiquitinated, leading to its degradation (PubMed:17190603). Ubiquitination is promoted by HUL5 (PubMed:17190603).
TFIIA is a component of the transcription machinery of RNA polymerase II and implicated in the regulation of basal transcription. Interacts with TBP (the TATA-binding protein).
TFIIA is a heterodimer composed of the large TOA1 and a small TOA2 subunits. Interacts with KAP122.
Beta subunit of a guanine nucleotide-binding protein (G protein). G proteins are involved as modulators or transducers in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Involved in the determination of the cAMP level according to nutritional conditions, most probably as a regulator of cAMP phosphodiesterase. Required for the control of pseudohyphal and haploid invasive growth.
G proteins are composed of 3 units, alpha, beta and gamma. GPB1 interacts with the alpha subunit GPA2.
Catalyzes the oxidation of D-arabinose, L-xylose, L-fucose and L-galactose in the presence of NADP(+).
Heterodimer of a heavy chain and a light chain.
Present with 30200 molecules/cell in log phase SD medium.
Expression decreases in response to ergosterol perturbation or upon entry into stationary phase.
Conversion of folates to polyglutamate derivatives.
May be involved in positioning the distal bud pole signal.
May be a component of the ubiquitination pathway.
Present with 7721 molecules/cell in log phase SD medium.
Serine/threonine protein kinase involved in a signal transduction pathway that plays a role in yeast cell morphogenesis and cell growth. This pathway seems to start by SMP3; then involve the kinase PKC1 that may act on this kinase. BCK1 probably phosphorylates MKK1 and MKK2 which themselves phosphorylate the MPK1 kinase.
Transporter protein required for adaptation to high stress imposed by low-chain organic acids, in particular by acetic acid, and for resistance to azoles, especially to ketoconazole and fluconazole.
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Present with 121000 molecules/cell in log phase SD medium.
There are three genes for G3PDH in yeast.
Cells deleted for both ISU1 and ISU2 have decreased activity of several respiratory enzymes that contain Fe-S clusters. As a result, cells grow poorly on carbon sources requiring respiration and also accumulate abnormally high levels of iron in their mitochondria. Knockdown of ISU1 in ISU2 knockout cells decreases cytosolic tRNA thiolation, and increases association between SSQ1 and GRX5 (PubMed:31040179, PubMed:23615440).
Component of the core Fe-S cluster (ISC) assembly machinery. Interacts with frataxin (By similarity). Interacts with the mitochondrial co-chaperones JAC1 and SSQ1 (By similarity). Interacts with NFS1 (By similarity). Interacts with ferredoxin YAH1; interacts with the reduced form (By similarity).
Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins. First, a [2Fe-2S] cluster is transiently assembled on the scaffold proteins ISU1 and ISU2. In a second step, the cluster is released from ISU1/ISU2, transferred to glutaredoxin GRX5, followed by the formation of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on ISU1/ISU2 depends on the function of the cysteine desulfurase complex NFS1-ISD11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin (YFH1) as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase ARH1 and ferredoxin YAH1, which receive their electrons from NADH. Fe-S cluster release from ISU1/ISU2 is achieved by interaction with the Hsp70 chaperone SSQ1, assisted by the DnaJ-like co-chaperone JAC1 and the nucleotide exchange factor MGE1 (PubMed:23615440). ISU1 is the major isoform in yeast, while ISU2 is not detectable in cells grown to stationary phase (By similarity). ISU2 is the minor isoform in yeast and is not detectable in cells grown to stationary phase (PubMed:10588895). Also involved in production of a sulfur precursor required for thiolation of cytoplasmic tRNAs (PubMed:31040179).
Regulatory subunit (R2) of the histone H2A phosphatase complex (HTP-C) consisting of PPH3, PSY2 and PSY4. Interacts with SPT4 and SPT5.
Regulatory subunit of the histone H2A phosphatase complex, which dephosphorylates H2AS128ph (gamma-H2A) that has been displaced from sites of DNA lesions in the double-stranded DNA break repair process. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint.
Non-catalytic component of the proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.
Present with 2680 molecules/cell in log phase SD medium.
Required for translation of the mitochondrial OLI1 transcript coding for the mitochondrial ATP synthase subunit 9.
Component of the retromer complex which consists of VPS29, VPS26, VPS35, VPS5 and VPS17. Component of a retromer subcomplex consisting of VPSD5 and VPS17.
Plays a role in vesicular protein sorting. Required for retention of late Golgi membrane proteins and vacuolar biogenesis. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. The VPS5-VPS17 subcomplex may assemble onto the membrane to promote vesicle formation.
Interacts strongly with QSR1. Part of an oligomeric protein complex that is loosely associated with ribosomes.
May be involved in the late step of 60S ribosomal subunit assembly or modification in the cytoplasm.
Accepts the ubiquitin-like protein NEDD8/RUB1 from the UBA3-ULA1 E1 complex and catalyzes its covalent attachment to other proteins. The major substrate is CDC53/Cullin.
Belongs to the ubiquitin-conjugating enzyme family. UBC12 subfamily.
The acetylation of Met-1 is cotranslational, and not regulatory. The N-acetylmethionine increases affinity for DCUN1D1 by about 2 orders of magnitude and is crucial for NEDD8 transfer to cullins.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB9 is part of the upper jaw surrounding the central large cleft and thought to grab the incoming DNA template. Involved in the regulation of transcription elongation. Involved in DNA repair of damage in the transcribed strand. Mediates a transcription-coupled repair (TCR) subpathway of nucleotide excision repair (NER).
Catalyzes the trans-addition of the 3 molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. Required for the membrane attachment of YPT1 and SEC4. May be involved in vesicle trafficking and protein sorting.
Component of the oligosaccharyltransferase (OST) complex, which appears to exist in two assemblies comprising OST1, OST2, OST4, OST5, STT3, SWP1, WPB1, and either OST3 or OST6 (PubMed:8175708, PubMed:16297388, PubMed:16096345, PubMed:15831493, PubMed:15886282, PubMed:9405463, PubMed:29301962). OST assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains OST1 and OST5, subcomplex 2 contains STT3, OST3, and OST4, and subcomplex 3 contains OST2, WBP1, and SWP1 (PubMed:29301962). Interacts with SEC61, SBH1 and SSS1 (PubMed:15831493).
Belongs to the DDOST 48 kDa subunit family.
Present with 14900 molecules/cell in log phase SD medium.
The cytoplasmic C-terminal domain contains a functional dilysine-retrieval motif, which is involved in the retrograde Golgi-to-ER transport of the protein.
Function in mitochondrial RNA splicing in the excision of mitochondrial group I introns aI5 beta from COX1 and bI3 from COB transcripts and thus would be involved in obtaining the correct structure of the intron, to allow the RNA catalyzed reactions to occur.
Homodimer. Forms a ribonucleoprotein complex composed of maturase bI3 and 2 dimers of MRS1 that assemble around the bI3 RNA.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM11 methyltransferase family.
Catalytic subunit of an S-adenosyl-L-methionine-dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs.
Autophosphorylated and phosphorylated by the CLN2-CDC28 complex in a cell cycle dependent manner.
Interacts with BEM1, CDC42, CLN2, STE4 and the 14-3-3 proteins BMH1 and BMH2.
MAP4K component of the MAPK pathway required for the mating pheromone response, haploid invasive growth and diploid pseudohyphal development. Links the pheromone response G-protein beta gamma subunits to downstream signaling components. Needed for mating in haploid cells, induction of a mating-specific gene FUS1, induction of mating-specific morphologies, and pheromone-induced proliferation arrest. Required for the regulation of the actin polarization and bud emergence during cell cycle in G1. Involved in the high osmolarity glycerol (HOG) response. Phosphorylates 'Thr-307' and 'Ser-302' or 'Ser-306' of STE11 and 'Ser-357' of MYO3. Phosphorylates histone H2B to form H2BS10ph during meiosis and H(2)O(2)-induced apoptosis. Its interaction with CDC42 is required for both invasive growth and the formation of pseudohyphae. Its interaction with STE4 is required for the pheromone signaling.
The CRIB domain is required for the association with CDC42.
Involved in extracellular amino acid uptake. Required for the trafficking of the GAP1 nitrogen-regulated general amino acid permease from the Golgi to the plasma membrane.
Activated by hyperosmotic shock after mannitol treatment.
A dominant mutation in CLN2 gene (CLN2-1), advances the G1- to S-phase transition in cycling cells and impairs the ability of cells to arrest in G1 phase in response to external signals.
Involved in splicing of intron aI5-beta of the mitochondrial COX1 transcript.
To baculovirus occlusion-derived virus envelope protein E27 (ODV-E27).
Component of the linker nucleocytoskeleton and cytoskeleton (LINC) complex composed of at least MPS2, MPS3 and CSM4 (PubMed:32967926). Interacts with HTZ1 (PubMed:21518795). Interacts with REC8 (PubMed:30417519). Interacts with CSM4; ECO1, EST1, JEM1, CDC31, NDJ1, MPS2 and SIR4 (PubMed:12486115, PubMed:12493774, PubMed:15355977, PubMed:16923827, PubMed:17245108, PubMed:17495028, PubMed:18039933, PubMed:18585352).
Component of the linker nucleocytoskeleton and cytoskeleton (LINC) complex that regulates telomere movement and meiotic recombination during meiosis (PubMed:17245108, PubMed:18585352, PubMed:32967926). Connects the spindle pole body with the nuclear envelope through its interaction with MPS2 and mediates meiotic bouquet formation and rapid chromosome movements in meiotic prophase (PubMed:16923827, PubMed:17495028, PubMed:22017544). Functions as an integral membrane anchor for telomeres and is a nuclear receptor for the SIR4 pathway of telomere tethering and gene inactivation (PubMed:18039933, PubMed:19390087). Essential for nuclear division and fusion and required for the first step of spindle pole body duplication in G1 (PubMed:12486115, PubMed:12493774). Functions in sister chromatid cohesion establishment (PubMed:15355977, PubMed:16682351). Recruits double-strand breaks (DSBs) to the nuclear periphery for chromosome healing (PubMed:19390086, PubMed:19217407, PubMed:20016273).
Phosphorylation at Ser-189 and Ser-190 by CDC7 and CDC28 during meiosis regulates of the localization on nuclear envelope for meiotic chromosome motion and nuclear envelope remodeling.
The SUN domain is involved in the binding to MPS2 and is important for modulating chromosome motion events that act in meiotic chromosome juxtaposition and by extension, promoting proper morphogenesis of the synaptonemal complex.
Component of the SRB8-11 complex which consists of SRB8, SSN2/SRB9, SSN3/SRB10 and SSN8/SRB11. The SRB8-11 complex associates with the Mediator complex. The SSN3/SRB10 and SSN8/SRB11 kinase-cyclin pair also associate with the RNA polymerase II holoenzyme. Interacts with ASK10.
Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The SRB8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II RPB1 at serines 2 and 5. The SSN3/SRB10 and SSN8/SRB11 kinase-cyclin pair may also positively and negatively regulate numerous transcriptional activators in response to changes in nutritional and physiological conditions.
Involved in pre-mRNA splicing. Important for bud site selection.
Catalyzes the formation of CDP-diacylglycerol (CDP-DAG) from phosphatidic acid (PA) in the mitochondrial inner membrane. Required for the biosynthesis of the dimeric phospholipid cardiolipin, which stabilizes supercomplexes of the mitochondrial respiratory chain in the mitochondrial inner membrane.
Deficient in cardiolipin. Blocked in the import of presequence-containing proteins as well as of non-cleavable carrier proteins into mitochondria.
Magnesium. Also active with cobalt or copper.
Was initially identified as protein involved in the translocation of transit peptide-containing proteins across the mitochondrial inner membrane by its role in maintaining the integrity and stability of the inner membrane translocase TIM23 complex (PubMed:16943180, PubMed:16790493). It has later been shown that this phenotype can be attributed to the pleiotropic effects of mitochondria lacking cardiolipin (PubMed:19114592).
Belongs to the CWC complex (or CEF1-associated complex), a spliceosome subcomplex composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with CEF1, CLF1, NTC20, PRP45 and SYF1.
Belongs to the WD repeat PRL1/PRL2 family.
Involved in pre-mRNA splicing. May also be required for cell cycle progression at G2/M (By similarity).
Belongs to the AB hydrolase superfamily. LDAH family.
Shows both triacylglycerol (TAG) lipase and ester hydrolase activities. May play a role in TAG homeostasis.
Involved in resistance to GST substrate o-dinitrobenzene (o-DNB).
The PY-motifs are required for the interaction with RSP5 ubiquitin-ligase.
Component of the TIM22 complex, whose core is composed of TIM18, TIM22 and TIM54, associated with the peripheral proteins MRS5/TIM12 and the 70 kDa heterohexamer composed of TIM9 and TIM10 (or TIM8 and TIM13). Interacts directly with both the TIM22 protein and the TIM9-TIM10 heterohexamer. Interacts with multi-pass transmembrane proteins in transit.
Essential component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as external driving force. In the TIM22 complex, it acts as a docking point for the soluble TIM9-TIM10 heterohexamer that guides the target proteins in transit through the aqueous mitochondrial intermembrane space.
The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIM12 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity).
Belongs to the glucose-6-phosphate 1-epimerase family.
Catalyzes the interconversion between the alpha and beta anomers from at least three hexose 6-phosphate sugars (Glc6P, Gal6P, and Man6P).
Belongs to the DNA 3' phosphatase family.
Dephosphorylate DNA's 3'-phosphate termini. Has a role in the repair of breaks in single-stranded DNA.
Expression is regulated by the cell integrity signaling pathway and by pheromone.
Key enzyme involved in DNA replication and DNA repair. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA. Possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5'-3' helicase and endonuclease activities. While the ATPase and endonuclease activities are well-defined and play a key role in Okazaki fragments processing and DSB repair, the 5'-3' DNA helicase activity is atypical: it cannot load onto its tracking strand internally and has an absolute free 5'-end requirement. Helicase activity may promote the motion of DNA2 on the flap, helping the nuclease function.
Phosphorylated at Ser-17 and Ser-237 by CDK1 in response to DNA damage, leading to promote recruitment to double-strand break (DSB) sites and DNA resection.
Belongs to the DmpD/TodF/XylF esterase family.
Interacts with MMS4 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks with regressed leading strands and nicked Holliday junctions. Cleavage probably occurs approximately half a helical turn upstream of the free 5'-end in these structures. May be required in mitosis for the processing of stalled replication fork intermediates arising spontaneously or subsequent to treatment with DNA damaging agents such as methylmethane sulfonate (MMS), camptothecin (CPT) or UV. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI). This involves consecutive cleavage of D-loops and nicked Holliday junctions leading to sister chromatid crossover. In contrast to MSH4-MSH5 dependent crossover, double Holliday junctions do not seem to be involved. Spore formation and viability are severely impaired in deletion strains.
Two distinct classes of meiotic crossovers have been demonstrated in budding yeast. Class I crossovers exhibit crossover interference and require MSH4 and MSH5 for their resolution, while class II crossovers exhibit no crossover interference and require MUS81 and MMS4. While class I crossovers represent the majority of crossovers in S.cerevisiae, they are virtually absent in S.pombe, which lacks orthologs of MSH4 and MSH5.
Component of the PAM complex, at least composed of SSC1 (mtHsp70), MGE1, TIM44, PAM16/TIM16, PAM17 and PAM18/TIM14. Interacts with SSQ1.
Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of SSC1 to substrate proteins and the association of SSC1 with TIM44.
May participate in the control of processing of mutational intermediates appearing during error-prone bypass of DNA damage.
Present with 120000 molecules/cell in log phase SD medium.
RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Required for the delivery of cortical endoplasmic reticulum into the emerging bud.
This enzyme catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.
Belongs to the eukaryotic ribosomal protein eL37 family.
Belongs to the Dus family. Dus2 subfamily.
Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs (PubMed:12003496, PubMed:14970222). Specifically modifies U20 in cytoplasmic tRNAs (PubMed:12003496, PubMed:14970222). Also able to mediate dihydrouridylation of some mRNAs, thereby affecting their translation (By similarity).
Essential protein involved in ribosomal RNA processing.
Shows a slower growth rate on YPD and minimal medium at 15 degrees Celsius. Synthetically sick with temperature-sensitive CDC13-1 mutant.
Associates with pre-60S ribosomal particles. Predominantly associated with the 27SA2 pre-rRNA. Can associate with a subset of box H/ACA and box C/D small nucleolar RNPs (snoRNPs) required for peptidyl transferase center modification and with small RNAs snR37 and snR42. Interacts with URB2. Together with DBP6, NOP8, URB2 and RSA3, forms an RNA-independent complex, which is required during early maturation of nascent 60S ribosomal subunits.
Required for 60S ribosomal subunit formation and pre-rRNA processing. Required for normal accumulation of 25S and 5.8S rRNAs.
ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1 and GET2, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the GET1-GET2 receptor, and returning it to the cytosol to initiate a new round of targeting. Cooperates with the HDEL receptor ERD2 to mediate the ATP-dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER. Involved in low-level resistance to the oxyanions arsenite and arsenate, and in heat tolerance.
Homodimer. Component of the Golgi to ER traffic (GET) complex, which is composed of GET1, GET2 and GET3. Within the complex, GET1 and GET2 form a heterotetramer which is stabilized by phosphatidylinositol binding and which binds to the GET3 homodimer (PubMed:32910895). Interacts with the chloride channel protein GEF1.
Present with 17300 molecules/cell in log phase SD medium.
Glycosylated. Phosphorylated. Phosphorylation serves a negative regulatory role.
Lack of SLG1 leads to a significant defect of 1,3-beta-glucan synthesis and confers sensitivity to caffeine, SDS, Calcofluor and alkaline pH stress. Deletion of residues 21-256 results in non-functional protein, removal of residues 21-110 yields a protein still able to confer some tolerance to alkaline stress, and deletion of residues 116-256 has no effect on the function.
Plays a role during G1 to regulate entering or exiting the cell cycle. Involved in stress responses. Has a role in cell wall integrity signaling. Activates ROM1 or ROM2 catalyzed guanine nucleotide exchange toward RHO1. Important regulator of the actin cytoskeleton rearrangements in conditions of cell wall expansion and membrane stretching. Specifically required for the actin reorganization induced by hypo-osmotic shock. Multicopy suppressor of 1,3-beta-glucan synthase (GS). Activates GS upstream of RHO1. Acts positively on the PKC1-MAPK pathway. Activates transiently SLT2 during alkaline stress, which leads to an increase in the expression of several specific genes.
Present with 664 molecules/cell in log phase SD medium.
The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of the RAD6/UBC2-BRE1 ubiquitin ligase complex, which ubiquitinates histone H2B to form H2BK123ub1. Also required for the methylation of histone H3 by the COMPASS complex to form H3K4me, by SET2 to form H3K36me, and by DOT1 to form H3K79me. RNA polymerase II associated protein important for transcription of a subset of genes. Required for both positive and negative regulation. Negatively regulates MAK16 expression. Also required for efficient CLN2 transcription in late G1 and may be involved in transcription of galactose-inducible genes.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily.
Catalyzes the removal of elemental sulfur from cysteine to produce alanine (PubMed:15220327). It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters (PubMed:10406803, PubMed:10551871, PubMed:15220327, PubMed:31040179). Plays a role in both tRNA-processing and mitochondrial metabolism (PubMed:15220327). Involved in the 2-thio-modification of both 5-carboxymethylaminomethyl-2-thiouridine in mitochondrial tRNAs and 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) in cytoplasmic tRNAs (PubMed:14722066, PubMed:15220327, PubMed:8444805).
Impairs cysteine desulfurase activity of mitochondria. Leads to strong accumulation of free iron, not bound to heme or Fe/S clusters, in mitochondria, as well as to decreased amounts of the mitochondrial Fe/S proteins including aconitase and succinate dehydrogenase. Leads also to accumulation of 5-methoxycarbonylmethyluridine (mcm5U) and a concomitant decrease in 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) in cytoplasmic tRNAs. Increases association between GRX5 and SSQ1 (PubMed:23615440).
the N-terminal beta-strand formed by residues 99-104 is essential for the function.
This is one of two stabilizing factors of the inactive mitochondrial F0F1-ATPase. It binds to the F0 part and facilitates the binding of both the inhibitor and the 9 kDa protein to F1.
Acts as component of the core factor (CF) complex which is essential for the initiation of rDNA transcription by RNA polymerase I. After binding of UAF (upstream activation factor) to an upstream element of the promoter, CF is recruited in a SPT15/TBP-dependent manner to form a preinitiation complex.
Component of the core factor (CF) complex, which consists of RRN6, RRN7 and RRN11. The CF heterotrimer may further dimerize to form a hexamer. RRN11 interacts with RRN6, RRN7 and SPT15.
Present with 476 molecules/cell in log phase SD medium.
Responsible for synthesis of pseudouridine from uracil-32 in mitochondrial transfer RNAs.
The active factor is excreted into the culture medium by haploid cells of the alpha mating type and acts on cells of the opposite mating type (type A). It mediates the conjugation process between the two types by inhibiting the initiation of DNA synthesis in type a cells and synchronizing them with type alpha.
Secondary mitochondrial glycine transporter required for the biosynthesis of heme at high glycine concentrations. Imports the precursor glycine into the mitochondrial matrix, where it is condensed with succinyl-CoA to produce 5-aminolevulinate (ALA), the first step of heme biosynthesis.
May be involved in the processing or stability of mitochondrial mRNAs.
Phosphorylated. Phosphorylation promotes binding to RNA.
Present with 2080 molecules/cell in log phase SD medium.
DNA damage-responsive protein that may be required for maintaining the rate of spontaneous mutagenesis. Shows low ATP and GTP hydrolysis activity. Dispensable for acquisition of thermotolerance and does not play a significant role in recovery or protection of cells from acute heat shock.
Expression is induced by DNA damage, as well as by salt, oxidative, and heat-shock stress.
Shows a slightly altered sensitivity to killing by 4-nitroquinoline-1-oxide and to heat shock; and a 6- to 14-fold reduction of the spontaneous mutation rate of reversion of a HIS4 mutation.
sequence is a contaminating peptide from a S.cerevisiae glycogen synthase purification.
Impairs mRNA export and transcription elongation, and induces strong transcription-associated hyperrecombination phenotypes.
Part of the 26S proteasome. Associates with the nuclear pore complex (NPC)-associated TREX-2 complex and the COP9 signalosome. Interacts with CSN12 and THP3.
Versatile protein that might stabilize multiple protein complexes involved in diverse pathways. Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis. Associates also with the TREX-2 complex that is required for transcription-coupled mRNA export, and the COP9 signalosome, which is involved in deneddylation.
Belongs to the NTC complex (or PRP19-associated complex), composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2, and PRP19. The NTC complex associates with the spliceosome after the release of the U1 and U4 snRNAs and forms the CWC spliceosome subcomplex (or CEF1-associated complex) reminiscent of a late-stage spliceosome composed also of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8, PRP9, PRP11, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNU114, SPP2, RSE1 and YJU2. Interacts with CEF1, CWC2, CLF1, and SYF1.
Involved in pre-mRNA splicing and cell cycle control. As a component of the NTC complex (or PRP19-associated complex), associates to the spliceosome to mediate conformational rearrangement or to stabilize the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation. The cell cycle arrest of SYF2 defective cells may be due to the inefficient splicing of TUB1. Also involved in DNA repair.
Belongs to the mitochondrion-specific ribosomal protein mS45 family.
Present with 20800 molecules/cell in log phase SD medium.
Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
Has broad nucleoside selectivity (uridine, adenosine and cytidine) and most likely functions to transport nucleosides across intracellular membranes.
Acts as a membrane-bound chaperone in endoplasmic reticulum quality control. Probably facilitates presentation of substrate to membrane-bound components of the degradation machinery.
Interacts with mutated PMA1-D378N but not wild type PMA1. Interacts with EUG1, KAR2, MPD1 and PDI1.
Produced by alternative initiation at Met-47 of isoform Mitochondrial.
Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.
Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and dUMP as phosphate acceptors, but can also use CMP, dCMP, AMP, GMP, dGMP and dTMP. ATP and dATP are the best phosphate donors, but can also use GTP, dGTP, dCTP, and dTTP to some degree.
There is controversy about the substrate specificity of the enzyme. Next to the primary substrate UMP, PubMed:1333436 and Ref.8 report that the enzyme accepts also CMP and AMP as nucleoside monophosphates, but not GMP, whereas PubMed:2172245 and PubMed:8391780 report activity with GMP and dTMP, but not AMP or CMP.
Belongs to the RNase HII family. Eukaryotic subfamily.
Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.
Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
This is a truncated version of a putative glutamine--fructose-6-phosphate aminotransferase. Strain S288c has a frameshift in position 258, which disrupts the gene coding for this protein and produces two ORFs YMR084W and YMR085W. A contiguous sequence for this protein can be found in strain YJM789 (AC A6ZME2).
Cell cycle-regulated. Expression peaks during mitosis.
Component of the outer cell wall layer (By similarity). May be involved in meiosis and sporulation.
Essential for the beta oxidation of unsaturated fatty acids.
Homohexamer, dimer of trimers. Interacts with DCI1.
Component of the septin complex which consists of CDC3, CDC10, CDC11, CDC12 and probably SHS1 and rearranges to a cortical collar of highly ordered filaments at the mother-bud-neck. A complex formed by CDC3, CDC10, CDC11 and CDC12 is capable of forming long filaments in vitro and the components seem to be present in a 2:2:2:2 arrangement in vivo. The filaments are proposed to be formed by the end-to-end polymerization of CDC3-CDC12-CDC11 complexes with CDC10 serving as a bridge to bundle the polymers into paired filaments. Component of the GIN4 complex composed of at least BNI5, CDC3, CDC10, CDC11, CDC12, GIN4, NAP1 and SHS1. Self-associates. Interacts with SIZ1 and SYP1.
Phosphorylated by CDC28. Phosphorylation at the end of G1 may facilitate initiation of a new cell cycle by promoting disassembly of the obsolete septin ring from the previous cell cycle.
Sumoylated during mitosis on the mother cell side of the bud neck by UBC9/SIZ1. Sumoylation probably plays a central role in regulating septin ring disassembly during the cell cycle.
Component of the PAM complex, at least composed of SSC1 (mtHsp70), MGE1, TIM44, PAM16/TIM16, PAM17 and PAM18/TIM14. In the complex, SSC1 interacts directly with PAM18 and TIM44. Interacts with NAP1.
Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Constitutes the ATP-driven core of the motor and binds the precursor preprotein. Required for the import of the processed frataxin homolog YFH1 into the mitochondrion.
S.cerevisiae displays strain polymorphism with regard to Endo.SceI endouclease activity. This is due to the mitochondrion-encoded, catalytic subunit ENS2, which exhibits strain polymorphism. It can be either present as continuous ORF in the mitochondrial genome (e.g. strain IAM 4274), present but disrupted by the insertion of GC clusters (e.g. strain D273-10B/A), or completely absent in the mitochondrial genome (e.g. strain S288c). Sequences for the 2 subunits ENS2 (AC P12294) and SSC1 (AC P0CS91) for an active Endo.SceI endonuclease can be found in strain IAM 4274.
Acts in signal transduction. Activates CDC42, RHO1 and RHO2. Negatively regulates 1,3-beta-glucan synthesis. May be responsible for the down-regulation of CDC42 during mating.
Negative mutants fail to enter the G0 phase under conditions of carbon limitation.
Plays a role in the coordination of growth and proliferation. Required for entry into G0 phase under conditions of carbon limitation. Involved in the general stress response; acts together with PSR1 to activate stress response element (STRE)-mediated gene expression, possibly through dephosphorylation of MSN2.
Belongs to the WD repeat DDB2/WDR76 family.
Closely coexpressed with replication factor A (RF-A), the cohesion complex and the DNA polymerases alpha, delta and epsilon.
DNA-binding protein that binds to both single- and double-stranded DNA. Binds preferentially to UV-damaged DNA in vitro (PubMed:22367945). May be involved in DNA-metabolic processes (PubMed:23349438).
Belongs to the major facilitator superfamily. Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
Belongs to the eukaryotic ribosomal protein eL32 family.
Homooligomer. Interacts with PEX27 and PEX34.
Required for regulation of peroxisome size and maintenance. Has a role in the import of peroxisomal matrix proteins. Imports RHO1 into the peroxisome. Also promotes peroxisome division and biogenesis.
Positive activator of the proline utilization pathway. Binds to the promoters of PUT1 and PUT2 genes. Recognizes and binds to the DNA sequence 5'-CGG-N(10)-CCG-3'.
Belongs to the class II fructose-bisphosphate aldolase family.
Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution.
Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.
Present with 1020000 molecules/cell in log phase SD medium.
Catalyzes the transamination of ornithine into L-glutamate gamma-semialdehyde, the second step of arginine degradation.
Present with 72000 molecules/cell in log phase SD medium.
Belongs to the arsenical resistance-3 (ACR3) (TC 2.A.59) family.
Expression is highly induced by arsenite and antimonite.
Heterologous expression endows plants with greater arsenic resistance by enhancing arsenite efflux. Reduces arsenic accumulation in rice grains (PubMed:22107880). Does not lower significantly arsenic tissue levels in Arabidopsis (PubMed:22380876).
Leads to sensitivity to antimony, tellurite, cadmium, and phenylarsine oxide.
Plasma membrane transporter that confers resistance to toxic metalloids by mediating extrusion of arsenite (As(III)) and antimonite (Sb(III)) out of cells. Displays low-affinity As(III)/H(+) and Sb(III)/H(+) exchange activity.
Alpha-glucosidase with specificity for isomaltase, methyl-alpha-glucoside, and palatinose.
May function as an amino acid transporter mediating the export of cationic amino acids from the vacuole. Required for optimal growth in synthetic medium.
Resistant to fluconazole. Increased resistance to caspofungin. Suppresses CDC13-1 temperature sensitivity.
Up-regulated by addition of ammonia or amino acids to a nitrogen-depleted medium. Down-regulated by excess lysine.
Guanine nucleotide exchange factor for Arf GTPases, stimulating the nucleotide exchange from the GDP-bound to the GTP-bound form. Catalyzes both the GDP release by and the GTP binding to ARF2. Has no exchange activity on Rab GTPases. Involved in vesicular transport.
The SEC7 domain is sufficient for nucleotide exchange activity.
Activates long-chain fatty acids (LCFA) by esterification of the fatty acids into metabolically active CoA-thioesters for subsequent degradation or incorporation into phospholipids. Also facilitates the transport of LCFAs into the cell, either by active transport or by decreasing the intracellular LCFA concentration (PubMed:8206942, PubMed:11477098, PubMed:12601005, PubMed:27136724). It may supplement intracellular myristoyl-CoA pools from exogenous myristate. Preferentially acts on C12:0-C16:0 fatty acids with myristic and pentadecanic acid (C15:0) having the highest activities (PubMed:8206942). Also involved in long-chain base (LCB) uptake of sphingolipids. In contrast ot LCFA uptake, LCB uptake does not require ATP, suggesting that the enzyme is directly involved in active LCB uptake (PubMed:27136724). Involved in the sphingolipid-to-glycerolipid metabolic pathway, converting the shingolipid metabolite hexadecenoic acid to hexadecenoyl-CoA, which is then further converted to glycerolipids (PubMed:22633490).
The N-myristoylated protein is further palmitoylated by ERF2, PFA4 and slightly by PFA5, but not by PFA3.
Its role might be as part of the apparatus concerned with the nuclear events of the cell cycle.
Present with 2229 molecules/cell in log phase SD medium.
RAD53-dependent phosphorylated in response to DNA damage.
Transcriptional repressor of photolyase PHR1. Recognizes and binds the sequence AG(4) in the upstream repressing sequence of PHR1. Derepresses PHR1 transcription when phosphorylated.
Mannosyltransferase that transfers a mannose residue from GDP-mannose to a range of acceptors in vitro, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage.
Has a role in the DNA error-free postreplication repair (PRR) pathway. Lacks catalytic activity by itself. The UBC13/MMS2 heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'.
Component of the N-terminal acetyltransferase C (NatC) complex, which is composed of MAK3, MAK10 and MAK31.
Component of the NatC N-terminal acetyltransferase, which catalyzes acetylation of the N-terminus Met of L-A virus Gag protein. MAK10 has a role in the propagation of L-A and M viruses, perhaps in the viral assembly. It is apparently directly needed for optimum respiration.
Responsible for addition of the terminal mannose residues to the outer chain of core N-linked polysaccharides and to O-linked mannotriose. Implicated in late Golgi modifications.
By transcription factor PDR1, by transcription factor HAA1 in response to acetaldehyde accumulation and by the non-steroidal anti-inflammatory drug indomethacin.
Cell membrane polyamine/proton antiporter, involved in the detoxification of excess polyamines in the cytoplasm. Catalyzes polyamine uptake at alkaline pH and excretion at acidic pH. Recognizes spermidine, spermine and putrescine, the polyamine analogs methylglyoxal bis(guanylhydrazone) (MGBG) and paraquat, the antimalarial drug quinidine, and cycloheximide. Confers resistance to the non-steroidal anti-inflammatory drug indomethacin.
Belongs to the actin family. ARP6 subfamily.
PDR1 and PDR3 jointly control the transcription level of both SNQ2 and PDR5.
Abolishes diphthamide modification of elongation factor 2 (PubMed:32576952). Abolishes the interaction between DPH1 and DPH3 (PubMed:18627462). Resistance to diphtheria toxin, sordarin, and zymocin (PubMed:18627462, PubMed:27694803, PubMed:32576952). Sensitive to hygromycin B (PubMed:32576952).
Belongs to the DPH1/DPH2 family. DPH2 subfamily.
Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the DPH1 subunit.
Component of the 2-(3-amino-3-carboxypropyl)histidine synthase complex composed of DPH1, DPH2, KTI11/DPH3 and a NADH-dependent reductase, predominantly CBR1 (PubMed:31463593, PubMed:24422557, PubMed:18627462). Interacts with DPH1; the interaction is direct (PubMed:15485916, PubMed:23645155, PubMed:31463593). Interacts with KTI11/DPH3 (PubMed:12940988, PubMed:27694803, PubMed:18627462).
Present with 3486 molecules/cell in log phase SD medium.
Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (PubMed:8406038, PubMed:24422557, PubMed:27694803, PubMed:31463593, PubMed:32576952, PubMed:34154323). DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising KTI11/DPH3 and a NADH-dependent reductase, predominantly CBR1 (PubMed:8406038, PubMed:24422557, PubMed:27694803, PubMed:31463593, PubMed:34154323). Facilitates the reduction of the catalytic iron-sulfur cluster found in the DPH1 subunit (PubMed:31463593).
Present with 40400 molecules/cell in log phase SD medium.
Component of the lid subcomplex of the 19S proteasome regulatory particle complex (also named PA700 complex). The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. Interacts directly with RPN8 and STS1.
Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. RPN11 is the only catalytically active member of the lid and serves as the essential deubiquitinase of the proteasome.
The JAMM motif is required for the deubiquitination and degradation of ubiquitinated substrates.
Interacts with URE2 and GDH2. Interacts also with the TORC1 kinase complex.
Serine/threonine-protein kinase involved in the phosphorylation of the NAD(+)-dependent glutamate dehydrogenase GDH2. When overexpressed, confers hypersensitivity to rapamycin and induces rapid nuclear accumulation of GLN3 to activate the transcription of nitrogen-regulated genes.
Present with 51900 molecules/cell in log phase SD medium.
Homodimer (By similarity). Interacts with SSQ1 (PubMed:23615440). Interacts with BOL1 (PubMed:27532773).
Monothiol glutaredoxin involved in mitochondrial iron-sulfur (Fe/S) cluster transfer (PubMed:11950925, PubMed:12730244, PubMed:23615440). Receives 2Fe/2S clusters from scaffold protein ISU1 and mediates their transfer to apoproteins, to the 4Fe/FS cluster biosynthesis machinery, or export from mitochondrion (PubMed:27532773, PubMed:23615440).
Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Necessary for cell growth.
Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5; loaded onto DNA, forms a head-head double hexamer. Interacts with CSM1.
Early fractionation of eukaryotic MCM proteins yielded a variety of dimeric, trimeric and tetrameric complexes with unclear biological significance. The MCM2-7 hexamer is the proposed physiological active complex.
Has a role in spindle assembly and stability. Required to ensure a timely exit form mitosis. Essential to maintain pre-anaphase spindle polarity. Associates to the plus ends of the microtubules at the kinetochore and spindle midzone. A component of the FEAR (CDC14 Early Anaphase Release) network which promotes CDC14 release from the nucleolus during early anaphase. Required for proper chromosome segregation during meiosis I where it prevents premature sister chromatid separation.
Phosphorylated by CDC5/Polo-like kinase at the onset of anaphase. Phosphorylation takes places at proximity to cleavage sites and is required for an efficient cleavage by ESP1. Phosphorylated also by CDC28.
Present with 314 molecules/cell in log phase SD medium.
Transcription activator involved in the regulation of genes expressed in response to environmental changes and metabolic requirements. According to genome-wide promoter binding and gene expression studies it is a coregulator for the expression of ribosomal genes, while its own expression is induced by the cell cycle specific activator SBF (SWI4-SWI6).
Although strongly related to DNA helicases, it lacks the helicase C-terminal domain, suggesting that it has no helicase activity.
Homodimer. Interacts with HAP1. Component of the HMC including HAP1, SRO9 and YDJ1.
Present with 119000 molecules/cell in log phase SD medium.
Probably involved in mitochondrial protein import. Is also required for efficient translocation of pre-pro-alpha-factor. Involved in heme regulation of HAP1, as a component of the high-molecular-weight (HMC) complex.
YDJ1 is a heat shock gene whose expression increases moderately at elevated temperatures.
Present with 40300 molecules/cell in log phase SD medium.
Interacts with the GDP-bound form of Rab GTPase YPT1. Interacts with YPT10.
Present with 7280 molecules/cell in log phase SD medium.
Regulates the GDP/GTP exchange reaction of SEC4 by inhibiting the dissociation of GDP from it, and the subsequent binding of GTP to SEC4. Plays an essential role in the yeast secretory pathway (PubMed:8157010). Extracts GDP-bound YPT7 from vacuolar membranes, antagonizing vacuolar membrane fusion (PubMed:11118206).
E2 ubiquitin-like--protein ligase mediating SUMO/Smt3 attachment to septins and PCNA. Seems to be involved in degradation of S- (CLB5) and M-phase cyclins (CLB2).
Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.
Sterol O-acyltransferase that catalyzes the formation of stery esters.
DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. RPA14 seems to play a role in the stability of subunits RPO26 and RPA43. In vitro, the RPA14-RPA43 subcomplex binds single-stranded RNA.
Late stages of sporulation, during ascospore wall formation. Probably functions before partitioning of nuclei or is distributed to developing ascospores prior to the completion of pro-spore walls.
Probably involved in the processes of spore formation and contributes to ascospore thermoresistance by participating in the morphogenesis of ascospore walls. The enzyme may do this by modifying glucan linkages in the developing ascospore wall, thus strengthening it or lending it plasticity.
Serine/threonine protein kinase shown to have protein phosphorylation activity in vitro.
Belongs to the DHHC palmitoyltransferase family. PFA4 subfamily.
Leads to the retention of non-palmitoylated CHS3 in the endoplasmic reticulum and reduced levels of chitin on the cell wall.
Mediates the reversible addition of palmitate to target proteins, thereby regulating their membrane association and biological function. Palmitoylates several amino acid permeases (PubMed:16751107). Palmitoylates chitin synthase CHS3, which is required for its proper export from the ER (PubMed:16818716, PubMed:28346351). Can palmitoylate RAS2 in vitro (PubMed:12379641).
Ty1-NL1 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Likely plays only a minor role in eisosome assembly.
Catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Component of the TIM23 complex, at least composed of TIM23, TIM17, TIM50 and TIM21. The complex interacts with the TIM44 component of the PAM complex.
Monomer and homodimer. Associated with the 100 kDa subunit of the plasma membrane H(+)-ATPase.
Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins.
Was originally thought to be the catalytic subunit (PubMed:3061797). The low processing activity which was previously observed with alpha-MPP which has been purified from a mitochondrial extract is most likely due to contamination by the beta-subunit. Does not seem to have protease activity as it lacks the zinc-binding site (PubMed:9299349).
Inhibitor of the DOA4 deubiquitinase involved in the regulation of protein degradation by the proteasome and maintenance of a normal level of free ubiquitin.
Belongs to the succinate/malate CoA ligase alpha subunit family.
Induced during growth on nonfermentable carbon sources and repressed during growth on glucose.
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA (PubMed:9874242). The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit (By similarity).
Belongs to the WD repeat peroxin-7 family.
Receptor required for the peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal, such as 3-oxoacyl-CoA thiolase (PubMed:7957058, PubMed:7535304, PubMed:23812376). Specifically binds to cargo proteins containing a PTS2 peroxisomal targeting signal in the cytosol (PubMed:23812376). Cargo protein-binding triggers interaction with PEX21 and formation of a ternary complex composed of PEX21 and PEX7 along with PTS2-containing cargo proteins, which is tranlocated into peroxisomes by passing through the PEX13-PEX14 docking complex (PubMed:9094717, PubMed:23812376).
Component of the TFIIIC complex composed of TFC1, TFC3, TFC4, TFC6, TFC7 and TFC8. The subunits are organized in two globular domains, tauA and tauB, connected by a proteolysis-sensitive and flexible linker. Interacts with TFC3, TFC4 and TFC6.
Present with 15800 molecules/cell in log phase SD medium.
TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and similar genes. Participates in the interconnection of tauA with tauB via its contacts with TFC3 and TFC6. Serves as a scaffold critical for tauA-DNA spatial configuration and tauB-DNA stability.
Non essential disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May be involved in glycosylation, prolyl hydroxylation and triglyceride transfer. Able to fold proteins by being directly oxidized by ERO1.
May be involved in specific transport of UDP-Gal from the cytosol to the Golgi lumen. Involved in the maintenance of optimal conditions for the folding of secretory pathway proteins in the endoplasmic reticulum. Overexpression confers resistance to the immunosuppressive drug, leflunomide.
May function as an amino acid transporter mediating the export of cationic amino acids from the vacuole.
Accumulates as a carbonylated protein in absence of PIM1, suggesting that the PIM1 protease is responsible for the degradation of its oxidized form in mitochondria.
Required for the maintenance of the cell wall integrity.
Target of SBF and MBF transcription factor complexes that activate gene expression during the G1/S transition of the cell cycle.
Component of the nucleotide excision repair factor 1 (NEF1) complex consisting of RAD1, RAD10 and RAD14.
Involved in nucleotide excision repair. Binds specifically to damaged DNA. Required for the incision step.
Belongs to the eukaryotic ribosomal protein eL33 family.
Important for the export of protein containing nuclear export signal (NES) out of the nucleus. Stimulates the GTPase activity of GSP1 and GSP2.
Present with 2030 molecules/cell in log phase SD medium.
Final receptor of the SLN1-YPD1-SSK1 two-component regulatory system, which controls activity of the HOG1 pathway in response to changes in the osmolarity of the extracellular environment. Under normal osmotic conditions, maintained in a phosphorylated and inactive state by the phosphorelay intermediate protein YPD1. Under conditions of high osmolarity, the histidine kinase SLN1 is no longer active and the unphosphorylated form of SSK1 interacts with and activates SSK2 and SSK22, two MAPKKKs that further stimulate the PBS2-HOG1 MAPKK-MAPK cascade. Unphosphorylated SSK1 is subsequently degraded by the UBC7-dependent ubiquitin-proteasome system to down-regulate the HOG1 pathway after completion of the osmotic adaptation.
The phosphorelay mechanism involves the sequential transfer of a phosphate group from 'His-576' (H1) to 'Asp-1144' (D1) of SLN1, then to 'His-64' (H2) of YPD1 and finally to Asp-554 (D2) of SSK1.
Belongs to the glycogen debranching enzyme family.
Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation.
Belongs to the bacterial ribosomal protein bL28 family.
Present with 4000 molecules/cell in log phase SD medium.
PMT3 and PMT5 form a functional heterodimer. Forms also a minor complex with PMT2.
Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT3 and more rarely with PMT2 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Component of the 20S proteasome chaperone. Forms a heterodimer with PBA1 that binds to proteasome precursors.
Deletion induces the unfolded protein response (UPR).
Involved in 20S proteasome assembly. Required for maximal proteasome activity. Affects the chymotrypsin-like activity of the proteasome. Can be degraded by the proteasome. Involved in the endoplasmic reticulum-associated degradation (ERAD).
Forms a complex with the Rab escort protein (REP) MRS6, which is recognized by Rab geranylgeranyltransferase BET2-BET4. Interacts with the Rab GDP dissociation inhibitor GDI1, which can retrieve from and deliver to membranes the GDP-bound and prenylated form of YPT1. Interacts with YIP1, which is required for proper membrane targeting of prenylated YPT1. Interacts with YIF1, YIP3, YIP4 and YIP5.
In PubMed:3042385 the location of any palmitoylation was not determined. Mutagenesis of either Cys-205 or Cys-206 would disrupt normal geranylgeranylation, and there would be no primary membrane association for secondary S-palmitoylation to occur at some other position, for example Cys-23. Mutagenesis of both Cys-205 and Cys-206 is lethal, so protein production could not have been observed.
Prenylation is required for interaction with GDI1 and YIP1.
Rab activation is generally mediated by a guanine exchange factor (GEF), while inactivation through hydrolysis of bound GTP is catalyzed by a GTPase activating protein (GAP). YPT1 is activated by the GEFs DSS4 and TRAPP complex, and inactivated by GAPs GYP1, GYP5 and GYP8.
The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. YPT1 regulates the trafficking of secretory vesicles from the endoplasmic reticulum (ER) to the Golgi. Vesicular transport depends on shuttling of YPT1 between membrane and cytosol by GDI1, probably by recycling it to its membrane of origin after a vesicle fusion event. Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum. Also involved in the recycling of membrane proteins.
Interacts with NMD helicase UPF1 (PubMed:17984081). Interacts with CDC33 (PubMed:16467471).
Plays a role in nonsense-mediated mRNA decay (NMD) (PubMed:16467471, PubMed:17984081). Recruits UPF1 to cytoplasmic mRNA decay bodies (P-bodies) (PubMed:17984081). Negative regulator of gene expression. Inhibits translation most likely through effects on eIF-4E (CDC33) (PubMed:16467471). Involved in telomere maintenance (PubMed:10688642).
Results in stabilization of NMD targets.
Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Impairs growth on beta-alanine but can still utilize pantothenic acid.
Probable 3-methyl-2-oxobutanoate hydroxymethyltransferase required for pantothenic acid biosynthesis (PubMed:11154694). Acts downstream in the pantothenic acid pathway (PubMed:11154694).
Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The AP-1 complex interacts directly with clathrin.
Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit APL4 and beta-type subunit APL2), a medium adaptin (mu-type subunit APM1) and a small adaptin (sigma-type subunit APS1). Interacts with CHC1. Interacts with APM2, probably forming an alternative AP-1-like complex.
Has statistically significant lower desiccation tolerance capacity.
Hydrophilin which is essential to overcome the simple stress of the desiccation-rehydration process.
Up-regulated in response to osmotic stress.
Interacts with POL1, EST1, FUN12, STM1, STN1 and TEN1.
Single-stranded telomeric DNA-binding protein that regulates telomere replication. Has a role in both positive and negative regulation. Promotes [TG(1-3)] strand lengthening via interaction with EST1. Promotes [C(1-3)A] strand re-synthesis by DNA polymerase alpha via interaction with POL1. Negatively regulates telomere elongation of the G strand via binding with STN1 thereby inhibiting telomerase activity.
Heterodimer of a 32 kDa catalytic subunit and a larger 60 kDa polypeptide subunit.
Mitochondrial DNA endonuclease involved in intron homing. It introduces a specific double-strand break in the DNA of the COX1 gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Recognizes with limited specificity and cleaves the sequence 5'-ATCTTCTCTTGATTAGCCCTGATCTACGG-3' after the nucleotide sequence ATTA leaving a four-base overhang and a 3'-OH.
The mature protein may arise from proteolytic cleavage of an in-frame translation of some COX1 exons plus the intron containing the aI5_alpha open reading frame.
Functions as a sorting receptor in the Golgi compartment required for the intracellular sorting and delivery of soluble vacuolar proteins, like carboxypeptidase Y (CPY) and proteinase A.
Nonessential DNA polymerase. Required for DNA damage induced mutagenesis. Involved in DNA repair, mitochondrial DNA repair and translesion synthesis. Translesion synthesis in S.cerevisiae may use a specialized DNA polymerase that is not required for other DNA replicative processes. Has a role in the bypass of abasic (AP) sites. Highly inefficient in incorporating nucleotides opposite the AP site, but efficiently extends from nucleotides, particularly an A, inserted opposite the lesion.
Involved in spore and ascus formation. Required for the efficient assembly of the precursors of the prospore membrane to a continuous prospore membrane.
Positive regulator of protein phosphatase SIT4. Involved in the general amino acid control (GAAC) response regulated by TOR. Involved in the dephosphorylation of the elongator complex subunit IKI3.
Cell cycle-dependent phosphorylation of three serine residues prevents SWI5 from entering the nucleus, and it accumulates in the cytoplasm. As a consequence of CDC28 kinase inactivation at the end of anaphase, the three serine residues are dephosphorylated and SWI5 enters the nucleus to activate transcription. It is then rapidly degraded. Threonine phosphorylation also seems to occur.
Determines the mother-cell-specific transcription of the HO endonuclease gene that is responsible for the initiation of mating-type switching in yeast. Recognizes a specific sequence in the promoter of the HO gene. Activates EGT2 transcription in a concentration-dependent manner. Synthesized during G2 and early mitosis.
Belongs to the AAA ATPase family. PCH2 subfamily.
Induced at the onset of meiosis I and reaches a maximum level during pachytene (at protein level).
Required for the pachytene checkpoint, the meiotic checkpoint that prevents chromosome segregation when defects in recombination and synaptonemal complex formation occurred. Represses meiotic recombination in the rDNA, probably by excluding the meiosis-specific protein HOP1 from the nucleolar region.
During G2 phase of cell cycle. Promoter is bound by the FKH2 transcription factor.
Acts as a GTPase-activating protein (GAP) for SAR1 (PubMed:24947508). Contrary to its SEC23 homolog, NEL1 does not associate with SEC24 and its homologs, nor does it associate with the COPII components, suggesting that it is unlikely that NEL1 functions as a structural component of the vesicle coat machinery (PubMed:24947508). May function as a signaling molecule (PubMed:24947508).
Belongs to the SEC23/SEC24 family. SEC23 subfamily.
Leads to a significant growth defect in the temperature-sensitive SAR1-D32G mutant background.
Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP1/NBP35 subfamily.
Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Required for biogenesis and export of both ribosomal subunits, which may reflect a role in assembly of the Fe/S clusters in RLI1, a protein which performs rRNA processing and ribosome export.
Interacts with NVJ1 (PubMed:15367582, PubMed:28319008). Interacts with the AAA ATPase AFG2; regulates OSH1 membrane association. AFG2 is required for membrane dissociation of OSH1 (Probable). Interacts with SCS2 (PubMed:12727870).
Lipid transport protein (LTP) involved in non-vesicular transfer of lipids between membranes. Functions in phosphoinositide-coupled directional transport of various lipids by carrying the lipid molecule in a hydrophobic pocket and transferring it between membranes through the cytosol. Involved in maintenance of intracellular sterol distribution and homeostasis (PubMed:8017104, PubMed:11238399, PubMed:15173322). Involved in non-vesicular transport of ergosterol and PI(4)P at the NVJ. Binds sterol and PI4P in a mutually exclusive manner (PubMed:28319008). May be involved in formation of PMN vesicles by altering the membrane lipid composition (PubMed:15173322).
The FFAT (two phenylalanines in an acidic tract) motif is required for interaction with SCS2 and is required for targeting the protein to the ER.
The PH domain strongly binds to phosphoinositides and is required for targeting the protein to the late Golgi membranes.
The ankyrin repeats are required for targeting the protein to the NV junction by interacting with NVJ1.
Autophosphorylated. Phosphorylated by casein kinase II (CK2). Phosphorylation by CK2 stimulates RIO1 kinase activity and targets it for degradation at the G1/S transition of the cell cycle.
Belongs to the protein kinase superfamily. RIO-type Ser/Thr kinase family.
Can use both Mg(2+) and Mn(2+) in vitro and shows higher activity with Mn(2+) but Mg(2+) is likely to be the in vivo cofactor.
Required for the final endonucleolytic cleavage at site D converting 20S pre-rRNA into the mature 18S rRNA. Required for the final steps of cytoplasmic maturation of the 40S ribosomal subunit. The association with the very late 40S subunit intermediate seems to follow RIO2 association with precursors of the 40S subunit and may involve a translation-like checkpoint point cycle preceeding the binding to the 60S ribosomal subunit. Despite the protein kinase domain is proposed to act predominantly as an ATPase. The catalytic activity regulates its dynamic association with the 40S subunit. Has a role in the cell cycle where it is required for entrance into S-phase and in the control of the onset of anaphase. Appears to also be involved in the maintenance of chromosome stability and correct mitotic segregation.
Accessory component of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:29526695). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:29526695). Functions with VMA21 in assembly of the V0 complex (PubMed:18799613).
Present with 12764 molecules/cell in log phase SD medium.
Reduces association of VMA6 with the V-type proton ATPase (PubMed:29526695). Decreases VPH1 protein level (PubMed:29526695).
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and VOA1) (PubMed:29526695). Interacts with VMA21 (PubMed:18799613). Associates with the assembling V0 complex (PubMed:18799613).
Required for the activation of chitin synthase III (CHS3) activity during the sporulation process.
Interacts with MOB1. MOB1-binding is required for a late mitotic event.
Kinase activity is regulated by BUB2, CDC15 and CDC5, and is maximal during nuclear division. CDK1 kinase inhibits cellular DBF2-MOB1 kinase activity via phosphorylation of both CDC15 and MOB1.
Periodically expressed in the cell cycle, with a peak before the onset of budding.
Phosphorylation of Ser-374 and Thr-544 by CDC15 is essential for activation of DBF2 kinase activity.
Ser/Thr-protein kinase involved in the mitotic exit network (MEN) and required after the metaphase to anaphase cell cycle transition. Phosphorylates CHS2 to regulate its dynamics and chitin synthesis at the division site during cytokinesis. Coordinates septin and actomyosin ring (AMR) functions during cytokinesis through the phosphorylation of HOF1. In complex with MOB1, phosphorylates CDC14 at sites adjacent to its nuclear localization sequence, thereby retaining CDC14 in the cytoplasm. Binds also to SWI5 and CLB2 mRNAs cotranscriptionally to regulate their decay. In the nucleus, the DBF2-MOB1 complex regulates passenger protein localization during anaphase. Mediates sorbic acid stress tolerance through promoting vacuolar H(+)-ATPase function, probably through phosphorylation of VMA1 and VMA2 subunits.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YJR028W ORF.
Activity is dependent of phosphatidylinositol 4,5-bisphosphate and the regulator SRF1. Inhibited by magnesium.
Required for meiosis and spore formation. Seems to be involved in the coordinate induction of late meiotic events. PLD activity is induced under sporulation conditions and seems to be necessary to complete the meiotic cycle, but not for vegetative cell growth.
Belongs to the class I-like SAM-binding methyltransferase superfamily. EEF2KMT family.
Increases sensitivity to antibiotics that target translation and decreases translational fidelity.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono-, di- and trimethylates elongation factor 2 (EFT1/EFT2) at 'Lys-509'.
Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. RPC25/RPC8 and RPC17/RPC9 form a Pol III subcomplex.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNA. The RPC25/RPC8-RPC17/RPC9 subcomplex may bind Pol III transcripts emerging from the adjacent exit pore during elongation.
High-affinity uptake of maltose and maltotriose. Also transports turanose but not alpha-methylglucoside, melezitose or trehalose.
Overexpression affects chitinase expression, cell separation and budding pattern, and increases trehalose accumulation and heat resistance by inhibiting protein kinase CBK1. Overexpression also suppresses temperature-induced hyperosmosensitivity and sensitivity to cell wall degrading enzymes. Overexpression of both LRE1 and PBN1 confers resistance to laminarinase.
Belongs to the universal ribosomal protein uL11 family.
Component of the mitochondrial large ribosomal subunit (mt-LSU) (PubMed:9151978). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins (PubMed:24675956).
Interacts with the t-SNARE SSO1 and the v-SNARE SNC2.
Required to maintain the prospore membrane to the nucleus during sporulation in order to capture the daughter nuclei and form the spores. Mediates the fusion of exocytic vesicles with the plasma membrane during sporulation through its interactions with the t-SNARE SSO1 and v-SNARE SNC2.
The inhibitory region sequesters the protein in the nucleus.
The positive regulatory region is essential and contains an amphipathic helix with hydrophobic and positive charged faces involved in the localization of the protein to the membranes through its binding to phospholipids.
Lipid raft-associated protein involved in the targeting of PMA1 from Golgi to the plasma membrane (PubMed:7822420, PubMed:11739806). May induce clustering of PMA1, which facilitates partition of PMA1 into lipid rafts after leaving the ER and its transport to the cell surface (PubMed:11739806).
Belongs to the eukaryotic ribosomal protein eL29 family.
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 10 subunits. The complex is composed of 3 respiratory subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10 (PubMed:10873857, PubMed:11880631, PubMed:18390544, PubMed:30598554). The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a monomer or a dimer of cytochrome c oxidase (complex IV, CIV), resulting in 2 different assemblies (supercomplexes III(2)IV and III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556, PubMed:30598554). CYT1 interacts with COX5A at the CIII-CIV interface (PubMed:30598554).
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (Probable). Cytochrome c1 is a catalytic core subunit containing a c-type heme. It transfers electrons from the [2Fe-2S] iron-sulfur cluster of the Rieske protein to cytochrome c (PubMed:18390544).
Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
During the diauxic shift. In response to oxidative stress.
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide. The disulfide is subsequently reduced by thioredoxin.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Has a role in telomere silencing, which is the repression of chromatin structure which leads to a stop in the transcription of nearby genes. Also has a role in the regulation of telomere length. Acts as an alkyl-hydroperoxide reductase in the nucleus during post-diauxic growth. Preferentially reduces alkyl-hydroperoxides rather than hydrogen peroxide. Acts as an antioxidant necessary for stationary phase survival.
Involved in the organization of the outer spore wall layers and especially in the assembly of the chitosan layer.
Expression is regulated by carbon source, with very low expression with succinate, acetate, ethanol or pyruvate as carbon source.
Mitochondrial transporter that mediates uptake of thiamine pyrophosphate (ThPP) into mitochondria.
Present with 6680 molecules/cell in log phase SD medium.
Present with 27400 molecules/cell in log phase SD medium.
Chromatin reader component of the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK (PubMed:10026213, PubMed:15647753, PubMed:21685874, PubMed:24307402). In the SAGA complex, SGF29 specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3) (PubMed:21685874). SGF29 is also required for heterochromatin boundary formation function (PubMed:24307402). SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes At the promoters, SAGA is required for recruitment of the basal transcription machinery (PubMed:10026213). It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8) (PubMed:10026213). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs) (PubMed:10026213). SLIK is proposed to have partly overlapping functions with SAGA (PubMed:15647753). It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus (PubMed:15647753).
Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Interacts with dimethylated and trimethylated 'Lys-4' of histone H3 (H3K4me2 and H3K4me3), with a preference for the trimethylated form (H3K4me3). Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9.
The SGF29 C-terminal (also named tudor-like) domain mediates binding to methylated 'Lys-4' of histone H3 (H3K4me).
Belongs to the eukaryotic ATPase epsilon family.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Undergoes rapid but transient induction upon transfer to sporulation medium.
Ty1-OL is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.
Belongs to the protein-tyrosine phosphatase family. Non-receptor class myotubularin subfamily.
Exhibits increased phosphatidylinositol 3-monophosphate (PI3P) level.
Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P). Involved in the control of PI3P-dependent signaling and in the maintenance of endosomal system integrity.
Transcriptional repressor required to restrict transcription of ECB-dependent genes to the G1/M phase by repressing their transcription during the interval from late G1 to M phases. Genes that contain a ECB (early cell box) element in their transcription regulatory region are transcribed only during G1/M phases. In vitro, is capable of binding to the DNA of the leucine tRNA gene.
Transcriptionally activated by SWI4-SWI6 heterodimer.
mRNA-binding protein that may play a role in modulating the expression of cytoplasmic mRNA.
By transcription factors AFT1 and AFT2 upon iron deprivation.
Metalloreductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane. Also participates in Cu(2+) reduction and Cu(+) uptake.
Belongs to the TFIIE alpha subunit family.
Present with 35900 molecules/cell in log phase SD medium.
Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase (By similarity).
TFIIE is a tetramer of two alpha (TFA1) and two beta (TFA2) subunits.
As accessory component of the DNA polymerase epsilon complex participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair.
Belongs to the DNA polymerase epsilon subunit B family.
Phosphorylated in a cell cycle dependent manner during late G1 phase. Phosphorylation may facilitate the interaction with POL2 or the activity of DNA polymerase II. Phosphorylation is independent of DNA replication but dependent upon CDC28 in vivo. Both Ser-141 and Ser-613 are phosphorylated in vivo, but in vitro only Ser-141 is phosphorylated by CDC28.
Present with 3110 +/- 251 molecules/cell in log phase SD medium.
Belongs to the UbiD family. UbiD-like/FDC subfamily.
Binds 1 prenylated FMN (prenyl-FMN) per subunit.
Catalyzes the reversible decarboxylation of aromatic carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives 4-vinylphenol, 4-vinylguaiacol, and styrene, respectively, which play the role of aroma metabolites (PubMed:20471595, PubMed:25647642). Not essential for ubiquinone synthesis (PubMed:20471595).
Homodimer (PubMed:25862228). May form higher order oligomers (PubMed:25647642).
Involved in the organization of the secretory pathway. Required to maintain a functional Golgi apparatus.
Leads to internal accumulation of precursor CPY.
Serine/threonine-protein kinase involved in vacuolar processing and morphology.
Could influence the NAM7/UPF1 function, possibly at the level of mRNA turnover. Participates in mitochondrial biogenesis.
Repressed by glucose. Cotranscribed with NAM7 in the absence of CYP1.
Could be a component of the mitochondrial translation system with a role in promoting accuracy of translational initiation.
Involved in the partitioning of the mitochondrial organelle and mitochondrial DNA (mtDNA) inheritance.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerases II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. During a transcription cycle, Pol II, general transcription factors and the Mediator complex assemble as the preinitiation complex (PIC) at the promoter. 11-15 base pairs of DNA surrounding the transcription start site are melted and the single-stranded DNA template strand of the promoter is positioned deeply within the central active site cleft of Pol II to form the open complex. After synthesis of about 30 bases of RNA, Pol II releases its contacts with the core promoter and the rest of the transcription machinery (promoter clearance) and enters the stage of transcription elongation in which it moves on the template as the transcript elongates. Pol II appears to oscillate between inactive and active conformations at each step of nucleotide addition. Pol II is composed of mobile elements that move relative to each other. The core element with the central large cleft comprises RPB3, RBP10, RPB11, RPB12 and regions of RPB1 and RPB2 forming the active center. The clamp element (portions of RPB1, RPB2 and RPB3) is connected to the core through a set of flexible switches and moves to open and close the cleft. The cleft is surrounded by jaws: an upper jaw formed by portions of RBP1, RPB2 and RPB9, and a lower jaw. The jaws are thought to grab the incoming DNA template. The fork loop 1 (RPB2) interacts with the RNA-DNA hybrid, possibly stabilizing it.
The binding of ribonucleoside triphosphate to the RNA polymerase II transcribing complex probably involves a two-step mechanism. The initial binding seems to occur at the entry (E) site and involves a magnesium ion coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates ribosomal protein S18 (RPS18A and RPS18B) at 'Lys-48' and dimethylates ribosomal protein L23 (RPL23A and RPL23B) at 'Lys-106' and 'Lys-110'.
Required for cytoplasm to vacuole transport (Cvt), pexophagy and mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Functions in protein retrieval from the endocytic pathway. Required for proper sorting of the v-SNARE protein SNC1.
The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization of ATG20 to the perivacuolar punctate structures.
Deletion leads to a K1 killer toxin hypersensitivity.
Involved in gene expression controlled by TOR kinase and nutrient signaling. May also be involved in positioning the proximal bud pole signal.
Stimulates the exchange of RHO1 GDP-bound form into GTP-bound form.
Plays a role in endocytosis and trafficking to the vacuole. Functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress.
Belongs to the mannose-6-phosphate isomerase type 1 family.
Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Could be the product of a pseudogene. This is the C-terminal part of a DUP240 protein in strain S288c due to a naturally occurring frameshift at position 8 compared to other strains. A complete sequence for YAR023C can be found in other strain backgrounds (AC P0CI38).
Belongs to the DEAD box helicase family. DEAH subfamily. DDX15/PRP43 sub-subfamily.
Component of the NTR complex (NTC-related complex), composed of NTR1, NTR2 and PRP43. Interacts with NTR1 and NTR2. Interacts with SPP382.
Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA.
Accepts electrons from ETF and reduces ubiquinone.
Displays higher growth rate and higher sensitivity to superoxide and heat stress, on nonfermentable carbon sources. Leads to decreased intracellular oxidation upon heat shock.
Belongs to the chitin synthase family. Class IV subfamily.
Decreases cell wall chitin level (PubMed:28346351). Resistance to Calcofluor White (cell wall stressor) (PubMed:28346351). Decreases conjugation frequency (PubMed:9234668).
Homodimer (PubMed:28346351). May form higher order oligomers (PubMed:28346351). Seems to interact with BNI4 and SKT5 which link CHS3 to septins (PubMed:9314530, PubMed:28346351).
Palmitoylated by PFA4; required for proper export from the ER.
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer (Probable) (PubMed:9760183). Appears to be responsible for synthesis of the majority of the chitin found in the cell wall periphery (PubMed:2050738). It is involved in the synthesis of the chitin ring that forms in the cell wall just before bud emergence (PubMed:2050738). This ring remains at the base of the bud as the bud grows and ultimately forms part of the bud scar marking the division site on the mother cell (PubMed:2050738). Also catalyzes the synthesis of chitin laid down during mating and spore cell-wall synthesis (PubMed:2050737, PubMed:2050738, PubMed:1293886).
Was originally thought that the N- and C-termini were extracellular (PubMed:16847258). However, more recent data suggests that the N- and C-termini are cytoplasmic (PubMed:28346351).
Putative transcription factor that functions in pseudohyphal growth.
Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively) (PubMed:332086). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:332086).
In yeast there are three glucose-phosphorylating isoenzymes, designated hexokinase I, II and glucokinase.
Subject to allosteric control. Substrate inhibition by ATP.
Putative transcription factor involved in halotolerance.
Interacts with mitochondrial outer membrane voltage-dependent anion channel (VDAC) POR1.
Membrane-bound O-acyltransferase involved in the remodeling of glycosylphosphatidylinositol (GPI) anchors. Acts only on GPI-anchored proteins, but not on free GPI lipids. Acts as an acyltransferase for GPI anchors that adds C26 fatty acids to the sn2 position of lyso-PI-containing GPI anchors. PER1 first deacylates, GUP1 subsequently reacylates the anchor lipid, thus replacing a shorter fatty acid (C16:0 or C18:0) by C26:0 (PubMed:16597698, PubMed:18036137). Also involved in lipid metabolism, having profound effects on sphingolipid-sterol-ordered domains integrity and assembly (PubMed:18786505). Together with GUP2, has an influence on the chemical composition of the yeast extracellular matrix (yECM) in yeast multicellular aggregates, such as biofilms and colonies (PubMed:25589358). Involved in cell integrity and apoptosis (PubMed:22617017, PubMed:30184078).
Results in an increase in triglyceride (TG) synthesis with a concomitant decrease in phospholipid (PL) synthesis and exhibits an altered plasma membrane lipid composition (PubMed:10747858). Shows defects in cell wall assembly and stability and abnormal cell wall morphology (PubMed:17042752). Deficient in GPI anchor remodeling, mutant cells only contain the primary, unremodeled phosphatidylinositol (PI) and are unable to attach remodeled PI or ceramides to the anchor (PubMed:16597698). Defective in sterol lipid distribution (PubMed:18786505).
Was originaly thought to be involved in active uptake of glycerol driven by electrogenic proton symport (PubMed:10931309), but has later been shown to be an acyltransferase and that effects on glycerol transport may be indirect (PubMed:10694878, PubMed:15381122).
Controls the pre-rRNA processing machinery in conjunction with IFH1. Presumably acts as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator.
Present with 23800 molecules/cell in log phase SD medium.
Substrate-binding subunit (component A) of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane.
Present with 14834 (+/-203) molecules/cell in log phase SD medium.
The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14. Component of the 1.8 MDa SAGA complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9.
Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines, but also purine-derived lesions, alkylation damage as well as abasic sites. Can also repair the oxidation products of 8-oxoguanine.
Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.
Greatly increases spontaneous and hydrogen peroxide-induced mutation frequency.
Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM7 family.
S-adenosyl-L-methionine-dependent protein methyltransferase that trimethylates the N-terminal glycine 'Gly-2' of elongation factor 1-alpha (TEF1 and TEF2), before also catalyzing the mono- and dimethylation of 'Lys-3' (PubMed:21858014, PubMed:26545399). May be involved in rDNA silencing and in lifespan determination (PubMed:12736687).
Was originally thought to be a nicotinamide N-methyltransferase.
Interacts according to large scale protein interaction studies with MEC3 and ULP1.
Belongs to the class VI-like SAM-binding methyltransferase superfamily. CHO2 family.
Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME). Preferentially converts di-C16:1 substrates.
Heterodimer with TFC8. Component of the TFIIIC complex composed of TFC1, TFC3, TFC4, TFC6, TFC7 and TFC8. The subunits are organized in two globular domains, tauA and tauB, connected by a proteolysis-sensitive and flexible linker. Interacts with TFC1, TFC3, TFC4 and directly with TFC8.
TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauB domain of TFIIIC that binds boxB DNA promoter sites of tRNA and similar genes. Cooperates with TFC3 in DNA binding.
Involved in osmoregulatory glycerol response, probably through its interaction with PLC1 which regulates the expression of GDP1.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YPR137C-A ORF.
Connects the ubiquitin pathway to autophagy by functioning as a ubiquitin-ATG8 adapter and thus mediating autophagic clearance of ubiquitin conjugates under starvation conditions. The CUE5-dependent selective autophagy pathway plays an important role in clearance of cytotoxic protein aggregates. Not required for cytoplasmic to vacuole pathway (cvt), mitophagy, pexophagy, or ribophagy.
Interacts with ATG8 (via AIM motif), CLB2, and ubiquitin (via CUE domain).
The ATG8-interaction motif (AIM) is required for the association with ATG8.
C-8 sterol isomerase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (Ref.5). ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol (Ref.5). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672).
Catalytic activity is inhibited by the morphilines tridemorph, fenpropimorph, and fenpropidin.
Expression is increased during ergosterol starvation, during anaerobic growth or in the presence of SR31747A, a sterol isomerase inhibitor (PubMed:10734216). Exogenously-supplied zymosterol is entirely transformed into ergosterol, which represses ERG2 expression (PubMed:10734216). However, exogenously-supplied ergosterol does not affect ERG2 expression (PubMed:10734216).
Causes only a modest decline in CLB2 cluster genes expression, but this expression is abolished when both FKH1 and FKH2 are deleted (PubMed:10959837). Leads to a defect in silencing HMRa (PubMed:10747051). Causes a form of yeast pseudohyphal growth, when FKH2 is also deleted (PubMed:10747051). Affects cell-cycle progression and CLB2 mRNA expression (PubMed:10747051).
Interacts with MCM1 (PubMed:10959837). Interacts with NDD1 (PubMed:12865300). Interacts with the origin recognition complex (ORC) composed of ORC1 to ORC6 (PubMed:22265405).
The FHA domain is necessary for the interaction with NDD1.
Transcription factor that regulates the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle (PubMed:10959837, PubMed:10894548, PubMed:10894549, PubMed:11562353, PubMed:12702877, PubMed:17283050, PubMed:24504085). The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20 as well as SWI5 and ACE2, transcription factors required for the subsequent temporal wave of cell cycle regulated gene expression in the M/G1 phase interval (PubMed:10959837, PubMed:10894548, PubMed:11562353). Involved in HMRa silencing (PubMed:10747051). FKH1 and FKH2 associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing (PubMed:12702877). Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation (PubMed:22438832). FKH1 and FKH2 function also in controlling yeast cell morphology by preventing preudohyphal growth (PubMed:10747051, PubMed:10894548). Acts as a rate-limiting replication origin activator via its interactin with the origin recognition complex (ORC) (PubMed:22265405, PubMed:26728715).
Regulates exocytosis by functioning as a GAP for SEC4. Stimulates specifically the GTPase activity of YPT6. Also required for efficient polarization of the actin patches.
Present with 124000 molecules/cell in log phase SD medium.
Belongs to the TRAPP small subunits family. BET3 subfamily.
Belongs to the AB hydrolase superfamily. AB hydrolase 4 family.
Displays enzymatic activity both for medium-chain fatty acid (MCFA) ethyl ester synthesis and hydrolysis (esterase activity). MCFA are toxic for yeast and this enzyme could thus be involved in their detoxification by esterification.
Belongs to the UPL family. TOM1/PTR1 subfamily.
Interacts with the ADA3/NGG1 subunit of the SAGA complex. Interacts with KRR1.
Probable ubiquitin ligase protein involved in many cellular processes, such as transcription regulation, maintenance of nuclear structure, cell cycle, mRNA export and rRNA maturation. E3 ubiquitin ligase proteins mediate ubiquitination and subsequent proteasomal degradation of target proteins. Involved in transcription regulation by interacting, and probably mediating, ubiquitination of some subunit of the SAGA complex. Required for SPT7 ubiquitination. Participates in mRNA export from the nucleus by regulating the transport of hnRNP proteins. Required for the shuttling of hnRNP protein NAB2, probably by mediating ubiquitination of a protein associated with NAB2. Also required for full induction of the general stress and heat-shock responses. Involved in 18S rRNA maturation by affecting several early steps in the rRNA processing pathway.
Could be involved in late stage of protein degradation.
Cell wall biogenesis protein that participates in the organization of the beta-glucan assembly (PubMed:27246500). Involved in the mechanism responsible for cell tolerance to polyhexamethylene biguanide (PHMB), an antifungal agent (PubMed:27246500).
Positively regulated by cell integrity signaling through MPK1 in response to cell wall perturbation (PubMed:10594829, PubMed:11016834). Induction is dependent on transcription factor RLM1 (PubMed:10594829, PubMed:11016834). Expression is also up-regulated 7-fold upon exposure to polyhexamethylene biguanide (PHMB) (PubMed:27246500).
Reduces significantly the growth rate of cells exposed to polyhexamethylene biguanide (PHMB) (PubMed:27246500). Leads to increased resistance to zymolyase treatment, indicating alterations in the beta-glucan network (PubMed:27246500).
Belongs to the mitochondrion-specific ribosomal protein mL67 family.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (PubMed:25609543, PubMed:24675956). mL67/MHR1 also has extraribosomal functions, being involved in regulation of mitochondrial DNA recombination, maintenance and repair, and generation of homoplasmic cells (PubMed:11121487, PubMed:12198175, PubMed:14565971, PubMed:16337661, PubMed:7664749, PubMed:9736700). mL67/MHR1 also acts as transcription factor involved in regulation of RNA polymerase II-dependent transcription (PubMed:12034822).
Beta subunit of the SNF1 kinase complex, which is required for transcriptional, metabolic, and developmental adaptations in response to glucose limitation. Has a structural role, mediating heterotrimer formation, and a regulatory role, defining carbon source-regulated subcellular location and substrate specificity of the SNF1 kinase complex. Promotes the PKA-regulated relocalization of the SNF1 kinase complex to the vacuolar membrane in response to various types of carbon stress.
Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
There are two genes coding for OPRT in yeast.
Belongs to the uridine kinase family. NRK subfamily.
Catalyzes the phosphorylation of nicotinamide riboside (NR) and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN).
Component of the RAD24-RFC complex which consists of RAD14, RFC2, RFC3, RFC4 and RFC5 and associates with the checkpoint clamp DDC1:MEC3:RAD17 complex. RAD24 interacts with ECO1.
Participates in checkpoint pathways arrest of the cell cycle, a mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. Regulates the DNA damage checkpoint pathway throughout the cell cycle, when associated with RCF5. Component of the RFC-like RAD24-RFC complex which loads the checkpoint clamp DDC1:MEC3:RAD17 complex and is involved in DNA repair pathways. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA.
Component of the SUMO-targeted ubiquitin ligase (STUbL) complex SLX5/SLX8 that mediates ubiquitination and subsequent desumoylation of sumoylated proteins and proteins containing SUMO-like domains for their degradation (PubMed:11139495, PubMed:16325482, PubMed:18032921, PubMed:17669696, PubMed:17848550, PubMed:18499666, PubMed:18948542, PubMed:31015336). The STUbL complex SLX5/SLX8 stimulates ubiquitin conjugating enzymes, including UBC1, UBC4, UBC5 and UBC13-MMS2, and mediates the proteolytic down-regulation of sumoylated proteins (PubMed:18032921). The STUbL complex SLX5/SLX8 is involved in ubiquitin-mediated degradation of histone variant CSE4, preventing mislocalization to euchromatin (PubMed:26960795). The complex plays an essential role in maintenance of chromosome stability and links SUMO-dependent ubiquitination to a centromere-specific function during mitosis (PubMed:23785440). The complex is involved in proteolysis of spindle positioning protein KAR9 and ensures correct spindle function by regulating levels of microtubule-associated proteins (PubMed:26906737). During replication, the complex helps to prevent DNA lesions via recombination and has a role in localizing the DNA damage protein DCD2 (PubMed:16325482, PubMed:17591698). The complex especially ubiquitinates the nuclease YEN1 and prevents persistent accumulation of a fraction of YEN1 associated with sites of activity in late G2/M and helps maintain the balance between pro- and anti-crossover pathways during homologous recombination (PubMed:30479332). It is also involved in ubiquitin-mediated degradation of DNA repair proteins RAD52 and RAD57 (PubMed:18032921). Finally, the complex is recruited to distinct genomic hotspots of non-H2B protein ubiquitination (ub-hotspots) by the sumoylated transcription factor-like protein EUC1 where it ubiquitinates EUC1 and presumably other targets (PubMed:31015336).
Component of the heterodimeric SUMO-targeted ubiquitin ligase (STUbL) complex composed of SLX5 and SLX8.
Required for nuclear fusion, chromosome disjunction, and nuclear segregation during mitosis. Probably required for the formation or stabilization of microtubules during mitosis and for spindle pole body fusion during conjugation.
Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway. Also catalyzes the conversion of O-acetylserine (OAS) into cysteine, the last step in the cysteine biosynthesis pathway (PubMed:7765825, PubMed:4609980, PubMed:795806). However, it seems that in S.cerevisiae cysteine biosynthesis occurs exclusively through the cystathionine pathway and not via direct incorporation of sulfur into OAS (PubMed:1732168). It therefore has no metabolic role in cysteine biosynthesis and may only have a regulatory role controlling OAS levels (PubMed:12586406).
Autophosphorylation increases in response to DNA damage.
Interacts with the PAB-dependent poly(A)-nuclease (PAN) complex regulatory subunit PAN3 via its forkhead-associated (FHA) domain.
Transducer of the DNA damage signal. Phosphorylates SML1 on serine residues. Cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress.
Interacts with profilin at the FH1 domain.
May organize microtubules by mediating spindle positioning and movement in the budding process. Potential target of the RHO family members (By similarity).
NAD-dependent (R,R)-butanediol dehydrogenase which catalyzes oxidation of (R,R)-butane-2,3-diol to (3R)-acetoin, of meso-butanediol to (3S)-acetoin, and reduction of acetoin. Allows the use of 2,3-butanediol as an aerobic carbon source.
Present with 8730 molecules/cell in log phase SD medium.
Transcription factor that regulates pseudohyphal differentiation, invasive growth, floculation, adhesion and starch metabolism in response to nutrient availability.
Positive regulatory factor required for depression of the coregulated phospholipid biosynthetic enzymes. Also involved in the expression of ITR1.
By furfural and 5-hydroxymethylfurfural (HMF).
NADPH-dependent aldehyde reductase involved in the detoxification of aldehyde inhibitors derived from lignocellulosic biomass conversion. Reduces commonly detected inhibitors in biomass conversion hydrolysates such as furfural, 5-hydroxymethylfurfural (HMF), cinnamic aldehyde, benzaldehyde, phenylacetaldehyde, and anisaldehyde.
Interacts with LOC1, NOP12, SIZ2, ULS1 and WSS1.
Required for the processing of the 27S pre-rRNA. Probably involved in the step of the processing of the 27 SA precursor into the 27 SB intermediate.
Stimulates the GTPase activity of BUD1/RSR1. Participates in the regulation of bud-site selection.
Associates with nucleolar pre-ribosomal particles. Interacts with DBP6. Together with DBP6, NOP8, URB1 and URB2, forms an RNA-independent complex, which is required during early maturation of nascent 60S ribosomal subunits.
Required for efficient biogenesis of the 60S ribosomal subunit.
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
DNA-dependent ATPase. Required in the control of double strand breaks transition and crossover during meiosis. Unwinds DNA in the 3' TO 5' direction. Prefers single-stranded DNA.
Expression is induced by the presence of aromatic amino acids and the lack of preferred nitrogen sources (e.g. ammonia, glutamine) and requires the transcription activator ARO80.
Fusel oils are important flavor and aroma compounds in yeast-fermented products contributing to the quality of beverages and food. In low concentration they are generally desirable, whereas high concentrations may spoil the product. By adjusting growth conditions and substrate their production is sought to be influenced. Phenylethanol, having a rose-like aroma, is an important fragrance in the cosmetic industry and can be produced by fermentation.
One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-acids). In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids derived from phenylalanine (phenylpyruvate), tryptophan (3-(indol-3-yl)pyruvate), and probably tyrosine (4-hydroxyphenylpyruvate), but also isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate) and methionine (4-methylthio-2-oxobutanoate), whereas transaminated leucine (4-methyl-2-oxopentanoate, also alpha-keto-isocaproate) is a low efficiency substrate and transaminated valine and pyruvate are no substrates. In analogy to the pyruvate decarboxylases the enzyme may in a side-reaction catalyze condensation (or carboligation) reactions leading to the formation of 2-hydroxy ketone, collectively called acyloins.
Component of the heterotrimeric Ssh1 complex, which is composed of SSH1, SBH2 and SSS1.
Part of the Ssh1 complex, which probably is the major component of a channel-forming translocon complex that may function exclusively in the cotranslational pathway of protein endoplasmic reticulum (ER) import.
Non-catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:2141385). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:2141385).
Present with 131000 molecules/cell in log phase SD medium.
PubMed:1371275 sequence was incorrectly thought to originate from bovine.
Component of the Golgi-associated retrograde protein (GARP) complex, also called VFT (VPS fifty-three) complex, composed of VPS51, VPS52, VPS53 and VPS54. Interacts also with TLG1 and YPT6.
Involved in retrograde transport from early and late endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1 to the Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles. May also be involved in the actin cytoskeleton organization.
By mating pheromones. By cells of the opposite mating type.
Required for efficient mating. Plays a role in maintenance of cell wall integrity during mating. Important for mating cell projection shape and conjugation bridge diameter. Plays a role in cell fusion and nuclear migration.
Acts as a mitochondrial iron-sulfur (Fe-S) cluster assembly factor that facilitates [4Fe-4S] cluster insertion into a subset of mitochondrial proteins such as lipoyl synthase (LS) and succinate dehydrogenase (SDH) (PubMed:27532772). Required during the last step of iron-sulfur protein assembly when the iron-sulfur cluster is inserted into the target protein (PubMed:27532772). Probably acts together with the monothiol glutaredoxin GRX5, earlier than BOL3 and NFU1 in the [4Fe-4S] cluster insertion process (PubMed:27532773). Not required for [2Fe-2S] cluster insertion into mitochondrial proteins (PubMed:27532772).
No visible phenotype (PubMed:27532773, PubMed:27532772). Cells lacking BOL1 and BOL3 display defects in a subset of mitochondrial [4Fe-4S] enzymes (PubMed:27532772).
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). Required for proper protein synthesis within the mitochondrion.
Protein kinase which is essential for the initiation of meiosis and sporulation.
Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Together with cyclin PCL8, negatively controls glycogen accumulation under favorable growth conditions. The PCL10-PHO85 cyclin-CDK holoenzyme has glycogen synthase kinase activity and phosphorylates and negatively regulates glycogen synthase GSY2. Also has minor GLC8 kinase activity.
Forms a cyclin-CDK complex with PHO85. Interacts with GSY2, independent of the presence of PHO85.
Belongs to the cyclic nucleotide phosphodiesterase class-II family.
Controls the level of cAMP in yeast cells, together with the high-affinity cAMP phosphodiesterase (PDE2).
Expressed in daughter cells after execution of mitotic exit. Expression is controlled by the ACE2 and SWI5 transcription factors.
Negative regulator of the mitotic exit network (MEN), required for multiple cell cycle checkpoints. Acts in the daughter cell to inhibit the mitotic exit pathway once MEN has executed its function. Through its binding ability to TEM1, interferes with the TEM1-CDC5 association, required for CDC5 kinase activation and MEN activation. Required for daughter cell separation and chromosome stability. Involved in copper sensitivity.
E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit.
Phosphorylated at Ser-313 by pyruvate dehydrogenase kinases PKP1 (PDK1) and PKP2 (PDK2), and dephosphorylated by pyruvate dehydrogenase phosphatases PTC5 and PTC6.
Present with 100000 molecules/cell in log phase SD medium.
Confers sensitivity for growth for cadmium, manganese, nickel, selenium and iron.
Vacuolar transporter which plays a role in sequestration of divalent heavy metal ions.
AGC kinase which plays a role in TOR complex 1 (TORC1) signaling pathway which mediates temporal control of cell growth in response to nutrients (PubMed:11062466). Required for phosphorylation of ribosomal protein S6 (RPS6A/RPS6B) at 'Ser-232' and 'Ser-233' (PubMed:25767889).
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily.
Belongs to the PIGG/PIGN/PIGO family. PIGO subfamily.
Involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI third mannose which links the GPI-anchor to the C-terminus of the proteins by an amide bond. Involved in cell wall biosynthesis.
Belongs to the BUR kinase complex composed of SGV1/BUR1 and BUR2. Interacts with BUR2 and RBP1.
Serine/threonine-protein kinase component of the BUR kinase complex involved in transcription regulation. This complex phosphorylates 'Ser-120' of the UBC2/RAD6 ubiquitin-conjugating enzyme (E2), leading to monoubiquitination of histone H2B, the localization of the PAF1 complex to the chromatin, and the silencing of telomeric-associated genes. Also required for histone H3 'Lys-4' trimethylation. May phosphorylate the 'Ser-5' of the RBP1 carboxy-terminal domain (CTD) repeats. Necessary for the recovery from pheromone-induced growth arrest in the cell cycle G1 phase. The kinase activity of the complex requires the presence of BUR2.
Deletion, when combined with a conditional mutation in clathrin heavy chain or deletion of GGA genes, accentuates growth defects and increases disruption of clathrin-dependent alpha-factor maturation and transport of carboxypeptidase Y to the vacuole. Causes mislocalization of AP-1, especially in cells at high density (postdiauxic shift), but doesn't affect GGA protein distribution. Sensitive to diltiazem-HCl and hypersensitive to chlorpromazine.
Interacts with the clathrin-associated adapter complex AP-1.
Involved in the trans-Golgi network (TGN)-endosome transport. Important for the correct localization of the adapter protein complex AP-1.
Belongs to the PHP hydrolase family. HisK subfamily.
Activates the transcription of lysine biosynthesis genes. This activation is dependent on the inducer alpha-aminoadipate semialdehyde and repressed by lysine.
Required for hydroxylation of C-4 in the sphingoid moiety of ceramide. Catalyzes the conversion of sphinganine to phytosphingosine in sphingolipid biosynthesis. Involved in the response to syringomycin.
Forms a complex with 2 TSA2 subunits. Binds phosphatidylinositol (PtdIns).
Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Activates SPO14/PLD1 (phospholipase D1) by stimulating phosphoinositide synthesis via the STT4 PtdIns 4-kinase. Modulates ArfGAP function through effects on SPO14 activity. Inhibits phosphatidylcholine degradation by PLB1 (phospholipase B1). May also regulate post-Golgi membrane-trafficking events and have a role resistance to oxidative stress. Inhibits fatty acid synthase activity in response to heme depletion and oleic acid starvation, preventing saturated fatty acid (SFA) accumulation (PubMed:17803462).
Involved in glycoprotein quality control as it is important for the targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations it further trims the carbohydrates to Man(5)GlcNAc(2).
Present with 8260 molecules/cell in log phase SD medium.
Belongs to the diacylglycerol acyltransferase family.
Catalyzes the terminal and only committed step in triacylglycerol (TAG) synthesis by using diacylglycerol (DAG) and fatty acyl-CoA as substrates. Required for storage lipid synthesis. Major DAG esterifying enzyme in stationary phase when TAG production is particularly active. Involved in lipid particle synthesis from the endoplasmic reticulum, promoting localized TAG production at discrete ER subdomains, and in ergosterol biosynthesis (PubMed:11741946, PubMed:11751830, PubMed:11751875, PubMed:14640980, PubMed:15155725, PubMed:21321129, PubMed:32349126). Also has monoacylglycerol acyltransferase (MGAT) activity, catalyzing the acyl-CoA-dependent esterification of monoacylglycerol to diacylglycerol (PubMed:20554061). Can also utilize ceramide instead of DAG, acylating the ceramides by attaching a fatty acid to the hydroxy group on the first carbon atom of the long-chain base to produce 1-O-acylceramides (PubMed:22738231).
Component of the retromer complex which consists of VPS29, VPS26, VPS35, VPS5 and VPS17. Component of a retromer subcomplex consisting of VPS29, VPS26 and VPS35.
Plays a role in vesicular protein sorting. Required for the endosome-to-Golgi retrieval of the vacuolar protein sorting receptor VPS10. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. The VPS29-VPS26-VPS35 subcomplex may be involved in cargo selection.
Could be involved in a ubiquitin-related process important for DNA damage tolerance.
Histone chaperone that stabilizes pre-existing histone tetramers and regulates replication-independent histone exchange on chromatin (PubMed:26109053). Required for normal chromatin refolding in the coding region of transcribed genes, and for the suppression of spurious transcription (PubMed:26109053). Global regulatory protein that plays positive as well as negative regulatory roles in transcription (PubMed:2072912).
Interacts with tetramers formed by histone H3 and H4 (PubMed:26109053). Interacts with SAP1 and CDC23 (PubMed:8654588, PubMed:8710860). Component of the SAGA complex, a large multiprotein complex that modifies the chromatin, at least composed of SPT2, SPT7, SPT8, SPT20/ADA5, HFI1/ADA1, ADA2, ADA3/NGG1, TRA1 and GCN5 (PubMed:9885573).
The acidic C-terminal domain mediates interaction with histone H3/H4 complexes.
Induced during anaerobic growth and strongly by cold shock.
Catalyzes the NAD(+)-dependent conversion of homoisocitrate to alpha-ketoadipate.
Inhibited by the reaction product NADH. Inhibited by oxalate; this is a non-competitive inhibitor.
Present with 19079 molecules/cell in log phase SD medium.
Component of the chromatin-remodeling INO80 complex, at least composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3, IES4, IES6, ACT1, IES2, IES5 and INO80. Exists as monomers and dimers, but the dimer is most probably the biologically relevant form required for stable interactions with histones that exploits the twofold symmetry of the nucleosome core (By similarity).
Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin remodeling complex. Exhibits low basal ATPase activity, and unable to polymerize. Strongly prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting it may act as a nucleosome recognition module within the complex.
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation (Potential). Binds to the 18S rRNA but non-specifically (PubMed:10085088).
Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is essential for mitotic growth and for repression of CHA1 expression.
Dimerizes via the C-terminal coiled coil. Interacts directly with HTL1, NPL6, RSC6 and the N-terminus of STH1. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin.
Pseudouridylate synthase responsible for the pseudouridine-2819 formation in mitochondrial 21S rRNA. May modulate the efficiency or the fidelity of the mitochondrial translation machinery.
Belongs to the GTP-binding SRP family. SRP54 subfamily.
Fungal signal recognition particle (SRP) complex consists of a 7S RNA molecule (scR1) and at least six protein subunits: SRP72, SRP68, SRP54, SEC65, SRP21 and SRP14. SRP54 interacts with SRP101.
Has a two domain structure: the G-domain binds GTP; the M-domain binds the 7S RNA and also binds the signal sequence.
Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the arrest of nascent chain elongation during membrane targeting. SRP54 binds to the signal sequence of presecretory protein when they emerge from the ribosomes. SRP54 interacts with the scR1 RNA and mediates the association of the resulting SRP-RNC complex with the signal recognition particle receptor (SR) via its alpha subunit SRP101. Both, SRP54 and SRP101, are locked in their GTP bound forms in the SRP-RNC-SR complex, which dissociates upon transferring the signal sequence to the protein-conducting channel (translocon). After signal sequence transfer, SRP54 and SRP101 act as reciprocal GTPAse-activating proteins (GAPs), thereby resolving their association.
DNA polymerase alpha mutation suppressor.
Involved in RNA splicing. Is required for the association of U4/U6 snRNP with U5 snRNP in an early step of spliceosome assembly.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. TRM10 family.
S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNAs.
Belongs to the proteasome subunit S1 family.
Required for cell cycle progression. Has a role in the completion of START.
Belongs to the V-ATPase V0D/AC39 subunit family.
Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:8509410). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:8509410). This subunit is a non-integral membrane component of the membrane pore domain and is required for proper assembly of the V0 sector (PubMed:8509410). Might be involved in the regulated assembly of V1 subunits onto the membrane sector or alternatively may prevent the passage of protons through V0 pores (PubMed:8509410).
Acts as an alpha-ketoglutarate-dependent dioxygenase active on sulfonates. Although taurine is a poor substrate, a variety of other sulfonates are utilized, with the best natural substrates being isethionate and taurocholate.
Forms a redox-dependent disulfide bond, which plays a structural role and regulates its conformational stability and activity.
Protease activity is induced in response to various mitochondrial stress, such as changes in membrane potential, oxidative stress or chronic hyperpolarization, and depends on its C-terminal region.
Protease that is part of the quality control system in the inner membrane of mitochondria (PubMed:12963738, PubMed:22219186, PubMed:24648523, PubMed:27325672). Activated in response to various mitochondrial stress, leading to the proteolytic cleavage of target proteins, such as OXA1 and COX1 (PubMed:12963738, PubMed:22219186, PubMed:24648523). Cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins (PubMed:12963738, PubMed:27325672). Cleaves the misfolded multi-pass membrane protein OXA1 (PubMed:12963738). Involved in quality control of cytochrome oxidase assembly: mediates the cleavage of COX1 in cells lacking COA2 (PubMed:22219186). Required for the stability of the respiratory supercomplexes (PubMed:26365306). Required for TOR signaling (PubMed:27325672).
Reduced ability to form viable colonies on glucose medium after acute treatment with hydrogen peroxide or chronic exposure to carbonyl cyanide m-chlorophenylhydrazone (CCCP) (PubMed:24648523). Cells are resistant to rapamycin and display reduced TOR signaling (PubMed:27325672). Oxidative-stress response is impaired (PubMed:27325672).
Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, TRA1 and YNG2. Interacts with SWC4.
Belongs to the Mediator complex subunit 31 family.
Involved in chromosome segregation during meiosis. Promotes efficient recombinational repair and functions in the protection of the genome from spontaneous and induced DNA damage like mutations and gross chromosomal rearrangements (GCRs).
Belongs to the Mediator complex subunit 12 family.
Component of the SRB8-11 complex which consists of SRB8, SSN2/SRB9, SSN3/SRB10 and SSN8/SRB11. The SRB8-11 complex associates with the Mediator complex. The SSN3/SRB10 and SSN8/SRB11 kinase-cyclin pair also associate with the RNA polymerase II holoenzyme.
Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The SRB8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II RPB1 at serines 2 and 5.
Cytoplasmic isozyme of C-1-tetrahydrofolate synthase. The trifunctional enzyme catalyzes the interconversion of the one-carbon derivatives of tetrahydrofolate (THF) between different oxidation states by the enzymatic activities 10-formyltetrahydrofolate synthetase, 5,lO-methenyltetrahydrofolate cyclohydrolase, and 5,lO-methylenetetrahydrofolate dehydrogenase. Involved in the generation of one-carbon intermediates in the biosynthesis of the purine bases.
Belongs to the ABC transporter superfamily. ABCB family. Mitochondrial peptide exporter (TC 3.A.1.212) subfamily.
Belongs to the helicase family. UvrD subfamily.
Required for mitochondrial genome maintenance and mitochondrial DNA inheritance.
Belongs to the biotin--protein ligase family.
Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl-CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase.
Belongs to the proteasome subunit S9 family.
Component of the lid subcomplex of the 19S proteasome regulatory particle complex (also named PA700 complex). The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits.
Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, RPN6 is required for proteasome assembly.
Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, TRA1 and YNG2. Component of the NuA3 complex, composed of at least NTO1, SAS3, TAF14, YNG1 and EAF6.
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Component of the NuA3 histone acetyltransferase complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation.
Three distinct zinc-containing RNA polymerases are found in eukaryotic nuclei: polymerase I for the ribosomal RNA precursor, polymerase II for the mRNA precursor, and polymerase III for 5S and tRNA genes.
Calcium-permeable, cation-selective stretch-activated channel (SAC). Required for calcium influx and for vitality of MATa cells in a late, pheromone-induced event of the mating process requiring calcium induced signaling. Functions together with CCH1 to ensure that adequate levels of Ca(2+) are supplied to PMR1 to sustain secretion and growth. Required for growth in low-calcium environments. Together with CCH1, essential for tolerance to iron stress, which leads to an increased oxidative poise, and to cold stress.
Interacts with CCH1 to form a Ca(2+) influx channel. Forms an oligomer with a molecular mass of 200 kDa by disulfide bonds.
Truncation mutant consisting of amino acids 1-360 is fully functional. Truncation mutants consisting of amino acids 1-400 and 1-22 are partially functional. Truncation mutants consisting of amino acids 1-455, 1-133, and a mutant in which amino acids 3-22 are deleted, are not functional in Ca(2+) uptake.
Arginine attenuator peptide (AAP) that has a regulatory role in the production of arginine-specific carbamoyl phosphate synthetase. Encoded by an upstream open reading frame (uORF) within the 5'-leader region of arginine-specific carbamoyl phosphate synthetase small chain (CPA1) mRNA, it attenuates the translation of the downstream CPA1 ORF. In the presence of high concentrations of arginine, ribosomes translating the uORF encoding AAP stall at the termination codon, resulting in reduced translation from the downstream CPA1 initiation codon.
Belongs to the arginine attenuator peptide family.
Has a role in cell morphogenesis and cell fusion and may antagonize the PKC1 pathway.
Belongs to the proteasome subunit S11 family.
Present with 12400 molecules/cell in log phase SD medium.
Belongs to the Mediator complex subunit 13 family.
Phosphorylated. PKA-dependent phosphorylation at 'Ser-608' is enhanced by activation of the RAS signaling pathway.
Component of the homotypic vacuole fusion and vacuole protein sorting (HOPS) complex, which is composed of a core of the 4 class C Vps proteins PEP5/VPS11, PEP3/VPS18, VPS16, VPS33 associated to VAM6/VPS39 and VPS41/VAM2. HOPS associates with phosphoinositides and the PX domain of VAM7. Component of the class C core vacuole/endosome tethering (CORVET) complex, which is composed of a core of the 4 class C Vps proteins PEP5/VPS11, PEP3/VPS18, VPS16, VPS33 associated to VPS3/PEP6 and VPS8. Interacts with PEP3, PEP7 and VAM7. Interacts with the E2 ubiquitin-conjugating enzyme UBC4 and histones H3 and H4.
Required for vacuolar biogenesis and for trafficking of hydrolase precursors to the vacuole. Mediates transport at the vacuolar membrane where it may be responsible for tethering transport vesicles on the target membranes. It is required for gluconeogenic growth of yeast. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion (PubMed:3062374, PubMed:10978279, PubMed:10944212, PubMed:16601699). Acts as component of the CORVET complex that is required for transport between endosome and vacuole. CORVET is an effector for the endosomal Rab GTPase VPS21 (PubMed:17488625). Probable ubiquitin-protein ligase involved in the degradation-related ubiquitination of histones. Contributes to the post-translational regulation of histone protein levels by polyubiquitination of excess histones for subsequent degradation (PubMed:22570702).
Involved in protein translation. Together with DOM34, may function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs.
Present with 2750 molecules/cell in log phase SD medium.
Alpha-1,2-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth mannose to trimannosyl-GPIs during GPI precursor assembly. The presence of a fourth mannose in GPI is essential in fungi. Involved in plasmid maintenance with SMP2.
Belongs to the glycosyltransferase 22 family. PIGZ subfamily.
Belongs to the gamma-glutamylcyclotransferase family. ChaC subfamily.
Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. Allows utilization of gluthathione through subsequent cleavage of the Cys-Gly dipeptide by Cys-Gly metallodipeptidase DUG1.
It is uncertain whether Met-1 or Met-59 is the initiator.
Phosphoinositide phosphatase which catalyzes the hydrolysis of phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P) (PubMed:10625610, PubMed:11792713). Has low activity towards phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) (PubMed:10625610). May be involved in the coordination of the activities of the secretory pathway and the actin cytoskeleton (PubMed:11514624).
Present with 48000 molecules/cell in log phase SD medium.
Probable protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP42 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation.
Interacts with SKP1. Component of the probable SCF(MDM30) complex containing CDC53, SKP1, RBX1 and MDM30. Interacts with SKP1 and FZO1.
Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins (By similarity). Recognizes FZO1 and regulates the amount of FZO1. Regulatory factor for the mitochondrial fusion machinery. Required for mitochondrial DNA maintenance.
Negative regulator of PRP3 and PRP4 genes.
Component of the RNA polymerase II holoenzyme. Interacts with RPO21 and SSN8.
Phosphorylated in response to various stresses. stress-induced phosphorylation is partially dependent on HOG1.
Positive regulator of FPS1 glycerol channel required for the glycerol efflux. As a component of the RNA polymerase II holoenzyme, is required for SSN8 destruction in response to oxidative stress but not heat shock. Required for cell survival in response to heat shock independent of SSN8.
Present with 10100 molecules/cell in log phase SD medium.
Was originally thought to be the ubiquinone-binding protein (QP-C).
Probable constituent of the synaptonemal complex during meiosis. May interact with RED1.
Reduces aromatic alpha-keto amides, aliphatic and aromatic alpha-keto esters, but not beta-keto esters.
Transiently induced shortly after the switch from aerobic to anaerobic growth (at protein level).
Interacts with UBC2. Interacts with RPN2, RPT1 and RPT6 from the 26S proteasome.
Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
Present with 477 molecules/cell in log phase SD medium.
Acts a component of the ESCRT-III complex required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB) (PubMed:11559748, PubMed:12194857). The sequential action of ESCRT-0, -I, and -II together with the ordered assembly of ESCRT-III links membrane invagination to cargo sorting (PubMed:12194857). Membrane scission in the neck of the growing vesicle releases mature, cargo-laden ILVs into the lumen (PubMed:24139821, PubMed:24711499). ESCRT-III is critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery (PubMed:24139821, PubMed:24711499). SNF7 is the most abundant ESCRT-III subunit which forms membrane-sculpting filaments with 30 Angstrom periodicity and a exposed cationic membrane-binding surface (PubMed:26670543). Its activation requires a prominent conformational rearrangement to expose protein-membrane and protein-protein interfaces (PubMed:26670543). SNF7 filaments then form spirals that could function as spiral springs (PubMed:26522593). The elastic expansion of compressed SNF7 spirals generates an area difference between the two sides of the membrane and thus curvature which could be the origin of membrane deformation leading eventually to fission (PubMed:26522593). SNF7 recruits BRO1, which in turn recruits DOA4, which deubiquitinates cargos before their enclosure within MVB vesicles (PubMed:11029042, PubMed:15935782). ESCRT-III is also recruited to the nuclear envelope (NE) by integral INM proteins to surveil and clear defective nuclear pore complex (NPC) assembly intermediates to ensure the fidelity of NPC assembly (PubMed:25303532).
Core component of the ESCRT-III complex (endosomal sorting required for transport complex III) (PubMed:12194857, PubMed:18854142). ESCRT-III appears to be sequentially assembled as a flat lattice on the endosome membrane and forms a transient 450 kDa complex that contains DID4, oligomerized SNF7, VPS20 and VPS24 (PubMed:18854142). SNF7 polymerizes into spirals at the surface of lipid bilayers (PubMed:26522593). SNF7 polymerization is nucleated by association of SNF7 with VPS20; the process is terminated through association of VPS24, possibly by capping the SNF7 filament (PubMed:24058170, PubMed:24711499). Interacts with VTA1; the interaction requires DID2 (PubMed:16601096, PubMed:24058170). Interacts with BRO1 (PubMed:15086794, PubMed:15935782, PubMed:24058170). Interacts with DOA4 (PubMed:26427873). Interacts with HEH1 and HEH2 (PubMed:25303532). Interacts with RIM20 and YGR122W (PubMed:24058170).
Exhibits defects in the sorting and processing of native vacuolar proteins (PubMed:3062374).
The N-terminus (residues 1 to 11) forms an amphipathic helix which is required for the association to membrane.
Was originally thought to be a nuclear protein and mutations were shown to prevent full derepression of the SUC2 (invertase) gene.
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NUP57 is part of the NUP57 subcomplex (NIC96, NSP1, NUP49, NUP57) interacting with NUP49 and NSP1. Interacts through its FG repeats with karyopherins.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP57 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, and pre-ribosome transport.
Present with 9310 molecules/cell in log phase SD medium.
Eukaryotic translation initiation factor 2 (eIF-2) is a heterotrimer composed of an alpha, a beta and a gamma subunit. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a multifactor complex (MFC) that may bind to the 40S ribosome.
Phosphorylated; phosphorylation on Ser-52 by the GCN2 protein kinase occurs in response to low amino acid, carbon, or purine availability.
eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.
4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by acpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group (By similarity).
Belongs to the acyl carrier protein (ACP) family.
Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity). May be involved in the synthesis of very-long-chain fatty acids. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity).
Complex I is composed of about 30 different subunits.
Present with 60500 molecules/cell in log phase SD medium.
By transcription factor MAC1 upon copper deprivation.
Cell surface metalloreductase. May be involved in copper homeostasis.
Component of a COP9 signalosome-like (CSN) complex, composed of RRI1/CSN5, CSN9, RRI2/CSN10, PCI8/CSN11, CSN12 and CSI1. Interacts with PRT1 and RPG1, 2 subunits of the core complex of translation initiation factor 3 (eIF3).
Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes The CSN complex is involved in the regulation of the mating pheromone response. PCI8 may also be involved in transcriptional and translational control.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.
Belongs to the SMC family. SMC4 subfamily.
Forms a heterodimer with SMC2. Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: BRN1, YCS4 and YCG1/YCS5.
The flexible SMC hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with SMC2, forming a V-shaped heterodimer.
Belongs to the bacterial ribosomal protein bL9 family.
Present with 92 molecules/cell in log phase SD medium.
The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble form, and which forms a parallel in-register beta-sheet in its amyloid form (By similarity). The first 37 residues of this domain are sufficient for aggregation, propagation, and transmission of the [SWI+] prion.
[SWI+] is the prion form of SWI1 (PubMed:18362884). [SWI+] is the result of a conformational change of the cellular SWI1 protein that becomes self-propagating and infectious. This conformational change generates a form of SWI1 that assembles into amyloid fibrils (PubMed:20679490). [SWI+]-aggregates sequester soluble SWI1, resulting in reduced growth on carbon sources other than glucose, reminiscent of a partial loss of function of the SWI/SNF chromatin-remodeling complex. [SWI+] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [SWI+] propagation (PubMed:18362884). [SWI+] propagation is highly dependent upon the action of members of the Hsp70 molecular chaperone system, specifically the Hsp70 SSA, two of its J-protein co-chaperones, SIS1 and YDJ1, and the nucleotide exchange factors of the Hsp110 family (SSE1/2). Both under- and overexpression of components of this system initiate rapid loss of the prion from the cell population. It is speculated that prion properties of transcription factors may generate an optimized phenotypic heterogeneity that buffers yeast populations against diverse environmental insults (PubMed:21379326).
Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. Interacts with NUM1.
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Binds 1 dipyrromethane group covalently.
Catalyzes the tetrapolymerization of the monopyrrole porphobilinogen (PBG) into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
The porphobilinogen subunits are added to the dipyrromethane group.
Involved in the guiding of mitochondrial tubules to the bud tip during cell division.
Phosphorylated by the cyclin-CDK PCL7-PHO85.
Belongs to the Mediator complex subunit 6 family.
Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. MED6 interacts directly with SRB4/MED17 and SRB7/MED21.
Present with 4824 molecules/cell in log phase SD medium.
Could be the product of a pseudogene. This is the C-terminal part of the ABC transporter NFT1. S288c has a stop codon in position 1219, which disrupts the gene coding for this protein and produces two ORFs YKR103W and YKR104W. A contiguous sequence for ABC transporter NFT1 can be found in strains Sigma 1278B, EG123 and SK1 (AC P0CE70).
Present with 6350 molecules/cell in log phase SD medium.
Belongs to the cytochrome c oxidase subunit 5B family.
Present with 9410 molecules/cell in log phase SD medium.
Abnormal activation of TORC1 signaling during high hydrostatic pressure (mechanical stress) (PubMed:32801125). Abnormal punctate localization of TOR1 (PubMed:32801125). Increases cellular levels of glutamine and alanine during high hydrostatic pressure (mechanical stress) (PubMed:32801125). Sensitive to rapamycin and high hydrostatic pressure (mechanical stress) (PubMed:29698392, PubMed:32801125). Simultaneous disruption of PIB2 results in loss of viability (PubMed:29698392).
Component of the GSE complex composed of GTR1, GTR2, SLM4, MEH1 and LTV1. Component of the EGO complex, at least composed of GTR2, SLM4 and MEH1.
Component of the GSE complex, a GTPase complex required for intracellular sorting of GAP1 out of the endosome (PubMed:16732272). Component of the EGO complex, a complex involved in the regulation of microautophagy (PubMed:15989961).
Belongs to the HAD-like hydrolase superfamily. SerB family.
Present with 13800 molecules/cell in log phase SD medium.
Guanine nucleotide-exchange factor (GEF) for RHO1 that stimulates the exchange of RHO1 GDP-bound form into GTP-bound form. Required for signaling of cell wall defects to RHO1.
The DH domain mediates interaction with RHO1.
Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate in the pyrimidine salvage pathway.
In response to the DNA-damaging agent MMS.
Involved in ER-associated protein degradation (ERAD).
ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair (PubMed:10952318, PubMed:12887900). Its ability to induce transcription of some phosphate-responsive genes is modulated by inositol polyphosphates (PubMed:10952318, PubMed:10361278). The INO80 complex is involved in DNA repair by associating with 'Ser-129' phosphorylated H2A histones as a response to DNA damage (PubMed:15607974, PubMed:15607975).
The DBINO region is involved in binding to DNA.
Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple spliceosome snRNP complexes containing the U6 snRNA (U4/U6 snRNP, U4/U6.U5 snRNP, and free U6 snRNP). It binds directly to the U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. It probably also is involved in degradation of nuclear pre-mRNA by targeting them for decapping. LSM4 binds specifically to the 3'-terminal U-tract of U6 snRNA. LSM2-LSM8 probably is involved in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM4, probably in a complex that contains LSM2-LSM7 but not LSM1 or LSM8, associates with the precursor of the RNA component of RNase P (pre-P RNA) and may be involved in maturing pre-P RNA. LSM4 is required for processing of pre-tRNAs, pre-rRNAs and U3 snoRNA.
Component of the heptameric LSM1-LSM7 complex that forms a seven-membered ring structure with a doughnut shape. The LSm subunits are arranged in the order LSM1, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. Except for LSM1, where a C-terminal helix crosses the ring structure to form additional interactions with LSM3 and LSM6, each subunit interacts only with its two neighboring subunits. The LSM1-LSM7 complex interacts with PAT1; within the complex PAT1 has direct interactions with LSM2 and LSM3. Component of the heptameric LSM2-LSM8 complex that forms a seven-membered ring structure with a doughnut shape; an RNA strand can pass through the hole in the center of the ring structure. The LSm subunits are arranged in the order LSM8, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. LSM2-LSM8 associates with PAT1 and XRN1. A complex comprising LSM2-LSM7 without LSM1 or LSM8 may exist. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
Interacts with MEI4, MER2 and REC104. Component of the MER2-MEI4-REC114 complex.
Required for the production of double-strand breaks (DSBs) in meiotic recombination initiation; not required for mitosis. Plays a role in activation of the DSB nuclease SPO11 at recombination hotspots. Prevents accumulation of meiotic double strand break intermediates and is needed for the proper timing of the first meiotic division. Component of the MER2-MEI4-REC114 complex which seems to be required for meiotic double-strand break (DSB) formation.
Homodimer. Interacts with BUG1 (via C-terminus), probably forming a heterooligomer consisting of a GRH1 dimer and a BUG1 dimer. Interacts with COPII coat components SEC23, SEC24, SFB2 and SFB3.
Involved in the spindle assembly checkpoint. Involved in ER to Golgi vesicle-mediated transport by either facilitating USO1-dependent and -independent tethering or increasing target accuracy of fusion events of COPII-coated vesicles.
N-terminal acetylation; by N-terminal acetyltransferase NatC.
Belongs to the eukaryotic RPC3/POLR3C RNA polymerase subunit family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.
Protein phosphatase with specificity for serine, threonine, and tyrosine residues; has a role in the DNA synthesis phase of the cell cycle.
Required for initiation of meiotic chromosome synapsis. Involved in synaptonemal complex formation, a structure that tethers a pair of homologous chromosomes along their lengths and plays a central role in recombination and homolog segregation during meiosis. Required for the normal localization of MSH4 to chromosomes.
Expression is dramatically increased under nitrogen starvation conditions and is regulated by the transcription factor GCN4 (PubMed:26565778).
Involved in both selective and non-selective autophagy (PubMed:26565778). Does not appear to play a role in determining the size of autophagosomes, but rather influences their formation rate (PubMed:26565778). With ATG9, plays a role in the delivery of donor membrane to expanding phagophore (PubMed:26565778).
Reduces the autophagy flux induced by nitrogen starvation as well as the flux of the cytoplasm-to-vacuole targeting (cvt) pathway (PubMed:26565778).
The C-terminal 10 residues are required for the association with ATG9 (PubMed:26565778).
Component of the 7-subunit TFIIH core complex composed of XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in NER. The core complex associates with the 3-subunit CTD-kinase module TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription (PubMed:15220919). Interacts with TFB2 (PubMed:19172752).
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription. TFB5 is required for stable recruitment of TFIIH to a promoter, but not for stability of TFIIH subunits.
Forms a transiant heterodimeric complex with DCK1, that acts as a guanine nucleotide exchange factor (GEF) for the small GTPase RHO5 (PubMed:25598154). DCK1, LMO1 and RHO5 relocate to mitochondria upon oxidative stress and trigger cell death (PubMed:25598154). The DCK1/LMO1/RHO5 signaling module mediates mitochondrial turnover under nitrogen starvation conditions via mitophagy (PubMed:25598154). The DCK1/LMO1/RHO5 signaling module also plays a role in cell wall integrity signaling (PubMed:25598154).
Leads to hyper-resistance to cell wall stress agents such as calcofluor white and Congo red.
Present with 42600 molecules/cell in log phase SD medium.
Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl diphosphate to proteins having the C-terminal sequence Cys-Ile-Ile-Leu or Cys-Val-Leu-Leu. Acts, among other substrates, on Rho1 and Rho2 and CDC42 proteins. Participates in a RAS-like C-terminal modification of proteins involved in nuclear division and bud growth. It is involved in bud positioning and cell polarity (PubMed:2034682, PubMed:1400380). The beta subunit is responsible for isoprenoid and peptide-binding (PubMed:9109664, PubMed:10491163).
Heterodimer of an alpha (RAM2) and a beta (CDC43) subunit.
Essential component of TORC2, which regulates cell cycle-dependent polarization of the actin-cytoskeleton and cell wall integrity. TORC2 controls polarity of the actin cytoskeleton, which is required for orienting the secretory pathway toward discrete growth sites, via the RHO1/PKC1/MAPK cell integrity pathway. TSC11 may exert its functions through two distinct mechanisms, one mediated by AVO1 and the other mediated by AVO2 and SLM1.
Phosphorylated by TOR2; when part of TORC2.
The target of rapamycin complex 2 (TORC2) is composed of at least AVO1, AVO2, BIT61, LST8, TOR2 and TSC11. TORC2 likely forms a homodimer. Contrary to TORC1, TORC2 does not bind to and is not sensitive to FKBP-rapamycin. TSC11 binds to the N-terminal HEAT repeat region in TOR2 and is required for TORC2 integrity by tethering AVO1 and AVO2 to the complex.
GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5).
In eukaryotes EC 6.3.5.5 is synthesized by two pathway-specific (arginine and pyrimidine) genes under separate control.
In the central section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.
Present with 11000 molecules/cell in log phase SD medium.
This protein is a 'fusion' protein encoding three enzymatic activities of the pyrimidine pathway (GATase, CPSase, and ATCase).
Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway (PubMed:2185248). Does not arginylate cysteine residues (By similarity).
Component of the oligosaccharyltransferase (OST) complex, which appears to exist in two assemblies comprising OST1, OST2, OST4, OST5, STT3, SWP1, WPB1, and either OST3 or OST6 (PubMed:8175708, PubMed:10677492, PubMed:16297388, PubMed:16096345, PubMed:15831493, PubMed:15886282, PubMed:9405463, PubMed:29301962). OST assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains OST1 and OST5, subcomplex 2 contains STT3, OST3, and OST4, and subcomplex 3 contains OST2, WBP1, and SWP1 (PubMed:29301962). Interacts with SEC61, SBH1 and SSS1 (PubMed:15831493).
May play a role in proper chromosome segregation. Suppresses the high-frequency loss of mini-chromosomes when overexpressed, and this suppression is completely dependent on silencing protein SIR4.
In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily.
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts by mediating the C-terminal thiocarboxylation of sulfur carrier URM1. Its N-terminus first activates URM1 as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 to form thiocarboxylation (-COSH) of its C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.
Associates with mRNPs. Interacts with YRA1.
Involved in export of poly(A) mRNAs from the nucleus. Recruited to the coding sequences as well as poly-A sites of active genes.
Component of the VPS34 PI3-kinase complex II composed of VPS15, VPS30, VPS34 and VPS38.
Involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through generating a specific pool of phosphatidylinositol 3-phosphate allowing the recruitment of the retromer complex proteins to the endosome). Mediates the interaction between VPS30 and the VPS34-VPS15 core complex, leading to the recruitment of VPS30 to the membrane.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YER137C-A ORF.
Required for a novel path of interorganelle communication between mitochondria, peroxisomes and the nucleus, thereby maintaining a functional metabolic interaction between the tricarboxylic acid and glyoxylate cycles. In particular, required for the retrograde expression of the peroxisomal isoform of citrate synthase, CIT2.
Involved in karyogamy. Component of a cortical adaptor complex that orients cytoplasmic microtubules. It may be involved in anchoring cytoplasmic microtubules to the cell cortex.
Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone KAR2.
Associated with nuclear form of the RNA exosome complex. Interacts with RRP4, RRP6, RRP45 and RRP46.
Required for exosome-dependent processing of pre-rRNA and small nucleolar RNA (snRNA) precursors. Involved in processing of 35S pre-rRNA at the A0, A1 and A2 sites. Required for activity of RRP6 in 7S pre-rRNA processing. Also has a role in 3'-processing of U4 and U5 small nuclear RNAs (snRNAs). Acts as a mRNA export factor. Mediates mRNA degradation upon UV irradiation. Maintains genome integrity where it is involved in both non-homologous end joining (NHEJ) and homologous recombination pathway repair of double strand DNA breaks. During NHEJ, required for joining 3'-overhanging ends. Also involved in telomere length regulation and maintenance.
Involved in double-strand break (DSB) formation during meiotic recombination through stabilization of SPO11 association with meiotic chromosome and helping SPO11 to recruit other DSB proteins like REC102 and REC104 to meiotic chromosomes. Also a component of the SKI complex involved in 3'-mRNA degradation pathway. Represses dsRNA virus propagation by specifically blocking translation of viral mRNAs, perhaps recognizing the absence of CAP or poly(A). Essential for controlling the propagation of M double-stranded RNA (dsRNA) and thus for preventing virus-induced cytopathology.
Component of very early pre-60S ribosomal particles containing 27SA2 pre-rRNA. Interacts with URB1. Together with DBP6, NOP8, URB1 and RSA3, forms an RNA-independent complex, which is required during early maturation of nascent 60S ribosomal subunits.
Required for 27S pre-rRNA processing. Has an early role during 60S ribosomal subunit assembly.
Product of a dubious gene prediction unlikely to encode a functional protein. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set.
Metalloreductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane (By similarity).
Dephosphorylation by SIT4 activates NPR1 kinase activity.
Hyperphosphorylated in nitrogen-rich growth medium. Nitrogen limitation (or rapamycin treatment) leads to substantial, though not complete dephosphorylation. Autophosphorylation plays only a minor role and seems not to be regulated by the quality of the nitrogen source.
Nutrient-regulated protein kinase that promotes the activity of at least 6 distinct transport systems for nitrogenous nutrients under conditions of nitrogen catabolite derepression. Under poor nitrogen growth conditions, required for post-Golgi sorting of the general amino acid permease GAP1 and the three known ammonia permeases, MEP1/2/3, to the plasma membrane. Contributes also to the stability and the retention of GAP1 at the plasma membrane. Inversely, promotes the degradation of tryptophan permease TAT2 under the same conditions. Activity is regulated by the TOR signaling pathway via phosphatase SIT4. Although thought to be involved in regulation of GLN3-dependent transcription by nitrogen catabolite repression, this seems to be an indirect effect from the reduced uptake of the nitrogen-repressing compound.
Involved in the structural organization of the cis-Golgi and in vesicle targeting/fusion stages of ER to Golgi transport.
The GRIP domain binds to ARF1, which leads to the Golgi localization of RUD3.
3' to 5' exoribonuclease required for proper 3' end maturation of MRP RNA and of the U5L snRNA.
Interacts with SIK1/NOP56 and NOP1. Interacts with the trimethylguanosine synthase TGS1. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.
Present with 34700 molecules/cell in log phase SD medium.
Required for pre-18S rRNA processing. May bind microtubules.
Interacts with the clathrin adapter GGA2 and the clathrin adapter complex AP-1.
Eukaryotic translation initiation factor 2 (eIF-2) is a heterotrimer composed of an alpha, a beta and a gamma subunit. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a multifactor complex (MFC) that may bind to the 40S ribosome. SUI3 interacts with GCD6 and TIF5/eIF-5.
eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.
Forms a ternary complex with intron derived RNA and the imported mitochondrial leucyl-tRNA synthetase NAM2. The proteins do not interact directly with each other.
Mitochondrial mRNA maturase required for splicing of intron 4 of the cytochrome b (COB) gene, containing its own coding sequence, and intron 4 in COX1, coding for the related homing endonuclease aI4. In vivo splicing requires in addition the imported mitochondrial leucyl-tRNA synthetase NAM2. Both proteins seem to stimulate the intrinsic ribozyme activity of intron bI4 through binding to and stabilizing specific secondary and tertiary structure elements in the RNA.
Residues 385 to 638 are sufficient for maturase activity.
The mature protein may arise from proteolytic cleavage of an in-frame translation of COB exons 1 to 4 plus intron 4, containing the bI4 open reading frame. Cleavage would take place close to the Met-385 resulting in an active maturase of about 30 kDa.
Low-affinity glucose transporter. Can also transport xylose.
Xylose uptake is strongly inhibited by glucose.
Interacts with HTA1 and associates with the spliceosome.
Involved in mRNA splicing. Required for snRNA accumulation and manufacture of snRNPs.
Catalyzes the final step in the CDP-choline route leading to phosphatidylcholin (PC). Preferentially uses CDP-monomethylethanolamine as aminoalcohol substrate. Shows highest activity toward di- and mono-unsaturated diacylglycerol species as lipid substrates. The CDP-choline pathway only contributes to net PC synthesis if exogenous choline is present. In its absence, this pathway recycles choline from PC turnover and may contribute to maintaining the proper PC species composition.
Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Together with cyclin PCL10, negatively controls glycogen accumulation under favorable growth conditions. Involved in phosphorylation and negative regulation of glycogen synthase GSY2. Also has minor GLC8 kinase activity.
Belongs to the threonine synthase family.
Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
Present with 26000 molecules/cell in log phase SD medium.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Catalyzes the attachment of aspartate to tRNA(Asp) in the mitochondrion.
Belongs to the gamma-glutamyl phosphate reductase family.
Catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
Catalyzes the dephosphorylation and concomitant reactivation of the E1 alpha subunit (PDA1) of the pyruvate dehydrogenase complex.
Present with 7550 molecules/cell in log phase SD medium.
Processed by mitochondrial inner membrane protease (IMP) complex and released to the intermembrane space.
Expressed periodically during cell division. Requires ACE2, CBK1, MOB2 and SWI5. Expression is also increased under microgravity conditions.
Involved in cell wall metabolism and required for the separation of the mother and daughter cells.
Present with 503000 molecules/cell in log phase SD medium.
By iron deprivation. Repressed by iron excess.
Iron transport multicopper ferroxidase required for Fe(2+) ion high affinity uptake. Required to oxidize Fe(2+) to Fe(3+), which is then transported into the cell via the ferric iron permease FTR1. Essential component of copper-dependent iron transport.
Mediates the hydrolysis of steryl esters. Required for mobilization of steryl ester, thereby playing a central role in lipid metabolism.
Regulates the cell cycle in a nutrient dependent manner. Accumulates in presence of nutrients and directs the destabilization of DMA1 and DMA2, whose accumulation results in a G1 block. Regulates also the abundance of GCD11 an essential component of the translational initiation factor 2.
Converts proline to delta-1-pyrroline-5-carboxylate.
Proline oxidase requires a functional electron transport chain aerobiosis for its activity.
The expression of proline oxidase is controlled by proline and oxygen.
Belongs to the eukaryotic RPA43 RNA polymerase subunit family.
Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA. Interacts with RPO26/ABC23 and with the initiation factor RRN3.
Contains an average of four phosphates per molecule.
DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. Through its association with RRN3 is involved in recruitment of Pol I to rDNA promoters. In vitro, the A13-A43 subcomplex binds single-stranded RNA.
Belongs to the DNA repair metallo-beta-lactamase (DRMBL) family.
Expression is increased by ultraviolet light and agents which induce DNA cross-links such as nitrogen mustard and psoralen.
Required for DNA interstrand cross-link repair. This requires cleavage of cross-linked DNA to generate DNA double strand breaks (DSBs). This protein has 5' exonuclease activity on single-stranded and double-stranded DNA, which appears to be necessary for the processing of DNA double strand breaks prior to ligation.
By transcription factor GCN4. Rapidly degraded under starvation conditions.
Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Positively controls degradation of transcription factor GCN4 under favorable growth conditions. The PCL5-PHO85 cyclin-CDK holoenzyme phosphorylates GCN4, which is required for its degradation by the E3 ubiquitin ligase complex SCF(Cdc4). Amino acid starvation reduces PCL5-PHO85-associated GCN4 kinase activity and leads to stabilization of GCN4.
Belongs to the DEAD box helicase family. DDX54/DBP10 subfamily.
Interacts with RRP1 and associates with pre-ribosomal particles.
Could be the product of a pseudogene. Transposon Ty4-P (YPLCTy4-1) contains a frameshift at position 1105, which disrupts the ORF coding for protein TY4B. It is probably not functional.
Proteolytically processed into capsid protein (CA), Ty4 protease (PR), integrase (IN) and reverse transcriptase/ribonuclease H (RT) proteins (By similarity). Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein, and this cleavage is a prerequisite for subsequent processing at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs.
Belongs to the DHHC palmitoyltransferase family. SWF1 subfamily.
Palmitoyltransferase that targets several endosomal SNAREs. Palmitoylates the SNAREs SNC1, SNC2, SYN8 and TLG1, at cysteine residues close to the cytoplasmic end of their transmembrane domain. May have a role in the cellular quality control of transmembrane domain-containing proteins.
Transcriptional inhibitor with a significantly increased number of target genes in response to oleate.
Belongs to the PEX28-32 family. PEX29 subfamily.
Activator protein that regulates the ubiquitin ligase activity and substrate specificity of the anaphase promoting complex/cyclosome (APC/C). Required for the ubiquitination and subsequent degradation of the B-type cyclin CLB1 by the APC/C complex during meiosis. Required for meiosis I, late meiotic gene expression and spore wall assembly.
Expressed and spliced only during meiosis dependent on the splicing factor MER1.
Becomes hyperphosphorylated when wild-type cells are arrested in mitosis. Phosphorylated by MPS1.
Central component of the spindle assembly checkpoint. Thought to recruit MAD2 to unattached kinetochores. During checkpoint activity, MAD2 is relayed from the MAD1-MAD2 complex to the mitotic checkpoint complex (MCC). The formation of a MAD1-BUB1-BUB3 complex seems to be required for the spindle checkpoint mechanism.
Forms a stable heteromer with MAD2 throughout the cell cycle. Part of complex consisting of MAD1, BUB1 and BUB3 after activation of spindle checkpoint.
By D-lactate. Induced during respiratory adaptation.
Catalyzes the stereospecific oxidation of D-lactate to pyruvate.
Required for normal rate of cell proliferation.
Involved in the nuclear retention of improperly spliced pre-mRNAs.
Alkyl/aryl-sulfatase. Enables the use of SDS and 4-nitrocatechol as sulfur source.
Belongs to the metallo-beta-lactamase superfamily. Type III sulfatase family.
Expression is increased in sulfur-limited chemostat cultures.
The presence of this bacterial-like protein in S.cerevisiae results probably from a recent horizontal gene transfer event.
Expression is induced in zinc-limited conditions by the zinc-responsive transcription factor ZAP1.
Reduces zinc transport into the vacuole and hence limits the over-accumulation of zinc caused by the deletion of ZRT3.
Vacuolar transporter that regulates zinc homeostasis by mediating zinc transport and storage into the vacuole (PubMed:2693940, PubMed:10856230, PubMed:11263974, PubMed:12161436, PubMed:12556516, PubMed:18930916). ZRC1 senses zinc availability in the cytosol, which might be performed through the histidine repeat motifs, and transports zinc from the cytosol to the vacuole if zinc in cytosol is abundant, confering resistance to zinc toxicity (PubMed:11263974). Plays a role in resistance to zinc shock resulting from sudden influx of zinc into cytoplasm when ZRT1 and ZRT2 are induced in response to zinc depletion (PubMed:11263974, PubMed:12556516).
ZRC1 has a paralog, COT1, that arose from the whole genome duplication.
Seems to be involved in cell wall organization and biogenesis.
May be involved in ion homeostasis together with BTN1 or BTN2.
Induced under aerobic conditions and by mild heat stress.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. ERF3 subfamily.
Heterodimer of two subunits, one of which binds GTP. Interacts with polyadenylate-binding protein PAB1, and TPA1.
Involved in translation termination. Stimulates the activity of ERF1. Binds guanine nucleotides. Recruited by polyadenylate-binding protein PAB1 to poly(A)-tails of mRNAs. Interaction with PAB1 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening.
[PSI+] is the prion form of SUP35 (PubMed:8978027). [PSI+] is the result of a conformational change of the cellular SUP35 protein that becomes self-propagating and infectious. This conformational change generates a form of SUP35 that assembles into amyloid fibrils. [PSI+]-aggregates sequester soluble SUP35, resulting in defects in faithful translation termination by read-through of translation termination codons (PubMed:8670813). [PSI+] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [PSI+] propagation (PubMed:9335589). It is speculated that the prion form would be at least mildly deleterious in most environments, but it might sometimes increase evolvability in certain harsh environments (PubMed:19917766).
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. NPR/HAL subfamily. HAL5 sub-subfamily.
Protein kinase involved in salt tolerance and pH sensitivity, probably by regulating plasma membrane potential and cation influx. Positively controls the TRK1-TRK2 potassium transport system in response to potassium starvation. Stabilizes TRK1 in the plasma membrane by preventing its vacuolar sorting and degradation. Also stabilizes other plasma membrane nutrient transporters like CAN1, FUR4 and HXT1. May itself be subject to regulation by ARL1.
Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor. Acetylation during GPI-anchor biosynthesis is not essential for the subsequent mannosylation and is usually removed soon after the attachment of GPIs to proteins.
Target of the antifungal compound 1-[4-butylbenzyl]isoquinoline that inhibits cell wall localization of GPI-anchored mannoproteins.
Present with 8320 molecules/cell in log phase SD medium.
GAL2 is a facilitated diffusion transporter required for both the high-affinity galactokinase-dependent and low-affinity galactokinase-independent galactose transport processes.
Interacts with CAF4, DNM1 and FIS1, components of the mitochondrial fission machinery. Interacts via its N-terminal, coiled-coil extension (NTE) with FIS1, and via its WD repeats with DNM1.
Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein, binding to FIS1 on the mitochondrial outer membrane and recruiting the dynamin-like GTPase DNM1 to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division.
High-affinity manganese transporter involved in manganese uptake from the extracellular environment. Contributes also to cellular accumulation of other divalent metal ions such as cadmium, cobalt, copper, iron and nickel.
Catayzes the decarboxylation/dehydration of prephenate to phenylpyruvate.
Belongs to the AAA ATPase family. MSP1 subfamily.
Homohexamer; in presence of ATP (PubMed:30858337, PubMed:32541053, PubMed:28712723). Interacts with PEX3; leading to inhibit the translocase activity (PubMed:28906250, PubMed:32541053).
Impaired transmembrane tail-anchored protein localization, characterized by mislocalization of PEX15 to the mitochondrion outer membrane.
Interaction with PEX3 inhibits the translocase activity by preventing unfolding of target proteins.
Outer mitochondrial translocase required to remove mislocalized tail-anchored transmembrane proteins on mitochondria (PubMed:24843043, PubMed:24821790, PubMed:28906250, PubMed:30858337, PubMed:31445887, PubMed:28712723). Specifically recognizes and binds exposed hydrophobic surfaces of mistargeted tail-anchored transmembrane proteins (PubMed:30858337). Acts as a dislocase that mediates the ATP-dependent extraction of mistargeted tail-anchored transmembrane proteins from the mitochondrion outer membrane (PubMed:24843043, PubMed:24821790, PubMed:28906250, PubMed:30858337, PubMed:32541053, PubMed:28712723). Able to unfold protein substrates by processive threading through its central pore (PubMed:32541053). Once extracted from the mitochondrion outer membrane, substrate proteins are then transferred to the endoplasmic reticulum, where they are ubiquitinated and degraded by the proteasome (PubMed:31445887). Also mediates extraction of excess tail-anchored proteins from the peroxisomal membrane (PubMed:28906250). In normal conditions, MSP1 translocase activity is inhibited by PEX3 at peroxisomes; only catalyzes removal of excess tail-anchored proteins (PubMed:28906250).
C-5 sterol desaturase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:1864507). ERG3 catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol (PubMed:1864507). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672).
Present with 36200 molecules/cell in log phase SD medium.
The ERG3 promoter contains 2 upstream activation sequences, UAS1 and UAS2 (PubMed:8772195). UAS1 regulates gene expression but does not affect sterol regulation (PubMed:8772195). UAS2 is required for sterol regulation (PubMed:8772195). The absence of sterol esterification leads to a decrease of ERG3 expression (PubMed:8772195).
Binds two magnesium or manganese ions per subunit.
Catalyzes the second and fifth step in the 'de novo' purine biosynthesis pathway; contains phosphoribosylamine--glycine ligase (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS) activities.
In the C-terminal section; belongs to the AIR synthase family.
In the N-terminal section; belongs to the GARS family.
Present with 35800 molecules/cell in log phase SD medium.
Component of the core Fe-S cluster (ISC) assembly machinery. Interacts with frataxin (PubMed:14741370, PubMed:12947415, PubMed:20815377, PubMed:25228696). Interacts with the mitochondrial co-chaperones JAC1 and SSQ1 (PubMed:12756240, PubMed:15123690, PubMed:22306468, PubMed:23946486, PubMed:23615440). Interacts with NFS1 (PubMed:23946486, PubMed:25228696). Interacts with ferredoxin YAH1; interacts with the reduced form (PubMed:25358379).
Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins. First, a [2Fe-2S] cluster is transiently assembled on the scaffold proteins ISU1 and ISU2. In a second step, the cluster is released from ISU1/ISU2, transferred to glutaredoxin GRX5, followed by the formation of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on ISU1/ISU2 depends on the function of the cysteine desulfurase complex NFS1-ISD11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin (YFH1) as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase ARH1 and ferredoxin YAH1, which receive their electrons from NADH. Fe-S cluster release from ISU1/ISU2 is achieved by interaction with the Hsp70 chaperone SSQ1, assisted by the DnaJ-like co-chaperone JAC1 and the nucleotide exchange factor MGE1. ISU1 is the major isoform in yeast, while ISU2 is not detectable in cells grown to stationary phase (PubMed:10588895, PubMed:12970193, PubMed:14741370, PubMed:15123690, PubMed:16341089, PubMed:16431909, PubMed:23615440, PubMed:25358379). Also involved in production of a sulfur precursor required for thiolation of cytoplasmic tRNAs (PubMed:31040179).
Involved in the formation of nucleus-vacuole (NV) junctions during piecemeal microautophagy of the nucleus (PMN). NV junctions are interorganelle interfaces mediated by NVJ1 in the nuclear envelope and VAC8 on the vacuole membrane. Together, NVJ1 and VAC8 form Velcro-like patches through which teardrop-like portions of the nucleus are pinched off into the vacuolar lumen and degraded by the PMN process. Acts also as an outer-nuclear membrane receptor for OSH1 and TSC13.
Belongs to the class I-like SAM-binding methyltransferase superfamily. BMT5 family.
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(3) position of uridine 2634 (m3U2634) in 25S rRNA.
Component of the CFIA complex, which is composed of RNA14, RNA15, PCF11 and CLP1. Interacts with RNA14, RNA15 and RTT103. Interacts directly with the phosphorylated CTD domain of RPB1/RNA polymerase II.
Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Independently involved in RNA polymerase II transcript termination. Binds RNA. Seems to bridge RNA polymerase II and the native transcript and may be involved in dismantling the RNA polymerase II elongation complex.
Belongs to the TFIIF beta subunit family.
Present with 520 molecules/cell in log phase SD medium.
Interacts with CRM1, MSL5, PRP8, and the RNA polymerase II largest subunit (RPB1). MSL5, MUD2 and PRP40 interact to form the commitment complex 2 (CC2), a precursor of mature spliceosomes.
Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. This protein is associated with snRNP U1. Two commitment complexes, CC1 and CC2, have been defined in yeast. CC1 is a basal complex dependent only on the 5' splice site. CC2 is a complex of lower mobility and is dependent on a branchpoint as well as a 5' splice site region. This protein is involved in CC2 formation where it binds to the branchpoint binding protein MSL5, bridging the U1 snRNP-associated 5' splice site and the MSL5-associated branch point 3' intron splice site.
The WW and FF domains bind to the phosphorylated carboxy-terminal domain of RPB1.
ATP-dependent kinase that could be involved in endoplasmic reticulum membrane assembly.
Present with 161 molecules/cell in log phase SD medium.
Maintains high levels of reduced glutathione in the cytosol.
Belongs to the saccharopine dehydrogenase family.
Component of serine palmitoyltransferase (SPT), which catalyzes the committed step in the synthesis of sphingolipids, the condensation of serine with palmitoyl CoA to form the long chain base 3-ketosphinganine.
LCB1 and LCB2 encode essential subunits of the enzyme and form a heterodimer. Component of the SPOTS complex, at least composed of LCB1/2 (LCB1 and/or LCB2), ORM1/2 (ORM1 and/or ORM2), SAC1 and TSC3. Interacts with LCB2 and TSC3.
The first transmembrane domain is not required for stability, membrane association, interaction with LCB2, or enzymatic activity. The second and third transmembrane domains are required for stability and interaction with LCB2.
Belongs to the mitochondrion-specific ribosomal protein mL43 family.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (Probable). Also has an extraribosomal function, being essential for mitochondrial genome integrity. May interact with MHR1 to take part in the mtDNA repair mechanism (PubMed:25609543).
Has a respiratory growth defect. Shows complete loss of growth on nonfermentable carbon source and a gradual loss of mtDNA with replicative cell growth and an increasing number of generations.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YDR210C-C ORF.
Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety in natural or engineered linear fusion proteins, irrespective of their size or the presence of an N-terminal extension to ubiquitin.
3' exoribonuclease required for 5S rRNA maturation and for the proper maturation of the 5' cistron of the tRNA-Arg3 dicistronic gene. Involved with REX2 in the maturation of the 5.8S rRNA, and with REX2 and REX3, in the 3' processing of the U5L snRNA.
Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
Possibly involved in the synthesis of a specialized molecule, probably related to a fatty acid, which is essential for mitochondrial respiration. Is essential for oxygen uptake and the presence of cytochromes A and B.
Present with 12100 molecules/cell in log phase SD medium.
Component of the Sm core complex, present in spliceosomal snRNP U1, U2, U4/U6 and U5. The core complex contains SMB1, SMD1, SMD2, SMD3, SME1, SMX3 and SMX2 (Sm proteins B, D1, D2, D3, E, F and G, respectively), and is probably a heptameric ring structure. SMX2 specifically interacts with SME1. Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
Involved in mRNA and protein export from nucleus.
Forms a channel through the cell membrane that allows diffusion of small hydrophilic molecules.
Belongs to the WD repeat BOP1/ERB1 family.
Component of the NOP7 complex, composed of ERB1, NOP7 and YTM1. The complex is held together by ERB1, which interacts with NOP7 via its N-terminal domain and with YTM1 via a high-affinity interaction between the seven-bladed beta-propeller domains of the 2 proteins. The NOP7 complex associates with the 66S pre-ribosome. Also interacts with NOG1.
Associates with ERV25, ERP1 and ERP2. Interacts also with SAR1, SEC23 and SEC24.
Constituent of COPII-coated endoplasmic reticulum-derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi.
Present with 20000 molecules/cell in log phase SD medium.
Belongs to the cytochrome b5 family. MAPR subfamily.
The cytochrome b5 heme-binding domain lacks the conserved iron-binding His residues at positions 81 and 105.
Belongs to the SMC family. SMC5 subfamily.
The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of smc6, forming a V-shaped heterodimer.
Component of a late pre-40S ribosomal particle, composed of the 40S ribosomal proteins and the non-ribosomal factors DIM1, DIM2, ENP1, HRR25, LTV1, NOB1, RIO2 and TSR1.
Required for the final endonucleolytic cleavage of 20S pre-rRNA at site D in the cytoplasm, converting it into the mature 18S rRNA. Involved in normal export of the pre-40S particles from the nucleus to the cytoplasm. No longer associates with pre-40S subunits in RPS19 disruptions, suggesting it acts after the ribosomal protein in 18S rRNA maturation.
Present with 41000 molecules/cell in log phase SD medium.
Associates with the PP2a (PPH21 and PPH22) and SIT4 protein phosphatase catalytic subunits. Interacts with PPG1, PPH3 and TIP41.
Involved in negative regulation of the TOR signaling pathway in response to type of available nitrogen source. Inhibitor of PP2A phosphatase SIT4, which results in inhibition of nuclear export of MSN2, due to lack of dephosphorylation by SIT4. Also required for rapamycin induced activation of expression of many nitrogen discrimination pathway (NDP) genes. In complex with PPH21, required for organization of the actin cytoskeletom during the cell cycle via a Rho GTPase-dependent mechanism.
Phosphorylated by TOR kinases. Dephosphorylated by CDC55, TPD3 and SIT4.
ATPase-dedicated chaperone that assists the formation of the RPT6-RPT3 ATPase pair, an early step in proteasome assembly. Plays a key role in maintaining homeostatic proteasome levels and adjusting proteasome assembly when demands increase, such as during proteasome stresses. Function overlaps with RPN14.
Decreases cell fitness. Causes severe growth defects and an overload of polyubiquitinated conjugates when associated with a RPT6 thermosensitive proteasome mutant.
Expression is increased in absence of RPN14 and upon treatment with tunicamycin, an agent which causes accumulation of misfolded proteins in the endoplasmic reticulum.
Interacts with RPT6. Interacts with the 40S and 60S ribosomal subunits.
Present with 151000 molecules/cell in log phase SD medium.
Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton.
Required for normal levels of gene conversion events during meiosis.
Belongs to the mitochondrion-specific ribosomal protein mS37 family.
Component of a cullin-RING ligase (CRL) composed of 4 subunits: the RING protein HRT1, the cullin RTT101, a linker protein MMS1, and the substrate receptor CRT10. Interacts with MMS1.
Substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-CRT10). RTT101(MMS1-CRT10) may regulate nucleotide synthesis through transcriptional regulation of RNR genes encoding ribonucleotide reductases.
Cortical patch protein involved in endocytosis. May serve as an adapter to link INP52 and INP53 to the cortical actin cytoskeleton.
Interacts with CAP1, RVS167, SLA1, INP52 and INP53. The INP52 and INP53 C-terminal Sac1 domains are required for the binding with BSP1.
By transcription factors SBF (SWI4-SWI6 cell-cycle box binding factor) and SWI5 in a cell cycle-regulated manner. Peaks in G1 phase.
Forms a cyclin-CDK complex with PHO85. Interacts with RVS167.
G1/S-specific cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Essential for the control of the cell cycle at the G1/S (start) transition. Together with cyclin PCL1, positively controls degradation of sphingoid long chain base kinase LCB4. The PCL2-PHO85 cyclin-CDK holoenzyme phosphorylates LCB4, which is required for its ubiquitination and degradation. PCL2-PHO85 also phosphorylates RVS167, linking cyclin-CDK activity with organization of the actin cytoskeleton.
Catalytic component of the MIS complex, a complex that mediates N6-methyladenosine (m6A) methylation on some mRNAs during meiosis and is required for sporulation. M6A, which takes place on the adenosine of 5'-[AG]GAC-3' consensus sites of some mRNAs, is probably required to initiate sporulation. Positive regulator for IME2.
Second trifunctional enzyme acting on the beta-oxidation pathway for fatty acids, possessing hydratase-dehydrogenase-epimerase activities. Converts trans-2-enoyl-CoA via D-3-hydroxyacyl-CoA to 3-ketoacyl-CoA.
Belongs to the actin family. ARP4 subfamily.
Chromatin interaction component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. ARP4 recognizes H2AS128ph (gamma-H2A) and is required for NuA4 complex integrity. Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the INO80 complex which remodels chromatin by shifting nucleosomes. Its ability to induce transcription of some phosphate-responsive genes is modulated by inositol polyphosphates. The INO80 complex is involved in DNA repair by associating to gamma-H2A as a response to DNA damage.
Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, SWC4, TRA1, VID21, YAF9 and YNG2. Component of the chromatin-remodeling INO80 complex, at least composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3, IES4, IES6, ACT1, IES2, IES5 and INO80. Component of the SWR1 chromatin remodeling complex composed of at least ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4, SWC5, SWC7 and SWR1, and perhaps BDF1. Interacts with histones H4 (HHF1 and HHF2), H3 (HHT1 and HHT2) and H2A (HTA1 and HTA2).
Component of the phosphatidylinositol N-acetylglucosaminyltransferase (GPI-GlcNAc transferase) complex composed of at least GPI1, GPI2, GPI3, GPI15, GPI19 and ERI1 (Probable). Interacts with GPI2 (PubMed:15163411). Interacts with GTP-bound RAS2 in an effector loop-dependent manner (PubMed:12832483).
Defects cause hyperactive Ras phenotypes, probably due to diminished GPI-anchor protein production.
Probable component of the GPI-GlcNAc transferase (GPI-GnT) complex in the endoplasmic reticulum, a complex that catalyzes transfer of GlcNAc from UDP-GlcNAc to an acceptor phosphatidylinositol, the first step in the production of GPI-anchors for cell surface proteins. Ras may inhibit the enzyme activity of the GPI-GnT complex via the association between ERI1 and RAS2.
Required for survival during stationary phase.
Abnormal activation of TORC1 signaling in nitrogen-replete conditions (glutamine or leucine nitrogen source), and during high hydrostatic pressure (mechanical stress) (PubMed:28993463, PubMed:29698392, PubMed:28483912, PubMed:32801125). Increases cellular levels of glutamine and alanine during high hydrostatic pressure (mechanical stress) (PubMed:32801125). Sensitive to rapamycin (TORC1 signaling-inhibitor), caffeine, and high hydrostatic pressure (mechanical stress) (PubMed:28993463, PubMed:29698392, PubMed:34535752, PubMed:26510498, PubMed:32801125). Abnormal TORC1-reactivation following inactivaton by rapamycin (TORC1 signaling-inhibitor) (PubMed:28993463). Resistance to tunicamycin (endoplasmic reticulum stressor) administered together with FK506 (calcineurin inhibitor) (PubMed:26510498). Abnormal localization of TOR1 to vacuoles (PubMed:28993463). Localization of GTR1 and GTR2 to vacuoles is normal (PubMed:28993463) Localization of TORC1 to vacuoles is normal (PubMed:28483912). Simultaneous disruption of GTR1 results in TOR1 mislocalization and loss of TORC1 activity and viability (PubMed:29698392). Simultaneous disruption of EGO1 results in loss of viability (PubMed:29698392). Macroautophagy appears normal (PubMed:28993463).
Activated by glutamine (PubMed:34535752, PubMed:29698392). May also be activated by cysteine (PubMed:34535752).
Functions as an intracellular glutamine sensor that directly activates the TORC1 signaling pathway, to promote cell growth when glutamine is available (PubMed:34535752, PubMed:29698392, PubMed:28483912, PubMed:26510498, PubMed:32801125). May play a role in repressing NPR1 activity independently of TORC1 signaling (PubMed:28993463).
Interacts with the TORC1 complex when activated by glutamine or cysteine (PubMed:34535752, PubMed:29698392, PubMed:28483912). Interacts with TOR1; glutamine enhances the interaction (PubMed:34535752, PubMed:29698392, PubMed:28483912). Interacts with KOG1; glutamine enhances the interaction (PubMed:29698392). Interacts with TCO89 (PubMed:29698392). Interacts with LST8; glutamine enhances the interaction (PubMed:29698392). Interacts with TOR2; glutamine enhances the interaction (PubMed:29698392).
The FYVE-type zinc finger domain contributes to vacuolar localization.
Hyperphosphorylated during acute stress.
Required for a complete transcriptional response to osmotic stress, through recruitment of HOG1 followed by pol II recruitment to the promoters of GPD1 and other HOG-dependent genes.
Homodimer. Binds in a GTP-dependent manner to the GRIP domain of IMH1. Interacts with MON2.
Recruits golgins such as IMH1 to the Golgi. Can bind and hydrolyze GTP. May be involved in trafficking events within the endosomal system.
Prospore-specific dityrosine transporter responsible for translocation of dityrosine through the prospore membrane and required for the formation of the outermost layer of the spore.
Component of the oligosaccharyltransferase (OST) complex, which appears to exist in two assemblies comprising OST1, OST2, OST4, OST5, STT3, SWP1, WPB1, and either OST3 or OST6 (PubMed:8175708, PubMed:16297388, PubMed:16096345, PubMed:15831493, PubMed:15886282, PubMed:9405463, PubMed:29301962). OST assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains OST1 and OST5, subcomplex 2 contains STT3, OST3, and OST4, and subcomplex 3 contains OST2, WBP1, and SWP1 (PubMed:29301962). Interacts with SEC61 and SSS1 (PubMed:15831493).
Belongs to the nitronate monooxygenase family. NMO class I subfamily.
Catalyzes the oxidation of alkyl nitronates to produce the corresponding carbonyl compounds and nitrites.
Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage.
Belongs to the tRNA(His) guanylyltransferase family.
Binds to membranes enriched in phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin.
Involved in the transport of siderophore triacestylfusarinine C and so has a role in iron homeostasis.
Central component of the TOM (translocase of outer membrane) receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM20 and TOM70 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore. Docks TOM20 and TOM70 for interaction with the general TOM40 import pore (GIP) complex. May regulate the TOM machinery organization, stability and channel gating.
Forms part of the preprotein translocase complex of the outer mitochondrial membrane (TOM complex) which consists of at least 7 different proteins (TOM5, TOM6, TOM7, TOM20, TOM22, TOM40 and TOM70). Interacts with TOM20 and TOM70. Interacts with FCJ1.
Its cytoplasmic domain associates with the cytoplasmic domains of TOM20 and TOM70. Its intermembrane space domain provides a trans binding site for presequences and the single membrane anchor is required for a stable interaction between the GIP complex proteins.
Present with 6610 molecules/cell in log phase SD medium.
Initiation of mating type interconversion. This protein is a site-specific endonuclease that cleaves a site in the mat locus on chromosome III. The double-strand break is followed by a unidirectional gene conversion event that replaces the information at the mat locus by information copied from either of the two homologous loci (HMR and HML) that reside at the extremity of the chromosome III. Endonuclease expression takes place in late G1 just before cells enter S phase.
Rapidly degraded via the ubiquitin-26S proteasome system through two ubiquitin-conjugating enzymes UBC2/RAD6 and UBC3/CDC34.
The metal-binding domain form zinc-fingers that are involved in binding of the DNA.
Interacts with MST28. Binds to coatomer proteins of COPI and SEC23/SEC24 of COPII coated vesicles.
Involved in protein trafficking vesicle formation, probably by stabilizing of coatomer at the Golgi membrane and thus allowing the efficient formation of COPI coated vesicles.
Circular dichroism measurements suggest that the protein is largely unstructured in the absence of interaction with PAP1.
Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. In the CPF complex probably interacts directly with PAP1 and YTH1. Interacts with RNA14.
Polymerase-regulating component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase PAP1. This inhibits the extension of an oligo(A) primer by limiting access of the RNA substrate to the C-terminal RNA binding domain of PAP1. Seems to tether PAP1 to the cleavage factor I.
Redox component that participates in c-type cytochrome biogenesis in the mitochondrial intermembrane space. May play a role in the reduction of heme prior to its ligation to apocytochrome c by cytochrome c heme lyase. Has oxidoreductase activity in vitro.
C-terminal 700 AA are mainly in alpha-helices and beta-sheets.
In the C-terminal section; belongs to the glycosyltransferase 20 family.
Regulatory subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-glucose in a two step process. May stabilize the trehalose synthase complex, and confer sensitivity to physiological concentrations of phosphate and to fructose 6-phosphate.
Belongs to the PIGG/PIGN/PIGO family. PIGN subfamily.
Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. Ethanolamine phosphate on the alpha-1,4-linked mannose is essential for further mannosylation by GPI10 and is necessary for an efficient recognition of GPI lipids and GPI proteins by the GPI transamidase, for the efficient transport of GPI anchored proteins from endoplasmic reticulum to Golgi and for the physiological incorporation of ceramides into GPI anchors by lipid remodeling. Also involved in non-mitochondrial ATP movements across membrane and participates in Golgi and endoplasmic reticulum function, Also required for the incorporation of BGL2 into the cell wall.
Interacts with CSF1; CSF1 channels phosphatidylethanolamine to MCD4 in the endoplasmic reticulum at contact sites to support GPI anchor biosynthesis.
Target of the inhibitor of GPI biosynthesis YW3548/BE49385A.
Grows more slowly in amino acid-free medium (SD).
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Responsible for the transfer of the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly.
Interacts with snoRNA U3. Interacts with EMG1, MPP10 and NOC4. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.
Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm.
Involved in regulation of Ty1 transposition. Inhibits Ty1 transposition at a post-transcriptional and pre-integrational stage of the Ty1 retrotransposition cycle.
Required for spore wall assembly and ascus formation (PubMed:11470404, PubMed:15590821). Involved in the formation and elongation of prospore membranes (PubMed:26605945, PubMed:27303688).
Assembly factor required for Rieske Fe-S protein RIP1 incorporation into the cytochrome b-c1 (CIII) complex. Functions as a chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane. Modulates the mitochondrial matrix zinc pool.
Belongs to the complex I LYR family. MZM1 subfamily.
Leads to respiratory growth defect and increases frequency of mitochondrial genome loss.
Component of the ASTRA chromatin remodeling machinery complex composed of at least RVB1, RVB2, TRA1, TEL2, TT1 and TTI2. Component of the TTT complex composed of TEL2, TTI1 and TTI2. Interacts with TEL2 and TTI1.
Component of the ASTRA complex probably in chromatin remodeling.
Component of the spindle pole body (SPB) half-bridge involved in the initial steps of SPB duplication.
Forms a complex with CDC31 and interacts with SPC110. Associates with the spindle pole body half bridge.
A developmentally regulated protein important for microtubule functions. Targets KAR3 to the cytoplasmic microtubules during mating. Essential for KAR3 function during prophase of meiosis I. Required for interhomolog recombination, synapsis of homologous chromosomes and establishment of a meiosis I spindle.
Component of the phosphatidylinositol N-acetylglucosaminyltransferase (GPI-GlcNAc transferase) complex composed of at least GPI1, GPI2, GPI3, GPI15, GPI19 and ERI1 (Probable). Interacts with ERI1 (PubMed:15163411).
Expression is maximal during lag and early exponential phases of growth, decreasing upon further entry into exponential growth.
Low-affinity glucose transporter. HXT1 is as well involved in the transport of mannose.
Component of the pre-66S ribosomal particle. Interacts with NOP7, RRP1 and RRP5.
Essential for the organization of the actin cytoskeleton, fluid phase endocytosis and vesicle trafficking, together with YSC84.
May play a role in chromatin organization.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. TRM4 subfamily.
Methylates cytosine to m5C at several positions in different tRNAs and pre-tRNAs containing intron. Able to modify tRNAs at all four positions (34, 40, 48 and 49) at which m5C has been found in tRNAs. May be involved in ribosome biogenesis as its disruption leads to increased sensitivity to the antibiotic paromomycin.
Present with 16100 molecules/cell in log phase SD medium.
Interacts with snoRNA U3. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.
Probable ATP-binding RNA helicase. Required for 18S rRNA synthesis. May play a role in restructuring of the pre-rRNA.
Binds to intron-containing transcripts and is involved in quality control for the export of spliced mRNAs from the nucleus (PubMed:14676199, PubMed:14769921, PubMed:24452287). Binds to pre-mRNAs until splicing is completed or until faulty mRNAs are degraded. On correctly spliced mRNAs, GBP2 and HRB1 recruit MEX67 to allow nuclear export. On faulty mRNAs, GBP2 and HRB1 associate with the TRAMP complex that guides those pre-mRNAs to the exosome for degradation (PubMed:24452287).
Present with 60865 molecules/cell in log phase SD medium.
Subunit of the eukaryotic elongation factor 1 complex (eEF1). Probably plays a role in anchoring the complex to other cellular components. May be involved in transcriptional regulation of MXR1.
The eukaryotic elongation factor 1 complex (eEF1) is probably a heterohexamer. Two trimeric complexes, each composed of eEF1A (TEF1 or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or TEF4), are probably dimerized via the eF1Bgamma subunits. The eEF1B subcomplex with the GEF activity is formed of eEF1Balpha and eEF1Bgamma. CAM1 interacts with EFB1. Component of a complex bound to MXR1 promoter region.
There are 2 isoforms for eEF1Bgamma in yeast.
Ths GST-like domain mediates the interaction to eEFB1 and may be responsible for dimerization of the eEF1 complex.
Major phosphatase responsible with PTP3 for tyrosine dephosphorylation of MAP kinase HOG1 to inactivate its activity. May also be involved in the regulation of MAP kinase FUS3. May be implicated in the ubiquitin-mediated protein degradation.
Associates with the NTC complex (or PRP19-associated complex), composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2, and PRP19. The NTC complex associates with the spliceosome after the release of the U1 and U4 snRNAs and forms the CWC spliceosome subcomplex (or CEF1-associated complex) reminiscent of a late-stage spliceosome composed also of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8, PRP9, PRP11, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNU114, SPP2, RSE1 and YJU2. Interacts directly with PRP8 (via SCwid domain). Interacts directly with SNU114 (via C-terminus).
Involved in pre-mRNA splicing. May function at or prior to the first catalytic step of splicing at the catalytic center of the spliceosome, together with ISY1. May do so by stabilizing the catalytic center or the position of the RNA substrate.
Acts as component of the nascent polypeptide-associated complex (NAC), which promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane. Also blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum. BTT1 may act as a transcription factor that exert a negative effect on the expression of several genes that are transcribed by RNA polymerase II.
Part of the nascent polypeptide-associated complex (NAC), consisting of EGD2 and either EGD1 or BTT1. NAC associates with ribosomes via EGD1 or BTT1.
Sequentially removes both fatty acyl groups from diacylglycerophospholipids and therefore has both phospholipase A and lysophospholipase activities. Substrate preference is phosphatidylserine > phosphatidylinositol. Does not cleave phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid and phosphatidylinositol-bisphosphate (PubMed:10497163). Mainly responsible for the degradation of phosphatidylinositol in vivo (PubMed:15588231).
Belongs to the eukaryotic NMN adenylyltransferase family. POF1 subfamily.
Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Involved in the salvage pathway for NAD(+) biosynthesis via NMN (PubMed:24759102). Involved in the filamentation pathway. Suppresses the filamentation defect of a KSS1 deletion (PubMed:21460040).
Interacts with KSS1 (PubMed:21460040). Interacts with UBC7 (PubMed:22204397).
Lowers cellular NAD(+) levels and decreases the efficiency of nicotinamide riboside (NR) utilization, resistance to oxidative stress, and NR-induced life span extension (PubMed:24759102). Highly sensitive to heat shock and higher sensitivity to ER stress agents than wild-type cells (PubMed:22204397).
Interacts with the caspase-like ESP1, and prevents its protease activity probably by covering its active site. Interacts with CDC20.
Phosphorylated by CDC28. The phosphorylation may be important for ESP1 localization to the nucleus.
Regulatory protein, which plays a central role in chromosome stability. Probably acts by blocking the action of key proteins. During the mitosis, it blocks Separase/ESP1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. At the onset of anaphase, it is ubiquitinated, conducting to its destruction and to the liberation of ESP1.
Ubiquitinated by the anaphase promoting complex (APC) at the onset of anaphase, conducting to its degradation.
The PIP2-OAF1 heterodimer acts as a transcriptional activator to induce the transcription of genes encoding proteins involved in fatty acid beta-oxidation, a response called oleic acid induction, when cells grow on fatty acids as sole carbon source. Recognizes and binds to the oleate response element (ORE) (or peroxisome box), two inverted CGG triplets spaced by 14 to 18 intervening nucleotides, in the promoter region of a number of genes (such as CTA1, FOX1 to FOX3, FAA2, PAS8, PAS10, etc.) for peroxisomal proteins. OAF1 acts as the sensor for oleate and inhibits PIP2 activity under non-inducing conditions. Activity is repressed by glucose.
the 9aaTAD motif (residues 1034 to 1042) is a transactivation domain present in a large number of yeast and animal transcription factors.
Required for peroxisomal protein import which maintains the function of peroxisomes.
Although this protein promotes prion formation and it has a Asn/Gln-rich prion-like domain, it does not seem to have a prion form by itself.
By heat shock. Can thereby reach physiological protein levels high enough to promote prion-formation.
Overproduction promotes the de novo induction of the [PSI+] prion form of SUP35. The prion-inducing effect depends on the association with the actin cytoskeleton. Also implicated in prion maintenance during heat stress.
Ubiquitinated by RSP5. Ubiquitination reduces the protein abundance and its prion-inducing ability.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YGR161C-C ORF.
Belongs to the HDA2/3 family. HDA2 subfamily.
Heterodimer with HDA3. Component of the HDA1 histone deacetylase complex composed of at least one HDA1 homodimer and one HDA2/HDA3 heterodimer. Interacts with HDA1 and HDA3.
Belongs to the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3 and PML1. May also belong to the CWC complex (or CEF1-associated complex) composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with IST3 and PML1.
Required for efficient splicing and pre-mRNA nuclear retention. May also be involved in positioning the proximal bud pole signal.
Cytoplasmic aldehyde dehydrogenase involved in ethanol oxidation. Involved in pantothenic acid production through the conversion of 3-aminopropanal to beta-alanine, an intermediate in pantothenic acid (vitamin B5) and coenzyme A (CoA) biosynthesis.
Leads to diminished in vitro and in vivo O-mannosylation activity.
PMT1 and PMT2 form a functional heterodimer. The complex interacts with endoplasmic reticulum proteins EMP24, ERV25, ERP1, ERP2, CDC48, HRD1, USA1, YOS9, ERO1, PDI1, UBR1, Cue4, DFM1 and TED1. Forms also a minor complex with PMT5.
Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT2 and more rarely with PMT5 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export.
Histidine kinase that acts as an osmosensor at the plasma membrane. Part of the bifurcated SLN1-YPD1-SKN7/SSK1 two-component regulatory system, which controls activity of the HOG1 pathway and gene expression in response to changes in the osmolarity of the extracellular environment. Under normal osmotic conditions, the histidine kinase autophosphorylates His-576. This phosphate is subsequently transferred to Asp-1144, from where it is relayed to 'His-64' of the phosphorelay intermediate protein YPD1. Under high osmolarity conditions, the histidine kinase is no longer active.
The phosphorelay mechanism involves the sequential transfer of a phosphate group from His-576 (H1) in the histidine kinase domain (transmitter domain) to Asp-1144 (D1) of the response regulatory domain (receiver domain). This transfer probably occurs between two SLN1 molecules, rather than intramolecularly. The phosphate group is further transferred to 'His-64' (H2) of YPD1 and finally to 'Asp-554' (D2) of SSK1 or 'Asp-427' (D2) of SKN7.
Interacts with YIF1, YIP1, YIP3, YIP4 and YIP5. Interacts with TRS130.
Present with 5955 molecules/cell in log phase SD medium.
Required for protein transport in the secretory pathway. Probably involved in regulation of secretory vesicle formation at the trans-Golgi compartment. Plays a role in autophagy.
Specialized component of the nuclear membrane that may be involved in the connection of the spindle pole body (SPB) to the nuclear envelope.
Has several reductase activities that are NAD(P)H-dependent and involve FMN as a cofactor, ferricyanide being the best substrate for reduction. May be involved in ferric iron assimilation.
Induced by low temperature and by cycloheximide.
Component of the endoplasmic reticulum-associated protein degradation (ERAD) pathway. Recruits the soluble ubiquitin-conjugating enzyme UBC7 to the cytoplasmic face of the endoplasmic reticulum membrane where it functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Targets the E2 conjugating enzyme UBC7 to the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains, and to the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). Has also a role in cold adaptation, perhaps through effects on sterol biosynthesis.
Forms a heterodimer with UBC7. Interacts with SSM4/DOA10 and UBX2/SEL1.
Expression is repressed by the addition of iron (PubMed:1570306, PubMed:1431884). Induced by transcription factor MAC1 upon copper deprivation (PubMed:7814363, PubMed:9153234, PubMed:9726978, PubMed:10341420). Induced by transcription factor AFT1 upon iron deprivation (PubMed:7720713, PubMed:9200812, PubMed:9726978, PubMed:10341420, PubMed:16024809).
Responsible for the reduction of the azo bond of azo dyes, making yeasts efficient azo dye decolorizers.
Positive regulation of genes required for catabolism of GABA (UGA4, UGA1, and UGA2), urea (DUR1 and DUR2), arginine and allantoin.
Involved in the recombinational repair of double-strand breaks (DSB) in DNA during mitosis and meiosis. Has DNA dependent ATPase activity. Promotes D-loop (displacement loop) formation with RAD51 recombinase. Modifies the topology of double-stranded DNA during the D-loop reaction to facilitate the invasion of the homologous duplex molecule by the initiating single-stranded DNA substrate. Required for adaptation from G2/M checkpoint arrest induced by a double strand break, by participating in monitoring the extent of single-stranded DNA produced by resection of DNA ends. This role is distinct from its roles in recombination. Promotes colocalization of RAD51 and DMC1 during meiotic recombination. Involved in crossover interference.
It is uncertain whether Met-1 or Met-35 is the initiator. In many S.cerevisiae strains, it is not possible to extend the sequence at the N-terminus beyond Met-35 because of a frameshift in the upstream sequence when compared to strain S288c. However, experimental evidence indicates that the longer protein is made in S288c.
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of sodium or lithium ions to allow salt tolerance.
Lacks the conserved His residues essential for binding the catalytic zinc ion. Lacks the conserved residues important for substrate binding and catalysis. Its enzyme activity is therefore unsure.
Present with 39300 molecules/cell in log phase SD medium.
Probably interacts with nascent polypeptides in the endoplasmic reticulum. It is an essential gene only in the absence of PDI. Its native disulfide isomerase activity is very low.
Interacts with the chaperones HSP82 and HSC82.
With SBE22, is involved in cell wall integrity and polarity processes like bud growth, through the transport of CHS3 and UTR2 to sites of growth.
Component of the inner kinetochore constitutive centromere-associated network (CCAN) (also known as central kinetochore CTF19 complex in yeast), which is composed of at least AME1, CHL4, CNN1, CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1 (PubMed:22561346). Interacts with CBF1 (PubMed:7579695).
Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly (PubMed:8408221, PubMed:7579695, PubMed:22561346).
Present with 465 molecules/cell in log phase SD medium.
Expressed 7.5 hours after induction of meiosis.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. Through its FG repeats NUP100 interacts with numerous karyopherins including KAP95, and MEX67.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP100 plays an important role in several nuclear export and import pathways including poly(A)+ RNA and protein transport.
Accumulates approximately 19 times higher amounts of isoamyl acetate compared to wild-type in laboratory scale sake brewing.
Belongs to the 'GDSL' lipolytic enzyme family. IAH1 subfamily.
Plays a crucial role in the hydrolysis of isoamyl acetate in sake mash (Ref.2). Hydrolyzes short chain esters from acetate (C2) to hexanoate (C6), showing more specificity for shorter chain exters. No activity for decanoate (C10) esters (PubMed:21069734).
Belongs to the bacterial ribosomal protein bL21 family.
Contains many Ser/Thr-rich domain and repeats.
Although cells lacking TIM18 live well and do not display any strong phenotype, they do not survive in the absence of mitochondrial DNA.
Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as external driving force. Its role in the complex is unclear but it may be involved in the assembly and stabilization of the TIM22 complex.
Present with 4440 molecules/cell in log phase SD medium.
Essential for respiratory growth and required for maintenance of mtDNA. Required for cell survival in the absence of prohibitins.
Belongs to the eukaryotic release factor 1 family.
Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA.
Heterodimer of two subunits, one of which binds GTP. Interacts with TPA1.
Catalyzes the committed step of phosphatidylethanolamine synthesis via the CDP-ethanolamine branch of the Kennedy pathway. Also exhibits choline kinase activity, thus contributing to phosphatidylcholine synthesis via the CDP-choline pathway, but its preferred substrate is ethanolamine.
Induced by zinc-depletion via the transcription factor ZAP1. Expression is sensitive to intracellular zinc levels (PubMed:16551612). Repressed by inositol (PubMed:15201274).
Involved in the resistance to DNA-damaging agents.
Component of the Golgi-associated retrograde protein (GARP) complex, also called VPS fifty three (VFT) complex, composed of VPS51, VPS52, VPS53 and VPS54. Interacts with the t-SNARE TLG1.
Involved in retrograde transport from early and late endosomes to late Golgi. Links the Golgi-associated retrograde protein (GARP) complex to the t-SNARE TLG1, leading to the fusion between the endosomal vesicles with the late Golgi. May also be indirectly involved in apical bud growth.
DNA-binding protein that induces severe bending of DNA. Required for DNA-binding by the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. Also augments the fidelity of transcription by RNA polymerase III independently of any role in the FACT complex. Required for transcriptional initiation fidelity of some but not all tRNA genes. Seems to be functionally redundant with NHP6A.
Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of STP22, VPS28, SRN2 and MVB12 in a 1:1:1:1 stoichiometry. Self-associates. Interacts with VPS27; the interaction mediates the association with the ESCRT-0 complex. Interacts with VPS20; the interaction mediates the association with the ESCRT-III complex.
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity).
Phosphatase that is active on 2-deoxy-D-glucose 6-phosphate (2-DOG-6P), as well as on fructose-1-P.
Belongs to the WD repeat DCAF13/WDSOF1 family.
Interacts with snoRNA U3. Interacts with NOP1 and MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.
Present with 6620 molecules/cell in log phase SD medium.
Component of the SEA complex composed of at least IML1/SEA1, RTC1/SEA2, MTC5/SEA3, NPR2, NPR3, SEA4, SEC13 and SEH1. Forms a heterodimer with NPR3.
Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis (PubMed:21454883). Mediates inactivation of the TORC1 complex in response to amino acid starvation (PubMed:19521502, PubMed:26510498). Post-transcriptional regulator of nitrogen permeases (PubMed:19521502). May be involved in putative NPR1-dependent phosphorylation of nitrogen permeases or in the processing and targeting of nitrogen permeases at the level of the endoplasmic reticulum (PubMed:19521502).
TORC1 abnormally activated in presence of rapamycin.
Present with 4190 molecules/cell in log phase SD medium.
Transporter protein required for ammonia export. Involved in acetate resistance.
Abnormal activation of TORC1 signaling (PubMed:32801125). Abnormal punctate localization of TOR1 (PubMed:32801125). Sensitive to high hydrostatic pressure (mechanical stress) (PubMed:32801125).
Component of the GSE complex composed of GTR1, GTR2, SLM4, MEH1 and LTV1 (PubMed:16732272). Component of the EGO complex, at least composed of GTR2, SLM4 and MEH1 (PubMed:15989961).
Acts as central component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromers and in several promoters. The association of CBF3C with CBF3D and SGT1 is required for CBF3C activation and CBF3 assembly.
Component of the CBF3 copmplex, which is formed of CBF3A/CBF2, CBF3B/CEP3, CBF3C/CTF13 and CBF3D. CBF3C interacts with CBF3D and SGT1.
Required for the assembly of mitochondrial cytochrome c oxidase.
Activated by tyrosine and threonine phosphorylation after pheromone treatment or carbon/nitrogen limitation.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily.
Dually phosphorylated on Thr-183 and Tyr-185 by STE7 in response to pheromone or carbon/nitrogen limitation, which activates the enzyme. Activated FUS3 down-regulates KSS1 phosphorylation.
In the nucleus, KSS1 forms a complex with DIG1, DIG2 and STE12; in contrast to FUS3 the interaction of KSS1 with STE12 does not depend on DIG1 and DIG2. Phosphorylated KSS1 shows reduced interaction with STE12. During pheromone activation and phosphorylation, KSS1 forms a membrane-associated complex with the scaffold protein STE5, the MAPKK STE7, the MAPKKK STE11, and the G-protein beta subunit GBB/STE4; interacting directly with POF1, STE7 and STE5 proteins.
Together with closely related FUS3, KSS1 is the final kinase in the signal transduction cascade regulating activation/repression of the mating and filamentation pathways, induced by pheromone and nitrogen/carbon limitation, respectively. Phosphorylated KSS1 activates both pathways, whereas activated FUS3 activates the mating but suppresses the filamentation pathway. KSS1 activity is down-regulated by FUS3 during pheromone induction to prevent inappropriate activation of the filamentation pathway. During induction of filamentation, KSS1 activates the transcription factor STE12 resulting in its binding to and activation of filamentation specific genes. Non-activated KSS1 has a kinase-independent repressive effect on STE12 transcriptional activity, that is mediated by direct binding to STE12 and depends on the presence of DIG1 and DIG2, and that is required for the suppression of filamentation under normal growth conditions. SSN3/SRB10 contributes further to the suppression of filamentation under these conditions by reducing STE12 stability independent of KSS1. FUS3 can partially compensate for the lack of KSS1 but filamentation becomes constitutively induced at a low level in the absence of any signal. KSS1 phosphorylates STE7, STE5, FAR1, DIG1, DIG2, STE12, and SST2.
Vacuolar effluxer which mediate the efflux of leucine and other amino acids resulting from autophagic degradation. The release of autophagic amino acids allows the maintenance of protein synthesis and viability during nitrogen starvation.
Component of the nuclear pore complex (NPC) (PubMed:17546040). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. Part of the NUP82 subcomplex, interacts with NUP82 through its C-terminal coiled coil (PubMed:9736720, PubMed:17546040, PubMed:23223634, PubMed:25646085). This subcomplex is the base for interactions with NUP116 and GLE2, with NUP42 and GLE1 and with DYN2 (PubMed:17546040, PubMed:23223634). Interacts directly with DYN2 (PubMed:17546040, PubMed:23223634, PubMed:25646085). Interacts through its FG repeats with karyopherins, such as heterodimeric mRNA transport factor MEX67/MTR2, CRM1 (XPO1), and PSE1 (GSP1-GDP dependent). Interaction with CRM1 (XPO1) is GSP1-GTP dependent and stimulated by RNA1. NUP159 also interacts with GLE1 and the ATP-dependent RNA helicase DBP5.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP159 plays an important role in several nuclear export pathways including poly(A)+ RNA, pre-ribosome, and protein export.
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
The COPII coat is composed of at least 5 proteins: the SEC23/24 complex, the SEC13/31 complex, and the protein SAR1. SEC13 and SEC31 make a 2:2 tetramer that forms the edge element of the COPII outer coat. The tetramer self-assembles in multiple copies to form the complete polyhedral cage. Interacts (via WD 8) with SEC13. Interacts with EMP24, ERV25, SEC16 and SHR3.
By weak acids like sorbate through the WAR1 transcription activator.
Plasma membrane transporter which mediates resistance to water-soluble, monocarboxylic acids with chain lengths of from C1 to C7 by active extrusion of the preservative anions from the cytosol. Also involved in the export of aromatic and branched-chain organic acids produced in amino acid catabolism.
Active in protein import into the nucleus. Its major import substrate is transcription elongation factor TFIIS.
GTP-bound Ran dissociates the isolated NMD5/TFIIS complex.
Component of the R2TP complex composed at least of RVB1, RVB2, TAH1 and PIH1. Interacts also with HSP90.
ATP-dependent DNA helicase able to unwind duplex DNA or DNA- RNA heteroduplex (PubMed:9545297). Displacement of the DNA strand occurs in the 3' to 5' direction with respect to the single-stranded DNA flanking the duplex (PubMed:9545297). Acts as an integral component of the S-phase checkpoint response, which arrests cells due to DNA damage or blocked fork progression during DNA replication (PubMed:10640278). Can create a deleterious topological substrate that TOP3 preferentially resolves. The TOP3-SGS1 protein complex may function as a eukaryotic reverse gyrase introducing positive supercoils into extrachromosomal ribosomal DNA rings (PubMed:7969174). Together with topoisomerase II has a role in chromosomal segregation (PubMed:7736577). Maintains rDNA structure where it has a role in re-starting stalled replication forks (PubMed:12228808).
Belongs to the helicase family. RecQ subfamily.
Expression is regulated through the cell cycle with an accumulation in S phase.
Heterodimer with TOP3 (PubMed:7969174, PubMed:15899853). Forms a complex with TOP3 and RMI1 (PubMed:15889139). Forms a ternary complex with a MLH1-MLH3 heterodimer (MutLbeta) during meiosis (PubMed:12200140). Interacts with TOP2 (PubMed:7736577).
Belongs to the TRAPP small subunits family. Sedlin subfamily.
Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family.
Endosomal/prevacuolar electroneutral Na(+)/H(+) exchanger which mediates intracellular sequestration of Na(+) cations, regulates vacuolar pH and contributes to osmotolerance following sudden exposure to hyperosmotic media. Contributes also to the postdiauxic/stationary phase resistance to osmotic stress and allows for the continued growth of cells until the acquired osmotolerance response can occur. Involved in hygromycin resistance probably through its influence on the electrochemical proton gradient affecting secondarily the entrance of hygromycin. Mediates pH-dependent vesicle trafficking out of the endosome. Contributes to K(+) sequestration and homeostasis.
Numerous studies suggest that the C-terminal tail of the Na(+)/H(+) exchangers assumes a cytosolic orientation and constitutes a regulatory region. This cytosolic localization is confirmed by phosphorylation analysis (PubMed:15665377 and PubMed:18407956). However, residues Asn-515, Asn-550 and Asn-563 have been shown to be glycosylated and localized at the lumenal side (PubMed:11036065). These contradictory results suggest an unusual topology of the C-terminal tail which may contain membrane spans formed by beta-sheets or even may switch from one side to the other of the membrane.
Belongs to the Mediator complex subunit 5 family.
Present with 2491 molecules/cell in log phase SD medium.
May play a role in vesicular budding and traffic between compartments of the Golgi apparatus.
The highly charged acidic domain may serve a structural role to interact with lipids or proteins on the cytoplasmic surface of the Golgi apparatus.
Delta(14)-sterol reductase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:1418625, PubMed:8125337). ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol (PubMed:1418625, PubMed:8125337). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672).
Inhibited by the morpholine antifungal drug fenpropimorph.
Leads to the accumulation of ergosta-8,14-dienol as the major sterol.
This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Required for translation of the mitochondrial OLI1 transcript encoding subunit 9 of mitochondrial ATP synthase.
Present with 6990 molecules/cell in log phase SD medium.
Serine/threonine protein kinase that is thought to function in regulating kinetochore activity and entry into meiosis. Could phosphorylate IME1.
Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 snRNP, spliceosomal U4/U6.U5 snRNP, and free U6 snRNP). It binds directly to the U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. It probably also is involved in degradation of nuclear pre-mRNA by targeting them for decapping. LSM7 binds specifically to the 3'-terminal U-tract of U6 snRNA. LSM2-LSM8 probably is involved in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM7, probably in a complex that contains LSM2-LSM7 but not LSM1 or LSM8, associates with the precursor of the RNA component of RNase P (pre-P RNA) and may be involved in maturing pre-P RNA.
Component of the heptameric LSM1-LSM7 complex that forms a seven-membered ring structure with a doughnut shape. The LSm subunits are arranged in the order LSM1, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. Except for LSM1, where a C-terminal helix crosses the ring structure to form additional interactions with LSM3 and LSM6, each subunit interacts only with its two neighboring subunits. The LSM1-LSM7 complex interacts with PAT1; within the complex PAT1 has direct interactions with LSM2 and LSM3. Component of the heptameric LSM2-LSM8 complex that forms a seven-membered ring structure with a doughnut shape; an RNA strand can pass through the hole in the center of the ring structure. The LSm subunits are arranged in the order LSM8, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. LSM2-LSM8 associates with PAT1 and XRN1. A complex comprising LSM2-LSM7 without LSM1 or LSM8 may exist. Component of the spliceosome U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
Interacts with the TRAPP II complex; TRAPP II subunits TRS33 and TRS65 are required for this interaction.
Required, together with the TRAPP II subunit TRS33, for TRAPP II complex assembly or stability, and for proper Golgi localization of TRAPP and the Rab GTPase YPT31.
High-affinity glucose transporter. Is only indispensable for growth on low glucose-containing media, because S.cerevisiae possesses other sugar transporters.
Involved in oxidative stress resistance and N-glycosylation.
Transcription factor regulating the cell cycle specific transcription of a spindle pole body (SPB) calmodulin binding protein SPC110. Required for full induction of SPC110 transcription in late G1. Binds to DNA consensus sequence 5'-[AT]AA[TC]AAACAA[AT]-3'. Dosage dependent suppressor of calmodulin mutants which have specific defects in SPB assembly.
Involved in maintaining an adequate ionic strength homeostasis of the cellular aqueous environment, necessary for normal growth rate. Required for survival upon exposure to K1 killer toxin and hence plays a role in cell wall glucan synthesis. Required for dithiothreitol (DTT) resistance. Involved in cell cycle progression.
In TFIID, TAF8 heterodimerizes with TAF10. The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14.
Present with 4684 (+/-522) molecules/cell in log phase SD medium.
Associates specifically with the PHO80-PHO85 and PCL7-PHO85 cyclin-CDK complexes, and much of this interaction is mediated through the PHO80 and PCL7 cyclin subunits. Interacts with the transcription factor PHO4.
Inhibits the kinase activity of the cyclin-CDKs PHO80-PHO85 and PCL7-PHO85 under low-phosphate conditions.
Phosphorylated by the cyclin-CDK PHO80-PHO85. Phosphorylation mediates the formation of a stable interaction with the cyclin-CDK and is required for function as an active inhibitor of the complex under phosphate starvation conditions.
Component of the heterotrimeric Sec61 complex, which is composed of SSH1, SBH1 and SSS1. Presumably three to four Sec61 heterotrimers assemble into an oligomeric ring with a central aqueous pore. In cotranslational ER import, the pore diameter varies from 9-15 A in a ribosome-free resting state to 40-60 A in a functional state when associated with the ribosome. The Sec61 complex is part of a channel-forming translocon complex whose composition seem to change dependent upon different functional states. During post-translational ER import the Sec61 complex associates with the Sec62/63 complex to form the Sec complex. SBH1 interacts OST2, OST4 and WBP1 components of the OT complex.
Part of the Sec61 complex, which is the major component of a channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). The functional states of the translocon complex include co- and post-translational ER import, cotranslational membrane protein integration and retrograde transport of misfolded proteins out of the ER. In the cotranslational pathway, ribosomes synthesizing presecretory proteins are targeted to the translocon by the cytosolic signal recognition particle (SRP) and its ER-localized receptor. The association of the Sec61 complex with the ribosome is mediated by the 28S rRNA of the large ribosomal subunit. SRP-independent post-translational translocation requires the association of additional factors, such as the Sec62/63 complex and KAR2.
Carnitine O-acetyltransferase involved in the shutteling of acetyl-CoA in the cell.
Interacts with MYO2 (via C-terminal tail domain). Interacts with YIF1, YIP3, YIP4 and YIP5.
Involved in the positive control of both endoplasmic reticulum (ER) and mitochondrion inheritance during cell divison. Required for the MYO2-dependent retention of newly inherited mitochondria at the bud tip in developing daughter cells.
Present with 7180 molecules/cell in log phase SD medium.
Tetramer composed of an alpha chain, an alpha', one beta chain and one beta' chain (PubMed:12242279). Interacts with FACT subunits POB3 and SPT16 (PubMed:12242279). Interacts with YTA7 (PubMed:22156209).
Belongs to the membrane magnesium transporter (TC 1.A.67) family.
Interacts (via N-terminus) with GCN1 (via C-terminus); this interaction reduces the GCN1-GCN20 complex formation and prevents the interaction of GCN1 with GCN2 protein kinase and GCN2 activation in amino acid-starved cells (PubMed:15126500, PubMed:21239490). Interacts (via C-terminus) with ACT1; this interaction occurs in a GCN1-independent manner (PubMed:15126500, PubMed:21239490). Interacts with RPL39; this interaction occurs in a GCN1-independent manner (PubMed:22404850). Associates (via middle region) with ribosomes; this association occurs in a GCN1-independent manner and persists under amino acid starvation conditions (PubMed:22404850).
Translational regulator that ensures constant high levels of translation under amino acid starvation. Plays a role as a negative regulator of the GCN2 kinase activity; impairs GCN1-mediated GCN2 activation, and hence GCN2-mediated eIF-2-alpha phosphorylation in amino acid-starved cells and subsequent down-regulation of protein synthesis (PubMed:15126500, PubMed:15937339, PubMed:24333428). In normal conditions, it resides in a actin complex and has no activity (PubMed:15126500).
Involved in cellular morphogenesis. Required for traffic between late Golgi and early endosomes, and for the normal structure and organization of the endoplasmic reticulum.
A version of this protein truncated after amino acid 200 is not active in the beta-hydroxyethyl disulfide (HED) assay.
Active as '1-Cys' thiol transferase against beta-hydroxyethyl disulfide (HED), as dehydroascorbate reductase and as dimethylarsinic acid reductase, while not active against the standard GST substrate 1-chloro-2,4-dinitrobenzene (CDNB). May be involved in cell wall organization and biogenesis.
Under oxidative stress conditions. By agents such as diamide, 1-chloro-2,4-dinitrobenzene, tert-butyl hydroperoxide (t-BOOH) and cadmium in a transcriptional factors YAP1 and/or MSN2/4-dependent manner.
Acetylated by the NuA4 histone acetyltransferase (HAT) complex.
Homodimer and potential homooligomers. Interacts with ATG1 kinase and the ATG19 and ATG34 cargo protein transporters. Interacts with ATG9, ATG17, ATG20, ATG30, ATG32, ATG36 and YPT1.
Involved in cytoplasm to vacuole transport (Cvt), pexophagy, mitophagy and nucleophagy. Recruits mitochondria for their selective degradation via autophagy (mitophagy) during starvation, through its interaction with ATG32. Works as scaffold proteins that recruit ATG proteins to the pre-autophagosome (PAS), the site of vesicle/autophagosome formation. Required for ATG9 anterograde transport from the mitochondria to the PAS. Recruits also the ATG19-prAPE1 complex to the PAS. Required for the Cvt vesicles completion. Plays a significant role in life span extension.
Present with 86 molecules/cell in log phase SD medium.
Component of the NuA3 complex, which consists of at least NTO1, SAS3, TAF14, YNG1 and EAF6.
Component of the NuA3 histone acetyltransferase complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation.
Residues 156 to 543 compose a region conserved in chromatin associated proteins.
Present with 71 molecules/cell in log phase SD medium.
Putative mannosidase involved in glycoprotein quality control since it is involved in the targeting of misfolded glycoproteins for ER-associated protein degradation (ERAD).
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
GTPase-activating protein (GAP) for CDC42 and less efficiently for RHO1. Negative regulator of the pheromone-response pathway through the STE20 protein kinase.
Component of the ribosome quality control complex (RQC), composed of the E3 ubiquitin ligase RKR1/LTN1, RQC1 and RQC2, as well as CDC48 and its ubiquitin-binding cofactors associated with the 60S ribosomal subunits (PubMed:23178123, PubMed:23479637, PubMed:25349383).
E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation (PubMed:23178123). Mediates ubiquitination of proteins derived from mRNAs lacking stop codons (non-stop proteins) and other translation arrest products induced by poly-lysine sequences and tandem rare codons. Ubiquitination leads to CDC48 recruitment for extraction and degradation of the incomplete translation product (PubMed:20835226, PubMed:23825054, PubMed:24261871). May indirectly play a role in chromatin function and transcription (PubMed:17283062).
Present with 222 molecules/cell in log phase SD medium.
Controls the pre-rRNA processing machinery in conjunction with FHL1. Could convert FHL1 from a repressor to an activator.
Interacts with NOP19 (PubMed:21941128). Interacts with UBP10 (PubMed:22902402, PubMed:26149687).
Probable ATP-binding RNA helicase. Required for 18S rRNA synthesis.
Appears to be a structural component of the chitin synthase 3 complex.
Interacts (via OIR domain) with ORC1 (via BAH domain). Interacts with SIR4. Interacts with CAC1.
Involved in the establishment, but not the maintenance, of heterochromatic silencing at the cryptic mating-type loci HMR and HML. Is recruited by interacting with the ORC1 subunit of the origin recognition complex (ORC), which binds to HML-I or HMR-E silencers, DNA elements that direct the formation of silent chromatin at the mating-type loci. Establishes transcriptional silencing by recruiting the three other SIR proteins, SIR2, SIR3, and SIR4, that function directly in silenced chromatin and establish repression. Also found in centromeric chromatin. Binds to and helps retain CAC1, a subunit of chromatin assembly factor I (CAF-I) at centromeric loci independent on the other SIR proteins.
Present with 37105 molecules/cell in log phase SD medium.
Binds to vacuolar cis-SNARE complexes composed of the v-SNAREs NYV1, VTI1 and YKT6, and the t-SNAREs VAM3 and VAM7. Interacts with SEC18.
SNARE complex protein that binds to cis-SNARE complexes on membranes and is required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus and for homotypic vacuole fusion. During the priming step of membrane fusion, is released from cis-SNARE complexes by SEC18 to establish a pool of unpaired SNAREs, which are required for interactions in trans during docking and fusion steps. Can displace HOPS from SNARE complexes, which may be a prerequisite for trans-SNARE complex disassembly and subsequent rounds of priming, docking and fusion.
Interacts with HRI1 (PubMed:21460040). Interacts with ELP1/IKI3; the interaction leads to ELP1/IKI3 phosphorylation (PubMed:21460040).
Protein kinase which phosphorylates serine and threonine residues (PubMed:1495994). Can use casein as a substrate (PubMed:1495994). Phosphorylates elongator complex member ELP1/IKI3 on 'Ser-1198' and 'Ser-1202' which promotes the tRNA modification function of the complex (PubMed:25569479). Associated with repair of damaged DNA and meiosis (PubMed:1887218).
One of the three SNF1 protein kinases (with SAK1 and ELM1) which are required for growth on nonfermentable carbon sources and nonpreferred sugars and for response to environmental stress. Activates SNF1 by phosphorylation of its activation-loop 'Thr-210'. Required for the regulation by SNF1 of the transcription of a large set of genes, the modification the activity of metabolic enzymes, and the control of various nutrient-responsive cellular developmental processes. Phosphorylates also GAL83, MIG1 and SIP2.
The C-terminus (residues 351 to 560) is required for efficient SNF1 pathway signaling.
Essential for sporulation and seems to have a role at the time of, or after, initiation of nuclear division. Appears to have a role in outer spore wall formation.
Acts a component of the CCAT-binding factor, which is a transcriptional activator and binds to the upstream activation site (UAS2) of the CYC1 gene and other genes involved in mitochondrial electron transport and activates their expression. Recognizes the sequence 5'-CCAAT-3'.
Belongs to the NFYB/HAP3 subunit family.
Transports carnitine, acetylcarnitine, propionylcarnitine and to a much lower extent medium- and long-chain acylcarnitines.
Belongs to the DASH complex HSK3 family.
Belongs to the DASH complex DAD3 family.
ATP-dependent DNA helicase involved in DNA repair at least for UV-induced lesions. The polarity of the helicase activity was determined to be 3' to 5'.
Belongs to the TFIIE beta subunit family.
Present with 1150 molecules/cell in log phase SD medium.
Binds to platinated DNA and confers sensitivity to the anticancer drug cisplatin. Activate the expression of the COX5B gene.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RKM5 family.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates 60S ribosomal protein L1 (RPL1A and RPL1B) at 'Lys-46'.
Associates with the pre-40S ribosomal subunit. Component of the GSE complex composed of GTR1, GTR2, SLM4, MEH1 and LTV1. Interacts directly with GTR1. Interacts with CRM1.
Involved in protein transport. Non-ribosomal factor required for efficient nuclear export of the ribosomal 40S subunit. Component of the GSE complex, a GTPase complex required for intracellular sorting of GAP1 out of the endosome.
Phosphorylated, leading to its dissociation from the 40S pre-40S ribosome.
May act as a xanthine phosphoribosyltransferase involved in the synthesis of purine nucleotides. Such activity is however unclear in vivo.
Present with 6500 wall-bound molecules/cell in log phase YPD medium.
Required for proper cell wall integrity and for the correct assembly of the mannoprotein outer layer of the cell wall. Important for apical bud growth.
During exponential phase in rich medium and repressed in minimum medium, hyper-osmolar medium or in sporulating conditions.
This is a truncated version of aquaporin-2. In strain S288c and many laboratory strains, a natural 11 bp deletion in position 109 leads to a frameshift, which disrupts the gene coding for this protein and produces two ORFs YLL052C and YLL053C. A contiguous sequence for aquaporin-2 can be found in strain Sigma 1278B (AC P0CD89).
Water channel required to facilitate the transport of water across membranes. Involved in freeze tolerance, osmotolerance and cell flocculation in liquid cultures (By similarity). Is non-functional in most laboratory strains.
Belongs to the VAMP-associated protein (VAP) (TC 9.B.17) family.
Targets proteins containing a FFAT motif to membranes (By similarity). Involved in regulation of phospholipid metabolism.
The MSP domain is required for binding to the FFAT motif of target proteins.
Belongs to the glutamate synthase family.
Forms L-glutamate from L-glutamine and 2-oxoglutarate. Represents an alternative pathway to L-glutamate dehydrogenase for the biosynthesis of L-glutamate. Participates with glutamine synthetase in ammonia assimilation processes. The enzyme is specific for NADH, L-glutamine and 2-oxoglutarate.
Present with 18900 molecules/cell in log phase SD medium.
Belongs to the DASH complex DAD4 family.
Component of a cullin-RING ligase (CRL) composed of 4 subunits: the RING protein HRT1, the cullin RTT101, a linker protein MMS1, and the substrate receptor MMS22. This complex further interacts with RTT107 and CTF4 to form RTT101-MMS1-MMS22-RTT107 and RTT101-MMS1-MMS22-CTF4 complexes respectively. Interacts (via C-ter) with MMS1 (via N-ter). Interacts with RTT107.
Substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-MMS22). RTT101(MMS1-MMS22) promotes fork progression through damaged DNA or natural pause sites by stabilizing replication proteins like the replication fork-pausing complex (FPC) and leading-strand polymerase at stalled replication forks. RTT101(MMS1-MMS22) ubiquitinates the acetylated histones H3K56ac-H4 at lysine residues H3K121, H3K122 and H3K125. Ubiquitination is required for efficient histone deposition during replication-coupled nucleosome assembly, probably by facilitating the transfer of H3-H4 from ASF1 to other chaperones involved in histone deposition.
Both inositol and phosphate regulate GIT1 transcription and expression is positively regulated by the transcription factor PHO4 (PubMed:12912892).
Glycerophosphodiester transporter that mediates uptake of both glycerophosphoinositol (GroPIns) and glycerophosphocholine (GroPCho) as sources of the nutrients inositol and phosphate (PubMed:9691030, PubMed:12912892, PubMed:16141200).
Impairs the uptake of glycerophosphoinositol (GroPIns) (PubMed:9691030). Impairs also the uptake of glycerophosphocholine (GroPCho) (PubMed:9691030).
Acts as a negative regulator of polarized growth via an alternative mechanism to ZDS1. In heat-stressed cells appears to play a role in localizing BCY1 to the cytoplasm. Seems to interact with, and down-regulate, CDC42. Also acts as a suppressor of PKC1. May act as an integration point for distinct signaling pathways helping to maintain a balance among these different pathways.
Component of the nuclear pore complex (NPC) (PubMed:24152732). NPC constitutes the exclusive means of nucleocytoplasmic transport (PubMed:24152732). NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope (PubMed:24152732). Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof (PubMed:24152732). Interacts with NAB2, a hnRNP required for mRNA export (PubMed:12531921). Interacts with MLP2 (PubMed:16027220).
PubMed:8154186 misquoted the gene name as 'MPL1'.
Together with the closely related MLP2, involved in the structural and functional organization of perinuclear chromatin (PubMed:10638763). Together with MLP2, associates with the nuclear pore complex and form filamentous structures along the nuclear periphery (PubMed:10085285, PubMed:24152732). Has a role in the localization of Esc1 to nucleolar regions (PubMed:24152732). Together with MLP2, mediates tethering of the some telomeres to the nuclear periphery, probably mediated by YKU70/YKU80 (HDF1/HDF2) heterodimer and show perinuclear location dependent silencing (PubMed:11862215). MLP1 and MLP2 are involved in telomere length regulation but not silencing or telomere anchoring (PubMed:12490156). Recognizes the 5'-splice site of pre-mRNAs and retains unspliced pre-mRNA in the nucleus without affecting splicing itself (PubMed:12490156, PubMed:12531921, PubMed:14718167).
Required for correct translation termination and probably involved in regulation of hypoxic gene expression in association TPA1. Inhibits replication of Brome mosaic virus.
Involved in the selective degradation of mitochondria via autophagy during starvation and at post-log phase.
It appears that the main modified species for L12 contains 6 methyl groups, 2 on Pro-2, 3 on Lys-4 and 1 on Arg-67. Although not reproduced with a second method, methylation at Lys-11 cannot be ruled out.
Present with 50300 molecules/cell in log phase SD medium.
Present with 68500 molecules/cell in log phase SD medium.
Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 2 subfamily.
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). In mitochondria, constitutes the nondiscriminating glutamyl-tRNA synthase that generates the mitochondrial mischarged glutamyl-tRNA(Gln) substrate for the tRNA-dependent amidotransferase (AdT), which generates mitochondrial glutaminyl-tRNA(Gln) by transamidation of glutamyl-tRNA(Gln).
Present with 48700 molecules/cell in log phase SD medium.
Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome.
Interacts with RBG1 and with translating ribosomes.
Probable receptor, which is involved in metabolic pathways that regulate lipid metabolism such as fatty acid oxidation.
Regulated by OAF1 and PIP2. Highly expressed in presence of glucose. Expressed at lower level in presence of glycerol or glycerol and oleate. Highly expressed in the presence of saturated fatty-acids such as myristate.
By UV radiation and heat shock. The mRNA is stabilized during stationary phase.
DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. Efficiently incorporates nucleotides opposite to other UV or oxidative DNA damages like O(6)-methylguanine, 7,8-dihydro-8-oxoguanine, 2,6-diamino-4-hydroxy-5-formamidopyrimidine of 2'-deoxyguanosine (FaPydG), or p-benzoquinone DNA adducts.
Interacts with POL30. This interaction is essential for the polymerase eta function.
Component of the SUMO-targeted ubiquitin ligase (STUbL) complex SLX5/SLX8 that mediates ubiquitination and subsequent desumoylation of sumoylated proteins and proteins containing SUMO-like domains for their degradation (PubMed:11139495, PubMed:16325482, PubMed:18032921, PubMed:17669696, PubMed:17848550, PubMed:18499666, PubMed:18948542, PubMed:31015336). The STUbL complex SLX5/SLX8 stimulates ubiquitin conjugating enzymes, including UBC1, UBC4, UBC5 and UBC13-MMS2, and mediates the proteolytic down-regulation of sumoylated proteins (PubMed:18032921). The STUbL complex SLX5/SLX8 is involved in ubiquitin-mediated degradation of histone variant CSE4, preventing mislocalization to euchromatin (PubMed:26960795). The complex plays an essential role in maintenance of chromosome stability and links SUMO-dependent ubiquitination to a centromere-specific function during mitosis (PubMed:23785440). The complex is involved in proteolysis of spindle positioning protein KAR9 and ensures correct spindle function by regulating levels of microtubule-associated proteins (PubMed:26906737). During replication, the complex helps prevent DNA lesions via recombination and has a role in localizing the DNA damage protein DCD2 (PubMed:16325482, PubMed:17591698). The complex especially ubiquitinates the nuclease YEN1 and prevents persistent accumulation of a fraction of YEN1 associated with sites of activity in late G2/M and helps maintain the balance between pro- and anti-crossover pathways during homologous recombination (PubMed:30479332). It is also involved in ubiquitin-mediated degradation of DNA repair proteins RAD52 and RAD57 (PubMed:18032921). Along with SIR2, promotes silencing of genes at telomeric or ribosomal DNA (rDNA) loci (PubMed:18086879). Finally, the complex is recruited to distinct genomic hotspots of non-H2B protein ubiquitination (ub-hotspots) by the sumoylated transcription factor-like protein EUC1 where it ubiquitinates EUC1 and presumably other targets (PubMed:31015336).
Component of the heterodimeric SUMO-targeted ubiquitin ligase (STUbL) complex composed of SLX5 and SLX8 (PubMed:11139495, PubMed:18032921, PubMed:17669696, PubMed:17848550, PubMed:18948542). Interacts with sirtuin SIR2 (PubMed:18086879). Interacts with KAR9 (PubMed:26906737). Interacts with EUC1 (PubMed:31015336).
Leads to severe mitotic defects that include aneuploidy, spindle mispositioning, fish hooks and aberrant spindle kinetics.
The region between Ser-201 and Leu-335 is required recruitment of SLX5 to ub-hotspots via interacion with EUC1.
GTP-binding component of the eukaryotic elongation factor 1 complex (eEF1). In its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be recycled by its guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) before binding another molecule of aminoacyl-tRNA. Required for nuclear export of aminoacyl-tRNAs. May also be involved in translational quality control by targeting cotranslationally damaged proteins to the proteasome. Also exhibits actin filament-binding and -bundling activities and is involved in cytoskeleton organization. Plays a role as a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells (PubMed:21849502).
Present with 827 molecules/cell in log phase SD medium.
The eukaryotic elongation factor 1 complex (eEF1) is probably a heterohexamer. Two trimeric complexes, each composed of eEF1A (TEF1 or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or TEF4), are probably dimerized via the eF1Bgamma subunits. eEF1A interacts directly with eEF1Balpha. Interacts with elongation factor 3 (YEF3 or HEF3), BNI1, SRV2 and ZPR1. Binds to actin and forms a ternary complex with BNI1 and profilin. Interacts with the proteasome, probably via RPT1. Interacts with CEX1 and NAP1. Interacts with GCN2 (via C-terminus); this interaction is direct, occurs in amino acid-repleted cells, may be stabilzed in a ribosome-dependent manner, reduces GCN2-mediated eIF-2-alpha phosphorylation and is lost in amino acid-starved cells and by uncharged tRNAs (PubMed:21849502). Associates with ribosomes (PubMed:21849502).
High-conductance magnesium-selective channel that mediates the influx of magnesium into the mitochondrial matrix (PubMed:12628916, PubMed:17827224, PubMed:20653776, PubMed:23999289). Essential for the splicing of mRNA group II introns in mitochondria by affecting mitochondrial magnesium concentrations, which are critical for group II intron splicing. It also suppresses a variety of mitochondrial intron mutations and its absence may disturb the assembly of mitochondrial membrane complexes (PubMed:11544180).
Homopentamer (PubMed:23999289). Forms homooligomers. Interacts with MFM1 (PubMed:20653776).
Was originally (PubMed:1551905 and PubMed:8252639) identified in genetic screens for bona fide RNA splicing factors, but it has later been shown that not the MRS2 protein per se but certain magnesium concentrations are essential for group II intron splicing.
Part of a checkpoint which monitors spindle integrity and prevents premature exit from mitosis. This cell-cycle arrest depends upon inhibition of the GTP-binding protein TEM1 by the BFA1/BUB2 complex.
Catalyzes the deamidation of nicotinamide, an early step in the NAD(+) salvage pathway. Positively regulates SIR2-mediated silencing and longevity by preventing the accumulation of intracellular nicotinamide, an inhibitor of SIR2, during times of stress. Acts also on nicotinyl hydroxamate.
Has a cis-peptide bond at 162-Val-Ala-163.
Induced during the stationary phase of growth, by calorie restriction, by various hyperosmotic shocks or by low-intensity stress (at protein level).
Inhibited by N-ethylmaleimide, HgCl(2) and PCMB. Competitively inhibited by NAD, NMN and 3-acetylpyridine.
Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit plays a role in transcriptional response to stress. It is involved in both repression and activation of mRNAs regulated by the target of rapamycin (TOR) kinases, and in the synthesis of rRNA.
Forms a heterodimer with IML3 (PubMed:12589047, PubMed:24075991). CHL4-IML3 is part of a larger constitutive centromere-associated network (CCAN) (also known as central kinetochore CTF19 complex in yeast), which is composed of at least AME1, CHL4, CNN1, CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1 (PubMed:12408861, PubMed:22561346). Interacts with CTF3 and CTF19 (PubMed:12589047).
Component of the DSC E3 ligase complexes composed of at least TUL1, DSC2, DSC3, UBX3, CDC48 as well as VLD1 for the vacuole-localized complex or GLD1 for the Golgi/endosome-localized complex.
Component of the DSC E3 ubiquitin ligase complexes that tags proteins present in Golgi, endosome and vacuole membranes and function in protein homeostasis under non-stress conditions and support a role in protein quality control.
Could be the product of a pseudogene. YIL165C seems to be the C-terminal part of a putative nitrilase-like protein formed of NIT1/YIL164C and YIL165C.
Belongs to the complex I LYR family. SDHAF3 subfamily.
Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit SDH2 of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. Acts together with SDHAF1 (SDH6).
By ethanol (PubMed:8420957). Repressed by galactose (PubMed:8420957).
Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria.
Produced by alternative initiation at Met-23 of isoform Mitochondrial.
Involved in the repair of double-strand breaks in DNA during vegetative growth via recombination and single-strand annealing. Anneals complementary single-stranded DNA.
Associates with CYC8/SSN6 to form the CYC8-TUP1 (or TUP1-SSN6) corepressor complex that is composed of 4 copies of TUP1 and one copy of CYC8. Interacts with histone H3, histone H4, MATALPHA2, RFX1, SKO1, PGD1, HDA1, HDA2, HOS1, HOS2 and RPD3.
Present with 5840 molecules/cell in log phase SD medium.
ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. Contributes to the blocking of bulk poly(A)+ mRNA export in ethanol-stressed cells. May also be involved in early transcription.
Associates with the nuclear pore complex. Interacts with NUP159, GLE1, GFD1 and ZDS1. The interaction with NUP159 is necessary for the association to the nuclear pore complex. Interacts also with the TFIIH complex subunits TFB1, TFB2 and RAD3.
Belongs to the DEAD box helicase family. DDX19/DBP5 subfamily.
May be involved in vacuolar sorting and osmoregulation.
Essential determinant for low-affinity spermidine transport.
Interacts with the G protein beta-gamma subunit complex (STE4-STE18 complex).
Not essential for growth. Inhibits early G-protein signaling events following pheromone stimulation. May help create heterodimerizable beta-tubulin by facilitating the efficient transfer of nascent beta-tubulin polypeptides to the folding apparatus.
Plays a role in maintenance of chromatin structure during RNA polymerase II transcription elongation thereby repressing transcription initiation from cryptic promoters. Mediates the reassembly of nucleosomes onto the promoters of at least a selected set of genes during repression; the nucleosome reassembly is essential for transcriptional repression. Essential for viability.
Present with 8890 molecules/cell in log phase SD medium.
High copy suppressor of a cyclic AMP-dependent protein kinase mutant.
Component of the SSU processome, a pre-ribosomal particle required for the maturation of the 18S rRNA from the 35S pre-rRNA precursor.
Component of the ribosomal small subunit (SSU) processome, or 90S pre-ribosomal particle, composed of the 35S pre-rRNA precursor, the U3 snoRNA, and at least 40 protein subunits. Component of the PWP2/UTP-B subcomplex composed of DIP2, PWP2, UTP6, UTP13, UTP18 and UTP21. Interacts with U3 snoRNA. Interacts with MPP10.
Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1 subfamily.
Involved in the maintenance of proper DNA topology and chromosome integrity via annealing of single-stranded DNA breaks. Modulates DNA polymerase delta during replication or replication-associated repair. May function as a modulator for SGS1 when DNA is damaged.
Belongs to the SMC family. RAD50 subfamily.
Homodimer (By similarity). Forms a complex with MRE11.
Involved in DNA double-strand break repair (DSBR). The rad50/mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific exonuclease activity. Rad50 provides ATP-dependent control of mre11 by unwinding and/or repositioning DNA ends into the mre11 active site.
The zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another RAD50 molecule, thereby forming a V-shaped homodimer.
Compromises mitochondrial function and integrity, increases mitophagy (PubMed:27280386, PubMed:34830155, PubMed:32690699). Vacuolar protein missorting (PubMed:27280386, PubMed:28334785). Decreases number of clathrin-coated vesicles in cell (PubMed:34830155). Abnormal cortical reticulophagy; decreases packaging of endoplasmic reticulum (ER) into autophagosomes (PubMed:32690699). Abnormal sporulation; defective prospore membrane formation (PubMed:27280386, PubMed:24036347, PubMed:22442115). Accumulation of vesicles within the prospore membrane lumen and reduction of phosphatidylinositol and phosphatidic acid in the membrane (PubMed:22442115, PubMed:24036347). Abnormal actin cytoskeleton organization (PubMed:28334785). Sensitive to the arginine analog canavanine (PubMed:34830155, PubMed:28334785). Synthetic lethal with MMM1 (PubMed:26370498, PubMed:27280386). Localization of SPO71 to the prospore membrane is normal (PubMed:24036347).
Interacts (via SHR-BD domain) with SPO71 (via PxP motif); during prospore membrane formation (PubMed:24036347, PubMed:30018089). Interacts (via SHR-BD domain) with YPT35 (via PxP motif) (PubMed:30018089). Interacts (via SHR-BD domain) with MCP1 (via PxP motif) (PubMed:30018089, PubMed:28864540). Interacts with CDC31 (PubMed:28122955). Interacts (via C-terminus) with ARF1; the interaction is direct (PubMed:34830155). Interacts with the actin cytoskeleton (PubMed:28334785).
Mediates the transfer of lipids between membranes at organelle contact sites (PubMed:30093493, PubMed:24036347, PubMed:22442115). Binds phospholipids, including phosphatidic acid (PA), phosphorylated phosphatidylinositol (PI), phosphatidylcholine (PC), phosphatidylethanolamine (PE), ceramide, and phosphatidylserine (PS) (PubMed:30093493, PubMed:34830155, PubMed:28122955, PubMed:28334785). Involved in mitochondrial lipid homeostasis, in a MCP1-dependent manner (PubMed:27280386, PubMed:34830155, PubMed:32690699). Involved in cortical reticulophagy (also known as cortical endoplasmic reticulum (ER) macroautophagy), acting at the late endosome to package ER into autophagosomes (PubMed:32690699). Involved in the formation of the prospore membrane during sporulation, in a SPO71-dependent manner (PubMed:24036347, PubMed:22442115). Involved in Golgi vesicle transport, in a CDC31-dependent and ARF1-dependent manner (PubMed:28122955, PubMed:9314526, PubMed:34830155). Plays a role in actin cytoskeleton organization (PubMed:28334785).
The SHR-BD domain binds to PxP motifs found in interaction partners.
Converts monoacylglycerides (MAG) to free fatty acids and glycerol. Has a preference for palmitoyl-MAG (PubMed:26991558). Does not play a significant role in ethyl ester biosynthesis (PubMed:16361250). Also possesses ester hydrolase and low but persistent TAG lipase activity (PubMed:29225428).
Proton-conducting pore forming of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:1825730). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:1825730).
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and VOA1) (PubMed:25971514, PubMed:27776355, PubMed:29526695). The decameric c-ring forms the proton-conducting pore, and is composed of eight proteolipid subunits c, one subunit c' and one subunit c'' (PubMed:25971514, PubMed:27776355, PubMed:29526695).
Forms a conjugate with ATG5. Forms a thioester bond with the 'Cys-133' of ATG10. Interacts with the ATG7 C-terminal 40 amino acids domain. The ATG12-ATG5 conjugate forms a complex with several units of ATG16. The ATG12-ATG5 conjugate associates also with ATG3. Interacts with COG2.
Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes. ATG12-ATG5 rearranges the ATG3 catalytic center and enhances its E2 activity.
Responsible for conferring a stable 5'-end on cytochrome b mRNA.
Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
Belongs to the protein N5-glutamine methyltransferase family.
Methylates MRF1 on 'Gln-287' using S-adenosyl L-methionine as methyl donor.
Catalyzes the isomerization of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR.
External NADH dehydrogenase required for optimum cellular growth with a number of nonfermentable carbon sources, including ethanol. With NDE2, performes the mitochondrial oxidation of cytosolic NADH under these growth conditions. Regulates the mitochondrial glycerol-3-phosphate dehydrogenase, GUT2, also involved in cytosolic NADH oxidation.
Component of a microsomal membrane-bound long-chain fatty acid elongation system, which produces the 20-26-carbon very long-chain fatty acids (VLCFA) from long-chain fatty acid precursors and is involved ceramide and inositol sphingolipid biosynthesis. Component of elongase II, which elongates 16-18 carbon fatty acyl-CoAs such as palmitoyl-CoA and stearoyl-CoA to 20-22-carbon fatty acids by incorporation of malonyl-CoA (PubMed:9211877, PubMed:12684876). Involved in the synthesis of 1,3-beta-glucan (PubMed:7768822). The enzymes active site faces the cytosol, whereas VLCFA length is determined by a lysine near the luminal end of transmembrane helix 6 (PubMed:17719544). Plays an important role in lipotoxic cell death induced by oleic acid through maintaining a balanced fatty acid composition in thr plasma membrane (PubMed:29458843).
The C-terminal di-lysine-like motif may confer endoplasmic reticulum localization.
Phosphorylation is not involved in the interaction of the acidic P proteins with the ribosome, however it is suggested to affect the ribosome activity and to participate in a possible ribosome regulatory mechanism.
Present with 428000 molecules/cell in log phase SD medium.
Interacts with VPS21, VPS45, PEP3 and PEP5.
Required for vacuole segregation and vacuole protein sorting. Possibly part of a complex which tethers the vacuole membrane to microtubules, either directly or via kinesin or dynein-like motor proteins. Probably functions in several interorganelle traffic pathways.
Mitochondrial inner membrane carrier protein that mediates the import of NAD(+) into mitochondria (PubMed:16291748, PubMed:32906142, PubMed:33087354). Can transport NAD(+) by unidirectional transport or by exchange with intramitochondrially generated dAMP and dGMP (PubMed:16291748). Also able to transport NAD(+) by exchange with AMP, GMP or deamido-NAD (+) in vitro (PubMed:16291748).
Was first identified as the mitochondrial pyruvate transporter (PubMed:12887330). However, later experiments showed that was a NAD(+) transporter (PubMed:16291748).
Component of the septin complex which consists of CDC3, CDC10, CDC11, CDC12 and probably SHS1 and rearranges to a cortical collar of highly ordered filaments at the mother-bud-neck. A complex formed by CDC3, CDC10, CDC11 and CDC12 is capable of forming long filaments in vitro and the components seem to be present in a 2:2:2:2 arrangement in vivo. The filaments are proposed to be formed by the end-to-end polymerization of CDC3-CDC12-CDC11 complexes with CDC10 serving as a bridge to bundle the polymers into paired filaments. Component of the GIN4 complex composed of at least BNI5, CDC3, CDC10, CDC11, CDC12, GIN4, NAP1 and SHS1. Self-associates. Interacts with BEM4, KCC4, SPR28 and SYP1.
Present with 9280 molecules/cell in log phase SD medium.
The basic motif is essential for the association with PI(4)P and PI(5)P.
The coiled coil domain is required for the interaction with CDC3 and BEM4, but not for interaction with CDC12 or with itself.
Binds 1 magnesium ion per subunit. Can also use Zn(2+) as cofactor.
Blocks galactose utilization, but does not impair growth on glucose.
Induced in response to galactose and severely repressed in response to glucose.
Major phosphoglucomutase isozyme that catalyzes the reversible interconversion of glucose 1-phosphate and glucose 6-phosphate (PubMed:5784209). Constitutes about 80-90% of the phosphoglucomutase activity in the cell (PubMed:14264884, PubMed:5231755). Key enzyme in hexose metabolism. The forward reaction is an essential step in the energy metabolism of galactose since the product of the galactose pathway enzymes in yeast is glucose 1-phosphate. The reverse reaction is an essential step for biosynthesis when carbon sources other than galactose are the energy source because glucose 1-phosphate is the starting point for the synthesis of UDP-glucose, which acts as a precursor for the synthesis of oligosaccharides and trehalose (PubMed:14264884).
O-glycosylated with mannose residues (By similarity). Substrate of UDP-glucose--glycoprotein glucose phosphotransferase, linking glucose in a phosphodiester linkage to O-linked mannose (PubMed:8385141, PubMed:7929458).
Present with 3790 molecules/cell in log phase SD medium.
May be involved in assembly and disassembly of the actin cytoskeleton.
Belongs to the anion exchanger (TC 2.A.31) family.
Functions in boric acid/borate export across the plasma membrane, and thereby protects yeast cells from boron toxicity. Involved in the trafficking of proteins to the vacuole.
Homodimer. Interacts with POL30, RAD18, UBC9 and UBC13.
Probable helicase, member of the UBC2/RAD6 epistasis group. Functions with the DNA repair protein RAD18 in error-free postreplication DNA repair. Involved in the maintenance of wild-type rates of instability of simple repetitive sequences such as poly(GT) repeats. Seems to be involved in maintaining a balance which acts in favor of error-prone non-homologous joining during DNA double-strand breaks repairs. Recruits the UBC13-MMS2 dimer to chromatin for DNA repair.
Component of the cell wall. Major cell wall protein in stationary phase cells. Required to stabilize the cell wall in the absence of multiple GPI-anchored mannoproteins.
Induced in stationary phase and under conditions of stress and starvation (at protein level).
Involved in membrane organization. Required for the formation of membrane compartments of CAN1 (MCCs), localization of CAN1 at the MCCs and subsequent invagination of the plasma membrane at the MCCs sites. Involved in eisosome organization and might act as a sensor of sphingolipids that regulates plasma membrane function. Involved in a novel pathway of export of proteins that lack a cleavable signal sequence. It may be an accessory subunit to an essential core component of the non-classical export machinery. Non-classical export pathway functions also as an alternative clearance/detoxification pathway to eliminate damaged material, when the basic repair pathway is not sufficient.
The C terminus is necessary to target MCC-specific transporters into MCC and for the formation of the plasma membrane invaginations.
Present with 5820 molecules/cell in log phase SD medium.
Belongs to the CDP-alcohol phosphatidyltransferase class-II family.
Essential for the viability of mitochondrial petite mutant. Catalyzes the committed step to the synthesis of the acidic phospholipids.
Belongs to the calcineurin regulatory subunit family.
Composed of a catalytic subunit (A) and a regulatory subunit (B).
Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
This protein has four functional calcium-binding sites.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RMT2 methyltransferase family.
Monomer. Interacts with nucleoporins NUP49, NUP57 and NUP100.
S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that methylates the delta-nitrogen atom of arginine residues to form N5-methylarginine (type IV) in target proteins (PubMed:9873020). Monomethylates ribosomal protein L12 (RPL12A/RPL12B) at 'Arg-67' (PubMed:11856739).
Belongs to the cAMP-dependent kinase regulatory chain family.
Binding of cAMP to the 2 tandem cyclic-nucleotide binding domains (CNB-A and CNB-B) induces a conformational change in BCY1, causing the interaction surface with the catalytic subunit to be destroyed and eventually the dissociation of the R dimer from the C subunits.
Phosphorylated by YAK1 in response to glucose starvation. Phosphorylated by MCK1 at Thr-129 upon TOR complex 1 (TORC1) inhibition. Thr-129 phosphorylation activates BCY1 to inhibit PKA. TORC1 inhibits phosphorylation of RxxS/T sites but has no effect on Ser-145 phosphorylation. The phosphorylation sites can be clustered in several groups, all localized in the N-terminal part. The first cluster termed cluster I (CI) is located close to the N-terminus and includes Ser-3, Ser-4 and Ser-9 (PubMed:11134339, PubMed:12704202). The second includes Ser-68, Ser-70, Ser-74, Ser-77, Ser-79, Ser-81, Ser-83, and Ser-84. This cluster of phosphorylation sites, termed cluster II (CII), is important for BCY1 cytoplasmic localization and function (PubMed:11134339, PubMed:12704202, PubMed:20702584). The third cluster of phosphorylated residues consists of Thr-144, Ser-145, Ser-147, Thr-150, and Thr-160. This cluster falls within or near the so-called autoinhibitory domain where the catalytic subunit of PKA autophosphorylates the highly conserved Ser-145 to inhibit BCY1 (PubMed:20702584). A last cluster of phosphorylated residues included Thr-129, Ser-130, and Thr-131 and is termed cluster III (CIII). Sites in CIII (and to a lesser extent in CII) are hyperphosphorylated in response to rapamycin (PubMed:20702584).
Regulatory subunit of the cyclic AMP-dependent protein kinase (PKA), an effector of the Ras/cAMP pathway. Inhibits PKA activity in the absence of cAMP. cAMP activates PKA and promotes growth and proliferation in response to good nutrient conditions. Together with ZDS1, provides a negative feedback control on the cell wall integrity-signaling pathway by acting as a negative regulator of MAP kinase SLT2/MPK1.
The inactive holoenzyme of cAMP-dependent protein kinase is a tetramer, composed of 2 regulatory subunits (R, encoded by BCY1) and two catalytic subunits (C, encoded by the 3 partially redundant TPK1, TPK2, and TPK3 genes). Activation by cAMP causes dissociation of the holoenzyme, producing 2 active catalytic monomers C and a regulatory dimer R(2).
The inhibitor sequence (IS) is a substrate recognition motif that docks to the active site cleft of the catalytic subunit rendering the holoenzyme inactive.
Acts as a component of chromatin assembly factor 1 (CAF-1), which assembles histone octamers onto replicating DNA in vitro. It performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. p50 and p60 form complexes with newly synthesized histones H3 and acetylated H4 in cell extracts (By similarity).
Component of chromatin assembly factor 1 (CAF-1), which is composed of MSI1/p50, CAC2/p60 and CAC1/p90 (Probable). Interacts with RTT106 (PubMed:19683497).
Involved in telomere length regulation and required for survival upon exposure to K1 killer toxin. Promotes fully efficient non-homologous end-joining (NHEJ) by a mechanism activated in postdiauxic/stationary phase.
Phosphorylation is required for PDR12 induction.
transcription factor which binds to a weak acid response element (WARE) to mediate stress induction of PDR12 and FUN34, encoding an acid transporter and a putative ammonia transporter, respectively.
Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them.
Belongs to the mediator complex subunit 2 family.
Present with 10785 molecules/cell in log phase SD medium.
Involved in the biogenesis of the 60S ribosomal subunit. May act as a specificity factor that binds precursor rRNAs and tethers the enzymes that carry out the early 5' to 3' exonucleolytic reactions that generate the mature rRNAs.
(orthologuous-specific) Binds to aminoacylated tRNA(Phe) less tightly than to deacylated tRNA(Phe) (PubMed:10983975). Binds to double-stranded RNA (PubMed:9430731).
Abolishes phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/SUI2) during amino acid, purine, and glucose starvation (PubMed:8336737, PubMed:10733573). Inhibits GCN4 derepression in glucose, amino acid, or purine-starved cells (PubMed:8336737, PubMed:10733573). Decreases vacuolar free amino acid levels during glucose starvation (PubMed:10733573). Sensitive to the purine analog 8-azaadenine (PubMed:8336737). Increases duration of lag phase on return to glucose-rich medium following glucose starvation (PubMed:10733573).
Autophosphorylated, autophosphorylation on Thr-882 and Thr-887 increases kinase activity.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily.
Homodimer; homodimerization is important for kinase activation by uncharged tRNAs (PubMed:9566889, PubMed:10983975, PubMed:11250908, PubMed:17202131, PubMed:15964839). Interacts (via N-terminal RWD domain) with GCN1 (via N- and C-terminus); this interaction stimulates GCN2 kinase activity in a GCN20-dependent manner in response to amino acid starvation (PubMed:10775272, PubMed:11101534, PubMed:10801780, PubMed:11350982, PubMed:21849502). Interacts (via N-terminus) with the GCN1-GCN20 complex on translating ribosomes in amino acid-starved cells; GCN1 may bind near the ribosomal A-site and promotes the transfer of uncharged tRNAs from the A-site to the tRNA-binding domain in GCN2 for its subsequent kinase activation, and hence allowing GCN4 translational activation and derepression of amino acid biosynthetic genes (PubMed:10775272, PubMed:11101534). Interacts (via C-terminus) with TIF11; this interaction is direct, occurs in amino acid-repleted cells, may be stabilzed in a ribosome-dependent manner, reduces GCN2-mediated eIF-2-alpha phosphorylation but not GCN2 autophosphorylation and is lost in amino acid-starved cells and by uncharged tRNAs (PubMed:21849502). Associates (via C-terminus) with ribosomes (PubMed:2038314, PubMed:9430731, PubMed:10983975, PubMed:22888004).
Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/SUI2) on 'Ser-52' in response to low amino acid, carbon, or purine availability (PubMed:1739968, PubMed:7623840, PubMed:8798780, PubMed:9528799, PubMed:10983975, PubMed:17202131, PubMed:8336737, PubMed:10733573). Plays a role as an activator of the general amino acid control (GAAC) pathway required for adapatation to nutrient starvation. Converts phosphorylated eIF-2-alpha/SUI2 either to a competitive inhibitor of translation initiation factor eIF-2B, leading to a global protein synthesis repression, and thus to a reduced overall utilization of amino acids, or to a translational initiation activation of specific mRNAs, such as the transcriptional activator GCN4, and hence allowing GCN4-mediated reprogramming of transcription to alleviate nutrient depletion (PubMed:2660141, PubMed:2188100, PubMed:1739968, PubMed:7621831, PubMed:7623840, PubMed:8798780, PubMed:10801780, PubMed:11350982, PubMed:24333428, PubMed:10733573). Binds uncharged tRNAs (PubMed:7623840, PubMed:10983975).
The C-terminal domain negatively regulates kinase activity via an autoinhibitory association with the protein kinase and histidyl-tRNA synthetase-like domains in amino acid-repleted cells, that is counteracted by uncharged tRNAs in amino acid-starved cells (PubMed:7623840, PubMed:8798780, PubMed:10983975, PubMed:11250908). The C-terminal, histidyl-tRNA synthetase-like region and protein kinase domains are necessary for homodimer formation (PubMed:9566889, PubMed:10983975, PubMed:11250908). The C-terminal and protein kinase domains are necessary for ribosome association (PubMed:9566889, PubMed:10983975). The C-terminal and histidyl-tRNA synthetase-like regions are required for uncharged tRNAs binding in amino acid-starved cells (PubMed:7623840, PubMed:8798780, PubMed:9430731, PubMed:10983975).
The kinase activity is stimulated upon binding to uncharged tRNAs (PubMed:7623840).
Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation.
Controls the nucleo-mitochondrial dependence of galactose, maltose and raffinose utilization. Becomes essential in the absence of functioning mitochondria.
Contributes to proper distribution and/or efficient assembly of nuclear pores. Required for normal pore density in the daughter nucleus during telophase.
Belongs to the TRAFAC class translation factor GTPase superfamily. Bms1-like GTPase family. BMS1 subfamily.
May act as a molecular switch during maturation of the 40S ribosomal subunit in the nucleolus. The depletion of BMS1 interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits.
Involved in cell wall composition and integrity and response to osmotic stress.
Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in bud site selection maybe via the regulation of expression of bipolar budding components.
Cytosolic inhibitor of vacuolar proteinase B (yscB), probably regulating protease B activity during limited proteolysis. PBI2 is a component of the LMA1 complex, which is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi.
Originally, 2 inhibitors of protease B, inhibitor I(B)2 and inhibitor I(B)1, have been isolated from commercial baker's yeast, which consists of both S.cerevisiae and S.carlsbergensis. It has been shown that S.cerevisiae only produces inhibitor 2, and S.carlsbergensis only produces inhibitor 1 (PubMed:328499). A sequence for inhibitor 1 from S.carlsbergensis has been determined (AC P0CT05).
Part of the heterodimeric LMA1 complex together with the thioredoxin II/TRX2. LMA1 binds to the ATPase SEC18.
Present with 2753 molecules/cell in log phase SD medium.
The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. Interacts with AMA1.
Interacts with SNX3, TVP18, TVP23, YIP1 and YIP4. Interacts with SEC4; The C-terminal cysteines in the Rab GTPase SEC4 are essential for the interaction. Interacts with YPT1, YPT6, YPT7, YPT10, YPT11, YPT31, YPT32 and YPT52; These proteins are all Rab GTPases.
Possible role in vesicle-mediated transport. May be involved in proper membrane localization of Rab GTPases.
Expression is increased during growth on glucose, in the presence of heme, and during oxygen limiting growth conditions and, unexpectedly, during anaerobic growth (PubMed:1730736). Two upstream activating sequences, UASl and UASZ, and an upstream repressor element, URS1, plus a second possible or cryptic repressor element, URSP, are present in promoter (PubMed:1730736). HAP1 participates in activation from UASl but not from UAS2, whereas the ROXl repressor represses expressio of ERG11 (PubMed:1730736).
It is the main target for antifungal compounds of the triazole family like ketoconazole which inhibits by coordinating the iron atom at the sixth ligand position.
Lanosterol 14-alpha demethylase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:369554, PubMed:105731). ERG11 catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis (PubMed:369554, PubMed:105731). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672).
Present with 73200 molecules/cell in log phase SD medium.
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in the anticodon loop on a specific subset of tRNAs both in the cytosol and the mitochondrion, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). This modification optimizes the codon:anticodon fit in the ribosome and promotes translational fidelity. Competes with the farnesyl pyrophosphate synthase ERG20 for the common substrate dimethylallyl diphosphate (DMAPP).
The core aggregation region, although lacking the prion-typical Gln/Asn (Q/N)-rich domain, is required for the formation of the amyloid-like fibrillar aggregates.
[MOD+] is the prion form of MOD5. [MOD+] is the result of a conformational change of the cellular MOD5 protein that becomes self-propagating and infectious. This conformational change generates a form of MOD5 that assembles into amyloid-like fibrillar aggregates. [MOD+]-aggregates sequester soluble MOD5, resulting in decreased levels of (i(6)A)-modified tRNAs and higher ergosterol levels, due to less competition for ERG20, which uses the same substrate DMAPP than MOD5. [MOD+] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [MOD+] propagation. The [MOD+] state acquires resistance against antifungal agents such as flucanozole, ketoconazole and clotrimazole that inhibit ergosterol biosynthesis. De novo appearance of [MOD+] is favored in the presence of antifungal agents, and the growth advantage of [MOD+] is lost when the cells are released from the selective pressure. Thus, the conformational switch of MOD5 from a soluble state to a prion state allows the cell to adapt to the harmful environment of anti-fungal drugs by up-regulating ergosterol biosynthesis at the expense of tRNA modification.
Belongs to the 'GDXG' lipolytic enzyme family.
Required for the deacetylation of acetylated sterols. Involved in the resistance to eugenol and pregnenolone toxicity.
By UV light, methyl methane-sulfonate (MMS) or hydroxyurea (HU), and during meiosis.
Homotrimerization occurs through formation of a three-stranded coiled-coil structure generated by intermolecular interactions between HR-A/B regions allowing DNA-binding activity.
The phosphorelay mechanism involves the sequential transfer of a phosphate group from 'His-576' (H1) to 'Asp-1144' (D1) of SLN1, then to 'His-64' (H2) of YPD1 and finally to Asp-427 (D2) of SKN7.
Transcription factor that is part of a SLN1-YPD1-SKN7 two-component regulatory system, which controls gene expression in response to changes in the osmolarity of the extracellular environment. Under low osmotic conditions, phosphorylated and activated by the phosphorelay intermediate protein YPD1. Also activated in response to oxidative stress, independent on the two-component regulatory system. Regulates heat shock genes in response to oxidative stress and genes involved in cell wall integrity in response to osmotic changes.
Impairs the formation of autophagosomes (PubMed:28704456). Completely blocks the movement of the ER-staining dye R18 from the ER to IM precursors (PubMed:28704456).
Interacts with ATG18 (PubMed:17295840, PubMed:18586673, PubMed:22851171, PubMed:23230146, PubMed:30254161). Interacts with ATG9 (PubMed:29848619).
Lipid transfer protein required for autophagosome completion and peroxisome degradation (PubMed:8224160, PubMed:10029994, PubMed:11382760, PubMed:11382761, PubMed:11675007, PubMed:18586673, PubMed:18625846, PubMed:19371383, PubMed:19995911, PubMed:22728243, PubMed:23230146). Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion (PubMed:28704456, PubMed:29848619, PubMed:30254161). ATG2 binds to the ER exit site (ERES), which is the membrane source for autophagosome formation, using basic residues in its N-terminal region (NR) and to the expanding edge of the IM through its C-terminal region (PubMed:30254161). The latter binding is assisted by an ATG18-PtdIns3P interaction (PubMed:30254161). ATG2 then extracts phospholipids from the membrane source using its NR and transfers them to ATG9 to the IM through its predicted beta-sheet-rich structure for membrane expansion (PubMed:30254161). ATG2 is also involved in the recruitment of lipids to a restricted region close to the vacuole, termed the vacuole-isolation membrane contact site (VICS), which is also essential for autophagosome formation (PubMed:28704456). Necessary for the localization of ATG18 to the preautophagosomal structure (PAS) and the binding of ATG18 to ATG9 (PubMed:14723849, PubMed:18586673, PubMed:18625846, PubMed:19371383, PubMed:23230146). ATG2 is the most downstream ATG protein in the preautophagosomal structure organization process (PubMed:17295840). Involved in correct ATG9 trafficking through the preautophagosomal structure and in peroxisome degradation (PubMed:14723849). Plays a significant role in life span extension (PubMed:23337777).
The N-terminal region (NR) associates with the endoplasmic reticulum (ER) and is responsible for the formation of the isolation membrane at the PAS.
The amphipathic helix in the C-terminal region binds to membranes and facilitates ATG18 binding to PtdIns3P to target the ATG2-ATG18 complex to the PAS.
Specifically phosphorylates NAD in the presence of ATP, dATP, or CTP as phosphoryl donors.
Acts a component of the CCAT-binding factor, which is a transcriptional activator and binds to the upstream activation site (UAS2) of the CYC1 gene and other genes involved in mitochondrial electron transport and activates their expression. Recognizes the sequence 5'-CCAAT-3'. HAP5 is essential for DNA-binding activity. It may be the linchpin that binds to the subunit association domains (SAD) of HAP2 and HAP3 to bring these proteins together.
Belongs to the NFYC/HAP5 subunit family.
Required for resistance to the DNA-damaging agents methyl methanesulfonate (MMS), cisplatin and oxaliplatin, but not to mitomycin C. Plays a role in protection against mutation accumulation. May be a component of the recombination-repair pathway.
Component of the DOA10 ubiquitin ligase complex which contains E3 ligase SSM4/DOA10 and CDC48-binding protein UBX2/SEL1 (PubMed:16873066). Component of the HRD1 ubiquitin ligase complex which contains the E3 ligase HRD1, its cofactors HRD3, USA1 and DER1, substrate recruiting factor YOS9 and UBX2 (PubMed:16873066). In ERAD-L, HRD3 and YOS9 jointly bind misfolded glycoproteins in the endoplasmic reticulum (ER) lumen (PubMed:32327568). Movement of ERAD-L substrates through the ER membrane is facilitated by HRD1 and DER1 which have lateral gates facing each other and which distort the membrane region between the lateral gates, making it much thinner than a normal phospholipid bilayer (PubMed:32327568). Substrates insert into the membrane as a hairpin loop with one strand interacting with DER1 and the other with HRD1 (PubMed:32327568). Both the DOA10 and HRD1 ubiquitin ligase complexes interact with the heterotrimeric CDC48-NPL4-UFD1 ATPase complex which is recruited by UBX2 via its interaction with CDC48 and which moves ubiquitinated substrates to the cytosol for targeting to the proteasome (PubMed:15258615, PubMed:16179953, PubMed:16179952, PubMed:16873066).
Integral endoplasmic reticulum membrane protein that coordinates the assembly of the ER-associated protein degradation (ERAD) machinery at the ER membrane. Mediates binding of CDC48 to the E3 ubiquitin ligases SSM4/DOA10 and HRD1, and to ERAD substrates. Component of the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains. ERAD-C substrates are ubiquitinated through DOA10 in conjunction with the E2 ubiquitin-conjugating enzymes UBC6 and UBC7-CUE1. Also a component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). ERAD-L substrates are ubiquitinated through HRD1 in conjunction with the E2 ubiquitin-conjugating enzymes UBC1 and UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via the action of the CDC48-NPL4-UFD1 ATPase complex and targeted to the proteasome.
Probably cooperates with other heat shock proteins in the translocation of polypeptides through membranes. It may counteract the altering effect of heat shock on the plasma membrane.
Interacts with SNF1 kinase; via catalytic domain. Interacts with the glucose sensors SNF3 and RGT2.
Involved in modulation of glucose-regulated gene expression. Together with MTH1, represses the hexose transporter (HXT) genes in conditions of low glucose. Stimulates the SNF1 kinase by an interaction with the catalytic domain that antagonizes autoinhibition and promotes an active conformation of the kinase.
Acts as a negative regulator of the GCN2 kinase activity by disrupting the GCN1-GCN2 interaction in amino acid-starved cells (PubMed:19448108).
Interacts with GCN1; this interaction prevents the interaction of GCN1 with GCN2 protein kinase and GCN2 activation in amino acid-starved cells (PubMed:19448108). Interacts with RBG1 (PubMed:19448108). Associates with ribosomes; the association occurs in a GCN1-dependent manner (PubMed:19448108).
Lack of SFT2 is lethal in a strain lacking GOT1.
Nonessential protein required for the fusion of transport vesicles derived from the endocytic pathway with the Golgi complex. Can be partially replaced by GOT1.
Present with 7200 molecules/cell in log phase SD medium.
Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly. TUB4 is an important spindle pole body component that organizes both cytoplasmic and nuclear microtubule arrays.
Replication factor C (RFC) is a heteropentamer of subunits RFC1, RFC2, RFC3, RFC4 and RFC5 and forms a complex with POL30/PCNA in the presence of ATP. Component of the RAD24-RFC complex which consists of RAD24, RFC2, RFC3, RFC4 and RFC5 and associates with the checkpoint clamp DDC1:MEC3:RAD17 complex. Component of the ELG1-RFC complex which consists of ELG1, RFC2, RFC3, RFC4 and RFC5. Component of the CTF18-RFC complex, which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. RFC5 interacts with ECO1.
May play a role in retrograde transport of proteins from the Golgi to the endoplasmic reticulum.
Belongs to the DNA polymerase type-B-like family.
Catalytic subunit of the TRAMP5 complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates like cryptic transcripts generated by RNA polymerase II and III, or hypomethylated pre-tRNAi-Met. Polyadenylates RNA processing and degradation intermediates of snRNAs, snoRNAs and mRNAs that accumulate in strains lacking a functional exosome. TRF5 is also required for proper nuclear division in mitosis and sister chromatid cohesion. Involved in the regulation of histone mRNA levels. May mediate mitotic chromosome condensation.
Component of the TRAMP5 complex composed of at least AIR1, MTR4 and TFR5. Interacts with POL2, DPB2 and DPB11.
Was originally thought to have DNA polymerase activity.
Belongs to the arrestin family. PalF/RIM8 subfamily.
Expressed under acidic conditions and repressed by the processed, active form of RIM101 under alkaline conditions.
Required for the proteolytic cleavage of the transcriptional repressor RIM101 in response to alkaline ambient pH, which is necessary for sporulation and invasive growth.
Interacts with KRR1, NOP1, NSR1, PUF6 and UTP22, proteins involved in 18S rRNA synthesis. Interacts also with ribosomal proteins RPS1, RPS3, RPS4, RPS6, RPS11, RPL2, RPL3, RPL4, RPL7, RPL10, RPL20 and RPP0 as well as with the snoRNAs U3 and U14.
Involved in the 18S rRNA synthesis. Required for the early cleavages at sites A0, A1 and A2.
Required for telomeric clustering (bouquet stage) during meiosis 1 prophase, formation and efficient homolog pairing, meiosis 1 disjunction, and telomere deletion during meiosis. Promotes also meiotic recombination.
Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton.
Present with 8570 molecules/cell in log phase SD medium.
Required for normal export of the pre-40S particles from the nucleus to the cytoplasm. Its subcellular location and association with pre-40S subunit shifts from mixed cytoplasm/nucleus to all nuclear in RPS19 disruptions, suggesting it acts after the ribosomal protein.
Phosphorylated at Ser-457 by the TORC1 effector kinase NPR1 under nitrogen-limiting conditions which causes a conformational change in the C-terminal region (CTR) to form an open active conformation (PubMed:24476960, PubMed:27088325). Supplementation of nitrogen source leads to inactivation and instant Ser-457 dephosphorylation via plasma membrane PSR1 and PSR2 redundant phosphatases (PubMed:24476960).
The residue Asn-4 of the protein's N-terminal tail is the only site that is glycosylated.
Transporter for ammonium (both charged and uncharged NH3 and NH4) to use as a nitrogen source (PubMed:11069679, PubMed:11486013, PubMed:9234685, PubMed:9482721, PubMed:16477434, PubMed:18434596, PubMed:24476960, PubMed:27088325). The affinity of MEP2 is about twenty times higher than that of MEP1 (PubMed:9482721). MEP3 has the lowest affinity (PubMed:9482721). Under ammonium limitation acts as an ammonium sensor, generating a signal that leads to pseudohyphal (filamentous) growth (PubMed:9482721, PubMed:11069679, PubMed:16477434, PubMed:18434596, PubMed:32069286).
Within the cytoplasmic CTD, an enhancer domain, limited to residues 428-441, upregulates substrate translocation via the MEP2 hydrophobic core, while an autoinhibitory domain, comprised within the 450-485 region and including the NPR1-target serine Ser-457, counteracts the action of the enhancer domain (PubMed:32069286). In between, a linker domain, limited to residues 442-449, appears required for optimal activity when the kinase is present but dispensable when the kinase integrity is altered (PubMed:32069286).
RNA-binding protein that acts as a post-transcriptional regulator of phosphate metabolism by binding to the 3'-UTR region of PHO4 mRNA, decreasing its stability (PubMed:24206186). Acts by recognizing and binding N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs (PubMed:24269006, PubMed:26318451).
Belongs to the CWC16 family. YJU2 subfamily.
Component of the spliceosome. Present in the activated B complex, the catalytically activated B* complex which catalyzes the branching, the catalytic step 1 C complex catalyzing the exon ligation, and the postcatalytic P complex containing the ligated exons (mRNA) and the excised lariat intron (PubMed:19935684, PubMed:27445308, PubMed:27459055, PubMed:29146871). Interacts (via C-terminus) with CLF1 (PubMed:23438600). Interacts (via N-terminus) with SYF1 (PubMed:23438600). Interacts with U2 snRNA; this interaction is direct (PubMed:23438600). Identified in the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2 (PubMed:11884590).
Expressed in exponential-phase cells grown in rich medium.
Part of the spliceosome which catalyzes two sequential transesterification reactions, first the excision of the non-coding intron from pre-mRNA and then the ligation of the coding exons to form the mature mRNA (PubMed:19935684, PubMed:27445308, PubMed:27459055, PubMed:29146871). Plays a role (via N-terminus) in stabilizing the structure of the spliceosome catalytic core and docking of the branch helix into the active site, producing 5'-exon and lariat intron-3'-intermediates (PubMed:23438600, PubMed:27459055). Further stabilizes spliceosome conformation for 3'-splice site docking (via C-terminus) promoting exon ligation (PubMed:29146871).
Can use acetyl-CoA to synthesize acetate esters from various alcohols, producing ethyl acetate, isoamyl acetate, isobutyl acetate, butyl acetate, hexyl acetate, heptyl acetate and octyl acetate (PubMed:12957907, PubMed:12937998, PubMed:16845703, PubMed:17891501). ATF2 seems to play only a minor role in the acetate ester synthesis, compared to ATF1 (PubMed:12957907). Plays an active role in the detoxification hydroxysteroids and possibly certain phytochemicals, in association with the efflux pumps PDR5 and SNQ2 (PubMed:10103065).
Results in an 18% decrease in isoamyl acetate formation and causes a 13% reduction of ethyl acetate formation (PubMed:12957907). Leads to the complete elimination of acetyl-CoA:pregnenolone acetyltransferase activity and consequently abolishes the esterification of pregnenolone and increases the toxicity of pregnenolone (PubMed:10103065).
Segments of the N- and C-terminal domains (residues 19-36 and 515-532, respectively) are predicted to be amphipathic helices and are essential for endoplasmic reticulum membrane association (PubMed:25093817).
Component of the RPD3 histone deacetylase complex RPD3C(L) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. TOD6 binds to sequences containing the core CGATG, which resembles the PAC (Polymerase A and C) motif.
Belongs to the cysteine synthase/cystathionine beta-synthase family.
Guanine nucleotide exchange factor for SEC4, catalyzing the dissociation of GDP from SEC4 and also potently promoting binding of GTP. Activation of SEC4 by SEC2 is needed for the directed transport of vesicles to sites of exocytosis. Binds the Rab GTPase YPT32, but does not have exchange activity on YPT32.
Interacts with SEC4. Interacts with YPT32, preferentially in its GTP-bound form.
The N-terminal domain (1-374) is sufficient for the exchange factor activity.
Involved in the determination of the onset of polarized growth. Required for the ubiquitin-dependent degradation of RPN4. Cooperates with UBR2 to transfer ubiquitin from RAD6 to RPN4.
Is a short-lived protein whose degradation is dependent on the UBR2/RAD6 ubiquitin-protein ligase.
The MYND-type zinc finger is essential for the ubiquitin-dependent degradation of RPN4.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YMR046C ORF.
As a subunit of eukaryotic initiation factor 2 (eIF-2), involved in the early steps of protein synthesis. In the presence of GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex and initiation factors eIF-1, eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a step that determines the rate of protein translation. The 43S PIC binds to mRNA and scans downstream to the initiation codon, where it forms a 48S initiation complex by codon-anticodon base pairing. This leads to the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF-5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release of Pi, which makes GTP hydrolysis irreversible, causes the release of the eIF-2-GDP binary complex from the 40S subunit, an event that is essential for the subsequent joining of the 60S ribosomal subunit to form an elongation-competent 80S ribosome. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP exchange factor (GEF) eIF-2B.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EIF2G subfamily.
Eukaryotic translation initiation factor 2 (eIF-2) is a heterotrimeric G-protein composed of an alpha, a beta and a gamma subunit. The factors eIF-1, eIF-1A, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a multifactor complex (MFC) that may bind to the 40S ribosome.
Plays a role in vesicular protein sorting. Required for the endosome-to-Golgi retrieval of the vacuolar protein sorting receptor VPS10. Vacuolar carboxypeptidase Y (CPY) sorting is completely dependent on the presence of functional VPS35. The latter may play a role in the function, modification or packaging of a CPY-specific receptor complex. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. The VPS29-VPS26-VPS35 subcomplex may be involved in cargo selection.
Component of the Sm core complex, present in spliceosomal snRNP U1, U2, U4/U6 and U5. The core complex contains SMB1, SMD1, SMD2, SMD3, SME1, SMX3 and SMX2 (Sm proteins B, D1, D2, D3, E, F and G, respectively), and is probably a heptameric ring structure. SMB1 specifically interacts with SMD3. Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1. Interacts with the trimethylguanosine synthase TGS1.
Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine at position 1191 (Psi1191) in 18S rRNA (PubMed:27084949). It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA (PubMed:27084949). Required for processing 35S pre-rRNA at site D (PubMed:19806183).
Belongs to the TDD superfamily. TSR3 family.
Minor growth defect caused by late 18S rRNA processing defects, leading to a ribosomal subunit imbalance with a reduced 40S to 60S ratio.
Formation of pseudouridines at positions 38 and 39 in the anticodon stem and loop of transfer RNAs.
Required for viability in the absence of the kinesin-related CIN8 mitotic motor. Seems to be involved in the assembly of alpha-tubulin.
Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). The 5 acidic ribosomal P-proteins form the stalk structure of the 60S subunit. They are organized as a pentameric complex in which uL10/P0 interacts with 2 heterodimers, P1A-P2B and P1B-P2A. uL10 directly interacts with 28S rRNA (PubMed:16573688). uL10 interacts with YFL034W (PubMed:15286401).
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. uL10 forms part of the P stalk that participates in recruiting G proteins to the ribosome.
Component of the Sm core complex, present in spliceosomal snRNP U1, U2, U4/U6 and U5. The core complex contains SMB1, SMD1, SMD2, SMD3, SME1, SMX3 and SMX2 (Sm proteins B, D1, D2, D3, E, F and G, respectively), and is probably a heptameric ring structure. SMD3 specifically interacts with SMB1. Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Also binds telomerase RNA and is required for its accumulation.
Belongs to the PAPS reductase family. CysH subfamily.
The NADP dependent reduction of PAPS into sulfite involves thioredoxin which probably plays the role of a thiol carrier.
Could be O-glycosylated in the serine/threonine-rich domain.
Expression is highly increased during spheroplast regeneration.
Plasma membrane signaling mucin that promotes activation of the MAPK for the filamentous growth pathway. May regulate beta-glucan synthesis. Overexpression provides resistance to HM-1 killer toxin.
Belongs to the universal ribosomal protein uL1 family. Highly divergent.
Component of the 90S pre-ribosomes. Interacts with FAF1.
Involved in rRNA-processing and ribosome biosynthesis.
Participates in the repair of X-ray-induced damage to DNA and in meiosis. It may act in part by stabilizing a repair complex of other RAD genes.
Inhibited by the regulatory subunits VHS3 and SIS2.
Interacts with SIS2 and VHS3, which regulate its activity.
Was originally thought to originate from a rabbit cDNA library and was known as protein phosphatase Z (PP-Z).
Component of the aurora kinase complex composed of at least BIR1, BNL1, IPL1 and SLI15.
Component of the aurora kinase complex, also called chromosomal passenger complex (CPC), essential for chromosome segregation and metaphase chromosome alignment. Mediates the SLI15-BIR1 interaction within the CPC.
Component of the heterotrimeric Sec61 complex, which is composed of SSH1, SBH1 and SSS1. Presumably three to four Sec61 heterotrimers assemble into an oligomeric ring with a central aqueous pore. In cotranslational ER import, the pore diameter varies from 9-15 A in a ribosome-free resting state to 40-60 A in a functional state when associated with the ribosome. The Sec61 complex is part of a channel-forming translocon complex whose composition seem to change dependent upon different functional states. During post-translational ER import the Sec61 complex associates with the Sec62/63 complex to form the Sec complex. SSH1 is a component of the heterotrimeric Ssh1 complex, which is composed of SSH1, SBH2 and SSS1. SSS1 interacts with OST1, OST4, SWP1 and WBP1, components of the OT complex.
Part of the Sec61 complex, which is the major component of channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). The functional states of the translocon complex include co- and post-translational ER import, cotranslational membrane protein integration and retrograde transport of misfolded proteins out of the ER. In the cotranslational pathway, ribosomes synthesizing presecretory proteins are targeted to the translocon by the cytosolic signal recognition particle (SRP) and its ER-localized receptor. The association of the Sec61 complex with the ribosome is mediated by the 28S rRNA of the large ribosomal subunit. SRP-independent post-translational translocation requires the association of additional factors, such as the Sec62/63 complex and KAR2. Also part of the Ssh1 complex, which probably is the major component of a channel-forming translocon complex that may function exclusively in the cotranslational pathway of protein ER import.
Belongs to the group II decarboxylase family.
Interacts with itself. Interacts with MPC54, NUD1 and SPO21/MPC70.
Involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. Probable component of a core structural unit of the scaffold that initiates synthesis of the prospore membrane.
Present with 98400 molecules/cell in log phase SD medium.
Produced by alternative initiation at an upstream UUG codon in-frame of the first AUG used for isoform Cytoplasmic.
Activator of the chitin synthase CHS3 which polymerizes chitin, a structural polymer of the fungal cell wall.
Decreases CHS3 chitin synthase activity (PubMed:9234668). Decreases cellular chitin level (PubMed:9234668). Resistance to Calcofluor White (cell wall stressor) (PubMed:9234668). Normal CHS3 RNA level (PubMed:9234668). Decreases conjugation frequency (PubMed:9234668).
Farnesylation is required for chitin synthase CHS3 activity but is not required for SKT5 membrane association.
Induced by Calcofluor White (PubMed:9234668). Repressed by alpha-factor (PubMed:9234668). Unchanged during sporulation (PubMed:9234668).
May interact with CHS3 and seems to be an adapter (along with BNI4) to link CHS3 to septins.
Associates with the pre-60S ribosomal particle and the nucleopore complex.
Pre-ribosomal factor involved in 60S ribosomal protein subunit export from the nucleus.
Probable constituent of the synaptonemal complex during meiosis. May interact with HOP1. Required for meiosis I chromosome segregation.
Required for normal levels of the cell wall 1,6-beta-glucan. Involved in a protein folding machinery chaperoning proteins acting in various physiological processes including cell wall synthesis and lysis of autophagic bodies. Controls actin cytoskeleton polarization to the mother-bud neck and CLB2 protein stability.
Involved in the asymmetrical organization of phosphatidylethanolamine in the plasma membrane.
Induced by hydrogen peroxide. Repressed by superoxide radicals and anoxia.
Involved in aging, oxidative stress response, and in the regulation of mitochondrial biogenesis. Inactivation of UTH1 increases life span, leads to higher resistance to heat stress and against hydrogen peroxide, and increases sensitivity to the superoxide radical-generating drug paraquat and to copper. Also required for the selective autophagic degradation of mitochondria (mitophagy) in response to nitrogen starvation. Involved in the remodeling of the cell wall during the various phases of yeast culture development and under various environmental conditions and plays a role in septation. Involved in cell sensitivity to boric acid.
Leads to increased resistance to zymolyase treatment and to boric acid.
Present with 56900 molecules/cell in log phase SD medium.
Component of a fungal signal recognition particle (SRP) complex that consists of a 7SL RNA molecule (scR1) and at least six protein subunits: SRP72, SRP68, SRP54, SEC65, SRP21 and SRP14 (PubMed:7925282). At least SRP14, SRP21, SRP68 and SRP72 are proposed to get assembled together with scR1 RNA as a pre-SRP complex in the nucleolus which is exported to the cytoplasm (PubMed:7925282).
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:7925282, PubMed:10921896). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER (PubMed:10921896, PubMed:7925282). The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER (By similarity). Binds signal recognition particle RNA (7SL RNA) in presence of SRP68 (By similarity). Can bind 7SL RNA with low affinity (By similarity). The SRP complex possibly participates in the elongation arrest function (PubMed:10921896).
Expression is up-regulated by the transcription factor RPN4.
Leads to an altered morphology of lipid droplets with a smaller size.
Phospholipase involved in maintaining the lipid droplet morphology (PubMed:25014274). Has phospholipase activity with broad substrate specificity, acting on glycerophospholipids phosphatidylethanolamine (PE), phosphatidic acid (PA), phosphatidycholine (PC) and phosphatidylserine (PS), primarily at sn-2 position (PubMed:25014274). It can later remove fatty acids from the sn-1 position of the produced lysophospholipids such as lysophosphatidylethanolamine (LPE) (PubMed:25014274). Shows also activity toward phosphatidylglycerol, but, in contrast to what was observed with the other phospholipids tested, prefers the sn-1 position (PubMed:25014274).
Present with 42800 molecules/cell in log phase SD medium.
Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin remodeling complex. Also involved in the regulation of telomere length.
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Essential for thiamine biosynthesis. The kinase activity is involved in the salvage synthesis of TH-P from the thiazole.
In the C-terminal section; belongs to the Thz kinase family.
In the N-terminal section; belongs to the thiamine-phosphate synthase family.
Acetylation at Lys-496 and Lys-801 by ESA1 promotes synthesis of diacylglycerol.
Mg(2+)-dependent phosphatidate (PA) phosphatase which catalyzes the dephosphorylation of PA to yield diacylglycerol (PubMed:16467296, PubMed:16968695, PubMed:17910939, PubMed:17971454, PubMed:20876142, PubMed:21081492, PubMed:29765047). Required for de novo lipid synthesis and formation of lipid droplets (PubMed:21422231). Controls transcription of phospholipid biosynthetic genes and nuclear structure by regulating the amount of membrane present at the nuclear envelope (PubMed:15889145). Involved in plasmid maintenance, in respiration and in cell proliferation (PubMed:8437575).
Phenylglyoxal and propranolol inhibit activity in dose-dependent manners with IC(50) values of 1.3 mM and 0.2 mM, respectively.
Phosphorylated by CDC28 at the onset of mitosis, and dephosphorylated by the NEM1-SPO7 complex. Phosphorylation regulates recruitment on promoters of lipid biosynthetic enzymes.
The N-terminal amphipathic helix (residues 1 to 18) is involved in the membrane recruitment.
Interacts with ROY1, YIF1, YIP3, YIP4 and YIP5.
Required for transport in the endocytic pathway and for correct sorting of the vacuolar hydrolases suggesting a possible intersection of the endocytic with the vacuolar sorting pathway.
Putative mitochondrial redox protein which could be involved in the reduction of small toxic molecules.
5'->3' double-stranded DNA exonuclease involved in mismatch repair and eventually also in mitotic recombination between direct repeats. Also has a minor role in the correction of large DNA mismatches that occur in the heteroduplex DNA during meiotic recombination at the HIS4 locus.
Belongs to the XPG/RAD2 endonuclease family. EXO1 subfamily.
Interacts with mismatch repair protein MSH2.
Induces the SOS system when expressed in E.coli, therefore, it may play a role in DNA metabolism and/or in genome stability.
Disrupts iron-sulfur (Fe-S) cluster assembly (PubMed:31040179). Normal cytosolic tRNA thiolation (PubMed:31040179).
Interacts with the Fe/S cluster assembly proteins ISU1, MGE1, GRX5 and JAC1.
Required for the assembly of iron-sulfur (Fe/S) clusters in mitochondria (PubMed:10779357, PubMed:11273703, PubMed:12756240, PubMed:15123690, PubMed:15958384, PubMed:16431909, PubMed:9660806, PubMed:31040179). Assisted by the DnaJ-like co-chaperone JAC1 and the nucleotide exchange factor MGE1, it mediates ATP-dependent Fe-S cluster transfer from the scaffold proteins ISU1/ISU2 to GRX5 (PubMed:11273703, PubMed:12756240, PubMed:15123690, PubMed:15958384, PubMed:16431909, PubMed:31040179, PubMed:26545917, PubMed:23615440).
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.
GTPase involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs. Involved in the expression of cytochrome c oxidase subunit 1 (COX1). Works in association with the small subunit of mitoribosomes.
Belongs to the ETF alpha-subunit/FixB family.
NADP-dependent alcohol dehydrogenase with a broad substrate specificity. The oxidative reactions are more than 100 times less efficient than the corresponding reductions, suggesting that the enzyme acts as an aldehyde reductase, rather than as an alcohol dehydrogenase.
Component of a multicomponent complex composed of six to seven proteins, which has a collective molecular mass greater than 150 kDa. Interacts with GSP1 and YRB2.
Guanine nucleotide exchange factor that promotes the exchange of GSP1/GSP2-bound GDP by GTP and controls RNA metabolism and transport. Involved in yeast pheromone response pathway and in mRNA metabolism. Involved in nuclear pore complex (NPC) assembly and required for mRNA and ribosome nuclear export. Binds chromatin and is involved NPC-mediated transcriptional control.
Belongs to the DHHC palmitoyltransferase family. ERF2/ZDHHC9 subfamily.
The ERF2-SHR5 complex is a palmitoyltransferase specific for Ras proteins. Palmitoylates RAS2, which is required for its proper plasma membrane localization.
Component of the U4/U5/U6 snRNP, binding principally to the u5 snRNP. It is not absolutely required for the second step of pre-mRNA splicing at low temperatures but is required at higher temperatures. It may stabilize a particular conformation of the U5 snRNP or orient the U5 snRNP within the U4/U5/U6 snRNP or within the spliceosome.
Homodimer. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
Component of the inner layer of the cell wall.
Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (By similarity). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs (PubMed:22961381). Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1) (PubMed:22961381). Also has 5'-3' exonuclease activity (PubMed:22961381).
Involved in cytoskeletal organization and cellular growth. May exert its effects on the cytoskeleton directly, or indirectly via proline-binding proteins (e.g. profilin) or proteins possessing SH3 domains.
May be involved in the Ras/cAMP signaling pathway.
Component of the ER membrane protein complex (EMC).
Utilization of purines as secondary nitrogen sources, when primary sources are limiting.
DNA polymerase alpha mutation suppressor. Suppressor of group II intron splicing defects of a mutation in MRS2. May play a role in mitochondrial mRNA splicing.
Interacts (via PxP motif) with VPS13 (via SHR-BD domain).
Recruits the lipid transfer protein Vps13 to mitochondria thereby promoting vacuole-mitochondria contacts (PubMed:28864540, PubMed:30018089, PubMed:34830155). Involved in mitochondrial lipid homeostasis (PubMed:23781023, PubMed:28864540).
Component of the NDC80 complex, which consists of TID3/NDC80, NUF2, SPC24 and SPC25. The NDC80 complex is formed by two subcomplexes, TID3/NDC80-NUF2 and SPC24-SPC25, which are joined end-to-end through their coiled-coil domains. It has a rod-like structure with a length of 570 Angstroms and globular domains at either end. The TID3/NDC80-NUF2 globular domains are probably directed to microtubules, the SPC24-SPC25 globular domains to the centromere. Can also interact with MPS2.
May have a role related to the spindle integrity function of the DAM1 complex, which is essential for proper chromosome segregation. Causes growth arrest when highly overexpressed.
Present with 264 molecules/cell in log phase SD medium.
Mitochondrial inner membrane carrier protein that mediates the import of NAD(+) into mitochondria (PubMed:16291748, PubMed:32906142). Can transport NAD(+) by unidirectional transport or by exchange with intramitochondrially generated dAMP and dGMP (PubMed:16291748). Also able to transport NAD(+) by exchange with AMP, GMP or deamido-NAD (+) in vitro (PubMed:16291748).
Belongs to the adenylate kinase family. AK3 subfamily.
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon GTP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent GTP hydrolysis.
Depending on the yeast strain, the GTP:AMP phosphotransferase is encoded by ADK2 with or without a single base pair deletion/insertion near the 3' end of the open reading frame, resulting in a long or a short form. The ADK2 short form (this entry) is also referred to as PAK3, while the long form has been named AKY3. A sequence of the long form can be found in strain D273-10B (AC E9P974). The modified C-terminus in the long form contributes to protein folding and is critical for protein stability.
Expression level is low on glucose or other fermentable carbon sources. Induced about 3-fold on glycerol, and significantly induced by ethanol.
Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities. Does not accept ATP as phosphate donor.
Belongs to the SLC43A transporter (TC 2.A.1.44) family.
Could be an enzyme that inactivates 6-azauracil by modifying it.
Belongs to the DASH complex DAM1 family.
The DASH complex is an approximately 210 kDa heterodecamer, which consists of ASK1, DAD1, DAD2, DAD3, DAD4, DAM1, DUO1, HSK3, SPC19 and SPC34, with an apparent stoichiometry of one copy of each subunit. DASH oligomerizes into a 50 nm ring composed of about 16 molecules that encircles the microtubule. Integrity of the complex and interactions with central kinetochore proteins are regulated by the spindle assembly checkpoint kinase IPL1. Interacts with TID3.
Cell cycle-regulated. Protein levels increase as cells begin S phase and remain high through late mitosis.
Heterodimer with CDC7 to form the DBF4-dependent kinase (DDK) complex. Interacts (via PBD-binding motif) with CDC5 (via POLO box domains). Interacts (via N-terminus) with ORC2, ORC3 and RAD53. Binds to ARS1 origin DNA.
Regulatory subunit of the CDC7-DBF4 kinase, also called DBF4-dependent kinase (DDK), which is involved in cell cycle regulation of premitotic and premeiotic chromosome replication and in chromosome segregation. DDK plays an essential role in initiating DNA replication at replication origins by phosphorylating the MCM2 and MCM4 subunits of the MCM2-7 helicase complex. DBF4 recruits the catalytic subunit CDC7 to MCM2 and to origins of replication. DDK has also postreplicative functions in meiosis. DDK phosphorylates the meiosis-specific double-strand break protein MER2 for initiation of meiotic recombination. Interacts with CDC5 during meiosis to promote double-strand breaks and monopolar spindle orientation. Inhibits CDC5 activity during mitosis through direct binding to its PBD.
Binds the proteasome. Interacts with karyopherin SRP1 and proteasome subunit RPN11.
Involved in ubiquitin-mediated protein degradation. Regulatory factor in the ubiquitin/proteasome pathway that controls the turnover of proteasome substrates. Targets proteasomes to the nucleus and facilitates the degradation of nuclear proteins. Required for efficient chromosome segregation. Restores protein transport and ribosomal RNA stability.
Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Necessary for activation of the CDC28 kinase.
Belongs to the proteasome subunit S14 family.
Present with 9890 molecules/cell in log phase SD medium.
E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 and ATG8 for its conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Plays a role in the regulation of filamentous growth and chronological longevity.
Homodimer; homodimerization is required for ATP-binding (PubMed:11139573, PubMed:21193819, PubMed:29295865). Interacts with ATG8 through a thioester bond between Cys-507 and the C-terminal 'Gly-116' of ATG8 and with ATG12 through a thioester bond between Cys-507 and the C-terminal 'Gly-186' of ATG12 (PubMed:10233150, PubMed:11100732, PubMed:16874032, PubMed:18544538, PubMed:22055191). Interacts also with ATG3 (PubMed:11139573, PubMed:17227760, PubMed:22056771, PubMed:23142976).
The C-terminal 40 residues are required for homodimerization, as well as the interactions with ATG3, ATG8 and ATG12; and the C-terminal 17 residues are required for the ATG8 lipidation.
The GxGxxG motif is important for the function, possibly through binding with ATP.
Identified in the GID complex. In the absence of glucose, the complex contains VID30/GID1, the E3 ubiquitin-ligase RMD5/GID2, VID28/GID5, GID7, GID8, and FYV10/GID9. When cells are shifted to glucose-containing medium, VID24/GID4 is induced and becomes part of the complex (PubMed:22645139). Interacts with RMD5/GID2; the interaction is direct (PubMed:22044534). Within the GID complex, interacts directly with VID28/GID5, GID8 and RMD5/GID2 (PubMed:22645139).
It is not certain that this protein has E3 ubiquitin-protein ligase activity by itself. Lacks a detectable RING-type zinc finger domain; the sequence in this region is highly divergent and lacks most of the expected Cys residues. Still, Cys-434 in this highly divergent region is required for ubiquitination of FBP1, suggesting a direct role in catalyzing ubiquitination.
Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium (PubMed:12686616, PubMed:22044534). Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:12686616, PubMed:22044534). May catalyze ubiquitination of target proteins in complex with RMD5 (Probable). Required for survival upon exposure to K1 killer toxin (PubMed:12663529).
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB3 is part of the core element with the central large cleft and the clamp element that moves to open and close the cleft. Seems to be involved in transcription termination.
Present with 10000 molecules/cell in log phase SD medium.
Present with 169000 molecules/cell in log phase SD medium.
Involved in pseudohyphal growth, cell wall metabolism and required for the separation of the mother and daughter cells.
Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI.
Forms a complex with GPI16, GPI17, GPI8 and GAA1.
Interacts with the snRNP via the Nop domain.
Present with 1260 molecules/cell in log phase SD medium.
Promotes the association of the U4/U6.U5 tri-snRNP particle with pre-spliceosomes to form the mature spliceosomal complex.
The coiled coil domain is formed by two non-contiguous helices.
Likely to play a role in iron homeostasis.
Mild slow-growth phenotype in response to reduced iron levels.
Belongs to the eukaryotic ribosomal protein eL38 family.
Present with 50200 molecules/cell in log phase SD medium.
Present with 5525 molecules/cell in log phase SD medium.
With TAX4, acts as a positive regulator of INP51 activity and phosphatidylinositol 4,5-bisphosphate turnover. Negatively regulates signaling through the cell integrity pathway, including the MAP kinase SLT2. Seems also to be involved in rDNA silencing.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily.
Catalyzes the irreversible reduction of the cytotoxic compound methylglyoxal (MG, 2-oxopropanal) to (S)-lactaldehyde as an alternative to detoxification of MG by glyoxalase I GLO1. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation. Also catalyzes the reduction of 3-methylbutanal to 3-methylbutanol. Acts as a suppressor of 3-methylbutanol-induced filamentation by modulating the levels of 3-methylbutanal, the signal to which cells respond by filamentation. Also involved in ergosterol metabolism.
Causes hyperfilamentation, probably due to the elevated levels of 3-methylbutanal in the mutant.
Present with 5458 molecules/cell in log phase SD medium.
Repressed by SKO1. During osmotic stress, this repression is relieved. Induced by transcription factor YAP1 during oxidative stress, and induced by ionic and heat stress. Induced by isoamylalcohol.
Used as a biocatalyst, because the enzyme accepts a broad range of substrates including aliphatic and aromatic ketones, chloroketones, diketones as well as beta-ketoesters which are reduced with high stereoselectivity.
Component of the transcription/export (TREX) complex, which is at least is formed of SUB2, TEX1 and YRA1 and the THO complex composed of HPR1, MFT1, THO2 and THP1.
Component the TREX complex, which operates in coupling transcription elongation to mRNA export.
Activator of specific mitochondrial mRNAs. PET54 is involved in the excision of intron aI5-beta from pre-mRNA for cytochrome c oxidase I (COX1) and plays a role in promoting the translation of COX3.
Seems to act indirectly to modify IME2 activity, thus permitting IME2 to carry out later meiotic functions.
Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
Was originally erroneously assigned as a beta subunit.
Involved in size control and cell cycle.
Belongs to the class I-like SAM-binding methyltransferase superfamily.
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(3) position of uridine 2843 (m3U2843) in 25S rRNA.
Leads to rapamycin resistance when grown on glutamate as the sole nitrogen source.
NAD(+)-dependent glutamate dehydrogenase which degrades glutamate to ammonia and alpha-ketoglutarate.
Phosphorylated by a complex containing the NNK1 kinase.
Acts as a component of chromatin assembly factor 1 (CAF-1), which assembles histone octamers onto replicating DNA in vitro. It performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. p50 and p60 form complexes with newly synthesized histones H3 and acetylated H4 in cell extracts (By similarity). Independently, MSI1 is involved in regulation of the RAS/cAMP pathway via sequestration of NPR1.
Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
Interacts with protein kinase NPR1 (PubMed:11238915). Component of chromatin assembly factor 1 (CAF-1), which is composed of MSI1/p50, CAC2/p60 and CAC1/p90 (PubMed:11238915). Interacts with RTT106 (PubMed:19683497).
Appears in S phase cells and remains present during mitosis until metaphase. Degraded at the onset of anaphase. During meiosis it is present until anaphase II and is then degraded. Not present in G1 cells.
Plays a central role in chromosome cohesion during mitosis and meiosis divisions by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms. Probably act by protecting REC8 and RAD21 from separase degradation during anaphase. Also acts as a spindle checkpoint component required for sensing tension between sister chromatids during mitosis, its degradation when they separate preventing cell cycle arrest and chromosome loss in anaphase, a time when sister chromatids are no longer under tension.
Present with 7040 molecules/cell in log phase SD medium.
Belongs to the triosephosphate isomerase family.
Present with 207000 molecules/cell in log phase SD medium.
Involved in nucleotide excision repair (NER) of damaged DNA. Required for the repair of RNA polymerase I-transcribed rDNA and RNA polymerase II-transcribed DNA regions. May have a role in stabilizing the DNA repair proteins RAD4 and RAD34.
Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration.
Regulatory subunit of the histone acetylase B (HAT-B) complex. The complex acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. HAT2 is required for high affinity binding of the acetyltransferase to histone H4, for the nuclear location of HAT1 and for the HAT1-HIF1 interaction. Alone, it is unable to bind to H4, requiring HAT1 for high affinity interaction with the histone tail. HAT2 has also a HAT1 independent function in life-span regulation.
Repressed in presence of farnesol, probably through a intracellular decrease of diacylglycerol.
Component of multiple cullin-RING ligases (CRLs) composed of 4 subunits: the RING protein HRT1, a cullin, a linker protein, and one of many alternative substrate receptors. Component of SCF E3 ubiquitin ligase complexes containing the cullin CDC53, the linker protein SKP1/CBF3D, and substrate receptors containing F-box motifs like DAS1 or GRR1. Component of RTT101(MMS1) E3 ubiquitin ligase complexes containing the cullin RTT101, the linker protein MMS1, and substrate receptors belonging to a protein family described as DCAF (DDB1- and CUL4-associated factor) like MMS22. Component of CRL3 E3 ubiquitin ligase complexes containing the cullin CUL3, the linker protein ELC1, and substrate receptors containing SOCS-box motifs like ELA1. Interacts with CDC53, CUL3, RTT101, CDC4 and CDC34/UBC3.
Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes (CRLs), which mediate the ubiquitination of target proteins. Recruits the E2 ubiquitin-conjugating enzyme CDC34/UBC3 to the complex and brings it into close proximity to the substrate. Also stimulates CDC34/UBC3 autoubiquitination and promotes the neddylation of CDC53 and RTT101. Component of the SCF(CDC4) ubiquitin ligase required for ubiquitination of the cyclin-dependent kinase inhibitor SIC1 and for the G1-to-S phase transition. Component of the RTT101(MMS1-MMS22) ubiquitin ligase that promotes fork progression through damaged DNA or natural pause sites. Component of the CRL3(ELA1) ubiquitin ligase required for ubiquitination of RPB1, the largest subunit of RNA polymerase II (Pol II), which targets Pol II for proteasomal degradation in DNA-damaged cells.
It is uncertain whether Met-1 or Met-8 is the initiator.
The RING-type zinc finger domain is essential for ubiquitin ligase activity.
Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex.
Homodimer. Component of the endosomal sorting complex required for transport II (ESCRT-II), which consists of 2 copies of VPS25, 1 copy of SNF8, and 1 copy of VPS36. The ESCRT-II complex interacts directly with the VPS20 subunit of the ESCRT-III complex.
Stimulates decapping of both stable and unstable mRNA during mRNA decay. Does not affect nonsense-mediated mRNA decay. Required for normal P-body assembly.
After transfer of sugars to endogenous macromolecular acceptors, the enzyme converts nucleoside diphosphates to nucleoside monophosphates which in turn exit the Golgi lumen in a coupled antiporter reaction, allowing entry of additional nucleotide sugar from the cytosol.
Palmitoylated by AKR1, which is required for proper plasma membrane localization of YCK2.
As part of the CRL3 E3 ubiquitin ligase complex; polyubiquitylates monoubiquitylated RNA polymerase II subunit RPO21 to trigger its proteolysis; plays a role in global genomic repair.
Heterodimer with ELC1 (PubMed:10430890, PubMed:10753924). Component of a CRL3 E3 ubiquitin ligase complex consisting of the cullin CUL3, the linker protein ELC1, the substrate receptor ELA1, and the RING protein HRT1 (Probable). Interacts with the large RNA polymerase II subunit RPO21 in a DEF1-dependent manner (PubMed:23993092). Interacts (via C-terminus) with DEF1 (via CUE domain); the interaction is direct (PubMed:23993092).
Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with PRP2.
Involved in pre-mRNA splicing; specifically in the final stages of spliceosome maturation. Promotes the first step of splicing.
Expression decreased by the copper-sensing transcription factor MAC1.
Required for the uptake of Fe(3+) ions. May participate in the transport of electrons from cytoplasm to an extracellular substrate (Fe(3+) ion) via FAD and heme intermediates (By similarity). Involved in iron homeostasis.
Belongs to the eukaryotic ATPase B chain family.
Lacks the conserved His residues essential for binding the catalytic zinc ion. Its enzyme activity is therefore unsure.
Belongs to the eukaryotic RPA34 RNA polymerase subunit family.
Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA. Forms a TFIIF-like heterodimer with RPA49; the heterodimer formed by RPA34 and RPA49 can be dissociated from the Pol I core giving rise to a 12 subunit form A* of Pol I (formerly called pol A) that shows impaired transcript elongation activity and increased sensitivity to alpha-amanitin. The heterodimer formed by RPA34 and RPA49 stabilizes subunit RPA12 and stimulates RPA12-dependent RNA cleavage.
DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. The heterodimer formed by RPA34 and RPA49 stimulates transcript elongation by Pol I.
2-[3-carboxy-3-(methylammonio)propyl]-L-histidine and the corresponding dimethyl compound can also act as acceptors.
Belongs to the diphthine synthase family.
Present with 13480 molecules/cell in log phase SD medium.
S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis.
Probably not a functional protein. Cells lacking A2 show no obvious alterations in mating, sporulation and cell growth (By similarity).
S.cerevisiae mating-type protein A2 is identical to residues 92-210 of ALPHA2 and should not be confused with the mating-type protein A2 of other yeast species.
There is no sequence for the expressed copy of a2 in strain S288c, because this strain is of mating type alpha. A sequence for the expressed copy of a2 can be found in other strains (AC P0CY12).
Mitophagy-specific receptor that recruits the autophagic machinery to mitochondria and regulates selective degradation of mitochondria. Mitophagy contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Recruits ATG11 to the surface of mitochondria. Promotes also autophagy-dependent peroxisome degradation.
Phosphorylation of Ser-114 and Ser-119 are critically important for mitophagy and for the ATG11-ATG32 interaction. Phosphorylation depends on both HOG1 and PBS2.
Component of the RQT (ribosome quality control trigger) complex, composed of SLH1, CUE3, and RQT4 (PubMed:28757607, PubMed:32203490). Interacts with ubiquitin; the interaction is direct (PubMed:28757607). Interacts with SLH1 (PubMed:28757607). Interacts with RQT4 (PubMed:28757607, PubMed:28223409). Interacts with HEL2 (PubMed:28757607). Associates with translating ribosomes (PubMed:28757607, PubMed:28223409).
Involved in activation of the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation (PubMed:28757607, PubMed:28223409, PubMed:32203490). As part of the ribosome quality control trigger (RQT) complex, recognizes HEL2-dependent ubiquitination of RPS20 on stalled ribosomes (PubMed:28757607).
Siderophore-iron reductase responsible for reducing extracellular iron prior to import. Catalyzes the reductive uptake of Fe(3+) bound to dihydroxamate rhodotorulic acid. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane.
Belongs to the adenylosuccinate synthetase family.
Inhibited by GMP. Inhibited by chloride. Inhibited in a highly specific manner by the binding of a 44-base DNA oligonucleotide carrying the ARS core consensus sequence.
Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Present with 56800 molecules/cell in log phase SD medium.
In the C-terminal section; belongs to the NAD synthetase family.
Involved in the pentose phosphate pathway via hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
High affinity cysteine-specific transporter. Major contributor to cysteine transport when cysteine, at low concentrations, is provided as the sole sulfur source.
Induced under nitrogen starvation conditions, co-regulated by GCN4 and GLN3. Regulated by the MET4-based sulfur regulatory network. Expression is maximum in nonrepressing sulfur conditions and considerably repressed in the presence of organic sulfur. Induced by chromate.
Belongs to the glycogen phosphorylase family.
Decreases cellular phosphatidylcholine levels (PubMed:24146988). Growth on non-fermentable carbon sources is severely decreased (lactate or glycerol) (PubMed:24146988). Sensitive to sodium dodecyl sulfate, and sorbitol (PubMed:24146988).
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Increases in strong (1 mM) hydrogen peroxide stress, and decreases in milder (0.5 mM) hydrogen peroxide stress.
Inhibited by the translational inhibitors neomycin and alpha-sarcin, which suppress the ATPase activity.
Monomer. Interacts with elongation factor 1A (eEF1A). Interacts through its N-terminus with 18S rRNA. Associates with ribosomes (PubMed:22888004).
Present with 870578 molecules/cell in log phase SD medium.
Ribosome-dependent ATPase that functions in cytoplasmic translation elongation (PubMed:7657623, PubMed:6456269, PubMed:29300771). Required for the ATP-dependent release of deacylated tRNA from the ribosomal E-site during protein biosynthesis (PubMed:7657623). Stimulates the eEF1A-dependent binding of aminoacyl-tRNA to the ribosomal A-site, which has reduced affinity for tRNA as long as the E-site is occupied (PubMed:7657623). Plays a role as a negative regulator of the GCN2 kinase activity; impairs GCN1-mediated GCN2 activation on ribosomes by reducing GCN1-ribosome affinity, and hence GCN2-mediated eIF-2-alpha phosphorylation in amino acid-starved or repleted cells (PubMed:22888004).
The heat repeats and the C-terminal domain are necessary for impairing GCN1 function on ribosomes, and hence preventing GCN2 kinase activity in amino acid-starved or repleted cells (PubMed:22888004).
Belongs to the adaptor complexes medium subunit family. Delta-COP subfamily.
Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts with DSL1.
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Component of the checkpoint clamp complex composed of DDC1, MEC3 and RAD17. The interaction with MEC3 is performed in a RAD17-dependent manner. The checkpoint clamp complex loads onto DNA. Interacts with the DNA polymerase zeta subunit REV7. 2 RAD17 subunits form also a hetero trimer with one MEC3 subunit.
Component of the checkpoint clamp complex involved in the surveillance mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. Associates with sites of DNA damage and modulates the MEC1 signaling pathway and the activation of RAD53 in response to DNA damage at phase G1. The complex also physically regulates DNA polymerase zeta-dependent mutagenesis by controlling the access of polymerase zeta to damaged DNA. Contrary to its human counterpart, the 9-1-1 complex, the checkpoint clamp complex shows no detectable exonuclease activity.
Expressed constitutively at a high level and is moderately induced by high temperatures dependent on transcription factor HSF1.
Interacts with the co-chaperone SGT1. Interacts directly with the substrate CNA2. Interacts with NAP1.
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction such as CNA2. Undergoes a functional cycle that is linked to its ATPase activity (By similarity). Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.
Present with 132053 molecules/cell in log phase SD medium.
The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.
Belongs to the class I-like SAM-binding methyltransferase superfamily. UbiG/COQ3 family.
Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9 (PubMed:15792955, PubMed:24406904). Interacts directly with COQ4 (PubMed:15792955).
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. Catalyzes the methylation of 3,4-dihydroxy-5-hexaprenylbenzoate (DHHB) to 3-methoxy-4-hydroxy-5-hexaprenylbenzoate (HMHB) and the methylation of 2-hexaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinol (3-demethylubiquinol-6) to ubiquinol-6.
Regulated in response to catabolite repression.
Belongs to the V-ATPase H subunit family.
Increases the ATPase activity of membrane-detached V-ATPase V1 (PubMed:27295975). Abolishes growth at pH 7.5 and in the presence of calcium chloride, abrogates growth at pH 5.0 (PubMed:27295975).
Present with 22500 molecules/cell in log phase SD medium.
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:8349704, PubMed:27295975). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:8349704, PubMed:27295975). This subunit is essential for activity, but not assembly, of the enzyme complex (PubMed:8349704, PubMed:27295975). This subunit is also required for silencing the ATPase activity of V-ATPase when V1 is detached from V0 (PubMed:27295975).
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and VOA1) (PubMed:8349704, PubMed:25971514, PubMed:18055462, PubMed:27295975). Interacts with YND1 (PubMed:10954728).
Participates in the folding of proteins containing disulfide bonds.
Homocysteine S-methyltransferase involved in the conversion of S-adenosylmethionine (AdoMet) to methionine to control the methionine/AdoMet ratio. Also converts S-methylmethionine (SMM) to methionine.
A structure shows that CysB motif binds zinc but a later study has suggested it might bind 1 4Fe-4S cluster instead.
Catalytic component of DNA polymerase alpha, which in complex with DNA primase (DNA polymerase alpha:primase) constitutes a replicative polymerase (PubMed:10898792, PubMed:22119860, PubMed:31488849). POL1 has a role in promoting telomere replication during interaction with CDC13 (PubMed:10898792).
DNA polymerase alpha:primase is a four subunit enzyme complex, which is assembled throughout the cell cycle, and consists of the two DNA polymerase subunits A POL1 and B POL12, and the DNA primase large PRI2 and small PRI1 subunits (PubMed:3061469). Subunit B POL12 binds to subunit A POL1 (PubMed:19494830). POL1 interacts with CDC13, POB3, SPT16 and MCM10 (PubMed:10898792, PubMed:16675460, PubMed:8621497, PubMed:9199353).
Produced by +1 ribosomal frameshifting between codon Leu-431 and Gly-432 of the YOR192C-A ORF.
Associates with the 60S ribosomal subunit. Interacts with ARB1.
Belongs to the TRAFAC class YlqF/YawG GTPase family. LSG1 subfamily.
GTPase required for the nuclear export of the 60S ribosomal subunit. Acts by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm.
Present with 19400 molecules/cell in log phase SD medium.
Present with 1026 molecules/cell in log phase SD medium.
Homodimer. Interacts with calmodulin (CMD1) and the myosin light chain MLC1 through its IQ repeats. Binds to the membrane receptors SEC4 and VAC17 to transport secretory vesicles and the vacuole, respectively. Binds to KAR9, which transports BIM1-coated cytoplasmic microtubules that are attached to the spindle pole body into the emerging bud, thereby correctly orienting the mitotic spindle. Interacts with YPT11 and MMR1 to accelerate mitochondrial distribution to the bud. Interacts with SHE4 and localizes it to the bud tip. Interacts with RHO3 and SMY1, putative regulators of MYO2 function. Interacts with SRO7.
Moves with an average velocity of 3 um/s along actin cables.
Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Essential for the delivery of secretory vesicles to sites of active growth during bud emergence and cytokinesis. Required for segregation and inheritance of peroxisomes, late Golgi compartments, mitochondria and the vacuole to the daughter cell during cell division. Also required for correct alignment of the spindle during mitosis.
Present with 4339 molecules/cell in log phase SD medium.
The coiled-coiled domain is necessary for dimerization.
The tail domain is a globular cargo-binding domain involved in vectorial vesicle transport.
Catalytic subunit of the TRAMP complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates like cryptic transcripts generated by RNA polymerase II and III, or hypomethylated pre-tRNAi-Met. Polyadenylates RNA processing and degradation intermediates of snRNAs, snoRNAs and mRNAs that accumulate in strains lacking a functional exosome. TRF4 is also required for proper nuclear division in mitosis, DNA damage repair and sister chromatid cohesion. Involved in the regulation of histone mRNA levels. May mediate mitotic chromosome condensation.
Component of the TRAMP complex (also called TRF4 complex) composed of at least HUL4, MTR4, PAP2/TRF4 and either AIR1 or AIR2. Interacts with NOP53 and POL2. Interacts directly with AIR2.
May act as a phosphoinositide 3-phosphatase by regulating PtdIns(3,4,5)P3 levels.
Interacts (farnesylated) with PEX3; farnesylation is required for this interaction. Interacts with PEX2, PEX5, PEX10, PEX11, PEX12, PEX13, PEX14, PEX17, PEX22, PEX25, PEX30 and PEX32; the interaction requires well-defined PEX19-binding sites within the peroxisomal membrane protein targeting signal (mPTS) of the PMPs and is independent on the presence of PEX3. Interacts with VPS1.
Required for proper post-translational import and stabilization of peroxisomal membrane proteins (PMPs). Acts as a cytosolic import receptor for PMPs and delivers them to the docking factor PEX3 at the peroxisomal membrane for subsequent insertion into the membrane. Acts as a chaperone in stabilizing or maintaining PMPs in the lipid bilayer. Directs PEX17, a peripheral component of the peroxisomal matrix protein translocation machinery, to peroxisomes. Stabilizes VPS1, a protein required for peroxisomal fission, at the peroxisomal membrane. Also acts in conjunction with PEX3 in the formation of peroxisomes from preperoxisomal compartments at the endoplasmic reticulum during de novo peroxisome synthesis, probably via the import of additional PMPs.
Increases sensitivity to H(2)O(2) and decreases activation of YAP1-dependent gene expression.
Involved in oxidative stress response and redox homeostasis. Required for hydrogen peroxide-induced activation of YAP1. Acts in a parallele pathway to YBP1.
Expression is sensitive to carbon catabolite repression, but nearly insensitive to nitrogen catabolite repression.
Malate synthase which takes part in the glyoxylate cycle (PubMed:1454530). MLS1 activity is essential for cells to grow on oleic acid as a sole carbon source (PubMed:11846793). Two steps of the glyoxylate cycle take place in the cytosol, the splitting of isocitrate into succinate and glyoxylate, and the dehydrogenation of malate to oxaloacetate (PubMed:1454530). However, the formation of malate from glyoxylate and acetyl-CoA undertaken MLS1, occurs in the peroxisomes when cells are grown on oleic acid (Probable). The source of acetyl-CoA being either peroxisomal when breaking down fatty acids, or cytosolic when extra-cellular two-carbon substrates are used, therefore, although not strictly essential, the peroxisomal localization of MLS1 appears to be advantageous for cells growing on oleic acid, in that acetyl-CoA production and utilization are thereby intimately compartmentalized together to increase efficiency (Probable).
Strongly decreases the growth rate on ethanol or acetate medium.
Catalytic component of DNA polymerase delta (DNA polymerase III) which participates in chromosomal DNA replication (PubMed:2670563, PubMed:22119860, PubMed:31488849). Required during synthesis of the lagging DNA strands at the replication fork, binds at/or near replication origins and moves along DNA with the replication fork (PubMed:31488849). Participates in leading strand synthesis during replication initiation and termination (PubMed:31488849). Has 3'-5' proofreading exonuclease activity that corrects errors arising during DNA replication (PubMed:1648480).
DNA polymerase delta is a heterotrimer of POL3, POL32 and HYS2. Interacts with PCNA.
Belongs to the peroxiredoxin family. Prx6 subfamily.
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this 1-Cys peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide with a cysteine from another protein or with a small thiol molecule. C(P) is reactivated by glutathionylation and subsequent reduction by either glutaredoxin GRX2 or thioredoxin reductase TRR2, coupled with reduced glutathione (GSH).
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Involved in mitochondrial protection of cadmium-induced oxidative stress.
Heterodimers with NPA3/GPN1 or GPN2 (PubMed:23324351, PubMed:23267056). Binds to RNA polymerase II (RNAPII) (By similarity).
Small GTPase required for proper nuclear localization of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import (PubMed:23267056). Promotes sister chromatid separation during anaphase (PubMed:23324351).
Has minor DNA joining activity. Can act on oligo(PDT)/poly(rA) substrate.
Interacts with LIF1 via its BRCT domain. Interacts with POL4 in the DNL4-LIF1 complex.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. TRM7 subfamily.
Causes severe growth and translation defects, which is due to reduced decoding of Phe codons by hypomodified tRNA(Phe).
Interacts with TRM732; for 2'-O-methylation of cytidine 32 in substrate tRNAs. Interacts with RTT10/TRM734; for 2'-O-methylation of position 34 in substrate tRNAs.
Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of tRNA(Phe), tRNA(Trp) and tRNA(Leu(UAA)). Requires TRM732 for methylation of the cytidine at position 32 and RTT10/TRM734 for methylation of the nucleotides at position 34 in substrate tRNAs. Lack of either of these modifications in tRNA(Phe) reduces formation of wybutosine from 1-methylguanosine at position 37.
Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides.
Single strand DNA specific 5' exonuclease involved in mitochondrial DNA replication and recombination. Releases dinucleotides as main products of catalysis. Has the capacity to slide across 5'double-stranded DNA or 5'RNA sequences and resumes cutting two nucleotides downstream of the double-stranded-to-single-stranded junction or RNA-to-DNA junction, respectively.
Leads to defects in unfolded protein response.
Expression is induced in the presence of citrinin (PubMed:26713447). Expression is induced by the PDR1 and YRR1 multidrug resistance transcription factors (PubMed:11470516, PubMed:11909958).
Mitochondrial protein that is involved in citrinin resistance.
Dual substrate-specific glycerol-3-phosphate/dihydroxyacetone phosphate sn-1 acyltransferase, catalyzing the first and committed reaction in the de novo synthesis of glycerophospholipids and triacylglycerols (TAGs). Prefers Gly-3-P over dihydroxyacetone phosphate and has a marked preference for 16-carbon fatty acyl chains. Transfers a fatty acid from fatty acyl-CoA to the sn-1 position of glycerol-3-phosphate to produce lysophosphatidic acid (LysoPA). These lipids not only are precursors of glycerolipids, but also are dynamic components of signal transduction systems that control cell physiology (PubMed:11544256). SCT1 is the primary supplier of diacylglycerols (DAG), used mainly in TAG synthesis and phosphatidylcholine (PC) synthesis through the CDP-choline pathway (PubMed:12167660). Regulates fatty acid desaturation, that is, the ratio of unsaturated versus saturated fatty acyl chains, by competing with the desaturase OLE1 for the common substrate C16:0-CoA. Sequesters C16:0-CoA into lipids, thereby shielding it from desaturation by OLE1 (PubMed:22323296).
Belongs to the RNase H2 subunit C family. Highly divergent.
Interacts with SKP1/CBF3D. Part of SCF E3 ubiquitin ligase complexes containing SKP1, CDC53, HRT1 and some F-box proteins. Interacts with CIR1/CDC35.
Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Required for both entry into S phase and kinetochore function. Also involved in cyclic AMP (cAMP) pathway, possibly by participating in the assembly or the conformational activation of specific multiprotein complexes.
Belongs to the transient receptor (TC 1.A.4) family.
Required for release of calcium ions from the vacuole in response to hyperosmotic shock.
Flippase activator that phosphorylates DFN1 and DFN2 and which is involved in the generation of phospholipid asymmetry in membranes by the inward translocation of phospholipids.
Involved in N-linked oligosaccharide assembly. Required for the translocation of Man(5)GlcNAc(2)-PP-dolichol from the cytoplasmic side to the lumenal side of the endoplasmic reticulum membrane.
May be involved in cellular response to stress. Required to maintain mitochondrial DNA (mtDNA) integrity and stability. Required for ethanol metabolism and tolerance during heat shock.
Interacts with TRM7; for 2'-O-methylation of cytidine 32 in substrate tRNAs.
Required together with TRM7 for the methylation of the 2'-O-ribose of cytidine at position 32 of the tRNA anticodon loop of tRNA(Phe) and tRNA(Leu(UAA)).
Interacts with EXP1 (PubMed:28727280). PSG1-N' interacts with ERAD-related proteins involved in PMA1 quality control including EPS1, CDC48, UBX2 and SSM4 (PubMed:28727280). PSG1-C' interacts with the TLG1/2 SNARE complex proteins TLG1, TLG2 and VTI1 (PubMed:28727280).
Leads to enhanced degradation of PMA1 in the vacuole.
PSG1 is cleaved by KEX2 in two stable peptides, PSG1-N' and PSG1-C', the former supporting a role in maturation quality control, the latter having a role in modulating vesicular trafficking.
The precursor protein is cleaved into two polypeptide chains, PSG1-N' and PSG1-C'. The cleavage is performed in the Golgi apparatus by Ca(+)-dependent serine protease KEX2 between Arg-229 and Asp-230.
With EXP1, the specific cargo receptor protein for the plasma membrane ATPase PMA1, is involved in the transport and/or maturation of PMA1 (PubMed:28727280). EXP1 and PSG1 probably act sequentially to promote PMA1 sorting between the ER and the Golgi, with EXP1 promoting PMA1 export from the ER to the Golgi while PSG1 has a role in PMA1 maturation or quality control in the Golgi (PubMed:28727280). PSG1 might also couple PMA1 sorting and maturation in the early secretory pathway with the glycosylation machinery (Probable).
Belongs to the CTL (choline transporter-like) family.
Probably involved in transport through the plasma membrane.
Belongs to the nucleoporin NSP1/NUP62 family.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NSP1 interacts alternatively with NUP82 or NUP57 through its C-terminal coiled coil in two distinct NPC subcomplexes, the NUP82 subcomplex and the NUP57 subcomplex (NIC96, NSP1, NUP49, NUP57). The NUP82 subcomplex is the base for interactions with NUP116 and GLE2 and with NUP42 and GLE1. Interacts through its FG repeats with karyopherins, such as KAP95, KAP123, PSE1, LOS1, NTF2, the heterodimeric mRNA transport factor MEX67/MTR2, and GSP1.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NSP1 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, pre-ribosome, signal recognition particle (SRP), and protein transport.
Exists either as a homo- or heterooligomer.
Catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Together with DPP1, regulates intracellular DGPP and PA levels which are phospholipid molecules believed to play a signaling role in stress response. Can also use lysophosphatidic acid (LPA) as a substrate. Substrate preference is PA > DGPP > LPA.
PA phosphatase activity is magnesium ion-independent and potently inhibited by N-ethylmaleimide. Also inhibited by phenylglyoxal and propranolol.
The phosphatase sequence motif I (including Arg-143) and II (including His-189) are part of the cytoplasmic loop 2 and phosphatase sequence motif III (including His-235) is part of the cytoplasmic loop 3.
Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain VTC4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation (PubMed:19390046). The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen (PubMed:25315834, PubMed:19390046). PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase (PubMed:25315834). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important intracellular signaling molecules (PubMed:27080106). Inositol polyphosphate binding promotes vacuolar polyphosphate synthesis (PubMed:27080106). The VTC complex also plays a role in vacuolar membrane fusion (PubMed:11102525, PubMed:11823419). Required for SEC18/NSF activity in SNARE priming, membrane binding of LMA1 and V(0) trans-complex formation (PubMed:11823419).
Present with 2915 molecules/cell in log phase SD medium.
By ketoconazole. the promoter contains a sterol regulatory element motif, which has been identified as a UPC2-binding site.
Involved in membrane organization. Required for the formation of membrane compartments of CAN1 (MCCs), localization of CAN1 at the MCCs and subsequent invagination of the plasma membrane at the MCCs sites. Involved in eisosome organization and might act as a sensor of sphingolipids that regulates plasma membrane function. Involved in a novel pathway of export of proteins that lack a cleavable signal sequence. Non-classical export pathway functions also as an alternative clearance/detoxification pathway to eliminate damaged material, when the basic repair pathway is not sufficient.
Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself.
Autoubiquitinated by the E3 ubiquitin ligase complex in conjunction with the E2 enzyme CDC34.
Interacts with SKP1. Component of the probable SCF(YDR306C) complex containing CDC53, SKP1, RBX1 and YDR306C.
The F-box domain contains an unusual insert of 18 residues (131-148).
Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity; specifically the MCM2-MCM5 association is proposed to be reversible and to mediate a open ring conformation which may facilitate DNA loading. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity.
Involved in the processing of the 20S pre-rRNA. Required for survival upon K1 Killer toxin exposure.
May be involved in the mRNA export process (By similarity). Forms the [NU+] prion and induces [PSI+] prion formation.
The N-terminal 153 residues are responsible for the prion properties of NEW1.
May contain a covalently attached chromophore.
Phosphorylated by cyclin-dependent kinases CDC28 and PHO85 in association with G1-cyclins, promoting degradation of SIC1 and exit form G1.
Substrate and inhibitor of the cyclin-dependent protein kinase CDC28. Its activity could be important for faithful segregation of chromosomes to daughter cells. It acts in response to a signal from a post-start checkpoint.
Transporter required for vacuolar uptake of histidine and lysine.
Involved in endoplasmic reticulum to Golgi transport. Involved in a protein-transport step blocked by brefeldin A, which disrupts the Golgi apparatus and its incoming protein flux. May also be involved for mass growth or cell proliferation.
Up-regulated during cold stress and following nutrient replenishment by dilution of cells fron exhausted to fresh minimal medium.
Expression induced during phosphate starvation. Repressed by inorganic phosphate.
Partially mediates extracellular nucleotide derived phosphate hydrolysis along with NPP1 and NPP2.
Depletion causes defects in processing of pre- rRNA and assembly of ribosomal subunits.
Involved in resistance to methylmercury. Overexpression suppresses a PAM1-SLV3 double null mutation.
Belongs to the TORC subunit TCO89 family.
Component of TORC1, which regulates multiple cellular processes to control cell growth in response to environmental signals. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls ribosome biogenesis via control of rRNA, ribosomal protein and tRNA gene expression, and rRNA processing. TORC1 positively controls protein biosynthesis by regulation of mRNA stability, translation initiation factor activity, and high-affinity amino acid permeases that serve to provide amino acids for use by the translation machinery. TORC1 also promotes growth by sequestering a number of nutrient and general stress-responsive transcription factors in the cytoplasm. TORC1 negatively controls macroautophagy, a process to recycle surplus cytoplasmic mass under nutrient starvation conditions.
Present with 243 molecules/cell in log phase SD medium.
The target of rapamycin complex 1 (TORC1) is composed of at least KOG1, LST8, TCO89 and either TOR1 (TORC1-A) or TOR2 (TORC1-B) (PubMed:14736892). Interacts with PIB2; following activation of PIB2 by glutamine or cysteine (PubMed:29698392). TORC1 binds to and is inhibited by FKBP-rapamycin (PubMed:14736892).
Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for simple Y, 5'-flap and replication fork-like structures. It cleaves the strand bearing the 5'-non-homologous arm at the branch site junction and generates ligatable, nicked products from the 5'-flap or replication fork substrates. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. Has Holliday junction resolvase activity in vitro.
Transcription factor that regulates ERG9, but seems to have a more global function in transcription.
Forms a transiant heterodimeric complex with LMO1, that acts as a guanine nucleotide exchange factor exchange factor (GEF) for the small GTPase RHO5 (PubMed:25598154). DCK1, LMO1 and RHO5 relocate to mitochondria upon oxidative stress and trigger cell death (PubMed:25598154). The DCK1/LMO1/RHO5 signaling module mediates mitochondrial turnover under nitrogen starvation conditions via mitophagy (PubMed:25598154). The DCK1/LMO1/RHO5 signaling module plays also a function in cell wall integrity signaling (PubMed:25598154).
Present with 3497 molecules/cell in log phase SD medium.
Targets proteins containing a FFAT motif to endoplasmic reticulum membranes. Regulates phospholipid biosynthesis by modulating the subcellular localization of the transcriptional repressor OPI1.
DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair and base excision repair. Resolves abortive DNA ligation intermediates formed either at base excision sites, or when DNA ligases attempt to repair non-ligatable breaks induced by reactive oxygen species. Catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined (PubMed:16964241, PubMed:24362567). Likewise, catalyzes the release of 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA, but has higher specific activity with 5'-linked adenosine (AppDNA) (By similarity).
The HIT domain is required for enzymatic activity.
ATP-binding RNA helicase component of the TREX complex involved in transcription elongation and required for the export of mRNA out of the nucleus. SUB2 also plays a role in pre-mRNA splicing and spliceosome assembly. May be involved in rDNA and telomeric silencing, and maintenance of genome integrity.
Belongs to the DEAD box helicase family. DECD subfamily.
Component of the TREX complex composed of at least SUB2, TEX1, YRA1 and the four THO complex components: HPR1, MFT1, THO2 and THP1. Interacts with HPR1, YRA1, and YRA2. SUB2 may mediate the interaction between the THO complex and YRA1. Associates with growing mRNP complexes during transcription. This association requires the presence of HPR1. Interacts also with SAC3.
Belongs to the FAD-dependent oxidoreductase family.
Putative FAD-dependent oxidoreductase involved in the resistance to cercosporin and other singlet oxygen-generating photosensitizers. Translocates from mitochondria to the nucleus under apoptotic conditions, where it degrades DNA and induces apoptosis.
Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Belongs to the aldolase class II family. MtnB subfamily.
Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) composed of at least BLI1, BLS1, CNL1, KXD1, SNN1 and VAB2. Interacts with VAC8.
Decreases TORC1 activation in response to glutamine.
Serine/threonine-protein kinase required for cytoplasm to vacuole transport (Cvt) and autophagy as a part of the autophagy-specific VPS34 PI3-kinase complex I. This complex is essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Is also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). By regulating VPS34 kinase activity, VPS15 appears to be essential for the efficient delivery of soluble hydrolases to the yeast vacuole.
Truncation of 30 residues from the C-terminus results in a temperature-conditional defect in protein sorting.
Accumulates 20% of ergosterol of wild type.
Belongs to the NADPH--cytochrome P450 reductase family.
By galactose and on the plasma membrane by iron or copper deficiency. Repressed by glucose.
Present with 46600 molecules/cell in log phase SD medium.
This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis. Has NADPH-dependent ferrireductase activity on the plasma membrane.
Heterodimer with MND1. MND1-HOP2 binds preferentially to dsDNA.
Required for proper homologous chromosome pairing and efficient cross-over and intragenic recombination during meiosis. Stimulates DMC1-dependent homologous strand assimilation required for the resolution of meiotic double-strand breaks.
Causes a block in ER to Golgi transport. Exhibits exaggerated ER structures displaying interconnected networks of ER cisternae. Cells arrest at all stages of the vegetative cycle.
Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. The complex interacts with ARF1 and PAB1.
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. Required for mitochondrial morphology.
Regulatory subunit, binds to type-1 protein phosphatase. Functions with HEX2/REG1 and SNF1 protein kinase to regulate growth. Might regulate SNF1 directly or indirectly.
Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines, but also purine-derived lesions, alkylation damage and cytosine photoproducts generated by UV irradiation as well as abasic sites. Has also 8-oxoguanine DNA glycosylase activity. The AP lyase can incise AP sites opposite all four bases. May also play a role in the regulation of mtDNA copy number by introducing a double-stranded break (DSB) at the mtDNA replication origin ori5, initiating the rolling-circle mtDNA replication.
Does not possess a consensus sequence for a C-terminal iron-sulfur center typical of all other endonuclease III homologs.
Greatly increases spontaneous and hydrogen peroxide-induced mutation frequency. Causes mitochondrial genome instability. Suppresses mitochondrial point mutation rates, frameshifts and recombination rates, probably because NTG1 can generate mutagenic intermediates in yeast mitochondrial DNA.
Monosumoylated. Sumoylation is associated with targeting of NTG1 to nuclei containing oxidative DNA damage.
Non-catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body.
tRNA splicing endonuclease is a heterotetramer composed of SEN2, SEN15, SEN34 and SEN54. Interacts directly with SEN34.
Involved in the transport of biosynthetic membrane proteins from the prevacuolar/endosomal compartment to the vacuole. Required for multivesicular body (MVB) protein sorting. Catalyzes the ATP-dependent dissociation of class E VPS proteins from endosomal membranes, such as the disassembly of the ESCRT-III complex.
Monomer or homodimer (in nucleotide-free form). Decamer, dodecamer or tetradecamer of two stacked respective homooligomeric rings (when bound to ATP); the dodecameric form seems to be predominant. Interacts with VPS20. Interacts with VTA1; the interaction requires the dimeric structure of VTA1; 6 homodimers of VTA1 appear to associate with the dodecameric VSP4 complex. Interacts with DID2. Interacts with DID4. Interacts with IST1; IST1 competes with VTA1 for binding with VPS4.
Channel-forming protein essential for import of protein precursors into mitochondria.
Forms part of the preprotein translocase complex of the outer mitochondrial membrane (TOM complex) which consists of at least 7 different proteins (TOM5, TOM6, TOM7, TOM20, TOM22, TOM40 and TOM70). Interacts with mitochondrial targeting sequences. Interacts with FCJ1.
Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
MSU1 and SUV3 are the two components of the mitochondrial degradosome (mtEXO).
Required for intron-independent turnover and processing of mitochondrial RNA. Participates in 3' mtRNA processing where it hydrolyzes single-stranded RNA or partially double-stranded RNA with 3' single-stranded tails.
Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter (By similarity). Interacts with PLP2; this interaction leads to inhibition of CCT complex mediated actin folding (PubMed:17429077).
Involved in the regulation of calcium ion homeostasis. Binds to the calcineurin-dependent response element. Transcriptionally regulates PMC1, PMR1, PMR2A and FKS2.
Phosphorylated. Dephosphorylated by calcineurin which leads to rapid translocation from the cytoplasm to the nucleus. Phosphorylated by the cyclin-CDK PHO80-PHO85.
Dual specificity phosphatase that dephosphorylates MAP kinase FUS3 on both a Tyr and a Ser or Thr. Has a role in adaptation to pheromone.
Component of the 66S pre-ribosomal particle. Interacts with NOP7, RRP1, RRP15 and SHE2.
Present with 3650 molecules/cell in log phase SD medium.
Required for efficient assembly and nuclear export of the 60S ribosomal subunit. Involved in asymmetric localization of ASH1 mRNA.
Ubiquitinated at 'Lys-6' and 'Lys-8' by HEL2/UBC4, to activate the ribosome quality control (RQC) pathway in response to stalled ribosomes.
Component of the R2TP complex composed at least of RVB1, RVB2, TAH1 and PIH1. Interacts also with HSP90, RRP43, NOP53 and NOP58.
Involved in pre-rRNA processing and required for the NOP58-snoRNA interaction.
Belongs to the metallo-dependent hydrolases superfamily. ATZ/TRZ family.
Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Belongs to the pantothenate synthetase family.
Required for pantothenic acid biosynthesis.
Cell cycle regulated, with a peak in mid to late S phase.
Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Together with cyclin PCL6, controls glycogen phosphorylase and glycogen synthase activities in response to nutrient availablility. The PCL7-PHO85 cyclin-CDK holoenzyme has GLC8 kinase activity and phosphorylates and inactivates the phosphatase PP1-2 inhibitor GLC8, causing activation of PP1-2, which then dephosphorylates and activates glycogen phosphorylase. PCL7-PHO85 also phosphorylates MMR1 and YJL084C.
Forms a cyclin-CDK complex with PHO85. Interacts with the substrate proteins MMR1 and YJL084C. Interacts with the CDK inhibitor (CKI) PHO81.
The PCL7-PHO85 cyclin-CDK is inhibited by PHO81 in low-phosphate conditions.
Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit. Unlikely to play a significant role in nonsense-mediated mRNA decay (NMD).
Beta subunit of a guanine nucleotide-binding protein (G proteins). G proteins are involved as modulators or transducers in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Involved in the determination of the cAMP level according to nutritional conditions, most probably as a regulator of cAMP phosphodiesterase. Required for the control of pseudohyphal and haploid invasive growth.
Interacts with SKP1 and YPT32; SKP1 is required for the interaction with YPT32.
Non-SCF-type F-box protein involved in the endocytic with the vacuolar sorting pathway. Acts as a repressor of YPT52 by inhibiting the formation of active, GTP-bound, YPT52. Involved in the defense mechanism against methylmercury toxicity.
The F-box domain is required for interaction with SKP1 and defense against methylmercury toxicity.
May be involved in membrane protein folding.
Expression is up-regulated by the MCM1 alpha cell-type-specific transcription factor.
MATalpha-specific protein that interferes with a-factor, the pheromone secreted by MATa cells (PubMed:24121774). Contributes to mating efficiency (PubMed:24121774). Acts to bind and sequester a-factor rather than to degrade it, and promotes the efficient mating of MATalpha cells by keeping the a-factor concentration at the plasma membrane within the narrow range needed for accurate pheromone gradient detection (Probable).
Involved in amino acid efflux from the vacuole to the cytoplasm. Capable of transporting aspartate and glutamate. Requires ATP for function.
Methylated by HMT1 (PubMed:9499403, PubMed:10024178). The methylation is required for nuclear export (PubMed:9499403).
RNA-binding protein, which is involved in the polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor CFIA complex and the cleavage and polyadenylation factor (CPF) complex. May be involved in regulation of poly(A) site selection. Is involved in nonsense-mediated mRNA decay. Seems to bind to an RNA downstream sequence element (DSE) located 3' of a nonsense codon and may mark the transcript for decay.
Required for degradation of unstable forms of cytochrome c.
Mitochondrial aminoacyl-tRNA synthetase that catalyzes the attachment of tryptophan to tRNA(Trp).
Component of the vacuole-localized DSC E3 ubiquitin ligase complex involved in the targeting of the complex to the vacuole membrane via the AP3 pathway to ubiquinate vacuolar membrane proteins (PubMed:29355480). Competes with GLD1 to determine the subcellular localizations of the DSC complex (PubMed:29355480).
Part of the vacuole-localized DSC E3 ligase complex composed of at least TUL1, DSC2, DSC3, UBX3, CDC48 and VLD1.
Involved in nuclear export of the lipid kinase MSS4 and of the 60S ribosomal subunit. May also play a role in directing MSS4 to the plasma membrane. Plays a role in actin cytoskeleton organization and vesicular transport.
Phosphorylated by the PHO85-PCL1 kinase complex.
Interacts with MDM31. Participates in a complex of about 175 kDa.
Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is essential for mitotic growth and suppresses formamide sensitivity of the RSC8 mutants.
Interacts directly with RSC8. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin.
Positively regulated by signaling through MPK1 in response to cell wall perturbation. Expression is regulated by the ACE2 and SWI5 transcription factors.
Belongs to the UTP23/FCF1 family. UTP23 subfamily.
Involved in rRNA-processing and ribosome biogenesis.
Present with 1590000 molecules/cell in log phase SD medium.
Belongs to the mitochondrion-specific ribosomal protein mL59 family.
Acts as a non-essential regulatory component of the translation initiation factor 2B (eIF2-B or GCD complex), which catalyzes the exchange of eukaryotic initiation factor 2 (eIF-2)-bound GDP for GTP and is regulated by phosphorylated eIF-2 (PubMed:8506384, PubMed:9472020). It activates the translation of GCN4 in response to low amino acid, carbon, or purine availability, by suppressing the inhibitory effects of multiple uORFs present in the leader of GCN4 mRNA (PubMed:10733573). It may promote either repression or activation of GCN4 expression depending on amino acid availability (PubMed:8506384). Modulation of GCN3 regulatory function in response to amino acid availability occurs post-translationally (PubMed:8506384, PubMed:9472020).
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Converts specifically D-serine to pyruvate and ammonia. May play a role in D-serine detoxification.
Sodium cyanoborohydride, N-ethylmaleimide, hydroxylamine, phenyhydrazin and EDTA are inhibitors of the catalytic activity.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. SPB1 subfamily.
Component of the nucleolar and nucleoplasmic pre-60S ribosomal particle. Interacts with the snoRNA-associated proteins NOP1 and NOP58.
Required for proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Specifically methylates the guanosine in position 2922 of the 25S rRNA at the stage of 27S pre-rRNA maturation. Methylates also the uridine in position 2921 in the absence of methylation of this residue guided by snoRNA snR52 at the stage of 35S pre-rRNA maturation.
Present with 58200 molecules/cell in log phase SD medium.
Belongs to the methyltransferase superfamily. Trimethylguanosine synthase family.
Catalyzes the two serial methylation steps for the conversion of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is specific for guanine, and N7 methylation must precede N2 methylation. Hypermethylates the m3G cap on TLC1 telomerase which affects telomere silencing and telomere length regulation. Required for pre-mRNA splicing, pre-rRNA processing and small ribosomal subunit synthesis. Involved in nucleolar structural organization.
Monomer (By similarity). Interacts with the spliceosomal snRNP core component SMB1 and the snoRNP components CBF5 and NOP58.
Substrate inhibited by S-adenosyl-L-homocysteine.
Involved in the synthesis of mannosyl phosphorylinositol ceramide (PubMed:9323360, PubMed:12954640). Catalyzes the addition of mannosyl to phosphorylinositol ceramide. Suppressor of RVS161 mutation (PubMed:9323360, PubMed:12954640).
Leads to altered sphingolipid synthesis.
Component of the decapping complex composed of DCP1 and DCP2. Interacts with mRNAs, DHH1, LSM1, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, and the cap-binding proteins PAB1 and TIF4632/eIF-4G.
Component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body. DCP1 is activated by the DEAD-box helicase DHH1 and destabilizes the eIF-4F cap-binding complex from the mRNA.
Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PubMed:9624178). Acts downstream of STT4, but in a pathway that does not involve PKC1. May be involved in the organization of the actin cytoskeleton (PubMed:8152413).
ATP-binding RNA helicase involved in ribosome assembly.
Belongs to the DEAD box helicase family. DDX27/DRS1 subfamily.
Has a role in promoting intracellular monovalent cation sequestration via the exchange of monovalent cations and especially Na(+) for hydrogen ions across the vacuolar membrane.
Could be the product of a pseudogene. This is a truncated version of an allantoate permease subfamily member protein. Strain S288c has a stop codon in position 170, which disrupts the gene coding for this protein and produces two ORFs YOL163W and YOL162W.
Component of the signal peptidase complex (SPC) composed of a catalytic subunit SEC11 and three accessory subunits SPC1, SPC2 and SPC3 (PubMed:9148931). The complex induces a local thinning of the ER membrane which is used to measure the length of the signal peptide (SP) h-region of protein substrates (By similarity). This ensures the selectivity of the complex towards h-regions shorter than 18-20 amino acids (By similarity). Interacts with SEC11 (PubMed:10206957). SPC associates with the translocon complex (PubMed:9148931).
Essential component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (PubMed:9148931, PubMed:9148930). Essential for the SPC catalytic activity, possibly by stabilizing and positioning the active center of the complex close to the lumenal surface (PubMed:9148931, PubMed:9148930). Essential for viability (PubMed:9148931, PubMed:9148930).
Homohexamer (By similarity). Interacts with THI11 (PubMed:12271461).
Belongs to the Dus family. Dus1 subfamily.
Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs (PubMed:12003496, PubMed:14970222). Specifically modifies U16 and U17 in cytoplasmic tRNAs (PubMed:12003496, PubMed:14970222). Also able to mediate dihydrouridylation of some mRNAs, thereby affecting their translation (By similarity).
Present with 65600 molecules/cell in log phase SD medium.
Belongs to the AB hydrolase superfamily. MetX family.
Phosphorylation of Ser-397 is induced 2-fold in response to mating pheromone.
Interacts with ribosomes. Interacts with EAP1 and MSL5 (via the GYP domain).
Interacts with PRM8. Binds to COPII coated vesicles (By similarity).
Expressed in both haploid and diploid yeast cells.
Inhibited by chelating agents like EDTA, TPEN and 1,1-phenanthroline, as well as NEM, free cysteine and DTT.
Involved in the N-terminal endoproteolytic cleavage of the P2 precursor of the a-factor mating pheromone. Capable of proteolysing the established mammalian insulin-degrading enzymes (IDEs) substrates amyloid-beta peptide and insulin B-chain.
It is uncertain whether Met-1 or Met-53 is the initiator. Met-53 is probably the physiologically relevant initiator methionine, as Met-1 is dispensable for the expression of functional STE23, whereas Met-53 is not.
Component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain. ZUO1 can act as a J-protein for SSB1/SSB2 only when associated with SSZ1.
Present with 86400 molecules/cell in log phase SD medium.
The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. APC2 interacts directly with APC11 thereby anchoring APC11 to the core complex.
Component of the mitochondrial large ribosomal subunit (mt-LSU) (PubMed:2060626, PubMed:9162110). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins (PubMed:24675956).
Present with 7850 molecules/cell in log phase SD medium.
Belongs to the actin family. ARP3 subfamily.
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC23 interacts with BET3 in order to target TRAPPI complex to COPII involved in internalization of plasma membrane proteins like the maltose transporter.
The COPII coat is composed of at least 7 proteins: the SEC23/24 complex, the SEC13/31 complex, SFB2, SFB3 and the protein SAR1. Forms two other heterodimeric complexes with SFB3 and PDR17. Interacts with BET1, BET3, BOS1, EMP24, GRH1, SEC16, SEC22 and SYS1.
Ubiquitinated. Ubiquitination is required for the formation of the SEC23/24 complex. Deubiquitinated by the UBP3/BRE5 complex.
Involved in protein transport from endosomes to the vacuole.
In the C-terminal section; belongs to the AIR carboxylase family. Class I subfamily.
Homotetramer. Component of the NTC complex (or PRP19-associated complex), composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2, and PRP19. The NTC complex associates with the spliceosome after the release of the U1 and U4 snRNAs and forms the CWC spliceosome subcomplex (or CEF1-associated complex) reminiscent of a late-stage spliceosome composed also of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8, PRP9, PRP11, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNU114, SPP2, RSE1 and YJU2. Interacts with CLF1, ISY1, NTC20, PRP19, PRP46, SYF1 and SYF2. Interacts with CWC2.
Probable ubiquitin-protein ligase involved in pre-mRNA splicing. Acts as a central component of the NTC complex (or PRP19-associated complex) that associates to the spliceosome to mediate conformational rearrangement or to stabilize the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation. It is also probably involved in DNA repair.
The tetramer is an elongated particle consisting of four globular WD40 domains held together by a central stalk.
Has a role in controlling the cellular iron ion levels. Mobilizes vacuolar stores of iron in conditions of low iron levels.
Abnormal localization of ASH1 protein to daughter cell, with protein mislocalized to mother and daughter (PubMed:15082763). Decreases HO mRNA level (PubMed:15082763).
Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Recruited to specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease, via its interaction with SHE3.
Belongs to the bacterial ribosomal protein bL31 family. Highly divergent.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (PubMed:25609543, PubMed:24675956). Overexpression of bL31m suppresses mutations in the COX2 leader peptide-encoding and initiation codon regions (PubMed:11259585, PubMed:15166137).
Contains two functional domains. The central domain is sufficient for general mitochondrial translation but not suppression of COX2 mutants. The C-terminus sequence is sufficient for dosage suppression of COX2 mutants.
Overexpression suppresses mutations in the COX2 leader peptide-encoding and initiation codon regions.
Belongs to the ornithine cyclodeaminase/mu-crystallin family.
Activator of decapping that functions as a general and active mechanism of translational repression and required for P-body formation. First decay factor recruited to mRNA, at a time when the mRNA is still associated with translation factors. Subsequently, PAT1 recruits the hepta-heterodimer LSM1-LSM7 complex to P-bodies. In association with the LSM1-LSM7 complex, stabilizes the 3' terminus of mRNAs. This association is also required for mosaic virus genomic RNA translation. Modulates the rates of mRNA-decapping that occur following deadenylation. Might be required for promoting the formation or the stabilization of the preinitiation translation complexes. Required for 40S ribosomal subunit joining to capped and/or polyadenylated mRNA. With other P-body components, enhances the formation of retrotransposition-competent Ty1 virus-like particles. Necessary for accurate chromosome transmission during cell division.
Associates with the 40S ribosomal subunit. Associates with the heptameric LSM1-LSM7 complex. Interacts directly with LSM2 and LSM3 within the LSM1-LSM7 complex. Interacts with DHH1, LSM1, LSM5, RPB4, RPB7 and with topoisomerase TOP2. Interacts with CDC33, PAB1, TIF4631 and TIF4632 in an RNA-dependent manner. Binds mRNAs.
The region at residues 254 to 422 is required for stimulation of decapping. The region at residues 422 to 763 is required for PAT1 and LSM1 to accumulate in P-bodies and responsible for translation repression and P-body assembly.
Present with 7650 molecules/cell in log phase SD medium.
This is a truncated version of the ABC transporter NFT1. S288c has a stop codon in position 1219, which disrupts the gene coding for this protein and produces two ORFs YKR103W and YKR104W. A contiguous sequence for ABC transporter NFT1 can be found in strains Sigma 1278B, EG123 and SK1 (AC P0CE70).
Component of the MIS complex, a complex that mediates N6-methyladenosine (m6A) methylation on some mRNAs during meiosis and is required for sporulation.
Mutant is sporulation defective and fails to perform premeiotic DNA synthesis.
Expression is regulated by the AZF1 transcription factor.
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 10 subunits. The complex is composed of 3 respiratory subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10 (PubMed:10873857, PubMed:11880631, PubMed:18390544, PubMed:30598554). The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a monomer or a dimer of cytochrome c oxidase (complex IV, CIV), resulting in 2 different assemblies (supercomplexes III(2)IV and III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556, PubMed:30598554). QCR6 interacts with COX5A at the CIII-CIV interface (PubMed:30598554).
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.
Required for high-fidelity chromosome segregation during the later part of each cell cycle. Acts in opposition to the phosphatase PP1. Has a role in attaching the kinetochores to the microtubules and ensuring that sister kinetochores connect to opposite poles. The promotion of bi-orientation is achieved by selectively detaching kinetochore-microtubule attachments that are not under tension. Phosphorylates histone H3 to form H3S10ph during mitosis and meiosis. Phosphorylates RGD1 in vitro.
May be an autophosphorylating tyrosine kinase, a bifunctional (serine/tyrosine-specific) protein kinase, or a serine kinase that is a substrate for an associated tyrosine kinase. MCK1 is a transcriptional activator of IME1, it stimulates spore maturation, and play a positive regulatory role in both mitotic centromere function and activation of early meiotic gene expression.
Belongs to the PPP phosphatase family. PP-4 (PP-X) subfamily.
Catalytic subunit of the histone H2A phosphatase complex (HTP-C) containing PPH3, PSY2 and PSY4. Inactivated in a complex with phosphatase methylesterase PPE1 (PP2Ai). Interacts with phosphatase 2A activator RRD1, which can reactivate PP2Ai by dissociating the catalytic subunit from the complex. Interacts with SPT5 and TAP42.
Forms the histone H2A phosphatase complex in association with the regulatory subunits PSY2 and PSY4, which dephosphorylates H2AS128ph (gamma-H2A) that has been displaced from sites of DNA lesions in the double-stranded DNA break repair process. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint. PPH3 is directly involved in the dephosphorylation and activation of the transcription factor GLN3 in response to nutrient availability.
Reversibly methyl esterified on Leu-308 by leucine carboxyl methyltransferase 1 (PPM1) and protein phosphatase methylesterase 1 (PPE1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization (By similarity).
Was originally thought (PubMed:641056) to be a translation initiation factor but further analysis (PubMed:19424157 and PubMed:19338753) clearly suggests that it is involved in translation elongation and not translation initiation. subclass.
mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Critical for the efficient synthesis of peptide bonds between consecutive proline residues. Can resolve ribosomal stalling caused by consecutive prolines during translation (By similarity). Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Essential for polarized growth, a process necessary for G1/S transition. May mediate large range of effects of the polyamine spermidine in the cell.
G proteins are composed of 3 units, alpha, beta and gamma. The beta-gamma subunit complex (STE4-STE18 complex) interacts with PLP1 and PLP2.
Implicated in the pheromone A- and alpha-factor response pathway. The beta and gamma chains of the putative yeast mating response pathway G protein play a positive role in initiation of the mating response.
Belongs to the NTC complex (or PRP19-associated complex), composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2, and PRP19. The NTC complex associates with the spliceosome after the release of the U1 and U4 snRNAs and forms the CWC spliceosome subcomplex (or CEF1-associated complex) reminiscent of a late-stage spliceosome composed also of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8, PRP9, PRP11, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNU114, SPP2, RSE1 and YJU2. Interacts with PRP19.
Involved in pre-mRNA splicing by stabilizing the NTC (or PRP19-associated complex). As a component of the NTC complex, associates to the spliceosome to mediate conformational rearrangement or to stabilize the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation.
Belongs to the bacterial ribosomal protein bL12 family.
Component of the mitochondrial large ribosomal subunit (mt-LSU) (PubMed:15221522, PubMed:16451194). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins (PubMed:24675956).
Homodimer. The dimers can then associate to form a ring-shaped homohexamer. Interacts with NPL3, BRE5, MTR4, SNF2, SUM1, and SSD1.
S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that catalyzes both the mono- and asymmetric (type I) dimethylation of the guanidino nitrogens of arginine residues in a variety of RNA-binding proteins such as heterogeneous nuclear ribonucleoproteins (hnRNPs) and small nuclear ribonucleoproteins (snRNPs) (PubMed:8668183, PubMed:8647869). Methylates NAB2, NPL3, HRP1 and YRA1, shuttling hnRNPs involved in mRNA processing and export, facilitating their export out of the nucleus (PubMed:8668183, PubMed:9499403, PubMed:10652296, PubMed:11779864, PubMed:15314027). Methylation of NPL3 weakens its interaction with THO2, a component of the TREX (transcription/export) complex important for transcriptional elongation and recruitment of mRNA export factors (PubMed:15314027, PubMed:20053728). Methylates the hnRNP HRB1, but does not influence its subcellular location (PubMed:9499403). Methylates the nucleolar proteins GAR1, NOP1 and NSR1 (PubMed:12756332). Methylates the snRNP SNP1 and modulates the cotranscriptional recruitment of splicing factors (PubMed:20823272). Dimethylates free histone H4 (HHF1/HHF2) at 'Arg-4' (H4R3me2a) and plays a role in preservation and establishment of silent chromatin domains (PubMed:12097318, PubMed:17158743). Mono- and dimethylates ribosomal protein S2 (RPS2) at 'Arg-11' (PubMed:20035717). Methylates the catalytic subunit of the SWI/SNF chromatin-remodeling complex SNF2 (PubMed:22997150).
Histone-binding component of the NuA3 histone acetyltransferase complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation. YNG1 is required for the HAT activity of NuA3 but not for its integrity. Mediates the interaction of SAS3 with nucleosomes.
Interacts with H3K4me3 and to a lesser extent with H3K4me2. Component of the NuA3 complex, composed of at least NTO1, SAS3, TAF14, YNG1 and EAF6. Interacts with histone H3-K4 trimethylated.
Belongs to the dynein heavy chain family.
Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required to maintain uniform nuclear distribution in hyphae. May play an important role in the proper orientation of the mitotic spindle into the budding daughter cell yeast. Probably required for normal progression of the cell cycle.
Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function.
The dynein complex consists of at least two heavy chains and a number of intermediate and light chains. Interacts with DYN3.
ATP-dependent RNA helicase required for ribosome biogenesis. Involved in the release of U14 snoRNA in pre-ribosomal complexes. Required for pre-rRNA cleavage at site A2.
Belongs to the DEAD box helicase family. DDX10/DBP4 subfamily.
Interacts with the U3 and U14 snoRNAs. Associates with pre-ribosomal complexes.
Belongs to the methyltransferase superfamily.
Probable S-adenosylmethionine-dependent methyltransferase which mediates cantharidin resistance.
HSP SSA4 expression is restricted to conditions of stress.
Interacts with actin and cofilin in a ternary complex.
Involved in the depolymerization of actin filaments. Enhances the filament disassembly activity of cofilin and restricts cofilin localization to cortical actin patches.
F-box protein probably involved in ubiquitin conjugation pathway. Involved in the resistance to ciclopirox olamine (CPO), a synthetic antifungal agent.
Component of the mitochondrial large ribosomal subunit (mt-LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. uL22m forms the wall of the exit tunnel.
Component of the E3 ubiquitin ligase complexes SCF with HRT1, some cullins like CDC53, and some F-box proteins like MET30 CDC4 and SAF1. Interacts with CDC53 and MET30 to form the E3 ubiquitin ligase complex SCF(Met30) which also contains MET4. Forms complex SCF(Cdc4) together with CDC4 and CDC53. Component of the CBF3 complex, which is formed of CBF3A/CBF2, CBF3B/CEP3, CBF3C/CTF13 and CBF3D. Component of the RAVE complex composed of RAV1, RAV2 and SKP1/CBF3D. Interacts with RCY1, ROY1, CBF3D and SGT1.
Essential component of the E3 ubiquitin ligase complex SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins like phosphorylated SIC1. Participates in the attachment of chromosomes to the spindle. Acts as a regulatory component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromeres and in several promoters. The association of CBF3C with CBF3D and SGT1 is required for CBF3C activation and CBF3 assembly. SKP1/CBF3D could retrieve cyclins or cyclin-CDK-like proteins into the kinetochore thus providing cell cycle-regulated kinetochore activity. Involved in the regulation of methionine biosynthesis genes. Facilitates association of CDC53 with CDC4 and of ROY1 with YPT52.
Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate.
Not known. It is a suppressor of protein phosphatase 2A depletion.
VPS4-associated protein involved in trafficking to the vacuole.
Promotes K(+) uptake, by the potassium transporter TRK1-TRK2, which leads to the subsequent cellular resistance to toxic cations such as Na(+), Li(+) and Ca(2+).
Does not bind efficiently to phosphoinositides and does not associate with membranes.
Positive regulator of FPS1 glycerol channel required for the glycerol efflux.
Required for polarized growth and efficient budding.
Polyol dehydrogenase that catalyzes the reversible NAD(+)-dependent oxidation of various sugar alcohols. Is active with D-sorbitol (D-glucitol) and xylitol as substrates, leading to the C2-oxidized product D-fructose and D-xylulose, respectively. Is likely involved in the utilization of D-sorbitol as a sole carbon source for growth. Has no activity on mannitol and primary alcohols such as ethanol.
Grows more slowly in amino acid-free medium (SD), when combined with disruption of MPC3.
Mainly expressed when grown on glucose containing growth medium.
Nonessential component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. Together with SPT15/TBP UAF seems to stimulate basal transcription to a fully activated level. UAF30 seems to play a role in silencing transcription by RNA polymerase II.
Phosphorylated by serine/threonine protein kinase IPL1.
Required for high-fidelity chromosome segregation during the later part of each cell cycle in association with the protein kinase IPL1. Stimulates IPL1 kinase activity and facilitates its association with the mitotic spindle. Has a role in attaching the kinetochores to the microtubules and ensuring that sister kinetochores connect to opposite poles.
Belongs to the JARID1 histone demethylase family.
Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated H3 'Lys-4'.
Present with 290 molecules/cell in log phase SD medium.
The JmjC domain is required for enzymatic activity.
Cell cycle-dependent with low levels at START and a peak in mitosis (at protein level).
Interacts with AXL1, AXL2, IQG1 and SEC3.
Required for establishment of the axial budding pattern in haploid cells. Cooperates with other bud site selection proteins to recognize a spatial landmark during mitosis and they subsequently become a landmark for downstream polarity establishment factors that coordinate axial budding and cytokinesis. Involved in the septin organization at the bud neck.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Plays a major role in negative regulation of the heat shock transcription factor (HSF).
Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to organize PAM16-PAM18 (TIM16-TIM14) heterodimer.
Component of the PAM complex, at least composed of mtHsp70, MGE1, TIM44, PAM16, PAM17 and PAM18/TIM14.
RNA-dependent helicase required for nonsense-mediated decay (NMD) of aberrant mRNAs containing premature stop codons and modulates the expression level of normal mRNAs (PubMed:8896465, PubMed:30218034). Also capable of unwinding double-stranded DNA and translocating on single-stranded DNA (PubMed:30218034).
Interacts with MST27. Binds to coatomer proteins of COPI and SEC23/SEC24 of COPII coated vesicles.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NUP157 may be part of a NPC subcomplex containing NUP53, NUP170, and NUP59. In addition it may bind to MAD2.
Not known; suppressor of sulfoxide ethionine resistance.
Interacts directly with SSP1. Probable component of a SPB complex composed of ADY3, SSP1, DON1, MPC54, SPO21/MPC70, NUD1 and CNM67.
Involved in the pathway that organizes the prospore membrane (PSM) during sporulation. Mediates the assembly of the DON1 ring structure at the leading edge of PSM during meiosis II. May constitute a physical link between SSP1-containing PSM precursors and the spindle pole body (SPB) and may facilitate the recruitment of other factors that are required to promote spore wall formation.
Belongs to the acetyltransferase family. MAK3 subfamily.
Catalytic component of the NatC N-terminal acetyltransferase, which catalyzes acetylation of the N-terminus Met of L-A virus GAG protein and possibly GRH1.
By sodium ions. Induction at low salt concentrations (0.3 M) is mediated by the high-osmolarity glycerol (HOG)-MAP kinase pathway, a system activated by non-specific osmotic stress, and by the protein kinase A pathway. At high salt concentrations (0.8 M) is mediated by the protein phosphatase calcineurin, which is specifically activated by sodium ions.
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the sodium or lithium ions to allow salt tolerance. Is negatively modulated by SIS2/HAL3.
Binds DNA in a sequence-specific manner.
Copurifies with proteins HOL1, MMP1, PEX7 and PLB1.
The mating factor alpha-1 precursor is identical in S.italicus, S.uvarum and S.cerevisiae, except for the number of tandem repeat units: 5, 3 and 4 respectively.
Transporter for ammonium (both charged and uncharged NH3 and NH4) to use as a nitrogen source. Can also transport methylamine. The affinity of MEP1 is about twenty times lower than that of MEP2. MEP3 has the lowest affinity.
Although strongly related to the DcpS enzyme, it has apparently no scavenger mRNA-decapping activity.
Plays a role in the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Stress-induced regulatory protein that modulates the m7GpppX diphosphatase activity of DCS1.
Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA.
Activates HIS4 transcription only in combination with PHO2/BAS2. BAS1 is also involved in the regulation of the purine biosynthesis pathway.
Component of a ubiquitin-protein ligase complex consisting of the cullin CUL3, the linker protein ELC1, the substrate receptor ELA1, and the RING protein HRT1.
It is unsure how the mitochondrial and cytoplasmic forms of this protein are produced. The cytoplasmic form may be produced by alternative initiation at a downstream in-frame AUG codon at position 34, lacking a mitochondrial transit peptide.
Present with 4120 molecules/cell in log phase SD medium.
Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding. Postspliced cytoplasmic tRNAs are imported into the nucleus, where this first step seems to take place, after which they are reexported to the cytoplasm, where the yW sythesis is completed by cytoplasmic enzymes.
Formylates methionyl-tRNA in mitochondria and the cytoplasm (PubMed:10781559, PubMed:30409808). Responsible for the formylation of the 8 N-terminally formylated (Nt-formylated) mitochondrial matrix proteins that are encoded by mitochondrial DNA (PubMed:10781559, PubMed:12549912). Nt-formylated proteins in the cytoplasm are strongly up-regulated in stationary phase or upon starvation for specific amino acids (His or Lys) and are targeted for degradation by a PSH1 E3 ubiquitin ligase-mediated fMet/N-end rule pathway. Increased Nt-formylation of cytosolic proteins appears to be important for adaptation to these stresses. Stationary phase-degraded Nt-formylated proteins include histone H3-like centromeric protein CSE4, Mediator complex subunit 3 (PGD1) and small ribosomal subunit protein uS8-A (RPS22A) (PubMed:30409808).
Formylation of the initiator Met-tRNA is not essential for mitochondrial protein synthesis in S.cerevisiae.
Phosphorylated by GCN2 in response to nutrient deprivation. Phosphorylation mediates retention of FMT1 in the cytoplasm.
Terminates the cell cycle delay. Reverses the CDC28 phosphorylation catalyzed by SWE1.
mRNA stabilization factor specific for the 0.95 kb OLI1 mRNA. Also involved in OLI1 ring formation.
Co-chaperone that binds to the molecular chaperone HSP82 and stimulates its ATPase activity. Binding to HSP82 promotes a conformational switch in the catalytic loop of HSP82, facilitating the interaction of the catalytic 'Arg-380' with ATP in the N-terminal nucleotide-binding domain. Although not essential, it confers thermotolerance when intracellular levels of HSP82 are limiting.
Present with 13939 molecules/cell in log phase SD medium.
Belongs to the Nup84/Nup107 nucleoporin family.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NUP84 is part of the heptameric 0.5 MDa autoassembling NUP84 NPC subcomplex (NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1).
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP84 is involved in nuclear poly(A)+ RNA export, in NPC assembly and distribution, as well as in nuclear envelope organization.
Heterodimer of MLH1 and PMS1, called MutLalpha, which is the major MMR MutL activity correcting base-base mismatches as well as IDLs. The heterodimer binds double strand DNA independently of a mismatch with positive cooperativity and has more than one DNA binding site. Forms a ternary complex with either the MSH2-MSH6 (MutSalpha) or the MSH2-MSH3 heterodimer (MutSbeta), which recognize and bind to mismatch DNA. Ternary complex formation is promoted by ATP binding. Heterodimer of MLH1 and MLH3, called MutLbeta, which is involved in correction of a specific subset of IDLs when associated with MutSbeta. Heterodimer of MLH1 and MLH2.
Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of different MutL heterodimers that form a ternary complex with the MutS heterodimers, which initially recognize the DNA mismatches. This complex is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in maintaining the genetic stability of simple sequence repeats, the repair of heteroduplex sites present in meiotic recombination intermediates, and the promotion of meiotic crossing-over.
To S.pombe bem46 and M.tuberculosis Rv2307c.
Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from SEC61 may govern the activity of the translocon. SEC66 is required to attach or retain SEC72 in the SEC63 complex. It is essential for growth at elevated temperatures.
Component of the heterotetrameric Sec62/63complex composed of SEC62, SEC63, SEC66 and SEC72. The Sec62/63 complex associates with the Sec61 complex to form the Sec complex. Part of a complex consisting of KAR2, SEC63, SEC66 and SEC72.
Present with 40600 molecules/cell in log phase SD medium.
Required for cellular morphogenesis and polarization of the cortical cytoskeleton. It might act in concert with proteins such as CDC42 and CDC43 to limit the region of cortical patch formation to the cortex of the bud. Required for the accumulation and/or maintenance of plasma membrane H(+)-ATPase on the cell surface.
Component of the DSC E3 ligase complexes composed of at least TUL1, DSC2, DSC3, UBX3, CDC48 as well as VLD1 for the vacuole-localized complex or GLD1 for the Golgi/endosome-localized complex (PubMed:29355480). Interacts with CDC48 (PubMed:15258615).
Component of the DSC E3 ubiquitin ligase complexes that tag proteins present in Golgi, endosome and vacuole membranes and function in protein homeostasis under non-stress conditions and support a role in protein quality control (PubMed:25078903, PubMed:29355480). Involved in CDC48-dependent protein degradation through the ubiquitin/proteasome pathway. Involved in delivery of substrates to the 26S proteasome. Also required for membrane fusion (By similarity).
Present with 233 molecules/cell in log phase SD medium.
Present with 103000 molecules/cell in log phase SD medium.
Required for respiration. Stabilizes the mitochondrial bicistronic mRNA encoding ATP6 and ATP8, 2 subunits of the proton-translocating ATP synthase.
Glycosylated (possible); but there is not yet direct biochemical evidence for it.
Belongs to the cytidine and deoxycytidylate deaminase family. ADAT3 subfamily.
In contrast to other cytidine and deoxycytidylate deaminase, lacks to conserved Glu active site in position 218 which is replaced by a Val residue, suggesting that it acts as a regulatory subunit.
Belongs to the enoyl-CoA hydratase/isomerase family. Mitochondrion-specific ribosomal protein mS47 subfamily.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (PubMed:14566057, PubMed:25609543, PubMed:28154081). mS47 has enzymatic activity in vitro, and is able to catalyze the specific hydrolysis of 3-hydroxyisobutyryl-CoA (HIBYL-CoA). However, because the turnover rate of mS47/EHD3 is only a fraction of that of the homologous mammalian enzyme, the physiological function of this activity remains unclear (PubMed:12697341). Has an indirect role in endocytic membrane trafficking (PubMed:11378903).
Component of the mitochondrial small ribosomal subunit (mt-SSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. mS47 forms a protuberance of the yeast mitoribosome and retains a solvent-exposed cavity liekly capable of accommodating a substrate, in accordance with it being an active enzyme as well as an integral constituent of the mitoribosome.
Present with 3950 molecules/cell in log phase SD medium.
Hydroxylation at Pro-64 affects translation termination efficiency. The stereochemistry of the 3,4-dihydroxyproline has not yet been determined.
Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 snRNP, U4/U6.U5 snRNP, and free U6 snRNP). It binds directly to the U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. It probably also is involved in degradation of nuclear pre-mRNA by targeting them for decapping. LSM5 binds specifically to the 3'-terminal U-tract of U6 snRNA. LSM2-LSM8 probably is involved in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM5, probably in a complex that contains LSM2-LSM7 but not LSM1 or LSM8, associates with the precursor of the RNA component of RNase P (pre-P RNA) and may be involved in maturing pre-P RNA. LSM5 is required for processing of pre-tRNAs, pre-rRNAs and U3 snoRNA.
Component of the heptameric LSM1-LSM7 complex that forms a seven-membered ring structure with a doughnut shape. The LSm subunits are arranged in the order LSM1, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. Except for LSM1, where a C-terminal helix crosses the ring structure to form additional interactions with LSM3 and LSM6, each subunit interacts only with its two neighboring subunits. The LSM1-LSM7 complex interacts with PAT1; within the complex PAT1 has direct interactions with LSM2 and LSM3. Component of the heptameric LSM2-LSM8 complex that forms a seven-membered ring structure with a doughnut shape; an RNA strand can pass through the hole in the center of the ring structure. The LSm subunits are arranged in the order LSM8, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. LSM2-LSM8 associates with PAT1 and XRN1. A complex comprising LSM2-LSM7 without LSM1 or LSM8 may exist. Component of the spliceosome U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1. Interacts with PAT1.
By acetate as carbon source in the growth medium. Is inactivated by addition of glucose (catabolite inactivation).
Targeted for proteasomal degradation when cells are shifted to glucose-containing growth medium.
The isoenzyme MDH2 may function primarily in the glyoxylate cycle.
Functions as an E3 ubiquitin-protein ligase. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate.
The FYVE domain mediates phosphatidylinositol 3-phosphate binding and is necessary and sufficient for targeting to endosome and vacuole membranes.
Component of the SPC110 complex containing at least CMD1, SPC29, SPC42 and SCP110. Interacts with BBP1.
Component of the spindle pole body (SPB) required for the proper execution of spindle pole body (SPB) duplication. Links the central plaque component SPC42 to the inner plaque component SPC110.
MPS1-mediated phosphorylation at Thr-240 is required for spindle pole body duplication.
Catalytic component of the RPD3 histone deacetylase (HDAC) complexes RPD3C(L) and RPD3C(S) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression, DNA damage response, osmotic stress response and developmental events. Is involved in rDNA and telomere silencing and in double strand breaks repair. Required for both full transcription repression and activation of many genes including cell type-specific genes (STE6, TY2 and HO), cell differentiation-specific genes (SPO13), genes that respond to external signals (PHO5) and TRK2. The RPD3 complexes regulate also chromosomal replication timing.
Component of the RPD3C(L) complex composed of at least ASH1, CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6. Component of the RPD3C(S) complex composed of at least EAF3, RCO1, RPD3, SIN3, and UME1. Interacts with cyclophilins CPR1, CPR6 and CPR7, with the kinase HOG1, and with ESS1, CYC8 and HAC1.
The ESA1-RPD3 (ER) motif is common to ESA1 and RPD3 and is required for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone deacetylase (HDAC) activity.
Interacts with GRH1 (via C-terminus), probably forming a heterooligomer consisting of a GRH1 dimer and a BUG1 dimer.
Involved in ER to Golgi vesicle-mediated transport by either facilitating USO1-dependent and -independent tethering or increasing target accuracy of fusion events of COPII-coated vesicles.
Belongs to the proteasome subunit S2 family.
Present with 306000 molecules/cell in log phase SD medium.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. Interacts with NUP188.
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. POM152 is important for the de novo assembly of NPCs.
Can heterodimerize with SPM1. Interacts with KDX1 and SLT2.
May function as a transcription factor downstream of MPK1 that is subject to activation by the MPK1 mitogen-activated protein kinase pathway. Binds to the DNA sequence 5'-CTA[TA](4)TAG-3'. At least some RML1 target genes are involved in cell wall biosynthesis.
Expression is increased about 5-fold by ethanol.
Impairs growth on non-fermentable carbon sources (PubMed:11353088). Results in sensitivity to a combination of low osmolarity and high temperature (PubMed:11353088). Results also in the reduced expression of genes involved in non-fermentable carbon source utilization including MLS1, FBP1, ACO1, PCK1, ICL1, MDH2, SFC1, ADY2, GDH2, FUM1, CIT1 and CIT2, when cells were shifted from glucose to ethanol (PubMed:25673751). Leads to reduced PCK1 and FBP1 enzymatic activities (PubMed:25673751). Leads to defective mitochondrial morphology with unclear structures of the inner membrane cristae when grown in ethanol (PubMed:25673751).
Transcription factor that regulates respiratory growth and plays a critical role in stress adaptation during non-fermentative growth (PubMed:11353088, PubMed:20975739, PubMed:25673751). Binds to promoters of genes involved in non-fermentative metabolism, including processes such as gluconeogenesis (PCK1, FBP1 and MDH2), glyoxylate shunt (MLS1 and ICL1) and the tricarboxylic acid cycle (ACO1) (PubMed:25673751). Plays a role in maintaining mitochondrial morphology and function (PubMed:25673751). Also plays a role in tolerance to pH and osmotic stress, especially during the oxidative metabolism (PubMed:25673751).
Belongs to the vitamin-B12 independent methionine synthase family.
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Belongs to the glycerophosphoryl diester phosphodiesterase family.
Leads to the accumulation of phosphatidyl glycerol.
Phosphatidylglycerol phospholipase required for the removal of excess phosphatidylglycerol (PG) via a phospholipase C-type degradation mechanism.
Belongs to the tyrosyl-DNA phosphodiesterase family.
DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 3'-phosphodiester bond, giving rise to DNA with a free 3' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase I active site tyrosine residue. Hydrolyzes 3'-phosphoglycolates on protruding 3' ends on DNA double-strand breaks due to DNA damage by radiation and free radicals. Cleaves also 5' phosphotyrosyl adducts resulting from dead-end complexes between DNA and the active site tyrosine of topoisomerase II. Contributes to DNA repair after radiation damage. Acts on blunt-ended double-strand DNA breaks and on single-stranded DNA. May have low 3'exonuclease activity and may be able to remove a single nucleoside from the 3'end of DNA and RNA molecules with 3'hydroxyl groups. Has no exonuclease activity towards DNA or RNA with a 3'phosphate (By similarity).
Belongs to the PPP phosphatase family. PP-5 (PP-T) subfamily.
Expression peaks in early log phase and decreases dramatically during the stationary phase (at protein level).
Interacts (via TPR repeats) with HSP82 (via C-terminal MEEVD pentapeptide).
Protein phosphatase that specifically binds to and dephosphorylates the molecular chaperone Hsp90 (HSC82 and HSP82). Dephosphorylation positively regulates the Hsp90 chaperone machinery.
Stimulated by arachidonic acid and other unsaturated fatty acids, and by arachidoyl coenzyme A.
The TPR repeats mediate protein-protein interactions with substrate proteins, but also autoinhibit PPT1 phosphatase activity.
Throughout most of the cell cycle it forms a double ring that coincides with the septins. After the onset of mitosis, forms a ring-like structure which colocalizes with the medial actin ring. Mediates cytoskeletal rearrangements required for cytokinesis. In conjunction with the medial actin ring exhibits contraction-like action.
Although it shares weak sequence similarity with SUA7/TFIIB, displays a similar subdomain organization as SUA7/TFIIB, with a N-terminal zinc finger, a connecting region (composed of B-reader and B-linker regions), followed by 2 cyclin folds.
Component of RNA polymerase I core factor complex (CF) that acts as a SUA7/TFIIB-like factor and plays a key role in multiple steps during transcription initiation such as pre-initiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment. After binding of UAF (upstream activation factor) to an upstream element of the promoter, CF is recruited in a SPT15/TBP-dependent manner to form a pre-initiation complex.
Component of the core factor (CF) complex, which consists of RRN6, RRN7 and RRN11. The CF heterotrimer may further dimerize to form a hexamer. RRN7 interacts with RRN6, RRN11, SPT15 and RRN9.
Present with 398 molecules/cell in log phase SD medium.
Involved in spore wall assembly (PubMed:23966878). May be involved in the modulation of rDNA transcription (PubMed:19270272).
Belongs to the helicase family. IRC3 subfamily.
Interacts with the cohesin subunit IRR1. Interacts with PRP8, HEX3, NFI1, WSS1, RFC1 and YJL149W.
ABC transporter which may be involved in multidrug resistance.
Under the control of the iron homeostasis regulating AFT1 and AFT2 transcription factors. Up-regulated upon SUB2 overexpression.
Component of the origin recognition complex (ORC) composed of at least ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. Interacts with ORC6. Component of a cullin-RING ligase (CRL)-like complex composed of at least the cullin RTT101, a linker protein MMS1, and the potential substrate receptor ORC5. Interacts with RTT101 and MMS1.
Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication. This subunit is a candidate for the mediation of ATP-dependent binding of ORC to origins. May also be a substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-ORC5).
Acts as a copper chaperone, transporting copper to the Cu(A) site on the cytochrome c oxidase subunit II (COX2).
Factor for control of RNA levels of a group of leucine-specific genes.
Mediates export of peptides with molecular masses of 2100 to 600 daltons generated upon proteolysis of mitochondrial inner membrane proteins.
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Non-essential E3 ubiquitin-protein ligase that specifically catalyzes 'Lys-29'- and 'Lys-48'-linked polyubiquitin chains (By similarity). Accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (By similarity). Associates with the proteasome and promotes elongation of ubiquitin chains on substrates bound to the proteasome (PubMed:17190603). Elongation of ubiquitin chains on substrates bound to the proteasome promotes proteasomal processivity (PubMed:20008553). Also promotes ubiquitin elongation of 26S proteasome subunit RPN10 (PubMed:17190603). Involved in the stress response required to maintain cell fitness following heat-shock: acts by mediating ubiquitination of cytosolic misfolded proteins, leading to their subsequent degradation (PubMed:21983566).
E2-like enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy and nucleophagy. Acts as an E2-like enzyme that catalyzes the conjugation of ATG12 to ATG5. ATG12 conjugation to ATG5 is required for proper localization of ATG8 to the preautophagosomal structure (PAS). Likely serves as an ATG5-recognition molecule.
Forms homooligomers. Interacts with ATG7 and ATG12.
Polyol dehydrogenase that catalyzes the reversible NAD(+)-dependent oxidation of various sugar alcohols. Is active with D-sorbitol (D-glucitol) and xylitol as substrates, leading to the C2-oxidized product D-fructose and D-xylulose, respectively.
Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with MSL1.
Belongs to the U2 small nuclear ribonucleoprotein A family.
Involved in pre-mRNA splicing. Associates to U2 snRNA in a MSL1 dependent manner and is required for normal accumulation of U2 snRNA. Required for the spliceosome assembly and the efficient addition of U2 snRNP onto the pre-mRNA.
Involved in N-linked glycosylation. Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage.
Component of the inositol phosphorylceramide synthase complex composed of at least AUR1 and KEI1. Interacts (via C-terminal region) with COP1 and SEC21. Note=The interaction with AUR1 seems to occur with the full-length protein before cleavage by KEX2 since both full-length and short chains of KEI1 interact with AUR1.
Regulatory component of the inositol phosphorylceramide (ICP) synthase which catalyzes the addition of a phosphorylinositol group onto ceramide to form inositol phosphorylceramide, an essential step in sphingolipid biosynthesis. Helps the medial Golgi localization of IPC synthase in a COPI vesicle-dependent manner.
The precursor protein is cleaved into two polypeptide chains, KEI1N and KEI1C. The cleavage is performed in the Golgi apparatus by the KEX2 protease which recognizes residue Arg-135. Generation of KEX2 cleavage site may have been an accidental event in evolution without specific advantages or disadvantages in IPC synthesis.
Interacts with RHB1, IST2, TDA3 and YIF1.
V-SNARE binding protein that facilitates specific protein retrieval from a late endosome to the Golgi. Modulates the rate of arginine uptake. Involved in pH homeostasis. Required for the correct localization of IST2. May be involved in ion homeostasis together with IST2.
High-affinity manganese transporter involved in mobilizing manganese from vesicular stores iin conditions of low manganese ion concentrations.
mRNA-binding protein which stimulates mRNA decapping by DCP1 and DCP2. Involved in the regulation of expression of multiple genes involved in glycolysis and gluconeogenesis.
Belongs to the ketopantoate reductase family.
Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Regulates protein folding in the endoplasmic reticulum lumen. Probably acts as a J-protein for the Hsp70-type chaperone KAR2 by stimulating its ATP-dependent reaction cycle and initiating folding reactions. Also involved in the endoplasmic reticulum-associated degradation (ERAD) process. Cooperates with KAR2 and another J-protein JEM1 to facilitate the export of ERAD substrates to the cytoplasm by maintaining them in a translocation-competent state and preventing their aggregation in the endoplasmic reticulum lumen.
Acts in signal transduction. Activates RHO1.
Sequentially removes both fatty acyl groups from diacylglycerophospholipids and therefore has both phospholipase B and lysophospholipase activities. It also displays transacylase activity. Substrate preference is phosphatidylserine > phosphatidylinositol >> phosphatidylcholine > phosphatidylethanolamine (PubMed:10497163, PubMed:8051052). The substrate specificity is pH- and ion-dependent. In contrast with activities observed at optimum pH 3.5, the order of substrate preference at pH 5.5 is phosphatidylcholine = phosphatidylethanolamine >> phosphatidylinositol. Degrades predominantly phosphatidylcholine and to some extent phosphatidylinositol in vivo (PubMed:15588231).
Phosphorylation results in the activation of the kinase activity.
Component of several multiprotein Golgi SNARE complexes. Identified in a Golgi SNARE complex consisting of t-SNARES SED5, YKT6, and the v-SNARE SFT1. Interacts with BET1. Interacts with BOS1. Interacts with SEC22. Interacts with PEP12. Interacts with self.
Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. Rescues alpha-factor maturation defects.
Lack of late Golgi SNARE proteins, TLG1 and TLG2. Spores are temperature sensitive and fail to germinate at 37 degrees Celsius. 10 to 20% of cells possess a variety of aberrant structures, including fragmentation of the vacuole, a common occurrence in secretory defects, and substantial accumulation of membranes in some cells. These structures are considered to be abnormal Golgi remnants. Endoplasmic reticulum (ER) retention defective, erd phenotype, which is characterized by hypersecretion of ER-resident proteins. This results from a defect in retrograde directed vesicles. Severely compromised viability when another Golgi protein, COY1P is overexpressed. Incomplete maturation of alpha-factor via defective localization of KEX2.
Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type I sub-subfamily.
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (PubMed:8227017, PubMed:8407984, PubMed:17976194, PubMed:23124206, PubMed:25829489, PubMed:29290583). Phosphatidylethanolamine formed in the mitochondria is exported to other membranes to fullfill their requirements for PtdEtn (PubMed:8530379, PubMed:11294902, PubMed:29290583). Required for normal mitochondrial morphology and proper mitochondrial fusion during yeast mating (PubMed:23045528). Involved in lipid droplet biogenesis at the endoplasmic reticulum membrane (PubMed:34818062). Required for induction of mitophagy during nitrogen starvation (PubMed:30510114). Appears to play a specific role in supporting respiratory complex III activity (PubMed:30926815).
Functional localization of the protein to the endoplasmic reticulum (ER) has been disputed. ER-localization of the enzyme may be difficult to detect in nutrient-rich or respiratory-demanding growth conditions.
Glycosylated at Asn-34 in the endoplasmic reticulum.
Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme (PubMed:25829489, PubMed:30858161). The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase (By similarity).
The cellular level of phosphatidylethanolamine is decreased, and phosphatidylcholine levels are increased (PubMed:9294443, PubMed:24146988, PubMed:30926815). Decreases induction of mitophagy in nitrogen starvation following growth on a respiratory carbon source; recruitment of ATG8 to mitochondria is impaired (PubMed:30510114). Growth on non-fermentable carbon sources is severely decreased (lactate, ethanol and glycerol) (PubMed:24146988, PubMed:34818062, PubMed:30926815). Growth on the fermentable carbon source galactose is severely decreased (PubMed:28473294). Increases RNA level of genes involved in transport, generation of precursor metabolites and energy, carbohydrate metabolism, and stress responses (PubMed:24146988). Leads to respiratory defects; respiratory complex III and IV activity is impaired (PubMed:30926815). Simultaneous disruption of PSD2 exacerbates respiratory defects (PubMed:30926815).
The precursor is imported via the TOM complex into mitochondria, where the N-terminal presequence is cleaved by the matrix-located proteases MPP (MAS1-MAS2) and OCT1.
Associates with the SNF1 kinase complex. Interacts with SNF1 and REG1.
Serine/threonine-protein kinase that phosphorylates SNF1, the catalytic subunit of the SNF1 kinase complex. Acts as an activator of the SNF1 kinase complex and controls its nuclear localization upon glucose and nitrogen depletion. Also required for SNF1 kinase activation under other stress conditions like alkaline pH or presence of cadmium.
The kinase domain is not sufficient by themself for proper function and that the non-conserved N-terminal and C-terminal domains are critical for the biological activity. The C-terminus promotes interaction of ELM1 and TOS3 kinases with SNF1.
Involved in the transport of siderophore enterobactin and so has a role in iron homeostasis.
Acts as a chaperone during the assembly of the 26S proteasome, specifically of the 19S regulatory complex (RC) and appears to have an overlapping role with RPN14.
Interacts with MCD4; CSF1 channels phosphatidylethanolamine to MCD4 in the endoplasmic reticulum at contact sites to support GPI anchor biosynthesis.
Tube-forming lipid transport protein which provides phosphatidylethanolamine for glycosylphosphatidylinositol (GPI) anchor synthesis in the endoplasmic reticulum (PubMed:35015055). Required for the glucose and other nutrients uptake at low temperature (PubMed:10781556).
Plays a general regulatory role in the cyclic AMP-dependent protein kinase-stimulated (PKA) signal transduction pathway by regulating the expression of genes important in growth and development. May inhibit the switch from unicellular to filamentous growth.
Negatively regulates the high-osmolarity glycerol (HOG) pathway through its negative regulation of the HOG1 kinase activity. Mediates the binding between the PTC1 phosphatase and the PBS2 MAP/ERK kinase (MEK). With PTC1, regulates endoplasmic reticulum inheritance through the cell wall integrity (CWI) MAPK pathway by modulating the MAPK, SLT2.
Catalyzes the reversible oxidation of (R)-2-hydroxyglutarate to 2-oxoglutarate coupled to reduction of pyruvate to (R)-lactate. Can also use oxaloacetate as electron acceptor instead of pyruvate producing (R)-malate.
Putative cysteine synthase that catalyzes the conversion of O-acetyl-L-serine (OAS) into cysteine, the last step in the cysteine biosynthesis pathway. However, this CS-like protein is unlikely to function in cysteine biosynthesis. It seems that in S.cerevisiae cysteine biosynthesis occurs exclusively through the cystathionine pathway and not via direct incorporation of sulfur into OAS.
Possesses omega-amidase activity (PubMed:28373563). The role of omega-amidase is to remove potentially toxic intermediates by converting 2-oxoglutaramate and 2-oxosuccinamate to biologically useful 2-oxoglutarate and oxaloacetate, respectively.
S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Probably methylates N-4 position of wybutosine-86 to produce wybutosine-72.
Required for synthesis of the major beta-glucans of the yeast cell wall.
Also catalyzes the conversion of 5-fluorocytosine (5FC) to 5-fluorouracil (5FU); this activity allows the formation of a cytotoxic chemotherapeutic agent from a non-cytotoxic precursor. yCD/5FC is one of the most widely used enzyme/prodrug combinations for gene-directed enzyme prodrug therapy (GDEPT) for the treatment of cancers. 5FU is an anticancer drug used to treat breast, colon, rectal, stomach, and pancreatic cancers, and is the drug of choice for treating colorectal carcinoma. However, the drug has high gastrointestinal and hematological toxicities. In contrast, the prodrug 5FC is fairly non-toxic to human, because of the lack of CD activity in human cells. By producing 5FU in the tumor, the CD/5FC system minimizes the undesired toxic effects of 5FU.
Catalyzes the hydrolytic deamination of cytosine to uracil or 5-methylcytosine to thymine. Is involved in the pyrimidine salvage pathway, which allows the cell to utilize cytosine for pyrimidine nucleotide synthesis.
Present with 5180 molecules/cell in log phase SD medium.
Multidrug resistance transporter involved in resistance and adaptation to quinidine and to the herbicide barban (4-chloro-2-butynyl [3-chlorophenyl] carbamate). Implicated in potassium uptake.
Belongs to the TRAFAC class YlqF/YawG GTPase family. NOG2 subfamily.
GTPase that associates with pre-60S ribosomal subunits in the nucleolus and is required for their nuclear export and maturation.
Present with 67700 molecules/cell in log phase SD medium.
Component of the DSC E3 ubiquitin ligase complexes that tag proteins present in Golgi, endosome and vacuole membranes and function in protein homeostasis under non-stress conditions and support a role in protein quality control (PubMed:25078903, PubMed:29355480). Involved in endocytic protein trafficking (PubMed:21777356).
C-24(28) sterol reductase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:8125337, PubMed:10722850, PubMed:12882006). ERG4 Catalyzes the last step of ergosterol biosynthesis by converting ergosta-5,7,22,24(28)-tetraen-3beta-ol into ergosterol (PubMed:10722850, PubMed:12882006). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672).
Leads to pleiotropic defects such as hypersensitivity to divalent cations and a number of drugs such as cycloheximide, miconazole, 4-nitroquinoline, fluconazole, and sodium dodecyl sulfate (PubMed:10722850). Leads also to sensitivity to the Golgi-destabilizing drug brefeldin A (PubMed:10722850).
Was originally thought to be a transport protein.
Alanine:glyoxylate aminotransferase activity is reduced by 98% relative to wild-type.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family.
Has alanine:glyoxylate aminotransferase activity.
Present with 339 molecules/cell in log phase SD medium. Expression levels higher in stationary phase than in exponential growth phase when grown in complex medium with glucose.
Catalyzes the oxidation of NADH generated inside the Mitochondrion.
Essential splicing protein required for U2 snRNP binding to pre-mRNA during spliceosome assembly.
Present with 1830 molecules/cell in log phase SD medium.
To mammalian SAP 145. Some, to C.elegans ZK632.11.
Involved in the pathway that organizes the prospore membrane (PSM) during sporulation.
May interact directly with ADY3. Probable component of a spindle pole body (SPB) complex composed of ADY3, SSP1, DON1, MPC54, SPO21/MPC70, NUD1 and CNM67.
Belongs to the fungal Na(+)/H(+) exchanger family.
Sodium export from cell, takes up external protons in exchange for internal sodium ions.
Belongs to the WD repeat LIS1/nudF family.
Dimerization mediated by the LisH domain may be required to activate dynein.
Positively regulates the activity of the minus-end directed microtubule motor protein dynein. Plays a central role in positioning the mitotic spindle at the bud neck during cell division. Targets cytoplasmic dynein to microtubule plus ends, thereby promoting dynein-mediated microtubule sliding along the bud cortex and consequently the movement of the mitotic spindle to the bud neck. Following plus end binding, dynein may be offloaded to the cortex by NUM1. Required for viability in the absence of the kinesin-related microtubule-dependent motor protein CIN8.
Self-associates. Interacts with NDL1. May form a complex with dynein.
Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. MET8 subfamily.
Catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme.
Specific and potent inhibitor of carboxypeptidase Y.
Catalytic component of the RPD3C(S) histone deacetylase complex responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression, DNA damage response, osmotic stress response and developmental events.
Component of the RPD3C(S) complex composed of at least EAF3, RCO1, RPD3, SIN3, and UME1.
This protein is coded in group-II intron 1 of OXI3 (COX1).
Accumulates pre-mRNA splicing intermediates.
Interacts with DBR1. Interacts with SYF1, a component of the NTC complex. Interacts with lariat-introns and lariat-intermediates.
Involved in branched RNA metabolism, modulating the turnover of lariat-intron pre-mRNAs by the lariat-debranching enzyme DBR1. Enhances the debranching activity of DBR1 in vitro.
Belongs to the Nudix hydrolase family. PCD1 subfamily.
Coenzyme A diphosphatase which mediates the cleavage of CoA into 3',5'-ADP and 4'-phosphopantetheine. Has a strong preference for oxidized CoA disulfide (CoASSCoA) as substrate. May be required to remove potentially toxic oxidized CoA disulfide to maintain the capacity for beta-oxidation of fatty acids. Can degrade 8-oxo-dGTP in vitro; however, such activity may not be relevant in vivo.
The size of the cleaved transit peptide can be of 7 or 8 residues.
Component of the HOPS complex which is composed of PEP5, VPS16, PEP3, VPS33, VPS39 and VPS41. HOPS associates with phosphoinositides and the PX domain of VAM7. Interacts with VPS41 and VAM7.
Required for vacuolar assembly. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion.
Belongs to the mitochondrion-specific ribosomal protein mL46 family.
May be directly involved in signal transduction and/or cell cycle regulation. It is necessary for maintaining growth rate or spore germination. Could show both activity toward tyrosine-protein phosphate as well as with serine-protein phosphate.
Acts late in the splicing of pre-mRNA. Mediates the release of the spliced mRNA from spliceosomes.
Belongs to the DEAD box helicase family. DEAH subfamily. DDX8/PRP22 sub-subfamily.
Belongs to the DNA polymerase delta/II small subunit family.
DNA polymerase delta is a heterotrimer of POL3, POL32 and HYS2.
Present with 626 molecules/cell in log phase SD medium.
The PAL motif is required for normal active site conformation.
GTPase activating protein of RHO3 and RHO4. Acts in concert with MID2 in cell integrity, which is functionally linked to the PKC pathway. Involved in various stress responses. Required at low pH for activation of the PKC pathway. Important during mating response.
Induced by stress including low pH, heat shock and oxidative shock. Basal and acid-stressed expression level is regulated by transcription factors MSN2 and MSN4 as well as the HOG pathway.
Lack of RGD1 diminishes the PKC pathway activity.
Phosphorylated in vivo. In vitro, phosphorylated by IPL1.
Alpha subunit of the heterotrimeric guanine nucleotide-binding protein (G protein) involved in glucose-induced cAMP signaling. Binds to its cognate transmembrane receptor GPR1, which senses extracellular carbon sources, and activates cAMP-PKA signaling and governs diploid pseudohyphal differentiation and haploid invasive growth. The G protein beta-mimic proteins GPB1 and GPB2 inhibit GPA2-GPR1 coupling, probably to reduce signaling in the absence of glucose.
Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by the G protein coupled receptor (GPCR) GPR1, which serves as a guanine nucleotide-exchange factor (GEF), and inactivated by RGS2, acting as a GTPase-activating protein (GAP) for GPA2.
G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. GPA2 interacts with the kelch repeat beta-mimic proteins GPB1 and GPB2 and with the gamma subunit GPG1. Interacts with the G protein coupled receptor GPR1. Interacts also with regulators of G protein signaling (RGS) protein RGS2.
Myristoylation at Gly-2 and palmitoylation at Cys-4 are required for membrane localization and function of the protein.
Present with 4570 molecules/cell in log phase SD medium.
Component of the GIN4 complex composed of at least BNI5, CDC3, CDC10, CDC11, CDC12, GIN4, NAP1 and SHS1 which forms a ring at the bud neck.
Serine/threonine-protein kinase which regulates the localization and the function of the septins during mitosis. Phosphorylates SHS1.
Belongs to the ribose 5-phosphate isomerase family.
Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit APL3 and beta-type subunit APL1), a medium chain (mu-type subunit APM4) and a small adaptin (sigma-type subunit APS2). Interacts with APL1.
Belongs to the galactose-1-phosphate uridylyltransferase type 1 family.
Binds 1 zinc ion per subunit. Zinc binding seems to play a structural role.
Component of the PI(3,5)P2 regulatory complex, composed of ATG18, FIG4, FAB1, VAC14 and VAC7. VAC14 nucleates the assembly of the complex and serves as a scaffold. Interacts with ATG2, ATG9 and VAC17. The ATG2-ATG18 complex is essential for autophagosome formation.
The 377 first amino acids might form a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2), leading to the association of the protein to the membrane. Association to the membrane can also occur through binding to phosphatidylinositol 3-monophosphate (PI3P).
The L/FRRG motif is essential for the cytoplasm to vacuole transport (Cvt) pathway, for the recruitment of ATG8 and ATG16 to the PAS in nutrient-rich medium, and for its recruitment to and dissociation from the PAS under starvation conditions.
The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). May negatively regulate FAB1 activity by sequestering or masking VAC7 from FAB1. Necessary for proper vacuole morphology. Plays an important role in osmotically-induced vacuole fragmentation. Required for cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy and starvation-induced autophagy. Involved in correct ATG9 trafficking to the pre-autophagosomal structure. Might also be involved in premeiotic DNA replication. With ATG2, protects ATG8 from ATG4-mediated cleavage.
Belongs to the ketol-acid reductoisomerase family.
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes the second common step in the parallel biosynthesis of isoleucine and valine. Converts alpha-aceto-alpha-hydroxybutyrate (AHB) to alpha,beta-dihydroxy-beta-methylvalerate (DHMV) and alpha-acetolactate (AL) to alpha,beta-dihydroxy-isovalerate (DHV) in isoleucine and valine biosynthesis, respectively.
Present with 883000 molecules/cell in log phase SD medium.
Associates with PAG1/TAO3 and interacts with MOB2.
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. COT1 subfamily.
Protein kinase that seems to play a role in the regulation of cell morphogenesis and proliferation.
Catalyzes the production of acetyl-CoA. Provides the acetyl-CoA source for histone acetylation in the nucleus. 'Anaerobic' isozyme of acetyl-coenzyme A synthetase, which is required for growth on fermentable carbon sources such as glucose. May be involved in the PDH (pyruvate dehydrogenase complex) bypass.
Present with 9020 molecules/cell in log phase SD medium.
Involved in the catabolism of quinolinic acid (QA).
Involved in DNA mismatch repair (MMR), correcting insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of a MutL heterodimer with MLH1, which probably forms a ternary complex with the MutSbeta heterodimer that initially recognizes the DNA mismatches. This complex is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Plays a role in the repair of heteroduplex sites present in meiotic recombination intermediates and is involved in maintaining the genetic stability of simple sequence repeats by correction of frameshift intermediates.
Present with 72 molecules/cell in log phase SD medium.
Belongs to the mediator complex subunit 3 family.
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. PGD1/MED3 is also involved in direct repeat recombination.
Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. PGD1/MED3 interacts directly with the CYC8-TUP1 corepressor proteins.
Belongs to the importin beta family. Importin beta-1 subfamily.
Binds to nucleoporin FxFG but not GLFG repeat regions. Ran-GTP can disrupt the importin alpha/beta heterodimer by binding to the beta subunit and releases both subunits from the docking site.
Forms a complex with the importin alpha subunit (SRP1/KAP60) (PubMed:7622450). Interacts with Ran (GSP1); interacts specifically with the GTP-bound form of Ran (GTP-Ran), protecting it from GTP hydrolysis and nucleotide exchange (PubMed:8621381, PubMed:9321403). Interacts with nucleoporin NUP1 (PubMed:8521485, PubMed:15878174).
Importin beta subunit that functions in nuclear protein import through association with the importin alpha subunit, which binds to the classical nuclear localization signal (cNLS) in cargo substrates (PubMed:7622450). Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by importin beta through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:8521485). At the nucleoplasmic side of the NPC, GTP-Ran binds to importin beta and the three components separate, leading to release of the cargo (PubMed:15864302). Importin alpha and beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin beta. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:11423015). Mediates the nuclear import of histones H2A and H2B (PubMed:11309407). Mediates the nuclear import of transcription factor GCN4 (PubMed:14648200).
The stoichiometric complex between importin beta and Ran-GTP renders the latter inaccessible to Ran-specific GTPase activating protein (Ran-GAP) thereby inhibiting GTP hydrolysis stimulated by Ran-GAP.
Antagonizes telomeric silencing in yeast. May recruit SIR4 to non-telomeric sites or repression.
Homotetramer. Interacts with SIR4 N-terminal domain. Interacts with a complex composed of SIN3 and RPD3. Identified in the Set3C complex with HOS2, HST1, SNT1, CPR1, HOS4/YIL112W and SET3.
The LisH domain mediates tetramerization and interaction with SNT1.
Adaptor protein complex 3 (AP-3) is a heterotetramer composed of 2 large adaptins (APL5 and APL6), a medium adaptin (APM3) and a small adaptin (APS3). Interacts with VPS41.
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Involved in ammonia regulation of the GAP1 permease.
Adrenodoxin reductase transfers electrons from NADPH to adrenodoxin, which subsequently donates them to the cytochrome P450 forms.
Belongs to the ferredoxin--NADP reductase type 1 family.
Lethality in aerobic growth conditions and also during fermentation.
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 10 subunits. The complex is composed of 3 respiratory subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10 (PubMed:30598554). The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a monomer or a dimer of cytochrome c oxidase (complex IV, CIV), resulting in 2 different assemblies (supercomplexes III(2)IV and III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556, PubMed:30598554). QCR10 interacts with CYT1, QCR9 and RIP1 on the intermembrane space (IMS) and with COR2 and QCR7 on the matrix side (PubMed:30598556, PubMed:30598554).
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (Probable). QCR10 has a role in CIII assembly and RIP1 stability (PubMed:8175712, PubMed:30598556, PubMed:30598554).
Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (RPB1). This promotes the activity of RNA polymerase II.
Component of the RAVE complex composed of RAV1, RAV2 and CBF3D/SKP1. Within the complex, it interacts directly with RAV2 and CBF3D. Interacts with the V-ATPase V1 subunits VMA1, VMA2 and VMA8.
Component of the RAVE complex, which is required for stable assembly of the vacuolar ATPase complex V-ATPase under many conditions. Required for transport between the early endosome and the late endosome/prevacuolar compartment (PVC), suggesting that assembly of vacuolar ATPase at the early endosome is required for transport from the early endosome to the PVC.
Found in a nuclear export complex with RanGTP, exportin and pre-miRNA (By similarity). Forms a complex with YRB1. Interacts with BUD5, CEX1, RRP12, SRM1, and DIS3/RRP44.
GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Essential for cell viability. By analogy with Ras, Ran may be activated when GTP is exchanged for bound GDP by RCC1 and inactivated when GTP is hydrolyzed by Ran upon activation by RanGAP1.
Positive regulator of allophanate-induced genes in S.cerevisiae.
Central component in the thioredoxin system. Reduces thioredoxins 1 and 2.
Present with 292000 molecules/cell in log phase SD medium.
Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole.
Palmitoylated on one or more of its N-terminal cysteine residues by PFA3, which is required for vacuole fusion.
Interacts with NOP1. Binds to the 35S pre-rRNA and the U3 snoRNA.
Involved in pre-rRNA processing. Required for maintaining steady-state levels of 40S ribosomal subunit. Required for the initial processing of pre-rRNA at the A0 to A2 sites, leading to the processing of the 23S pre-rRNA intermediate to the 18S rRNA.
By oxygen at the level of transcription through heme (PubMed:2546055). Expression drops rapidly when the oxygen concentration falls below 0.5 uM O(2) (PubMed:9169434).
Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of 12 subunits. The complex is composed of a catalytic core of 3 subunits COX1, COX2 and COX3, encoded in the mitochondrial DNA, and 9 supernumerary subunits COX4, COX5A (or COX5B), COX6, COX7, COX8, COX9, COX12, COX13 and COX26, which are encoded in the nuclear genome (PubMed:7851399, PubMed:30598556, PubMed:30598554). COX5A is the predominant subunit V during aerobic/normoxic growth, it gets replaced by COX5B under anaerobic/hypoxic conditions (PubMed:2546055). The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a dimer of ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), resulting in 2 different assemblies (supercomplexes III(2)IV and III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556, PubMed:30598554). COX5A interacts with COR1, CYT1 and QCR6 at the CIII-CIV interface (PubMed:30598556, PubMed:30598554).
PHB1 subunits are targeted to mitochondria by an unconventional non-cleavable targeting sequence present at their N-terminus.
Present with 9690 molecules/cell in log phase SD medium.
Prohibitin probably acts as a holdase/unfoldase for the stabilization of newly synthesized mitochondrial proteins. Has an antiproliferative activity. Regulates replicative life span.
Catalytic activity is inactivated under iron-limiting conditions.
Dihydroxyacid dehydratase that catalyzes the third step in the common pathway leading to biosynthesis of branched-chain amino acids (PubMed:20008079, PubMed:21798060, PubMed:21987576, PubMed:22954227, PubMed:25280745, PubMed:26543501, PubMed:27532773, PubMed:28505306, PubMed:31303893, PubMed:30850698, PubMed:33620449, PubMed:8299945). Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively (PubMed:27532773, PubMed:20008079). Required for the synthesis of alpha-isopropylmalate which modulates the activity of LEU3 and subsequently regulates the expression of LEU1 (PubMed:20008079).
Expression is significantly repressed when the pH changes from pH 5.0 to 3.0.
Present with 171000 molecules/cell in log phase SD medium.
Strongly reduces the iron responsiveness of expression of LEU1 by affecting the synthesis of alpha-isopropylmalate.
The branched chain alcohol isobutanol exhibits superior physicochemical properties as an alternative biofuel (PubMed:21798060, PubMed:22954227, PubMed:25280745, PubMed:26543501, PubMed:28505306, PubMed:31303893, PubMed:30850698). Overexpression of isobutanol pathway enzymes such as ILV3 can enhance production of alcohol precursors and are of great interest for biofuel production (PubMed:21798060, PubMed:22954227, PubMed:25280745, PubMed:26543501, PubMed:28505306, PubMed:31303893, PubMed:30850698).
It is required for meiosis I chromosome division during sporulation. A component of the FEAR (CDC14 early anaphase release) network which promotes CDC14 release from the nucleolus during early anaphase.
Its negative tail is functionally important.
Catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol.
Cytosolic aldehyde dehydrogenase which utilizes NADP(+) as the preferred coenzyme. Performs the conversion of acetaldehyde to acetate.
Present with 135000 molecules/cell in log phase SD medium.
The activity is stimulated two- to fourfold by divalent cations but is unaffected by K(+) ions.
Component of a microsomal membrane bound long-chain fatty acid elongation system, which produces the 20-26-carbon very long-chain fatty acids (VLCFA) from long-chain fatty acid precursors and is involved ceramide and inositol sphingolipid biosynthesis. Component of elongase III, which synthesizes 20-26-carbon fatty acids from 18-carbon-fatty acyl-CoA primers such as stearoyl-CoA by incorporation of malonyl-CoA (PubMed:9211877, PubMed:12684876). The enzymes active site faces the cytosol, whereas VLCFA length is determined by a lysine near the luminal end of transmembrane helix 6 (PubMed:17719544). Plays an important role in lipotoxic cell death induced by oleic acid through maintaining a balanced fatty acid composition in thr plasma membrane (PubMed:29458843). Affects plasma membrane H(+)-ATPase activity. May act on a glucose-signaling pathway that controls the expression of several genes that are transcriptionally regulated by glucose such as PMA1, HXT3 and SNF3 (PubMed:8027068).
The C-terminal di-lysine motifs may confer endoplasmic reticulum localization.
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins (PubMed:18625724, PubMed:19194512, PubMed:20802492, PubMed:21902732, PubMed:31040179). Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the FAD- and FMN-containing protein TAH18 (PubMed:20802492). TAH18-DRE2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit RNR2 (PubMed:21931161, PubMed:24733891). Has anti-apoptotic effects in the cell. Involved in negative control of H(2)O(2)-induced cell death (PubMed:19194512).
In the presence of oxygen, the A site-bound [2Fe-2S] cluster is labile and the B site-bound [4Fe-4S] cluster is readily converted into a [2Fe-2S] cluster, a reason why recombinant protein is often isolated with a single [2Fe-2S] cluster.
Inviable (PubMed:18625724). Decreases cytosolic iron-sulfur (Fe-S) protein assembly (PubMed:31040179).
Monomer (By similarity). Interacts with TAH18 (PubMed:19194512, PubMed:21902732). Interacts with MIA40 (PubMed:21700214).
The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine (PubMed:22487307). It is required for correct assembly of the 2 Fe-S clusters (ECO:0000255|HAMAP-Rule:MF_03115, PubMed:27166425).
The twin Cx2C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space.
Involved in 7-aminocholesterol resistance.
GTPase-activating protein for the ADP ribosylation factor family.
Belongs to the glycosyl hydrolase 28 family.
Involved in transport of isoleucine, leucine, valine, cysteine, methionine, phenylalanine, tyrosine and tryptophan.
Involved in the control of mitotic chromosome transmission. Required during cell division for faithful partitioning of the ER-nuclear envelope membranes which, in S.cerevisiae, enclose the duplicated chromosomes.
Involved in regulation of translation and mRNA degradation. Represses translation by binding the eIF4G subunit (TIF4631 or TIF4632) of the eIF4F complex dependent on its RGG domain, forming an mRNP repressed for translation initiation.
Abolishes recruitment of the mediator complex to the upstream activating sequence (UAS) of amino-acid starvation responsive genes (PubMed:19940160). Decreases RNA level of genes involved in amino acid biosynthesis and cofactor biosynthesis during amino acid starvation or methyl methanesulfonate stress (PubMed:11390663, PubMed:8336737, PubMed:29628310). Growth dependent on amino acid supplementation (PubMed:10733573). Sensitive to amino acid starvation (PubMed:10549298). Sensitive to purine starvation (PubMed:8336737). Decreases cellular glycogen levels during glucose starvation (PubMed:10733573).
Belongs to the bZIP family. GCN4 subfamily.
Homodimer (PubMed:1473154, PubMed:3678204). Each subunit binds overlapping and non-identical half-sites that flank the central CG base-pair in the pseudo-palindromic motif 5'-ATGA[CG]TCAT-3' (PubMed:1473154, PubMed:7664107, PubMed:2204805, PubMed:3678204). Interacts with the mediator tail; the interaction with GAL11/MED15 is direct (PubMed:19940160, PubMed:9488488, PubMed:10549298). Interacts with the SAGA histone acetyltransferase complex (PubMed:19940160, PubMed:9488488, PubMed:10549298). Interacts with the SWI/SNF chromatin remodeling complex (PubMed:19940160, PubMed:10549298).
Master transcriptional regulator that mediates the response to amino acid starvation (PubMed:11390663, PubMed:29628310). Binds variations of the DNA sequence 5'-ATGA[CG]TCAT-3' in canonical nucleosome-depleted 5'-positioned promoters, and also within coding sequences and 3' non-coding regions (PubMed:29628310, PubMed:11390663, PubMed:1473154, PubMed:2277632, PubMed:1939099, PubMed:7664107, PubMed:2204805, PubMed:3678204, PubMed:3532321, PubMed:3530496). During nutrient starvation (low or poor amino acid, carbon or purine sources), it activates genes required for amino acid biosynthesis and transport, autophagy, cofactor biosynthesis and transport, mitochondrial transport, and additional downstream transcription factors (PubMed:11390663, PubMed:29628310, PubMed:8336737, PubMed:1939099, PubMed:10733573, PubMed:7862116). Activates transcription by recruiting multiple coactivators, including the mediator complex, the SAGA complex, and the SWI/SNF complex, to enable assembly of the pre-initiation complex at core promoters (PubMed:19940160, PubMed:9488488, PubMed:10549298).
Phosphorylated by the cyclin-CDK PCL5-PHO85. Phosphorylation of Thr-165 induces degradation of GCN4 by the E3 ubiquitin ligase complex SCF(Cdc4).
Residues 89 to 100 and 106 to 125 define the N-terminal activation domain (NTAD) and the central acidic activation domain (CAAD) respectively, which can function independently to promote high-level transcription of the target genes.
Translation is induced by amino acid or purine starvation, or during growth in low or poor carbon sources (PubMed:6387704, PubMed:6433345, PubMed:8336737, PubMed:10733573, PubMed:9582292). Translational repression during nutrient-rich conditions is dependent on four uORFs (upstream open reading frames) present in the 5'-UTR of the mRNA; these promote ribosome dissociation (PubMed:6387704, PubMed:6433345, PubMed:3516411, PubMed:2676723, PubMed:8336737, PubMed:9582292). Translational induction occurs in conditions reducing translation machinery efficiency, leading to ribosomes scanning over the uORFs, and increased translation of the mRNA (PubMed:1986242). The rapid translational induction is followed by transcriptional induction at later time-points, independently of the uORF sequences (PubMed:9582292).
Belongs to the iron/manganese superoxide dismutase family.
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Abolishes cellular acid trehalase activity (PubMed:7502577, PubMed:19703229). Abolishes growth on trehalose carbon source (PubMed:8647289).
Belongs to the glycosyl hydrolase 65 family.
Periplasmic acid trehalase that catalyzes hydrolysis of the disaccharide trehalose and required for growth on trehalose as carbon source (PubMed:7502577, PubMed:8647289, PubMed:19703229, PubMed:8764988). Growth on trehalose is strictly respiratory (By similarity).
The functional relevance of vacuolar localization is disputed.
Ubiquitinated in the N-terminal region; ubiquitination is not required for vacuolar targeting.
Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for the ferulic acid decarboxylase FDC1/ubiD (PubMed:25647642). The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN (By similarity). Involved in the decarboxylation of phenylacrylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives which play the role of aroma metabolites. Also involved in the degradation of the food preservative sorbic acid (2,4-hexadienoic acid) to a volatile hydrocarbon, 1,3-pentadiene. Not essential for ubiquinone synthesis (PubMed:17889824, PubMed:20471595). Can rescue Q biosynthesis in E.coli strains lacking UbiX (PubMed:17889824). Has mRNA binding activity (PubMed:20844764).
The activity of wine yeasts to decarboxylate phenylacrylic acids is one of their biological properties related to the production of phenolic off-flavors (POF) in winemaking.
Was initially thought to be a phenylacrylic acid decarboxylase (PubMed:11693915, PubMed:17766451). However, direct assays could not confirm decarboxylase activity (PubMed:12903944, PubMed:25852989). It has been shown that this enzyme synthesizes the essential cofactor for the associated decarboxylase FDC1. It is therefore thought that decarboxylation defects due to the disruption of this gene were in fact a secondary effect of inactive FDC1 decarboxylase missing its essential cofactor (PubMed:25647642).
Forms a heterodimer with NOC2. This complex may be associated with pre-ribosomal particles. Also interacts with MCM2, MCM5 and ORC1.
Required for synthesis of 60S ribosomal subunits and the transport of pre-ribosomes from the nucleoplasm to the cytoplasm. Also required for initiation of DNA replication. May function downstream of the origin recognition complex (ORC complex) in the loading of CDC6 and the minichromosome maintenance complex (MCM complex) onto chromatin during the G1 phase of the cell cycle. Essential for growth.
Belongs to the poly(A) polymerase family.
Binds 2 magnesium ions. Also active with manganese.
Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. Interacts with FIR1 and RRP6.
Polymerase component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB.
Associates with U3 snoRNP but is not its structural component. Associates with RCL1.
Belongs to the RNA 3'-terminal cyclase family. Type 2 subfamily.
Does not have cyclase activity. Plays a role in 40S-ribosomal-subunit biogenesis in the early pre-rRNA processing steps at sites A0, A1 and A2 that are required for proper maturation of the 18S RNA. Essential for viability.
Interacts with TBP and the transcription factor GCN4.
Present with 47277 molecules/cell in log phase SD medium.
Transcriptional coactivator that stimulates GCN4-dependent transcriptional activity by bridging the DNA-binding region of GCN4 and TBP (SPT15), thereby recruiting TBP to GCN4-bound promoters.
Belongs to the thymidylate synthase family.
Inhibited by 5-fluoro-2'-deoxyuridine 5'-monophosphate (FdUMP).
Thymidylate synthase required for de novo biosynthesis of pyrimidine deoxyribonucleotides. Required for both nuclear and mitochondrial DNA synthesis.
Transcribed in a periodic manner during the cell cycle with maximal mRNA levels occurring just prior to the onset of DNA replication. The promoter contains 8-base-pair motifs (ACGCGTNA) called the MluI cell-cycle boxes (MCBs), which mediate transcription regulation by SWI6.
Present with 114000 molecules/cell in log phase SD medium.
Required for intron-independent turnover and processing of mitochondrial RNA. It is a key control element in nuclear-mitochondrial interactions.
Component of the mitochondria-localized RNase mitochondrial RNA-processing (RNase MRP) composed of one single RNA encoded by the NME1 gene and at least 31 proteins. Absent in the nucleus-localized RNase MRP (NuMRP).
Involved in spore wall assembly (PubMed:23966878). May be a component of the mitochondrial RNase MRP (MtMRP), a ribonucleoprotein endoribonuclease involved in the cleaving RNA transcripts to generate primers for DNA replication in mitochondria (PubMed:20086051). Causes growth arrest when highly overexpressed (PubMed:7762298).
Present with 8640 molecules/cell in log phase SD medium.
Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YGR027W-A ORF.
Identified in a Set3C complex with SET3, HST1, HOS2, SIF2, CPR1 and HOS4.
Part of the Set3C complex, which is required to repress early/middle sporulation genes during meiosis.
Expression is under the control of GAL4 and REB1, and is both positively controlled by galactose and negatively by glucose. Also induced by salt stress and in response to DNA replication stress.
Glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. Has mRNA binding activity.
Affects vacuolar morphology and decreases survival upon hyperosmotic stress.
Belongs to the SLC12A transporter family.
Catalyzes the coordinated symport of chloride with potassium ions across the vacuolar membrane. Involved in vacuolar osmoregulation.
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. SKI6 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation.
Was originally thought to have exonuclease activity but it was later shown (PubMed:17173052 and PubMed:17174896) that only DIS3/RRP44 subunit of the exosome core has this activity.
May be a component of a protein phosphatase type 2A (PP2A) complex. Negatively regulates SIT4 phosphatase, a modulators of caffeine sensitivity.
Cyclin-dependent protein kinase (CDK) catalytic subunit that regulates multiple cell cycle and metabolic processes in response to nutrient availability. Associates with different cyclins, that control kinase activity, substrate specificity and subcellular location of the kinase. Regulates metabolic processes when associated with PHO80 cyclin family members (PH080, PCL6, PCL7, PCL8 and PCL10), and cell cycle and morphogenesis processes when associated with PCL1,2 cyclin family members (PCL1, PCL2, CLG1, PCL5 and PCL9) (PubMed:10490639, PubMed:10692159, PubMed:11602261, PubMed:12006994, PubMed:12098764, PubMed:12101234, PubMed:12407105, PubMed:12857883, PubMed:15057567, PubMed:15082539, PubMed:15598647, PubMed:15721288, PubMed:16308562, PubMed:16455487, PubMed:3067079, PubMed:7973730, PubMed:8108735, PubMed:8539622, PubMed:9584169, PubMed:9593297, PubMed:9725902, PubMed:9843683, PubMed:12455686). When associated with PHO80, negatively regulates the expression of phosphate-starvation-responsive genes under phosphate-rich conditions (PubMed:8108735, PubMed:3067079). The PHO80-PHO85 cyclin-CDK holoenzyme phosphorylates and inactivates the transcription factor PHO4 by promoting its export to the cytoplasm (PubMed:8108735). PHO80-PHO85 phosphorylates and inactivates protein kinase RIM15 by retaining it in the cytoplasm, antagonizing RIM15-induced entry into stationary phase (PubMed:16308562). PHO80-PHO85 also phosphorylates and inactivates the calcineurin-responsive transcription factor CRZ1, linking cyclin-CDK activity to calcium signaling (PubMed:16455487). PHO80-PHO85 phosphorylates MMR1 (PubMed:12006994). Together with the cyclins PCL6/PCL7 and PCL8/PCL10, negatively controls glycogen accumulation (PubMed:10490639, PubMed:11602261, PubMed:15721288, PubMed:8539622, PubMed:9584169, PubMed:12407105). When associated with cyclins PCL6 and PCL7, controls glycogen phosphorylase and glycogen synthase activities (PubMed:11602261, PubMed:15721288, PubMed:12407105). PCL6-PHO85 and PCL7-PHO85 phosphorylate and inactivate the phosphatase PP1-2 inhibitor GLC8, causing activation of PP1-2, which then dephosphorylates and activates glycogen phosphorylase (PubMed:12407105). PCL7-PHO85 phosphorylate ALY2 (PubMed:12098764). PCL10-PHO85 phosphorylates and negatively regulates glycogen synthase GSY2 (PubMed:9584169). Association with PCL1 and PCL2 is required for cell cycle progression at start in the absence of the CDC28-dependent G1 cyclins CLN1 and CLN2 (PubMed:7973730, PubMed:7973731). PCL1-PHO85 is involved in phosphorylation of the CDK inhibitor (CKI) SIC1, which is required for its ubiquitination and degradation, releasing repression of b-type cyclins and promoting exit from mitosis (PubMed:9725902). When associated with cyclins PCL1 and PCL2, positively controls degradation of sphingoid long chain base kinase LCB4 via phosphorylation of LCB4, which is required for its ubiquitination and degradation (PubMed:15598647). PCL1-PHO85 also phosphorylates HMS1, NCP1 and NPA3, which may all have a role in mitotic exit (PubMed:15082539). PCL2-PHO85 also phosphorylates RVS167, linking cyclin-CDK activity with organization of the actin cytoskeleton (PubMed:9843683, PubMed:12857883). When associated with PCL5, positively controls degradation of transcription factor GCN4 via phosphorylation of GCN4, which is required for its degradation by the E3 ubiquitin ligase complex SCF(Cdc4) (PubMed:12455686, PubMed:12101234). When associated with PCL9, may have a role in bud site selection in G1 phase (PubMed:9593297). PHO85 also phosphorylates the transcription factor SWI5 (PubMed:10692159).
Monomer. Forms a cyclin-CDK complex with at least 10 different cyclin partners: PCL1, PCL2, PHO80, CLG1, PCL5, PCL6, PCL7, PCL8, PCL9 and PCL10. Interacts with GLC8 and RIM15.
Phosphorylation of Tyr-18 seems to be important to discriminate between the different cyclin partners for binding.
Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NDC1 may form a subcomplex with ASM4 and NUP53 at the NPC. Interactions at the SPB have not been determined.
Functions as a component of the nuclear pore complex (NPC) and the spindle pole body (SPB), probably by playing a key role in de novo assembly and insertion of both structures in the nuclear envelope. In SPB duplication NDC1 is required for the insertion of the cytoplasmic side of the SPB in the nuclear envelope, thus allowing for the assembly of the nucleoplasmic SPB side. NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors.
Involved in the lipid remodeling steps of GPI-anchor maturation. Lipid remodeling steps consist in the generation of 2 saturated fatty chains at the sn-2 position of GPI-anchors proteins. Required for phospholipase A2 activity that removes an acyl-chain at the sn-2 position of GPI-anchors during the remodeling of GPI. Required for efficient transport of GPI-anchor proteins.
Interacts with RIM15, DHH1, PBP1, PBP4 and LSM12.
Plays a role in cell wall integrity. Affects the cell wall polymer composition in the growing region of the cell.
Involved in cell cycle progression and surviving DNA damage.
High affinity transport of glutamine. Also transports Leu, Ser, Thr, Cys, Met and Asn.
Expression is induced in the late growth phase and is negatively controlled by the cAMP-dependent protein kinase A (PKA).
Participates in mitochondrial biogenesis and stress response.
In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
Alpha-1,2-mannosyltransferase, responsible for addition of the first alpha-1,2-linked mannose to form the branches on the mannan backbone of oligosaccharides.
Leads to calcium resistance and vanadate sensitivity.
Two isoenzymes, hexokinase-1 and hexokinase-2, can phosphorylate keto- and aldohexoses in yeast, whereas a third isoenzyme, GLK, is specific for aldohexoses. All glucose phosphorylating enzymes are involved in glucose uptake.
Interacts with SCC4 (PubMed:9990856, PubMed:10882066, PubMed:26038942). Interacts with the cohesin complex, which is composed of: the SMC1 and SMC3 heterodimer attached via their hinge domain, MCD1/SCC1 which link them, and IRR1/SCC3, which interacts with MCD1 (PubMed:9990856).
Phosphorylated at alternative sites Ser-43, Ser-74, Ser-162, Thr-360, Ser-1179 and Ser-1183 when the principal phosphorylation sites Thr-67, Ser-127, Ser-157, Ser-163, Thr-231, Thr-236, Ser-305 and Ser-320 are mutated to alanines.
Plays a structural role in chromatin and is involved in sister chromatid cohesion (PubMed:9990856, PubMed:14614819, PubMed:25173104, PubMed:26354421). Forms a complex with SCC4 required for the stable association of the cohesin complex with chromatin, which may act by hydrolyzing ATP from SMC1 and SMC3 heads (PubMed:10882066, PubMed:14614819). Binds to the nucleosome-free promoter regions of ribosomal protein genes and tRNA genes. Involved in transcriptional regulation by cooperating with the RSC complex to maintain nucleosome exhaustion at its binding sites (PubMed:25173104).
The N-terminus (residues 1-181) is sufficient for the interaction with SCC4 (PubMed:26038942).
Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol. Sensitive to H.mrakii HM-1 killer toxin.
Belongs to the glycosyltransferase 58 family.
Involved in positioning the proximal bud pole signal.
Heterodimer with ALG13 to form a functional enzyme.
Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER.
Intracellular phospholipase B that catalyzes the double deacylation of phosphatidylcholine (PC) to glycerophosphocholine (GroPCho). Plays an important role in membrane lipid homeostasis. Responsible for the rapid PC turnover in response to inositol, elevated temperatures, or when choline is present in the growth medium (PubMed:15044461, PubMed:15611060, PubMed:16777854). NTE1 activity impacts the repressing transcriptional activity of OPI1, the main regulator of phospholipid synthesis gene transcription (PubMed:19841481).
Positively regulated by SEC14. Inhibited by organophosphorus esters in the order phenyl saligenin phosphate (PSP) > phenyldipentyl phosphinate (PDPP) = diisopropyl fluorophosphate (DFP) > and paraoxon (PXN).
Negatively regulates early sporulation-specific genes. Seems to exert its function by positively regulating the Ras/cAMP pathway. Required for growth under alkaline conditions. Acts synergetically with PMD1.
May be involved in cellular signaling or cytoskeletal functions. May play a role in morphogenetic control.
Cleaves proteins C-terminally to mono- and paired-basic residues. Involved in the shedding of a subset of GPI-anchored plasma membrane proteins from the cell surface, including itself, GAS1 and MSB2. May also play a role in the maturation of GPI-mannoproteins associated with the cell wall. Can process the alpha-mating factor precursor. Required for cell wall integrity.
Consists of an alpha and a beta subunit, which are maintained together by a disulfide bond.
Positively regulated by cell integrity signaling through MPK1 in response to cell wall perturbation.
The zymogen is transported to the periplasm, where the propeptide is removed and the enzyme is further subjected to an internal, autocatalytic cleavage to generate an alpha/beta two-subunit endopeptidase. The proteolytic processing at the cell surface is regulated by the environmental pH.
Involved in negative regulation of fatty acid metabolism.
Can convert acyl and alkyl dihydroxyacetone-phosphate (DHAP) into glycerolipids and ether lipids, respectively. Required for the biosynthesis of phosphatidic acid via the DHAP pathway, where it reduces 1-acyl DHAP to lysophosphatidic acid (LPA) (PubMed:1512203, PubMed:10617610). Also has triacylglycerol (TAG) lipase activity. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs (PubMed:24187129). Required for spore germination (PubMed:10617610). Plays a role in cell wall biogenesis, but this effect may be indirect by affecting the activities of cell wall synthesis enzymes (PubMed:23956635). Lipolysis of TAG by AYR1 is essential for starvation-induced autophagy (PubMed:26162625). Forms an NADPH-regulated cation-selective channel in the mitochondrial outer membrane (PubMed:28916712).
Expressed during vegetative growth with a maximum level of transcription at G1 phase, after which it is decreased during the remainder of the cell cycle.
Inhibited by divalent cations and N-ethylmaleimide. Activity is reduced under anaerobic growth conditions.
Present with 3671 molecules/cell in log phase SD medium.
Reduces the activities of beta-1,3-glucan synthase and chitin synthase III, while increasing chitin synthase I and II activities. Shows altered cell wall composition as well as susceptibility towards cell wall inhibitors such as zymolyase, calcofluor white, and nikkomycin Z.
Forms a complex with LTO1; the complex bridges the interaction between the CIA complex and RLI1 (PubMed:23318452, PubMed:26182403). Interacts with RLI1 (PubMed:23318452, PubMed:26182403).
The complex LTO1:YAE1 functions as a target specific adapter that recruits apo-RLI1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery.
Involved in mRNA processing and export (PubMed:1429834, PubMed:8675010, PubMed:15542855, PubMed:19061647). Required for efficient splicing of a large set of pre-mRNAs by efficient co-transcriptional recruitment of the splicing machinery (PubMed:19061647, PubMed:23209445). Remains associated with the mRNP during early steps of translation elongation (PubMed:15542855).
Methylated by HMT1. The methylation is required for nuclear export.
Present with 78700 molecules/cell in log phase SD medium.
Interacts with MER2 and REC114. Component of the MER2-MEI4-REC114 complex.
Required for meiotic induction of recombination, viable spore production and chromosome synapsis. Component of the MER2-MEI4-REC114 complex which seems to be required for meiotic double-strand break (DSB) formation.
Has three domains each corresponding to an enzymatic activity, namely in N- to C-terminal order: ligase, kinase and cyclic phosphodiesterase (CPDase).
One of the two proteins required for the splicing of precursor tRNA molecules containing introns. The ligation activity requires three enzymatic activities: phosphorylation of the 5' terminus of the 3' half-tRNA in the presence of ATP, opening of the 2'3'-cyclic phosphodiester bond of the 5' half-tRNA leaving a 2'-phosphomonoester and ligation of the two tRNA halves in an ATP-dependent reaction.
Present with 3110 molecules/cell in log phase SD medium.
tRNA ligase is a relatively rare protein with about 400 copies per yeast cell.
Required for the proper function of SLD3 at the initiation of DNA replication. Binds to SLD3 and reduces its affinity for CDC45, a component of the replication fork. Required for mitochondrial morphology.
Component of the CFIA complex, which is composed of RNA14, RNA15, PCF11 and CLP1. Interacts directly with RNA14. Interacts with polyadenylate-binding protein PAB1.
RNA-binding component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Binds to A-rich RNA sequence elements.
Belongs to the globin family. Two-domain flavohemoproteins subfamily.
Consists of two distinct domains; a N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.
In the presence of oxygen and NADH, it has NADH oxidase activity, which leads to the generation of superoxide and H(2)O(2). Under anaerobic conditions, it also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity.
Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the fungus from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.
Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Within the SAGA complex, SUS1, SGF11, SGF73 and UBP8 form an additional subcomplex of SAGA called the DUB module (deubiquitination module). Interacts directly with SGF73, SUS1 and UBP8.
Component of the transcription regulatory histone acetylation (HAT) complex SAGA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SGF11 is involved in transcriptional regulation of a subset of SAGA-regulated genes. Within the SAGA complex, participates in a subcomplex with SUS1, SGF73 and UBP8 required for deubiquitination of H2B and for the maintenance of steady-state H3 methylation levels. It is required to recruit UBP8 and SUS1 into the SAGA complex.
The C-terminal SGF11-type zinc-finger domain together with the C-terminal catalytic domain of UBP8 forms the 'catalytic lobe' of the SAGA deubiquitination module.
The long N-terminal helix forms part of the 'assembly lobe' of the SAGA deubiquitination module.
Cell cycle-regulated with highest activity in S phase. Moderately induced by DNA-damage.
Heterotetramer of two large (R1) and two small (R2) subunits. S.cerevisiae has two different R1 subunits (RNR1 and RNR3) and two different R2 subunits (RNR2 and RNR4). The functional form of the small subunits is a RNR2-RNR4 heterodimer, where RNR2 provides the iron-radical center and RNR4 is required for proper folding of RNR2 and assembly with the large subunits. Under normal growth conditions, the active form of the large subunits is a homodimer of the constitutively expressed RNR1. In damaged cells or cells arrested for DNA synthesis, the reductase consists of multiple species because of the association of the small subunits (RNR2-RNR4) with either the RNR1 homodimer or a heterodimer of RNR1 and the damage-inducible RNR3. RNR1 interacts with the ribonucleotide reductase inhibitor SML1.
Present with 293000 molecules/cell in log phase SD medium.
Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the R1 subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site. Inhibited by SML1.
Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (PubMed:2644273, PubMed:7615509, PubMed:10206957, PubMed:11058593). Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids (By similarity).
Component of the signal peptidase complex (SPC) composed of a catalytic subunit SEC11 and three accessory subunits SPC1, SPC2 and SPC3 (PubMed:1846444, PubMed:9148931). The complex induces a local thinning of the ER membrane which is used to measure the length of the signal peptide (SP) h-region of protein substrates (By similarity). This ensures the selectivity of the complex towards h-regions shorter than 18-20 amino acids (By similarity). Interacts with SPC3 (PubMed:10206957). SPC associates with the translocon complex (PubMed:1846444, PubMed:9148931).
Leads to accumulation of core-glycosylated glycoprotein precursors.
The C-terminal short (CTS) helix is essential for catalytic activity (By similarity). It may be accommodated as a transmembrane helix in the thinned membrane environment of the complex, similarly to the signal peptide in the complex substrates (By similarity).
Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.
Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose. Although not essential, addition of ethanolamine phosphate to the second mannose plays an important role in cell separation via the GPI-based modification of daughter-specific proteins.
Originally MSC2 was identified in a screen for mutants that show an increase in meiotic unequal sister-chromatid recombination (SCR). MSC2 may also be involved in chromosome instability, rather than SRC.
Probably act as a zinc ion transporter moving zinc from the nucleus/endoplasmic reticulum to the cytoplasm. Involved in zinc ion homeostasis and cellular distribution.
Protein transport. Might participate in post-Golgi transport.
Consists of an RNA moiety (RPM1) and the protein component (RPM2). Both are necessary for full enzymatic activity.
Ribonuclease P generates mature tRNA molecules by cleaving their 5'-ends.
ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (PubMed:2167309). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity).
Present with 6700 molecules/cell in log phase SD medium.
Interacts with FHL1 to form a repressor complex. The formation of the CRF1-FHL1 complex is inhibited by the TOR pathway.
Transcription factor, corepressor with FHL1 of ribosomal protein genes. May be involved in the blocking of the spread of silencing.
Belongs to the class I-like SAM-binding methyltransferase superfamily. METTL21 family.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono- and dimethylates elongation factor 2 (EFT1/EFT2) at 'Lys-613' and methylates elongation factor 3A (YEF3).
Involved in the regulation of lipid homeostasis in the endoplasmic reticulum, thereby impacting nuclear pore complex biogenesis and localization, and nucleocytoplasmic mRNA transport.
Activated by tyrosine and threonine phosphorylation (PubMed:9032256, PubMed:9211927, PubMed:11113180, PubMed:12455951, PubMed:12477803). Inactivated by dephosphorylation via recruitment of PTC1 to the PBS2-HOG1 complex after adaptation to osmotic stress (PubMed:14685261). PTP2 and PTP3 inactivate HOG1 by dephosphorylating Tyr-176, while the PP2Cs PTC1 and PTC2 or PTC3 dephosphorylate Thr-174 in the activation loop (PubMed:9032256, PubMed:9211927, PubMed:11113180, PubMed:12455951, PubMed:12477803).
By osmotic stress, cold stress, citric acid, and in presence of bacterial lipopolysaccharides (LPS).
Dually phosphorylated on Thr-174 and Tyr-176, which activates the enzyme.
Interacts with CDC37, HOT1, KIN28, PTP2, PTP3, RBP1, RCK2, RPD3, SIC1, SMP1 and SIN4.
Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment (PubMed:7523111, PubMed:8662716, PubMed:8943326, PubMed:10198063, PubMed:10970855, PubMed:11230135, PubMed:11796711, PubMed:12743037, PubMed:14680476, PubMed:16321140, PubMed:16896207, PubMed:17363249, PubMed:17220467, PubMed:17346711). Controls osmotic regulation of transcription via the stress response element (STRE) in promoters of target genes (PubMed:7523111, PubMed:11336700). Upon osmotic shock, associates with the SKO1-SSN6-TUP1 complex, phosphorylates SKO1, and converts it into an activator that subsequently recruits Swi/Snf and SAGA complexes (PubMed:11230135, PubMed:12086627, PubMed:17429070). Activates the SMP1 transcription factor and the RCK2 kinase, both also involved in the regulation of the expression of a subset of osmotic stress-related genes (PubMed:10805732, PubMed:12482976). Phosphorylation of HSL1 by HOG1 leads to a G2 arrest essential for cell survival at high osmolarity (PubMed:16688223). Mediates also cell-cycle arrest in G1 phase by the dual targeting of SIC1 (PubMed:15448699). Regulates MFA2 ARE-mediated translation in response to carbon source (PubMed:16260593). Targets RPD3 histone deacetylase to osmoresponsive promoters to induce gene expression on stress (PubMed:14737171). Required for the Golgi apparatus localization of MNN1 (PubMed:9817752). Plays an essential role in maintaining water homeostasis, arsenite detoxification, copper-resistance, cold-resistance, hydrogen peroxide response, adaptation to citric acid stress, and repression of the mating pathway activity (PubMed:9744864, PubMed:11922108, PubMed:11136466, PubMed:15177185, PubMed:15060153, PubMed:15773992, PubMed:16920868, PubMed:16371351, PubMed:16790423, PubMed:16885417, PubMed:16857590). Functions as an arsenic sensor and effector via direct binding to arsenic and subsequent phosphorylation of the ARR1 transcription factor (PubMed:31772124).
Present with 29600 molecules/cell in log phase SD medium.
ATP-dependent rRNA helicase required for pre-ribosomal RNA processing. Involved in the maturation of the 35S-pre-rRNA and to its cleavage to mature 18S rRNA.
ATPase activity is stimulated upon the addition of RNA.
Belongs to the DEAD box helicase family. DDX47/RRP3 subfamily.
Leads to improper processing of 35S precursor rRNA.
Required for replication fork blocking activity at the replication fork barrier (RFB) site in rDNA and for recombination hot-spot (HOT1) activity, regulating the recombination rate and the number of rDNA copies. Binds directly to two separated sequences in the RFB.
Plays a central role both in proteasomal degradation of misfolded proteins and DNA repair. Central component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol. Involved in DNA excision repair. May play a part in DNA damage recognition and/or in altering chromatin structure to allow access by damage-processing enzymes.
Decreases acetylation of histone H3 'Lys-9' and 'Lys-23' (PubMed:19172748). Simultaneous disruption of GCN5 abolishes acetylation of histone H3 'Lys-9' and 'Lys-27' (PubMed:21256037). Abnormal protein sorting to vacuole (PubMed:12134085).
Histone chaperone which acts as a cofactor stimulating histone H3 acetylation by RTT109 (PubMed:21256037, PubMed:17320445, PubMed:31387991, PubMed:29300933, PubMed:19172748). Preferentially stimulates histone H3 'Lys-9' acetylation by RTT109 (PubMed:21256037, PubMed:31387991, PubMed:29300933). May also stimulate histone H3 'Lys-56' acetylation by RTT109 (PubMed:17320445). Assembles nucleosomes (in vitro) (PubMed:19172748).
Homodimer (PubMed:31387991, PubMed:21256037, PubMed:21454705, PubMed:19172748). Homotetramer (PubMed:27036862). Forms a complex with RTT109; consisting of a VPS75 dimer contacted by two RTT109 subunits (PubMed:21256037, PubMed:20560668, PubMed:17320445, PubMed:31387991, PubMed:18719104, PubMed:21454705). Interacts with RTT109; the interaction is direct (PubMed:20560668, PubMed:17272723, PubMed:17320445, PubMed:31387991, PubMed:18719104, PubMed:21256037). Interacts with ASF1 (PubMed:31387991). Interacts with histone H3/H4 heterodimers and heterotetramers via histone H3 (PubMed:31387991, PubMed:21454705, PubMed:27036862).
The C-terminal part interacts with the N-terminal part of histone H3 and promotes acetylation of histone H3 'Lys-9'.
Putative oxidoreductase that negatively regulates the retrieval of cargo from late endosomes to the Golgi. Regulates YIF1 and KEX2 localization. Required for fast DNA replication.
Belongs to the acetolactate synthase small subunit family.
Regulatory subunit of mitochondrial acetolactate synthase, which catalyzes the first of a series of common steps in the biosynthesis of the branched-chain amino acids. Stimulates activity of the acetolactate synthase catalytic subunit ILV2 seven- to tenfold and confers sensitivity to inhibition by valine and activation by ATP.
The acetolactate synthase complex contains the catalytic regulatory subunit ILV2 and the regulatory small subunit ILV6.
Present with 43800 molecules/cell in log phase SD medium.
Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:7514599, PubMed:11278748). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:11278748, PubMed:7514599). Is present only in Golgi- and endosome-residing V-ATPase complexes; enzymes containing this subunit have a 4-fold lower ratio of proton transport to ATP hydrolysis than complexes containing the vacuolar isoform and do not dissociate V1 and V0 in response to glucose depletion (PubMed:11278748, PubMed:7514599).
ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. ADO1 does not play a major role in adenine utilization in yeast. Its physiological role could primarily be to recycle adenosine produced by the methyl cycle.
Belongs to the carbohydrate kinase PfkB family.
Results in a severe reduction of adenosine kinase activity.
5' to 3' DNA replicative helicase recruited to paused replisomes to promote fork progression throughout nonhistone protein-DNA complexes, naturally occurring impediments that are encountered in each S phase where replication forks pauses. Needed for normal fork progression through over 1000 discrete sites scattered throughout the genome, like rDNA, tRNA genes, centromeres, active replication origins, or transcriptional silencers. Required for timely replication of the telomere and subtelomeric DNA and for wild-type levels of telomeric silencing. Involved in regulation of Ty1 transposition and protects the genome from instability at nascent sites of retrotransposition. Involved in DNA repair during stalled replication fork, regulation of fragile sites expression and essential for genome stability. Also plays a role in mtDNA replication. Has G-quadruplex (G4) unwinding activity and can suppress G4-induced genome instability when PIF1 levels are low.
The N-terminal part (residues 1 to 249) is essential for function and confers locus specificity.
Belongs to the adrenodoxin/putidaredoxin family.
Required for Fe-S cluster incorporation into mitochondrial and cytosolic apoproteins. May be part of a novel electron transport chain.
Probable E3 ubiquitin-protein ligase, component of the TRAMP (TRF4) complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates.
Interacts with the exosome and with the SKI complex composed of at least SKI2, SKI3 and SKI8. Interacts directly with SKI3 and SKI8.
Represses the expression of non-poly(A) mRNAs like L-A or M viruses and is therefore involved in antiviral system. Mediates interactions via its N-terminus between the exosome and the SKI complex which operate in the 3'-to-5' mRNA-decay pathway. By interacting with NAM7, is also required for nonsense-mediated 3'-to-5' mRNA-decay (NMD). May recognize a stalled 80S ribosome at the 3'-end of a nonstop mRNA which leads to the recruitment of the exosome and SKI complexes to the mRNAs to be degraded.
The N-terminal domain (residues 1 to 264) is required and sufficient for interaction with the exosome and SKI complexes and for 3'-to-5' mRNA degradation.
Alternates between an inactive form bound to GDP and an active form bound to GTP (PubMed:1910037). Activated by a guanine nucleotide-exchange factor (GEF) and inactivated by a GTPase-activating protein (GAP) (PubMed:1910037).
Ras-related protein which binds GDP/GTP and possesses intrinsic GTPase activity (PubMed:1910037). Involved in development of cell polarity during the cell division cycle, and essential for bud emergence (PubMed:2690082).
Belongs to the SAICAR synthetase family.
Catalyzes the reaction of 4-carboxy-5-aminoimidazole ribotide (CAIR) and aspartic acid with the formation of N-succinyl-5-amino-imidazole-4-carboxamide ribotide (SAICAR) in the purine biosynthesis pathway.
Involved in 3' mRNA processing. Positively regulates poly(A) synthesis.
Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
Catalyzes three sequential steps of tetrahydrofolate biosynthesis.
In the C-terminal section; belongs to the DHPS family.
In the N-terminal section; belongs to the DHNA family.
In the central section; belongs to the HPPK family.
Present with 4589 molecules/cell in log phase SD medium.
May have a role in copper and iron homeostasis.
Belongs to the terpene cyclase/mutase family.
Catalytic activity requires the presence of ERG27.
Lanosterol synthase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:1731628, PubMed:12842197, PubMed:16235265). ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core (PubMed:1731628, PubMed:12842197). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672).
Present with 2193 molecules/cell in log phase SD medium.
Belongs to the ribonuclease III family. Mitochondrion-specific ribosomal protein mL44 subfamily.
Component of the mitochondrial large ribosomal subunit (mt-LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. mL44 forms a heterodimer with mL57 and stabilizes rRNA expansion segments 1/2 at a membrane-facing protuberance close to the point of attachment of the ribosome to the translocon in the membrane.
Belongs to the protein-tyrosine phosphatase family. Non-receptor class CDC14 subfamily.
Component of the RENT (regulator of nucleolar silencing and telophase) complex which is composed of at least NET1, CDC14 and SIR2. Interacts with CDC5, CRM1, SIC1, TOF2 and UTP7.
Protein phosphatase which antagonizes mitotic cyclin-dependent kinase CDC28, the inactivation of which is essential for exit from mitosis. To access its substrates, is released from nucleolar sequestration during mitosis. Plays an essential in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint. Involved in chromosome segregation, where it is required for meiosis I spindle dissambly as well as for establishing two consecutive chromosome segregation phases. Allows damaged actomyosin rings to be maintained to facilitate completion of cell division in response to minor perturbation of the cell division machinery. Inhibits transcription of ribosomal genes (rDNA) during anaphase and controls segregation of nucleolus by facilitating condensin targeting to rDNA chromatin in anaphase. Dephosphorylates SIC1, a CDC28 inhibitor, and SWI5, a transcription factor for SIC1, and induces degradation of mitotic cyclins, likely by dephosphorylating the activator of mitotic cyclin degradation, CDH1. Dephosphorylates the microtubule bundling factor ASE1 which is required to define a centered and focused mitotic spindle midzone that can drive continuous spindle elongation. Dephosphorylates the anaphase-promoting complex inhibitor ACM1, leading to its degradation. Facilitates INN1-CYK3 complex formation which promotes cytokinesis through the dephosphorylation of CDC28-phosphosphorylated INN1. Reverts also the inhibitory CDC28 phosphorylation of CHS2 for endoplasmic reticulum export, ensuring that septum formation is contingent upon chromosome separation and exit from mitosis. Additional substrates for CDC14 are the formins BNI1 and BNR1, as well as CDC6, DBP2, DSN1, INCENP, KAR9, MCM3, ORC2, ORC6, SLD2, and SWI6. Activity is inhibited by interaction with NET1 which sequesters it to the nucleolus.
Belongs to the glycosyl hydrolase 18 family. Chitinase class V subfamily.
Chitinase is required for cell separation during growth of S.cerevisiae.
Extensively glycosylated with a series of short O-linked mannose oligosaccharides ranging in size from Man(2) to Man(5).
Belongs to the XPG/RAD2 endonuclease family. GEN subfamily.
Endonuclease which resolves Holliday junctions by the introduction of symmetrically related cuts across the junction point, to produce nicked duplex products in which the nicks can be readily ligated. Four-way DNA intermediates, also known as Holliday junctions, are formed during homologous recombination and DNA repair, and their resolution is necessary for proper chromosome segregation. Involved in DNA-damage repair in vegetative cells.
May be required for packaging pre-mRNAs into ribonucleoprotein structures amenable to efficient nuclear RNA processing. Binds to poly(A)+ RNA. Appears to act in the maintenance of CLN3 mRNA levels.
Present with 5830 molecules/cell in log phase SD medium.
DNA-binding protein that recognizes sites within both the enhancer and the promoter of rRNA transcription, as well as upstream of many genes transcribed by RNA polymerase II. It is essential for cell growth. May stimulate or inhibit transcription. Specifically recognizes the sequence 5'-CCGGGTA-3' or 5'-CGGGTRR-3' (where R is any purine). A member of the general regulatory factors (GRFs) which act as genome partitioners. Acts as a chromatin insulator which are known as STARs (Subtelomeric anti-silencing region). STARs prevent negative or positive transcription influence by extending across chromatin to a promoter.
Present with 7510 molecules/cell in log phase SD medium.
Forms a complex with ATG20 and ATG17 (PubMed:12048214). Binds also to SNC1 and SNX41 (PubMed:12554655).
Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells (PubMed:12048214, PubMed:12554655, PubMed:15800066, PubMed:17420293, PubMed:18818209, PubMed:19793921, PubMed:20729555, PubMed:20861302, PubMed:21429936, PubMed:8663607). Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and pexophagy (PubMed:12048214, PubMed:12554655, PubMed:15800066, PubMed:17420293, PubMed:18818209, PubMed:19793921, PubMed:20729555, PubMed:20861302, PubMed:21429936, PubMed:8663607). Involved in proper sorting of the v-SNARE protein SNC1 (PubMed:12554655).
The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctate structures.
Cleaved in the vicinity of position 160 to give an X-DNA-binding N-terminal subpeptide and a non-DNA-binding C-terminal subpeptide.
Cruciform DNA-binding protein which exerts an enhancing effect on the cleavage of cruciform DNA (X-DNA) by endonuclease VII from bacteriophage T4.
Belongs to the cyclophilin-type PPIase family. PPIase D subfamily.
Induced early in sporulation. Not detected during vegetative growth.
Regulates spindle pole duplication in meiosis I, but not in mitosis. Required for meiosis I, meiosis II chromosome segregation and spore formation. Binds phosphatidylinositol (4)P mono- and polyphosphates.
Belongs to the importin beta family. Importin beta-3 subfamily.
Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for classical and arginine/glycine-rich nuclear localization signals (cNLS and rg-NLS) in cargo substrates (PubMed:15367670). Its predominant cargo substrate seems to be ribosomal proteins and ribosome biogenesis trans- and cis-acting factors (PubMed:9182759, PubMed:9321403, PubMed:15367670). Required for nuclear transport of YAP1, NOP1 and SOF1 (PubMed:11274141, PubMed:15367670). Mediates the nuclear import of histones H3 and H4 (PubMed:11694505). Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins. The complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:11423015). At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo (PubMed:9321403). The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:11423015).
Interacts with Ran (GSP1); interacts specifically with the GTP-bound form of Ran (GTP-Ran), protecting it from GTP hydrolysis and nucleotide exchange (PubMed:9321403). Interacts with RPL25; this interaction is dissociated by binding to Ran-GTP (PubMed:9321403). Interacts with YAP1; this interaction is dissociated by binding to Ran-GTP (PubMed:11274141). Interacts with NOP1; via its rg-NLS (PubMed:15367670). Interacts with SOF1; via its cNLS (PubMed:15367670). Interacts with histones H3 and H4; via their NLS (PubMed:11694505). Interacts with ABF1 (PubMed:15522095).
Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. Indirectly involved in regulation of budding and haploid invasive growth.
C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of UBA4, then thiocarboxylated (-COSH) via the rhodanese domain of UBA4.
Homodimer; homodimerization may provide an autoprotection to the highly active C-terminal residue before attacking its substrates. Interacts with NCS2 and NCS6. Forms a conjugate with the target protein AHP1.
GTPase-activating protein (GAP) that most effectively accelerates the intrinsic GTPase activity of Ypt/Rab-type GTPase YPT7 involved in vacuole docking and fusion (PubMed:10091609, PubMed:11210571). It is also active, but to a lesser extent, on YPT31, YPT32, YPT1, YPT6 and SEC4 (PubMed:10091609, PubMed:11210571). Provides a catalytic arginine (arginine finger) in trans to accelerate the GTP hydrolysis rate of the substrate GTPase (Probable).
Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway. Component of an evolutionarily conserved system for ubiquitin-mediated mitochondria-associated protein degradation (MAD), which is necessary to maintain mitochondrial, cellular, and organismal viability.
Leads to progressive mitochondrial failure, hypersensitivity to oxidative stress, and decreased chronological life span.
Interacts with MSP1; leading to inhibit the translocase activity of MSP1.
Involved in peroxisome biosynthesis (PubMed:1894692). Acts as a regulator of MSP1 by inhibiting the ability of MSP1 to unfold target proteins (PubMed:32541053).
Lack of this protein causes the peroxisomal-deficient phenotype and mislocalization in the cytosol of peroxisomal matrix proteins.
Deletion of the C-terminal 34 residues abolishes ATR1 activity, while deletion of the C-terminal 23 residues have a minor effect.
Putative component of the machinery responsible for pumping aminotriazole (and possibly other toxic compounds) out of the cell. Probable ATP-dependent export permease. Appears to confer resistance only to aminotriazole.
Plays a key role in amino acid metabolism.
Component of the NDC80 complex, which consists of TID3/NDC80, NUF2, SPC24 and SPC25. The NDC80 complex is formed by two subcomplexes, TID3/NDC80-NUF2 and SPC24-SPC25, which are joined end-to-end through their coiled-coil domains. It has a rod-like structure with a length of 570 Angstroms and globular domains at either end. The TID3/NDC80-NUF2 globular domains are probably directed to microtubules, the SPC24-SPC25 globular domains to the centromere.
Component of the core factor (CF) complex, which consists of RRN6, RRN7 and RRN11. The CF heterotrimer may further dimerize to form a hexamer. RRN6 interacts with RRN7, RRN11 and RRN9.
Present with 237 molecules/cell in log phase SD medium.
Required for growth under high NaCl, alkaline pH and cell wall stress.
Heterodimer of CSH1 and CSG2, and SUR1 and CSG2.
Required for calcium regulation. May regulate calcium accumulation by a non-vacuole organelle. Also regulates the activity of CSH1 and SUR1 during mannosyl phosphorylinositol ceramide synthesis.
Component of the NatC N-terminal acetyltransferase, which catalyzes acetylation of the N-terminus Met of L-A virus Gag protein. MAK31 is necessary for the structural stability of L-A double-stranded RNA-containing particles. Necessary for growth at 37 degrees Celsius as well as for maintenance of the killer plasmid.
Present with 52700 molecules/cell in log phase SD medium.
The eukaryotic translation initiation factor 3 (eIF-3) core complex is composed of TIF32, PRT1, NIP1, TIF34 and TIF35. A subcomplex of TIF32, NIP1 and PRT1 mediates the interaction with eIF-1, TIF5/eIF-5 and HCR1. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a multifactor complex (MFC) that may bind to the 40S ribosome. TIF32, NIP1 and TIF-5/eIF-5 comprise a minimal 40S-ribosome-binding unit. TIF32 interacts with 18S ribosomal RNA and RPS0A.
Flavin-dependent enoate reductase that catalyzes the chemo- and stereoslective hydrogenation of electron-poor alkenes. The enzyme is reduced by NADPH, and oxygen, quinones, and alpha,beta-unsaturated aldehydes and ketones can act as electron acceptors to complete catalytic turnover. The physiological oxidant remains elusive (By similarity). Has a prooxidant activity, increasing reactive oxygen species (ROS) levels when overexpressed. Formation of OYE2-OYE3 heterodimers contribute to the induction of programmed cell death upon oxidative stress (PubMed:17897954).
Affects mRNA transport from the nucleus to the cytoplasm.
DnaJ-like chaperone required for the folding capacity of the endoplasmic reticulum.
Acts as component of the essential kinetochore-associated NDC80 complex, which is involved in chromosome segregation and spindle checkpoint activity.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily.
Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.
Inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the E1 alpha subunit (PDA1), thus contributing to the regulation of glucose metabolism. Also involved in telomere maintenance.
Possible microtubule-based motor that can interact or substitute with myosin 2 (MYO2).
Cell wall protein that participates directly in adhesive cell-cell interactions during yeast flocculation, a reversible, asexual and Ca(2+)-dependent process in which cells adhere to form aggregates (flocs) consisting of thousands of cells. The lectin-like protein sticks out of the cell wall of flocculent cells and selectively binds mannose residues in the cell walls of adjacent cells.
The number of the intragenic tandem repeats varies between different S.cerevisiae strains. There is a linear correlation between protein size and the extend of adhesion: the more repeats, the stronger the adhesion properties and the greater the fraction of flocculating cells (By similarity). The Ser/Thr-rich repeats are also important for proper cell wall targeting of the protein.
Functions as component of the transcription regulatory histone acetylation (HAT) complex SAGA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs).
Can transport glutamate, aspartate, glutamine, asparagine, serine, alanine and glycine.
The YXXZ (Tyr-Xaa-Xaa-Zaa, where Zaa is a hydrophobic residue) motif mediates the targeting to the lysosomal compartments.
ATP-dependent RNA helicase involved spliceosome assembly and in nuclear splicing. Catalyzes an ATP-dependent conformational change of U2 snRNP. Bridges U1 and U2 snRNPs and enables stable U2 snRNP association with intron RNA.
Belongs to the DEAD box helicase family. DDX46/PRP5 subfamily.
Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with CUS2.
mRNA splicing factors, PRP9, PRP11, and PRP21, are necessary for addition of the U2 snRNP to the pre-mRNA in an early step of spliceosome assembly.
Functions as a component of the nuclear pore complex (NPC) and the COPII coat. It is one of 5 proteins constituting the COPII coat, which is involved in anterograde (ER to Golgi) double-membrane transport vesicle formation. First the small GTPase SAR1, activated by and binding to the integral ER membrane protein SEC12, exchanges GDP for GTP and recruits the heterodimer SEC23/24, which in turn recruits the heterotetramer SEC13-SEC31. The polymerization of COPII coat complexes then causes physically the deformation (budding) of the membrane, leading to the creation of a transport vesicle. The COPII complex is dissociated upon SAR1-GTP hydrolysis to SAR1-GDP. SEC23 functions as the SAR1 GTPase activating protein, whose activity is stimulated in the presence of SEC13/31. SEC13 is directly or indirectly required for normal ER membrane and nuclear envelope morphology. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution. Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis.
The basic repeat unit of a COPII coated vesicle is composed of 5 proteins: the small GTPase SAR1, the heterodimeric SEC23-SEC24 complex, and the heterotetrameric SEC13-SEC31 complex. This repeat unit polymerizes to induce membrane deformation into a transport vesicle. Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. SEC13 is part of the heptameric 0.5 MDa autoassembling NUP84 NPC subcomplex (NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1). Component of the SEA complex composed of at least IML1/SEA1, RTC1/SEA2, MTC5/SEA3, NPR2, NPR3, SEA4, SEC13 and SEH1.
NADP-dependent alcohol dehydrogenase with a broad substrate specificity.
Present with 21700 molecules/cell in log phase SD medium.
Belongs to the transglutaminase-like superfamily. PNGase family.
Inhibited by Z-VAD-fmk, a well-known caspase inhibitor. Also inhibited by Man9GlcNAc2-iodoacetoamide. Both molecules inhibit enzyme activity through covalent binding of the carbohydrate to the single Cys-191 residue.
Interacts with RAD23 subunit of 26S proteasome.
Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins. Involved in the formation of free oligosaccharide in cytosol.
Acyl-CoA-dependent lysophosphatidic acid acyltransferase with preference for oleoyl-CoA. Involved in triacylglyceride homeostasis and lipid droplet formation. Involved in vacuolar protein sorting.
Transcription activator involved in the regulation of genes expressed in response to environmental changes and metabolic requirements. According to genome-wide promoter binding and gene expression studies it regulates, among others, genes involved in ribosome biogenesis, and protein synthesis. It may also be involved in pleiotropic drug resistance. When overexpressed it confers increased resistance to cisplatin, the DNA-alkylating agents methylmethanosulfonate, and mitomycin C, the antimalarial drugs quinidine, mefloquine, and chloroquine, and increases cellular tolerance to sodium and lithium. Preferentially binds 5'-TTACTAA-3'.
Belongs to the mitochondrion-specific ribosomal protein mS43 family.
Component of the mitochondrial small ribosomal subunit (mt-SSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. mS43 forms a dimer with mS42, building a large protuberance adjacent to the mRNA channel exit in the mt-SSU body.
Induced in activity >100-fold in response to zinc-limiting growth conditions. Not expressed in zinc-replete cells.
Implicated in yeast microtubule function.
Alternate catalytic subunit of the 1,3-beta-glucan synthase (GS) complex. Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall. Required for spore wall assembly. Negative regulation of activity by SMK1 is important for spore wall deposition. Activity is positively regulated by RHO1.
Component of the 1,3-beta-glucan synthase (GS) complex, composed of two alternate catalytic subunits FKS1 or GSC2, and a regulatory subunit RHO1. Interacts with SMK1.
Deletion leads to caspofungin resistance.
Under starvation and during sporulation. Also by pheromones and calcium in a calcineurin-dependent manner.
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. MTR3 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation.
Belongs to the NTC complex (or PRP19-associated complex), composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2, and PRP19. The NTC complex associates with the spliceosome after the release of the U1 and U4 snRNAs and forms the CWC spliceosome subcomplex (or CEF1-associated complex) reminiscent of a late-stage spliceosome composed also of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8, PRP9, PRP11, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNU114, SPP2, RSE1 and YJU2. Interacts with CEF1, CLF1, ISY1, NTC20, PRP22, PRP46 and SYF2.
Involved in pre-mRNA splicing and cell cycle control. As a component of the NTC complex (or PRP19-associated complex), associates to the spliceosome to mediate conformational rearrangement or to stabilize the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation.
Transporter required for vacuolar uptake of at least histidine and lysine.
PubMed:320000 sequence has several conflicting residues and reports microheterogeneities at additional postitions. Analysis of the sequence suggests that the sequenced protein was a mixture of at least 3 of the different isoforms of alcohol dehydrogenases found in yeast.
This isozyme preferentially catalyzes the conversion of primary unbranched alcohols to their corresponding aldehydes. Also shows activity toward secondary alcohols.
Cell wall anchoring subunit of the a-agglutinin heterodimer. S.cerevisiae a and alpha cells express the complementary cell surface glycoproteins a-agglutinin and alpha-agglutinin, respectively, which interact with one another to promote cellular aggregation during mating.
Extensively O-glycosylated by PMT1 and PMT2.
Belongs to the myo-inositol 1-phosphate synthase family.
Competitively inhibited by myo-2-inosose 1-phosphate, which is also an intermediate in the catalytic reaction (Ref.6). Competitively inhibited by 2-deoxy-myo-inositol 1-phosphate (dMIP), 1-deoxy-1-(phosphonomethyl)-myo-2-inosose (DPMI), dihydroxyacetone phosphate (DHAP), 6-deoxy-D-glucose 6-(E)-vinylhomophosphonate, 6-deoxy-D-glucitol 6-(E)-vinylhomophosphonate, 2,6-dideoxy-D-glucose 6-(E)-vinylhomophosphonate and 2,6-dideoxy-D-glucitol 6-(E)-vinylhomophosphonate (Ref.6, Ref.8). Inhibited by 2-deoxyglucitol 6-phosphate (dgtolP) (Probable).
Induced by valproate (PubMed:15576064). Repressed by inositol (PubMed:9294443, PubMed:15576064).
Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner (Ref.6, Ref.8, PubMed:23902760, PubMed:14684747). Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity).
Phosphorylation at Ser-184 and Ser-374 is associated with a decrease in activity (PubMed:23902760). Increasingly phosphorylated in presence of valproate (PubMed:23902760).
Involved in mRNA transport from nucleus to cytoplasm.
Present with 6340 molecules/cell in log phase SD medium.
Involved in the transport of siderophore ferrioxamine B and so has a role in iron homeostasis.
Belongs to the bacterial ribosomal protein bL33 family.
Component of the mitochondrial large ribosomal subunit (mt-LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. bL33m stabilizes the tRNA acceptor stem in the E-site.
Belongs to the ribonuclease III family. Mitochondrion-specific ribosomal protein mL57 subfamily.
Component of the mitochondrial large ribosomal subunit (mt-LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. mL57 forms a heterodimer with mL44 and stabilizes rRNA expansion segments 1/2 at a membrane-facing protuberance close to the point of attachment of the ribosome to the translocon in the membrane.
Present with 6500 molecules/cell in log phase SD medium.