Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O60128
data source: Provenance1
name: 40S ribosomal protein S3
name: O60128
name: P23396
name: 40S small ribosomal protein 3
xref: UnificationXref1822
feature: FragmentFeature373
cellular location: GO:0005829
comment: Reactome DB_ID: 3658757
display name: RPS3

mRNA Decay by 3' to 5' Exoribonuclease
type: Pathway
data source: Provenance1
pathway component: 3' to 5' Exoribonuclease Digestion of mRNA by the Exosome Complex
pathway component: Scavenging of the 7-methylguanosine Cap by DCPS
evidence: Evidence298
xref: UnificationXref1601
xref: RelationshipXref118
xref: UnificationXref1600
pathway order: PathwayStep291
pathway order: PathwayStep292
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10421
data source: Provenance1
name: 40S small ribosomal protein 28
name: P25112
name: 40S ribosomal protein S28
name: Q10421
xref: UnificationXref1820
feature: FragmentFeature372
cellular location: GO:0005829
comment: Reactome DB_ID: 3658749
display name: RPS28

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O13784
data source: Provenance1
name: O13784
name: P16632
name: 40S small ribosomal protein 24
name: 40S ribosomal protein S24
name: RPS24
xref: UnificationXref1817
feature: FragmentFeature371
cellular location: GO:0005829
comment: Reactome DB_ID: 3658717
display name: S19

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O59865
data source: Provenance1
name: P16632
name: 40S small ribosomal protein 24
name: O59865
name: 40S ribosomal protein S24
name: RPS24
xref: UnificationXref1815
feature: FragmentFeature370
cellular location: GO:0005829
comment: Reactome DB_ID: 3658713
display name: S19

Homologues of RPS5(1-204)
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1832
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658794

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P79009
data source: Provenance1
name: P25111
name: 40S ribosomal protein S25
name: 40S small ribosomal protein 25
name: P79009
xref: UnificationXref1826
feature: FragmentFeature375
cellular location: GO:0005829
comment: Reactome DB_ID: 3658726
display name: RPS25

O74172
type: Protein
entity reference: O74172
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: P25111
name: 40S ribosomal protein S25
name: 40S small ribosomal protein 25
xref: UnificationXref1824
feature: FragmentFeature374
cellular location: GO:0005829
comment: Reactome DB_ID: 3658722
display name: RPS25

Homologues of RPS25
type: Protein
data source: Provenance1
member physical entity: O74172
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1827
cellular location: GO:0005829
comment: Reactome DB_ID: 3658727
comment: Converted from EntitySet in Reactome

PTM: gamma carboxylation, hypusine formation and arylsulfatase activation
type: Pathway
data source: Provenance1
pathway component: REACT 31464.10
evidence: Evidence1283
xref: UnificationXref7987
xref: RelationshipXref1017
xref: UnificationXref7988
pathway order: PathwayStep1261
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Homologues of RPS24
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1818
cellular location: GO:0005829
comment: Reactome DB_ID: 3658718
comment: Converted from EntitySet in Reactome

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTQ6
data source: Provenance1
name: RIG protein
name: Q9UTQ6
name: 40S ribosomal protein S15
name: 40S small ribosomal protein 15
name: P11174
xref: UnificationXref1812
feature: FragmentFeature369
cellular location: GO:0005829
comment: Reactome DB_ID: 3658659
display name: RPS15

Stoichiometry909
type: Stoichiometry
physical entity: Protein845
stoichiometric coefficient: 1.0

Stoichiometry908
type: Stoichiometry
physical entity: alpha-ketoglutarate dehydrogenase E1 homodimer (name copied from entity in Homo sapiens)
stoichiometric coefficient: 12.0

Stoichiometry905
type: Stoichiometry
physical entity: Protein844
stoichiometric coefficient: 1.0

Stoichiometry904
type: Stoichiometry
physical entity: alpha-ketoglutarate dehydrogenase E2 holoenzyme (name copied from entity in Homo sapiens)
stoichiometric coefficient: 24.0

Stoichiometry907
type: Stoichiometry
physical entity: alpha-ketoglutarate dehydrogenase E1 holoenzyme (name copied from entity in Homo sapiens)
stoichiometric coefficient: 2.0

Stoichiometry906
type: Stoichiometry
physical entity: Thiamin diphosphate
stoichiometric coefficient: 1.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94715
data source: Provenance1
name: RIG protein
name: 40S ribosomal protein S15
name: 40S small ribosomal protein 15
name: O94715
name: P11174
xref: UnificationXref1810
feature: FragmentFeature368
cellular location: GO:0005829
comment: Reactome DB_ID: 3658655
display name: RPS15

Stoichiometry901
type: Stoichiometry
physical entity: alpha-keto acid dehydrogenase E3 homodimer (name copied from entity in Homo sapiens)
stoichiometric coefficient: 6.0

http://identifiers.org/pubmed/9809442
type: PublicationXref
id: 9809442
author: Marin-Garcia, J
author: Ananthakrishnan, R
author: Goldenthal, MJ
db: Pubmed
title: Cloning and molecular analysis of the human citrate synthase gene
source: Genome 41:733-738
year: 1998

Stoichiometry900
type: Stoichiometry
physical entity: Protein842
stoichiometric coefficient: 1.0

Stoichiometry903
type: Stoichiometry
physical entity: Lipoamide
stoichiometric coefficient: 1.0

Stoichiometry902
type: Stoichiometry
physical entity: Protein843
stoichiometric coefficient: 1.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9P7B2
data source: Provenance1
name: 40S small ribosomal protein 8
name: Q9P7B2
name: RPS8(2-208)
name: 40S ribosomal protein S8
xref: UnificationXref1796
feature: FragmentFeature363
cellular location: GO:0005829
comment: Reactome DB_ID: 3658815
display name: P09058

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14049
data source: Provenance1
name: O14049
name: 40S small ribosomal protein 8
name: RPS8(2-208)
name: 40S ribosomal protein S8
xref: UnificationXref1794
feature: FragmentFeature362
cellular location: GO:0005829
comment: Reactome DB_ID: 3658811
display name: P09058

MPS-1
type: Protein
entity reference: O74330
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: 40S small ribosomal protein 27
name: O74330
name: 40S ribosomal protein S27
name: Metallopan-stimulin 1
name: P42677
xref: UnificationXref1801
feature: FragmentFeature365
cellular location: GO:0005829
comment: Reactome DB_ID: 3658740
display name: RPS27

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74893
data source: Provenance1
name: O74893
name: P17075
name: 40S small ribosomal protein 20
name: 40S ribosomal protein S20
xref: UnificationXref1799
feature: FragmentFeature364
cellular location: GO:0005829
comment: Reactome DB_ID: 3658699
display name: RPS20

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74322
data source: Provenance1
name: 40S small ribosomal protein 12
name: O74322
name: P25398
name: 40S ribosomal protein S12
xref: UnificationXref1804
feature: FragmentFeature366
cellular location: GO:0005829
comment: Reactome DB_ID: 3658641
display name: RPS12

Homologues of RPS12
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1807
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658646

Homologues of RPS15
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1813
cellular location: GO:0005829
comment: Reactome DB_ID: 3658660
comment: Converted from EntitySet in Reactome

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14062
data source: Provenance1
name: 40S small ribosomal protein 12
name: O14062
name: P25398
name: 40S ribosomal protein S12
xref: UnificationXref1806
feature: FragmentFeature367
cellular location: GO:0005829
comment: Reactome DB_ID: 3658645
display name: RPS12

http://identifiers.org/pubmed/10676816
type: PublicationXref
id: 10676816
author: Cerione, RA
author: Nassar, N
author: Hoffman, GR
db: Pubmed
title: Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI
source: Cell 100:345-56
year: 2000

Homologues of RPS8(2-208)
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1797
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658816

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09757
data source: Provenance1
name: 40S small ribosomal protein 9
name: Q09757
name: 40S ribosomal protein S9
name: P46781
xref: UnificationXref1789
feature: FragmentFeature360
cellular location: GO:0005829
comment: Reactome DB_ID: 3658820
display name: RPS9

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O59675
data source: Provenance1
name: 40S small ribosomal protein 9
name: O59675
name: 40S ribosomal protein S9
name: P46781
xref: UnificationXref1791
feature: FragmentFeature361
cellular location: GO:0005829
comment: Reactome DB_ID: 3658824
display name: RPS9

Homologues of RPS9
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1792
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658825

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:O42952
data source: Provenance1
name: Q05472
name: 40S small ribosomal protein 30
name: 40S ribosomal protein S30
name: O42952
xref: UnificationXref1787
feature: FragmentFeature359
cellular location: GO:0005829
comment: Reactome DB_ID: 3658763
display name: FAU

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74718
data source: Provenance1
name: O74718
name: GSPT2
xref: UnificationXref1784
feature: FragmentFeature358
cellular location: GO:0005829
comment: Reactome DB_ID: 3660548
display name: eRF3

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10267
data source: Provenance1
name: hUpf3B
name: UPf3B
name: Q10267
xref: UnificationXref1780
feature: FragmentFeature357
cellular location: GO:0005829
comment: Reactome DB_ID: 3659893
display name: UPF3B

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10267
data source: Provenance1
name: Regulator of nonsense transcripts 3A
name: Q10267
name: REN3A_HUMAN
xref: UnificationXref1779
feature: FragmentFeature356
cellular location: GO:0005829
comment: Reactome DB_ID: 3663504
display name: UPF3A

UPF3
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1781
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3663505

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10055
data source: Provenance1
name: Q10055
name: Eukaryotic initiation factor 4A-III
name: IF4A3_HUMAN
xref: UnificationXref1776
feature: FragmentFeature355
cellular location: GO:0005829
comment: Reactome DB_ID: 3663497
display name: EIF4A3

http://identifiers.org/pubmed/18414735
type: PublicationXref
id: 18414735
author: Kufer, TA
db: Pubmed
title: Signal transduction pathways used by NLR-type innate immune receptors
source: Mol Biosyst 4:380-6
year: 2008

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O42847
data source: Provenance1
name: RBM8A/Y14
name: O42847
xref: UnificationXref1772
feature: FragmentFeature354
cellular location: GO:0005829
comment: Reactome DB_ID: 3659898
display name: RBM8A

http://identifiers.org/pubmed/642006
type: PublicationXref
id: 642006
author: Gall, JG
author: Blackburn, EH
db: Pubmed
title: A tandemly repeated sequence at the termini of the extrachromosomal ribosomal RNA genes in Tetrahymena
source: J Mol Biol 120:33-53
year: 1978

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O13824
data source: Provenance1
name: O13824
name: Regulator of nonsense transcripts 2
name: RENT2_HUMAN
xref: UnificationXref1766
feature: FragmentFeature351
cellular location: GO:0005829
comment: Reactome DB_ID: 3663503
display name: UPF2

Q1MTR2
type: Protein
entity reference: Q1MTR2
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1768
feature: FragmentFeature352
cellular location: GO:0005829
comment: Reactome DB_ID: 3659895
display name: RNPS1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43037
data source: Provenance1
name: magoh
name: O43037
xref: UnificationXref1770
feature: FragmentFeature353
cellular location: GO:0005829
comment: Reactome DB_ID: 3659899
display name: MAGOH

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P47979
data source: Provenance1
name: TTP_HUMAN
name: Tristetraproline
name: P47979
xref: UnificationXref1746
feature: FragmentFeature348
cellular location: GO:0005829
comment: Reactome DB_ID: 3663134
display name: ZFP36

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14089
data source: Provenance1
name: O14089
name: Transportin-1
name: Importin beta-2
xref: UnificationXref1745
feature: FragmentFeature347
cellular location: GO:0005829
comment: Reactome DB_ID: 3663126
display name: TNPO1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P79063
data source: Provenance1
name: TB3-1
name: Eukaryotic release factor 1
name: Eukaryotic peptide chain release factor subunit 1
name: C11 protein
name: eRF1
name: P79063
xref: UnificationXref1764
feature: FragmentFeature350
cellular location: GO:0005829
comment: Reactome DB_ID: 3660553
display name: ETF1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09820
data source: Provenance1
name: Q09820
name: RENT1_HUMAN
name: Regulator of nonsense transcripts 1
xref: UnificationXref1755
feature: FragmentFeature349
cellular location: GO:0005829
comment: Reactome DB_ID: 3663488
display name: UPF1

Proteasome subunit Z
type: Protein
entity reference: Q09841
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Q09841
name: Multicatalytic endopeptidase complex chain Z
name: Proteasome subunit beta type 7
name: Proteasome subunit beta type 7 precursor
name: Macropain chain Z
xref: UnificationXref1725
feature: FragmentFeature344
cellular location: GO:0005829
comment: Reactome DB_ID: 3657796
display name: PSMB7

ZFP36L1
type: Protein
entity reference: P47979
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Butyrate response factor 1
name: TISB_HUMAN
xref: UnificationXref1736
feature: FragmentFeature346
cellular location: GO:0005829
comment: Reactome DB_ID: 3663159
display name: P47979

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74894
data source: Provenance1
name: O74894
name: TBP-7
name: TAT-binding protein-7
name: MIP224
name: 26S protease regulatory subunit 6B
name: MB67 interacting protein
xref: UnificationXref1727
feature: FragmentFeature345
cellular location: GO:0005829
comment: Reactome DB_ID: 3657814
display name: PSMC4

Stoichiometry935
type: Stoichiometry
physical entity: sulfur
stoichiometric coefficient: 1.0

Stoichiometry936
type: Stoichiometry
physical entity: Protein856
stoichiometric coefficient: 2.0

Stoichiometry933
type: Stoichiometry
physical entity: Protein854
stoichiometric coefficient: 1.0

Stoichiometry934
type: Stoichiometry
physical entity: SmallMolecule209
stoichiometric coefficient: 1.0

Stoichiometry931
type: Stoichiometry
physical entity: SmallMolecule169
stoichiometric coefficient: 1.0

Stoichiometry932
type: Stoichiometry
physical entity: 5'-Adenylic acid
stoichiometric coefficient: 1.0

Stoichiometry930
type: Stoichiometry
physical entity: Protein853
stoichiometric coefficient: 1.0

RelationshipXref1102
type: RelationshipXref
id: 3664944
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664944

RelationshipXref1101
type: RelationshipXref
id: GO:0019948
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1104
type: RelationshipXref
id: 3664967
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664967

RelationshipXref1103
type: RelationshipXref
id: GO:0016740
db: GENE ONTOLOGY
relationship type: MI:0355

Stoichiometry939
type: Stoichiometry
physical entity: Complex305
stoichiometric coefficient: 2.0

RelationshipXref1100
type: RelationshipXref
id: 3664953
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664953

Stoichiometry937
type: Stoichiometry
physical entity: Complex305
stoichiometric coefficient: 2.0

Stoichiometry938
type: Stoichiometry
physical entity: Complex305
stoichiometric coefficient: 2.0

RelationshipXref1109
type: RelationshipXref
id: 3661733
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661733

RelationshipXref1105
type: RelationshipXref
id: GO:0016925
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1106
type: RelationshipXref
id: 3662941
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662941

RelationshipXref1107
type: RelationshipXref
id: GO:0007411
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1108
type: RelationshipXref
id: GO:0031018
db: GENE ONTOLOGY
relationship type: MI:0359

http://identifiers.org/pubmed/9438390
type: PublicationXref
id: 9438390
author: Webster, MK
author: Bardwell, WM
author: Meyer, AN
author: Donoghue, DJ
author: Robertson, SC
author: d'Avis, PY
db: Pubmed
title: Constitutive activation of fibroblast growth factor receptor 3 by mutations responsible for the lethal skeletal dysplasia thanatophoric dysplasia type I
source: Cell Growth Differ 9:71-8
year: 1998

Stoichiometry944
type: Stoichiometry
physical entity: Protein863
stoichiometric coefficient: 1.0

Stoichiometry945
type: Stoichiometry
physical entity: Complex312
stoichiometric coefficient: 2.0

Stoichiometry946
type: Stoichiometry
physical entity: SmallMolecule49
stoichiometric coefficient: 1.0

Stoichiometry947
type: Stoichiometry
physical entity: Protein864
stoichiometric coefficient: 1.0

Stoichiometry940
type: Stoichiometry
physical entity: Protein859
stoichiometric coefficient: 4.0

Stoichiometry941
type: Stoichiometry
physical entity: Protein860
stoichiometric coefficient: 2.0

Stoichiometry942
type: Stoichiometry
physical entity: Protein861
stoichiometric coefficient: 4.0

Stoichiometry943
type: Stoichiometry
physical entity: SmallMolecule49
stoichiometric coefficient: 1.0

RelationshipXref1113
type: RelationshipXref
id: GO:0016044
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1112
type: RelationshipXref
id: GO:0016197
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1111
type: RelationshipXref
id: GO:0006890
db: GENE ONTOLOGY
relationship type: MI:0359

Stoichiometry948
type: Stoichiometry
physical entity: Complex314
stoichiometric coefficient: 2.0

RelationshipXref1110
type: RelationshipXref
id: GO:0048205
db: GENE ONTOLOGY
relationship type: MI:0359

Stoichiometry949
type: Stoichiometry
physical entity: Protein865
stoichiometric coefficient: 1.0

http://identifiers.org/pubmed/9188485
type: PublicationXref
id: 9188485
author: Folk, JE
author: Park, MH
author: Wolff, EC
db: Pubmed
title: Enzyme-substrate intermediate formation at lysine 329 of human deoxyhypusine synthase
source: J Biol Chem 272:15865-71
year: 1997

Stoichiometry910
type: Stoichiometry
physical entity: Protein846
stoichiometric coefficient: 1.0

Stoichiometry913
type: Stoichiometry
physical entity: Flavin adenine dinucleotide
stoichiometric coefficient: 1.0

Stoichiometry914
type: Stoichiometry
physical entity: Succinate dehydrogenase flavoprotein (subunit A), oxidised (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry911
type: Stoichiometry
physical entity: PhysicalEntity138
stoichiometric coefficient: 1.0

Stoichiometry912
type: Stoichiometry
physical entity: Protein847
stoichiometric coefficient: 1.0

Stoichiometry917
type: Stoichiometry
physical entity: Succinate dehydrogenase Iron Sulphur (subunit B) (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry918
type: Stoichiometry
physical entity: Protein849
stoichiometric coefficient: 1.0

Stoichiometry915
type: Stoichiometry
physical entity: PhysicalEntity139
stoichiometric coefficient: 1.0

Stoichiometry916
type: Stoichiometry
physical entity: Protein848
stoichiometric coefficient: 1.0

Stoichiometry919
type: Stoichiometry
physical entity: Protein850
stoichiometric coefficient: 4.0

http://identifiers.org/pubmed/8541526
type: PublicationXref
id: 8541526
author: Park, JG
author: Hunter, S
author: Schreiber, AD
author: Indik, ZK
db: Pubmed
title: The molecular dissection of Fc gamma receptor mediated phagocytosis
source: Blood 86:4389-99
year: 1995

http://identifiers.org/pubmed/1371749
type: PublicationXref
id: 1371749
author: Saxty, BA
author: Groot, PH
author: Kmetz, PJ
author: Near, JC
author: Hughes, SA
author: Franklin, M
author: Wells, TN
author: Gloger, IS
author: Elshourbagy, NA
db: Pubmed
title: Cloning and expression of a human ATP-citrate lyase cDNA
source: Eur J Biochem 204:491-9
year: 1992

Stoichiometry920
type: Stoichiometry
physical entity: PhysicalEntity138
stoichiometric coefficient: 1.0

Stoichiometry921
type: Stoichiometry
physical entity: FADH2
stoichiometric coefficient: 1.0

Stoichiometry922
type: Stoichiometry
physical entity: Protein847
stoichiometric coefficient: 1.0

Stoichiometry923
type: Stoichiometry
physical entity: Complex302
stoichiometric coefficient: 1.0

Stoichiometry924
type: Stoichiometry
physical entity: Succinate dehydrogenase Iron Sulphur (subunit B) (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry925
type: Stoichiometry
physical entity: Protein849
stoichiometric coefficient: 1.0

Stoichiometry926
type: Stoichiometry
physical entity: SmallMolecule167
stoichiometric coefficient: 1.0

Stoichiometry927
type: Stoichiometry
physical entity: Protein853
stoichiometric coefficient: 1.0

Stoichiometry928
type: Stoichiometry
physical entity: 5'-Adenylic acid
stoichiometric coefficient: 1.0

Stoichiometry929
type: Stoichiometry
physical entity: Protein854
stoichiometric coefficient: 1.0

http://identifiers.org/pubmed/8631325
type: PublicationXref
id: 8631325
author: Peng, HL
author: Chao, YC
author: Chang, HY
author: Duggleby, RG
author: Huang, JG
db: Pubmed
title: Sequence differences between human muscle and liver cDNAs for UDPglucose pyrophosphorylase and kinetic properties of the recombinant enzymes expressed in Escherichia coli.
source: Eur J Biochem 235:173-9
year: 1996

Stoichiometry970
type: Stoichiometry
physical entity: SmallMolecule49
stoichiometric coefficient: 2.0

Stoichiometry971
type: Stoichiometry
physical entity: Protein876
stoichiometric coefficient: 2.0

Stoichiometry972
type: Stoichiometry
physical entity: Zn(II)
stoichiometric coefficient: 4.0

Stoichiometry978
type: Stoichiometry
physical entity: Protein884
stoichiometric coefficient: 4.0

Stoichiometry977
type: Stoichiometry
physical entity: Protein883
stoichiometric coefficient: 2.0

http://identifiers.org/pubmed/19443651
type: PublicationXref
id: 19443651
author: Wang, Jianghai
author: Fukui, Lisa
author: Lee, Brian
author: Cai, Sheng
author: Chen, Yuan
author: Hu, Weidong
db: Pubmed
title: Conformational transition associated with E1-E2 interaction in small ubiquitin-like modifications
source: J. Biol. Chem. 284:20340-8
year: 2009

Stoichiometry979
type: Stoichiometry
physical entity: Protein885
stoichiometric coefficient: 1.0

Stoichiometry974
type: Stoichiometry
physical entity: SmallMolecule31
stoichiometric coefficient: 2.0

Stoichiometry973
type: Stoichiometry
physical entity: Protein877
stoichiometric coefficient: 4.0

Stoichiometry976
type: Stoichiometry
physical entity: Protein881
stoichiometric coefficient: 2.0

Stoichiometry975
type: Stoichiometry
physical entity: SmallMolecule31
stoichiometric coefficient: 2.0

Stoichiometry982
type: Stoichiometry
physical entity: Protein886
stoichiometric coefficient: 2.0

Stoichiometry983
type: Stoichiometry
physical entity: Protein887
stoichiometric coefficient: 2.0

Stoichiometry980
type: Stoichiometry
physical entity: gamma-L-Glutamyl-L-cysteinyl-glycine
stoichiometric coefficient: 2.0

Stoichiometry981
type: Stoichiometry
physical entity: SmallMolecule189
stoichiometric coefficient: 2.0

Removal of DNA patch containing abasic residue
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction17
evidence: Evidence25
xref: UnificationXref117
xref: UnificationXref116
pathway order: PathwayStep24
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/16738315
type: PublicationXref
id: 16738315
author: Lee, Hsiang-Ying
author: Gill, Grace
author: Catic, Andre
author: Di Bacco, A
author: Ouyang, Jian
author: Ploegh, Hidde
db: Pubmed
title: The SUMO-specific protease SENP5 is required for cell division
source: Mol. Cell. Biol. 26:4489-98
year: 2006

http://identifiers.org/pubmed/19957260
type: PublicationXref
id: 19957260
author: Lambert, DM
author: Ferrer, JL
author: Bauvois, C
author: Wouters, J
author: Borel, F
author: Labar, G
db: Pubmed
title: Crystal structure of the human monoacylglycerol lipase, a key actor in endocannabinoid signaling
source: Chembiochem 11:218-27
year: 2010

6,7-dihydrobiopterin [ChEBI:20680]
type: SmallMoleculeReference
name: 6,7-dihydrobiopterin
xref: UnificationXref4967

Stoichiometry989
type: Stoichiometry
physical entity: Protein889
stoichiometric coefficient: 1.0

Stoichiometry988
type: Stoichiometry
physical entity: ferriheme
stoichiometric coefficient: 1.0

Stoichiometry987
type: Stoichiometry
physical entity: ferroheme
stoichiometric coefficient: 1.0

Stoichiometry986
type: Stoichiometry
physical entity: Protein889
stoichiometric coefficient: 1.0

Stoichiometry985
type: Stoichiometry
physical entity: Protein888
stoichiometric coefficient: 2.0

Stoichiometry984
type: Stoichiometry
physical entity: SmallMolecule49
stoichiometric coefficient: 6.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94686
data source: Provenance1
name: 60S ribosomal protein L37a
name: P12751
name: O94686
xref: UnificationXref1937
feature: FragmentFeature421
cellular location: GO:0005829
comment: Reactome DB_ID: 3659206
display name: RPL37A

Q9HGL8
type: Protein
entity reference: Q9HGL8
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: 60S ribosomal protein L37a
name: P12751
xref: UnificationXref1935
feature: FragmentFeature420
cellular location: GO:0005829
comment: Reactome DB_ID: 3659202
display name: RPL37A

Stoichiometry950
type: Stoichiometry
physical entity: SmallMolecule49
stoichiometric coefficient: 1.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O42846
data source: Provenance1
name: 60S ribosomal protein L34
name: P49207
name: O42846
xref: UnificationXref1929
feature: FragmentFeature418
cellular location: GO:0005829
comment: Reactome DB_ID: 3659170
display name: RPL34

Homologues of RPL34
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1932
cellular location: GO:0005829
comment: Reactome DB_ID: 3659175
comment: Converted from EntitySet in Reactome

Homologues of RPL37A
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
member physical entity: Q9HGL8
xref: UnificationXref1938
cellular location: GO:0005829
comment: Reactome DB_ID: 3659207
comment: Converted from EntitySet in Reactome

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9URT8
data source: Provenance1
name: 60S ribosomal protein L34
name: P49207
name: Q9URT8
xref: UnificationXref1931
feature: FragmentFeature419
cellular location: GO:0005829
comment: Reactome DB_ID: 3659174
display name: RPL34

60S ribosomal protein L35a
type: Protein
entity reference: Q9USX4
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Q9USX4
name: P18077
xref: UnificationXref1921
feature: FragmentFeature415
cellular location: GO:0005829
comment: Reactome DB_ID: 3659183
display name: RPL35A

Homologues of RPL35A
type: Protein
data source: Provenance1
member physical entity: 60S ribosomal protein L35a
xref: UnificationXref1924
cellular location: GO:0005829
comment: Reactome DB_ID: 3659188
comment: Converted from EntitySet in Reactome

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74175
data source: Provenance1
name: Breast basic conserved protein 1
name: RPL13(2-211)
name: 60S ribosomal protein L13
xref: UnificationXref1927
feature: FragmentFeature417
cellular location: GO:0005829
comment: Reactome DB_ID: 3659005
display name: O74175

60S ribosomal protein L35a
type: Protein
entity reference: Q9USG6
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Q9USG6
name: P18077
xref: UnificationXref1923
feature: FragmentFeature416
cellular location: GO:0005829
comment: Reactome DB_ID: 3659187
display name: RPL35A

http://identifiers.org/pubmed/15153069
type: PublicationXref
id: 15153069
author: Lake, S
author: Climent, I
author: Swiezewska, E
author: Forsgren, M
author: Attersand, A
author: Dallner, G
author: Grünler, J
db: Pubmed
title: Isolation and functional expression of human COQ2, a gene encoding a polyprenyl transferase involved in the synthesis of CoQ
source: Biochem J 382:519-26
year: 2004

Stoichiometry959
type: Stoichiometry
physical entity: protoheme
stoichiometric coefficient: 1.0

Stoichiometry952
type: Stoichiometry
physical entity: Protein867
stoichiometric coefficient: 3.0

Stoichiometry951
type: Stoichiometry
physical entity: Protein866
stoichiometric coefficient: 4.0

Stoichiometry954
type: Stoichiometry
physical entity: Zn(II)
stoichiometric coefficient: 2.0

2-Deoxy-D-ribose 1-phosphate
type: SmallMoleculeReference
name: 2-Deoxy-D-ribose 1-phosphate [ChEBI:28542]
xref: UnificationXref4203

Stoichiometry953
type: Stoichiometry
physical entity: Protein868
stoichiometric coefficient: 2.0

Stoichiometry956
type: Stoichiometry
physical entity: Hydrogen peroxide
stoichiometric coefficient: 2.0

Stoichiometry955
type: Stoichiometry
physical entity: Protein869
stoichiometric coefficient: 2.0

Stoichiometry958
type: Stoichiometry
physical entity: NADPH
stoichiometric coefficient: 1.0

Stoichiometry957
type: Stoichiometry
physical entity: H2O
stoichiometric coefficient: 2.0

Stoichiometry960
type: Stoichiometry
physical entity: Protein870
stoichiometric coefficient: 1.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P25457
data source: Provenance1
name: P18124
name: 60S ribosomal protein L7
name: P25457
xref: UnificationXref1918
feature: FragmentFeature414
cellular location: GO:0005829
comment: Reactome DB_ID: 3659248
display name: RPL7

Stoichiometry961
type: Stoichiometry
physical entity: Complex321
stoichiometric coefficient: 4.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O60143
data source: Provenance1
name: P18124
name: O60143
name: 60S ribosomal protein L7
xref: UnificationXref1916
feature: FragmentFeature413
cellular location: GO:0005829
comment: Reactome DB_ID: 3659244
display name: RPL7

Homologues of RPL7
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1919
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659249

Activated TLR4 signalling
type: Pathway
data source: Provenance1
pathway component: REACT 99838.9
pathway component: REACT 28525.10
evidence: Evidence1047
xref: UnificationXref6689
xref: RelationshipXref880
xref: UnificationXref6688
pathway order: PathwayStep1020
pathway order: PathwayStep1028
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74904
data source: Provenance1
name: P42766
name: 60S ribosomal protein L35
name: O74904
xref: UnificationXref1914
feature: FragmentFeature412
cellular location: GO:0005829
comment: Reactome DB_ID: 3659179
display name: RPL35

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O75000
data source: Provenance1
name: O75000
name: 60S ribosomal protein L12
name: P30050
xref: UnificationXref1912
feature: FragmentFeature411
cellular location: GO:0005829
comment: Reactome DB_ID: 3659001
display name: RPL12

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:O42935
data source: Provenance1
name: P02433
name: 60S ribosomal protein L32
name: O42935
xref: UnificationXref1909
feature: FragmentFeature410
cellular location: GO:0005829
comment: Reactome DB_ID: 3659165
display name: RPL32

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P79015
data source: Provenance1
name: P02433
name: P79015
name: 60S ribosomal protein L32
xref: UnificationXref1907
feature: FragmentFeature409
cellular location: GO:0005829
comment: Reactome DB_ID: 3659161
display name: RPL32

Homologues of RPL32
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1910
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659166

http://identifiers.org/pubmed/18555844
type: PublicationXref
id: 18555844
author: Buehrer, B
author: Madan, AK
author: Fain, JN
author: Bahouth, SW
author: Tichansky, DS
db: Pubmed
title: Comparison of messenger RNA distribution for 60 proteins in fat cells vs the nonfat cells of human omental adipose tissue
source: Metabolism 57:1005-15
year: 2008

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14317
data source: Provenance1
name: P05387
name: O14317
name: 60S acidic ribosomal protein P2
xref: UnificationXref1904
feature: FragmentFeature408
cellular location: GO:0005829
comment: Reactome DB_ID: 3658978
display name: RPLP2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P08094
data source: Provenance1
name: P05387
name: 60S acidic ribosomal protein P2
name: P08094
xref: UnificationXref1902
feature: FragmentFeature407
cellular location: GO:0005829
comment: Reactome DB_ID: 3658974
display name: RPLP2

http://identifiers.org/pubmed/15276077
type: PublicationXref
id: 15276077
author: Chimienti, F
author: Seve, M
author: Favier, A
author: Coquerel, Y
author: Pennequin, A
author: Devergnas, S
author: Naud, N
author: Chantegrel, J
db: Pubmed
title: Differential regulation of zinc efflux transporters ZnT-1, ZnT-5 and ZnT-7 gene expression by zinc levels: a real-time RT-PCR study
source: Biochem Pharmacol 68:699-709
year: 2004

http://identifiers.org/pubmed/17266529
type: PublicationXref
id: 17266529
author: Hyde, JE
db: Pubmed
title: Targeting purine and pyrimidine metabolism in human apicomplexan parasites
source: Curr Drug Targets 8:31-47
year: 2007

Stoichiometry965
type: Stoichiometry
physical entity: flavin mononucleotide
stoichiometric coefficient: 1.0

Stoichiometry964
type: Stoichiometry
physical entity: Protein871
stoichiometric coefficient: 6.0

Stoichiometry963
type: Stoichiometry
physical entity: SmallMolecule31
stoichiometric coefficient: 2.0

Stoichiometry962
type: Stoichiometry
physical entity: SmallMolecule30
stoichiometric coefficient: 2.0

Stoichiometry969
type: Stoichiometry
physical entity: Protein875
stoichiometric coefficient: 3.0

Stoichiometry968
type: Stoichiometry
physical entity: Protein874
stoichiometric coefficient: 6.0

Stoichiometry967
type: Stoichiometry
physical entity: Protein873
stoichiometric coefficient: 2.0

Stoichiometry966
type: Stoichiometry
physical entity: Protein872
stoichiometric coefficient: 1.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74892
data source: Provenance1
name: 40S ribosomal protein S2
name: P15880
name: O74892
name: LLREP3 protein
name: 40S small ribosomal protein 2
name: RPS2(2-293)
xref: UnificationXref1884
feature: FragmentFeature399
cellular location: GO:0005829
comment: Reactome DB_ID: 3658695
display name: S4

Homologues of RPSA
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1889
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658834

http://identifiers.org/pubmed/12700044
type: PublicationXref
id: 12700044
author: Maness, PF
author: Thelen, K
author: Panicker, AK
author: Buhusi, M
db: Pubmed
title: Cellular signalling mechanisms of neural cell adhesion molecules
source: Front Biosci 8:d900-11
year: 2003

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7L8
data source: Provenance1
name: Colon carcinoma laminin-binding protein
name: 40S ribosomal protein SA
name: RPSA
name: 34/67 kDa laminin receptor
name: 40S small ribosomal protein P4
name: Q9Y7L8
name: NEM/1CHD4
name: P08865
name: Multidrug resistance- associated protein MGr1-Ag
xref: UnificationXref1886
feature: FragmentFeature400
cellular location: GO:0005829
comment: Reactome DB_ID: 3658829
display name: P40

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9P546
data source: Provenance1
name: Colon carcinoma laminin-binding protein
name: 40S ribosomal protein SA
name: RPSA
name: 34/67 kDa laminin receptor
name: Q9P546
name: 40S small ribosomal protein P4
name: NEM/1CHD4
name: P08865
name: Multidrug resistance- associated protein MGr1-Ag
xref: UnificationXref1888
feature: FragmentFeature401
cellular location: GO:0005829
comment: Reactome DB_ID: 3658833
display name: P40

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74329
data source: Provenance1
name: 40S ribosomal protein S29
name: 40S small ribosomal protein 29
name: O74329
name: P30054
xref: UnificationXref1891
feature: FragmentFeature402
cellular location: GO:0005829
comment: Reactome DB_ID: 3658753
display name: RPS29

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10101
data source: Provenance1
name: 40S small ribosomal protein 7
name: Q10101
name: 40S ribosomal protein S7
name: P23821
name: RPS7
xref: UnificationXref1893
feature: FragmentFeature403
cellular location: GO:0005829
comment: Reactome DB_ID: 3658807
display name: S8

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P05732
data source: Provenance1
name: Q02543
name: 60S ribosomal protein L18a
name: P05732
xref: UnificationXref1896
feature: FragmentFeature404
cellular location: GO:0005829
comment: Reactome DB_ID: 3659055
display name: RPL18A

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P78946
data source: Provenance1
name: 60S ribosomal protein L26
name: Q02877
name: P78946
xref: UnificationXref1898
feature: FragmentFeature405
cellular location: GO:0005829
comment: Reactome DB_ID: 3659105
display name: RPL26

Homologues of RPLP2
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1905
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658979

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P17478
data source: Provenance1
name: P17478
name: P05387
name: 60S acidic ribosomal protein P2
xref: UnificationXref1900
feature: FragmentFeature406
cellular location: GO:0005829
comment: Reactome DB_ID: 3658970
display name: RPLP2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P58234
data source: Provenance1
name: 40S ribosomal protein S19
name: 40S small ribosomal protein 19
name: P39019
name: P58234
xref: UnificationXref1865
feature: FragmentFeature391
cellular location: GO:0005829
comment: Reactome DB_ID: 3658689
display name: RPS19

Homologues of RPS10
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1875
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658631

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O13614
data source: Provenance1
name: P46783
name: O13614
name: 40S ribosomal protein S10
name: 40S small ribosomal protein 10
xref: UnificationXref1872
feature: FragmentFeature394
cellular location: GO:0005829
comment: Reactome DB_ID: 3658626
display name: RPS10

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O60144
data source: Provenance1
name: 40S ribosomal protein S16
name: 40S small ribosomal protein 16
name: O60144
name: P17008
xref: UnificationXref1868
feature: FragmentFeature392
cellular location: GO:0005829
comment: Reactome DB_ID: 3658666
display name: RPS16

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P79057
data source: Provenance1
name: P39028
name: P79057
name: 40S small ribosomal protein 23
name: 40S ribosomal protein S23
xref: UnificationXref1870
feature: FragmentFeature393
cellular location: GO:0005829
comment: Reactome DB_ID: 3658709
display name: RPS23

Single copy abundant mRNA protein
type: Protein
entity reference: Q9P4W9
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: 40S ribosomal protein S4, X isoform
name: P12750
name: Q9P4W9
name: SCR10
name: 40S small ribosomal protein 4
xref: UnificationXref1877
feature: FragmentFeature396
cellular location: GO:0005829
comment: Reactome DB_ID: 3658776
display name: RPS4X

Single copy abundant mRNA protein
type: Protein
entity reference: P87158
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: 40S ribosomal protein S4, X isoform
name: P12750
name: SCR10
name: P87158
name: 40S small ribosomal protein 4
xref: UnificationXref1879
feature: FragmentFeature397
cellular location: GO:0005829
comment: Reactome DB_ID: 3658780
display name: RPS4X

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14112
data source: Provenance1
name: P46783
name: O14112
name: 40S ribosomal protein S10
name: 40S small ribosomal protein 10
xref: UnificationXref1874
feature: FragmentFeature395
cellular location: GO:0005829
comment: Reactome DB_ID: 3658630
display name: RPS10

Homologues of RPS4X
type: Protein
data source: Provenance1
member physical entity: Single copy abundant mRNA protein
member physical entity: Q9USW5
xref: UnificationXref1882
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658785

Q9USW5
type: Protein
entity reference: Q9USW5
data source: Provenance1
name: Single copy abundant mRNA protein
name: Note: the coordinates are copied over from Homo sapiens.
name: 40S ribosomal protein S4, X isoform
name: P12750
name: SCR10
name: 40S small ribosomal protein 4
xref: UnificationXref1881
feature: FragmentFeature398
cellular location: GO:0005829
comment: Reactome DB_ID: 3658784
display name: RPS4X

http://identifiers.org/pubmed/15538381
type: PublicationXref
id: 15538381
author: Lu, M
author: Gherzi, R
author: Leuenberger, SA
author: Hemmings, BA
author: Stoecklin, G
author: Hess, D
author: Mallaun, M
author: Schmidlin, M
author: Moroni, C
author: Gross, B
db: Pubmed
title: The ARE-dependent mRNA-destabilizing activity of BRF1 is regulated by protein kinase B
source: EMBO J 23:4760-9
year: 2004

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P05764
data source: Provenance1
name: P35265
name: P05764
name: 40S ribosomal protein S21
name: 40S small ribosomal protein 21
xref: UnificationXref1849
feature: FragmentFeature384
cellular location: GO:0005829
comment: Reactome DB_ID: 3658703
display name: RPS21

Homologues of RPS3A
type: Protein
data source: Provenance1
member physical entity: 40S ribosomal protein S3a
xref: UnificationXref1854
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658772

40S ribosomal protein S3a
type: Protein
entity reference: Q09781
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: P49241
name: Q09781
name: 40S small ribosomal protein 3A
xref: UnificationXref1851
feature: FragmentFeature385
cellular location: GO:0005829
comment: Reactome DB_ID: 3658767
display name: RPS3A

40S ribosomal protein S3a
type: Protein
entity reference: O94438
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: P49241
name: 40S small ribosomal protein 3A
name: O94438
xref: UnificationXref1853
feature: FragmentFeature386
cellular location: GO:0005829
comment: Reactome DB_ID: 3658771
display name: RPS3A

Homologues of RPS19
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1866
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658690

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P79016
data source: Provenance1
name: 40S ribosomal protein S19
name: 40S small ribosomal protein 19
name: P39019
name: P79016
xref: UnificationXref1863
feature: FragmentFeature390
cellular location: GO:0005829
comment: Reactome DB_ID: 3658685
display name: RPS19

Stoichiometry990
type: Stoichiometry
physical entity: Protein890
stoichiometric coefficient: 1.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P79013
data source: Provenance1
name: P04643
name: P79013
name: 40S ribosomal protein S11
name: 40S small ribosomal protein 11
xref: UnificationXref1856
feature: FragmentFeature387
cellular location: GO:0005829
comment: Reactome DB_ID: 3658637
display name: RPS11

Stoichiometry992
type: Stoichiometry
physical entity: Protein892
stoichiometric coefficient: 2.0

Homologues of RPS27A(77-156)
type: Protein
data source: Provenance1
member physical entity: 40S ribosomal protein S27a
xref: UnificationXref1861
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658743

Stoichiometry991
type: Stoichiometry
physical entity: SmallMolecule49
stoichiometric coefficient: 1.0

40S ribosomal protein S27a
type: Protein
entity reference: P0C8R3
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: RPS27A(77-156)
name: 40S small ribosomal protein 27A
xref: UnificationXref1858
feature: FragmentFeature388
cellular location: GO:0005829
comment: Reactome DB_ID: 3658741
display name: P0C8R3

Stoichiometry994
type: Stoichiometry
physical entity: Zn(II)
stoichiometric coefficient: 2.0

40S ribosomal protein S27a
type: Protein
entity reference: UniProt:P0C016
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: RPS27A(77-156)
name: 40S small ribosomal protein 27A
xref: UnificationXref1860
feature: FragmentFeature389
cellular location: GO:0005829
comment: Reactome DB_ID: 3658742
display name: P0C016

Stoichiometry993
type: Stoichiometry
physical entity: Protein893
stoichiometric coefficient: 2.0

Stoichiometry995
type: Stoichiometry
physical entity: Protein895
stoichiometric coefficient: 2.0

Stoichiometry996
type: Stoichiometry
physical entity: Protein898
stoichiometric coefficient: 2.0

Stoichiometry997
type: Stoichiometry
physical entity: Riboflavin-5-phosphate
stoichiometric coefficient: 2.0

Stoichiometry998
type: Stoichiometry
physical entity: Protein899
stoichiometric coefficient: 4.0

Stoichiometry999
type: Stoichiometry
physical entity: SmallMolecule134
stoichiometric coefficient: 4.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9P3T6
data source: Provenance1
name: Q9P3T6
name: RPS5(1-204)
name: 40S small ribosomal protein 5
name: 40S ribosomal protein S5
xref: UnificationXref1831
feature: FragmentFeature377
cellular location: GO:0005829
comment: Reactome DB_ID: 3658793
display name: P46782

Homologues of RPS26
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1837
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658736

http://identifiers.org/pubmed/10448521
type: PublicationXref
id: 10448521
author: Seetharam, B
db: Pubmed
title: Receptor-mediated endocytosis of cobalamin (vitamin B12)
source: Annu. Rev. Nutr. 19:173-95
year: 1999

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14277
data source: Provenance1
name: O14277
name: RPS5(1-204)
name: 40S small ribosomal protein 5
name: 40S ribosomal protein S5
xref: UnificationXref1829
feature: FragmentFeature376
cellular location: GO:0005829
comment: Reactome DB_ID: 3658789
display name: P46782

40S small ribosomal protein 13
type: Protein
entity reference: UniProt:P28189
data source: Provenance1
name: P28189
name: Note: the coordinates are copied over from Homo sapiens.
name: RPS13(2-151)
name: 40S ribosomal protein S13
xref: UnificationXref1847
feature: FragmentFeature383
cellular location: GO:0005829
comment: Reactome DB_ID: 3658650
display name: Q02546

http://identifiers.org/pubmed/9335335
type: PublicationXref
id: 9335335
author: Bell, SP
author: Aparicio, OM
author: Weinstein, DM
db: Pubmed
title: Components and dynamics of DNA replication complexes in S. cerevisiae: redistribution of MCM proteins and Cdc45p during S phase.
source: Cell 91:59-69
year: 1997

40S ribosomal protein S17
type: Protein
entity reference: UniProt:O42984
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: P08708
name: 40S small ribosomal protein 17
name: O42984
xref: UnificationXref1842
feature: FragmentFeature381
cellular location: GO:0005829
comment: Reactome DB_ID: 3658674
display name: RPS17

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94754
data source: Provenance1
name: RPS18
name: 40S ribosomal protein S18
name: 40S small ribosomal protein 18
name: P25232
name: O94754
name: KE-3
xref: UnificationXref1845
feature: FragmentFeature382
cellular location: GO:0005829
comment: Reactome DB_ID: 3658681
display name: KE3

Homologues of RPS17
type: Protein
data source: Provenance1
member physical entity: 40S ribosomal protein S17
xref: UnificationXref1843
cellular location: GO:0005829
comment: Reactome DB_ID: 3658675
comment: Converted from EntitySet in Reactome

40S ribosomal protein S17
type: Protein
entity reference: Q9P7J6
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: P08708
name: Q9P7J6
name: 40S small ribosomal protein 17
xref: UnificationXref1840
feature: FragmentFeature380
cellular location: GO:0005829
comment: Reactome DB_ID: 3658670
display name: RPS17

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UT56
data source: Provenance1
name: 40S ribosomal protein S26
name: 40S small ribosomal protein 26
name: Q9UT56
name: P02383
xref: UnificationXref1834
feature: FragmentFeature378
cellular location: GO:0005829
comment: Reactome DB_ID: 3658731
display name: RPS26

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTG4
data source: Provenance1
name: 40S ribosomal protein S26
name: 40S small ribosomal protein 26
name: Q9UTG4
name: P02383
xref: UnificationXref1836
feature: FragmentFeature379
cellular location: GO:0005829
comment: Reactome DB_ID: 3658735
display name: RPS26

Porphyrin
type: SmallMoleculeReference
name: Porphyrin [ChEBI:8337]
xref: UnificationXref6164

http://identifiers.org/pubmed/16738331
type: PublicationXref
id: 16738331
author: Itahana, Yoko
author: Yeh, Edward T H
author: Zhang, Yanping
db: Pubmed
title: Nucleocytoplasmic shuttling modulates activity and ubiquitination-dependent turnover of SUMO-specific protease 2
source: Mol. Cell. Biol. 26:4675-89
year: 2006

Toll-Like Receptors Cascades
type: Pathway
data source: Provenance1
pathway component: REACT 89802.9
pathway component: Toll Like Receptor 9 (TLR9) Cascade
pathway component: REACT 126198.5
pathway component: REACT 144229.5
pathway component: REACT 83865.9
pathway component: REACT 98284.9
pathway component: REACT 112439.8
evidence: Evidence1052
xref: UnificationXref6699
xref: RelationshipXref878
xref: UnificationXref6698
pathway order: PathwayStep1022
pathway order: PathwayStep1030
pathway order: PathwayStep1033
pathway order: PathwayStep1025
pathway order: PathwayStep1026
pathway order: PathwayStep1018
pathway order: PathwayStep1021
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

The polymerase component of DNA polymerase alpha:primase synthesizes a 20-nucleotide primer on the G strand of the telomere
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1252
EC number: 2.7.7.7
xref: UnificationXref7848
xref: RelationshipXref1006
xref: UnificationXref7849
left: Deoxythymidine 5'-triphosphate
left: deoxycytidine 5'-triphosphate
left: 2'-deoxyguanosine 5'-triphosphate
left: 2'-deoxyadenosine 5'-triphosphate
left: Complex643
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex644

http://identifiers.org/pubmed/7564244
type: PublicationXref
id: 7564244
author: Mooyer, P
author: Wanders, RJ
db: Pubmed
title: D-2-hydroxyglutaric acidaemia: identification of a new enzyme, D-2-hydroxyglutarate dehydrogenase, localized in mitochondria
source: J Inherit Metab Dis 18:194-6
year: 1995

Formation of Processive Complex on the C-strand of the telomere
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1257
xref: UnificationXref7863
xref: UnificationXref7862
xref: RelationshipXref1006
left: Complex647
left: Complex494
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex648

Paused RNA Polymerase III Transcription Complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry329
component stoichiometry: Stoichiometry328
component: RNA Polymerase III Holoenzyme (name copied from entity in Homo sapiens)
component: PhysicalEntity68
xref: UnificationXref705
cellular location: GO:0005654
comment: Reactome DB_ID: 3660449

RFC dissociates after sliding clamp formation on the C-strand of the telomere
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1256
xref: UnificationXref7859
xref: UnificationXref7860
xref: RelationshipXref1006
left: Complex646
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex647
right: Complex489

Loading of PCNA - Sliding Clamp Formation on the C-strand of the telomere
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1255
xref: UnificationXref7857
xref: UnificationXref7856
xref: RelationshipXref1006
left: SmallMolecule7
left: Complex491
left: Complex645
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex646
right: SmallMolecule8

RFC binding displaces Pol Alpha on the C-strand of the telomere
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1254
xref: UnificationXref7854
xref: RelationshipXref1006
xref: UnificationXref7853
left: Complex644
left: Complex489
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex645
right: Complex477

UnificationXref1677
type: UnificationXref
id: Q9UTM3
db: UniProt

UnificationXref1676
type: UnificationXref
id: 3657755
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657755

Activated PKC alpha (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry345
component stoichiometry: Stoichiometry344
component stoichiometry: Stoichiometry346
component stoichiometry: Stoichiometry347
component: Homologues of PRKCA
component: SmallMolecule29
component: SmallMolecule27
component: SmallMolecule21
xref: UnificationXref846
cellular location: GO:0005886
comment: Reactome DB_ID: 3660504

UnificationXref1679
type: UnificationXref
id: O42897
db: UniProt

UnificationXref1678
type: UnificationXref
id: 3657840
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657840

UnificationXref1673
type: UnificationXref
id: O74440
db: UniProt

UnificationXref1672
type: UnificationXref
id: 3657834
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657834

UnificationXref1675
type: UnificationXref
id: Q09682
db: UniProt

UnificationXref1674
type: UnificationXref
id: 3657862
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657862

Recruitment of Dna2 endonuclease to the C strand
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1261
xref: UnificationXref7877
xref: UnificationXref7876
xref: RelationshipXref1006
left: Protein1108
left: Complex651
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex652

VAV3 Rho/Rac effectors:GDP (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry335
component stoichiometry: Stoichiometry334
component: Homologues of RHOA
component: SmallMolecule18
xref: UnificationXref758
cellular location: GO:0005829
comment: Reactome DB_ID: 3662879

Removal of remaining Flap from the C-strand
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1262
xref: UnificationXref7882
xref: UnificationXref7883
xref: RelationshipXref1006
left: Complex653
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex654

VAV3 Rho/Rac effectors:GTP (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry336
component stoichiometry: Stoichiometry337
component: Homologues of RHOA
component: SmallMolecule17
xref: UnificationXref759
cellular location: GO:0005829
comment: Reactome DB_ID: 3662880

Formation of C-strand Okazaki fragments
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1259
EC number: 2.7.7.7
xref: UnificationXref7870
xref: UnificationXref7869
xref: RelationshipXref1006
left: Deoxythymidine 5'-triphosphate
left: deoxycytidine 5'-triphosphate
left: 2'-deoxyguanosine 5'-triphosphate
left: 2'-deoxyadenosine 5'-triphosphate
left: Complex648
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex649

VAV2 Rho/Rac effectors:GDP (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry331
component stoichiometry: Stoichiometry330
component: PhysicalEntity71
component: SmallMolecule18
xref: UnificationXref751
cellular location: GO:0005829
comment: Reactome DB_ID: 3662873

UnificationXref1671
type: UnificationXref
id: Q9P7S2
db: UniProt

Formation of the Flap Intermediate on the C-strand
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1260
xref: UnificationXref7873
xref: UnificationXref7872
xref: RelationshipXref1006
left: Complex649
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex650

VAV2 Rho/Rac effectors:GTP (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry333
component stoichiometry: Stoichiometry332
component: PhysicalEntity71
component: SmallMolecule17
xref: UnificationXref752
cellular location: GO:0005829
comment: Reactome DB_ID: 3662874

UnificationXref1670
type: UnificationXref
id: 3657866
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657866

Protein kinase C, novel isoforms:DAG (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry342
component stoichiometry: Stoichiometry343
component: SmallMolecule21
component: PhysicalEntity72
xref: UnificationXref799
cellular location: GO:0005886
comment: Reactome DB_ID: 3662607

Activated conventional protein kinase C
type: Complex
data source: Provenance1
member physical entity: Activated PKC gamma (name copied from entity in Homo sapiens)
member physical entity: Activated PKC beta (name copied from entity in Homo sapiens)
member physical entity: Activated PKC alpha (name copied from entity in Homo sapiens)
xref: UnificationXref852
cellular location: GO:0005886
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3660510

Joining of adjacent Okazaki fragments of the C-strand
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1264
xref: UnificationXref7890
xref: RelationshipXref1006
xref: UnificationXref7889
left: Complex654
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex655

VAV family:PIP3 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry339
component stoichiometry: Stoichiometry338
component: SmallMolecule19
component: VAV family
xref: UnificationXref770
cellular location: GO:0005829
comment: Reactome DB_ID: 3662826

http://identifiers.org/pubmed/10501970
type: PublicationXref
id: 10501970
author: Francomano, CA
author: Munnich, A
author: King, LM
author: Wilkin, DJ
author: Clarke, CF
author: Ho, N
author: Jonassen, T
author: Vajo, Z
db: Pubmed
title: Conservation of the Caenorhabditis elegans timing gene clk-1 from yeast to human: a gene required for ubiquinone biosynthesis with potential implications for aging
source: Mamm Genome 10:1000-4
year: 1999

VAV family:PIP2 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry341
component stoichiometry: Stoichiometry340
component: VAV family
component: SmallMolecule20
xref: UnificationXref776
cellular location: GO:0005829
comment: Reactome DB_ID: 3662824

ADP is exchanged for ATP in the (ADP:CCT/TriC):tubulin complex
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1272
xref: UnificationXref7927
xref: UnificationXref7928
participant stoichiometry: Stoichiometry1850
participant stoichiometry: Stoichiometry1851
left: Complex657
left: SmallMolecule30
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule31
right: Complex659

Disassociation of Processive Complex and Completed Telomere End
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1266
xref: UnificationXref7896
xref: UnificationXref7895
xref: RelationshipXref1007
left: Complex655
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex494
right: Complex491
right: Complex656

EIF5A + spermidine <=> EIF5A(Dhp) + 1,3-diaminopropane
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1279
EC number: 2.5.1.46
xref: UnificationXref7968
xref: UnificationXref7969
left: Spermidine
left: PhysicalEntity236
left: SmallMolecule71
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: PhysicalEntity237
right: SmallMolecule72
right: SmallMolecule26
right: 1,3-diaminopropane

Exchange of ADP for ATP in CCT/TriC:actin complex
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1274
xref: UnificationXref7936
xref: UnificationXref7935
participant stoichiometry: Stoichiometry1864
participant stoichiometry: Stoichiometry1876
left: Complex660
left: SmallMolecule30
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex661
right: SmallMolecule31

http://identifiers.org/pubmed/10970868
type: PublicationXref
id: 10970868
author: Bell, SP
author: Klemm, RD
author: Lee, DG
author: Makhov, AM
db: Pubmed
title: Regulation of origin recognition complex conformation and ATPase activity: differential effects of single-stranded and double-stranded DNA binding.
source: EMBO J 19:4774-82
year: 2000

EIF5A(Dhp) + O2 => EIF5A(Hyp)
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1281
EC number: 1.14.99.29
xref: UnificationXref7983
xref: UnificationXref7984
left: SmallMolecule187
left: PhysicalEntity237
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: PhysicalEntity238

EIF5A(Dhp) + 1,3-diaminopropane <=> EIF5A + spermidine
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1280
EC number: 2.5.1.46
xref: UnificationXref7971
xref: UnificationXref7970
left: PhysicalEntity237
left: SmallMolecule26
left: 1,3-diaminopropane
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Spermidine
right: PhysicalEntity236
right: SmallMolecule71

http://identifiers.org/pubmed/15519848
type: PublicationXref
id: 15519848
author: Reissmann, S
author: Meyer, AS
author: Frydman, J
author: Spiess, C
db: Pubmed
title: Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets
source: Trends Cell Biol 14:598-604
year: 2004

D-Fructose 2,6-bisphosphate [ChEBI:28602]
type: SmallMoleculeReference
name: D-Fructose 2,6-bisphosphate
xref: UnificationXref2249

UnificationXref1669
type: UnificationXref
id: P50524
db: UniProt

http://identifiers.org/pubmed/12482854
type: PublicationXref
id: 12482854
author: Horton, JD
author: Moon, YA
db: Pubmed
title: Identification of two mammalian reductases involved in the two-carbon fatty acyl elongation cascade
source: J Biol Chem 278:7335-43
year: 2003

UnificationXref1668
type: UnificationXref
id: 3657873
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657873

UnificationXref1667
type: UnificationXref
id: 3657875
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657875

UnificationXref1666
type: UnificationXref
id: 3657751
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657751

UnificationXref1665
type: UnificationXref
id: O59770
db: UniProt

UnificationXref1664
type: UnificationXref
id: 3657739
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657739

UnificationXref1663
type: UnificationXref
id: P41878
db: UniProt

Coproporphyrinogen I
type: SmallMoleculeReference
name: Coproporphyrinogen I [ChEBI:3879]
xref: UnificationXref5350

UnificationXref1662
type: UnificationXref
id: 3657848
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657848

UnificationXref1661
type: UnificationXref
id: P87048
db: UniProt

phosphatidylinositol + UDP-N-acetyl-D-glucosamine -> N-acetylglucosaminyl-PI + UDP
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1284
xref: UnificationXref8013
xref: UnificationXref8012
left: 1-Phosphatidyl-D-myo-inositol
left: UDP-N-acetylglucosamine
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: N-acetylglucosaminyl-PI
right: uridine 5'-diphosphate

UnificationXref1660
type: UnificationXref
id: 3657747
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657747

http://identifiers.org/pubmed/9712840
type: PublicationXref
id: 9712840
author: Kikuchi, Y
author: Mizutani, M
author: Katada, T
author: Imai, M
author: Hoshino, S
author: Hanaoka, F
author: Ui, M
db: Pubmed
title: Molecular cloning of a novel member of the eukaryotic polypeptide chain-releasing factors (eRF). Its identification as eRF3 interacting with eRF1.
source: J Biol Chem 273:22254-9
year: 1998

N-acetylglucosaminyl-PI + H2O -> glucosaminyl-PI + acetate
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1285
EC number: 3.5.1.89
xref: UnificationXref8019
xref: UnificationXref8020
left: SmallMolecule22
left: N-acetylglucosaminyl-PI
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: glucosaminyl-PI
right: Acetate

glucosaminyl-PI + fatty acyl-CoA -> glucosaminyl-acyl-PI + CoA-SH
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1286
xref: UnificationXref8033
xref: UnificationXref8032
left: glucosaminyl-PI
left: Fatty acyl CoA
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: glucosaminyl-acyl-PI
right: CoA-SH

mannose(a1-4)glucosaminyl-acyl-PI + phosphatidylethanolamine -> (ethanolamineP) mannose(al1-4)glucosaminyl-acyl-PI + diacylglycerol
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1287
EC number: 2.7.8
xref: UnificationXref8047
xref: UnificationXref8046
left: mannose (a1-4) glucosaminyl-acyl-PI
left: phosphatidylethanolamine
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: PhysicalEntity240
right: 1,2-Diacylglyceroll

GlcNAc1P is dephosphorylated to UDP-N-acetyl-glucosamine
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1297
EC number: 2.7.7.23
xref: UnificationXref8112
xref: UnificationXref8113
left: N-Acetyl-D-glucosamine 1-phosphate
left: SmallMolecule103
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule48
right: UDP-N-acetylglucosamine

Isomerization of GlcNAc6P to GlcNAc1P
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1296
EC number: 5.4.2.3
xref: UnificationXref8107
xref: UnificationXref8106
left: N-Acetyl-D-glucosamine 6-phosphate
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: N-Acetyl-D-glucosamine 1-phosphate

Acetylation of glucosamine 6-phosphate to GlcNAc6P
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1295
EC number: 2.3.1.4
xref: UnificationXref8099
xref: UnificationXref8100
left: D-glucosamine 6-phosphate
left: SmallMolecule79
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule150
right: N-Acetyl-D-glucosamine 6-phosphate

Formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1294
EC number: 2.6.1.16
xref: UnificationXref8091
xref: UnificationXref8092
left: SmallMolecule65
left: L-Glutamine
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: D-glucosamine 6-phosphate
right: SmallMolecule97

Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction677
evidence: Evidence1182
xref: UnificationXref7516
xref: UnificationXref7515
pathway order: PathwayStep1159
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/15534001
type: PublicationXref
id: 15534001
author: Allison, JG
author: Williams, CC
author: Beckman, BS
author: Jones, FE
author: Vidal, GA
author: Burow, ME
author: Marrero, L
db: Pubmed
title: The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone
source: J Cell Biol 167:469-78
year: 2004

RelationshipXref1099
type: RelationshipXref
id: GO:0070139
db: GENE ONTOLOGY
relationship type: MI:0355

Phosphorylation of dolichol
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1292
EC number: 2.7.1.108
xref: UnificationXref8081
xref: UnificationXref8080
left: SmallMolecule219
left: Dolichol
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Cytidine diphosphate
right: Dolichyl phosphate

BiochemicalReaction731
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1289
xref: UnificationXref8067
xref: UnificationXref8068
left: mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI
left: dolichyl phosphate D-mannose
display name: mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI + dolichol phosphate D-mannose -> mannose (a1-2) mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI + dolichol phosphate
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: mannose (a1-2) mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI
right: dolichyl phosphate

RelationshipXref1097
type: RelationshipXref
id: GO:0030968
db: GENE ONTOLOGY
relationship type: MI:0359

(ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI + dolichol phosphate D-mannose -> mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI + dolichol phosphate
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1288
xref: UnificationXref8061
xref: UnificationXref8060
left: PhysicalEntity240
left: dolichyl phosphate D-mannose
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI
right: dolichyl phosphate

RelationshipXref1098
type: RelationshipXref
id: GO:0044267
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1095
type: RelationshipXref
id: GO:0006987
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1096
type: RelationshipXref
id: 3662451
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662451

RelationshipXref1093
type: RelationshipXref
id: 3663877
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663877

RelationshipXref1094
type: RelationshipXref
id: GO:0006626
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1091
type: RelationshipXref
id: 3663907
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663907

RelationshipXref1092
type: RelationshipXref
id: GO:0008320
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1090
type: RelationshipXref
id: GO:0004222
db: GENE ONTOLOGY
relationship type: MI:0355

UnificationXref1695
type: UnificationXref
id: O14250
db: UniProt

UnificationXref1694
type: UnificationXref
id: 3657830
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657830

UnificationXref1697
type: UnificationXref
id: O14126
db: UniProt

UnificationXref1696
type: UnificationXref
id: 3657743
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657743

UnificationXref1699
type: UnificationXref
id: 3657858
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657858

UnificationXref1698
type: UnificationXref
id: 3657810
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657810

Mannose-1-phosphate converted to GDP-Mannose
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1301
EC number: 2.7.7.13
xref: UnificationXref8140
xref: UnificationXref8141
left: D-Mannose 1-phosphate
left: SmallMolecule17
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule48
right: GDP-alpha-D-mannose

UnificationXref1691
type: UnificationXref
id: O74762
db: UniProt

UnificationXref1690
type: UnificationXref
id: 3657877
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657877

Fructose 6-phosphate isomerizes to Mannose 6-phosphate
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1299
EC number: 5.3.1.8
xref: UnificationXref8122
xref: UnificationXref8121
left: SmallMolecule65
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: D-Mannose 6-phosphate

UnificationXref1693
type: UnificationXref
id: Q10311
db: UniProt

Mannose 6-phosphate isomerizes to Mannose 1-phosphate
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1300
EC number: 5.4.2.8
xref: UnificationXref8130
xref: UnificationXref8131
left: D-Mannose 6-phosphate
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: D-Mannose 1-phosphate

UnificationXref1692
type: UnificationXref
id: 3657826
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657826

Addition of a third mannose to the N-glycan precursor by ALG2
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1310
xref: UnificationXref8186
xref: UnificationXref8187
left: (GlcNAc)2 (Man)2 (PP-Dol)1
left: GDP-alpha-D-mannose
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule18
right: (GlcNAc)2 (Man)3 (PP-Dol)1

Addition of a second mannose to the N-glycan precursor by ALG2
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1309
xref: UnificationXref8182
xref: UnificationXref8181
left: beta-D-mannosyldiacetylchitobiosyldiphosphodolichol
left: GDP-alpha-D-mannose
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule18
right: (GlcNAc)2 (Man)2 (PP-Dol)1

Flipping of the N-glycan precursor to inside the ER
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1312
xref: UnificationXref8201
xref: UnificationXref8200
left: (GlcNAc)2 (Man)5 (PP-Dol)1
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: (GlcNAc)2 (Man)5 (PP-Dol)1

Addition of a fourth and fifth mannose to the N-glycan precursor by ALG11
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1311
xref: UnificationXref8193
xref: UnificationXref8194
participant stoichiometry: Stoichiometry1890
participant stoichiometry: Stoichiometry1889
left: (GlcNAc)2 (Man)3 (PP-Dol)1
left: GDP-alpha-D-mannose
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule18
right: (GlcNAc)2 (Man)5 (PP-Dol)1

RelationshipXref1086
type: RelationshipXref
id: GO:0048208
db: GENE ONTOLOGY
relationship type: MI:0359

Addition of N-acetyl-D-glucosamine to Dolichyl phosphate
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1306
EC number: 2.7.8.15
xref: UnificationXref8160
xref: UnificationXref8161
left: Dolichyl phosphate
left: UDP-N-acetylglucosamine
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: N-acetyl-D-glucosaminyl-diphosphodolichol
right: SmallMolecule56

RelationshipXref1087
type: RelationshipXref
id: GO:0006888
db: GENE ONTOLOGY
relationship type: MI:0359

Synthesis of dolichyl-phosphate-glucose
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1303
EC number: 2.4.1.117
xref: UnificationXref8149
xref: UnificationXref8150
left: Dolichyl phosphate
left: SmallMolecule104
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Dolichyl beta-D-glucosyl phosphate

RelationshipXref1088
type: RelationshipXref
id: GO:0015035
db: GENE ONTOLOGY
relationship type: MI:0355

Addition of the first mannose to the N-glycan precursor by ALG13/14
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1308
EC number: 2.4.1.142
xref: UnificationXref8174
xref: UnificationXref8175
left: N,N'-diacetylchitobiosyldiphosphodolichol
left: GDP-alpha-D-mannose
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule18
right: beta-D-mannosyldiacetylchitobiosyldiphosphodolichol

RelationshipXref1089
type: RelationshipXref
id: 3663988
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663988

Addition of the second N-acetyl-glucosamine to the N-glycan precursor
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1307
EC number: 2.4.1.141
xref: UnificationXref8168
xref: UnificationXref8167
left: N-acetyl-D-glucosaminyl-diphosphodolichol
left: UDP-N-acetylglucosamine
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: N,N'-diacetylchitobiosyldiphosphodolichol
right: uridine 5'-diphosphate

RelationshipXref1082
type: RelationshipXref
id: 3663719
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663719

RelationshipXref1083
type: RelationshipXref
id: GO:0003924
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1084
type: RelationshipXref
id: 3661942
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661942

RelationshipXref1085
type: RelationshipXref
id: 3661972
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661972

RelationshipXref1080
type: RelationshipXref
id: 3663289
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663289

RelationshipXref1081
type: RelationshipXref
id: GO:0051787
db: GENE ONTOLOGY
relationship type: MI:0355

UnificationXref1686
type: UnificationXref
id: 3657787
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657787

UnificationXref1685
type: UnificationXref
id: Q9USQ9
db: UniProt

UnificationXref1684
type: UnificationXref
id: 3657763
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657763

UnificationXref1683
type: UnificationXref
id: O94517
db: UniProt

UnificationXref1689
type: UnificationXref
id: 3657806
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657806

UnificationXref1688
type: UnificationXref
id: O42931
db: UniProt

UnificationXref1687
type: UnificationXref
id: 3657767
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657767

Addition of the sixth mannose to the N-glycan precursor by ALG3.
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1313
xref: UnificationXref8213
xref: UnificationXref8212
left: (GlcNAc)2 (Man)5 (PP-Dol)1
left: Dolichyl phosphate D-mannose
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Dolichyl phosphate
right: (GlcNAc)2 (Man)6 (PP-Dol)1

UnificationXref1682
type: UnificationXref
id: 3657771
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657771

Addition of the seventh mannose to the N-glycan precursor by ALG9, inside the ER lumen
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1314
xref: UnificationXref8219
xref: UnificationXref8220
left: Dolichyl phosphate D-mannose
left: (GlcNAc)2 (Man)6 (PP-Dol)1
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Dolichyl phosphate
right: (GlcNAc)2 (Man)7 (PP-Dol)1

UnificationXref1681
type: UnificationXref
id: Q9UQY2
db: UniProt

UnificationXref1680
type: UnificationXref
id: 3657852
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657852

UnificationXref1637
type: UnificationXref
id: 3663144
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663144

http://identifiers.org/pubmed/11896061
type: PublicationXref
id: 11896061
author: Hang, Jun
author: Dasso, Mary
db: Pubmed
title: Association of the human SUMO-1 protease SENP2 with the nuclear pore
source: J. Biol. Chem. 277:19961-6
year: 2002

Addition of the eighth mannose to the N-glycan precursor by ALG12, inside the ER lumen
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1315
xref: UnificationXref8227
xref: UnificationXref8226
left: (GlcNAc)2 (Man)7 (PP-Dol)1
left: Dolichyl phosphate D-mannose
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Dolichyl phosphate
right: (GlcNAc)2 (Man)8 (PP-Dol)1

UnificationXref1636
type: UnificationXref
id: 3663141
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663141

UnificationXref1639
type: UnificationXref
id: 3663146
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663146

UnificationXref1638
type: UnificationXref
id: 3663145
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663145

Addition of a second glucose to the N-glycan precursor by ALG8
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1318
xref: UnificationXref8247
xref: UnificationXref8248
left: (Glc)1 (GlcNAc)2 (Man)9 (PP-Dol)1
left: Dolichyl beta-D-glucosyl phosphate
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Dolichyl phosphate
right: (Glc)2 (GlcNAc)2 (Man)9 (PP-Dol)1

Addition of a third glucose to the N-glycan precursor by an ALG10 homologue
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1319
xref: UnificationXref8254
xref: UnificationXref8255
left: Dolichyl beta-D-glucosyl phosphate
left: (Glc)2 (GlcNAc)2 (Man)9 (PP-Dol)1
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Dolichyl phosphate
right: (Glc)3 (GlcNAc)2 (Man)9 (PP-Dol)1

Addition of the last mannose to the N-glycan precursor by ALG3, inside the ER lumen.
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1316
xref: UnificationXref8232
xref: UnificationXref8231
left: (GlcNAc)2 (Man)8 (PP-Dol)1
left: Dolichyl phosphate D-mannose
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Dolichyl phosphate
right: (GlcNAc)2 (Man)9 (PP-Dol)1

Addition of the first glucose to the N-glycan precursor by ALG6
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1317
xref: UnificationXref8240
xref: UnificationXref8241
left: (GlcNAc)2 (Man)9 (PP-Dol)1
left: Dolichyl beta-D-glucosyl phosphate
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Dolichyl phosphate
right: (Glc)1 (GlcNAc)2 (Man)9 (PP-Dol)1

Trimming of the terminal mannose on the C branch
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1323
EC number: 3.2.1.24
xref: UnificationXref8294
xref: UnificationXref8295
left: Complex671
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex673
right: D-mannose

Trimming of the first mannose on the A branch
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1324
EC number: 3.2.1.24
xref: UnificationXref8301
xref: UnificationXref8300
left: Complex671
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex674
right: D-mannose

Trimming of the first glucose by glucosidase I
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1321
EC number: 3.2.1.106
xref: UnificationXref8271
xref: UnificationXref8272
left: Complex669
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: alpha-D-glucose
right: Complex670

C6 deamination of adenosine
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction519
pathway component: BiochemicalReaction518
evidence: Evidence862
xref: UnificationXref5677
xref: UnificationXref5678
pathway order: PathwayStep851
pathway order: PathwayStep850
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Trimming of the terminal mannose on the B branch
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1322
EC number: 3.2.1.24
xref: UnificationXref8289
xref: UnificationXref8288
left: Complex671
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex672
right: D-mannose

Trimming of the second mannose on the A branch
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1325
EC number: 3.2.1.24
xref: UnificationXref8306
xref: UnificationXref8307
left: Complex674
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex675
right: D-mannose

UnificationXref1632
type: UnificationXref
id: 450444
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=450444

UnificationXref1633
type: UnificationXref
id: REACT_27038
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_27038.1

UnificationXref1634
type: UnificationXref
id: O94432
db: UniProt

UnificationXref1635
type: UnificationXref
id: 3663140
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663140

UnificationXref1630
type: UnificationXref
id: 3665476
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665476

UnificationXref1631
type: UnificationXref
id: REACT_83961
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_83961.9

UnificationXref1629
type: UnificationXref
id: REACT_147301
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_147301.5

UnificationXref1628
type: UnificationXref
id: 3665475
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665475

UnificationXref1627
type: UnificationXref
id: REACT_31570
db: Reactome
id version: 10
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_31570.10

Re-addition of a glucose on the alpha 1,3 branch
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1326
xref: UnificationXref8320
xref: UnificationXref8321
left: Complex671
left: Dolichyl beta-D-glucosyl phosphate
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Dolichyl phosphate
right: Complex676

UnificationXref1626
type: UnificationXref
id: 3662756
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662756

Glycoproteins with major folding defects are sent to degradation by EDEMs
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1327
xref: UnificationXref8334
xref: UnificationXref8335
left: Complex675
left: Complex674
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex678
right: Complex677

UnificationXref1625
type: UnificationXref
id: 3662754
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662754

Coat Assembly
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1331
xref: UnificationXref8369
xref: UnificationXref8368
left: Complex679
left: Complex680
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex681

Loss of Sar1b GTPase
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1332
EC number: 3.6.5.1
EC number: 3.6.5.3
EC number: 3.6.5.2
EC number: 3.6.5.4
xref: UnificationXref8372
xref: UnificationXref8373
left: Complex681
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex683
right: SmallMolecule34
right: Complex680

Cargo, Sec31p:Sec13p, and v-SNARE recruitment
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1333
xref: UnificationXref8382
xref: UnificationXref8383
left: Protein1485
left: Complex681
left: Protein1484
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex684

Vesicle Budding
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1334
xref: UnificationXref8400
xref: UnificationXref8399
left: Complex684
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex686

Vesicle Uncoating
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1335
EC number: 3.6.5.1
EC number: 3.6.5.3
EC number: 3.6.5.2
EC number: 3.6.5.4
xref: UnificationXref8402
xref: UnificationXref8401
left: Complex686
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule34
right: Protein1483
right: Protein1485
right: Protein1467
right: Protein1484
right: Protein1475

MIA40:ERV1 (CHCHD4:GFER) Catalyzes Formation of Disulfide Bonds
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1341
xref: UnificationXref8438
xref: UnificationXref8437
left: Protein1499
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Products of MIA40:ERV1

MPP Cleaves Presequence of Inner Membrane Precursors
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1342
EC number: 3.4.24
xref: UnificationXref8470
xref: UnificationXref8471
left: Complex690
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex693

Precursor Proteins Enter TIMM23 PAM
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1343
xref: UnificationXref8483
xref: UnificationXref8484
left: Complex691
left: Precursors Imported to the Matrix by TIMM23 PAM
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex695

UnificationXref1623
type: UnificationXref
id: 3662750
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662750

UnificationXref1624
type: UnificationXref
id: P40383
db: UniProt

UnificationXref1621
type: UnificationXref
id: 429875
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=429875

UnificationXref1622
type: UnificationXref
id: REACT_20726
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20726.1

UnificationXref1620
type: UnificationXref
id: REACT_141653
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_141653.5

TIMM23 PAM Imports Proteins to Mitochondrial Matrix
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1345
xref: UnificationXref8497
xref: UnificationXref8496
left: SmallMolecule80
left: Complex696
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex691
right: SmallMolecule52
right: SmallMolecule84
right: Proteins Imported to the Matrix by TIMM23 PAM

UnificationXref1659
type: UnificationXref
id: O94579
db: UniProt

Dimerization of IRE1
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1350
xref: UnificationXref8511
xref: UnificationXref8510
participant stoichiometry: Stoichiometry1954
left: Note: the coordinates are copied over from Homo sapiens.
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex697

UnificationXref1658
type: UnificationXref
id: 3657876
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657876

MPP Cleaves Presequence of Matrix Precursors
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1344
EC number: 3.4.24
xref: UnificationXref8490
xref: UnificationXref8491
left: Complex695
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex696

Conjugation of SUMO2 to UBA2:SAE1
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1386
xref: UnificationXref8641
xref: UnificationXref8642
left: SmallMolecule7
left: Small ubiquitin-related modifier 2
left: Complex700
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex701
right: SmallMolecule14
right: AMP

Proteolytic Processing of SUMO3
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1383
xref: UnificationXref8626
xref: UnificationXref8625
left: O13351
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: O13351

Conjugation of SUMO1 to UBA2:SAE1
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1385
xref: UnificationXref8640
xref: UnificationXref8639
left: SmallMolecule7
left: O13351
left: Complex700
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex701
right: SmallMolecule14
right: AMP

Proteolytic Processing of SUMO1
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1381
xref: UnificationXref8617
xref: UnificationXref8618
left: O13351
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: O13351

Proteolytic Processing of SUMO2
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1382
xref: UnificationXref8622
xref: UnificationXref8621
left: Small ubiquitin-related modifier 2
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Small ubiquitin-related modifier 2

Autophosphorylation of IRE1 dimer
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1351
EC number: 2.7.11
xref: UnificationXref8514
xref: UnificationXref8515
participant stoichiometry: Stoichiometry1957
participant stoichiometry: Stoichiometry1956
left: Complex697
left: SmallMolecule30
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex698
right: SmallMolecule31

ADP Binding by Phosphorylated IRE1 Homodimer
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1352
xref: UnificationXref8519
xref: UnificationXref8520
participant stoichiometry: Stoichiometry1959
left: Complex698
left: SmallMolecule31
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex699

UnificationXref1650
type: UnificationXref
id: 3663156
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663156

UnificationXref1651
type: UnificationXref
id: 3663157
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663157

UnificationXref1652
type: UnificationXref
id: 3657871
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657871

UnificationXref1653
type: UnificationXref
id: O94393
db: UniProt

UnificationXref1654
type: UnificationXref
id: 3657870
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657870

UnificationXref1655
type: UnificationXref
id: P30655
db: UniProt

http://identifiers.org/pubmed/12474143
type: PublicationXref
id: 12474143
author: Carlson, Christopher G
author: Hoffbuhr, Kristen C
author: Kennaway, Nancy G
author: Glerum, D Moira
author: Antonicka, Hana
author: Leary, Scot C
author: Shoubridge, EA
author: Mattman, Andre
db: Pubmed
title: Mutations in COX15 produce a defect in the mitochondrial heme biosynthetic pathway, causing early-onset fatal hypertrophic cardiomyopathy
source: Am. J. Hum. Genet. 72:101-14
year: 2003

UnificationXref1656
type: UnificationXref
id: 3657797
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657797

UnificationXref1657
type: UnificationXref
id: Q10329
db: UniProt

UniProt:P28189
type: ProteinReference
xref: UnificationXref1846
organism: BioSource1

Conjugation of SUMO3 to UBA2:SAE1
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1387
xref: UnificationXref8643
xref: UnificationXref8644
left: SmallMolecule7
left: O13351
left: Complex700
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex701
right: SmallMolecule14
right: AMP

Transfer of SUMO3 from E1 to UBE2I (UBC9)
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1391
evidence: Evidence1389
evidence: Evidence1390
EC number: 2
xref: UnificationXref8651
xref: UnificationXref8650
left: Complex701
left: Note: the coordinates are copied over from Homo sapiens.
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Note: the coordinates are copied over from Homo sapiens.
right: Complex700

UnificationXref1649
type: UnificationXref
id: 3663155
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663155

Transport of L1 into endosomes
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1397
xref: UnificationXref8686
xref: UnificationXref8685
left: Complex702
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex702

UnificationXref1648
type: UnificationXref
id: 3663154
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663154

Phosphorylation of L1 by ERK
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1398
xref: UnificationXref8690
xref: UnificationXref8689
left: phospho-p-T185,Y187-MAPK1
left: SmallMolecule30
left: Complex702
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule31
right: Complex706

UnificationXref1647
type: UnificationXref
id: 3663153
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663153

Golgi vesicle lattice disassociation
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1411
xref: UnificationXref8738
xref: UnificationXref8739
left: PhysicalEntity254
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex709
right: ARFGAP1

MVB Vesicle Formation
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1414
xref: UnificationXref8773
xref: UnificationXref8772
left: Complex711
left: Complex712
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex715
right: Complex713

GAP Recruitment to the Coatomer:Arf1-GTP Complex
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1407
xref: UnificationXref8726
xref: UnificationXref8725
left: Complex707
left: ARFGAP1
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Complex710

Coatomer:Arf1-GTP:GAP lattice formation on golgi membrane
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1408
xref: UnificationXref8728
xref: UnificationXref8729
left: Complex710
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: PhysicalEntity252

Sculpting and pinching-off of Golgi vessicle
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1409
xref: UnificationXref8734
xref: UnificationXref8733
left: PhysicalEntity253
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: PhysicalEntity254

Hydrolysis of Arf1-GTP to Arf1-GDP
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence1410
xref: UnificationXref8737
xref: UnificationXref8736
left: Complex710
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule34
right: PhysicalEntity255

Signaling by ERBB2
type: Pathway
data source: Provenance1
pathway component: REACT 142773.5
pathway component: REACT 127315.5
pathway component: PLCG1 events in ERBB2 signaling
pathway component: REACT 149075.4
evidence: Evidence250
xref: UnificationXref1292
xref: UnificationXref1291
pathway order: PathwayStep244
pathway order: PathwayStep246
pathway order: PathwayStep245
pathway order: PathwayStep247
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UnificationXref1641
type: UnificationXref
id: 3663148
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663148

UnificationXref1642
type: UnificationXref
id: 3663149
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663149

UnificationXref1640
type: UnificationXref
id: 3663147
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663147

UnificationXref1645
type: UnificationXref
id: REACT_158472
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_158472.3

UnificationXref1646
type: UnificationXref
id: MOD:01148
db: MOD

UnificationXref1643
type: UnificationXref
id: 3663150
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663150

UnificationXref1644
type: UnificationXref
id: 3663151
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663151

DNA containing a hNTH1-bound apurinic/apyrimidinic site (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry22
component stoichiometry: Stoichiometry21
component: PhysicalEntity2
component: Protein3
xref: UnificationXref79
cellular location: GO:0005654
comment: Reactome DB_ID: 3660259

FEN1:PCNA complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry24
component stoichiometry: Stoichiometry23
component: Protein5
component: Protein4
xref: UnificationXref113
cellular location: GO:0005654
comment: Reactome DB_ID: 3660312

REV1:damaged DNA template complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry26
component stoichiometry: Stoichiometry25
component: Protein6
component: PhysicalEntity12
xref: UnificationXref128
cellular location: GO:0005654
comment: Reactome DB_ID: 3660280

REV1:lesioned DNA template with misinserted bases (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry27
component stoichiometry: Stoichiometry28
component: Protein6
component: PhysicalEntity13
xref: UnificationXref133
cellular location: GO:0005654
comment: Reactome DB_ID: 3660282

Pol eta:damaged DNA template complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry29
component stoichiometry: Stoichiometry30
component: Protein7
component: PhysicalEntity12
xref: UnificationXref144
cellular location: GO:0005654
comment: Reactome DB_ID: 3660291

Pol eta:lesioned DNA template inserted with correct base complement (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry32
component stoichiometry: Stoichiometry31
component: PhysicalEntity15
component: Protein7
xref: UnificationXref149
cellular location: GO:0005654
comment: Reactome DB_ID: 3660293

Pol zeta complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry34
component stoichiometry: Stoichiometry33
component: Protein8
component: Protein9
xref: UnificationXref160
cellular location: GO:0005654
comment: Reactome DB_ID: 3660306

Pol zeta:damaged DNA template complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry36
component stoichiometry: Stoichiometry35
component: Pol zeta complex (name copied from entity in Homo sapiens)
component: PhysicalEntity12
xref: UnificationXref161
cellular location: GO:0005654
comment: Reactome DB_ID: 3660307

http://identifiers.org/pubmed/18173545
type: PublicationXref
id: 18173545
author: Calamita, G
author: Svelto, M
author: Portincasa, P
author: Palasciano, G
db: Pubmed
title: Aquaporins in the hepatobiliary tract. Which, where and what they do in health and disease
source: Eur J Clin Invest 38:1-10
year: 2008

RelationshipXref1039
type: RelationshipXref
id: GO:0003977
db: GENE ONTOLOGY
relationship type: MI:0355

DNA containing a TDG-bound apurinic/apyrimidinic site (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry19
component stoichiometry: Stoichiometry20
component: PhysicalEntity2
component: Protein2
xref: UnificationXref71
cellular location: GO:0005654
comment: Reactome DB_ID: 3660256

RelationshipXref1031
type: RelationshipXref
id: 3662996
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662996

RelationshipXref1032
type: RelationshipXref
id: GO:0006489
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1033
type: RelationshipXref
id: GO:0004360
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1034
type: RelationshipXref
id: 3663081
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663081

RelationshipXref1035
type: RelationshipXref
id: GO:0004343
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1036
type: RelationshipXref
id: 3663090
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663090

RelationshipXref1037
type: RelationshipXref
id: GO:0004610
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1038
type: RelationshipXref
id: 3662960
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662960

RelationshipXref1030
type: RelationshipXref
id: GO:0004168
db: GENE ONTOLOGY
relationship type: MI:0355

RAD51:resected ends of DNA double-strand break (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry49
component stoichiometry: Stoichiometry48
component: Protein23
component: PhysicalEntity17
xref: UnificationXref234
cellular location: GO:0005654
comment: Reactome DB_ID: 3660163

Ku70:Ku80 heterodimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry50
component stoichiometry: Stoichiometry51
component: Protein25
component: Protein26
xref: UnificationXref265
cellular location: GO:0005654
comment: Reactome DB_ID: 3660016

RAD52:DNA double-strand break (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry45
component stoichiometry: Stoichiometry44
component: PhysicalEntity17
component: Protein20
xref: UnificationXref226
cellular location: GO:0005654
comment: Reactome DB_ID: 3660137

RAD51:RAD52:DNA double strand break end complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry46
component stoichiometry: Stoichiometry47
component: Protein23
component: Protein20
xref: UnificationXref231
cellular location: GO:0005654
comment: Reactome DB_ID: 3660138

XPC:HR23B:damaged DNA complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry56
component stoichiometry: Stoichiometry57
component: XPC:HR23B complex (name copied from entity in Homo sapiens)
component: PhysicalEntity12
xref: UnificationXref283
cellular location: GO:0005654
comment: Reactome DB_ID: 3659534

pre-incision complex in GG-NER (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry58
component stoichiometry: Stoichiometry76
component stoichiometry: Stoichiometry75
component stoichiometry: Stoichiometry59
component stoichiometry: Stoichiometry77
component stoichiometry: Stoichiometry64
component stoichiometry: Stoichiometry63
component: Protein34
component: RPA heterotrimer (name copied from entity in Homo sapiens)
component: Protein31
component: Protein44
component: TFIIH (name copied from entity in Homo sapiens)
component: XPC:HR23B:damaged DNA complex (name copied from entity in Homo sapiens)
component: PhysicalEntity21
xref: UnificationXref321
cellular location: GO:0005654
comment: Reactome DB_ID: 3659548

Ku:DNA double-strand break ends (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry52
component stoichiometry: Stoichiometry53
component: PhysicalEntity20
component: Ku70:Ku80 heterodimer (name copied from entity in Homo sapiens)
xref: UnificationXref266
cellular location: GO:0005654
comment: Reactome DB_ID: 3660017

XPC:HR23B complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry54
component stoichiometry: Stoichiometry55
component: Protein28
component: Protein27
xref: UnificationXref280
cellular location: GO:0005654
comment: Reactome DB_ID: 3659533

RelationshipXref1029
type: RelationshipXref
id: GO:0006501
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1028
type: RelationshipXref
id: GO:0016254
db: GENE ONTOLOGY
relationship type: MI:0359

dimeric phospho-ATM complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry39
component: Protein11
xref: UnificationXref184
cellular location: GO:0005654
comment: Reactome DB_ID: 3659909

RAD50:MRE11 complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry43
component stoichiometry: Stoichiometry42
component: Protein19
component: Protein18
xref: UnificationXref210
cellular location: GO:0005654
comment: Reactome DB_ID: 3659919

RelationshipXref1022
type: RelationshipXref
id: 3660639
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660639

RelationshipXref1023
type: RelationshipXref
id: GO:0016780
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1020
type: RelationshipXref
id: GO:0000225
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1021
type: RelationshipXref
id: 3660681
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660681

RelationshipXref1026
type: RelationshipXref
id: 3660687
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660687

RelationshipXref1027
type: RelationshipXref
id: 3660675
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660675

RelationshipXref1024
type: RelationshipXref
id: 3660669
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660669

RelationshipXref1025
type: RelationshipXref
id: GO:0004376
db: GENE ONTOLOGY
relationship type: MI:0355

dimeric ATM kinase (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry37
component: Protein10
xref: UnificationXref178
cellular location: GO:0005654
comment: Reactome DB_ID: 3659908

RNA Polymerase II holoenzyme complex (hyperphosphorylated) (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry104
component stoichiometry: Stoichiometry101
component stoichiometry: Stoichiometry100
component stoichiometry: Stoichiometry107
component stoichiometry: Stoichiometry105
component stoichiometry: Stoichiometry99
component stoichiometry: Stoichiometry106
component stoichiometry: Stoichiometry110
component stoichiometry: Stoichiometry109
component stoichiometry: Stoichiometry108
component stoichiometry: Stoichiometry103
component stoichiometry: Stoichiometry102
component: Protein47
component: Protein57
component: Protein48
component: Protein50
component: Protein51
component: Protein58
component: Protein49
component: Protein56
component: Protein54
component: Protein52
component: Protein55
component: Protein53
xref: UnificationXref384
cellular location: GO:0005654
comment: Reactome DB_ID: 3660190

Active Pol II transcription complex with damaged DNA hybrid (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry112
component stoichiometry: Stoichiometry111
component: RNA Polymerase II holoenzyme complex (hyperphosphorylated) (name copied from entity in Homo sapiens)
component: PhysicalEntity28
xref: UnificationXref385
cellular location: GO:0005654
comment: Reactome DB_ID: 3660191

Transcription-coupled (TC) repair complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry118
component stoichiometry: Stoichiometry117
component stoichiometry: Stoichiometry119
component stoichiometry: Stoichiometry115
component stoichiometry: Stoichiometry116
component stoichiometry: Stoichiometry114
component stoichiometry: Stoichiometry113
component: Protein62
component: Protein34
component: ERCC1:XPF complex (name copied from entity in Homo sapiens)
component: TFIIH (name copied from entity in Homo sapiens)
component: Protein61
component: Protein60
component: Protein59
xref: UnificationXref398
cellular location: GO:0005654
comment: Reactome DB_ID: 3660209

pre-incision complex with open DNA bubble (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry83
component stoichiometry: Stoichiometry85
component stoichiometry: Stoichiometry78
component stoichiometry: Stoichiometry79
component stoichiometry: Stoichiometry84
component stoichiometry: Stoichiometry82
component stoichiometry: Stoichiometry81
component stoichiometry: Stoichiometry80
component: Protein34
component: RPA heterotrimer (name copied from entity in Homo sapiens)
component: Protein31
component: XPC:HR23B complex (name copied from entity in Homo sapiens)
component: Protein44
component: TFIIH (name copied from entity in Homo sapiens)
component: PhysicalEntity21
component: PhysicalEntity23
xref: UnificationXref324
cellular location: GO:0005654
comment: Reactome DB_ID: 3659549

UnificationXref1613
type: UnificationXref
id: P87173
db: UniProt

ERCC1:XPF complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry87
component stoichiometry: Stoichiometry86
component: Protein45
component: Protein46
xref: UnificationXref331
cellular location: GO:0005654
comment: Reactome DB_ID: 3659560

UnificationXref1612
type: UnificationXref
id: 3662730
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662730

incision complex for GG-NER (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry88
component stoichiometry: Stoichiometry89
component: ERCC1:XPF complex (name copied from entity in Homo sapiens)
component: pre-incision complex with open DNA bubble (name copied from entity in Homo sapiens)
xref: UnificationXref334
cellular location: GO:0005654
comment: Reactome DB_ID: 3659561

UnificationXref1611
type: UnificationXref
id: Q9Y7M4
db: UniProt

Incision complex with 3'-incised damaged DNA (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry97
component stoichiometry: Stoichiometry92
component stoichiometry: Stoichiometry91
component stoichiometry: Stoichiometry90
component stoichiometry: Stoichiometry98
component stoichiometry: Stoichiometry96
component stoichiometry: Stoichiometry93
component stoichiometry: Stoichiometry95
component stoichiometry: Stoichiometry94
component: Protein34
component: RPA heterotrimer (name copied from entity in Homo sapiens)
component: Protein31
component: XPC:HR23B complex (name copied from entity in Homo sapiens)
component: Protein44
component: ERCC1:XPF complex (name copied from entity in Homo sapiens)
component: TFIIH (name copied from entity in Homo sapiens)
component: PhysicalEntity24
component: PhysicalEntity21
xref: UnificationXref341
cellular location: GO:0005654
comment: Reactome DB_ID: 3659562

UnificationXref1610
type: UnificationXref
id: 3662742
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662742

RPA heterotrimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry60
component stoichiometry: Stoichiometry61
component stoichiometry: Stoichiometry62
component: Protein33
component: Protein32
component: PhysicalEntity22
xref: UnificationXref296
cellular location: GO:0005654
comment: Reactome DB_ID: 3657951

TFIIH (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry68
component stoichiometry: Stoichiometry65
component stoichiometry: Stoichiometry69
component stoichiometry: Stoichiometry70
component stoichiometry: Stoichiometry67
component stoichiometry: Stoichiometry66
component stoichiometry: Stoichiometry74
component: CAK (name copied from entity in Homo sapiens)
component: Protein40
component: Protein35
component: Protein38
component: Protein39
component: Protein37
component: Protein36
xref: UnificationXref318
cellular location: GO:0005654
comment: Reactome DB_ID: 3659438

CAK (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry71
component stoichiometry: Stoichiometry72
component stoichiometry: Stoichiometry73
component: Protein41
component: Protein43
component: Protein42
xref: UnificationXref317
cellular location: GO:0005654
comment: Reactome DB_ID: 3659413

RelationshipXref1018
type: RelationshipXref
id: GO:0008194
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1017
type: RelationshipXref
id: GO:0043687
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1019
type: RelationshipXref
id: 3660663
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660663

RelationshipXref1013
type: RelationshipXref
id: 3662002
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662002

RelationshipXref1014
type: RelationshipXref
id: GO:0019135
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1015
type: RelationshipXref
id: 3662019
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662019

RelationshipXref1016
type: RelationshipXref
id: GO:0008612
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1010
type: RelationshipXref
id: GO:0051086
db: GENE ONTOLOGY
relationship type: MI:0359

http://identifiers.org/pubmed/8723348
type: PublicationXref
id: 8723348
author: Jefferson, AB
author: Pot, DA
author: Deuter-Reinhard, M
author: Masiarz, FR
author: Cousens, LS
author: Williams, LT
author: Chin, SM
author: Norris, FA
author: Kavanaugh, WM
author: Majerus, PW
db: Pubmed
title: Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2
source: Curr Biol 6:438-45
year: 1996

RelationshipXref1011
type: RelationshipXref
id: GO:0051084
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1012
type: RelationshipXref
id: GO:0034038
db: GENE ONTOLOGY
relationship type: MI:0355

UnificationXref1616
type: UnificationXref
id: 3662738
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662738

UnificationXref1617
type: UnificationXref
id: 3662749
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662749

UnificationXref1614
type: UnificationXref
id: 3662726
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662726

UnificationXref1615
type: UnificationXref
id: O42978
db: UniProt

UnificationXref1618
type: UnificationXref
id: 3662757
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662757

UnificationXref1619
type: UnificationXref
id: 3662764
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662764

RNA Polymerase II holoenzyme complex (hypophosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry143
component stoichiometry: Stoichiometry145
component stoichiometry: Stoichiometry144
component stoichiometry: Stoichiometry141
component stoichiometry: Stoichiometry148
component stoichiometry: Stoichiometry134
component stoichiometry: Stoichiometry140
component stoichiometry: Stoichiometry147
component stoichiometry: Stoichiometry146
component stoichiometry: Stoichiometry135
component stoichiometry: Stoichiometry139
component stoichiometry: Stoichiometry136
component stoichiometry: Stoichiometry142
component: Protein47
component: Protein69
component: Protein48
component: Protein57
component: Protein50
component: Protein58
component: Protein54
component: Protein56
component: Protein52
component: Protein53
component: Protein55
component: Protein49
component: TFIIF (name copied from entity in Homo sapiens)
xref: UnificationXref459
cellular location: GO:0005654
comment: Reactome DB_ID: 3660388

http://identifiers.org/pubmed/1894595
type: PublicationXref
id: 1894595
author: Burbaum, JJ
author: Schimmel, P
db: Pubmed
title: Structural relationships and the classification of aminoacyl-tRNA synthetases
source: J Biol Chem 266:16965-8
year: 1991

TFIIF (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry137
component stoichiometry: Stoichiometry138
component: Protein68
component: Protein67
xref: UnificationXref457
cellular location: GO:0005654
comment: Reactome DB_ID: 3658602

RNA Pol II (hypophosphorylated):capped pre-mRNA complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry133
component stoichiometry: Stoichiometry150
component stoichiometry: Stoichiometry149
component stoichiometry: Stoichiometry132
component: Protein70
component: RNA Polymerase II holoenzyme complex (hypophosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
component: PhysicalEntity37
component: Cap Binding Complex (CBC) (name copied from entity in Homo sapiens)
xref: UnificationXref462
cellular location: GO:0005654
comment: Reactome DB_ID: 3660389

UnificationXref1600
type: UnificationXref
id: 3665479
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665479

Cap Binding Complex (CBC) (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry131
component stoichiometry: Stoichiometry130
component: Protein66
component: Protein65
xref: UnificationXref450
cellular location: GO:0005654
comment: Reactome DB_ID: 3658543

NELF complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry128
component stoichiometry: Stoichiometry127
component stoichiometry: Stoichiometry126
component stoichiometry: Stoichiometry125
component: PhysicalEntity33
component: PhysicalEntity36
component: PhysicalEntity35
component: PhysicalEntity34
xref: UnificationXref445
cellular location: GO:0005654
comment: Reactome DB_ID: 3660377

UnificationXref1602
type: UnificationXref
id: O74499
db: UniProt

RNA Pol II (hypophosphorylated) complex bound to DSIF protein (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry151
component stoichiometry: Stoichiometry152
component: RNA Pol II (hypophosphorylated):capped pre-mRNA complex (name copied from entity in Homo sapiens)
component: DSIF complex (name copied from entity in Homo sapiens)
xref: UnificationXref463
cellular location: GO:0005654
comment: Reactome DB_ID: 3660390

UnificationXref1601
type: UnificationXref
id: REACT_144563
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_144563.5

DSIF complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry124
component stoichiometry: Stoichiometry123
component: Protein64
component: Protein63
xref: UnificationXref438
cellular location: GO:0005654
comment: Reactome DB_ID: 3660382

DSIF:NELF:early elongation complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry153
component stoichiometry: Stoichiometry129
component: NELF complex (name copied from entity in Homo sapiens)
component: RNA Pol II (hypophosphorylated) complex bound to DSIF protein (name copied from entity in Homo sapiens)
xref: UnificationXref464
cellular location: GO:0005654
comment: Reactome DB_ID: 3660391

Stalled Pol II in TC-NER (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry120
component: RNA Polymerase II holoenzyme complex (hyperphosphorylated) (name copied from entity in Homo sapiens)
xref: UnificationXref403
cellular location: GO:0005654
comment: Reactome DB_ID: 3660211

Active Pol II complex with repaired DNA template:mRNA hybrid (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry122
component stoichiometry: Stoichiometry121
component: PhysicalEntity32
component: RNA Polymerase II holoenzyme complex (hyperphosphorylated) (name copied from entity in Homo sapiens)
xref: UnificationXref424
cellular location: GO:0005654
comment: Reactome DB_ID: 3660217

RelationshipXref1009
type: RelationshipXref
id: GO:0006457
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1008
type: RelationshipXref
id: GO:0032201
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1007
type: RelationshipXref
id: GO:0000723
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1006
type: RelationshipXref
id: GO:0000722
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1004
type: RelationshipXref
id: GO:0003720
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1005
type: RelationshipXref
id: 3660701
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660701

RelationshipXref1002
type: RelationshipXref
id: GO:0000278
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1003
type: RelationshipXref
id: GO:0007004
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1000
type: RelationshipXref
id: GO:0000910
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1001
type: RelationshipXref
id: GO:0000087
db: GENE ONTOLOGY
relationship type: MI:0359

UnificationXref1603
type: UnificationXref
id: 3662747
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662747

UnificationXref1604
type: UnificationXref
id: O94408
db: UniProt

UnificationXref1605
type: UnificationXref
id: 3662743
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662743

UnificationXref1606
type: UnificationXref
id: O14352
db: UniProt

UnificationXref1607
type: UnificationXref
id: 3662734
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662734

UnificationXref1608
type: UnificationXref
id: 3662748
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662748

UnificationXref1609
type: UnificationXref
id: Q9UUI1
db: UniProt

pol II open pre-initiation complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry174
component stoichiometry: Stoichiometry175
component stoichiometry: Stoichiometry170
component stoichiometry: Stoichiometry169
component stoichiometry: Stoichiometry173
component stoichiometry: Stoichiometry190
component stoichiometry: Stoichiometry165
component: PhysicalEntity42
component: Protein84
component: TFIID (name copied from entity in Homo sapiens)
component: TFIIH (name copied from entity in Homo sapiens)
component: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
component: TFIIE (name copied from entity in Homo sapiens)
component: TFIIA (name copied from entity in Homo sapiens)
xref: UnificationXref507
cellular location: GO:0005654
comment: Reactome DB_ID: 3659963

http://identifiers.org/pubmed/21173190
type: PublicationXref
id: 21173190
author: Agarwal, AK
author: Prasad, SS
author: Garg, A
db: Pubmed
title: Enzymatic activities of the human AGPAT isoform 3 and isoform 5: localization of AGPAT5 to mitochondria
source: J Lipid Res 52:451-62
year: 2011

TFIIA (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry167
component stoichiometry: Stoichiometry166
component stoichiometry: Stoichiometry168
component: Protein83
component: Protein82
component: Protein81
xref: UnificationXref495
cellular location: GO:0005654
comment: Reactome DB_ID: 3659574

TFIID (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry164
component stoichiometry: Stoichiometry159
component stoichiometry: Stoichiometry157
component stoichiometry: Stoichiometry155
component stoichiometry: Stoichiometry162
component stoichiometry: Stoichiometry160
component stoichiometry: Stoichiometry158
component stoichiometry: Stoichiometry161
component stoichiometry: Stoichiometry156
component stoichiometry: Stoichiometry163
component stoichiometry: Stoichiometry154
component: PhysicalEntity39
component: Protein75
component: PhysicalEntity40
component: Protein79
component: Protein78
component: Protein77
component: Protein71
component: Protein80
component: PhysicalEntity38
component: Protein76
component: Protein72
xref: UnificationXref489
cellular location: GO:0005654
comment: Reactome DB_ID: 3659619

RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry189
component stoichiometry: Stoichiometry176
component: TFIIF (name copied from entity in Homo sapiens)
component: RNA Polymerase II holoenzyme complex (unphosphorylated) (name copied from entity in Homo sapiens)
xref: UnificationXref506
cellular location: GO:0005654
comment: Reactome DB_ID: 3658608

TFIIE (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry172
component stoichiometry: Stoichiometry171
component: PhysicalEntity41
component: Protein85
xref: UnificationXref501
cellular location: GO:0005654
comment: Reactome DB_ID: 3659625

Methylation
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction473
pathway component: BiochemicalReaction498
pathway component: BiochemicalReaction472
evidence: Evidence828
xref: UnificationXref5462
xref: UnificationXref5461
xref: RelationshipXref758
pathway order: PathwayStep779
pathway order: PathwayStep818
pathway order: PathwayStep780
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

pol II closed pre-initiation complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry198
component stoichiometry: Stoichiometry200
component stoichiometry: Stoichiometry199
component: pol II promoter:TFIID:TFIIA:TFIIB:Pol II:TFIIF complex (name copied from entity in Homo sapiens)
component: TFIIH (name copied from entity in Homo sapiens)
component: TFIIE (name copied from entity in Homo sapiens)
xref: UnificationXref513
cellular location: GO:0005654
comment: Reactome DB_ID: 3659967

RNA Polymerase II holoenzyme complex (unphosphorylated) (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry181
component stoichiometry: Stoichiometry188
component stoichiometry: Stoichiometry184
component stoichiometry: Stoichiometry182
component stoichiometry: Stoichiometry178
component stoichiometry: Stoichiometry186
component stoichiometry: Stoichiometry185
component stoichiometry: Stoichiometry177
component stoichiometry: Stoichiometry183
component stoichiometry: Stoichiometry187
component stoichiometry: Stoichiometry180
component stoichiometry: Stoichiometry179
component: Protein47
component: Protein57
component: Protein86
component: Protein48
component: Protein50
component: Protein58
component: Protein49
component: Protein56
component: Protein54
component: Protein52
component: Protein55
component: Protein53
xref: UnificationXref505
cellular location: GO:0005654
comment: Reactome DB_ID: 3658607

pol II promoter:TFIID:TFIIA:TFIIB complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry196
component stoichiometry: Stoichiometry193
component stoichiometry: Stoichiometry192
component: Protein84
component: pol II promoter:TFIID complex (name copied from entity in Homo sapiens)
component: TFIIA (name copied from entity in Homo sapiens)
xref: UnificationXref511
cellular location: GO:0005654
comment: Reactome DB_ID: 3659859

pol II promoter:TFIID:TFIIA:TFIIB:Pol II:TFIIF complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry197
component stoichiometry: Stoichiometry191
component: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
component: pol II promoter:TFIID:TFIIA:TFIIB complex (name copied from entity in Homo sapiens)
xref: UnificationXref512
cellular location: GO:0005654
comment: Reactome DB_ID: 3659860

pol II promoter:TFIID complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry194
component stoichiometry: Stoichiometry195
component: TFIID (name copied from entity in Homo sapiens)
component: PhysicalEntity43
xref: UnificationXref510
cellular location: GO:0005654
comment: Reactome DB_ID: 3659858

RelationshipXref1070
type: RelationshipXref
id: GO:0004583
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1072
type: RelationshipXref
id: 3662978
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662978

RelationshipXref1071
type: RelationshipXref
id: 3663016
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663016

RelationshipXref1074
type: RelationshipXref
id: GO:0006488
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1073
type: RelationshipXref
id: 3662990
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662990

RelationshipXref1076
type: RelationshipXref
id: 3663259
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663259

RelationshipXref1075
type: RelationshipXref
id: GO:0004573
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1078
type: RelationshipXref
id: 3663402
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663402

RelationshipXref1077
type: RelationshipXref
id: GO:0004559
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1079
type: RelationshipXref
id: GO:0003980
db: GENE ONTOLOGY
relationship type: MI:0355

Pol II initiation complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry208
component stoichiometry: Stoichiometry204
component stoichiometry: Stoichiometry205
component stoichiometry: Stoichiometry207
component stoichiometry: Stoichiometry212
component stoichiometry: Stoichiometry206
component: Protein84
component: TFIID (name copied from entity in Homo sapiens)
component: RNA Polymearse II:NTP:TFIIF complex (name copied from entity in Homo sapiens)
component: TFIIE (name copied from entity in Homo sapiens)
component: PhysicalEntity44
component: TFIIA (name copied from entity in Homo sapiens)
xref: UnificationXref544
cellular location: GO:0005654
comment: Reactome DB_ID: 3659965

pol II promoter:TFIID:TFIIA:TFIIB:Pol II:TFIIF:TFIIE complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry202
component stoichiometry: Stoichiometry201
component: pol II promoter:TFIID:TFIIA:TFIIB:Pol II:TFIIF complex (name copied from entity in Homo sapiens)
component: TFIIE (name copied from entity in Homo sapiens)
xref: UnificationXref520
cellular location: GO:0005654
comment: Reactome DB_ID: 3660149

pol II transcription complex containing 3 Nucleotide long transcript (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry231
component stoichiometry: Stoichiometry230
component stoichiometry: Stoichiometry228
component stoichiometry: Stoichiometry229
component stoichiometry: Stoichiometry232
component stoichiometry: Stoichiometry227
component stoichiometry: Stoichiometry233
component: Protein84
component: TFIID (name copied from entity in Homo sapiens)
component: TFIIH (name copied from entity in Homo sapiens)
component: PhysicalEntity47
component: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
component: TFIIE (name copied from entity in Homo sapiens)
component: TFIIA (name copied from entity in Homo sapiens)
xref: UnificationXref564
cellular location: GO:0005654
comment: Reactome DB_ID: 3659950

pol II transcription complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry220
component stoichiometry: Stoichiometry224
component stoichiometry: Stoichiometry222
component stoichiometry: Stoichiometry221
component stoichiometry: Stoichiometry225
component stoichiometry: Stoichiometry223
component stoichiometry: Stoichiometry226
component: Protein84
component: TFIID (name copied from entity in Homo sapiens)
component: TFIIH (name copied from entity in Homo sapiens)
component: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
component: TFIIE (name copied from entity in Homo sapiens)
component: TFIIA (name copied from entity in Homo sapiens)
component: PhysicalEntity46
xref: UnificationXref557
cellular location: GO:0005654
comment: Reactome DB_ID: 3659626

Pol II Initiation complex with phosphodiester-PPi intermediate (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry215
component stoichiometry: Stoichiometry219
component stoichiometry: Stoichiometry213
component stoichiometry: Stoichiometry218
component stoichiometry: Stoichiometry216
component stoichiometry: Stoichiometry217
component stoichiometry: Stoichiometry214
component: Protein84
component: TFIID (name copied from entity in Homo sapiens)
component: TFIIH (name copied from entity in Homo sapiens)
component: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
component: TFIIE (name copied from entity in Homo sapiens)
component: TFIIA (name copied from entity in Homo sapiens)
component: PhysicalEntity45
xref: UnificationXref549
cellular location: GO:0005654
comment: Reactome DB_ID: 3659969

http://identifiers.org/pubmed/8167409
type: PublicationXref
id: 8167409
author: McMahon, Jill A
author: Smolich, Beverly D
author: McMahon, Andrew P
author: Papkoff, Jackie
db: Pubmed
title: Wnt family proteins are secreted and associated with the cell surface
source: Mol. Biol. Cell 4:1267-75
year: 1993

RNA Polymearse II:NTP:TFIIF complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry211
component stoichiometry: Stoichiometry210
component stoichiometry: Stoichiometry209
component: TFIIH (name copied from entity in Homo sapiens)
component: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
component: SmallMolecule10
xref: UnificationXref543
cellular location: GO:0005654
comment: Reactome DB_ID: 3659964

Pol II transcription complex containing extruded transcript to +30 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry248
component stoichiometry: Stoichiometry249
component stoichiometry: Stoichiometry250
component: TFIIH (name copied from entity in Homo sapiens)
component: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
component: PhysicalEntity51
xref: UnificationXref582
cellular location: GO:0005654
comment: Reactome DB_ID: 3660046

pol II transcription complex containing 11 nucleotide long transcript (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry246
component stoichiometry: Stoichiometry245
component stoichiometry: Stoichiometry247
component: TFIIH (name copied from entity in Homo sapiens)
component: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
component: PhysicalEntity50
xref: UnificationXref577
cellular location: GO:0005654
comment: Reactome DB_ID: 3660037

pol II transcription complex containing 9 nucleotide long transcript (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry242
component stoichiometry: Stoichiometry243
component stoichiometry: Stoichiometry241
component: PhysicalEntity49
component: TFIIH (name copied from entity in Homo sapiens)
component: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
xref: UnificationXref574
cellular location: GO:0005654
comment: Reactome DB_ID: 3659974

pol II transcription complex containing 4 nucleotide long transcript (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry238
component stoichiometry: Stoichiometry237
component stoichiometry: Stoichiometry234
component stoichiometry: Stoichiometry239
component stoichiometry: Stoichiometry235
component stoichiometry: Stoichiometry236
component: PhysicalEntity48
component: TFIID (name copied from entity in Homo sapiens)
component: TFIIH (name copied from entity in Homo sapiens)
component: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
component: TFIIE (name copied from entity in Homo sapiens)
component: TFIIA (name copied from entity in Homo sapiens)
xref: UnificationXref569
cellular location: GO:0005654
comment: Reactome DB_ID: 3659972

RelationshipXref1063
type: RelationshipXref
id: 3662966
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662966

RelationshipXref1062
type: RelationshipXref
id: GO:0000026
db: GENE ONTOLOGY
relationship type: MI:0355

http://identifiers.org/pubmed/16483939
type: PublicationXref
id: 16483939
author: Pacek, M
author: Kubota, Y
author: Takisawa, H
author: Tutter, AV
author: Walter, JC
db: Pubmed
title: Localization of MCM2-7, Cdc45, and GINS to the site of DNA unwinding during eukaryotic DNA replication
source: Mol Cell 21:581-7
year: 2006

RelationshipXref1061
type: RelationshipXref
id: 3663083
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663083

RelationshipXref1060
type: RelationshipXref
id: GO:0000009
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1067
type: RelationshipXref
id: 3663054
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663054

RelationshipXref1066
type: RelationshipXref
id: 3662972
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662972

RelationshipXref1065
type: RelationshipXref
id: 3663042
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663042

RelationshipXref1064
type: RelationshipXref
id: GO:0034202
db: GENE ONTOLOGY
relationship type: MI:0355

http://identifiers.org/pubmed/9110970
type: PublicationXref
id: 9110970
author: Lingner, J
author: Shevchenko, A
author: Hughes, TR
author: Lundblad, V
author: Mann, M
author: Cech, TR
db: Pubmed
title: Reverse transcriptase motifs in the catalytic subunit of telomerase
source: Science 276:561-7
year: 1997

RelationshipXref1069
type: RelationshipXref
id: 3663002
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663002

RelationshipXref1068
type: RelationshipXref
id: GO:0000030
db: GENE ONTOLOGY
relationship type: MI:0355

CE:Pol II CTD:Spt5 complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry277
component stoichiometry: Stoichiometry276
component stoichiometry: Stoichiometry275
component stoichiometry: Stoichiometry274
component stoichiometry: Stoichiometry273
component stoichiometry: Stoichiometry272
component: Protein64
component: RNA polymerase II (phosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
component: PhysicalEntity52
component: TFIIH (name copied from entity in Homo sapiens)
component: Protein87
component: PhysicalEntity51
xref: UnificationXref602
cellular location: GO:0005654
comment: Reactome DB_ID: 3660059

http://identifiers.org/pubmed/3049610
type: PublicationXref
id: 3049610
author: Smith, BL
author: Agre, P
author: Denker, BM
author: Kuhajda, FP
db: Pubmed
title: Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules
source: J Biol Chem 263:15634-42
year: 1988

RNA Pol II with phosphorylated CTD: CE complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry270
component stoichiometry: Stoichiometry271
component stoichiometry: Stoichiometry268
component stoichiometry: Stoichiometry269
component: RNA polymerase II (phosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
component: PhysicalEntity52
component: TFIIH (name copied from entity in Homo sapiens)
component: PhysicalEntity51
xref: UnificationXref597
cellular location: GO:0005654
comment: Reactome DB_ID: 3660044

RNA Polymerase II (phosphorylated):TFIIF:capped pre-mRNA (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry280
component stoichiometry: Stoichiometry279
component: RNA polymerase II (phosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
component: PhysicalEntity37
xref: UnificationXref607
cellular location: GO:0005654
comment: Reactome DB_ID: 3658604

capped pre-mRNA:CBC:RNA Pol II (phosphorylated) complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry281
component stoichiometry: Stoichiometry278
component: RNA Polymerase II (phosphorylated):TFIIF:capped pre-mRNA (name copied from entity in Homo sapiens)
component: Cap Binding Complex (CBC) (name copied from entity in Homo sapiens)
xref: UnificationXref608
cellular location: GO:0005654
comment: Reactome DB_ID: 3658605

Pol II transcription complex with (ser5) phosphorylated CTD containing extruded transcript to +30 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry265
component stoichiometry: Stoichiometry267
component stoichiometry: Stoichiometry266
component: RNA polymerase II (phosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
component: TFIIH (name copied from entity in Homo sapiens)
component: PhysicalEntity51
xref: UnificationXref593
cellular location: GO:0005654
comment: Reactome DB_ID: 3660047

RNA Polymerase II holoenzyme complex (phosphorylated) (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry252
component stoichiometry: Stoichiometry258
component stoichiometry: Stoichiometry253
component stoichiometry: Stoichiometry257
component stoichiometry: Stoichiometry259
component stoichiometry: Stoichiometry256
component stoichiometry: Stoichiometry261
component stoichiometry: Stoichiometry260
component stoichiometry: Stoichiometry262
component stoichiometry: Stoichiometry254
component stoichiometry: Stoichiometry251
component stoichiometry: Stoichiometry255
component: Protein47
component: Protein69
component: Protein57
component: Protein48
component: Protein50
component: Protein58
component: Protein49
component: Protein56
component: Protein54
component: Protein52
component: Protein55
component: Protein53
xref: UnificationXref591
cellular location: GO:0005654
comment: Reactome DB_ID: 3658593

RNA polymerase II (phosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry264
component stoichiometry: Stoichiometry263
component: RNA Polymerase II holoenzyme complex (phosphorylated) (name copied from entity in Homo sapiens)
component: TFIIF (name copied from entity in Homo sapiens)
xref: UnificationXref592
cellular location: GO:0005654
comment: Reactome DB_ID: 3658603

http://identifiers.org/pubmed/16339074
type: PublicationXref
id: 16339074
author: Supakorndej, T
author: Tomlinson, RL
author: Terns, RM
author: Ziegler, TD
author: Terns, MP
db: Pubmed
title: Cell cycle-regulated trafficking of human telomerase to telomeres
source: Mol Biol Cell 17:955-65
year: 2006

Active RNA Polymerase I (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry288
component stoichiometry: Stoichiometry289
component: Protein92
component: RNA Polymerase I Holoenzyme (name copied from entity in Homo sapiens)
xref: UnificationXref632
cellular location: GO:0005654
comment: Reactome DB_ID: 3659391

RNA Polymerase I Holoenzyme (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry285
component stoichiometry: Stoichiometry282
component stoichiometry: Stoichiometry284
component stoichiometry: Stoichiometry286
component stoichiometry: Stoichiometry287
component stoichiometry: Stoichiometry283
component: Protein88
component: Protein89
component: Protein48
component: Protein50
component: Protein90
component: Protein91
xref: UnificationXref627
cellular location: GO:0005654
comment: Reactome DB_ID: 3659390

RNA Polymerase I Transcription Initiation complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry299
component stoichiometry: Stoichiometry301
component stoichiometry: Stoichiometry300
component: Acetylayed SL1:PhosUBF-1:rDNA promoter (name copied from entity in Homo sapiens)
component: TFIIH (name copied from entity in Homo sapiens)
component: Active RNA Polymerase I (name copied from entity in Homo sapiens)
xref: UnificationXref650
cellular location: GO:0005654
comment: Reactome DB_ID: 3659439

RelationshipXref1050
type: RelationshipXref
id: 3663048
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663048

RelationshipXref1052
type: RelationshipXref
id: GO:0003975
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1051
type: RelationshipXref
id: GO:0018279
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1058
type: RelationshipXref
id: GO:0000033
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1057
type: RelationshipXref
id: 3663061
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663061

RelationshipXref1059
type: RelationshipXref
id: 3663036
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663036

RelationshipXref1054
type: RelationshipXref
id: GO:0004577
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1053
type: RelationshipXref
id: 3662984
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662984

RelationshipXref1056
type: RelationshipXref
id: GO:0004578
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1055
type: RelationshipXref
id: 3663030
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663030

HsRPC4:HsRPC5 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry308
component stoichiometry: Stoichiometry307
component: PhysicalEntity63
component: PhysicalEntity62
xref: UnificationXref673
cellular location: GO:0005654
comment: Reactome DB_ID: 3660430

RNA Polymerase III Holoenzyme (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry326
component stoichiometry: Stoichiometry313
component stoichiometry: Stoichiometry317
component stoichiometry: Stoichiometry320
component stoichiometry: Stoichiometry322
component stoichiometry: Stoichiometry312
component stoichiometry: Stoichiometry321
component stoichiometry: Stoichiometry310
component stoichiometry: Stoichiometry309
component stoichiometry: Stoichiometry311
component stoichiometry: Stoichiometry315
component stoichiometry: Stoichiometry314
component stoichiometry: Stoichiometry316
component: Protein48
component: Protein50
component: HsRPC6:HsRPC3:HsRPC7 (name copied from entity in Homo sapiens)
component: Protein94
component: Protein95
component: Protein56
component: Protein55
component: HsRPC8:HsRPC9 (name copied from entity in Homo sapiens)
component: HsRPC4:HsRPC5 (name copied from entity in Homo sapiens)
component: Protein89
component: Protein49
component: Protein93
component: Protein91
xref: UnificationXref690
cellular location: GO:0005654
comment: Reactome DB_ID: 3660445

Elongating RNA Polymerase III Transcription Complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry327
component stoichiometry: Stoichiometry306
component: PhysicalEntity61
component: RNA Polymerase III Holoenzyme (name copied from entity in Homo sapiens)
xref: UnificationXref691
cellular location: GO:0005654
comment: Reactome DB_ID: 3660446

RNA Polymerase I promoter escape complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry304
component stoichiometry: Stoichiometry305
component stoichiometry: Stoichiometry302
component stoichiometry: Stoichiometry303
component: PhysicalEntity58
component: Acetylated SL1 (name copied from entity in Homo sapiens)
component: TFIIH (name copied from entity in Homo sapiens)
component: RNA Polymerase I Holoenzyme (name copied from entity in Homo sapiens)
xref: UnificationXref652
cellular location: GO:0005654
comment: Reactome DB_ID: 3659441

SL1 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry295
component stoichiometry: Stoichiometry294
component stoichiometry: Stoichiometry296
component: PhysicalEntity55
component: PhysicalEntity57
component: PhysicalEntity56
xref: UnificationXref647
cellular location: GO:0005654
comment: Reactome DB_ID: 3659396

Acetylated SL1 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry297
component stoichiometry: Stoichiometry293
component: SmallMolecule15
component: SL1 (name copied from entity in Homo sapiens)
xref: UnificationXref648
cellular location: GO:0005654
comment: Reactome DB_ID: 3659397

http://identifiers.org/pubmed/17008356
type: PublicationXref
id: 17008356
author: Monroy, N
author: Kretz, C
author: Mandel, JL
author: Payrastre, B
author: Dondaine, N
author: Tronchère, H
author: Zanoteli, E
author: Rohde, HM
author: Tosch, V
author: Laporte, J
db: Pubmed
title: A novel PtdIns3P and PtdIns(3,5)P2 phosphatase with an inactivating variant in centronuclear myopathy
source: Hum Mol Genet 15:3098-106
year: 2006

Phosphorylated UBF-1:rDNA promoter (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry290
component stoichiometry: Stoichiometry291
component: PhysicalEntity54
component: PhysicalEntity53
xref: UnificationXref640
cellular location: GO:0005654
comment: Reactome DB_ID: 3659399

Acetylayed SL1:PhosUBF-1:rDNA promoter (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry292
component stoichiometry: Stoichiometry298
component: Acetylated SL1 (name copied from entity in Homo sapiens)
component: Phosphorylated UBF-1:rDNA promoter (name copied from entity in Homo sapiens)
xref: UnificationXref649
cellular location: GO:0005654
comment: Reactome DB_ID: 3659400

http://identifiers.org/pubmed/8325892
type: PublicationXref
id: 8325892
author: Froguel, P
author: Velho, G
author: Stoffel, M
author: Vionnet, N
author: Cohen, D
author: Takeda, J
author: St. Charles, R
author: Bell, GI
author: Vaxillaire, M
author: Pilkis, SJ
author: Weber, IT
author: Gidh-Jain, M
author: Shimada, F
author: Nishi, S
author: Harrison, RW
author: Makino, H
author: Xu, LZ
db: Pubmed
title: Structure/function studies of human beta-cell glucokinase. Enzymatic properties of a sequence polymorphism, mutations associated with diabetes, and other site-directed mutants.
source: J Biol Chem 268:15200-4
year: 1993

HsRPC6:HsRPC3:HsRPC7 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry325
component stoichiometry: Stoichiometry323
component stoichiometry: Stoichiometry324
component: PhysicalEntity65
component: Protein97
component: Protein98
xref: UnificationXref689
cellular location: GO:0005654
comment: Reactome DB_ID: 3660440

HsRPC8:HsRPC9 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry318
component stoichiometry: Stoichiometry319
component: PhysicalEntity64
component: Protein96
xref: UnificationXref683
cellular location: GO:0005654
comment: Reactome DB_ID: 3660427

RelationshipXref1041
type: RelationshipXref
id: GO:0006048
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1040
type: RelationshipXref
id: 3663024
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663024

http://identifiers.org/pubmed/22649417
type: PublicationXref
id: 22649417
author: Siddle, Kenneth
db: Pubmed
title: Molecular basis of signaling specificity of insulin and IGF receptors: neglected corners and recent advances
source: Front Endocrinol (Lausanne) 3:34
year: 2012

RelationshipXref1049
type: RelationshipXref
id: GO:0004581
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1048
type: RelationshipXref
id: GO:0009298
db: GENE ONTOLOGY
relationship type: MI:0359

RelationshipXref1047
type: RelationshipXref
id: 3663072
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663072

RelationshipXref1046
type: RelationshipXref
id: GO:0004475
db: GENE ONTOLOGY
relationship type: MI:0355

RelationshipXref1045
type: RelationshipXref
id: 3663010
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663010

RelationshipXref1044
type: RelationshipXref
id: GO:0004615
db: GENE ONTOLOGY
relationship type: MI:0355

5-PP-InsP5
type: SmallMoleculeReference
name: 5-PP-InsP5 [ChEBI:2119]
name: 5-Diphosphoinositol pentakisphosphate
xref: UnificationXref2603

RelationshipXref1043
type: RelationshipXref
id: 3663250
db: Reactome Database ID Release 45
relationship type: RelationshipTypeVocabulary3
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663250

RelationshipXref1042
type: RelationshipXref
id: GO:0004476
db: GENE ONTOLOGY
relationship type: MI:0355

http://identifiers.org/pubmed/1939222
type: PublicationXref
id: 1939222
author: Cox, TM
author: Gardner, LC
author: Smith, SJ
db: Pubmed
title: Biosynthesis of delta-aminolevulinic acid and the regulation of heme formation by immature erythroid cells in man
source: J Biol Chem 266:22010-8
year: 1991

http://identifiers.org/pubmed/12655297
type: PublicationXref
id: 12655297
author: Janicke, RU
author: Schulze-Osthoff, K
author: Fischer, U
db: Pubmed
title: Many cuts to ruin: a comprehensive update of caspase substrates
source: Cell Death Differ 10:76-100
year: 2003

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43052
data source: Provenance1
name: Rho GTPase-activating protein 36
name: RHG36_HUMAN
name: ARHGAP36
xref: UnificationXref1384
feature: FragmentFeature268
cellular location: GO:0005829
comment: Reactome DB_ID: 3661559
display name: O43052

http://identifiers.org/pubmed/18240029
type: PublicationXref
id: 18240029
author: Luttrell, LM
db: Pubmed
title: Reviews in molecular biology and biotechnology: transmembrane signaling by G protein-coupled receptors
source: Mol Biotechnol 39:239-64
year: 2008

ARHGAP19(2-494)
type: Protein
entity reference: O43052
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: ARHGAP19
xref: UnificationXref1375
feature: FragmentFeature261
cellular location: GO:0005829
comment: Reactome DB_ID: 3661550
display name: O43052

ARHGAP30
type: Protein
entity reference: O74360
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1378
feature: FragmentFeature264
cellular location: GO:0005829
comment: Reactome DB_ID: 3661553
display name: O74360

Homologues of ARHGAP30
type: Protein
data source: Provenance1
member physical entity: ARHGAP30
xref: UnificationXref1380
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3661555

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43052
data source: Provenance1
name: RHG28_HUMAN
name: Rho GTPase-activating protein 28
name: ARHGAP28
xref: UnificationXref1377
feature: FragmentFeature263
cellular location: GO:0005829
comment: Reactome DB_ID: 3661552
display name: O43052

RHG23_HUMAN
type: Protein
entity reference: O94466
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Rho GTPase-activating protein 23
name: ARHGAP23
xref: UnificationXref1376
feature: FragmentFeature262
cellular location: GO:0005829
comment: Reactome DB_ID: 3661551
display name: O94466

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14014
data source: Provenance1
name: RHG33_HUMAN
name: ARHGAP33
name: Rho GTPase-activating protein 33
xref: UnificationXref1382
feature: FragmentFeature267
cellular location: GO:0005829
comment: Reactome DB_ID: 3661557
display name: O14014

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74360
data source: Provenance1
name: RHG33_HUMAN
name: ARHGAP33
name: Rho GTPase-activating protein 33
xref: UnificationXref1381
feature: FragmentFeature266
cellular location: GO:0005829
comment: Reactome DB_ID: 3661556
display name: O74360

Homologues of ARHGAP33
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1383
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3661558

ARHGAP30
type: Protein
entity reference: O14014
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1379
feature: FragmentFeature265
cellular location: GO:0005829
comment: Reactome DB_ID: 3661554
display name: O14014

http://identifiers.org/pubmed/16321791
type: PublicationXref
id: 16321791
author: Joseph, JW
author: MacDonald, PE
author: Rorsman, P
db: Pubmed
title: Glucose-sensing mechanisms in pancreatic beta-cells
source: Philos Trans R Soc Lond B Biol Sci 360:2211-25
year: 2005

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10164
data source: Provenance1
name: RHG12_HUMAN
name: Rho GTPase-activating protein 12
name: ARHGAP12
xref: UnificationXref1373
feature: FragmentFeature259
cellular location: GO:0005829
comment: Reactome DB_ID: 3661548
display name: Q10164

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43052
data source: Provenance1
name: ARHGAP18
xref: UnificationXref1374
feature: FragmentFeature260
cellular location: GO:0005829
comment: Reactome DB_ID: 3661549
display name: O43052

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43052
data source: Provenance1
name: O43052
name: STARD8
xref: UnificationXref1366
feature: FragmentFeature252
cellular location: GO:0005829
comment: Reactome DB_ID: 3661541
display name: STAR8

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10164
data source: Provenance1
name: Q10164
xref: UnificationXref1365
feature: FragmentFeature251
cellular location: GO:0005829
comment: Reactome DB_ID: 3661540
display name: SYDE2

C20orf95 protein
type: Protein
entity reference: O43052
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: ARHGAP40
xref: UnificationXref1368
feature: FragmentFeature254
cellular location: GO:0005829
comment: Reactome DB_ID: 3661543
display name: O43052

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43052
data source: Provenance1
name: StAR-related lipid transfer protein 13
name: STA13_HUMAN
name: STARD13
xref: UnificationXref1367
feature: FragmentFeature253
cellular location: GO:0005829
comment: Reactome DB_ID: 3661542
display name: O43052

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43052
data source: Provenance1
name: ARHGAP6
name: Rho GTPase-activating protein 6
name: RHG06_HUMAN
xref: UnificationXref1370
feature: FragmentFeature256
cellular location: GO:0005829
comment: Reactome DB_ID: 3661545
display name: O43052

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10164
data source: Provenance1
name: Rho GTPase-activating protein SYDE1
name: SYDE1_HUMAN
name: Q10164
xref: UnificationXref1369
feature: FragmentFeature255
cellular location: GO:0005829
comment: Reactome DB_ID: 3661544
display name: SYDE1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43052
data source: Provenance1
name: ARHGAP11B
xref: UnificationXref1372
feature: FragmentFeature258
cellular location: GO:0005829
comment: Reactome DB_ID: 3661547
display name: O43052

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10164
data source: Provenance1
name: RHG09_HUMAN
name: Rho GTPase-activating protein 9
name: ARHGAP9
xref: UnificationXref1371
feature: FragmentFeature257
cellular location: GO:0005829
comment: Reactome DB_ID: 3661546
display name: Q10164

http://identifiers.org/pubmed/9792106
type: PublicationXref
id: 9792106
author: Hazlett, TL
author: Sanchez, SA
author: Jameson, DM
author: Brunet, JE
db: Pubmed
title: Aggregation states of mitochondrial malate dehydrogenase
source: Protein Sci 7:2184-2189
year: 1998

http://identifiers.org/pubmed/8246982
type: PublicationXref
id: 8246982
author: Wagner, BJ
author: Brewer, G
author: DeHaven, K
author: Schaefer, AW
author: Long, L
author: Crater, D
author: Ehrenman, K
author: Zhang, W
author: DeMaria, CT
db: Pubmed
title: Purification, characterization, and cDNA cloning of an AU-rich element RNA-binding protein, AUF1
source: Mol Cell Biol 13:7652-65
year: 1993

http://identifiers.org/pubmed/15215243
type: PublicationXref
id: 15215243
author: Graf, SA
author: Shirihai, OS
author: Corson, ED
author: Haigh, SE
db: Pubmed
title: Targeting, import, and dimerization of a mammalian mitochondrial ATP binding cassette (ABC) transporter, ABCB10 (ABC-me)
source: J Biol Chem 279:42954-63
year: 2004

Stoichiometry805
type: Stoichiometry
physical entity: PhysicalEntity132
stoichiometric coefficient: 1.0

Stoichiometry806
type: Stoichiometry
physical entity: NF-Y (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry807
type: Stoichiometry
physical entity: PhysicalEntity133
stoichiometric coefficient: 1.0

Stoichiometry808
type: Stoichiometry
physical entity: SREBP1A/1C/2 Dimer (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry809
type: Stoichiometry
physical entity: SmallMolecule209
stoichiometric coefficient: 1.0

Stoichiometry800
type: Stoichiometry
physical entity: NF-Y (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry801
type: Stoichiometry
physical entity: SREBP1A/2 Dimer (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry802
type: Stoichiometry
physical entity: PhysicalEntity131
stoichiometric coefficient: 1.0

Stoichiometry803
type: Stoichiometry
physical entity: NF-Y (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry804
type: Stoichiometry
physical entity: SREBP1A/2 Dimer (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

UniProt:P56329
type: ProteinReference
xref: UnificationXref7312
organism: BioSource1

Stoichiometry818
type: Stoichiometry
physical entity: Protein719
stoichiometric coefficient: 1.0

Stoichiometry819
type: Stoichiometry
physical entity: SmallMolecule222
stoichiometric coefficient: 1.0

Stoichiometry816
type: Stoichiometry
physical entity: SmallMolecule222
stoichiometric coefficient: 1.0

Stoichiometry817
type: Stoichiometry
physical entity: Note: the coordinates are copied over from Homo sapiens.
stoichiometric coefficient: 1.0

Stoichiometry814
type: Stoichiometry
physical entity: SmallMolecule222
stoichiometric coefficient: 1.0

Stoichiometry815
type: Stoichiometry
physical entity: Note: the coordinates are copied over from Homo sapiens.
stoichiometric coefficient: 1.0

Stoichiometry812
type: Stoichiometry
physical entity: Protein717
stoichiometric coefficient: 2.0

Stoichiometry813
type: Stoichiometry
physical entity: Protein718
stoichiometric coefficient: 2.0

Stoichiometry810
type: Stoichiometry
physical entity: Protein709
stoichiometric coefficient: 1.0

Stoichiometry811
type: Stoichiometry
physical entity: Protein711
stoichiometric coefficient: 2.0

Stoichiometry827
type: Stoichiometry
physical entity: Protein736
stoichiometric coefficient: 1.0

Stoichiometry828
type: Stoichiometry
physical entity: Mg2+/Mn2+
stoichiometric coefficient: 1.0

Stoichiometry829
type: Stoichiometry
physical entity: Protein750
stoichiometric coefficient: 1.0

Stoichiometry823
type: Stoichiometry
physical entity: SmallMolecule232
stoichiometric coefficient: 3.0

Stoichiometry824
type: Stoichiometry
physical entity: SmallMolecule233
stoichiometric coefficient: 3.0

Stoichiometry825
type: Stoichiometry
physical entity: Protein732
stoichiometric coefficient: 2.0

Stoichiometry826
type: Stoichiometry
physical entity: Protein733
stoichiometric coefficient: 2.0

Stoichiometry820
type: Stoichiometry
physical entity: SmallMolecule225
stoichiometric coefficient: 1.0

Stoichiometry821
type: Stoichiometry
physical entity: Protein720
stoichiometric coefficient: 1.0

Stoichiometry822
type: Stoichiometry
physical entity: Protein723
stoichiometric coefficient: 1.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74440
data source: Provenance1
name: 26S proteasome non-ATPase regulatory subunit 7
name: 26S proteasome regulatory subunit S12
name: PSMD7(2-324)
name: Mov34 protein homolog
name: Proteasome subunit p40
xref: UnificationXref1674
feature: FragmentFeature318
cellular location: GO:0005829
comment: Reactome DB_ID: 3657862
display name: O74440

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9P7S2
data source: Provenance1
name: 26S proteasome regulatory subunit S9
name: 26S proteasome non-ATPase regulatory subunit 11
name: 26S proteasome regulatory subunit p44.5
name: Q9P7S2
xref: UnificationXref1672
feature: FragmentFeature317
cellular location: GO:0005829
comment: Reactome DB_ID: 3657834
display name: PSMD11

26S proteasome regulatory subunit p55
type: Protein
entity reference: Q9UTM3
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: 26S proteasome non-ATPase regulatory subunit 12
name: Q9UTM3
xref: UnificationXref1678
feature: FragmentFeature320
cellular location: GO:0005829
comment: Reactome DB_ID: 3657840
display name: PSMD12

Multicatalytic endopeptidase complex subunit C9
type: Protein
entity reference: Q09682
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Proteasome subunit L
name: Macropain subunit C9
name: Proteasome subunit alpha type 4
name: Q09682
name: Proteasome component C9
xref: UnificationXref1676
feature: FragmentFeature319
cellular location: GO:0005829
comment: Reactome DB_ID: 3657755
display name: PSMA4

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P41878
data source: Provenance1
name: P41878
name: 26S proteasome-associated pad1 homolog
xref: UnificationXref1664
feature: FragmentFeature314
cellular location: GO:0005829
comment: Reactome DB_ID: 3657739
display name: PSMD14

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P50524
data source: Provenance1
name: P50524
name: 26S proteasome regulatory subunit S14
name: 26S proteasome non-ATPase regulatory subunit 8
name: PSMD8
xref: UnificationXref1670
feature: FragmentFeature316
cellular location: GO:0005829
comment: Reactome DB_ID: 3657866
display name: p31

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O59770
data source: Provenance1
name: Multicatalytic endopeptidase complex subunit C8
name: Proteasome subunit alpha type 3
name: O59770
name: Macropain subunit C8
name: Proteasome component C8
xref: UnificationXref1666
feature: FragmentFeature315
cellular location: GO:0005829
comment: Reactome DB_ID: 3657751
display name: PSMA3

http://identifiers.org/pubmed/17560368
type: PublicationXref
id: 17560368
author: Peters, L
author: Meister, G
db: Pubmed
title: Argonaute proteins: mediators of RNA silencing
source: Mol Cell 26:611-23
year: 2007

Q9UQY2
type: Protein
entity reference: Q9UQY2
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Proteasome gamma chain
name: Proteasome subunit beta type 1
name: Macropain subunit C5
name: Multicatalytic endopeptidase complex subunit C5
name: Proteasome component C5
xref: UnificationXref1682
feature: FragmentFeature322
cellular location: GO:0005829
comment: Reactome DB_ID: 3657771
display name: PSMB1

O42897
type: Protein
entity reference: O42897
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Proteasome subunit p58
name: 26S proteasome non-ATPase regulatory subunit 3
name: 26S proteasome regulatory subunit S3
xref: UnificationXref1680
feature: FragmentFeature321
cellular location: GO:0005829
comment: Reactome DB_ID: 3657852
display name: PSMD3

http://identifiers.org/pubmed/1944596
type: PublicationXref
id: 1944596
author: Russell, DW
author: Andersson, S
author: Berman, DM
author: Jenkins, EP
db: Pubmed
title: Deletion of steroid 5 alpha-reductase 2 gene in male pseudohermaphroditism
source: Nature 354:159-61
year: 1991

O94517
type: Protein
entity reference: O94517
data source: Provenance1
name: Proteasome iota chain
name: Note: the coordinates are copied over from Homo sapiens.
name: 27 kDa prosomal protein
name: Proteasome subunit alpha type 6
name: PSMA6
name: Multicatalytic endopeptidase complex iota chain
name: PROS-27
name: Macropain iota chain
xref: UnificationXref1684
feature: FragmentFeature323
cellular location: GO:0005829
comment: Reactome DB_ID: 3657763
display name: p27K

Stoichiometry831
type: Stoichiometry
physical entity: PIK3R4:Mn2+ (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry830
type: Stoichiometry
physical entity: SmallMolecule134
stoichiometric coefficient: 1.0

Stoichiometry833
type: Stoichiometry
physical entity: SmallMolecule134
stoichiometric coefficient: 1.0

Stoichiometry832
type: Stoichiometry
physical entity: Protein751
stoichiometric coefficient: 1.0

Leukotriene D4 [ChEBI:6423]
type: SmallMoleculeReference
name: LTD4
name: Leukotriene D4
xref: UnificationXref3588

Stoichiometry835
type: Stoichiometry
physical entity: Protein752
stoichiometric coefficient: 1.0

Stoichiometry834
type: Stoichiometry
physical entity: PIK3C3:Mn2+ (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry837
type: Stoichiometry
physical entity: Protein754
stoichiometric coefficient: 1.0

Stoichiometry836
type: Stoichiometry
physical entity: Protein753
stoichiometric coefficient: 1.0

Stoichiometry839
type: Stoichiometry
physical entity: Protein761
stoichiometric coefficient: 1.0

Stoichiometry838
type: Stoichiometry
physical entity: Protein760
stoichiometric coefficient: 1.0

http://identifiers.org/pubmed/6311078
type: PublicationXref
id: 6311078
author: Hammarström, Sven
db: Pubmed
title: Leukotrienes
source: Annu Rev Biochem 52:355-77
year: 1983

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94393
data source: Provenance1
name: O94393
name: 26S proteasome non-ATPase regulatory subunit 9
name: 26S proteasome regulatory subunit p27
xref: UnificationXref1654
feature: FragmentFeature309
cellular location: GO:0005829
comment: Reactome DB_ID: 3657870
display name: PSMD9

phospho-p-S83,S87-Ub-HNRNPD-3
type: Protein
entity reference: O94432
data source: Provenance1
xref: UnificationXref1648
feature: ModificationFeature46
feature: FragmentFeature308
feature: ModificationFeature44
feature: ModificationFeature45
cellular location: GO:0005829
comment: Reactome DB_ID: 3663154

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94432
data source: Provenance1
name: Ub-HNRNPD-4
name: Heterogeneous nuclear ribonucleoprotein D0
name: Ubiquinated AUF1 isoform p37
name: O94432
name: HNRPD_HUMAN
xref: UnificationXref1647
feature: ModificationFeature46
feature: FragmentFeature307
cellular location: GO:0005829
comment: Reactome DB_ID: 3663153
display name: HNRNPD

Ubiquitinated AUF1 (isoform p37 or p40)
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
member physical entity: phospho-p-S83,S87-Ub-HNRNPD-3
xref: UnificationXref1649
cellular location: GO:0005829
comment: Reactome DB_ID: 3663155
comment: Converted from EntitySet in Reactome

phospho-p-S83,S87-HNRNPD-3
type: Protein
entity reference: O94432
data source: Provenance1
xref: UnificationXref1637
feature: ModificationFeature44
feature: ModificationFeature45
feature: FragmentFeature306
cellular location: GO:0005829
comment: Reactome DB_ID: 3663144

HNRNPD-4
type: Protein
entity reference: O94432
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: AUF1 isoform p37
name: HNRNPD isoform 4
name: Heterogeneous nuclear ribonucleoprotein D0
name: HNRPD_HUMAN
xref: UnificationXref1635
feature: FragmentFeature305
cellular location: GO:0005829
comment: Reactome DB_ID: 3663140
display name: O94432

http://identifiers.org/pubmed/8892014
type: PublicationXref
id: 8892014
author: Treacy, E
author: Thompson, GN
author: Pitt, JJ
author: Cotton, RG
author: Seller, K
author: Ramus, S
db: Pubmed
title: In vivo disposal of phenylalanine in phenylketonuria: a study of two siblings
source: J Inherit Metab Dis 19:595-602
year: 1996

Tumor necrosis factor type 1 receptor associated protein 2
type: Protein
entity reference: P87048
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: 26S proteasome subunit p97
name: 26S proteasome regulatory subunit S2
name: P87048
name: 55.11 protein
name: 26S proteasome non-ATPase regulatory subunit 2
xref: UnificationXref1662
feature: FragmentFeature313
cellular location: GO:0005829
comment: Reactome DB_ID: 3657848
display name: PSMD2

Stoichiometry840
type: Stoichiometry
physical entity: Protein762
stoichiometric coefficient: 1.0

O94579
type: Protein
entity reference: O94579
data source: Provenance1
name: Proteasome subunit alpha type 2
name: Note: the coordinates are copied over from Homo sapiens.
name: Multicatalytic endopeptidase complex subunit C3
name: Proteasome component C3
name: Macropain subunit C3
xref: UnificationXref1660
feature: FragmentFeature312
cellular location: GO:0005829
comment: Reactome DB_ID: 3657747
display name: PSMA2

PSA7L_HUMAN
type: Protein
entity reference: UniProt:Q10329
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Q10329
name: Proteasome subunit alpha type-7-like
xref: UnificationXref1658
feature: FragmentFeature311
cellular location: GO:0005829
comment: Reactome DB_ID: 3657876
display name: PSMA8

Proteasome component C13
type: Protein
entity reference: P30655
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Multicatalytic endopeptidase complex subunit C13
name: Macropain subunit C13
name: Proteasome subunit beta type 8
name: P30655
name: Proteasome subunit beta type 8 precursor
xref: UnificationXref1656
feature: FragmentFeature310
cellular location: GO:0005829
comment: Reactome DB_ID: 3657797
display name: PSMB8

Stoichiometry844
type: Stoichiometry
physical entity: Zn(II)
stoichiometric coefficient: 1.0

Stoichiometry843
type: Stoichiometry
physical entity: Protein765
stoichiometric coefficient: 1.0

Stoichiometry842
type: Stoichiometry
physical entity: Protein764
stoichiometric coefficient: 1.0

Stoichiometry841
type: Stoichiometry
physical entity: Protein763
stoichiometric coefficient: 1.0

Stoichiometry848
type: Stoichiometry
physical entity: Protein778
stoichiometric coefficient: 1.0

Stoichiometry847
type: Stoichiometry
physical entity: Protein775
stoichiometric coefficient: 1.0

Regulation of actin dynamics for phagocytic cup formation
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction610
pathway component: BiochemicalReaction611
pathway component: BiochemicalReaction609
pathway component: BiochemicalReaction612
evidence: Evidence1067
xref: UnificationXref6800
xref: UnificationXref6801
pathway order: PathwayStep1047
pathway order: PathwayStep1048
pathway order: PathwayStep1045
pathway order: PathwayStep1046
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Stoichiometry846
type: Stoichiometry
physical entity: Protein772
stoichiometric coefficient: 1.0

Stoichiometry845
type: Stoichiometry
physical entity: Protein768
stoichiometric coefficient: 1.0

Stoichiometry849
type: Stoichiometry
physical entity: Protein781
stoichiometric coefficient: 1.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36612
data source: Provenance1
name: 26S protease regulatory subunit 4
name: PSMC1(2-440)
name: P36612
xref: UnificationXref1708
feature: FragmentFeature336
cellular location: GO:0005829
comment: Reactome DB_ID: 3657802
display name: P26s4

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43063
data source: Provenance1
name: Proteasome subunit Y
name: Proteasome delta chain
name: Multicatalytic endopeptidase complex delta chain
name: Proteasome subunit beta type 6 precursor
name: O43063
name: Macropain delta chain
name: Proteasome subunit beta type 6
xref: UnificationXref1706
feature: FragmentFeature335
cellular location: GO:0005829
comment: Reactome DB_ID: 3657795
display name: PSMB6

26S proteasome non-ATPase regulatory subunit 13
type: Protein
entity reference: Q9US13
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: 26S proteasome regulatory subunit p40.5
name: 26S proteasome regulatory subunit S11
name: Q9US13
xref: UnificationXref1712
feature: FragmentFeature338
cellular location: GO:0005829
comment: Reactome DB_ID: 3657844
display name: PSMD13

O74445
type: Protein
entity reference: O74445
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Proteasome subunit p42
name: Conserved ATPase domain protein 44
name: PSMC6(2-389)
name: CADp44
name: 26S protease regulatory subunit S10B
xref: UnificationXref1710
feature: FragmentFeature337
cellular location: GO:0005829
comment: Reactome DB_ID: 3657822
display name: p44

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09720
data source: Provenance1
name: Proteasome subunit beta type 2
name: Macropain subunit C7-I
name: Multicatalytic endopeptidase complex subunit C7-I
name: Proteasome component C7-I
name: Q09720
xref: UnificationXref1716
feature: FragmentFeature340
cellular location: GO:0005829
comment: Reactome DB_ID: 3657779
display name: PSMB2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7T8
data source: Provenance1
name: Q9Y7T8
name: Proteasome theta chain
name: Proteasome component C10-II
name: Proteasome subunit beta type 3
name: Proteasome chain 13
xref: UnificationXref1714
feature: FragmentFeature339
cellular location: GO:0005829
comment: Reactome DB_ID: 3657783
display name: PSMB3

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P41836
data source: Provenance1
name: P41836
name: Probable 26S protease regulatory subunit 8
xref: UnificationXref1722
feature: FragmentFeature342
cellular location: GO:0005829
comment: Reactome DB_ID: 3657818
display name: PSMC5

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09841
data source: Provenance1
name: Q09841
name: Multicatalytic endopeptidase complex subunit MECl-1
name: Proteasome MECl-1
name: Proteasome subunit beta type 10 precursor
name: Macropain subunit MECl-1
name: Proteasome subunit beta type 10
xref: UnificationXref1719
feature: FragmentFeature341
cellular location: GO:0005829
comment: Reactome DB_ID: 3657775
display name: PSMB10

Proteasome chain 6
type: Protein
entity reference: P30655
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Macropain epsilon chain
name: Multicatalytic endopeptidase complex epsilon chain
name: Proteasome subunit X
name: Proteasome epsilon chain
name: Proteasome subunit MB1
name: P30655
name: Proteasome subunit beta type 5 precursor
name: Proteasome subunit beta type 5
xref: UnificationXref1724
feature: FragmentFeature343
cellular location: GO:0005829
comment: Reactome DB_ID: 3657791
display name: PSMB5

Stoichiometry850
type: Stoichiometry
physical entity: Protein792
stoichiometric coefficient: 1.0

http://identifiers.org/pubmed/11572773
type: PublicationXref
id: 11572773
author: Blackburn, EH
db: Pubmed
title: Switching and signaling at the telomere
source: Cell 106:661-73
year: 2001

Stoichiometry851
type: Stoichiometry
physical entity: Protein793
stoichiometric coefficient: 1.0

Stoichiometry857
type: Stoichiometry
physical entity: SmallMolecule53
stoichiometric coefficient: 3.0

Stoichiometry856
type: Stoichiometry
physical entity: Protein814
stoichiometric coefficient: 1.0

Stoichiometry859
type: Stoichiometry
physical entity: Protein815
stoichiometric coefficient: 2.0

http://identifiers.org/pubmed/9207117
type: PublicationXref
id: 9207117
author: Zhou, B
author: Gitschier, J
db: Pubmed
title: hCTR1: a human gene for copper uptake identified by complementation in yeast
source: Proc Natl Acad Sci U S A 94:7481-6
year: 1997

Stoichiometry858
type: Stoichiometry
physical entity: PDSS1:Mg2+ (name copied from entity in Homo sapiens)
stoichiometric coefficient: 2.0

Stoichiometry853
type: Stoichiometry
physical entity: Protein793
stoichiometric coefficient: 1.0

Stoichiometry852
type: Stoichiometry
physical entity: Protein794
stoichiometric coefficient: 1.0

Stoichiometry855
type: Stoichiometry
physical entity: SmallMolecule51
stoichiometric coefficient: 7.0

Stoichiometry854
type: Stoichiometry
physical entity: IPPP
stoichiometric coefficient: 7.0

Respiratory electron transport, ATP synthesis by chemiosmotic coupling, and heat production by uncoupling proteins.
type: Pathway
data source: Provenance1
pathway component: REACT 144371.5
evidence: Evidence618
xref: UnificationXref4057
xref: RelationshipXref466
xref: UnificationXref4056
pathway order: PathwayStep608
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

mRNA Splicing - Minor Pathway
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction523
pathway component: BiochemicalReaction520
pathway component: BiochemicalReaction522
pathway component: BiochemicalReaction521
evidence: Evidence869
xref: UnificationXref5768
xref: UnificationXref5767
xref: RelationshipXref784
pathway order: PathwayStep856
pathway order: PathwayStep858
pathway order: PathwayStep855
pathway order: PathwayStep857
display name: U12 Dependent Splicing
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P30655
data source: Provenance1
name: PSB11_HUMAN
name: Proteasome subunit beta type-11
name: P30655
xref: UnificationXref1690
feature: FragmentFeature327
cellular location: GO:0005829
comment: Reactome DB_ID: 3657877
display name: PSMB11

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:O42931
data source: Provenance1
name: 26S protease regulatory subunit 7
name: MSS1 protein
name: O42931
xref: UnificationXref1689
feature: FragmentFeature326
cellular location: GO:0005829
comment: Reactome DB_ID: 3657806
display name: PSMC2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10329
data source: Provenance1
name: PSMA7(2-248)
name: Proteasome subunit XAPC7
name: Proteasome subunit RC6-1
name: Proteasome subunit alpha type 7
xref: UnificationXref1687
feature: FragmentFeature325
cellular location: GO:0005829
comment: Reactome DB_ID: 3657767
display name: Q10329

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9USQ9
data source: Provenance1
name: PSMB4
name: Multicatalytic endopeptidase complex beta chain
name: Proteasome chain 3
name: Q9USQ9
name: Macropain beta chain
name: HsBPROS26
name: Proteasome beta chain
name: Proteasome subunit beta type 4 precursor
name: Proteasome subunit beta type 4
xref: UnificationXref1686
feature: FragmentFeature324
cellular location: GO:0005829
comment: Reactome DB_ID: 3657787
display name: HSN3

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14126
data source: Provenance1
name: O14126
name: TBP-1
name: Proteasome subunit P50
name: TAT-binding protein 1
name: 26S protease regulatory subunit 6A
xref: UnificationXref1698
feature: FragmentFeature331
cellular location: GO:0005829
comment: Reactome DB_ID: 3657810
display name: PSMC3

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14250
data source: Provenance1
name: PROS-30
name: Proteasome subunit alpha type 1
name: O14250
name: Proteasome nu chain
name: Multicatalytic endopeptidase complex subunit C2
name: Proteasome component C2
name: Macropain subunit C2
name: 30 kDa prosomal protein
xref: UnificationXref1696
feature: FragmentFeature330
cellular location: GO:0005829
comment: Reactome DB_ID: 3657743
display name: PSMA1

Q10311
type: Protein
entity reference: UniProt:Q10311
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: 26S proteasome non-ATPase regulatory subunit 10
name: 26S proteasome regulatory subunit p28
name: Gankyrin
xref: UnificationXref1694
feature: FragmentFeature329
cellular location: GO:0005829
comment: Reactome DB_ID: 3657830
display name: PSMD10

26S proteasome subunit p112
type: Protein
entity reference: O74762
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: 26S proteasome non-ATPase regulatory subunit 1
name: 26S proteasome regulatory subunit S1
name: O74762
xref: UnificationXref1692
feature: FragmentFeature328
cellular location: GO:0005829
comment: Reactome DB_ID: 3657826
display name: PSMD1

Stoichiometry861
type: Stoichiometry
physical entity: Flavin adenine dinucleotide
stoichiometric coefficient: 1.0

Stoichiometry862
type: Stoichiometry
physical entity: Protein820
stoichiometric coefficient: 1.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94444
data source: Provenance1
name: Antisecretory factor-1
name: ASF
name: Rpn10
name: 26S proteasome regulatory subunit S5A
name: PSMD4(2-377)
name: Multiubiquitin chain binding protein
name: O94444
name: 26S proteasome non-ATPase regulatory subunit 4
xref: UnificationXref1703
feature: FragmentFeature333
cellular location: GO:0005829
comment: Reactome DB_ID: 3657856
display name: AF

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43063
data source: Provenance1
name: Proteasome chain 7
name: Macropain chain 7
name: Multicatalytic endopeptidase complex chain 7
name: O43063
name: RING12 protein
name: Proteasome subunit beta type 9
name: Low molecular mass protein 2
name: Proteasome subunit beta type 9 precursor
xref: UnificationXref1701
feature: FragmentFeature332
cellular location: GO:0005829
comment: Reactome DB_ID: 3657798
display name: PSMB9

Stoichiometry860
type: Stoichiometry
physical entity: Protein817
stoichiometric coefficient: 1.0

Stoichiometry869
type: Stoichiometry
physical entity: Protein825
stoichiometric coefficient: 1.0

Stoichiometry868
type: Stoichiometry
physical entity: Protein824
stoichiometric coefficient: 3.0

Stoichiometry867
type: Stoichiometry
physical entity: Protein825
stoichiometric coefficient: 2.0

Stoichiometry866
type: Stoichiometry
physical entity: Protein824
stoichiometric coefficient: 2.0

Stoichiometry865
type: Stoichiometry
physical entity: GCH1 dimer (name copied from entity in Homo sapiens)
stoichiometric coefficient: 5.0

Stoichiometry864
type: Stoichiometry
physical entity: Protein823
stoichiometric coefficient: 2.0

Stoichiometry863
type: Stoichiometry
physical entity: iron (ferrous)
stoichiometric coefficient: 2.0

http://identifiers.org/pubmed/20110263
type: PublicationXref
id: 20110263
author: Kersten, S
author: de Groot, PJ
author: de Vries, SC
author: Muller, M
author: Degenhardt, T
author: Carlberg, C
author: Vaisanen, S
author: Heinaniemi, M
author: van der Meer, DL
db: Pubmed
title: Profiling of promoter occupancy by PPAR{alpha} in human hepatoma cells via ChIP-chip analysis
source: Nucleic Acids Res
year: 2010

Q9UT97
type: Protein
entity reference: Q9UT97
data source: Provenance1
name: Proteasome zeta chain
name: Note: the coordinates are copied over from Homo sapiens.
name: Multicatalytic endopeptidase complex zeta chain
name: Macropain zeta chain
name: Proteasome subunit alpha type 5
xref: UnificationXref1705
feature: FragmentFeature334
cellular location: GO:0005829
comment: Reactome DB_ID: 3657759
display name: PSMA5

http://identifiers.org/pubmed/15276183
type: PublicationXref
id: 15276183
author: Gangloff, M
author: Gay, NJ
db: Pubmed
title: MD-2: the Toll 'gatekeeper' in endotoxin signalling
source: Trends Biochem Sci 29:294-300
year: 2004

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P19117
data source: Provenance1
name: Pyrophosphate phospho-hydrolase
name: Inorganic pyrophosphatase
name: P19117
name: pyrophosphatase (inorganic) 1
xref: UnificationXref1513
feature: FragmentFeature283
cellular location: GO:0005829
comment: Reactome DB_ID: 3658522
display name: PPA1

UniProt:Q12701
type: ProteinReference
xref: UnificationXref1027
organism: BioSource1

DAP12 signaling
type: Pathway
data source: Provenance1
pathway component: REACT 79658.9
pathway component: REACT 80694.9
pathway component: REACT 149305.4
evidence: Evidence1072
xref: UnificationXref6822
xref: UnificationXref6823
pathway order: PathwayStep187
pathway order: PathwayStep173
pathway order: PathwayStep182
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P87118
data source: Provenance1
name: Pyrophosphate phospho-hydrolase
name: P87118
name: Inorganic pyrophosphatase
name: pyrophosphatase (inorganic) 1
xref: UnificationXref1515
feature: FragmentFeature284
cellular location: GO:0005829
comment: Reactome DB_ID: 3658526
display name: PPA1

Homologues of PPA2
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1532
cellular location: GO:0005759
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3663100

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9P324
data source: Provenance1
name: Q9P324
name: Retinol dehydrogenase 8 ecNumber1.1.1.300/ecNumber
name: RDH8_HUMAN
xref: UnificationXref1490
feature: FragmentFeature280
cellular location: GO:0042622
comment: Reactome DB_ID: 3664801
display name: RDH8

Stoichiometry871
type: Stoichiometry
physical entity: Protein824
stoichiometric coefficient: 1.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74628
data source: Provenance1
name: O74628
name: Retinol dehydrogenase 8 ecNumber1.1.1.300/ecNumber
name: RDH8_HUMAN
xref: UnificationXref1492
feature: FragmentFeature281
cellular location: GO:0042622
comment: Reactome DB_ID: 3664802
display name: RDH8

Stoichiometry870
type: Stoichiometry
physical entity: Protein824
stoichiometric coefficient: 4.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q1MTR7
data source: Provenance1
name: Short-chain dehydrogenase/reductase 3 ecNumber1.1.1.300/ecNumber
name: Q1MTR7
name: DHRS3_HUMAN
xref: UnificationXref1501
feature: FragmentFeature282
cellular location: GO:0042622
comment: Reactome DB_ID: 3664809
display name: DHRS3

Stoichiometry873
type: Stoichiometry
physical entity: Protein825
stoichiometric coefficient: 4.0

Homologues of PPA1
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1516
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658527

Stoichiometry872
type: Stoichiometry
physical entity: Protein825
stoichiometric coefficient: 3.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTI5
data source: Provenance1
name: retromer
name: Q9UTI5
xref: UnificationXref1453
feature: FragmentFeature278
cellular location: GO:0005829
comment: Reactome DB_ID: 3665019
display name: VPS29

SDP3
type: Protein
entity reference: O94291
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: retromer
name: O94291
xref: UnificationXref1456
feature: FragmentFeature279
cellular location: GO:0005829
comment: Reactome DB_ID: 3665029
display name: SNX3

Homologues of RDH8
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1493
cellular location: GO:0042622
comment: Reactome DB_ID: 3664803
comment: Converted from EntitySet in Reactome

Stoichiometry874
type: Stoichiometry
physical entity: Protein826
stoichiometric coefficient: 1.0

Stoichiometry875
type: Stoichiometry
physical entity: Protein827
stoichiometric coefficient: 1.0

Stoichiometry876
type: Stoichiometry
physical entity: SmallMolecule167
stoichiometric coefficient: 1.0

Stoichiometry877
type: Stoichiometry
physical entity: Protein828
stoichiometric coefficient: 1.0

Stoichiometry878
type: Stoichiometry
physical entity: alpha-keto acid dehydrogenase E3 holoenzyme (name copied from entity in Homo sapiens)
stoichiometric coefficient: 2.0

Stoichiometry879
type: Stoichiometry
physical entity: alpha-keto acid dehydrogenase E3 homodimer (name copied from entity in Homo sapiens)
stoichiometric coefficient: 6.0

THF-polyglutamate
type: SmallMoleculeReference
name: Tetrahydrofolyl-[Glu](n)
name: Tetrahydrofolyl-[Glu](n) [ChEBI:9484]
name: Tetrahydrofolyl-[Glu](n+1)
xref: UnificationXref4676

O74552
type: Protein
entity reference: O74552
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: retromer
name: VPS35
xref: UnificationXref1449
feature: FragmentFeature276
cellular location: GO:0005829
comment: Reactome DB_ID: 3665023
display name: MEM3

Stoichiometry880
type: Stoichiometry
physical entity: Protein829
stoichiometric coefficient: 12.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10243
data source: Provenance1
name: retromer
name: Q10243
name: VPS26A
xref: UnificationXref1451
feature: FragmentFeature277
cellular location: GO:0005829
comment: Reactome DB_ID: 3665015
display name: VPS26

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O59781
data source: Provenance1
name: Mitochondrial Rho GTPase 1
name: O59781
name: MIRO1_HUMAN
xref: UnificationXref1396
feature: FragmentFeature274
cellular location: GO:0005829
comment: Reactome DB_ID: 3661451
display name: RHOT1

Q01112
type: Protein
entity reference: Q01112
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Cell division control protein 42 homolog
name: CDC42_HUMAN
xref: UnificationXref1397
feature: FragmentFeature275
cellular location: GO:0005829
comment: Reactome DB_ID: 3661460
display name: CDC42

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14224
data source: Provenance1
name: Rho GDIbeta/GDI2
name: ARHGDIB
xref: UnificationXref1393
feature: FragmentFeature272
cellular location: GO:0005829
comment: Reactome DB_ID: 3661448
display name: O14224

Stoichiometry884
type: Stoichiometry
physical entity: Thiamin diphosphate
stoichiometric coefficient: 2.0

Rho GDIgamma/GDI3
type: Protein
entity reference: O14224
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: ARHGDIG
xref: UnificationXref1394
feature: FragmentFeature273
cellular location: GO:0005829
comment: Reactome DB_ID: 3661449
display name: O14224

Stoichiometry883
type: Stoichiometry
physical entity: Protein831
stoichiometric coefficient: 2.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10305
data source: Provenance1
name: GDI2/Rab GDI beta
name: Q10305
xref: UnificationXref1390
feature: FragmentFeature270
cellular location: GO:0005829
comment: Reactome DB_ID: 3661443
display name: GDI2

Stoichiometry882
type: Stoichiometry
physical entity: pyruvate dehydrogenase E2 trimer (name copied from entity in Homo sapiens)
stoichiometric coefficient: 20.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14224
data source: Provenance1
name: RHO-GDIalpha
name: Rho GDP-dissociation inhibitor 1
name: GDIR_HUMAN
name: ARHGDIA
xref: UnificationXref1392
feature: FragmentFeature271
cellular location: GO:0005829
comment: Reactome DB_ID: 3661447
display name: O14224

Stoichiometry881
type: Stoichiometry
physical entity: Protein830
stoichiometric coefficient: 3.0

GDI proteins
type: Protein
data source: Provenance1
member physical entity: Rho GDIgamma/GDI3
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1395
cellular location: GO:0005829
comment: Reactome DB_ID: 3661450
comment: Converted from EntitySet in Reactome

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10305
data source: Provenance1
name: Q10305
name: GDI1/Rab GDI alpha
xref: UnificationXref1389
feature: FragmentFeature269
cellular location: GO:0005829
comment: Reactome DB_ID: 3661442
display name: GDI1

Prolonged ERK activation events
type: Pathway
data source: Provenance1
pathway component: REACT 134566.5
pathway component: REACT 108512.9
evidence: Evidence236
xref: UnificationXref1262
xref: RelationshipXref97
xref: UnificationXref1263
pathway order: PathwayStep232
pathway order: PathwayStep233
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Stoichiometry887
type: Stoichiometry
physical entity: SmallMolecule80
stoichiometric coefficient: 2.0

Stoichiometry888
type: Stoichiometry
physical entity: Thiamin diphosphate
stoichiometric coefficient: 2.0

Stoichiometry885
type: Stoichiometry
physical entity: Protein832
stoichiometric coefficient: 2.0

Stoichiometry886
type: Stoichiometry
physical entity: pyruvate dehydrogenase E1 complex (name copied from entity in Homo sapiens)
stoichiometric coefficient: 22.0

Stoichiometry889
type: Stoichiometry
physical entity: pyruvate dehydrogenase E1 complex (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UUI1
data source: Provenance1
name: Q9UUI1
name: U6 snRNA-associated Sm-like protein LSm6
name: LSM6_HUMAN
xref: UnificationXref1610
feature: FragmentFeature300
cellular location: GO:0005829
comment: Reactome DB_ID: 3662742
display name: LSM6

Stoichiometry893
type: Stoichiometry
physical entity: pyruvate dehydrogenase E2 trimer (name copied from entity in Homo sapiens)
stoichiometric coefficient: 20.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7M4
data source: Provenance1
name: LSM3(2-102)
name: U6 snRNA-associated Sm-like protein LSm3
name: Q9Y7M4
name: LSM3_HUMAN
xref: UnificationXref1612
feature: FragmentFeature301
cellular location: GO:0005829
comment: Reactome DB_ID: 3662730
display name: LSM3

Stoichiometry892
type: Stoichiometry
physical entity: Protein829
stoichiometric coefficient: 12.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P87173
data source: Provenance1
name: U6 snRNA-associated Sm-like protein LSm1
name: P87173
name: LSM1_HUMAN
xref: UnificationXref1614
feature: FragmentFeature302
cellular location: GO:0005829
comment: Reactome DB_ID: 3662726
display name: LSM1

Stoichiometry895
type: Stoichiometry
physical entity: SmallMolecule84
stoichiometric coefficient: 2.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:O42978
data source: Provenance1
name: LSM5_HUMAN
name: O42978
name: U6 snRNA-associated Sm-like protein LSm5
name: LSM5(2-91)
xref: UnificationXref1616
feature: FragmentFeature303
cellular location: GO:0005829
comment: Reactome DB_ID: 3662738
display name: LSM5

Stoichiometry894
type: Stoichiometry
physical entity: pyruvate dehydrogenase E1 complex (name copied from entity in Homo sapiens)
stoichiometric coefficient: 21.0

XRN1_HUMAN
type: Protein
entity reference: P40383
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: P40383
name: 5'-3' exoribonuclease 1
xref: UnificationXref1625
feature: FragmentFeature304
cellular location: GO:0005829
comment: Reactome DB_ID: 3662754
display name: XRN1

Stoichiometry891
type: Stoichiometry
physical entity: alpha-keto acid dehydrogenase E3 homodimer (name copied from entity in Homo sapiens)
stoichiometric coefficient: 6.0

Stoichiometry890
type: Stoichiometry
physical entity: phosphorylated pyruvate dehydrogenase E1 complex (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Exosome complex exonuclease RRP45
type: Protein
entity reference: O74918
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: EXOS9_HUMAN
name: EXOSC9 (RRP45)
name: O74918
xref: UnificationXref1586
feature: FragmentFeature295
cellular location: GO:0005829
comment: Reactome DB_ID: 3662782
display name: EXOSC9

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9P7C9
data source: Provenance1
name: Scavenger mRNA-decapping enzyme DcpS
name: DCPS(1-337)
name: Q9P7C9
name: DCPS_HUMAN
xref: UnificationXref1597
feature: FragmentFeature296
cellular location: GO:0005829
comment: Reactome DB_ID: 3662761
display name: DCPS

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74499
data source: Provenance1
name: O74499
name: LSM7_HUMAN
name: U6 snRNA-associated Sm-like protein LSm7
xref: UnificationXref1603
feature: FragmentFeature297
cellular location: GO:0005829
comment: Reactome DB_ID: 3662747
display name: LSM7

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94408
data source: Provenance1
name: U6 snRNA-associated Sm-like protein LSm2
name: LSM2_HUMAN
name: O94408
xref: UnificationXref1605
feature: FragmentFeature298
cellular location: GO:0005829
comment: Reactome DB_ID: 3662743
display name: LSM2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14352
data source: Provenance1
name: LSM4_HUMAN
name: U6 snRNA-associated Sm-like protein LSm4
name: O14352
xref: UnificationXref1607
feature: FragmentFeature299
cellular location: GO:0005829
comment: Reactome DB_ID: 3662734
display name: LSM4

Procainamide [ChEBI:8428]
type: SmallMoleculeReference
name: Procainamide
xref: UnificationXref6345

http://identifiers.org/pubmed/8163052
type: PublicationXref
id: 8163052
author: Gomis, R
author: Malaisse, WJ
author: Sener, A
author: Fernandez-Alvarez, J
author: Conget, I
author: Rasschaert, J
db: Pubmed
title: Enzymatic, metabolic and secretory patterns in human islets of type 2 (non-insulin-dependent) diabetic patients
source: Diabetologia 37:177-81
year: 1994

http://identifiers.org/pubmed/15080793
type: PublicationXref
id: 15080793
author: Wenk, MR
author: Uhlén, P
author: Lee, E
author: De Camilli, P
author: Ehrlich, BE
author: Degray, B
author: Johenning, FW
db: Pubmed
title: InsP3-mediated intracellular calcium signalling is altered by expression of synaptojanin-1
source: Biochem J 382:687-94
year: 2004

Stoichiometry896
type: Stoichiometry
physical entity: Protein838
stoichiometric coefficient: 2.0

Stoichiometry897
type: Stoichiometry
physical entity: Protein840
stoichiometric coefficient: 1.0

Stoichiometry898
type: Stoichiometry
physical entity: Protein841
stoichiometric coefficient: 2.0

Stoichiometry899
type: Stoichiometry
physical entity: SmallMolecule86
stoichiometric coefficient: 2.0

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P37202
data source: Provenance1
name: Exosome complex exonuclease RRP44
name: P37202
name: RRP44_HUMAN
xref: UnificationXref1576
feature: FragmentFeature291
cellular location: GO:0005829
comment: Reactome DB_ID: 3662787
display name: DIS3

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9P7R3
data source: Provenance1
name: EXOS6_HUMAN
name: Exosome complex exonuclease MTR3
name: Q9P7R3
xref: UnificationXref1578
feature: FragmentFeature292
cellular location: GO:0005829
comment: Reactome DB_ID: 3662768
display name: EXOSC6

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09704
data source: Provenance1
name: Q09704
name: EXOS2_HUMAN
name: Exosome complex exonuclease RRP4
xref: UnificationXref1572
feature: FragmentFeature289
cellular location: GO:0005829
comment: Reactome DB_ID: 3662795
display name: EXOSC2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O59821
data source: Provenance1
name: O59821
name: 3'-5' exoribonuclease CSL4 homolog
name: EXOS1_HUMAN
xref: UnificationXref1574
feature: FragmentFeature290
cellular location: GO:0005829
comment: Reactome DB_ID: 3662799
display name: EXOSC1

Q10205
type: Protein
entity reference: UniProt:Q10205
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Exosome complex exonuclease RRP43
name: EXOS8_HUMAN
xref: UnificationXref1581
feature: FragmentFeature293
cellular location: GO:0005829
comment: Reactome DB_ID: 3662774
display name: EXOSC8

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O42894
data source: Provenance1
name: EXOS5_HUMAN
name: Exosome complex exonuclease RRP46
name: O42894
xref: UnificationXref1583
feature: FragmentFeature294
cellular location: GO:0005829
comment: Reactome DB_ID: 3662778
display name: EXOSC5

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P40384
data source: Provenance1
name: P40384
name: Meiotic recombination protein SPO11
name: SPO11_HUMAN
xref: UnificationXref1544
feature: FragmentFeature287
cellular location: GO:0005654
comment: Reactome DB_ID: 3663418
display name: SPO11

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O13903
data source: Provenance1
name: O13903
name: EXOS3_HUMAN
name: Exosome complex exonuclease RRP40
xref: UnificationXref1570
feature: FragmentFeature288
cellular location: GO:0005829
comment: Reactome DB_ID: 3662791
display name: EXOSC3

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P19117
data source: Provenance1
name: Inorganic pyrophosphatase 2, mitochondrial
name: pyrophosphatase (inorganic) 2
name: P19117
xref: UnificationXref1530
feature: FragmentFeature285
cellular location: GO:0005759
comment: Reactome DB_ID: 3663098
display name: PPA2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P87118
data source: Provenance1
name: Inorganic pyrophosphatase 2, mitochondrial
name: P87118
name: pyrophosphatase (inorganic) 2
xref: UnificationXref1531
feature: FragmentFeature286
cellular location: GO:0005759
comment: Reactome DB_ID: 3663099
display name: PPA2

UniProt:Q12706
type: ProteinReference
xref: UnificationXref1083
organism: BioSource1

3-Methyl-2-oxopentanoate
type: SmallMoleculeReference
name: 2-Oxo-3-methylvalerate
name: 3-Methyl-2-oxopentanoate [ChEBI:28654]
xref: UnificationXref4870

http://identifiers.org/pubmed/6434529
type: PublicationXref
id: 6434529
author: Chuang, DT
author: Cox, RP
author: Markovitz, PJ
db: Pubmed
title: Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities.
source: J Biol Chem 259:11643-6
year: 1984

Stoichiometry799
type: Stoichiometry
physical entity: SREBP1A/1C/2 Dimer (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry798
type: Stoichiometry
physical entity: PhysicalEntity130
stoichiometric coefficient: 1.0

Stoichiometry797
type: Stoichiometry
physical entity: NF-Y (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry795
type: Stoichiometry
physical entity: SmallMolecule22
stoichiometric coefficient: 4.0

Stoichiometry796
type: Stoichiometry
physical entity: SmallMolecule22
stoichiometric coefficient: 2.0

Stoichiometry793
type: Stoichiometry
physical entity: SmallMolecule44
stoichiometric coefficient: 3.0

Stoichiometry794
type: Stoichiometry
physical entity: SmallMolecule46
stoichiometric coefficient: 3.0

Stoichiometry791
type: Stoichiometry
physical entity: SmallMolecule187
stoichiometric coefficient: 3.0

Stoichiometry792
type: Stoichiometry
physical entity: SmallMolecule26
stoichiometric coefficient: 3.0

Stoichiometry790
type: Stoichiometry
physical entity: SmallMolecule22
stoichiometric coefficient: 4.0

E2F-enabled inhibition of pre-replication complex formation
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction685
evidence: Evidence1204
xref: UnificationXref7629
xref: UnificationXref7628
pathway order: PathwayStep1183
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/15720390
type: PublicationXref
id: 15720390
author: Fabre, AL
author: Orlean, P
author: Taron, CH
db: Pubmed
title: Saccharomyces cerevisiae Ybr004c and its human homologue are required for addition of the second mannose during glycosylphosphatidylinositol precursor assembly
source: FEBS J 272:1160-8
year: 2005

UnificationXref1790
type: UnificationXref
id: O59675
db: UniProt

UnificationXref1792
type: UnificationXref
id: 3658825
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658825

UnificationXref1791
type: UnificationXref
id: 3658824
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658824

UnificationXref1798
type: UnificationXref
id: O74893
db: UniProt

UnificationXref1797
type: UnificationXref
id: 3658816
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658816

UnificationXref1799
type: UnificationXref
id: 3658699
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658699

UnificationXref1794
type: UnificationXref
id: 3658811
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658811

UnificationXref1793
type: UnificationXref
id: O14049
db: UniProt

UnificationXref1796
type: UnificationXref
id: 3658815
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658815

UnificationXref1795
type: UnificationXref
id: Q9P7B2
db: UniProt

UnificationXref1781
type: UnificationXref
id: 3663505
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663505

UnificationXref1780
type: UnificationXref
id: 3659893
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659893

http://identifiers.org/pubmed/8755247
type: PublicationXref
id: 8755247
author: Migliaccio, E
author: Bonfini, L
author: Pelicci, PG
author: Pelicci, G
author: Lanfrancone, L
db: Pubmed
title: Not all Shc's roads lead to Ras
source: Trends Biochem Sci 21:257-61
year: 1996

UnificationXref1789
type: UnificationXref
id: 3658820
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658820

UnificationXref1788
type: UnificationXref
id: Q09757
db: UniProt

UnificationXref1787
type: UnificationXref
id: 3658763
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658763

UnificationXref1786
type: UnificationXref
id: O42952
db: UniProt

UnificationXref1785
type: UnificationXref
id: 3660549
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660549

UnificationXref1784
type: UnificationXref
id: 3660548
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660548

UnificationXref1783
type: UnificationXref
id: O74718
db: UniProt

UnificationXref1782
type: UnificationXref
id: 3663506
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663506

Homologues of ARHGAP32
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1356
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3661523

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10164
data source: Provenance1
name: Q10164
name: Bcr
xref: UnificationXref1351
feature: FragmentFeature243
cellular location: GO:0005829
comment: Reactome DB_ID: 3661514
display name: BCR

UnificationXref1779
type: UnificationXref
id: 3663504
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663504

UnificationXref1771
type: UnificationXref
id: O42847
db: UniProt

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTR5
data source: Provenance1
name: ARHG8_HUMAN
name: Q9UTR5
name: Neuroepithelial cell-transforming gene 1 protein
xref: UnificationXref1346
feature: FragmentFeature242
cellular location: GO:0005829
comment: Reactome DB_ID: 3661509
display name: NET1

UnificationXref1772
type: UnificationXref
id: 3659898
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659898

UnificationXref1773
type: UnificationXref
id: 3659900
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659900

UnificationXref1774
type: UnificationXref
id: 3663498
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663498

UnificationXref1775
type: UnificationXref
id: Q10055
db: UniProt

UnificationXref1776
type: UnificationXref
id: 3663497
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663497

UnificationXref1777
type: UnificationXref
id: 3663499
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663499

UnificationXref1778
type: UnificationXref
id: Q10267
db: UniProt

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P40995
data source: Provenance1
name: ARHGEF7
name: COOL1
name: Beta-Pix
name: P40995
xref: UnificationXref1339
feature: FragmentFeature236
cellular location: GO:0005829
comment: Reactome DB_ID: 3661502
display name: PIX

Homologues of ARHGEF12
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1343
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3661506

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7U5
data source: Provenance1
name: ARHGC_HUMAN
name: Rho guanine nucleotide exchange factor 12
name: ARHGEF12
name: Q9Y7U5
xref: UnificationXref1340
feature: FragmentFeature237
cellular location: GO:0005829
comment: Reactome DB_ID: 3661503
display name: LARG

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7U6
data source: Provenance1
name: ARHGC_HUMAN
name: Rho guanine nucleotide exchange factor 12
name: ARHGEF12
name: Q9Y7U6
xref: UnificationXref1341
feature: FragmentFeature238
cellular location: GO:0005829
comment: Reactome DB_ID: 3661504
display name: LARG

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTR5
data source: Provenance1
name: Q9UTR5
name: ARHGC_HUMAN
name: Rho guanine nucleotide exchange factor 12
name: ARHGEF12
xref: UnificationXref1342
feature: FragmentFeature239
cellular location: GO:0005829
comment: Reactome DB_ID: 3661505
display name: LARG

Homologues of NET1
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1347
cellular location: GO:0005829
comment: Reactome DB_ID: 3661510
comment: Converted from EntitySet in Reactome

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7U5
data source: Provenance1
name: ARHG8_HUMAN
name: Neuroepithelial cell-transforming gene 1 protein
name: Q9Y7U5
xref: UnificationXref1344
feature: FragmentFeature240
cellular location: GO:0005829
comment: Reactome DB_ID: 3661507
display name: NET1

UnificationXref1770
type: UnificationXref
id: 3659899
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659899

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7U6
data source: Provenance1
name: ARHG8_HUMAN
name: Neuroepithelial cell-transforming gene 1 protein
name: Q9Y7U6
xref: UnificationXref1345
feature: FragmentFeature241
cellular location: GO:0005829
comment: Reactome DB_ID: 3661508
display name: NET1

http://identifiers.org/pubmed/11742412
type: PublicationXref
id: 11742412
author: Saltiel, AR
author: Kahn, CR
db: Pubmed
title: Insulin signalling and the regulation of glucose and lipid metabolism
source: Nature 414:799-806
year: 2001

UnificationXref1769
type: UnificationXref
id: O43037
db: UniProt

UnificationXref1768
type: UnificationXref
id: 3659895
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659895

UnificationXref1762
type: UnificationXref
id: REACT_2376
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2376.2

UnificationXref1763
type: UnificationXref
id: P79063
db: UniProt

UnificationXref1760
type: UnificationXref
id: CHEBI:17843
db: ChEBI

UnificationXref1761
type: UnificationXref
id: 141679
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=141679

UnificationXref1766
type: UnificationXref
id: 3663503
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663503

UnificationXref1767
type: UnificationXref
id: Q1MTR2
db: UniProt

UnificationXref1764
type: UnificationXref
id: 3660553
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660553

UnificationXref1765
type: UnificationXref
id: O13824
db: UniProt

Homologues of ARHGAP31
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1359
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3661526

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74360
data source: Provenance1
name: ARHGAP31
name: O74360
xref: UnificationXref1357
feature: FragmentFeature246
cellular location: GO:0005829
comment: Reactome DB_ID: 3661524
display name: CdGAP

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74360
data source: Provenance1
name: ARHGAP32
name: O74360
xref: UnificationXref1353
feature: FragmentFeature244
cellular location: GO:0005829
comment: Reactome DB_ID: 3661518
display name: Grit

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14014
data source: Provenance1
name: ARHGAP32
name: O14014
xref: UnificationXref1355
feature: FragmentFeature245
cellular location: GO:0005829
comment: Reactome DB_ID: 3661522
display name: Grit

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43052
data source: Provenance1
name: O43052
name: Dlc-1
name: ARHGAP7
xref: UnificationXref1363
feature: FragmentFeature249
cellular location: GO:0005829
comment: Reactome DB_ID: 3661534
display name: DLC1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10164
data source: Provenance1
name: ArhGAP15
name: ARHGAP15
xref: UnificationXref1364
feature: FragmentFeature250
cellular location: GO:0005829
comment: Reactome DB_ID: 3661535
display name: Q10164

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14014
data source: Provenance1
name: ARHGAP31
name: O14014
xref: UnificationXref1358
feature: FragmentFeature247
cellular location: GO:0005829
comment: Reactome DB_ID: 3661525
display name: CdGAP

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09746
data source: Provenance1
name: Q09746
name: Trip10
name: TRIP10
xref: UnificationXref1361
feature: FragmentFeature248
cellular location: GO:0005829
comment: Reactome DB_ID: 3661530
display name: Rip1

UnificationXref1758
type: UnificationXref
id: 3663526
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663526

UnificationXref1757
type: UnificationXref
id: 3663527
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663527

UnificationXref1759
type: UnificationXref
id: 3663528
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663528

UnificationXref1753
type: UnificationXref
id: REACT_128867
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_128867.5

UnificationXref1754
type: UnificationXref
id: Q09820
db: UniProt

UnificationXref1755
type: UnificationXref
id: 3663488
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663488

UnificationXref1756
type: UnificationXref
id: 3663525
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663525

UnificationXref1750
type: UnificationXref
id: 3665496
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665496

UnificationXref1751
type: UnificationXref
id: REACT_130101
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_130101.5

UnificationXref1752
type: UnificationXref
id: 3665497
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665497

http://identifiers.org/pubmed/12669019
type: PublicationXref
id: 12669019
author: Desjardins, M
db: Pubmed
title: ER-mediated phagocytosis: a new membrane for new functions
source: Nat Rev Immunol 3:280-91
year: 2003

UnificationXref1749
type: UnificationXref
id: REACT_141943
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_141943.5

UnificationXref1748
type: UnificationXref
id: 3663136
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663136

UnificationXref1747
type: UnificationXref
id: 3663135
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663135

UnificationXref1746
type: UnificationXref
id: 3663134
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663134

UnificationXref1744
type: UnificationXref
id: O14089
db: UniProt

UnificationXref1745
type: UnificationXref
id: 3663126
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663126

UnificationXref1742
type: UnificationXref
id: 450597
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=450597

UniProt:P28040
type: ProteinReference
xref: UnificationXref5979
organism: BioSource1

UnificationXref1743
type: UnificationXref
id: REACT_26157
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_26157.1

UnificationXref1740
type: UnificationXref
id: 3665499
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665499

UnificationXref1741
type: UnificationXref
id: REACT_139276
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_139276.5

http://identifiers.org/pubmed/6434534
type: PublicationXref
id: 6434534
author: Gracy, RW
author: Yuan, PM
author: Lu, HS
db: Pubmed
title: Primary structure of human triosephosphate isomerase
source: J Biol Chem 259:11958-68
year: 1984

http://identifiers.org/pubmed/15274629
type: PublicationXref
id: 15274629
author: Takeuchi, N
author: Heck, A
author: Spencer, AC
author: Watanabe, K
author: Spremulli, LL
db: Pubmed
title: Characterization of the human mitochondrial methionyl-tRNA synthetase
source: Biochemistry 43:9743-54
year: 2004

http://identifiers.org/pubmed/7354069
type: PublicationXref
id: 7354069
author: Anderson, PM
author: Desnick, RJ
db: Pubmed
title: Purification and properties of uroporphyrinogen I synthase from human erythrocytes. Identification of stable enzyme-substrate intermediates.
source: J Biol Chem 255:1993-9
year: 1980

UnificationXref1730
type: UnificationXref
id: REACT_155194
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_155194.3

Utilization of Ketone Bodies
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction217
evidence: Evidence428
xref: UnificationXref2837
xref: UnificationXref2838
xref: RelationshipXref251
pathway order: PathwayStep419
display name: Ketone body catabolism
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UnificationXref1734
type: UnificationXref
id: REACT_26387
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_26387.1

UnificationXref1733
type: UnificationXref
id: 450523
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=450523

UnificationXref1732
type: UnificationXref
id: REACT_157138
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_157138.3

UnificationXref1731
type: UnificationXref
id: 3665498
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665498

UnificationXref1737
type: UnificationXref
id: 3663160
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663160

UnificationXref1738
type: UnificationXref
id: 3663169
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663169

UnificationXref1735
type: UnificationXref
id: P47979
db: UniProt

UnificationXref1736
type: UnificationXref
id: 3663159
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663159

UnificationXref1739
type: UnificationXref
id: REACT_145697
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_145697.5

http://identifiers.org/pubmed/17331073
type: PublicationXref
id: 17331073
author: Wei, Y
author: Hornemann, T
author: von Eckardstein, A
db: Pubmed
title: Is the mammalian serine palmitoyltransferase a high-molecular-mass complex?
source: Biochem J 405:157-64
year: 2007

http://identifiers.org/pubmed/14739303
type: PublicationXref
id: 14739303
author: Su, Xiaoqin
author: Shu, Hong-Bing
author: Han, Ke-Jun
author: Zhang, Jun
author: Bin, Liang-Hua
author: Xu, Liang-Guo
db: Pubmed
title: Mechanisms of the TRIF-induced interferon-stimulated response element and NF-kappaB activation and apoptosis pathways
source: J. Biol. Chem. 279:15652-61
year: 2004

http://identifiers.org/pubmed/7354072
type: PublicationXref
id: 7354072
author: Bodlaender, P
author: Shemin, D
author: Bevan, DR
db: Pubmed
title: Mechanism of porphobilinogen synthase. Requirement of Zn2+ for enzyme activity.
source: J Biol Chem 255:2030-5
year: 1980

UnificationXref1721
type: UnificationXref
id: P41836
db: UniProt

UnificationXref1720
type: UnificationXref
id: 3657874
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657874

UnificationXref1723
type: UnificationXref
id: 3657857
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657857

UnificationXref1722
type: UnificationXref
id: 3657818
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657818

UnificationXref1724
type: UnificationXref
id: 3657791
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657791

UnificationXref1725
type: UnificationXref
id: 3657796
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657796

UnificationXref1726
type: UnificationXref
id: O74894
db: UniProt

UnificationXref1727
type: UnificationXref
id: 3657814
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657814

UnificationXref1728
type: UnificationXref
id: 3657878
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657878

UnificationXref1729
type: UnificationXref
id: 3663158
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663158

Formation of the Early Elongation Complex
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction68
pathway component: BiochemicalReaction69
evidence: Evidence117
xref: RelationshipXref45
xref: UnificationXref613
xref: UnificationXref614
pathway order: PathwayStep115
pathway order: PathwayStep114
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UnificationXref1712
type: UnificationXref
id: 3657844
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657844

UnificationXref1711
type: UnificationXref
id: Q9US13
db: UniProt

UnificationXref1710
type: UnificationXref
id: 3657822
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657822

UnificationXref1719
type: UnificationXref
id: 3657775
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657775

UnificationXref1717
type: UnificationXref
id: 3657872
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657872

UnificationXref1718
type: UnificationXref
id: Q09841
db: UniProt

UnificationXref1715
type: UnificationXref
id: Q09720
db: UniProt

UnificationXref1716
type: UnificationXref
id: 3657779
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657779

UnificationXref1713
type: UnificationXref
id: Q9Y7T8
db: UniProt

UnificationXref1714
type: UnificationXref
id: 3657783
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657783

http://identifiers.org/pubmed/12515382
type: PublicationXref
id: 12515382
author: Arndt-Jovin, DJ
author: Ingelfinger, D
author: Achsel, T
author: Lührmann, R
db: Pubmed
title: The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci
source: RNA 8:1489-501
year: 2002

UnificationXref1701
type: UnificationXref
id: 3657798
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657798

Homologous DNA pairing and strand exchange
type: Pathway
data source: Provenance1
pathway component: Presynaptic phase of homologous DNA pairing and strand exchange
evidence: Evidence57
xref: UnificationXref242
xref: UnificationXref241
pathway order: PathwayStep56
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UnificationXref1700
type: UnificationXref
id: O43063
db: UniProt

UnificationXref1706
type: UnificationXref
id: 3657795
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657795

UnificationXref1707
type: UnificationXref
id: P36612
db: UniProt

UnificationXref1708
type: UnificationXref
id: 3657802
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657802

UnificationXref1709
type: UnificationXref
id: O74445
db: UniProt

UnificationXref1702
type: UnificationXref
id: O94444
db: UniProt

UnificationXref1703
type: UnificationXref
id: 3657856
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657856

UnificationXref1704
type: UnificationXref
id: Q9UT97
db: UniProt

UnificationXref1705
type: UnificationXref
id: 3657759
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657759

UniProt:P56286
type: ProteinReference
xref: UnificationXref7314
organism: BioSource1

UniProt:P56287
type: ProteinReference
xref: UnificationXref7389
organism: BioSource1

UniProt:P56288
type: ProteinReference
xref: UnificationXref7393
organism: BioSource1

UniProt:P56289
type: ProteinReference
xref: UnificationXref7945
organism: BioSource1

Metabolism of vitamins and cofactors
type: Pathway
data source: Provenance1
pathway component: REACT 90308.9
evidence: Evidence722
xref: RelationshipXref605
xref: UnificationXref4757
xref: UnificationXref4758
pathway order: PathwayStep712
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/9548747
type: PublicationXref
id: 9548747
author: Hammond, PW
author: Cech, TR
db: Pubmed
title: Euplotes telomerase: evidence for limited base-pairing during primer elongation and dGTP as an effector of translocation
source: Biochemistry 37:5162-72
year: 1998

http://identifiers.org/pubmed/9045610
type: PublicationXref
id: 9045610
author: Weaver, PL
author: Chuang, RY
author: Chang, TH
author: Liu, Z
db: Pubmed
title: Requirement of the DEAD-Box protein ded1p for messenger RNA translation.
source: Science 275:1468-71
year: 1997

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O42652
data source: Provenance1
name: Aspartate aminotransferase, cytoplasmic
name: AATC_HUMAN
name: O42652
xref: UnificationXref2395
feature: FragmentFeature522
cellular location: GO:0005829
comment: Reactome DB_ID: 3658227
display name: GOT1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O13844
data source: Provenance1
name: SLC25A1
name: tricarboxylate (citrate) transporter
xref: UnificationXref2408
feature: FragmentFeature523
cellular location: GO:0005743
comment: Reactome DB_ID: 3659947
display name: O13844

Q9Y7R8
type: Protein
entity reference: Q9Y7R8
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: malate dehydrogenase 2, NAD (mitochondrial)
name: malate dehydrogenase 2
name: Malate dehydrogenase, mitochondrial precursor
xref: UnificationXref2367
feature: FragmentFeature520
cellular location: GO:0005759
comment: Reactome DB_ID: 3658355
display name: MDH2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94320
data source: Provenance1
name: PXLP-GOT2
name: O94320
name: Transaminase A
name: glutamate oxaloacetate transaminase-2
name: Aspartate aminotransferase, mitochondrial precursor
name: aspartate aminotransferase, mitochondrial, apoenzyme monomer
xref: UnificationXref2382
feature: FragmentFeature521
feature: ModificationFeature64
cellular location: GO:0005759
comment: Reactome DB_ID: 3658236
display name: GOT2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74374
data source: Provenance1
name: Phosphoglucomutase
name: phosphoglucomutase 1
name: PGM1(2-562)
name: O74374
name: Glucose phosphomutase
xref: UnificationXref2436
feature: FragmentFeature526
cellular location: GO:0005829
comment: Reactome DB_ID: 3657990
display name: PGM1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74478
data source: Provenance1
name: Phosphoglucomutase-2
name: O74478
xref: UnificationXref2439
feature: FragmentFeature527
cellular location: GO:0005829
comment: Reactome DB_ID: 3657995
display name: PGM2

P09202
type: Protein
entity reference: P09202
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: fructose-1,6-bisphosphatase 1
name: D-fructose-1,6-bisphosphate 1-phosphohydrolase
xref: UnificationXref2420
feature: FragmentFeature524
cellular location: GO:0005829
comment: Reactome DB_ID: 3658111
display name: FBP1

P09202
type: Protein
entity reference: P09202
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: fructose-1,6-bisphosphatase 2
name: Fructose-1,6-bisphosphatase isozyme 2
name: D-fructose-1,6- bisphosphate 1-phosphohydrolase
xref: UnificationXref2422
feature: FragmentFeature525
cellular location: GO:0005829
comment: Reactome DB_ID: 3658113
display name: FBP2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O59819
data source: Provenance1
name: UDP-glucose pyrophosphorylase 2
name: UGP2(2-508)
name: O59819
name: UTP-glucose-1-phosphate uridylyltransferase
xref: UnificationXref2450
feature: FragmentFeature528
cellular location: GO:0005829
comment: Reactome DB_ID: 3658003
display name: UGP2

Homologues of UGP2(2-508)
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2453
cellular location: GO:0005829
comment: Reactome DB_ID: 3658008
comment: Converted from EntitySet in Reactome

http://identifiers.org/pubmed/3129195
type: PublicationXref
id: 3129195
author: Baeuerle, PA
author: Baltimore, D
db: Pubmed
title: Activation of DNA-binding activity in an apparently cytoplasmic precursor of the NF-kappa B transcription factor
source: Cell 53:211-7
year: 1988

RNA Polymerase II Transcription Initiation
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction57
pathway component: BiochemicalReaction59
pathway component: BiochemicalReaction58
evidence: Evidence103
xref: UnificationXref560
xref: RelationshipXref41
xref: UnificationXref561
pathway order: PathwayStep101
pathway order: PathwayStep99
pathway order: PathwayStep100
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Homologues of GAPDHS
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2282
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658070

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43026
data source: Provenance1
name: glyceraldehyde-3-phosphate dehydrogenase, testis-specific, monomer
name: O43026
xref: UnificationXref2280
feature: FragmentFeature512
cellular location: GO:0005829
comment: Reactome DB_ID: 3658068
display name: GAPDHS

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P78958
data source: Provenance1
name: glyceraldehyde-3-phosphate dehydrogenase, testis-specific, monomer
name: P78958
xref: UnificationXref2281
feature: FragmentFeature513
cellular location: GO:0005829
comment: Reactome DB_ID: 3658069
display name: GAPDHS

O60101
type: Protein
entity reference: O60101
data source: Provenance1
name: PRP 2
name: Note: the coordinates are copied over from Homo sapiens.
name: Phosphoglycerate kinase 1
name: Primer recognition protein 2
xref: UnificationXref2291
feature: FragmentFeature514
cellular location: GO:0005829
comment: Reactome DB_ID: 3658124
display name: PGK1

Homologues of ENO1
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2305
cellular location: GO:0005829
comment: Reactome DB_ID: 3658136
comment: Converted from EntitySet in Reactome

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P40370
data source: Provenance1
name: 2-phospho-D-glycerate hydro-lyase
name: P40370
name: Alpha enolase
name: Phosphopyruvate hydratase
name: Enolase 1
name: Non- neural enolase
name: enolase 1, (alpha)
name: ENO1
xref: UnificationXref2302
feature: FragmentFeature515
cellular location: GO:0005829
comment: Reactome DB_ID: 3658131
display name: NNE

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q8NKC2
data source: Provenance1
name: 2-phospho-D-glycerate hydro-lyase
name: Alpha enolase
name: Phosphopyruvate hydratase
name: Enolase 1
name: Non- neural enolase
name: enolase 1, (alpha)
name: Q8NKC2
name: ENO1
xref: UnificationXref2304
feature: FragmentFeature516
cellular location: GO:0005829
comment: Reactome DB_ID: 3658135
display name: NNE

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10208
data source: Provenance1
name: Pyruvate kinase, L isozyme
name: PKLR isoform 2
name: pyruvate kinase, liver and RBC
name: Red cell/liver pyruvate kinase
name: Q10208
name: PKLR isozyme L
xref: UnificationXref2318
feature: FragmentFeature518
cellular location: GO:0005829
comment: Reactome DB_ID: 3658492
display name: PKLR-2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10208
data source: Provenance1
name: PKM isozyme M1
name: pyruvate kinase, M1 isozyme
name: Q10208
name: PKM isoform 2
xref: UnificationXref2313
feature: FragmentFeature517
cellular location: GO:0005829
comment: Reactome DB_ID: 3658490
display name: PKM-2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UUE1
data source: Provenance1
name: Pyruvic carboxylase
name: Q9UUE1
name: Pyruvate carboxylase, mitochondrial precursor
name: pyruvate carboxylase
xref: UnificationXref2344
feature: FragmentFeature519
cellular location: GO:0005759
comment: Reactome DB_ID: 3658143
display name: PC

http://identifiers.org/pubmed/18772396
type: PublicationXref
id: 18772396
author: Zhang, X
author: Shinjo, SM
author: Rasheed, BA
author: Lin, JC
author: Carter, H
author: Jones, S
author: Keir, S
author: Parmigiani, G
author: Yan, H
author: McLendon, R
author: Olivi, A
author: Nikolsky, Y
author: Diaz Jr, LA
author: Tekleab, H
author: Vogelstein, B
author: Kinzler, KW
author: Velculescu, VE
author: Papadopoulos, N
author: Mankoo, P
author: Marie, SK
author: Parsons, DW
author: Busam, DA
author: Riggins, GJ
author: Bigner, DD
author: Karchin, R
author: Hartigan, J
author: Angenendt, P
author: Leary, RJ
author: Smith, DR
author: Strausberg, RL
author: Gallia, GL
author: Siu, IM
author: Nikolskaya, T
db: Pubmed
title: An integrated genomic analysis of human glioblastoma multiforme
source: Science 321:1807-12
year: 2008

http://identifiers.org/pubmed/17035995
type: PublicationXref
id: 17035995
author: De Camilli, P
author: Di Paolo, G
db: Pubmed
title: Phosphoinositides in cell regulation and membrane dynamics
source: Nature 443:651-7
year: 2006

PFK-B
type: Protein
entity reference: UniProt:O42938
data source: Provenance1
name: 6-phosphofructokinase, liver type
name: Note: the coordinates are copied over from Homo sapiens.
name: O42938
name: Phosphohexokinase
name: Phosphofructokinase 1
name: Phosphofructo-1-kinase isozyme B
xref: UnificationXref2233
feature: FragmentFeature507
cellular location: GO:0005829
comment: Reactome DB_ID: 3658085
display name: PFKL

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:O42938
data source: Provenance1
name: PFK-C
name: O42938
name: Phosphohexokinase
name: Phosphofructokinase 1
name: 6-phosphofructokinase, isozyme C
name: Phosphofructo-1-kinase isozyme C
name: 6-phosphofructokinase, type C
name: 6-phosphofructokinase, platelet type
name: K6PP_HUMAN
xref: UnificationXref2235
feature: FragmentFeature508
cellular location: GO:0005829
comment: Reactome DB_ID: 3658087
display name: PFKP

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09756
data source: Provenance1
name: glucokinase
name: Q09756
xref: UnificationXref2211
feature: FragmentFeature505
cellular location: GO:0005654
comment: Reactome DB_ID: 3660980
display name: GCK

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P78917
data source: Provenance1
name: P78917
name: Phosphoglucose isomerase
name: NLK
name: PGI
name: SA-36
name: Sperm antigen-36
name: Neuroleukin
name: Glucose-6-phosphate isomerase
name: PHI
name: Phosphohexose isomerase
xref: UnificationXref2225
feature: FragmentFeature506
cellular location: GO:0005829
comment: Reactome DB_ID: 3658103
display name: GPI

Homologues of GCK
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2212
cellular location: GO:0005654
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3660981

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P50521
data source: Provenance1
name: glucokinase
name: P50521
xref: UnificationXref2210
feature: FragmentFeature504
cellular location: GO:0005654
comment: Reactome DB_ID: 3660979
display name: GCK

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P78958
data source: Provenance1
name: Glyceraldehyde 3-phosphate dehydrogenase, liver
name: G3P2_HUMAN
name: glyceraldehyde-3-phosphate dehydrogenase monomer
name: G3P1_HUMAN
name: glyceraldehyde 3-phosphate dehydrogenase, liver
name: P78958
name: glyceraldehyde 3-phosphate dehydrogenase, muscle
xref: UnificationXref2277
feature: FragmentFeature511
cellular location: GO:0005829
comment: Reactome DB_ID: 3658065
display name: GAPDH

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43026
data source: Provenance1
name: Glyceraldehyde 3-phosphate dehydrogenase, liver
name: G3P2_HUMAN
name: glyceraldehyde-3-phosphate dehydrogenase monomer
name: G3P1_HUMAN
name: glyceraldehyde 3-phosphate dehydrogenase, liver
name: glyceraldehyde 3-phosphate dehydrogenase, muscle
name: O43026
xref: UnificationXref2275
feature: FragmentFeature510
cellular location: GO:0005829
comment: Reactome DB_ID: 3658061
display name: GAPDH

Homologues of GAPDH
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2278
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658066

P07669
type: Protein
entity reference: UniProt:P07669
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: triosephosphate isomerase monomer
name: TPI1
name: TPIS_HUMAN
name: Triosephosphate isomerase
xref: UnificationXref2261
feature: FragmentFeature509
cellular location: GO:0005829
comment: Reactome DB_ID: 3658078
display name: TIM

http://identifiers.org/pubmed/2040271
type: PublicationXref
id: 2040271
author: Sadahiro, S
author: Matsuda, T
author: Takenaka, M
author: Tanaka, T
author: Noguchi, T
author: Hirai, H
author: Imai, E
author: Yamada, K
db: Pubmed
title: Isolation and characterization of the human pyruvate kinase M gene
source: Eur J Biochem 198:101-6
year: 1991

Eukaryotic Translation Elongation
type: Pathway
data source: Provenance1
pathway component: REACT 142693.5
evidence: Evidence1173
xref: UnificationXref7488
xref: RelationshipXref971
xref: UnificationXref7489
pathway order: PathwayStep1152
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Homologues of GCK
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2200
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658047

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P50521
data source: Provenance1
name: glucokinase
name: P50521
xref: UnificationXref2197
feature: FragmentFeature498
cellular location: GO:0005829
comment: Reactome DB_ID: 3658042
display name: GCK

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09756
data source: Provenance1
name: glucokinase
name: Q09756
xref: UnificationXref2199
feature: FragmentFeature499
cellular location: GO:0005829
comment: Reactome DB_ID: 3658046
display name: GCK

Homologues of HK1
type: Protein
data source: Provenance1
member physical entity: HK I
xref: UnificationXref2203
cellular location: GO:0005829
comment: Reactome DB_ID: 3658050
comment: Converted from EntitySet in Reactome

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O42893
data source: Provenance1
name: N-seryl-glycosylphosphatidylinositolethanolamine-TREH
name: O42893
name: trehalase
xref: UnificationXref2186
feature: FragmentFeature497
feature: ModificationFeature63
cellular location: GO:0005886
comment: Reactome DB_ID: 3661190
display name: TREH

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09756
data source: Provenance1
name: HK III
name: HXK3_HUMAN
name: Q09756
name: Hexokinase type III
name: hexokinase leukocyte form
name: hexokinase 3
name: hexokinase type 3
xref: UnificationXref2205
feature: FragmentFeature503
cellular location: GO:0005829
comment: Reactome DB_ID: 3658052
display name: HK3

HK I
type: Protein
entity reference: Q09756
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Hexokinase, type I
name: Brain form hexokinase
name: Q09756
name: hexokinase 1
name: HXK1_HUMAN
name: hexokinase brain form
name: hexokinase type 1
xref: UnificationXref2202
feature: FragmentFeature501
cellular location: GO:0005829
comment: Reactome DB_ID: 3658049
display name: HK1

HK I
type: Protein
entity reference: P50521
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Hexokinase, type I
name: Brain form hexokinase
name: P50521
name: hexokinase 1
name: HXK1_HUMAN
name: hexokinase brain form
name: hexokinase type 1
xref: UnificationXref2201
feature: FragmentFeature500
cellular location: GO:0005829
comment: Reactome DB_ID: 3658048
display name: HK1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P50521
data source: Provenance1
name: HK III
name: HXK3_HUMAN
name: Hexokinase type III
name: P50521
name: hexokinase leukocyte form
name: hexokinase 3
name: hexokinase type 3
xref: UnificationXref2204
feature: FragmentFeature502
cellular location: GO:0005829
comment: Reactome DB_ID: 3658051
display name: HK3

Homologues of HK3
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2206
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658053

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UUJ6
data source: Provenance1
name: Q9UUJ6
name: lipin 2
xref: UnificationXref2805
feature: FragmentFeature559
cellular location: GO:0005789
comment: Reactome DB_ID: 3660004
display name: LPIN2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UUJ6
data source: Provenance1
name: Q9UUJ6
name: lipin 1
xref: UnificationXref2804
feature: FragmentFeature558
cellular location: GO:0005789
comment: Reactome DB_ID: 3660003
display name: LPIN1

LPIN1 or 2 or 3
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2806
cellular location: GO:0005789
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3660005
display name: lipins

AGPAT8
type: Protein
entity reference: O94361
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: ALCAT1
name: O94361
name: 1-acylglycerol-3-phosphate O-acyltransferase 8
name: Lysocardiolipin acyltransferase 1
xref: UnificationXref2793
feature: FragmentFeature557
cellular location: GO:0005789
comment: Reactome DB_ID: 3659995
display name: LCLAT1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P54874
data source: Provenance1
name: P54874
name: hydroxymethylglutaryl-CoA synthase
name: Hydroxymethylglutaryl-CoA synthase, mitochondrial precursor
name: 3-hydroxy-3-methylglutaryl coenzyme A synthase
name: HMG-CoA synthase
xref: UnificationXref2830
feature: FragmentFeature561
cellular location: GO:0005759
comment: Reactome DB_ID: 3659517
display name: HMGCS2

Q9UQW6
type: Protein
entity reference: Q9UQW6
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Acetyl-CoA acetyltransferase, mitochondrial
name: acetyl-CoA acetyltransferase
name: Acetoacetyl-CoA thiolase
name: ACAT1(35-427)
xref: UnificationXref2822
feature: FragmentFeature560
cellular location: GO:0005759
comment: Reactome DB_ID: 3658307
display name: ACAT1

Q9US20
type: Protein
entity reference: Q9US20
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Lysophosphatidic acid acyltransferase-beta
name: LPAAT-beta
name: 1-acylglycerol-3-phosphate O- acyltransferase 2
name: 1- AGP acyltransferase 2
name: 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
xref: UnificationXref2791
feature: FragmentFeature556
cellular location: GO:0005789
comment: Reactome DB_ID: 3659991
display name: AGPAT2

http://identifiers.org/pubmed/3356695
type: PublicationXref
id: 3356695
author: Panniers, R
author: Rowlands, AG
author: Henshaw, EC
db: Pubmed
title: The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2.
source: J Biol Chem 263:5526-33
year: 1988

LPAAT-alpha
type: Protein
entity reference: Q9US20
data source: Provenance1
name: Q9US20
name: Note: the coordinates are copied over from Homo sapiens.
name: G15 protein
name: Lysophosphatidic acid acyltransferase-alpha
name: 1-acylglycerol-3-phosphate O- acyltransferase 1
name: 1- AGP acyltransferase 1
name: 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
xref: UnificationXref2790
feature: FragmentFeature555
cellular location: GO:0005789
comment: Reactome DB_ID: 3659990
display name: AGPAT1

LPAAT
type: Protein
data source: Provenance1
member physical entity: AGPAT8
member physical entity: Q9US20
member physical entity: LPAAT-alpha
xref: UnificationXref2794
cellular location: GO:0005789
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659996
display name: AGPAT

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94511
data source: Provenance1
name: Trans-2,3-enoyl-CoA reductase
name: O94511
xref: UnificationXref2773
feature: FragmentFeature554
cellular location: GO:0005789
comment: Reactome DB_ID: 3663276
display name: TECR

http://identifiers.org/pubmed/17402747
type: PublicationXref
id: 17402747
author: Magni, G
author: Franchetti, P
author: Cimadamore, F
author: Cappellacci, L
author: Orsomando, G
author: Scotti, S
author: Sorci, L
author: Petrelli, R
db: Pubmed
title: Initial-rate kinetics of human NMN-adenylyltransferases: substrate and metal ion specificity, inhibition by products and multisubstrate analogues, and isozyme contributions to NAD+ biosynthesis
source: Biochemistry 46:4912-22
year: 2007

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94305
data source: Provenance1
name: O94305
name: Monoglyceride lipase
xref: UnificationXref2713
feature: FragmentFeature549
cellular location: GO:0005811
comment: Reactome DB_ID: 3660717
display name: MGLL

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09790
data source: Provenance1
name: Q09790
name: DIPP3A
name: NUDT10
xref: UnificationXref2661
feature: FragmentFeature548
cellular location: GO:0005829
comment: Reactome DB_ID: 3664569
display name: APS2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P78820
data source: Provenance1
name: ACACA_HUMAN
name: Btn-ACACA
name: P78820
name: Acetyl-CoA carboxylase 1
xref: UnificationXref2740
feature: FragmentFeature551
feature: ModificationFeature65
cellular location: GO:0005829
comment: Reactome DB_ID: 3659958
display name: ACC1

ATP citrate lyase
type: Protein
entity reference: Q9P7W3
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: ATP-citrate (pro-S-)-lyase
name: ATP-citrate synthase
name: Q9P7W3
name: citrate lyase monomer
name: Citrate cleavage enzyme
xref: UnificationXref2728
feature: FragmentFeature550
cellular location: GO:0005829
comment: Reactome DB_ID: 3659940
display name: ACLY

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O60135
data source: Provenance1
name: Long-chain-fatty-acid--CoA ligase 4
name: O60135
xref: UnificationXref2752
feature: FragmentFeature552
cellular location: GO:0005789
comment: Reactome DB_ID: 3659978
display name: ACSL4

Homologues of ACSL4
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2755
cellular location: GO:0005789
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659983

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9P7D7
data source: Provenance1
name: Long-chain-fatty-acid--CoA ligase 4
name: Q9P7D7
xref: UnificationXref2754
feature: FragmentFeature553
cellular location: GO:0005789
comment: Reactome DB_ID: 3659982
display name: ACSL4

http://identifiers.org/pubmed/2069720
type: PublicationXref
id: 2069720
author: Myöhänen, S
author: Kauppinen, L
author: Jänne, J
author: Wahlfors, J
author: Alhonen, L
db: Pubmed
title: Human spermidine synthase gene: structure and chromosomal localization
source: DNA Cell Biol 10:467-74
year: 1991

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74561
data source: Provenance1
name: O74561
name: IHPK3
xref: UnificationXref2628
feature: FragmentFeature545
cellular location: GO:0005829
comment: Reactome DB_ID: 3664558
display name: IP6K3

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09790
data source: Provenance1
name: Q09790
name: NUDT3
name: DIPP1
xref: UnificationXref2659
feature: FragmentFeature547
cellular location: GO:0005829
comment: Reactome DB_ID: 3664565
display name: DIPP

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09790
data source: Provenance1
name: Q09790
name: DIPP2
name: HDCMB47P
name: KIAA0487
xref: UnificationXref2645
feature: FragmentFeature546
cellular location: GO:0005829
comment: Reactome DB_ID: 3664567
display name: NUDT4

IHPK1
type: Protein
entity reference: O74561
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: KIAA0263
name: O74561
xref: UnificationXref2627
feature: FragmentFeature544
cellular location: GO:0005829
comment: Reactome DB_ID: 3664557
display name: IP6K1

PublicationXref226
type: PublicationXref
id: 12676795
author: Reichardt, LF
author: Huang, EJ
db: Pubmed
title: Trk receptors: roles in neuronal signal transduction
source: Annu Rev Biochem 72:609-42
year: 2003

IP6K1/3
type: Protein
data source: Provenance1
member physical entity: IHPK1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2629
cellular location: GO:0005829
comment: Reactome DB_ID: 3664559
comment: Converted from EntitySet in Reactome

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74561
data source: Provenance1
name: TCCCIA00113
name: IP6K2_HUMAN
name: O74561
name: Inositol hexakisphosphate kinase 2
name: IHPK2
xref: UnificationXref2591
feature: FragmentFeature543
cellular location: GO:0005654
comment: Reactome DB_ID: 3664553
display name: IP6K2

IHPK1
type: Protein
entity reference: O74561
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: KIAA0263
name: O74561
xref: UnificationXref2590
feature: FragmentFeature542
cellular location: GO:0005654
comment: Reactome DB_ID: 3664552
display name: IP6K1

IP6K1/2
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
member physical entity: IHPK1
xref: UnificationXref2592
cellular location: GO:0005654
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3664554

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43001
data source: Provenance1
name: O43001
name: KIAA0910
xref: UnificationXref2577
feature: FragmentFeature541
cellular location: GO:0005829
comment: Reactome DB_ID: 3664279
display name: SYNJ1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9USQ6
data source: Provenance1
name: Q9USQ6
name: KIAA0910
xref: UnificationXref2575
feature: FragmentFeature540
cellular location: GO:0005829
comment: Reactome DB_ID: 3664275
display name: SYNJ1

http://identifiers.org/pubmed/17590538
type: PublicationXref
id: 17590538
author: Ball, E
author: Takeuchi, M
author: Harigai, M
author: Kamatani, N
author: Furuichi, K
author: Abe, J
author: Momohara, S
db: Pubmed
title: Cloning and characterization of DPPL1 and DPPL2, representatives of a novel type of mammalian phosphatidate phosphatase
source: Gene 399:174-80
year: 2007

Homologues of SYNJ1
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2578
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3664280

O94413
type: Protein
entity reference: O94413
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Ribose-phosphate pyrophosphokinase I
name: PPRibP
name: phosphoribosyl pyrophosphate synthetase 1
name: PRS-I
name: Phosphoribosyl pyrophosphate synthetase I
name: Ribose-phosphate pyrophosphokinase I (EC 2.7.6.1) (Phosphoribosyl pyrophosphate synthetase I) (PPRibP) (PRS-I)
xref: UnificationXref2555
feature: FragmentFeature539
cellular location: GO:0005829
comment: Reactome DB_ID: 3659323
display name: PRPS1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTL3
data source: Provenance1
name: RPIA(1-237)
name: ribose 5-phosphate isomerase
name: Q9UTL3
xref: UnificationXref2538
feature: FragmentFeature538
cellular location: GO:0005829
comment: Reactome DB_ID: 3658453
display name: RPIA

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74455
data source: Provenance1
name: O74455
name: PGLS(2-258)
name: 6-phosphogluconolactonase
xref: UnificationXref2499
feature: FragmentFeature534
cellular location: GO:0005829
comment: Reactome DB_ID: 3658433
display name: 6PGL

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O00091
data source: Provenance1
name: O00091
name: Glucose-6-phosphate 1-dehydrogenase
xref: UnificationXref2489
feature: FragmentFeature533
cellular location: GO:0005829
comment: Reactome DB_ID: 3658033
display name: G6PD

O14105
type: Protein
entity reference: O14105
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Ribulose-phosphate 3-epimerase
name: Ribulose-5-phosphate-3- epimerase
name: HUSSY-17
name: ribulose phosphate 3-epimerase
name: ribulose-5-phosphate epimerase
name: phosphopentose isomerase
xref: UnificationXref2516
feature: FragmentFeature536
cellular location: GO:0005829
comment: Reactome DB_ID: 3658446
display name: RPE

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P78812
data source: Provenance1
name: 6-phosphogluconate dehydrogenase, decarboxylating
name: phosphogluconate dehydrogenase
name: P78812
name: 6-phosphogluconate 2-dehydrogenase
name: PGD(2-483)
xref: UnificationXref2508
feature: FragmentFeature535
cellular location: GO:0005829
comment: Reactome DB_ID: 3658439
display name: PGD

Homologues of GALE
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2479
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658026

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9HDU5
data source: Provenance1
name: Q9HDU5
name: Galactose-1-phosphate uridylyltransferase
xref: UnificationXref2472
feature: FragmentFeature530
cellular location: GO:0005829
comment: Reactome DB_ID: 3658015
display name: GALT

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7X5
data source: Provenance1
name: UDP- galactose 4-epimerase
name: UDP-galactose 4-epimerase
name: UDP-glucose 4-epimerase
name: UDP-galactose 4-epimerase apoenzyme
name: GALE_HUMAN
name: Galactowaldenase
name: Q9Y7X5
xref: UnificationXref2478
feature: FragmentFeature532
cellular location: GO:0005829
comment: Reactome DB_ID: 3658025
display name: GALE

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9HDU3
data source: Provenance1
name: UDP- galactose 4-epimerase
name: UDP-galactose 4-epimerase
name: UDP-glucose 4-epimerase
name: UDP-galactose 4-epimerase apoenzyme
name: GALE_HUMAN
name: Galactowaldenase
name: Q9HDU3
xref: UnificationXref2476
feature: FragmentFeature531
cellular location: GO:0005829
comment: Reactome DB_ID: 3658021
display name: GALE

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P78811
data source: Provenance1
name: UDP-glucose pyrophosphorylase 2
name: UGP2(2-508)
name: P78811
name: UTP-glucose-1-phosphate uridylyltransferase
xref: UnificationXref2452
feature: FragmentFeature529
cellular location: GO:0005829
comment: Reactome DB_ID: 3658007
display name: UGP2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O42700
data source: Provenance1
name: transaldolase 1
name: O42700
xref: UnificationXref2529
feature: FragmentFeature537
cellular location: GO:0005829
comment: Reactome DB_ID: 3658459
display name: TALDO1

S6K1-mediated signalling
type: Pathway
data source: Provenance1
pathway component: S6K1 signalling
pathway component: Activation of S6K1
evidence: Evidence206
xref: UnificationXref1107
xref: UnificationXref1108
pathway order: PathwayStep200
pathway order: PathwayStep203
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/22798961
type: PublicationXref
id: 22798961
author: Wang, Xiaohong
author: Li, Ju-Pi
author: Chuang, Huai-Chia
author: Tan, Tse-Hua
db: Pubmed
title: Regulation of PKC-? function by phosphorylation in T cell receptor signaling
source: Front Immunol 3:197
year: 2012

http://identifiers.org/pubmed/19416660
type: PublicationXref
id: 19416660
author: Ren, M
author: Xu, Y
author: Malhotra, A
author: Schlame, M
db: Pubmed
title: Formation of molecular species of mitochondrial cardiolipin. 1. A novel transacylation mechanism to shuttle fatty acids between sn-1 and sn-2 positions of multiple phospholipid species
source: Biochim Biophys Acta 1791:314-20
year: 2009

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O13963
data source: Provenance1
name: MVD(2-400)
name: Diphosphomevalonate decarboxylase
xref: UnificationXref2954
feature: FragmentFeature573
cellular location: GO:0005829
comment: Reactome DB_ID: 3661333
display name: O13963

Glutathione conjugation
type: Pathway
data source: Provenance1
pathway component: REACT 133499.5
evidence: Evidence832
xref: UnificationXref5526
xref: UnificationXref5525
xref: RelationshipXref763
pathway order: PathwayStep822
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/14660560
type: PublicationXref
id: 14660560
author: Yu, Y
author: Arnold, E
author: Shen, N
author: Ding, Jianping
author: Xu, X
author: Jin, Y
author: Xu, F
author: Jia, J
author: Liu, Y
db: Pubmed
title: Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: insights into substrate recognition, tRNA binding, and angiogenesis activity
source: J Biol Chem 279:8378-88
year: 2004

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10132
data source: Provenance1
name: Q10132
name: IDI1_HUMAN
name: Isopentenyl-diphosphate delta-isomerase 1
xref: UnificationXref2962
feature: FragmentFeature574
cellular location: GO:0005829
comment: Reactome DB_ID: 3661318
display name: IDI1

Homologues of FDPS
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
member physical entity: O14230
xref: UnificationXref2973
cellular location: GO:0005829
comment: Reactome DB_ID: 3661285
comment: Converted from EntitySet in Reactome

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O59703
data source: Provenance1
name: O59703
name: farnesyl diphosphate synthase
xref: UnificationXref2970
feature: FragmentFeature575
cellular location: GO:0005829
comment: Reactome DB_ID: 3661280
display name: FDPS

2-hydroxyphytanoyl-CoA lyase
type: Protein
entity reference: Q9Y7M1
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Q9Y7M1
name: 2-hydroxyacyl-CoA lyase 1
xref: UnificationXref2918
feature: FragmentFeature571
cellular location: GO:0005782
comment: Reactome DB_ID: 3662477
display name: HACL1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09780
data source: Provenance1
name: Q09780
name: Mevalonate kinase
xref: UnificationXref2943
feature: FragmentFeature572
cellular location: GO:0005829
comment: Reactome DB_ID: 3661311
display name: MVK

http://identifiers.org/pubmed/15381398
type: PublicationXref
id: 15381398
author: Jaffe, EK
db: Pubmed
title: The porphobilinogen synthase catalyzed reaction mechanism
source: Bioorg Chem 32:316-25
year: 2004

http://identifiers.org/pubmed/14660569
type: PublicationXref
id: 14660569
author: Chaussade, C
author: Mandel, JL
author: Liaubet, L
author: Payrastre, B
author: Pendaries, C
author: Tronchère, H
author: Laporte, J
author: Pirola, L
db: Pubmed
title: Production of phosphatidylinositol 5-phosphate by the phosphoinositide 3-phosphatase myotubularin in mammalian cells
source: J Biol Chem 279:7304-12
year: 2004

O14230
type: Protein
entity reference: O14230
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: farnesyl diphosphate synthase
xref: UnificationXref2972
feature: FragmentFeature576
cellular location: GO:0005829
comment: Reactome DB_ID: 3661284
display name: FDPS

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36596
data source: Provenance1
name: presqualene-di-diphosphate synthase
name: farnesyltransferase
name: Farnesyl-diphosphate farnesyltransferase
name: squalene synthase
name: P36596
xref: UnificationXref2987
feature: FragmentFeature577
cellular location: GO:0005789
comment: Reactome DB_ID: 3661325
display name: FDFT1

Q9C1W3
type: Protein
entity reference: UniProt:Q9C1W3
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: squalene epoxidase
name: Squalene monooxygenase
xref: UnificationXref3003
feature: FragmentFeature578
cellular location: GO:0005789
comment: Reactome DB_ID: 3661273
display name: SQLE

Q10231
type: Protein
entity reference: UniProt:Q10231
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Lanosterol synthase
xref: UnificationXref3013
feature: FragmentFeature579
cellular location: GO:0005789
comment: Reactome DB_ID: 3661305
display name: LSS

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36611
data source: Provenance1
name: P36611
name: NF-YB
xref: UnificationXref2862
feature: FragmentFeature565
cellular location: GO:0005654
comment: Reactome DB_ID: 3664204
display name: NFYB

3-hydroxy-3-methylglutaryl-coenzyme A reductase-1
type: Protein
entity reference: UniProt:Q10283
data source: Provenance1
name: HMGCR-1
name: Note: the coordinates are copied over from Homo sapiens.
name: HMDH_HUMAN
name: HMGCR isoform 1
xref: UnificationXref2868
feature: FragmentFeature566
cellular location: GO:0005789
comment: Reactome DB_ID: 3661298
display name: Q10283

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P79007
data source: Provenance1
name: Nuclear transcription factor Y subunit gamma
name: NFYC_HUMAN
name: NF-YC
name: P79007
xref: UnificationXref2858
feature: FragmentFeature563
cellular location: GO:0005654
comment: Reactome DB_ID: 3664208
display name: NFYC

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P24488
data source: Provenance1
name: P24488
name: NF-YA
xref: UnificationXref2860
feature: FragmentFeature564
cellular location: GO:0005654
comment: Reactome DB_ID: 3664212
display name: NFYA

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14400
data source: Provenance1
name: O14400
xref: UnificationXref2853
feature: FragmentFeature562
cellular location: GO:0005743
comment: Reactome DB_ID: 3661183
display name: GPD2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9USU1
data source: Provenance1
name: Q9USU1
name: Ral guanine nucleotide dissociation stimulator-like 1
name: RGL1_HUMAN
xref: UnificationXref2890
feature: FragmentFeature570
cellular location: GO:0005829
comment: Reactome DB_ID: 3664639
display name: RGL1

Homologues of RGL1
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2891
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3664640

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P26674
data source: Provenance1
name: Ral guanine nucleotide dissociation stimulator-like 1
name: P26674
name: RGL1_HUMAN
xref: UnificationXref2888
feature: FragmentFeature569
cellular location: GO:0005829
comment: Reactome DB_ID: 3664635
display name: RGL1

Hydroxymethylglutaryl-CoA synthase
type: Protein
entity reference: P54874
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: P54874
xref: UnificationXref2876
feature: FragmentFeature567
cellular location: GO:0005829
comment: Reactome DB_ID: 3661292
display name: HMGCS1

wee1
type: ProteinReference
name: UniProt:P07527 wee1
name: SPCC18B5.03
xref: UnificationXref7523
comment: FUNCTION Protein kinase that acts both on serines and on tyrosines. It acts as a dosage-dependent negative regulator of entry into mitosis (G2 to M transition). Phosphorylates and inhibits cdc2.CATALYTIC ACTIVITY ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.ENZYME REGULATION Negatively regulated by phosphorylation in the M-phase.PTM Phosphorylated in the C-terminal by NIM1/CDR1.SIMILARITY Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily.SIMILARITY Contains 1 protein kinase domain.
organism: BioSource1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10333
data source: Provenance1
name: Peroxisomal membrane protein 11A
name: Q10333
name: PX11A_HUMAN
xref: UnificationXref2884
feature: FragmentFeature568
cellular location: GO:0005778
comment: Reactome DB_ID: 3664628
display name: PEX11A

PublicationXref286
type: PublicationXref
id: 8276860
author: Cerione, RA
author: Aaronson, SA
author: Eva, A
author: Evans, T
author: Zheng, Y
author: Zangrilli, D
author: Hart, MJ
db: Pubmed
title: Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product
source: J Biol Chem 269:62-5
year: 1994

Lysine catabolism
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction444
pathway component: BiochemicalReaction442
pathway component: BiochemicalReaction445
pathway component: BiochemicalReaction443
evidence: Evidence752
xref: UnificationXref4957
xref: UnificationXref4958
xref: RelationshipXref641
pathway order: PathwayStep740
pathway order: PathwayStep741
pathway order: PathwayStep739
pathway order: PathwayStep742
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/9188692
type: PublicationXref
id: 9188692
author: Gill, GN
author: Kurten, RC
author: Cadena, DL
db: Pubmed
title: The product of the MLD gene is a member of the membrane fatty acid desaturase family: overexpression of MLD inhibits EGF receptor biosynthesis
source: Biochemistry 36:6960-7
year: 1997

http://identifiers.org/pubmed/7923172
type: PublicationXref
id: 7923172
author: Momparler, RL
author: Laliberte, J
db: Pubmed
title: Human cytidine deaminase: purification of enzyme, cloning, and expression of its complementary DNA
source: Cancer Res 54:5401-7
year: 1994

http://identifiers.org/pubmed/20435355
type: PublicationXref
id: 20435355
author: Palczewski, Krzysztof
db: Pubmed
title: Retinoids for treatment of retinal diseases
source: Trends Pharmacol. Sci. 31:284-95
year: 2010

http://identifiers.org/pubmed/20462400
type: PublicationXref
id: 20462400
author: Henley, Jeremy M
author: Wilkinson, Kevin A
db: Pubmed
title: Mechanisms, regulation and consequences of protein SUMOylation
source: Biochem. J. 428:133-45
year: 2010

CDK-mediated phosphorylation and removal of Cdc6
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction548
pathway component: BiochemicalReaction546
pathway component: BiochemicalReaction547
evidence: Evidence927
xref: UnificationXref6050
xref: UnificationXref6049
pathway order: PathwayStep910
pathway order: PathwayStep912
pathway order: PathwayStep911
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/8330740
type: PublicationXref
id: 8330740
author: Greider, CW
author: Collins, K
db: Pubmed
title: Tetrahymena telomerase catalyzes nucleolytic cleavage and nonprocessive elongation
source: Genes Dev 7:1364-76
year: 1993

http://identifiers.org/pubmed/2542324
type: PublicationXref
id: 2542324
author: Kishi, F
author: Kajii, T
author: Sakurai, M
author: Matsuura, S
author: Fujii, H
author: Nakazawa, A
author: Yamada, M
author: Tanizawa, Y
author: Miwa, S
author: Igarashi, M
db: Pubmed
title: Human adenylate kinase deficiency associated with hemolytic anemia. A single base substitution affecting solubility and catalytic activity of the cytosolic adenylate kinase.
source: J Biol Chem 264:10148-55
year: 1989

UniProt:P24339
type: ProteinReference
xref: UnificationXref919
organism: BioSource1

Axon guidance
type: Pathway
data source: Provenance1
pathway component: REACT 32304.10
pathway component: REACT 107867.9
evidence: Evidence1402
xref: RelationshipXref1107
xref: UnificationXref8698
xref: UnificationXref8697
pathway order: PathwayStep1370
pathway order: PathwayStep1375
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/10648173
type: PublicationXref
id: 10648173
author: Menear, K
author: Baldock, D
author: Graff, P
author: Jones, CE
author: Akhlaq, M
author: Graham, B
db: Pubmed
title: Purification and characterization of human Syk produced using a baculovirus expression system
source: Protein Expr Purif 18:86-94
year: 2000

http://identifiers.org/pubmed/19261456
type: PublicationXref
id: 19261456
author: Procko, E
author: Gaudet, R
db: Pubmed
title: Antigen processing and presentation: TAPping into ABC transporters
source: Curr Opin Immunol 21:84-91
year: 2009

UnificationXref1874
type: UnificationXref
id: 3658630
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658630

UnificationXref1875
type: UnificationXref
id: 3658631
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658631

UnificationXref1876
type: UnificationXref
id: Q9P4W9
db: UniProt

UnificationXref1877
type: UnificationXref
id: 3658776
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658776

UnificationXref1870
type: UnificationXref
id: 3658709
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658709

UnificationXref1871
type: UnificationXref
id: O13614
db: UniProt

UnificationXref1872
type: UnificationXref
id: 3658626
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658626

UnificationXref1873
type: UnificationXref
id: O14112
db: UniProt

UnificationXref1879
type: UnificationXref
id: 3658780
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658780

UnificationXref1878
type: UnificationXref
id: P87158
db: UniProt

UnificationXref1865
type: UnificationXref
id: 3658689
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658689

UnificationXref1866
type: UnificationXref
id: 3658690
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658690

UnificationXref1863
type: UnificationXref
id: 3658685
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658685

UnificationXref1864
type: UnificationXref
id: P58234
db: UniProt

UnificationXref1861
type: UnificationXref
id: 3658743
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658743

UnificationXref1862
type: UnificationXref
id: P79016
db: UniProt

UnificationXref1860
type: UnificationXref
id: 3658742
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658742

http://identifiers.org/pubmed/9949182
type: PublicationXref
id: 9949182
author: Pébusque, MJ
author: Grégoire, MJ
author: Zhang, B
author: Jonveaux, P
author: Popovici, C
author: Lafage-Pochitaloff, M
author: Birnbaum, D
db: Pubmed
title: The t(6;8)(q27;p11) translocation in a stem cell myeloproliferative disorder fuses a novel gene, FOP, to fibroblast growth factor receptor 1
source: Blood 93:1381-9
year: 1999

UnificationXref1869
type: UnificationXref
id: P79057
db: UniProt

UnificationXref1868
type: UnificationXref
id: 3658666
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658666

UnificationXref1867
type: UnificationXref
id: O60144
db: UniProt

http://identifiers.org/pubmed/4358634
type: PublicationXref
id: 4358634
author: Roth, DG
author: Deuel, TF
author: Shelton, E
db: Pubmed
title: Purification and properties of phosphoribosyl pyrophosphate synthetase from rat liver
source: J Biol Chem 249:291-296
year: 1974

UnificationXref1890
type: UnificationXref
id: O74329
db: UniProt

UnificationXref1891
type: UnificationXref
id: 3658753
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658753

UnificationXref1892
type: UnificationXref
id: Q10101
db: UniProt

UnificationXref1893
type: UnificationXref
id: 3658807
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658807

UnificationXref1894
type: UnificationXref
id: 3658836
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658836

UnificationXref1895
type: UnificationXref
id: P05732
db: UniProt

UnificationXref1896
type: UnificationXref
id: 3659055
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659055

UnificationXref1897
type: UnificationXref
id: P78946
db: UniProt

UnificationXref1898
type: UnificationXref
id: 3659105
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659105

UnificationXref1899
type: UnificationXref
id: P17478
db: UniProt

UniProt:P22193
type: ProteinReference
xref: UnificationXref7566
organism: BioSource1

http://identifiers.org/pubmed/1439791
type: PublicationXref
id: 1439791
author: Cerione, RA
author: Witte, ON
author: Leonard, D
author: Maru, Y
author: Evans, T
author: Hart, MJ
db: Pubmed
title: A GDP dissociation inhibitor that serves as a GTPase inhibitor for the Ras-like protein CDC42Hs
source: Science 258:812-5
year: 1992

UnificationXref1880
type: UnificationXref
id: Q9USW5
db: UniProt

UnificationXref1883
type: UnificationXref
id: O74892
db: UniProt

UnificationXref1884
type: UnificationXref
id: 3658695
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658695

UnificationXref1881
type: UnificationXref
id: 3658784
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658784

UnificationXref1882
type: UnificationXref
id: 3658785
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658785

UnificationXref1887
type: UnificationXref
id: Q9P546
db: UniProt

UnificationXref1888
type: UnificationXref
id: 3658833
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658833

UnificationXref1885
type: UnificationXref
id: Q9Y7L8
db: UniProt

UnificationXref1886
type: UnificationXref
id: 3658829
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658829

UnificationXref1889
type: UnificationXref
id: 3658834
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658834

http://identifiers.org/pubmed/13679574
type: PublicationXref
id: 13679574
author: Bouvier, M
author: Rousseau, G
author: Angers, S
author: Charest, PG
author: Kohout, T
author: Azzi, M
author: Piñeyro, G
db: Pubmed
title: Beta-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors
source: Proc Natl Acad Sci U S A 100:11406-11
year: 2003

Biotin transport and metabolism
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction403
pathway component: BiochemicalReaction401
pathway component: BiochemicalReaction402
evidence: Evidence701
xref: RelationshipXref579
xref: UnificationXref4641
xref: UnificationXref4640
pathway order: PathwayStep689
pathway order: PathwayStep690
pathway order: PathwayStep691
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/8131753
type: PublicationXref
id: 8131753
author: Lieber, MR
author: Harrington, JJ
db: Pubmed
title: The characterization of a mammalian DNA structure-specific endonuclease.
source: EMBO J 13:1235-46
year: 1994

http://identifiers.org/pubmed/14988808
type: PublicationXref
id: 14988808
author: Jakobs, C
author: Huck, JH
author: Verhoeven, NM
author: van der Knaap, MS
author: Struys, EA
author: Salomons, GS
db: Pubmed
title: Ribose-5-phosphate isomerase deficiency: new inborn error in the pentose phosphate pathway associated with a slowly progressive leukoencephalopathy
source: Am J Hum Genet 74:745-51
year: 2004

http://identifiers.org/pubmed/9883897
type: PublicationXref
id: 9883897
author: Csere, P
author: Lill, R
author: Kispal, G
db: Pubmed
title: Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p
source: FEBS Lett 441:266-70
year: 1998

http://identifiers.org/pubmed/9883880
type: PublicationXref
id: 9883880
author: Callebaut, I
author: Dehoux, P
author: Cossart, P
db: Pubmed
title: EVH1/WH1 domains of VASP and WASP proteins belong to a large family including Ran-binding domains of the RanBP1 family
source: FEBS Lett 441:181-5
year: 1998

http://identifiers.org/pubmed/14530973
type: PublicationXref
id: 14530973
author: Mackenzie, B
author: Hediger, MA
db: Pubmed
title: SLC11 family of H+-coupled metal-ion transporters NRAMP1 and DMT1
source: Pflugers Arch 447:571-9
year: 2004

Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction681
pathway component: BiochemicalReaction683
pathway component: BiochemicalReaction682
evidence: Evidence1196
xref: UnificationXref7596
xref: UnificationXref7595
pathway order: PathwayStep1173
pathway order: PathwayStep1174
pathway order: PathwayStep1172
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/9331217
type: PublicationXref
id: 9331217
author: Cooper, JA
author: Hart, MC
author: Korshunova, YO
db: Pubmed
title: Vertebrates have conserved capping protein alpha isoforms with specific expression patterns
source: Cell Motil Cytoskeleton 38:120-32
year: 1997

http://identifiers.org/pubmed/17222083
type: PublicationXref
id: 17222083
author: Lamarche-Vane, N
author: Tcherkezian, J
db: Pubmed
title: Current knowledge of the large RhoGAP family of proteins
source: Biol Cell 99:67-86
year: 2007

UnificationXref1815
type: UnificationXref
id: 3658713
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658713

UnificationXref1814
type: UnificationXref
id: O59865
db: UniProt

UnificationXref1813
type: UnificationXref
id: 3658660
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658660

UnificationXref1812
type: UnificationXref
id: 3658659
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658659

UnificationXref1819
type: UnificationXref
id: Q10421
db: UniProt

UnificationXref1818
type: UnificationXref
id: 3658718
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658718

UnificationXref1817
type: UnificationXref
id: 3658717
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658717

UnificationXref1816
type: UnificationXref
id: O13784
db: UniProt

http://identifiers.org/pubmed/15665109
type: PublicationXref
id: 15665109
author: Dirago, L
author: Mifsud, S
author: Hyland, C
author: Alexander, WS
author: Hilton, DJ
author: Carpinelli, MR
author: Nicola, NA
author: Metcalf, D
db: Pubmed
title: Anomalous megakaryocytopoiesis in mice with mutations in the c-Myb gene
source: Blood 105:3480-7
year: 2005

UnificationXref1810
type: UnificationXref
id: 3658655
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658655

UnificationXref1811
type: UnificationXref
id: Q9UTQ6
db: UniProt

UnificationXref1802
type: UnificationXref
id: 3658691
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658691

UnificationXref1801
type: UnificationXref
id: 3658740
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658740

UnificationXref1804
type: UnificationXref
id: 3658641
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658641

UnificationXref1803
type: UnificationXref
id: O74322
db: UniProt

UnificationXref1806
type: UnificationXref
id: 3658645
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658645

UnificationXref1805
type: UnificationXref
id: O14062
db: UniProt

UnificationXref1808
type: UnificationXref
id: 3658651
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658651

UnificationXref1807
type: UnificationXref
id: 3658646
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658646

UnificationXref1809
type: UnificationXref
id: O94715
db: UniProt

UnificationXref1800
type: UnificationXref
id: O74330
db: UniProt

UnificationXref1838
type: UnificationXref
id: 3658835
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658835

UnificationXref1839
type: UnificationXref
id: Q9P7J6
db: UniProt

UnificationXref1836
type: UnificationXref
id: 3658735
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658735

UnificationXref1837
type: UnificationXref
id: 3658736
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658736

UnificationXref1834
type: UnificationXref
id: 3658731
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658731

UnificationXref1835
type: UnificationXref
id: Q9UTG4
db: UniProt

UnificationXref1833
type: UnificationXref
id: Q9UT56
db: UniProt

UnificationXref1832
type: UnificationXref
id: 3658794
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658794

UnificationXref1831
type: UnificationXref
id: 3658793
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658793

UnificationXref1830
type: UnificationXref
id: Q9P3T6
db: UniProt

http://identifiers.org/pubmed/224930
type: PublicationXref
id: 224930
author: Inoue, K
author: Yamasawa, K
author: Nishimukai, H
db: Pubmed
title: Purification and partial characterization of aldehyde dehydrogenase from human erythrocytes.
source: Biochim Biophys Acta 569:117-23
year: 1979

http://identifiers.org/pubmed/18436705
type: PublicationXref
id: 18436705
author: Scheuner, D
author: Kaufman, RJ
db: Pubmed
title: The unfolded protein response: a pathway that links insulin demand with beta-cell failure and diabetes
source: Endocr Rev 29:317-33
year: 2008

http://identifiers.org/pubmed/22108505
type: PublicationXref
id: 22108505
author: Basler, Konrad
author: Herr, Patrick
db: Pubmed
title: Porcupine-mediated lipidation is required for Wnt recognition by Wls
source: Dev. Biol. 361:392-402
year: 2012

UnificationXref1827
type: UnificationXref
id: 3658727
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658727

UnificationXref1828
type: UnificationXref
id: O14277
db: UniProt

UnificationXref1829
type: UnificationXref
id: 3658789
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658789

UnificationXref1823
type: UnificationXref
id: O74172
db: UniProt

UnificationXref1824
type: UnificationXref
id: 3658722
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658722

UnificationXref1825
type: UnificationXref
id: P79009
db: UniProt

UnificationXref1826
type: UnificationXref
id: 3658726
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658726

UnificationXref1820
type: UnificationXref
id: 3658749
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658749

http://identifiers.org/pubmed/8647822
type: PublicationXref
id: 8647822
author: Sanchez, HB
author: Osborne, TF
author: Rosenfeld, JM
author: Vallett, SM
db: Pubmed
title: A direct role for sterol regulatory element binding protein in activation of 3-hydroxy-3-methylglutaryl coenzyme A reductase gene
source: J Biol Chem 271:12247-53
year: 1996

UnificationXref1822
type: UnificationXref
id: 3658757
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658757

UnificationXref1821
type: UnificationXref
id: O60128
db: UniProt

UnificationXref1858
type: UnificationXref
id: 3658741
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658741

UnificationXref1859
type: UnificationXref
id: P0C016
db: UniProt

UnificationXref1856
type: UnificationXref
id: 3658637
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658637

UnificationXref1857
type: UnificationXref
id: P0C8R3
db: UniProt

UnificationXref1851
type: UnificationXref
id: 3658767
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658767

UnificationXref1850
type: UnificationXref
id: Q09781
db: UniProt

UnificationXref1855
type: UnificationXref
id: P79013
db: UniProt

UnificationXref1854
type: UnificationXref
id: 3658772
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658772

UnificationXref1853
type: UnificationXref
id: 3658771
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658771

UnificationXref1852
type: UnificationXref
id: O94438
db: UniProt

http://identifiers.org/pubmed/22983114
type: PublicationXref
id: 22983114
author: Boutros, Michael
author: Bartscherer, Kerstin
author: Chaudhary, Varun
author: Gross, Julia Christina
db: Pubmed
title: Active Wnt proteins are secreted on exosomes
source: Nat. Cell Biol. 14:1036-45
year: 2012

UnificationXref1845
type: UnificationXref
id: 3658681
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658681

UnificationXref1846
type: UnificationXref
id: P28189
db: UniProt

UnificationXref1847
type: UnificationXref
id: 3658650
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658650

UnificationXref1848
type: UnificationXref
id: P05764
db: UniProt

UnificationXref1849
type: UnificationXref
id: 3658703
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658703

UnificationXref1840
type: UnificationXref
id: 3658670
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658670

UnificationXref1842
type: UnificationXref
id: 3658674
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658674

UnificationXref1841
type: UnificationXref
id: O42984
db: UniProt

UnificationXref1844
type: UnificationXref
id: O94754
db: UniProt

UnificationXref1843
type: UnificationXref
id: 3658675
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658675

http://identifiers.org/pubmed/6693436
type: PublicationXref
id: 6693436
author: Hu, SZ
author: Wang, TS
author: Korn, D
db: Pubmed
title: DNA primase from KB cells. Characterization of a primase activity tightly associated with immunoaffinity-purified DNA polymerase-alpha.
source: J Biol Chem 259:1854-65
year: 1984

http://identifiers.org/pubmed/12800216
type: PublicationXref
id: 12800216
author: Zhang, M
author: Zhu, F
db: Pubmed
title: DNA polymerase zeta: new insight into eukaryotic mutagenesis and mammalian embryonic development.
source: World J Gastroenterol 9:1165-9
year: 2003

http://identifiers.org/pubmed/1270801
type: PublicationXref
id: 1270801
author: Franklin, EC
author: Rosenthal, CJ
author: Greenspan, J
author: Frangione, B
db: Pubmed
title: Isolation and partial characterization of SAA-an amyloid-related protein from human serum
source: J Immunol 116:1415-8
year: 1976

http://identifiers.org/pubmed/2408761
type: PublicationXref
id: 2408761
author: Sharp, PA
author: Moore, CL
db: Pubmed
title: Accurate cleavage and polyadenylation of exogenous RNA substrate.
source: Cell 41:845-55
year: 1985

Advanced glycosylation endproduct receptor signaling
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction607
evidence: Evidence1060
xref: UnificationXref6749
xref: UnificationXref6748
pathway order: PathwayStep1041
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P05767
data source: Provenance1
name: 60S ribosomal protein L39
name: P05767
name: P02404
xref: UnificationXref1959
feature: FragmentFeature430
cellular location: GO:0005829
comment: Reactome DB_ID: 3659220
display name: RPL39

UniProt:P58234
type: ProteinReference
xref: UnificationXref1864
organism: BioSource1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTI8
data source: Provenance1
name: RPL36A
name: 60S ribosomal protein L44
name: Q9UTI8
xref: UnificationXref1962
feature: FragmentFeature431
cellular location: GO:0005829
comment: Reactome DB_ID: 3659235
display name: L36a

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14339
data source: Provenance1
name: RPL17
name: O14339
name: 60S ribosomal protein L17
xref: UnificationXref1956
feature: FragmentFeature429
cellular location: GO:0005829
comment: Reactome DB_ID: 3659039
display name: L23

Homologues of RPL13A
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1974
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659018

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O42848
data source: Provenance1
name: 60S ribosomal protein L13a
name: 23 kDa highly basic protein
name: O42848
xref: UnificationXref1969
feature: FragmentFeature434
cellular location: GO:0005829
comment: Reactome DB_ID: 3659009
display name: RPL13A

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10157
data source: Provenance1
name: Q10157
name: 60S ribosomal protein L11
name: P39026
xref: UnificationXref1964
feature: FragmentFeature432
cellular location: GO:0005829
comment: Reactome DB_ID: 3658995
display name: RPL11

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9URX6
data source: Provenance1
name: 60S ribosomal protein L31
name: Q9URX6
name: P12947
xref: UnificationXref1966
feature: FragmentFeature433
cellular location: GO:0005829
comment: Reactome DB_ID: 3659157
display name: RPL31

G alpha (q) signalling events
type: Pathway
data source: Provenance1
pathway component: REACT 97681.9
evidence: Evidence260
xref: UnificationXref1409
xref: UnificationXref1410
pathway order: PathwayStep147
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Homologues of RPL9
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
member physical entity: Q10232
xref: UnificationXref1979
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659270

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43004
data source: Provenance1
name: 60S ribosomal protein L13a
name: O43004
name: 23 kDa highly basic protein
xref: UnificationXref1973
feature: FragmentFeature436
cellular location: GO:0005829
comment: Reactome DB_ID: 3659017
display name: RPL13A

http://identifiers.org/pubmed/3893466
type: PublicationXref
id: 3893466
author: Jornvall, H
db: Pubmed
title: Alcohol dehydrogenases, aldehyde dehydrogenases, and related enzymes
source: Alcohol 2:61-6
year: 1985

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:O42991
data source: Provenance1
name: 60S ribosomal protein L13a
name: 23 kDa highly basic protein
name: O42991
xref: UnificationXref1971
feature: FragmentFeature435
cellular location: GO:0005829
comment: Reactome DB_ID: 3659013
display name: RPL13A

Homologues of RPL3
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1943
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659141

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P40372
data source: Provenance1
name: HIV-1 TAR RNA binding protein B
name: P40372
name: TARBP-B
name: 60S ribosomal protein L3
xref: UnificationXref1940
feature: FragmentFeature422
cellular location: GO:0005829
comment: Reactome DB_ID: 3659136
display name: RPL3

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36584
data source: Provenance1
name: HIV-1 TAR RNA binding protein B
name: TARBP-B
name: 60S ribosomal protein L3
name: P36584
xref: UnificationXref1942
feature: FragmentFeature423
cellular location: GO:0005829
comment: Reactome DB_ID: 3659140
display name: RPL3

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P79071
data source: Provenance1
name: P79071
name: Neoplasm-related protein C140
name: 60S ribosomal protein L6
name: TAXREB107
name: TAX-responsive enhancer element binding protein 107
xref: UnificationXref1945
feature: FragmentFeature424
cellular location: GO:0005829
comment: Reactome DB_ID: 3659240
display name: RPL6

Homologues of RPL15(2-204)
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1950
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659031

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74895
data source: Provenance1
name: RPL15(2-204)
name: O74895
name: 60S ribosomal protein L15
xref: UnificationXref1947
feature: FragmentFeature425
cellular location: GO:0005829
comment: Reactome DB_ID: 3659026
display name: P39030

Diphosphatidylglycerol
type: SmallMoleculeReference
name: cardiolipin
name: cardiolipin [ChEBI:28494]
name: cardiolipins
name: 1',3'-Bis(1,2-diacyl-sn-glycero-3-phospho)-sn-glycerol
xref: UnificationXref3387

http://identifiers.org/pubmed/8662720
type: PublicationXref
id: 8662720
author: Korenberg, J
author: Garrow, TA
author: Qi, H
author: Choi, YJ
author: Shane, B
author: Chen, L
db: Pubmed
title: Purification and properties of human cytosolic folylpoly-gamma-glutamate synthetase and organization, localization, and differential splicing of its gene
source: J Biol Chem 271:13077-87
year: 1996

60S ribosomal protein L29
type: Protein
entity reference: Q92366
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Cell surface heparin binding protein HIP
name: Q92366
xref: UnificationXref1952
feature: FragmentFeature427
cellular location: GO:0005829
comment: Reactome DB_ID: 3659132
display name: RPL29

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9US22
data source: Provenance1
name: RPL15(2-204)
name: Q9US22
name: 60S ribosomal protein L15
xref: UnificationXref1949
feature: FragmentFeature426
cellular location: GO:0005829
comment: Reactome DB_ID: 3659030
display name: P39030

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O59794
data source: Provenance1
name: RPL17
name: O59794
name: 60S ribosomal protein L17
xref: UnificationXref1954
feature: FragmentFeature428
cellular location: GO:0005829
comment: Reactome DB_ID: 3659035
display name: L23

Homologues of RPL17
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1957
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659040

Homologues of RPL36
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1998
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659197

PublicationXref107
type: PublicationXref
author: Dekker, L
title: Protein Kinase C
year: 2004

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36584
data source: Provenance1
name: RPL3L(2-407)
name: 60S ribosomal protein L3-like
name: P36584
xref: UnificationXref2005
feature: FragmentFeature450
cellular location: GO:0005829
comment: Reactome DB_ID: 3659143
display name: Q92901

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P40372
data source: Provenance1
name: RPL3L(2-407)
name: P40372
name: 60S ribosomal protein L3-like
xref: UnificationXref2004
feature: FragmentFeature449
cellular location: GO:0005829
comment: Reactome DB_ID: 3659142
display name: Q92901

Homologues of RPL3L(2-407)
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2006
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659144

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P52808
data source: Provenance1
name: P52808
name: RPL30(2-115)
name: 60S ribosomal protein L30
xref: UnificationXref2002
feature: FragmentFeature448
cellular location: GO:0005829
comment: Reactome DB_ID: 3659152
display name: P04645

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTP0
data source: Provenance1
name: RPL30(2-115)
name: Q9UTP0
name: 60S ribosomal protein L30
xref: UnificationXref2000
feature: FragmentFeature447
cellular location: GO:0005829
comment: Reactome DB_ID: 3659148
display name: P04645

Homologues of RPL30(2-115)
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2003
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659153

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q92365
data source: Provenance1
name: 60S ribosomal protein L36
name: Q92365
name: Q9Y3U8
xref: UnificationXref1997
feature: FragmentFeature446
cellular location: GO:0005829
comment: Reactome DB_ID: 3659196
display name: RPL36

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94658
data source: Provenance1
name: O94658
name: 60S ribosomal protein L36
name: Q9Y3U8
xref: UnificationXref1995
feature: FragmentFeature445
cellular location: GO:0005829
comment: Reactome DB_ID: 3659192
display name: RPL36

http://identifiers.org/pubmed/15585605
type: PublicationXref
id: 15585605
author: Takeda, K
author: Akira, S
db: Pubmed
title: TIRAP/Mal, TRIF and TRAM. Differential utilization of these TIR
source: Int Immunol 17:1-14
year: 2005

Homologues of RPL27A
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2013
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659124

Homologues of RPL23A
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1989
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659092

60S ribosomal protein L38
type: Protein
entity reference: UniProt:Q09900
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Q09900
name: P23411
xref: UnificationXref1983
feature: FragmentFeature440
cellular location: GO:0005829
comment: Reactome DB_ID: 3659215
display name: RPL38

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74391
data source: Provenance1
name: P29316
name: 60S ribosomal protein L23a
name: O74391
xref: UnificationXref1988
feature: FragmentFeature442
cellular location: GO:0005829
comment: Reactome DB_ID: 3659091
display name: RPL23A

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10330
data source: Provenance1
name: P29316
name: 60S ribosomal protein L23a
name: Q10330
xref: UnificationXref1986
feature: FragmentFeature441
cellular location: GO:0005829
comment: Reactome DB_ID: 3659087
display name: RPL23A

Q10232
type: Protein
entity reference: UniProt:Q10232
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: 60S ribosomal protein L9
name: P32969
xref: UnificationXref1978
feature: FragmentFeature438
cellular location: GO:0005829
comment: Reactome DB_ID: 3659269
display name: RPL9

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74905
data source: Provenance1
name: 60S ribosomal protein L9
name: O74905
name: P32969
xref: UnificationXref1976
feature: FragmentFeature437
cellular location: GO:0005829
comment: Reactome DB_ID: 3659265
display name: RPL9

60S ribosomal protein L38
type: Protein
entity reference: Q9USR7
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Q9USR7
name: P23411
xref: UnificationXref1981
feature: FragmentFeature439
cellular location: GO:0005829
comment: Reactome DB_ID: 3659211
display name: RPL38

Homologues of RPL38
type: Protein
data source: Provenance1
member physical entity: 60S ribosomal protein L38
xref: UnificationXref1984
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659216

Base Excision Repair
type: Pathway
data source: Provenance1
pathway component: REACT 101347.9
pathway component: REACT 96704.9
evidence: Evidence28
xref: UnificationXref122
xref: RelationshipXref9
xref: UnificationXref123
pathway order: PathwayStep23
pathway order: PathwayStep27
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94238
data source: Provenance1
name: CAG-ISL 7
name: 60S ribosomal protein L14
name: O94238
xref: UnificationXref1991
feature: FragmentFeature443
cellular location: GO:0005829
comment: Reactome DB_ID: 3659022
display name: RPL14

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P08093
data source: Provenance1
name: P25120
name: 60S ribosomal protein L8
name: P08093
xref: UnificationXref1993
feature: FragmentFeature444
cellular location: GO:0005829
comment: Reactome DB_ID: 3659261
display name: RPL8

http://identifiers.org/pubmed/15031527
type: PublicationXref
id: 15031527
author: Matsumoto, M
author: Seya, T
author: Funami, K
author: Oshiumi, H
db: Pubmed
title: Toll-like receptor 3: a link between toll-like receptor, interferon and viruses
source: Microbiol Immunol 48:147-54
year: 2004

http://identifiers.org/pubmed/19489725
type: PublicationXref
id: 19489725
author: Joazeiro, CA
author: Deshaies, RJ
db: Pubmed
title: RING domain E3 ubiquitin ligases
source: Annu Rev Biochem 78:399-434
year: 2009

http://identifiers.org/pubmed/8618861
type: PublicationXref
id: 8618861
author: Nevins, JR
author: DeGregori, J
author: Ohtani, K
db: Pubmed
title: Regulation of the cyclin E gene by transcription factor E2F1
source: Proc Natl Acad Sci U S A 92:12146-50
year: 1995

http://identifiers.org/pubmed/15063729
type: PublicationXref
id: 15063729
author: Kihara, A
author: Igarashi, Y
author: Mizutani, Y
db: Pubmed
title: Identification of the human sphingolipid C4-hydroxylase, hDES2, and its up-regulation during keratinocyte differentiation
source: FEBS Lett 563:93-7
year: 2004

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O42867
data source: Provenance1
name: RPL23
name: 60S ribosomal protein L23
name: O42867
xref: UnificationXref2033
feature: FragmentFeature460
cellular location: GO:0005829
comment: Reactome DB_ID: 3659083
display name: L17

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14388
data source: Provenance1
name: 60S ribosomal protein L27
name: RPL27(2-136)
name: O14388
xref: UnificationXref2030
feature: FragmentFeature459
cellular location: GO:0005829
comment: Reactome DB_ID: 3659114
display name: P08526

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74538
data source: Provenance1
name: 60S ribosomal protein L27
name: O74538
name: RPL27(2-136)
xref: UnificationXref2028
feature: FragmentFeature458
cellular location: GO:0005829
comment: Reactome DB_ID: 3659110
display name: P08526

Inositol phosphate metabolism
type: Pathway
data source: Provenance1
pathway component: REACT 159099.3
pathway component: REACT 152782.3
pathway component: REACT 159696.3
pathway component: REACT 154521.3
evidence: Evidence407
xref: RelationshipXref204
xref: UnificationXref2704
xref: UnificationXref2705
pathway order: PathwayStep385
pathway order: PathwayStep379
pathway order: PathwayStep398
pathway order: PathwayStep396
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

60S ribosomal protein L26-like 1
type: Protein
entity reference: P78946
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: RPL26L1(2-145)
name: P78946
xref: UnificationXref2040
feature: FragmentFeature463
cellular location: GO:0005829
comment: Reactome DB_ID: 3659106
display name: Q9UNX3

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10192
data source: Provenance1
name: Q10192
name: Q07020
name: 60S ribosomal protein L18
xref: UnificationXref2037
feature: FragmentFeature462
cellular location: GO:0005829
comment: Reactome DB_ID: 3659048
display name: RPL18

Q8TFH1
type: Protein
entity reference: Q8TFH1
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Q07020
name: 60S ribosomal protein L18
xref: UnificationXref2035
feature: FragmentFeature461
cellular location: GO:0005829
comment: Reactome DB_ID: 3659044
display name: RPL18

Homologues of RPL18
type: Protein
data source: Provenance1
member physical entity: Q8TFH1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2038
cellular location: GO:0005829
comment: Reactome DB_ID: 3659049
comment: Converted from EntitySet in Reactome

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74884
data source: Provenance1
name: 60S ribosomal protein L24
name: RPL24
name: O74884
xref: UnificationXref2044
feature: FragmentFeature465
cellular location: GO:0005829
comment: Reactome DB_ID: 3659096
display name: L30

Homologues of RPL24
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2047
cellular location: GO:0005829
comment: Reactome DB_ID: 3659101
comment: Converted from EntitySet in Reactome

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O13672
data source: Provenance1
name: 60S ribosomal protein L7a
name: PLA-X polypeptide
name: Surfeit locus protein 3
name: O13672
xref: UnificationXref2042
feature: FragmentFeature464
cellular location: GO:0005829
comment: Reactome DB_ID: 3659253
display name: RPL7A

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36585
data source: Provenance1
name: P46776
name: 60S ribosomal protein L27a
name: P36585
xref: UnificationXref2012
feature: FragmentFeature452
cellular location: GO:0005829
comment: Reactome DB_ID: 3659123
display name: RPL27A

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P57728
data source: Provenance1
name: P46776
name: P57728
name: 60S ribosomal protein L27a
xref: UnificationXref2010
feature: FragmentFeature451
cellular location: GO:0005829
comment: Reactome DB_ID: 3659119
display name: RPL27A

Q9P784
type: Protein
entity reference: Q9P784
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: 60S ribosomal protein L4
name: RPL4
xref: UnificationXref2015
feature: FragmentFeature453
cellular location: GO:0005829
comment: Reactome DB_ID: 3659224
display name: L1

Homologues of RPL4
type: Protein
data source: Provenance1
member physical entity: Q9P784
member physical entity: P35679
xref: UnificationXref2018
cellular location: GO:0005829
comment: Reactome DB_ID: 3659229
comment: Converted from EntitySet in Reactome

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14069
data source: Provenance1
name: 60S ribosomal protein L28
name: P46779
name: O14069
xref: UnificationXref2020
feature: FragmentFeature455
cellular location: GO:0005829
comment: Reactome DB_ID: 3659128
display name: RPL28

P35679
type: Protein
entity reference: P35679
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: 60S ribosomal protein L4
name: RPL4
xref: UnificationXref2017
feature: FragmentFeature454
cellular location: GO:0005829
comment: Reactome DB_ID: 3659228
display name: L1

60S ribosomal protein L19
type: Protein
entity reference: O42699
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: O42699
name: P14118
xref: UnificationXref2022
feature: FragmentFeature456
cellular location: GO:0005829
comment: Reactome DB_ID: 3659059
display name: RPL19

Homologues of RPL19
type: Protein
data source: Provenance1
member physical entity: 60S ribosomal protein L19
xref: UnificationXref2025
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659064

Homologues of RPL27(2-136)
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2031
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659115

60S ribosomal protein L19
type: Protein
entity reference: P05734
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: P14118
name: P05734
xref: UnificationXref2024
feature: FragmentFeature457
cellular location: GO:0005829
comment: Reactome DB_ID: 3659063
display name: RPL19

http://identifiers.org/pubmed/9461603
type: PublicationXref
id: 9461603
author: Aguado, B
author: Campbell, RD
db: Pubmed
title: Characterization of a human lysophosphatidic acid acyltransferase that is encoded by a gene located in the class III region of the human major histocompatibility complex
source: J Biol Chem 273:4096-105
year: 1998

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10056
data source: Provenance1
name: PAK-2p34
name: PAK2(213-524)
xref: UnificationXref2132
feature: FragmentFeature482
cellular location: GO:0005829
comment: Reactome DB_ID: 3662088
display name: Q10056

PublicationXref149
type: PublicationXref
author: Greene, E
author: Henikoff, S
title: Kinesin home page
url: http://www.cellbio.duke.edu/kinesin/

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P00046
data source: Provenance1
name: P00046
name: Cytochrome c
xref: UnificationXref2121
feature: FragmentFeature479
cellular location: GO:0005758
comment: Reactome DB_ID: 3660483
display name: CYCS

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P00046
data source: Provenance1
name: P00046
name: Cytochrome c
xref: UnificationXref2122
feature: FragmentFeature480
cellular location: GO:0005829
comment: Reactome DB_ID: 3660482
display name: CYCS

Homologues of PAK2(213-524)
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2133
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3662089

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P50527
data source: Provenance1
name: PAK-2p34
name: PAK2(213-524)
xref: UnificationXref2130
feature: FragmentFeature481
cellular location: GO:0005829
comment: Reactome DB_ID: 3662087
display name: P50527

phospho-p-3S1089,S1107-UPF1
type: Protein
entity reference: Q09820
data source: Provenance1
xref: UnificationXref2075
feature: ModificationFeature48
feature: FragmentFeature475
feature: ModificationFeature47
cellular location: GO:0005829
comment: Reactome DB_ID: 3663512

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74733
data source: Provenance1
name: Cleavage and polyadenylation specificity factor, 160 kDa subunit
name: CPSF 160 kDa subunit
name: O74733
name: CPSA_HUMAN
xref: UnificationXref2100
feature: FragmentFeature476
cellular location: GO:0005654
comment: Reactome DB_ID: 3658613
display name: CPSF1

O13794
type: Protein
entity reference: O13794
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Cleavage and polyadenylation specificity factor, 73 kDa subunit
name: CPSC_HUMAN
name: CPSF 73 kDa subunit
xref: UnificationXref2102
feature: FragmentFeature477
cellular location: GO:0005654
comment: Reactome DB_ID: 3658621
display name: CPSF3

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74740
data source: Provenance1
name: CPSB_HUMAN
name: Cleavage and polyadenylation specificity factor, 100 kDa subunit
name: O74740
name: CPSF 100 kDa subunit
xref: UnificationXref2104
feature: FragmentFeature478
cellular location: GO:0005654
comment: Reactome DB_ID: 3658617
display name: CPSF2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14253
data source: Provenance1
name: 80 kDa nuclear cap binding protein
name: O14253
name: NCBP 80 kDa subunit
name: CBP80
name: 80 kDa nuclear cap binding protein (NCBP 80 kDa subunit) (CBP80)
xref: UnificationXref2066
feature: FragmentFeature474
cellular location: GO:0005829
comment: Reactome DB_ID: 3659902
display name: NCBP1

http://identifiers.org/pubmed/8104944
type: PublicationXref
id: 8104944
author: Brown, WC
author: Campbell, JL
db: Pubmed
title: Interaction of proliferating cell nuclear antigen with yeast DNA polymerase delta.
source: J Biol Chem 268:21706-10
year: 1993

http://identifiers.org/pubmed/18043707
type: PublicationXref
id: 18043707
author: Hamm, HE
author: Oldham, WM
db: Pubmed
title: Heterotrimeric G protein activation by G-protein-coupled receptors
source: Nat Rev Mol Cell Biol 9:60-71
year: 2008

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74864
data source: Provenance1
name: 60S acidic ribosomal protein P0
name: RPLP0
name: O74864
xref: UnificationXref2062
feature: FragmentFeature472
cellular location: GO:0005829
comment: Reactome DB_ID: 3658965
display name: L10E

NCBP 20 kDa subunit
type: Protein
entity reference: Q9P383
data source: Provenance1
name: 20 kDa nuclear cap binding protein
name: NCBP2
name: Note: the coordinates are copied over from Homo sapiens.
name: NCBP interacting protein 1
name: Q9P383
name: CBP20
name: 20 kDa nuclear cap binding protein (NCBP 20 kDa subunit) (CBP20) (NCBP interacting protein 1) (NIP1)
xref: UnificationXref2065
feature: FragmentFeature473
cellular location: GO:0005829
comment: Reactome DB_ID: 3659901
display name: NIP1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9P769
data source: Provenance1
name: QM protein
name: Tumor suppressor QM
name: 60S ribosomal protein L10
name: Q9P769
name: Laminin receptor homolog
xref: UnificationXref2057
feature: FragmentFeature470
cellular location: GO:0005829
comment: Reactome DB_ID: 3658983
display name: RPL10

Q09127
type: Protein
entity reference: Q09127
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: QM protein
name: Tumor suppressor QM
name: 60S ribosomal protein L10
name: Laminin receptor homolog
xref: UnificationXref2059
feature: FragmentFeature471
cellular location: GO:0005829
comment: Reactome DB_ID: 3658987
display name: RPL10

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09668
data source: Provenance1
name: EBER associated protein
name: Epstein-Barr virus small RNA associated protein
name: Q09668
name: RPL22
name: Heparin binding protein HBp15
name: 60S ribosomal protein L22
xref: UnificationXref2055
feature: FragmentFeature469
cellular location: GO:0005829
comment: Reactome DB_ID: 3659077
display name: EAP

Homologues of RPL10
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
member physical entity: Q09127
xref: UnificationXref2060
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658988

http://identifiers.org/pubmed/8755573
type: PublicationXref
id: 8755573
author: Webster, MK
author: Meyer, AN
author: Donoghue, DJ
author: Hart, KC
author: Galvin, BD
db: Pubmed
title: Constitutive receptor activation by Crouzon syndrome mutations in fibroblast growth factor receptor (FGFR)2 and FGFR2/Neu chimeras
source: Proc Natl Acad Sci U S A 93:7894-9
year: 1996

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UUC1
data source: Provenance1
name: Q9UUC1
name: P46778
name: 60S ribosomal protein L21
xref: UnificationXref2050
feature: FragmentFeature467
cellular location: GO:0005829
comment: Reactome DB_ID: 3659068
display name: RPL21

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O42706
data source: Provenance1
name: O42706
name: P46778
name: 60S ribosomal protein L21
xref: UnificationXref2052
feature: FragmentFeature468
cellular location: GO:0005829
comment: Reactome DB_ID: 3659072
display name: RPL21

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q92354
data source: Provenance1
name: 60S ribosomal protein L24
name: RPL24
name: Q92354
xref: UnificationXref2046
feature: FragmentFeature466
cellular location: GO:0005829
comment: Reactome DB_ID: 3659100
display name: L30

Homologues of RPL21
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2053
cellular location: GO:0005829
comment: Reactome DB_ID: 3659073
comment: Converted from EntitySet in Reactome

Homologues of RPS27A(1-76)
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2167
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3657732

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P0C8R3
data source: Provenance1
name: RPS27A(1-76)
name: P0C8R3
name: ubiquitin (RPS27A)
xref: UnificationXref2165
feature: FragmentFeature495
cellular location: GO:0005829
comment: Reactome DB_ID: 3657730
display name: RPS27A

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P0C016
data source: Provenance1
name: RPS27A(1-76)
name: P0C016
name: ubiquitin (RPS27A)
xref: UnificationXref2166
feature: FragmentFeature496
cellular location: GO:0005829
comment: Reactome DB_ID: 3657731
display name: RPS27A

PublicationXref124
type: PublicationXref
author: Page, C
author: Vermylen, J
author: Fuster, V
author: Gresele, P
title: Platelets in thrombotic and non-thrombotic disorders.
source: 435-437
year: 2002

phospho-p-5S-PAK2(1-524)
type: Protein
entity reference: P50527
data source: Provenance1
xref: UnificationXref2147
feature: ModificationFeature52
feature: FragmentFeature489
feature: ModificationFeature55
feature: ModificationFeature54
feature: ModificationFeature53
feature: ModificationFeature51
cellular location: GO:0005829
comment: Reactome DB_ID: 3662077

phospho-p-5S-PAK2(1-524)
type: Protein
entity reference: UniProt:Q10056
data source: Provenance1
xref: UnificationXref2148
feature: ModificationFeature60
feature: ModificationFeature59
feature: FragmentFeature490
feature: ModificationFeature56
feature: ModificationFeature58
feature: ModificationFeature57
cellular location: GO:0005829
comment: Reactome DB_ID: 3662083

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09748
data source: Provenance1
name: DNM1L
name: Q09748
xref: UnificationXref2155
feature: FragmentFeature491
cellular location: GO:0005829
comment: Reactome DB_ID: 3662227
display name: Drp1

mRNA Decay by 5' to 3' Exoribonuclease
type: Pathway
data source: Provenance1
pathway component: 5' to 3' Exoribonuclease Digestion of Decapped mRNA
pathway component: Binding of Lsm1-7 Complex to Deadenylated mRNA
evidence: Evidence301
xref: RelationshipXref118
xref: UnificationXref1629
xref: UnificationXref1628
pathway order: PathwayStep295
pathway order: PathwayStep294
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09748
data source: Provenance1
name: DNM1L
name: Q09748
xref: UnificationXref2157
feature: FragmentFeature492
cellular location: GO:0005741
comment: Reactome DB_ID: 3662228
display name: Drp1

Homologues of K48poluUb-phospho-PAK-2p34(Thr402)
type: Protein
data source: Provenance1
member physical entity: phospho-K48poluUb-phospho-PAK-2p34(Thr402)
xref: UnificationXref2164
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3662108

phospho-K48poluUb-phospho-PAK-2p34(Thr402)
type: Protein
entity reference: P50527
data source: Provenance1
xref: UnificationXref2162
feature: ModificationFeature49
feature: ModificationFeature61
feature: FragmentFeature493
cellular location: GO:0005829
comment: Reactome DB_ID: 3662105

phospho-K48poluUb-phospho-PAK-2p34(Thr402)
type: Protein
entity reference: UniProt:Q10056
data source: Provenance1
xref: UnificationXref2163
feature: ModificationFeature50
feature: FragmentFeature494
feature: ModificationFeature62
cellular location: GO:0005829
comment: Reactome DB_ID: 3662107

UniProt:P07669
type: ProteinReference
xref: UnificationXref2260
organism: BioSource1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10056
data source: Provenance1
name: Q10056
name: PAK2(1-524)
xref: UnificationXref2145
feature: FragmentFeature488
cellular location: GO:0005829
comment: Reactome DB_ID: 3662070
display name: PAK2

Homologues of p-5S-PAK2(1-524)
type: Protein
data source: Provenance1
member physical entity: phospho-p-5S-PAK2(1-524)
xref: UnificationXref2149
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3662084

Homologues of PAK2(1-524)
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
member physical entity: P50527
xref: UnificationXref2146
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3662071

P50527
type: Protein
entity reference: P50527
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: PAK2(1-524)
xref: UnificationXref2144
feature: FragmentFeature487
cellular location: GO:0005829
comment: Reactome DB_ID: 3662066
display name: PAK2

PublicationXref114
type: PublicationXref
author: Krauss, G
title: Biochemistry of signal transduction and regulation
source: 259
year: 2003

Homologues of p-T402-PAK2(213-524)
type: Protein
data source: Provenance1
member physical entity: phospho-p-T402-PAK2(213-524)
xref: UnificationXref2136
cellular location: GO:0005829
comment: Reactome DB_ID: 3662094
comment: Converted from EntitySet in Reactome

http://identifiers.org/pubmed/21944752
type: PublicationXref
id: 21944752
author: Pierrel, F
author: Lill, R
author: Webert, H
author: Mühlenhoff, U
author: Fontecave, M
author: Ozeir, M
db: Pubmed
title: Coenzyme Q biosynthesis: Coq6 is required for the C5-hydroxylation reaction and substrate analogs rescue Coq6 deficiency
source: Chem Biol 18:1134-42
year: 2011

phospho-p-T402-PAK2(213-524)
type: Protein
entity reference: P50527
data source: Provenance1
xref: UnificationXref2134
feature: FragmentFeature483
feature: ModificationFeature49
cellular location: GO:0005829
comment: Reactome DB_ID: 3662091

http://identifiers.org/pubmed/8896597
type: PublicationXref
id: 8896597
author: Gill, SR
author: Compton, DA
author: Schroer, TA
author: Hasbani, MJ
author: Saredi, A
author: Bingham, JB
author: Gaglio, T
db: Pubmed
title: Opposing motor activities are required for the organization of the mammalian mitotic spindle pole
source: J Cell Biol 135:399-414
year: 1996

phospho-p-T402-PAK2(1-524)
type: Protein
entity reference: P50527
data source: Provenance1
xref: UnificationXref2139
feature: ModificationFeature49
feature: FragmentFeature485
cellular location: GO:0005654
comment: Reactome DB_ID: 3662100

phospho-p-T402-PAK2(1-524)
type: Protein
entity reference: UniProt:Q10056
data source: Provenance1
xref: UnificationXref2140
feature: FragmentFeature486
feature: ModificationFeature50
cellular location: GO:0005654
comment: Reactome DB_ID: 3662101

http://identifiers.org/pubmed/11470918
type: PublicationXref
id: 11470918
author: Wagner, H
author: Hausmann, S
author: Kirschning, CJ
author: Lipford, GB
author: Bauer, S
author: Redecke, V
author: Akira, S
author: Hacker, H
db: Pubmed
title: Human TLR9 confers responsiveness to bacterial DNA via species-specific CpG motif recognition
source: Proc Natl Acad Sci U S A 98:9237-42
year: 2001

phospho-p-T402-PAK2(213-524)
type: Protein
entity reference: UniProt:Q10056
data source: Provenance1
xref: UnificationXref2135
feature: FragmentFeature484
feature: ModificationFeature50
cellular location: GO:0005829
comment: Reactome DB_ID: 3662093

Homologues of p-T402-PAK2(1-524)
type: Protein
data source: Provenance1
member physical entity: phospho-p-T402-PAK2(1-524)
xref: UnificationXref2141
cellular location: GO:0005654
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3662102

ER Quality Control Compartment (ERQC)
type: Pathway
data source: Provenance1
pathway component: Glycoproteins with major folding defects are sent to degradation by EDEMs
pathway component: Trimming of the second mannose on the A branch
pathway component: Trimming of the terminal mannose on the C branch
pathway component: Trimming of the first mannose on the A branch
pathway component: Re-addition of a glucose on the alpha 1,3 branch
pathway component: Trimming of the terminal mannose on the B branch
evidence: Evidence1328
xref: UnificationXref8337
xref: UnificationXref8336
pathway order: PathwayStep1305
pathway order: PathwayStep1306
pathway order: PathwayStep1302
pathway order: PathwayStep1301
pathway order: PathwayStep1304
pathway order: PathwayStep1303
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/5666113
type: PublicationXref
id: 5666113
author: Luzzatto, L
author: Afolayan, A
db: Pubmed
title: Enzymic properties of different types of human erythrocyte glucose-6-phosphate dehydrogenase, with characterization of two new genetic variants
source: J Clin Invest 47:1833-42
year: 1968

PublicationXref165
type: PublicationXref
author: Machin, S
author: Allford, S
title: Haemostasis
source: Surgery (Oxford) 22:200a - 200d
year: 2004

PublicationXref164
type: PublicationXref
author: Marder, V
author: George, J
author: Colman, R
author: Goldhaber, S
author: Clowes, A
title: Hemostasis and Thrombosis: Basic Principles and Clinical Practice
year: 2005

GABA synthesis, release, reuptake and degradation
type: Pathway
data source: Provenance1
pathway component: REACT 138141.5
evidence: Evidence886
xref: UnificationXref5842
xref: UnificationXref5843
pathway order: PathwayStep872
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/21554866
type: PublicationXref
id: 21554866
author: Cox, Brian J
author: Biechele, Steffen
author: Rossant, Janet
db: Pubmed
title: Porcupine homolog is required for canonical Wnt signaling and gastrulation in mouse embryos
source: Dev. Biol. 355:275-85
year: 2011

alvespimycin [ChEBI:65324]
type: SmallMoleculeReference
name: alvespimycin
xref: UnificationXref6881

http://identifiers.org/pubmed/19359157
type: PublicationXref
id: 19359157
author: Lykke-Andersen, J
author: Rebbapragada, I
db: Pubmed
title: Execution of nonsense-mediated mRNA decay: what defines a substrate?
source: Curr Opin Cell Biol 21:394-402
year: 2009

UnificationXref1995
type: UnificationXref
id: 3659192
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659192

UnificationXref1996
type: UnificationXref
id: Q92365
db: UniProt

UnificationXref1997
type: UnificationXref
id: 3659196
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659196

UnificationXref1998
type: UnificationXref
id: 3659197
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659197

UnificationXref1991
type: UnificationXref
id: 3659022
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659022

UnificationXref1992
type: UnificationXref
id: P08093
db: UniProt

UnificationXref1993
type: UnificationXref
id: 3659261
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659261

UnificationXref1994
type: UnificationXref
id: O94658
db: UniProt

http://identifiers.org/pubmed/17698287
type: PublicationXref
id: 17698287
author: Grabowska, AM
author: Watson, SA
db: Pubmed
title: Role of gastrin peptides in carcinogenesis
source: Cancer Lett 257:1-15
year: 2007

UnificationXref1990
type: UnificationXref
id: O94238
db: UniProt

http://identifiers.org/pubmed/7378348
type: PublicationXref
id: 7378348
author: So, AG
author: Tan, CK
author: Downey, KM
author: Lee, MY
db: Pubmed
title: Purification of deoxyribonucleic acid polymerase delta from calf thymus: partial characterization of physical properties.
source: Biochemistry 19:2096-101
year: 1980

UnificationXref1999
type: UnificationXref
id: Q9UTP0
db: UniProt

UnificationXref1986
type: UnificationXref
id: 3659087
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659087

UnificationXref1987
type: UnificationXref
id: O74391
db: UniProt

UnificationXref1984
type: UnificationXref
id: 3659216
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659216

UnificationXref1985
type: UnificationXref
id: Q10330
db: UniProt

UnificationXref1982
type: UnificationXref
id: Q09900
db: UniProt

UnificationXref1983
type: UnificationXref
id: 3659215
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659215

UnificationXref1980
type: UnificationXref
id: Q9USR7
db: UniProt

UnificationXref1981
type: UnificationXref
id: 3659211
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659211

UnificationXref1989
type: UnificationXref
id: 3659092
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659092

UnificationXref1988
type: UnificationXref
id: 3659091
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659091

http://identifiers.org/pubmed/8089153
type: PublicationXref
id: 8089153
author: Hirst, M
author: Lou, L
author: Nakamura, J
author: Haliday, E
db: Pubmed
title: Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA
source: J Biol Chem 269:23830-23837
year: 1994

http://identifiers.org/pubmed/18367721
type: PublicationXref
id: 18367721
author: Skinner, SJ
author: Deleault, KM
author: Whitfield, ML
author: Brooks, SA
author: Gross, RH
author: Townley-Tilson, WH
author: Emmons, J
db: Pubmed
title: Identification of TTP mRNA targets in human dendritic cells reveals TTP as a critical regulator of dendritic cell maturation
source: RNA 14:888-902
year: 2008

http://identifiers.org/pubmed/17635743
type: PublicationXref
id: 17635743
author: Bluteau, D
author: Debili, N
author: Chang, Y
author: Vainchenker, W
db: Pubmed
title: From hematopoietic stem cells to platelets
source: J Thromb Haemost 5:318-27
year: 2007

Pyruvate
type: SmallMoleculeReference
name: Pyruvic acid
name: Pyroracemic acid
name: 2-Oxopropanoate
name: 2-Oxopropanoic acid
name: Pyruvate [ChEBI:32816]
xref: UnificationXref2309

http://identifiers.org/pubmed/14521508
type: PublicationXref
id: 14521508
author: Fransson, A
author: Aspenstrom, P
author: Saras, J
db: Pubmed
title: Rho GTPases have diverse effects on the organization of the actin filament system
source: Biochem J 377:327-37
year: 2004

http://identifiers.org/pubmed/19261609
type: PublicationXref
id: 19261609
author: Vitvitsky, V
author: Singh, S
author: Banerjee, R
author: Zhu, W
author: Chiku, T
author: Padovani, D
db: Pubmed
title: H2S biogenesis by human cystathionine gamma-lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia
source: J Biol Chem 284:11601-12
year: 2009

ChEBI:53023 (GlcNAc)2 (Man)6 (PP-Dol)1
type: SmallMoleculeReference
name: (GlcNAc)2 (Man)6 (PP-Dol)1
xref: UnificationXref8207

http://identifiers.org/pubmed/8428657
type: PublicationXref
id: 8428657
author: Yang, DC
author: Donovan, D
author: Vogeli, G
author: Vilalta, A
author: Wood, L
db: Pubmed
title: Cloning, sequencing and expression of a cDNA encoding mammalian valyl-tRNA synthetase
source: Gene 123:181-6
year: 1993

http://identifiers.org/pubmed/16024644
type: PublicationXref
id: 16024644
author: Shimamura, T
author: Shapiro, GI
author: Engelman, JA
author: Lowell, AM
db: Pubmed
title: Epidermal growth factor receptors harboring kinase domain mutations associate with the heat shock protein 90 chaperone and are destabilized following exposure to geldanamycins
source: Cancer Res 65:6401-8
year: 2005

UnificationXref1936
type: UnificationXref
id: O94686
db: UniProt

http://identifiers.org/pubmed/9268380
type: PublicationXref
id: 9268380
author: Fattaey, A
author: Booher, RN
author: Holman, PS
db: Pubmed
title: Human Myt1 is a cell cycle-regulated kinase that inhibits Cdc2 but not Cdk2 activity
source: J Biol Chem 272:22300-6
year: 1997

UnificationXref1935
type: UnificationXref
id: 3659202
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659202

UnificationXref1934
type: UnificationXref
id: Q9HGL8
db: UniProt

UnificationXref1933
type: UnificationXref
id: 3659231
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659231

UnificationXref1939
type: UnificationXref
id: P40372
db: UniProt

UnificationXref1938
type: UnificationXref
id: 3659207
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659207

UnificationXref1937
type: UnificationXref
id: 3659206
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659206

UnificationXref1931
type: UnificationXref
id: 3659174
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659174

UnificationXref1932
type: UnificationXref
id: 3659175
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659175

http://identifiers.org/pubmed/17222168
type: PublicationXref
id: 17222168
author: Agre, P
author: Frøkiaer, J
author: Nielsen, S
author: Kwon, TH
db: Pubmed
title: Regulation and dysregulation of aquaporins in water balance disorders
source: J Intern Med 261:53-64
year: 2007

UnificationXref1930
type: UnificationXref
id: Q9URT8
db: UniProt

(Glc)2 (GlcNAc)2 (Man)9 (PP-Dol)1
type: SmallMoleculeReference
name: ChEBI:53020 (Glc)2 (GlcNAc)2 (Man)9 (PP-Dol)1
xref: UnificationXref8242

ChEBI:53022 (GlcNAc)2 (Man)5 (PP-Dol)1
type: SmallMoleculeReference
name: (GlcNAc)2 (Man)5 (PP-Dol)1
xref: UnificationXref8188

ChEBI:53014 N(6)-carboxymethyl-L-lysine
type: SmallMoleculeReference
name: N(6)-carboxymethyl-L-lysine
xref: UnificationXref6727

(Glc)3 (GlcNAc)2 (Man)9 (PP-Dol)1
type: SmallMoleculeReference
name: ChEBI:53019 (Glc)3 (GlcNAc)2 (Man)9 (PP-Dol)1
xref: UnificationXref8249

UnificationXref1923
type: UnificationXref
id: 3659187
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659187

UnificationXref1922
type: UnificationXref
id: Q9USG6
db: UniProt

UnificationXref1925
type: UnificationXref
id: 3659273
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659273

UnificationXref1924
type: UnificationXref
id: 3659188
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659188

UnificationXref1927
type: UnificationXref
id: 3659005
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659005

UnificationXref1926
type: UnificationXref
id: O74175
db: UniProt

UnificationXref1929
type: UnificationXref
id: 3659170
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659170

UnificationXref1928
type: UnificationXref
id: O42846
db: UniProt

http://identifiers.org/pubmed/17222174
type: PublicationXref
id: 17222174
author: Van Schaftingen, E
author: Linster, CL
db: Pubmed
title: Vitamin C: biosynthesis, recycling and degradation in mammals
source: FEBS J 274:1-22
year: 2007

UnificationXref1920
type: UnificationXref
id: Q9USX4
db: UniProt

UnificationXref1921
type: UnificationXref
id: 3659183
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659183

UnificationXref1919
type: UnificationXref
id: 3659249
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659249

UnificationXref1918
type: UnificationXref
id: 3659248
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659248

UnificationXref1917
type: UnificationXref
id: P25457
db: UniProt

UnificationXref1916
type: UnificationXref
id: 3659244
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659244

UnificationXref1915
type: UnificationXref
id: O60143
db: UniProt

http://identifiers.org/pubmed/11264579
type: PublicationXref
id: 11264579
author: Hutson, SM
author: Conway, ME
author: Dunbar, J
author: Farber, GK
author: Yennawar, NH
db: Pubmed
title: The structure of human mitochondrial branched-chain aminotransferase.
source: Acta Crystallogr D Biol Crystallogr 57:506-15
year: 2001

UnificationXref1914
type: UnificationXref
id: 3659179
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659179

UnificationXref1913
type: UnificationXref
id: O74904
db: UniProt

UnificationXref1912
type: UnificationXref
id: 3659001
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659001

UnificationXref1911
type: UnificationXref
id: O75000
db: UniProt

UnificationXref1910
type: UnificationXref
id: 3659166
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659166

UnificationXref1909
type: UnificationXref
id: 3659165
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659165

UnificationXref1908
type: UnificationXref
id: O42935
db: UniProt

UnificationXref1905
type: UnificationXref
id: 3658979
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658979

UnificationXref1904
type: UnificationXref
id: 3658978
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658978

UnificationXref1907
type: UnificationXref
id: 3659161
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659161

UnificationXref1906
type: UnificationXref
id: P79015
db: UniProt

UnificationXref1901
type: UnificationXref
id: P08094
db: UniProt

UnificationXref1900
type: UnificationXref
id: 3658970
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658970

UnificationXref1903
type: UnificationXref
id: O14317
db: UniProt

UnificationXref1902
type: UnificationXref
id: 3658974
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658974

http://identifiers.org/pubmed/2900981
type: PublicationXref
id: 2900981
author: Palsdottir, A
author: Jensson, O
author: Arnason, A
author: Thorsteinsson, L
author: Grubb, A
author: Abrahamson, M
author: Olafsson, I
db: Pubmed
title: Mutation in cystatin C gene causes hereditary brain haemorrhage
source: Lancet 2:603-4
year: 1988

UnificationXref1979
type: UnificationXref
id: 3659270
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659270

UnificationXref1977
type: UnificationXref
id: Q10232
db: UniProt

http://identifiers.org/pubmed/18767960
type: PublicationXref
id: 18767960
author: Antonellis, A
author: Green, ED
db: Pubmed
title: The role of aminoacyl-tRNA synthetases in genetic diseases
source: Annu Rev Genomics Hum Genet 9:87-107
year: 2008

UnificationXref1978
type: UnificationXref
id: 3659269
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659269

http://identifiers.org/pubmed/2995985
type: PublicationXref
id: 2995985
author: Evans, DR
author: Kelly, RE
author: Pastra-Landis, SC
author: Lee, L
db: Pubmed
title: Oligomeric structure of the multifunctional protein CAD that initiates pyrimidine biosynthesis in mammalian cells
source: Proc Natl Acad Sci USA 82:6802-6806
year: 1985

http://identifiers.org/pubmed/6022858
type: PublicationXref
id: 6022858
author: Younathan, ES
author: Pynes, GD
db: Pubmed
title: Purification and some properties of inorganic pyrophosphatase from human erythrocytes
source: J Biol Chem 242:2119-23
year: 1967

http://identifiers.org/pubmed/1974050
type: PublicationXref
id: 1974050
author: Hurwitz, J
author: Lee, SH
db: Pubmed
title: Mechanism of elongation of primed DNA by DNA polymerase delta, proliferating cell nuclear antigen, and activator 1.
source: Proc Natl Acad Sci U S A 87:5672-6
year: 1990

UnificationXref1972
type: UnificationXref
id: O43004
db: UniProt

UnificationXref1971
type: UnificationXref
id: 3659013
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659013

UnificationXref1970
type: UnificationXref
id: O42991
db: UniProt

UnificationXref1976
type: UnificationXref
id: 3659265
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659265

UnificationXref1975
type: UnificationXref
id: O74905
db: UniProt

UnificationXref1974
type: UnificationXref
id: 3659018
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659018

UnificationXref1973
type: UnificationXref
id: 3659017
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659017

UnificationXref1966
type: UnificationXref
id: 3659157
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659157

UnificationXref1967
type: UnificationXref
id: 3659230
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659230

UnificationXref1968
type: UnificationXref
id: O42848
db: UniProt

UnificationXref1969
type: UnificationXref
id: 3659009
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659009

6-O-{alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(1->6)-2-O-[(2-aminoethyl)phosphoryl]-alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl}-O-acyl-1-phosphatidyl-1D-myo-inositols
type: SmallMoleculeReference
name: 6-O-{alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(1->6)-2-O-[(2-aminoethyl)phosphoryl]-alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl}-O-acyl-1-phosphatidyl-1D-myo-inositol [ChEBI:53059]
name: 6-O-{alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(1->6)-2-O-[(2-aminoethyl)phosphoryl]-alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl}-O-acyl-1-phosphatidyl-1D-myo-inositol
xref: UnificationXref8062

(GlcN)1 (Ino(acyl)-P)1 (Man)2 (EtN)1 (P)1
type: SmallMoleculeReference
xref: UnificationXref8052

6-O-[alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl]-O-acyl-1-phosphatidyl-1D-myo-inositols
type: SmallMoleculeReference
name: 6-O-[alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl]-O-acyl-1-phosphatidyl-1D-myo-inositol
name: 6-O-[alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl]-O-acyl-1-phosphatidyl-1D-myo-inositol [ChEBI:53056]
xref: UnificationXref8037

http://identifiers.org/pubmed/1335363
type: PublicationXref
id: 1335363
author: Birnbaumer, L
db: Pubmed
title: Receptor-to-effector signaling through G proteins: roles for beta gamma dimers as well as alpha subunits
source: Cell 71:1069-72
year: 1992

UnificationXref1961
type: UnificationXref
id: Q9UTI8
db: UniProt

UnificationXref1960
type: UnificationXref
id: 3659271
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659271

UnificationXref1963
type: UnificationXref
id: Q10157
db: UniProt

UnificationXref1962
type: UnificationXref
id: 3659235
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659235

UnificationXref1965
type: UnificationXref
id: Q9URX6
db: UniProt

UnificationXref1964
type: UnificationXref
id: 3658995
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3658995

UnificationXref1959
type: UnificationXref
id: 3659220
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659220

UnificationXref1957
type: UnificationXref
id: 3659040
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659040

UnificationXref1958
type: UnificationXref
id: P05767
db: UniProt

UnificationXref1955
type: UnificationXref
id: O14339
db: UniProt

UnificationXref1956
type: UnificationXref
id: 3659039
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659039

http://identifiers.org/pubmed/9305914
type: PublicationXref
id: 9305914
author: Ishimi, Y
db: Pubmed
title: A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex.
source: J Biol Chem 272:24508-13
year: 1997

Evidence9
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: At the beginning of this reaction, 1 molecule of 'hNTH1', and 1 molecule of 'Double-strand DNA containing a cytosine glycol' are present. At the end of this reaction, 1 molecule of 'hNTH1 glycosylase:cytosine glycol complex' is present. This reaction takes place in the 'nucleus'.

Evidence8
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: At the beginning of this reaction, 1 molecule of 'Double-strand DNA containing an uracil opposite to a guanine', and 1 molecule of 'G/T mismatch-specific thymine DNA glycosylase (EC 3.2.2.-)' are present. At the end of this reaction, 1 molecule of 'TDG glycosylase:uracil complex' is present. This reaction takes place in the 'nucleus'.

Evidence7
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: At the beginning of this reaction, 1 molecule of 'Double-strand DNA containing a thymine opposite to a guanine', and 1 molecule of 'G/T mismatch-specific thymine DNA glycosylase (EC 3.2.2.-)' are present. At the end of this reaction, 1 molecule of 'TDG glycosylase:thymine complex' is present. This reaction takes place in the 'nucleus' and is mediated by the 'DNA N-glycosylase activity' of 'G/T mismatch-specific thymine DNA glycosylase (EC 3.2.2.-)'.

UnificationXref1954
type: UnificationXref
id: 3659035
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659035

Evidence2
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9724657
comment: The recognition and cleavage of an altered base by a DNA glycosylase is thought to involve the diffusion of the enzyme along the minor grove of the DNA molecule. The enzyme presumably compresses the backbone of the affected DNA strand at the site of damage. This compression is thought to result in an outward rotation of the damaged residue into a "pocket" of the enzyme that recognizes and cleaves the altered base (Parikh et al., 1998).

UnificationXref1953
type: UnificationXref
id: O59794
db: UniProt

Evidence1
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: At the beginning of this reaction, 1 molecule of 'Double-strand DNA containing an adenine opposite to an 8-oxo guanine', and 1 molecule of 'MYH glycosylase' are present. At the end of this reaction, 1 molecule of 'MYH glycosylase:adenine complex' is present. This reaction takes place in the 'nucleus'.

UnificationXref1952
type: UnificationXref
id: 3659132
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659132

UnificationXref1951
type: UnificationXref
id: Q92366
db: UniProt

UnificationXref1950
type: UnificationXref
id: 3659031
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659031

Evidence6
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: At the beginning of this reaction, 1 molecule of 'Double-strand DNA containing an ethenocytosine', and 1 molecule of 'G/T mismatch-specific thymine DNA glycosylase (EC 3.2.2.-)' are present. At the end of this reaction, 1 molecule of 'TDG glycosylase:ethenocytosine complex' is present. This reaction takes place in the 'nucleus'.

Evidence5
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Depurination of a damaged nucleotide is mediated by a purine-specific DNA glycosylase. The glycosylase cleaves the N-C1' glycosidic bond between the damaged DNA base and the deoxyribose sugar generating a free base and an apurinic (AP) site.

Evidence4
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10583946
comment: Damaged purines are first cleaved by purine-specific glycosylases (see Lindahl and Wood 1999).

http://identifiers.org/pubmed/8114698
type: PublicationXref
id: 8114698
author: Nevins, JR
author: Ohtani, K
db: Pubmed
title: Functional properties of a Drosophila homolog of the E2F1 gene
source: Mol Cell Biol 14:1603-12
year: 1994

Evidence3
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10583946
comment: At the beginning of this reaction, 1 molecule of 'MYH glycosylase:adenine complex' is present. At the end of this reaction, 1 molecule of 'DNA containing an MYH-bound apurinic/apyrimidinic site', and 1 molecule of '8-oxoguanine' are present. This reaction takes place in the 'nucleus' and is mediated by the 'DNA N-glycosylase activity' of 'MYH glycosylase'.

UnificationXref1948
type: UnificationXref
id: Q9US22
db: UniProt

UnificationXref1949
type: UnificationXref
id: 3659030
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659030

UnificationXref1944
type: UnificationXref
id: P79071
db: UniProt

UnificationXref1945
type: UnificationXref
id: 3659240
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659240

UnificationXref1946
type: UnificationXref
id: O74895
db: UniProt

UnificationXref1947
type: UnificationXref
id: 3659026
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659026

UnificationXref1941
type: UnificationXref
id: P36584
db: UniProt

UnificationXref1940
type: UnificationXref
id: 3659136
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659136

UnificationXref1943
type: UnificationXref
id: 3659141
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659141

UnificationXref1942
type: UnificationXref
id: 3659140
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659140

Aquaporin-mediated transport
type: Pathway
data source: Provenance1
pathway component: REACT 82029.9
pathway component: REACT 158613.3
pathway component: REACT 158240.3
evidence: Evidence998
xref: RelationshipXref850
xref: UnificationXref6507
xref: UnificationXref6506
pathway order: PathwayStep982
pathway order: PathwayStep979
pathway order: PathwayStep977
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UnificationXref6294
type: UnificationXref
id: 427962
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=427962

tRNA(Leu)
type: SmallMolecule
entity reference: CHEBI:29169
data source: Provenance1
xref: UnificationXref7152
xref: UnificationXref7153
cellular location: GO:0005759
comment: Reactome DB_ID: 379788

UnificationXref6293
type: UnificationXref
id: REACT_19449
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19449.2

Ile-tRNA(Ile)
type: SmallMolecule
entity reference: CHEBI:29160
data source: Provenance1
xref: UnificationXref7146
xref: UnificationXref7145
cellular location: GO:0005759
comment: Reactome DB_ID: 379769

UnificationXref6292
type: UnificationXref
id: 427949
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=427949

tRNA(Ile)
type: SmallMolecule
entity reference: CHEBI:29174
data source: Provenance1
xref: UnificationXref7143
xref: UnificationXref7142
cellular location: GO:0005759
comment: Reactome DB_ID: 379750

UnificationXref6291
type: UnificationXref
id: REACT_19627
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19627.2

Gly-tRNA(Gly)
type: SmallMolecule
entity reference: CHEBI:29156
data source: Provenance1
xref: UnificationXref7136
xref: UnificationXref7135
cellular location: GO:0005759
comment: Reactome DB_ID: 379781

UnificationXref6290
type: UnificationXref
id: 428001
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428001

tRNA(Gly)
type: SmallMolecule
entity reference: CHEBI:29176
data source: Provenance1
xref: UnificationXref7133
xref: UnificationXref7134
cellular location: GO:0005759
comment: Reactome DB_ID: 379770

UniProt:Q10178
type: ProteinReference
xref: UnificationXref5742
organism: BioSource1

Gln-tRNA(Gln)
type: SmallMolecule
entity reference: CHEBI:29166
data source: Provenance1
xref: UnificationXref7128
xref: UnificationXref7127
cellular location: GO:0005759
comment: Reactome DB_ID: 379753

UniProt:Q10179
type: ProteinReference
xref: UnificationXref7010
organism: BioSource1

L-Glutamine
type: SmallMolecule
entity reference: L-Glutamine
data source: Provenance1
name: L-2-Aminoglutaramic acid
xref: UnificationXref7125
xref: UnificationXref7124
cellular location: GO:0005759
comment: Reactome DB_ID: 113522
display name: L-Gln

tRNA(Gln)
type: SmallMolecule
entity reference: CHEBI:29168
data source: Provenance1
xref: UnificationXref7122
xref: UnificationXref7123
cellular location: GO:0005759
comment: Reactome DB_ID: 379740

tRNA(Lys)
type: SmallMolecule
entity reference: CHEBI:29185
data source: Provenance1
xref: UnificationXref7162
xref: UnificationXref7163
cellular location: GO:0005759
comment: Reactome DB_ID: 379747

Lys-tRNA(Lys)
type: SmallMolecule
entity reference: CHEBI:16047
data source: Provenance1
xref: UnificationXref7165
xref: UnificationXref7166
cellular location: GO:0005759
comment: Reactome DB_ID: 379795

UnificationXref6288
type: UnificationXref
id: 428004
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428004

UnificationXref6289
type: UnificationXref
id: REACT_19793
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19793.2

Leu-tRNA(Leu)
type: SmallMolecule
entity reference: CHEBI:16624
data source: Provenance1
xref: UnificationXref7156
xref: UnificationXref7155
cellular location: GO:0005759
comment: Reactome DB_ID: 379773

UnificationXref6286
type: UnificationXref
id: 427983
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=427983

UnificationXref6287
type: UnificationXref
id: REACT_19696
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19696.2

UnificationXref6284
type: UnificationXref
id: 427955
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=427955

UnificationXref6285
type: UnificationXref
id: REACT_20377
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20377.2

Processing and Activation of SUMO
type: Pathway
data source: Provenance1
pathway component: REACT 168890.1
pathway component: REACT 168454.1
pathway component: REACT 167159.1
evidence: Evidence1393
xref: UnificationXref8654
xref: RelationshipXref1105
xref: UnificationXref8655
pathway order: PathwayStep1362
pathway order: PathwayStep1368
pathway order: PathwayStep1366
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UnificationXref6281
type: UnificationXref
id: REACT_20469
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20469.2

tRNA(Asn)
type: SmallMolecule
entity reference: CHEBI:29172
data source: Provenance1
xref: UnificationXref7092
xref: UnificationXref7093
cellular location: GO:0005759
comment: Reactome DB_ID: 379699

UnificationXref6280
type: UnificationXref
id: 428017
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428017

L-Asparagine
type: SmallMolecule
entity reference: CHEBI:17196
data source: Provenance1
name: 2-Aminosuccinamic acid
xref: UnificationXref7090
xref: UnificationXref7091
cellular location: GO:0005759
comment: Reactome DB_ID: 379703
display name: L-Asn

UnificationXref6283
type: UnificationXref
id: REACT_20104
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20104.2

tRNA(Asp)
type: SmallMolecule
entity reference: CHEBI:29186
data source: Provenance1
xref: UnificationXref7101
xref: UnificationXref7102
cellular location: GO:0005759
comment: Reactome DB_ID: 379715

UnificationXref6282
type: UnificationXref
id: 428006
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428006

Asn-tRNA(Asn)
type: SmallMolecule
entity reference: CHEBI:29265
data source: Provenance1
xref: UnificationXref7094
xref: UnificationXref7095
cellular location: GO:0005759
comment: Reactome DB_ID: 379718

Ala-tRNA(Ala)
type: SmallMolecule
entity reference: CHEBI:17732
data source: Provenance1
xref: UnificationXref7076
xref: UnificationXref7075
cellular location: GO:0005759
comment: Reactome DB_ID: 379730

tRNA(Ala)
type: SmallMolecule
entity reference: CHEBI:17732
data source: Provenance1
xref: UnificationXref7073
xref: UnificationXref7074
cellular location: GO:0005759
comment: Reactome DB_ID: 379729

Arg-tRNA(Arg)
type: SmallMolecule
entity reference: Arg-tRNA(Arg)
data source: Provenance1
xref: UnificationXref7084
xref: UnificationXref7085
cellular location: GO:0005759
comment: Reactome DB_ID: 379708

tRNA(Arg)
type: SmallMolecule
entity reference: CHEBI:29171
data source: Provenance1
xref: UnificationXref7081
xref: UnificationXref7082
cellular location: GO:0005759
comment: Reactome DB_ID: 379727

UniProt:Q10185
type: ProteinReference
xref: UnificationXref3583
organism: BioSource1

Asp-tRNA(Asp)
type: SmallMolecule
entity reference: CHEBI:29158
data source: Provenance1
xref: UnificationXref7105
xref: UnificationXref7104
cellular location: GO:0005759
comment: Reactome DB_ID: 379698

UnificationXref6277
type: UnificationXref
id: REACT_20082
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20082.2

UnificationXref6278
type: UnificationXref
id: 427963
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=427963

UnificationXref6279
type: UnificationXref
id: REACT_20458
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20458.2

tRNA(Glu)
type: SmallMolecule
entity reference: CHEBI:29175
data source: Provenance1
xref: UnificationXref7113
xref: UnificationXref7112
cellular location: GO:0005759
comment: Reactome DB_ID: 379754

Glu-tRNA(Glu)
type: SmallMolecule
entity reference: CHEBI:29157
data source: Provenance1
xref: UnificationXref7116
xref: UnificationXref7115
cellular location: GO:0005759
comment: Reactome DB_ID: 379744

UnificationXref6273
type: UnificationXref
id: REACT_19727
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19727.2

UnificationXref6274
type: UnificationXref
id: 428011
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428011

UnificationXref6275
type: UnificationXref
id: REACT_19710
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19710.2

UnificationXref6276
type: UnificationXref
id: 428042
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428042

tRNA(Ser)
type: SmallMolecule
entity reference: CHEBI:29179
data source: Provenance1
xref: UnificationXref7029
xref: UnificationXref7030
cellular location: GO:0005829
comment: Reactome DB_ID: 379762

Phe-tRNA(Phe)
type: SmallMolecule
entity reference: CHEBI:29153
data source: Provenance1
xref: UnificationXref7019
xref: UnificationXref7020
cellular location: GO:0005829
comment: Reactome DB_ID: 379792

UniProt:Q10157
type: ProteinReference
xref: UnificationXref1963
organism: BioSource1

tRNA(Phe)
type: SmallMolecule
entity reference: CHEBI:29184
data source: Provenance1
xref: UnificationXref7017
xref: UnificationXref7016
cellular location: GO:0005829
comment: Reactome DB_ID: 379767

Gly-tRNA(Gly)
type: SmallMolecule
entity reference: CHEBI:29156
data source: Provenance1
xref: UnificationXref7008
xref: UnificationXref7009
cellular location: GO:0005829
comment: Reactome DB_ID: 379784

UniProt:Q10159
type: ProteinReference
xref: UnificationXref3
organism: BioSource1

tRNA(Trp)
type: SmallMolecule
entity reference: CHEBI:29181
data source: Provenance1
xref: UnificationXref7052
xref: UnificationXref7051
cellular location: GO:0005829
comment: Reactome DB_ID: 379763

Thr-tRNA(Thr)
type: SmallMolecule
entity reference: CHEBI:29163
data source: Provenance1
xref: UnificationXref7044
xref: UnificationXref7043
cellular location: GO:0005829
comment: Reactome DB_ID: 379783

tRNA(Thr)
type: SmallMolecule
entity reference: CHEBI:29180
data source: Provenance1
xref: UnificationXref7041
xref: UnificationXref7040
cellular location: GO:0005829
comment: Reactome DB_ID: 379749

Ser-tRNA(Ser)
type: SmallMolecule
entity reference: CHEBI:29162
data source: Provenance1
xref: UnificationXref7033
xref: UnificationXref7032
cellular location: GO:0005829
comment: Reactome DB_ID: 379738

tRNA(Val)
type: SmallMolecule
entity reference: CHEBI:29183
data source: Provenance1
xref: UnificationXref7062
xref: UnificationXref7063
cellular location: GO:0005829
comment: Reactome DB_ID: 379793

Trp-tRNA(Trp)
type: SmallMolecule
entity reference: CHEBI:29159
data source: Provenance1
xref: UnificationXref7055
xref: UnificationXref7054
cellular location: GO:0005829
comment: Reactome DB_ID: 379765

UniProt:Q10153
type: ProteinReference
xref: UnificationXref3342
organism: BioSource1

Regulation of Rheb GTPase activity by AMPK
type: Pathway
data source: Provenance1
pathway component: TSC2 activates intrinsic GTPase activity of Rheb
evidence: Evidence209
xref: UnificationXref1121
xref: UnificationXref1120
pathway order: PathwayStep206
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Val-tRNA(Val)
type: SmallMolecule
entity reference: CHEBI:29164
data source: Provenance1
xref: UnificationXref7065
xref: UnificationXref7066
cellular location: GO:0005829
comment: Reactome DB_ID: 379790

SU5402
type: SmallMolecule
entity reference: CHEBI:63449
data source: Provenance1
xref: UnificationXref6938
xref: UnificationXref6937
cellular location: GO:0005829
comment: Reactome DB_ID: 2054052

phenyllactate
type: SmallMolecule
entity reference: Phenyllactate [ChEBI:8100]
data source: Provenance1
xref: UnificationXref6962
xref: UnificationXref6963
cellular location: GO:0005829
comment: Reactome DB_ID: 2160481

keto-phenylpyruvate
type: SmallMolecule
entity reference: 3-phenyl-2-oxopropanoate
data source: Provenance1
xref: UnificationXref6958
xref: UnificationXref6957
cellular location: GO:0005829
comment: Reactome DB_ID: 2160487

Ala-tRNA(Ala)
type: SmallMolecule
entity reference: CHEBI:17732
data source: Provenance1
xref: UnificationXref6978
xref: UnificationXref6977
cellular location: GO:0005829
comment: Reactome DB_ID: 379700

tRNA(Ala)
type: SmallMolecule
entity reference: CHEBI:17732
data source: Provenance1
xref: UnificationXref6976
xref: UnificationXref6975
cellular location: GO:0005829
comment: Reactome DB_ID: 379731

Asn-tRNA(Asn)
type: SmallMolecule
entity reference: CHEBI:29265
data source: Provenance1
xref: UnificationXref6988
xref: UnificationXref6987
cellular location: GO:0005829
comment: Reactome DB_ID: 379728

tRNA(Asn)
type: SmallMolecule
entity reference: CHEBI:29172
data source: Provenance1
xref: UnificationXref6985
xref: UnificationXref6984
cellular location: GO:0005829
comment: Reactome DB_ID: 379722

Cys-tRNA(Cys)
type: SmallMolecule
entity reference: CHEBI:29152
data source: Provenance1
xref: UnificationXref6997
xref: UnificationXref6998
cellular location: GO:0005829
comment: Reactome DB_ID: 379719

tRNA(Cys)
type: SmallMolecule
entity reference: CHEBI:29167
data source: Provenance1
xref: UnificationXref6994
xref: UnificationXref6995
cellular location: GO:0005829
comment: Reactome DB_ID: 379725

tRNA(Gly)
type: SmallMolecule
entity reference: CHEBI:29176
data source: Provenance1
xref: UnificationXref7005
xref: UnificationXref7006
cellular location: GO:0005829
comment: Reactome DB_ID: 379766

UniProt:Q10164
type: ProteinReference
xref: UnificationXref1328
organism: BioSource1

UniProt:Q10163
type: ProteinReference
xref: UnificationXref5696
organism: BioSource1

http://identifiers.org/pubmed/10522552
type: PublicationXref
id: 10522552
author: Ponka, P
db: Pubmed
title: Cell biology of heme
source: Am J Med Sci 318:241-56
year: 1999

UnificationXref6295
type: UnificationXref
id: REACT_19468
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19468.2

UnificationXref6296
type: UnificationXref
id: 427964
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=427964

UnificationXref6297
type: UnificationXref
id: REACT_19881
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19881.2

http://identifiers.org/pubmed/16116451
type: PublicationXref
id: 16116451
author: Szabó, SI
author: Makara, JK
author: Fegley, D
author: Freund, TF
author: Tontini, A
author: Duranti, A
author: Mor, M
author: Astarita, G
author: Piomelli, D
author: Rivara, S
author: Tarzia, G
author: Kathuria, S
db: Pubmed
title: Selective inhibition of 2-AG hydrolysis enhances endocannabinoid signaling in hippocampus
source: Nat Neurosci 8:1139-41
year: 2005

UnificationXref6298
type: UnificationXref
id: 427978
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=427978

UnificationXref6299
type: UnificationXref
id: REACT_20169
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20169.2

UniProt:Q10132
type: ProteinReference
xref: UnificationXref2961
organism: BioSource1

Midostaurin
type: SmallMolecule
entity reference: CHEBI:63452
data source: Provenance1
xref: UnificationXref6931
xref: UnificationXref6932
cellular location: GO:0005829
comment: Reactome DB_ID: 2038921
display name: PKC412

http://identifiers.org/pubmed/12949583
type: PublicationXref
id: 12949583
author: van den Bosch, M
author: Lowndes, NF
author: Bree, RT
db: Pubmed
title: The MRN complex: coordinating and mediating the response to broken chromosomes.
source: EMBO Rep 4:844-9
year: 2003

UniProt:Q9C0W7
type: ProteinReference
xref: UnificationXref8673
organism: BioSource1

PD173074
type: SmallMolecule
entity reference: CHEBI:63448
data source: Provenance1
xref: UnificationXref6934
xref: UnificationXref6935
cellular location: GO:0005829
comment: Reactome DB_ID: 2038919

Tyrosine kinase inhibitors of FGFR1 fusion mutants
type: SmallMolecule
data source: Provenance1
member physical entity: Dovitinib
member physical entity: SU5402
member physical entity: PD173074
member physical entity: Midostaurin
xref: UnificationXref6939
xref: UnificationXref6940
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 2045079

Dovitinib
type: SmallMolecule
entity reference: CHEBI:594834
data source: Provenance1
xref: UnificationXref6929
xref: UnificationXref6928
cellular location: GO:0005829
comment: Reactome DB_ID: 1839035
display name: TKI258

Herbimycin A
type: SmallMolecule
entity reference: CHEBI:5674
data source: Provenance1
xref: UnificationXref6888
xref: UnificationXref6889
cellular location: GO:0005829
comment: Reactome DB_ID: 1217510
display name: herbimycin

UnificationXref6250
type: UnificationXref
id: REACT_14295
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_14295.2

retaspimycin hydrochloride
type: SmallMolecule
entity reference: CHEBI:71956
data source: Provenance1
xref: UnificationXref6892
xref: UnificationXref6891
cellular location: GO:0005829
comment: Reactome DB_ID: 1217514
display name: IPI-504

alvespimycin
type: SmallMolecule
entity reference: alvespimycin [ChEBI:65324]
data source: Provenance1
xref: UnificationXref6882
xref: UnificationXref6883
cellular location: GO:0005829
comment: Reactome DB_ID: 1217507
display name: 17-DMAG

Geldanamycin
type: SmallMolecule
entity reference: CHEBI:5292
data source: Provenance1
xref: UnificationXref6885
xref: UnificationXref6886
cellular location: GO:0005829
comment: Reactome DB_ID: 1217505

Benzoquinoid ansamycins
type: SmallMolecule
data source: Provenance1
member physical entity: Herbimycin A
member physical entity: alvespimycin
member physical entity: retaspimycin hydrochloride
member physical entity: Geldanamycin
member physical entity: 17-AAG
xref: UnificationXref6894
xref: UnificationXref6893
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 1217511

UniProt:Q10133
type: ProteinReference
xref: UnificationXref738
organism: BioSource1

17-AAG
type: SmallMolecule
entity reference: CHEBI:64153
data source: Provenance1
xref: UnificationXref6880
xref: UnificationXref6879
cellular location: GO:0005829
comment: Reactome DB_ID: 1217506

UnificationXref6247
type: UnificationXref
id: 113538
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113538

UnificationXref6246
type: UnificationXref
id: REACT_14674
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_14674.2

UnificationXref6245
type: UnificationXref
id: 351979
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351979

UnificationXref6244
type: UnificationXref
id: REACT_3169
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3169.2

UnificationXref6243
type: UnificationXref
id: 29612
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29612

UnificationXref6242
type: UnificationXref
id: REACT_20441
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20441.1

UnificationXref6241
type: UnificationXref
id: 428037
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428037

UnificationXref6240
type: UnificationXref
id: REACT_20221
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20221.1

UnificationXref6249
type: UnificationXref
id: 351990
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351990

UnificationXref6248
type: UnificationXref
id: REACT_2613
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2613.2

http://identifiers.org/pubmed/2995393
type: PublicationXref
id: 2995393
author: Fitzpatrick, F
author: McGee, J
db: Pubmed
title: Enzymatic hydration of leukotriene A4. Purification and characterization of a novel epoxide hydrolase from human erythrocytes
source: J Biol Chem 260:12832-7
year: 1985

UniProt:Q10147
type: ProteinReference
xref: UnificationXref7909
organism: BioSource1

UnificationXref6234
type: UnificationXref
id: REACT_143624
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_143624.5

UnificationXref6233
type: UnificationXref
id: 3665469
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665469

UnificationXref6236
type: UnificationXref
id: REACT_13894
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_13894.1

UnificationXref6235
type: UnificationXref
id: 351626
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351626

UnificationXref6230
type: UnificationXref
id: 3662612
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662612

UnificationXref6232
type: UnificationXref
id: REACT_28922
db: Reactome
id version: 10
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_28922.10

UnificationXref6231
type: UnificationXref
id: 3662614
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662614

UnificationXref6238
type: UnificationXref
id: REACT_19989
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19989.1

UnificationXref6237
type: UnificationXref
id: 427956
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=427956

UnificationXref6239
type: UnificationXref
id: 427999
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=427999

UniProt:Q10110
type: ProteinReference
xref: UnificationXref630
organism: BioSource1

UnificationXref6271
type: UnificationXref
id: REACT_20264
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20264.2

UnificationXref6272
type: UnificationXref
id: 428020
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428020

UnificationXref6270
type: UnificationXref
id: 428038
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428038

UnificationXref6265
type: UnificationXref
id: 3662628
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662628

UnificationXref6264
type: UnificationXref
id: 3662627
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662627

UnificationXref6263
type: UnificationXref
id: Q9P380
db: UniProt

UnificationXref6262
type: UnificationXref
id: REACT_20481
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20481.1

UnificationXref6269
type: UnificationXref
id: GO:0043202
db: GENE ONTOLOGY

2'-deoxyinosine
type: SmallMoleculeReference
name: deoxyinosine
name: 2'-deoxyinosine [ChEBI:28997]
xref: UnificationXref4230

UnificationXref6268
type: UnificationXref
id: REACT_152751
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_152751.3

UnificationXref6267
type: UnificationXref
id: 3662631
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662631

UnificationXref6266
type: UnificationXref
id: 3662629
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662629

UniProt:Q9C0Z7
type: ProteinReference
xref: UnificationXref1090
organism: BioSource1

http://identifiers.org/pubmed/11278486
type: PublicationXref
id: 11278486
author: Chong, C
author: Tan, L
author: Lim, L
author: Manser, E
db: Pubmed
title: The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity
source: J Biol Chem 276:17347-53
year: 2001

UnificationXref6260
type: UnificationXref
id: REACT_19446
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19446.1

UnificationXref6261
type: UnificationXref
id: 428026
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428026

UnificationXref6252
type: UnificationXref
id: REACT_3188
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3188.2

UnificationXref6251
type: UnificationXref
id: 29500
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29500

UnificationXref6254
type: UnificationXref
id: REACT_2616
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2616.2

UnificationXref6253
type: UnificationXref
id: 29506
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29506

UnificationXref6256
type: UnificationXref
id: REACT_20059
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20059.1

UnificationXref6255
type: UnificationXref
id: 400144
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=400144

UnificationXref6258
type: UnificationXref
id: REACT_19695
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19695.1

UnificationXref6257
type: UnificationXref
id: 427981
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=427981

UnificationXref6259
type: UnificationXref
id: 428046
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428046

http://identifiers.org/pubmed/12016139
type: PublicationXref
id: 12016139
author: Jackson, SP
db: Pubmed
title: Sensing and repairing DNA double-strand breaks
source: Carcinogenesis 23:687-96
year: 2002

http://identifiers.org/pubmed/12123609
type: PublicationXref
id: 12123609
author: Snider, WD
author: Zhong, J
author: Markus, A
db: Pubmed
title: Raf and akt mediate distinct aspects of sensory axon growth
source: Neuron 35:65-76
year: 2002

http://identifiers.org/pubmed/10958673
type: PublicationXref
id: 10958673
author: Yoshida, H
author: Haze, K
author: Yura, T
author: Yanagi, H
author: Mori, K
author: Okada, T
author: Negishi, M
db: Pubmed
title: ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response
source: Mol Cell Biol 20:6755-67
year: 2000

http://identifiers.org/pubmed/18772128
type: PublicationXref
id: 18772128
author: Riekhof, WR
author: Voelker, DR
author: Gijon, MA
author: Zarini, S
author: Murphy, RC
db: Pubmed
title: Lysophospholipid acyltransferases and arachidonate recycling in human neutrophils
source: J Biol Chem 283:30235-45
year: 2008

http://identifiers.org/pubmed/19935646
type: PublicationXref
id: 19935646
author: Jang, HG
author: Dang, L
author: Keenan, MC
author: Vander Heiden, MG
author: Bennett, BD
author: Rabinowitz, JD
author: Driggers, EM
author: Gross, S
author: Ward, PS
author: Fantin, VR
author: Thompson, CB
author: Cantley, LC
author: Marks, KM
author: White, DW
author: Bittinger, MA
author: Prins, RM
author: Su, SM
author: Yen, KE
author: Liau, LM
author: Jin, S
db: Pubmed
title: Cancer-associated IDH1 mutations produce 2-hydroxyglutarate
source: Nature 462:739-44
year: 2009

Synthesis of Dolichyl-phosphate
type: Pathway
data source: Provenance1
pathway component: Phosphorylation of dolichol
evidence: Evidence1293
xref: UnificationXref8082
xref: RelationshipXref1032
xref: UnificationXref8083
pathway order: PathwayStep1271
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/19935667
type: PublicationXref
id: 19935667
author: Hall, RA
author: Ritter, SL
db: Pubmed
title: Fine-tuning of GPCR activity by receptor-interacting proteins
source: Nat Rev Mol Cell Biol 10:819-30
year: 2009

Ketone body metabolism
type: Pathway
data source: Provenance1
pathway component: Utilization of Ketone Bodies
pathway component: REACT 113077.8
evidence: Evidence429
xref: UnificationXref2839
xref: UnificationXref2840
xref: RelationshipXref252
pathway order: PathwayStep420
pathway order: PathwayStep418
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

phosphatidylethanolamine
type: SmallMolecule
entity reference: CHEBI:16038
data source: Provenance1
xref: UnificationXref8035
xref: UnificationXref8036
cellular location: GO:0005789
comment: Reactome DB_ID: 162803
display name: PE

CoA-SH
type: SmallMolecule
entity reference: CHEBI:15346
data source: Provenance1
xref: UnificationXref8028
xref: UnificationXref8029
cellular location: GO:0005788
comment: Reactome DB_ID: 162743

glucosaminyl-acyl-PI
type: SmallMolecule
entity reference: CHEBI:52572
data source: Provenance1
xref: UnificationXref8026
xref: UnificationXref8027
cellular location: GO:0005789
comment: Reactome DB_ID: 162856
display name: GlcN-acyl-PI

http://identifiers.org/pubmed/11988738
type: PublicationXref
id: 11988738
author: Lukas, J
author: Jackson, PK
author: Reimann, JD
author: Sorensen, CS
author: Hsu, JY
db: Pubmed
title: E2F-dependent accumulation of hEmi1 regulates S phase entry by inhibiting APC(Cdh1)
source: Nat Cell Biol 4:358-66
year: 2002

uridine 5'-diphosphate
type: SmallMolecule
entity reference: CHEBI:17659
data source: Provenance1
xref: UnificationXref7998
xref: UnificationXref7999
cellular location: GO:0005829
comment: Reactome DB_ID: 110096
display name: UDP

N-acetylglucosaminyl-PI
type: SmallMolecule
entity reference: CHEBI:15935
data source: Provenance1
name: N-acetyl-D-glucosaminylphosphatidylinositol
xref: UnificationXref7996
xref: UnificationXref7995
cellular location: GO:0005789
comment: Reactome DB_ID: 162341
display name: GlcNAc-PI

Fatty acyl CoA
type: SmallMolecule
entity reference: CHEBI:37554
data source: Provenance1
xref: UnificationXref8023
xref: UnificationXref8024
cellular location: GO:0005788
comment: Reactome DB_ID: 162768
display name: acyl-CoA

glucosaminyl-PI
type: SmallMolecule
entity reference: CHEBI:24275
data source: Provenance1
xref: UnificationXref8016
xref: UnificationXref8015
cellular location: GO:0005789
comment: Reactome DB_ID: 162839
display name: GlcN-PI

1,3-diaminopropane
type: SmallMolecule
entity reference: CHEBI:15725
data source: Provenance1
xref: UnificationXref7964
xref: UnificationXref7963
cellular location: GO:0005829
comment: Reactome DB_ID: 204628

UDP-N-acetylglucosamine
type: SmallMolecule
entity reference: UDP-N-acetyl-D-glucosamine
data source: Provenance1
name: UDP-N-acetyl-D-glucosamine
xref: UnificationXref7992
xref: UnificationXref7993
cellular location: GO:0005829
comment: Reactome DB_ID: 162756
display name: UDP-AcGlcN

1-Phosphatidyl-D-myo-inositol
type: SmallMolecule
entity reference: CHEBI:16749
data source: Provenance1
name: phosphatidylinositol
xref: UnificationXref7990
xref: UnificationXref7991
cellular location: GO:0005789
comment: Reactome DB_ID: 162339
display name: PI

Tyr-tRNA(Tyr)
type: SmallMolecule
entity reference: CHEBI:29161
data source: Provenance1
xref: UnificationXref7471
xref: UnificationXref7472
cellular location: GO:0005829
comment: Reactome DB_ID: 379785

NNNNNNNNNNNTTAGGGTTA - 3' (in human)
type: SmallMolecule
entity reference: CHEBI:15986
data source: Provenance1
xref: UnificationXref7813
xref: UnificationXref7814
cellular location: GO:0005654
comment: Reactome DB_ID: 163089
display name: G-strand chromosome end - Telomeric

G-strand Chromosome end with an additional single strand repeat - Telomeric
type: SmallMolecule
entity reference: CHEBI:15986
data source: Provenance1
xref: UnificationXref7827
xref: UnificationXref7826
cellular location: GO:0005654
comment: Reactome DB_ID: 177801
display name: NNNNNNNNNNNTTAGGGTTATTAGGGTTA - 3' (in human)

G-strand Chromosome end with two additional single strand repeats - Telomeric
type: SmallMolecule
entity reference: CHEBI:15986
data source: Provenance1
xref: UnificationXref7833
xref: UnificationXref7834
cellular location: GO:0005654
comment: Reactome DB_ID: 163085
display name: NNNNNNNNNNNTTAGGGTTATTAGGGTTATTAGGGTTA - 3' (in human)

Pro-tRNA(Pro)
type: SmallMolecule
entity reference: CHEBI:29154
data source: Provenance1
xref: UnificationXref7470
xref: UnificationXref7469
cellular location: GO:0005829
comment: Reactome DB_ID: 379746

Met-tRNA(Met)
type: SmallMolecule
entity reference: CHEBI:16635
data source: Provenance1
xref: UnificationXref7467
xref: UnificationXref7468
cellular location: GO:0005829
comment: Reactome DB_ID: 379794

Lys-tRNA(Lys)
type: SmallMolecule
entity reference: CHEBI:16047
data source: Provenance1
xref: UnificationXref7465
xref: UnificationXref7466
cellular location: GO:0005829
comment: Reactome DB_ID: 379736

Leu-tRNA(Leu)
type: SmallMolecule
entity reference: CHEBI:16624
data source: Provenance1
xref: UnificationXref7463
xref: UnificationXref7464
cellular location: GO:0005829
comment: Reactome DB_ID: 379757

Ile-tRNA(Ile)
type: SmallMolecule
entity reference: CHEBI:29160
data source: Provenance1
xref: UnificationXref7462
xref: UnificationXref7461
cellular location: GO:0005829
comment: Reactome DB_ID: 379787

His-tRNA(His)
type: SmallMolecule
entity reference: CHEBI:29155
data source: Provenance1
xref: UnificationXref7460
xref: UnificationXref7459
cellular location: GO:0005829
comment: Reactome DB_ID: 379786

http://identifiers.org/pubmed/19006241
type: PublicationXref
id: 19006241
author: Häberle, J
author: Höhne, W
author: Engel, K
db: Pubmed
title: Mutations and polymorphisms in the human argininosuccinate synthetase (ASS1) gene
source: Hum Mutat 30:300-7
year: 2009

Glu-tRNA(Glu)
type: SmallMolecule
entity reference: CHEBI:29157
data source: Provenance1
xref: UnificationXref7457
xref: UnificationXref7456
cellular location: GO:0005829
comment: Reactome DB_ID: 379751

Asp-tRNA(Asp)
type: SmallMolecule
entity reference: CHEBI:29158
data source: Provenance1
xref: UnificationXref7453
xref: UnificationXref7452
cellular location: GO:0005829
comment: Reactome DB_ID: 379707

Gln-tRNA(Gln)
type: SmallMolecule
entity reference: CHEBI:29166
data source: Provenance1
xref: UnificationXref7455
xref: UnificationXref7454
cellular location: GO:0005829
comment: Reactome DB_ID: 379772

Aminoacyl-tRNA
type: SmallMolecule
data source: Provenance1
member physical entity: Ser-tRNA(Ser)
member physical entity: Glu-tRNA(Glu)
member physical entity: Asn-tRNA(Asn)
member physical entity: His-tRNA(His)
member physical entity: Tyr-tRNA(Tyr)
member physical entity: Trp-tRNA(Trp)
member physical entity: Thr-tRNA(Thr)
member physical entity: Met-tRNA(Met)
member physical entity: Phe-tRNA(Phe)
member physical entity: Ala-tRNA(Ala)
member physical entity: Arg-tRNA(Arg)
member physical entity: Gln-tRNA(Gln)
member physical entity: Ile-tRNA(Ile)
member physical entity: Leu-tRNA(Leu)
member physical entity: Val-tRNA(Val)
member physical entity: Gly-tRNA(Gly)
member physical entity: Pro-tRNA(Pro)
member physical entity: Asp-tRNA(Asp)
member physical entity: Cys-tRNA(Cys)
member physical entity: Lys-tRNA(Lys)
xref: UnificationXref7474
xref: UnificationXref7473
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 37001

Arg-tRNA(Arg)
type: SmallMolecule
entity reference: Arg-tRNA(Arg)
data source: Provenance1
xref: UnificationXref7450
xref: UnificationXref7451
cellular location: GO:0005829
comment: Reactome DB_ID: 379720

(S)-2-Amino-3-(p-hydroxyphenyl)propionic acid
type: SmallMolecule
entity reference: CHEBI:17895
data source: Provenance1
name: L-Tyrosine
name: (S)-3-(p-Hydroxyphenyl)alanine
xref: UnificationXref7231
xref: UnificationXref7232
cellular location: GO:0005759
comment: Reactome DB_ID: 379710
display name: L-Tyr

Tyr-tRNA(Tyr)
type: SmallMolecule
entity reference: CHEBI:29161
data source: Provenance1
xref: UnificationXref7238
xref: UnificationXref7237
cellular location: GO:0005759
comment: Reactome DB_ID: 379755

tRNA(Tyr)
type: SmallMolecule
entity reference: CHEBI:29182
data source: Provenance1
xref: UnificationXref7234
xref: UnificationXref7235
cellular location: GO:0005759
comment: Reactome DB_ID: 379756

Val-tRNA(Val)
type: SmallMolecule
entity reference: CHEBI:29164
data source: Provenance1
xref: UnificationXref7246
xref: UnificationXref7247
cellular location: GO:0005759
comment: Reactome DB_ID: 379782

tRNA(Val)
type: SmallMolecule
entity reference: CHEBI:29183
data source: Provenance1
xref: UnificationXref7244
xref: UnificationXref7245
cellular location: GO:0005759
comment: Reactome DB_ID: 379735

Evidence811
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16176984
xref: http://identifiers.org/pubmed/666752
xref: http://identifiers.org/pubmed/16258391
comment: O2-dependent coproporpyrinogen oxidase (CPO) catalyzes the conversion of coproporphyrinogen III (COPRO3) to protoporphyrinogen IX (PPGEN9). The localization of the human enzyme to the mitochondrial intermembrane space is inferred from studies of the homologous rat enzyme (Elder and Evans 1978). The human enzyme functions as a homodimer (Lee et al. 2005). Enzyme deficiency is associated with hereditary coproporphyria in vivo.

Evidence810
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/6822570
xref: http://identifiers.org/pubmed/8644733
xref: http://identifiers.org/pubmed/9564029
comment: Cytosolic uroporphyrinogen decarboxylase (UROD) catalyzes the sequential removal of four carboxylic groups from the acetic acid side chains of uroporphyrinogen I (URO1) to form coproporphyrinogen I (COPRO1). UROD catalyzes this reaction less efficiently than the decarboxylation of uroporphyrinogen III (de Verneuil et al. 1983).

Evidence813
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11175906
xref: http://identifiers.org/pubmed/3327432
comment: Ferrochelatase (FECH) catalyzes the insertion of ferrous iron into protoporphyrin IX (PRIN9) to form heme. FECH is localized on the matrix surface of the inner mitochondrial membrane and this reaction takes place within the mitochondrial matrix. The enzyme functions as a homodimer with each monomer containing a nitric oxide-sensitive 2Fe-2S cluster. Enzyme deficiency is associated with erythropoietic protoporphyria in vivo, and inhibition of ferrochelatase activity is a clinically important consequence of lead poisoning (Piomelli et al. 1987).

Evidence812
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8771201
comment: Six electrons are oxidized in protophorphyrinogen IX (PPGEN9) to form the planar macrocycle protoporphyrin IX (PRIN9). This reaction is performed by the enzyme protoporphyrinogen oxidase (PPO). PPO functions as a homodimer containing one non-covalently-bound FAD. The protein resides on the outer surface of the inner mitochondrial membrane. PPO deficiency is associated with variegate porphyria in vivo.

Evidence815
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12474143
xref: http://identifiers.org/pubmed/15863660
xref: http://identifiers.org/pubmed/9878253
xref: http://identifiers.org/pubmed/15235026
comment: Heme A is the prosthetic group of cytochrome c oxidase, the terminal enzyme in the respiratory chain. It is formed by the action of cytochrome c oxidase assembly protein COX15 homolog (COX15) on heme O (Petruzzella et al. 1998, Antonicka et al. 2003). Defects in COX15 cause of mitochondrial complex IV deficiency (MT-C4D; MIM:220110), also called cytochrome c oxidase deficiency resulting in a disorder of the mitochondrial respiratory chain seen as heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs (Antonicka et al. 2003). Defects in COX15 also cause Leigh syndrome (LS; MIM:256000), an early-onset progressive neurodegenerative disorder characterised by the presence of focal, bilateral lesions in one or more areas of the central nervous system (Oquendo et al. 2004, Bugiani et al. 2005).

Evidence814
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9177788
xref: http://identifiers.org/pubmed/8078902
comment: Heme O and heme A are specifically synthesised for the heme-copper respiratory oxidases. Mitochondrial protoheme IX farnesyltransferase (COX10) mediates the transformation of protoheme IX (heme) and farnesyl diphosphate (FAPP) to heme O (Glerum & Tzagoloff 1994). COX10 is highly expressed in muscle, heart and brain (Murakami et al. 1997).

Evidence817
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Porphyrins are heterocyclic macrocycles, consisting of four pyrrole subunits (tetrapyrrole) linked by four methine (=CH-) bridges. The extensive conjugated porphyrin macrocycle is chromatic and the name itself, porphyrin, is derived from the Greek word for purple. The aromatic character of porphyrins can be seen by NMR spectroscopy. Porphyrins readily combine with metals by coordinating them in the central cavity. Iron (heme) and magnesium (chlorophyll) are two well known examples although zinc, copper, nickel and cobalt form other known metal-containing phorphyrins. A porphyrin which has no metal in the cavity is called a free base. Some iron-containing porphyrins are called hemes (heme-containing proteins or hemoproteins) and these are found extensively in nature ie. hemoglobin. Hemoglobin is quantitatively the most important hemoprotein. The hemoglobin iron is the transfer site of oxygen and carries it in the blood all round the body for cell respiration. Other examples are cytochromes present in mitochondria and endoplasmic reticulum which takes part in electron transfer events, catalase and peroxidase whic protect the body against the oxidant hydrogen peroxide and tryptophan oxygenase which is present in intermediary metabolism. Hemoproteins are synthesized in all mammalian cells and the major sites are erythropoietic tissue and the liver. The processes by which heme is synthesized, transported, and metabolized are a critical part of human iron metabolism (Severance and Hamze 2009); here the core processes of heme biosynthesis and catabolism have been annotated.

Evidence816
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16839620
xref: http://identifiers.org/pubmed/10522552
comment: Eight enzymes are involved in heme biosynthesis, four each in the mitochondria and the cytosol. The process starts in the mitochondria with the condensation of succinyl CoA (from the TCA cycle) and glycine to form 5-aminolevulinate (ALA). The next four steps take place in the cytosol. Two molecules of ALA are condensed to form the monopyrrole porphobilinogen (PBG). The next two steps convert four molecules of PBG into the cyclic tetrapyrrole uroporphyringen III, which is then decarboxylated into coproporphyrinogen III. The last three steps occur in the mitochondria and involve modifications to the tetrapyrrole side chains and finally, insertion of iron. In addition to these synthetic steps, a spontaneous cytosolic reaction allows the formation of uroporphyringen I which is then enzymatically decarboxylated to coproporphyrinogen I, which cannot be metabolized further in humans. Also, lead can inactivate ALAD, the enzyme that catalyzes PBG synthesis, and ferrochelatase, the enzyme that catalyzes heme synthesis. The porphyrias are disorders that arise from defects in the enzymes of heme biosynthesis. Defective pathway enzymes after ALA synthase result in accumulated substrates which can cause either skin problems, neurological complications, or both due to their toxicity in higher concentrations. They are broadly classified as hepatic porphyrias or erythropoietic porphyrias, based on the site of the overproduction of the substrate. Each defect is described together with the reaction it affects.

Evidence818
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16872679
xref: http://identifiers.org/pubmed/16584116
xref: http://identifiers.org/pubmed/15102545
comment: A number of CYPs take part in cholesterol biosynthesis and elimination, thus playing an important role in maintaining cholesterol homeostasis. Under normal physiological conditions, cholesterol intake (diet or synthesized de novo from acetyl CoA) equals cholesterol elimination (degraded to bile salts, secreted in bile and used in steroid hormone synthesis). These processes are under tight regulatory control and any disruption leads to increased cholesterol levels resulting in cardiovacular disease. The CYPs involved in cholesterol homeostasis could serve as potential targets for cholesterol-lowering drugs.

Evidence819
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12369887
xref: http://identifiers.org/pubmed/16584116
xref: http://identifiers.org/pubmed/15102545
xref: http://identifiers.org/pubmed/15128046
comment: The P450 isozyme system is the major phase 1 biotransforming system in man, accounting for more than 90% of drug biotransformations. This system has huge catalytic versatility and a broad substrate specificity, acting upon xenobiotica and endogenous compounds. It is also called the mixed-function oxidase system, the P450 monooxygenases and the heme-thiolate protein system. All P450 enzymes are a group of heme-containing isozymes which are located on the membrane of the smooth endoplasmic reticulum. They can be found in all tissues of the human body but are most concentrated in the liver. The name "cytochrome P450" (CYP) is derived from the spectral absorbance maximum at 450nm when carbon monoxide binds to CYP in its reduced (ferrous, Fe2+) state. The basic reaction catalyzed by CYP is mono-oxygenation, that is the transfer of one oxygen atom from molecular oxygen to a substrate. The other oxygen atom is reduced to water during the reaction with the equivalents coming from the cofactor NADPH. The basic reaction is; RH (substrate) + O2 + NADPH + H+ = ROH (product) + H2O + NADP+ The end results of this reaction can be (N-)hydroxylation, epoxidation, heteroatom (N-, S-) oxygenation, heteroatom (N-, S-, O-) dealkylation, ester cleavage, isomerization, dehydrogenation, replacement by oxygen or even reduction under anaerobic conditions. The metabolites produced from these reactions can either be mere intermediates which have relatively little reactivity towards cellular sysytems and are readily conjugated, or, they can be disruptive to cellular systems. Indeed, inert compounds need to be prepared for conjugation and thus the formation of potentially reactive metabolites is in most cases unavoidable. There are 57 human CYPs (in 18 families and 42 subfamilies), mostly concentrated in the endoplasmic reticulum of liver cells although many tissues have them to some extent (Nelson DR et al, 2004). CYPs are grouped into 14 families according to their sequence similarity. General…

UniProt:Q10192
type: ProteinReference
xref: UnificationXref2036
organism: BioSource1

tRNA(Thr)
type: SmallMolecule
entity reference: CHEBI:29180
data source: Provenance1
xref: UnificationXref7213
xref: UnificationXref7214
cellular location: GO:0005759
comment: Reactome DB_ID: 379791

L-Threonine
type: SmallMolecule
entity reference: CHEBI:16857
data source: Provenance1
xref: UnificationXref7216
xref: UnificationXref7215
cellular location: GO:0005759
comment: Reactome DB_ID: 379706
display name: L-Thr

Thr-tRNA(Thr)
type: SmallMolecule
entity reference: CHEBI:29163
data source: Provenance1
xref: UnificationXref7217
xref: UnificationXref7218
cellular location: GO:0005759
comment: Reactome DB_ID: 379779

tRNA(Trp)
type: SmallMolecule
entity reference: CHEBI:29181
data source: Provenance1
xref: UnificationXref7223
xref: UnificationXref7222
cellular location: GO:0005759
comment: Reactome DB_ID: 379774

(S)-alpha-amino-beta-(3-indolyl)-propionic acid
type: SmallMolecule
entity reference: CHEBI:16828
data source: Provenance1
name: L-Tryptophan
xref: UnificationXref6252
xref: UnificationXref7224
cellular location: GO:0005759
comment: Reactome DB_ID: 379709
display name: L-Trp

Trp-tRNA(Trp)
type: SmallMolecule
entity reference: CHEBI:29159
data source: Provenance1
xref: UnificationXref7226
xref: UnificationXref7225
cellular location: GO:0005759
comment: Reactome DB_ID: 379759

Ser-tRNA(Ser)
type: SmallMolecule
entity reference: CHEBI:29162
data source: Provenance1
xref: UnificationXref7206
xref: UnificationXref7207
cellular location: GO:0005759
comment: Reactome DB_ID: 379777

Regulation of Lipid Metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha)
type: Pathway
data source: Provenance1
pathway component: REACT 131294.5
evidence: Evidence438
xref: UnificationXref2898
xref: UnificationXref2899
pathway order: PathwayStep429
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

L-serine
type: SmallMolecule
entity reference: CHEBI:17115
data source: Provenance1
xref: UnificationXref7204
xref: UnificationXref7205
cellular location: GO:0005759
comment: Reactome DB_ID: 379732
display name: L-Ser

tRNA(Ser)
type: SmallMolecule
entity reference: CHEBI:29179
data source: Provenance1
xref: UnificationXref7203
xref: UnificationXref7202
cellular location: GO:0005759
comment: Reactome DB_ID: 379761

Pro-tRNA(Pro)
type: SmallMolecule
entity reference: CHEBI:29154
data source: Provenance1
xref: UnificationXref7196
xref: UnificationXref7197
cellular location: GO:0005759
comment: Reactome DB_ID: 379745

Evidence802
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16702333
comment: The main sulfur amino acids are methionine, cysteine, homocysteine and taurine. Of these, the first two are proteinogenic. This group of reactions contains all processes that 1) break down sulfur amino acids, 2) interconvert between them, and 3) synthesize them from solved sulfide which comes from sulfate assimilation and reduction. Only plants and microorganisms employ all processes. Humans cannot de novo synthesize any sulfur amino acid, nor convert cysteine to methionine (Brosnan & Brosnan, 2006).

Evidence801
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/20162368
comment: While in humans excess methionine is converted to homocysteine, homocysteine and its transsulfuration product cysteine can be degraded to several end products, two of which, taurine and hydrogen sulfide, have uses in other biological processes (Stipanuk & Ueki 2011).

Evidence800
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/20162368
comment: While the human body is very economical with sulfur amino acids (SAA), superfluous SAA are degraded via cysteine to toxic hydrogen sulfide which must be dealt with. The pathway to oxidize this gas is localized to mitochondria and is highly conserved, pointing back to a time when life was immersed in sulfide-rich waters. The pathway for sulfide oxidation consists of five reactions, one of which, the sulfur transfer from thiosulfate to glutathione, is still to be characterized fully. A mutation in one enzyme has been identified that is associated with ethylmalonyl encephalopathy and where tissue sulfide is elevated (Stipanuk & Ueki 2011).

Evidence806
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11032841
xref: http://identifiers.org/pubmed/15381398
xref: http://identifiers.org/pubmed/10706561
xref: http://identifiers.org/pubmed/11032836
xref: http://identifiers.org/pubmed/7354072
comment: 5-Aminolevulinic acid dehydratase (ALAD aka porphobilinogen synthase, PBGS), catalyzes the asymmetric condensation of two molecules of ALA to form porphobilinogen (PBG). The substrate that becomes the acetyl side chain-containing half of PBG is called A-side ALA; the half that becomes the propionyl side chains and the pyrrole nitrogen is called P-ALA (Jaffe 2004). PBG is the first pyrrole formed, the precursor to all tetrapyrrole pigments such as heme and chlorophyll. There are at least eight bonds that are made or broken during this reaction. The active form of the ALAD enzyme is an octamer complexed with eight Zn2+ ions, four that are strongly bound and four that are weakly bound. The four weakly bound ones are dispensible for enzyme activity in vitro (Bevan et al. 1980; Mitchell et al. 2001). Deficiencies of ALAD enzyme in vivo are associated with 5-aminolevulinate dehydratase-deficient porphyria (e.g., Akagi et al. 2000).

Evidence805
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11032836
comment: Lead binds to ALAD enzyme displacing half the zinc ions essential for its catalytic activity and inactivating it. Lead is a major environmental toxin and this enzyme is one of its principal molecular targets (Jaffe et al. 2001).

Evidence804
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1939222
xref: http://identifiers.org/pubmed/16121195
comment: The committed step for porphyrin synthesis is the formation of 5-aminolevulinate (ALA) by condensation of glycine (from the general amino acid pool) and succinyl-CoA (from the TCA cycle), in the mitochondrial matrix. The reaction is catalyzed by two different ALA synthases, one expressed ubiquitously (ALAS1) and the other only expressed in erythroid precursors (ALAS2). Both enzymes are expressed as homodimers and require pyridoxal 5-phosphate as a cofactor. No disease-causing mutations of ALAS1 have been recognised in humans. Mutations in ALAS2 cause X-linked sideroblastic anaemia (XLSA), characterised by a microcytic hypochromic anaemia.

Evidence803
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: This group of reactions is responsible for: 1) the breakdown of amino acids; 2) the synthesis of urea from ammonia and amino groups generated by amino acid breakdown; 3) the synthesis of the ten amino acids that are not essential components of the human diet; and 4) the synthesis of related nitrogen-containing molecules including carnitine and creatine. Transport of these molecuels across lipid bilayer membranes is annotated separately as part of the module on "transmembrane transport of small molecules".

Evidence809
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/6822570
xref: http://identifiers.org/pubmed/8644733
xref: http://identifiers.org/pubmed/9564029
comment: Cytosolic uroporphyrinogen decarboxylase (UROD) catalyzes the sequntial removal of four carboxylic groups from the acetic acid side chains of uroporphyrinogen III (URO3) to form coproporphyrinogen III (COPRO3) (de Verneuil et al. 1983). Human UROD is a dimer (Whitby et al. 1998). Heterogenous and homogenous deficiencies of UROD are associated with porphyria cutanea tarda and hepatoerythropoietic porphyria respectively in vivo (Moran-Jiminez et al. 1996).

Evidence807
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12773194
xref: http://identifiers.org/pubmed/7354069
comment: Cytosolic porphobilinogen deaminase catalyzes the polymerization of four molecules of porphobilinogen (PBG) to generate hydroxymethylbilane (HMB), an unstable tetrapyrrole. This reaction is the first step in the formation of the tetrapyrrole macrocycle. Two isoforms of porphobilinogen deaminase are generated by alternative splicing, one expresssed in erythroid tissues and one ubiquitously expressed in the body. Deficiencies of both forms of PBG deaminase are associated with acute intermittent porphyria.

Evidence808
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7592565
xref: http://identifiers.org/pubmed/3805019
comment: Cytosolic uroporphyrinogen III synthase (URO3S) catalyzes the conversion of HMB (hydroxymethylbilane) to uroporphyrinogen III, a reaction involving ring closure and intramolecular rearrangement. Uroporphyrinogen III represents a branch point for the pathways leading to formation of heme, chlorophyll and corrins. HMB is rapidly converted from a linear tetrapyrrole to the cyclic form. Deficiencies of URO3S in vivo are associated with congenital erythropoietic porphyria.

Met-tRNA(Met)
type: SmallMolecule
entity reference: CHEBI:16635
data source: Provenance1
xref: UnificationXref7178
xref: UnificationXref7177
cellular location: GO:0005759
comment: Reactome DB_ID: 379780

L-Phenylalanine
type: SmallMolecule
entity reference: CHEBI:17295
data source: Provenance1
name: (S)-alpha-amino-beta-phenylpropionic acid
xref: UnificationXref3853
xref: UnificationXref7183
cellular location: GO:0005759
comment: Reactome DB_ID: 379701
display name: L-Phe

L-Methionine
type: SmallMolecule
entity reference: CHEBI:16643
data source: Provenance1
xref: UnificationXref5170
xref: UnificationXref7172
cellular location: GO:0005759
comment: Reactome DB_ID: 379705
display name: L-Met

tRNA(Met)
type: SmallMolecule
entity reference: CHEBI:29173
data source: Provenance1
xref: UnificationXref7175
xref: UnificationXref7174
cellular location: GO:0005759
comment: Reactome DB_ID: 379741

tRNA(Pro)
type: SmallMolecule
entity reference: CHEBI:29177
data source: Provenance1
xref: UnificationXref7194
xref: UnificationXref7193
cellular location: GO:0005759
comment: Reactome DB_ID: 379775

tRNA(Phe)
type: SmallMolecule
entity reference: CHEBI:29184
data source: Provenance1
xref: UnificationXref7184
xref: UnificationXref7185
cellular location: GO:0005759
comment: Reactome DB_ID: 379760

Phe-tRNA(Phe)
type: SmallMolecule
entity reference: CHEBI:29153
data source: Provenance1
xref: UnificationXref7186
xref: UnificationXref7187
cellular location: GO:0005759
comment: Reactome DB_ID: 379789

http://identifiers.org/pubmed/16413920
type: PublicationXref
id: 16413920
author: Nimmerjahn, F
author: Ravetch, JV
db: Pubmed
title: Fcgamma receptors: old friends and new family members
source: Immunity 24:19-28
year: 2006

Evidence829
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7646467
comment: In the second step in the formation of glutathione, gamma-glutamylcysteine ligates with glycine to form glutathione (Gali and Board, 1995; ).

Evidence821
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16788062
comment: ACSS1 (acyl-CoA synthetase short-chain family member 1) in the mitochondrial matrix catalyzes the reaction of acetate, coenzyme A, and ATP to form acetyl-CoA, AMP, and pyrophosphate (Schwer et al. 2006).

Evidence822
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10631996
xref: http://identifiers.org/pubmed/224930
comment: ALDH1A1 (aldehyde dehydrogenase) in the cytosol catalyzes the reaction of acetaldehyde and NAD+ to form acetate and NADH + H+ (Inoue et al. 1979). The active form of the enzyme is a tetramer (Ni et al. 1999).

Evidence823
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17567461
xref: http://identifiers.org/pubmed/224930
xref: http://identifiers.org/pubmed/3893466
xref: http://identifiers.org/pubmed/9982
xref: http://identifiers.org/pubmed/2729894
xref: http://identifiers.org/pubmed/10441588
xref: http://identifiers.org/pubmed/18110463
comment: Ethanol and related alcohols can be ingested as part of the diet and are formed by microorganisms in the intestinal tract. Ethanol oxidation to acetate occurs primarily in liver cells in a multistep process first described by Racker (1949). First, in the cytosol, ethanol is oxidized to acetaldehyde, with the formation of NADH. Second, in the mitochondrion, acetaldehyde is oxidized to acetate with the formation of NADH. Finally, acetate in the mitochondrion can be condensed with coenzyme A to form acetyl CoA. Polymorphisms in the enzymes catalyzing the first two steps are associated with variation in the efficiency of alcohol catabolism in human populations (Chen et al. 1999; Lange et al. 1976; Jornvall 1985). The molecular mechanism by which cytosolic acetaldehyde enters the mitochondrial matrix is not known (Lemasters 2007). Cytosolic enzymes capable of oxidizing acetaldehyde to acetate have also been identified and characterized in vitro (Inoue et al. 1979) so a purely cytosolic pathway for ethanol oxidation to acetate and conversion to acetyl-CoA can be annotated. The role of this pathway in vivo is unclear, though limited attempts to correlate deficiencies in the cytosolic enzyme with alcohol intolerance have yielded suggestive data (Yoshida et al. 1989). Additional peroxisomal and microsomal pathways for the oxidation of ethanol to acetaldehyde have been described; their physiological significance is unclear and they are not annotated here.

Evidence824
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12369887
xref: http://identifiers.org/pubmed/16584116
xref: PublicationXref1327
xref: http://identifiers.org/pubmed/17125408
comment: Phase 1 of metabolism is concerned with functionalization, that is the introduction or exposure of functional groups on the chemical structure of a compound. This provides a 'handle' for phase 2 conjugating species with which to react with. Many xenobiotics are lipophilic and almost chemically inert (e.g. PAHs) so would not necessarily undergo a phase 2 reaction. Making them more chemically reactive would facilitate their excretion but also increases their chance of reacting with cellular macromolecules (e.g. proteins, DNA). There is a fine balance between producing a more reactive metabolite and conjugation reactions. There are two groups of enzymes in phase 1 - oxidoreductases and hydrolases. Oxidoreductases introduce an oxygen atom into or remove electrons from their substrates. The major oxidoreductase enzyme system is called the P450 monooxygenases. Other systems include flavin-containing monooxygenases (FMO), cyclooxygenases (COX) and monoamine oxidases (MAO). Hydrolases hydrolyse esters, amides, epoxides and glucuronides.

Evidence825
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17482904
comment: Glucose 1-phosphate and UTP are the precursors to UDP-glucuronate formation. After oxidation of the resultant complex, UDP-glucuronate is transported to the ER lumen.

RNA Polymerase I, RNA Polymerase III, and Mitochondrial Transcription
type: Pathway
data source: Provenance1
pathway component: REACT 95034.9
pathway component: REACT 158722.3
evidence: Evidence139
xref: UnificationXref729
xref: UnificationXref730
pathway order: PathwayStep127
pathway order: PathwayStep137
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Evidence826
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10836148
xref: http://identifiers.org/pubmed/14977861
xref: PublicationXref1332
comment: Glucuronidation conjugation utilizes UDP-glucuronosyltransferases (UGTs; EC 2.4.1.17) to catalyze a wide range of diverse endogenous and xenobiotic compounds. Glucuronidation is the major pathway in phase II metabolism and accounts for approximately 35% of drug conjugation. UGTs are microsomal membrane-bound and catalyze the transfer of a glucuronate group of uridine diphosphoglucuronate (UDPGA, a co-substrate) to the functional group of specific substrates. UDPGA is synthesized from glucose-1-phosphate (G1P). G1P is required for glycolysis and is present in high concentrations in the cell, making it is unlikely to be a limiting factor in UDPGA synthesis. UDP is added to G1P to form UDP-glucose which is then dehydrogenated to form UDPGA. The basic reaction is UDP-Glucuronate + acceptor -> UDP + acceptor-beta-D-glucuronide The effect of this conjugation is to confer polarity to the substrate which can then be easily excreted in urine or bile. Functional groups acted on include hydroxyl, carboxylate, amino and sulfate groups. There are 2 families of UGTs, UGT1 and UGT2 which are further sub-divided into 3 subfamilies, UGT1A, UGT2A and UGT2B. There are more than 26 different isozymes in humans, of which 18 are functional proteins. They are composed of 527-530 residues and have a molecular weight of 50-57KDa. The UGT1 family comprises of 9 proteins (UGT1A1, 1A3-1A10) but only 5 have been isolated in humans. Example substrates which are glucuronidated are acetaminophen by UGT1A6 and bilirubin by UGT1A1. Members of the UGT2 subfamily are each encoded by their own genes, in contrast to UGT1As which are encoded at the UGT1 locus. Example substrates are morphine conjugation by UGT2B7 and androgenic steroid conjugation by UGT2B17. Xenobiotics conjugated with glucuronic acid can be substrates for beta-glucuronidase, an enzyme common in gut microflora. This enzyme can release the parent or phase I metabolite which can be reabsorbed. It can then either re-exert it's original eff…

Evidence827
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8968737
comment: Dihydroxybenzoate is a typical substrate for Catechol O-methyltransferase

Evidence828
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15130560
xref: http://identifiers.org/pubmed/10331075
xref: http://identifiers.org/pubmed/10898761
xref: PublicationXref1332
comment: Methylation is a common but minor pathway of Phase II conjugation compared to glucuronidation or sulfonation. The cofactor used in methylation conjugation is S-adenosylmethionine (SAM). SAM is the second most widely used enzyme substrate after ATP and is involved in a wide range of important biological processes. SAM is sythesized from methionine's reaction with ATP, catalyzed by methionine adenosyltransferase (MAT). There are two genes, MAT1A and MAT2A, which encode for two homologous MAT catalytic subunits, 1 and 2. During conjugation with nucleophilic substrates, the methyl group attached to the sulfonium ion of SAM is transferred to the substrate forming the conjugate. SAM, having lost the methyl moiety, is converted to S-adenosylhomocysteine (SAH). SAH can be hydrolyzed to form adenosine and homocysteine. Homocysteine can either be converted to glutathione or methylated to form methionine, thus forming the starting point for SAM synthesis and completing the cycle. Fuctional groups attacked are phenols, catechols, aliphatic and aromatic amines and sulfhydryl-containing groups. The enzymes that catalyze the transfer of the methyl group to these functional groups are the methyltransferases (MT). MTs are small, cytosolic, monomeric enzymes that utilize SAM as a methyl donor. There are many MTs but the best studied ones are named on the basis of their prototypical substrates: COMT (catechol O-methyltransferase), TPMT (thiopurine methyltransferase), TMT (thiol methyltransferase), HNMT (histamine N-methyltransferase) and NNMT (nicotinamide N-methyltransferase). An example of each enzyme mentioned is given. In each case, a typical substrate for the enzyme is shown.

http://identifiers.org/pubmed/11779870
type: PublicationXref
id: 11779870
author: Tsurumi, T
author: Fujita, M
author: Kiyono, T
author: Nakamura, H
author: Ishimi, Y
db: Pubmed
title: Nuclear organization of DNA replication initiation proteins in mammalian cells.
source: J Biol Chem 277:10354-61
year: 2002

Evidence820
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10631996
xref: http://identifiers.org/pubmed/4065146
xref: http://identifiers.org/pubmed/18196
comment: ALDH2 (aldehyde dehydrogenase) in the mitochondrial matrix catalyzes the reaction of acetaldehyde and NAD+ to form acetate and NADH + H+ (Greenfield and Pietruszko 1977; Hempel et al. 1985). The active form of the enzyme is a tetramer (Ni et al. 1999).

http://identifiers.org/pubmed/12205100
type: PublicationXref
id: 12205100
author: Van Komen, S
author: Sigurdsson, S
author: Petukhova, G
author: Sung, P
db: Pubmed
title: Homologous DNA pairing by human recombination factors Rad51 and Rad54
source: J Biol Chem 277:42790-4
year: 2002

http://identifiers.org/pubmed/9564029
type: PublicationXref
id: 9564029
author: Kushner, JP
author: Phillips, JD
author: Hill, CP
author: Whitby, FG
db: Pubmed
title: Crystal structure of human uroporphyrinogen decarboxylase
source: EMBO J 17:2463-71
year: 1998

http://identifiers.org/pubmed/3413114
type: PublicationXref
id: 3413114
author: Cram, LS
author: Wu, JR
author: Ratliff, RL
author: Buckingham, JM
author: Moyzis, RK
author: Jones, MD
author: Meyne, J
author: Deaven, LL
author: Dani, M
db: Pubmed
title: A highly conserved repetitive DNA sequence, (TTAGGG)n, present at the telomeres of human chromosomes
source: Proc Natl Acad Sci U S A 85:6622-6
year: 1988

http://identifiers.org/pubmed/11130078
type: PublicationXref
id: 11130078
author: Sato, S
author: Takeda, K
author: Wagner, H
author: Sanjo, H
author: Takeuchi, O
author: Hoshino, K
author: Matsumoto, M
author: Kaisho, T
author: Kawai, T
author: Hemmi, H
author: Akira, S
db: Pubmed
title: A Toll-like receptor recognizes bacterial DNA
source: Nature 408:740-5
year: 2000

Evidence834
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref1327
comment: All organisms are constantly exposed to foreign chemicals every day. These can be man-made (drugs, industrial chemicals) or natural (alkaloids, toxins from plants and animals). Uptake is usually via ingestion but inhalation and transdermal routes are also common. The very nature of many chemicals that make them suitable for uptake by these routes, in other words their lipophilicty (favours fat solubility) is also the main reason organisms have developed mechanisms that convert them to hydrophilic (favours water solubility) compounds which are readily excreted via bile and urine. Otherwise, lipophilic chemicals would accumulate in the body and overwhelm defense mechanisms. This process is called biotransformation and is catalyzed by enzymes mainly in the liver of higher organisms but a number of other organs have considerable ability to process xenobiotica such as kidneys, gut and lungs. As well as xenobiotics, many endogenous compounds are commonly eliminated by this process. This mechanism is of ancient origin and a major factor for its development in animals is plants. Most animals are plant eaters and thus are subject to a huge variety of chemical compounds which plants produce to stop themselves being eaten. This complex set of enzymes have several features which make them ideal for biotransformation; (1) metabolites of the parent chemical are usually made more water soluble so it favours rapid excretion via bile and urine (2) the enzymes possess broad and overlapping specificity to be able to deal with newly exposed chemicals (3) metabolites of the parent generally don't have adverse biological effects. In the real world however, all these criteria have exceptions. Many chemicals are transformed into reactive metabolites. In pharmacology, the metabolites of some parent drugs exert the desired pharmacological effect but in the case of polycyclic aromatic hydrocarbons (PAHs), which can undergo epoxidation, it results in the formation of an electrophile which can …

Evidence835
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: As inferred from biochemical studies in yeast and phenotypic studies in mouse, Mitoferrin-1 (SLC25A37) and Mitoferrin-2 (SLC25A28) transport ferrous iron across the inner mitochondrial membrane. Mitoferrin-1 is essential for maintaining mitochondrial iron uptake in developing erythroid cells; mitoferrin-2 is ubiquitously expressed. Defects in Mitoferrin-1 and Mitoferrin-2 cause a reduction in mitochondrial iron acquisition and biogenesis of iron-sulfur clusters and heme.

Evidence832
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref1332
comment: Glutathione S-Transferases (GSTs; EC 2.5.1.18) are another major set of phase II conjugation enzymes. They can be found in the cytosol as well as being microsomal membrane-bound. Cytosolic GSTs are encoded by at least 5 gene families (alpha, mu, pi, theta and zeta GST) whereas membrane-bound enzymes are encoded by single genes. Soluble GSTs are homo- or hetero-dimeric enzymes (approximately 25KDa subunits) which can act on a wide range of endogenous and exogenous electrophiles. GSTs mediate conjugation using glutathione (GSH), a tripeptide synthesized from its precursor amino acids gamma-glutamate, cysteine and glycine. A generalized reaction is RX + GSH -> HX + GSR Glutathione conjugates are excreted in bile and converted to cysteine and mercapturic acid conjugates in the intestine and kidneys. GSH is the major, low molecular weight, non-protein thiol synthesized de novo in mammalian cells. As well as taking part in conjugation reactions, GSH also has antioxidant ability and can metabolize endogenous and exogenous compounds. The nucleophilic GSH attacks the electrophilic substrate forming a thioether bond between the cysteine residue of GSH and the electrophile. The result is generally a less reactive and more water-soluble conjugate that can be easily excreted. In some cases, GSTs can activate compounds to reactive species such as certain haloalkanes and haloalkenes. Substrates for GSTs include epoxides, alkenes and compounds with electrophilic carbon, sulfur or nitrogen centres. There are two types of conjugation reaction with glutathione: displacement reactions where glutathione displaces an electron-withdrawing group and addition reactions where glutathione is added to activated double bond structures or strained ring systems.

Evidence833
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11805192
xref: PublicationXref1332
comment: Phase II of biotransformation is concerned with conjugation, that is using groups from cofactors to react with functional groups present or introduced from phase I on the compound. The enzymes involved are a set of transferases which perform the transfer of the cofactor group to the substrate. The resultant conjugation results in greatly increasing the excretory potential of compounds. Although most conjugations result in pharmacological inactivation or detoxification, some can result in bioactivation. Most of the phase II enzymes are located in the cytosol except UDP-glucuronosyltransferases (UGT), which are microsomal. Phase II reactions are typically much faster than phase I reactions therefore the rate-limiting step for biotransformation of a compound is usually the phase I reaction. Phase II metabolism can deal with all the products of phase I metabolism, be they reactive (Type I substrate) or unreactive/poorly active (Type II substrate) compounds. With the exception of glutathione, the conjugating species needs to be made chemically reactive after synthesis. The availability of the cofactor in the synthesis may be a rate-limiting factor in some phase II pathways as it may prevent the formation of enough conjugating species to deal with the substrate or it's metabolite. As many substrates and/or their metabolites are chemically reactive, their continued presence may lead to toxicity.

Evidence838
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10899784
xref: http://identifiers.org/pubmed/22101253
xref: http://identifiers.org/pubmed/7050653
xref: http://identifiers.org/pubmed/20547883
comment: NADPH, ferredoxin reductase (FDXR, Adrenodoxin reductase), and ferredoxins (FDX1, FDX1L) comprise a short electron transport chain that provides electrons for biosynthesis of iron-sulfur clusters and steroid hormones (Sheftel et al. 2010, Shi et al. 2012, reviewed in Grinberg et al. 2000, Lambeth et al. 1982).

Evidence839
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19675643
xref: http://identifiers.org/pubmed/20873749
xref: http://identifiers.org/pubmed/22609301
xref: http://identifiers.org/pubmed/19021507
xref: http://identifiers.org/pubmed/22382365
xref: http://identifiers.org/pubmed/20522547
xref: http://identifiers.org/pubmed/20060739
comment: Iron-sulfur (Fe-S) proteins are localized in the cytosol, nucleus, and mitochondria of mammalian cells (reviewed in Stemmler et al. 2010, Rouault 2012, Bandyopadhyay et al. 2008, Lill 2009, Lill et al. 2012). Fe-S protein biogenesis in the mitochondrial matrix involves the iron-sulfur cluster (ISC) assembly machinery. Ferrous iron is transported across the inner mitochondrial membrane into the mitochondrial matrix by Mitoferrin-1 and Mitoferrin-2. (Mitoferrin-1 is enriched in erythroid cells while Mitoferrin-2 is ubiquitous.) Frataxin binds ferrous iron in the mitochondrial matrix. The cysteine desulfurase NFS1 in a subcomplex with ISD11 provides the sulfur by converting cyteine into alanine and forming a persulfide which is used for cluster formation on ISCU, the scaffold protein. Interaction between NFS1 and ISD11 is necessary for desulfurase activity. Frataxin binds to a complex containing NFS1, ISD11, and ISCU and is proposed to function as an iron donor to ISCU or as an allosteric switch that activates sulfur transfer and Fe-S cluster assembly (Tsai and Barondeau 2010). Cluster formation also involves the electron transfer chain ferredoxin reductase and ferredoxin. ISCU initially forms clusters containing 2 iron atoms and 2 sulfur atoms ([2Fe-2S] clusters). They are released by the function of HSP70-HSC20 chaperones and the monothiol glutaredoxin GLRX5 and used for assembly of [2Fe-2S] proteins. Assembly of larger clusters such as [4Fe-4S] clusters may involve the function of ISCA1, ISCA2, and IBA57. The clusters are transferred to apo-enzymes such as the respiratory complexes, aconitase, and lipoate synthase through dedicated targeting factors such as IND1, NFU1, and BOLA3.

Evidence836
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12785837
xref: http://identifiers.org/pubmed/20873749
xref: http://identifiers.org/pubmed/15509595
xref: http://identifiers.org/pubmed/11823441
xref: http://identifiers.org/pubmed/20522547
xref: http://identifiers.org/pubmed/18425540
xref: http://identifiers.org/pubmed/21776984
xref: http://identifiers.org/pubmed/21298097
comment: Frataxin (FXN) specifically binds 2 atoms of ferrous iron per monomer (reviewed in Stemmler et al. 2010). Iron bound to Frataxin may (Yoon and Cowan 2003, Gerber et al. 2003) or may not (Schmucker et al. 2011) enhance the interaction of Frataxin with NFS1, ICSU, and ISD11. Frataxin was shown to stimulate the cysteine desulfurase activity of NFS1 and was proposed to be a regulator of sulfur production (Tsai et al. 2010). The formation of sulfide by NFS1 is most efficiently observed when NFS1 is in complex with ISD11, ISCU, and FXN in the presence of cysteine and iron. This means that only the complete system of NFS1, ISD11, ISCU, FXN, cysteine, and iron is fully active as a desulfurase. FXN therefore seems to be a regulator of the cysteine desulfurase permitting sulfide production only when all components needed for Fe-S cluster synthesis are present and the ISCU-bound Fe-S cluster can be formed.

Evidence837
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1567230
comment: Two electrons and one proton are transferred from NADPH to the FAD moiety of ferredoxin reductase. A proton from the medium is also taken up by ferredoxin reductase.

Evidence830
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19463
xref: http://identifiers.org/pubmed/18357469
xref: http://identifiers.org/pubmed/2573352
comment: Extracellular glutathione can be hydrolyzed to give cysteinylglycine (Cys-Gly) and gamma glutamate, which, in the presence of amino acids, can form a gamma-glutamate:AA product (Heisterkamp et al, 2008). This hydrolysis provides cells with a cysteine supply and contributes to the maintainance of intracellular glutathione levels (Tate and Ross, 1977; Pawlak et al, 1989).

Evidence831
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3053703
comment: The combination of glutamate, cysteine and ATP is required to form glutathione. The steps involved in the synthesis and recycling of glutathione are outlined (Meister, 1988).

Evidence847
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: The capping enzyme binds the 5'-end of the nascent transcript soon after it is synthesized on the DNA template, and results in the formation of the capping complex along with the C-terminal domain of RNA polymerase II, and Spt5.

Evidence848
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9512541
comment: After the capping complex is formed, the RNA triphosphatase activity of the capping enzyme hydrolyzes the 5'-end phosphate group of the nascent mRNA transcript to a diphosphate. The RNA triphosphatase (RTP) domain of mammalian capping enzyme is a member of a superfamily of phosphatases that include the protein tyrosine phosphatases, some lipid phosphatases, and several nucleic acid phosphatases. This family uses a conserved nucleophilic cysteine residue to attack the target phosphate. A transient phospho-cysteinyl enzyme intermediate is then hydrolyzed to regenerate the enzyme active site. It should be noted that while higher eukaryotic capping enzymes use PTP-like triphosphatase domains, the yeast triphosphatases are a completely different class of enzymes. The yeast RTPs are metal-dependent phosphatases. RNA 5'-triphosphatase (RTP) catalyzed first reaction can be represented as:pppN(pN)n + GTP -> ppN(pN)n + Pi; (n=20-25)

Evidence849
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9512541
comment: A highly conserved lysine within the guanylyltransferase (GT) site of the mRNA capping enzyme attacks the alpha-phosphate of GTP. An enzyme-GMP covalent intermediate is formed.

Evidence843
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/20802492
xref: http://identifiers.org/pubmed/18625724
comment: Cytosolic Fe/S protein biogenesis depends on the electron transfer chain from NAD(P)H to the Fe/S protein (CIAPIN1 in humans, DRE2 in yeast) via the flavoprotein NDOR1 (TAH18 in yeast). The precise role of electrons in the assembly process is unclear but in the absence of the electron chain the stable [4Fe-4S] cluster of NUBP1 is not assembled. CIAPIN1 binds two Fe/S clusters of the [2Fe-2S] and the [4Fe-4S] type. The [2Fe-2S] cluster is reduced by NDOR1-NADPH.

Evidence844
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18573874
comment: A [4Fe-4S] cluster is assembled on a scaffold composed of the P-loop NTPases NUBP2 (CFD1 in yeast) and NUBP1 (Nbp35 in yeast) in a nucleotide-dependent fashion. The two proteins form a heterotetramer which transiently binds the [4Fe-4S] cluster in a bridged form between two subunits of the complex. The Fe/S cluster is bound to two highly conserved Cys residues in the C-termini of each of these proteins. NUBP1 contains an additional, stably associated [4Fe-4S] cluster at its N-terminus which is essential for function. Mitochondria play a crucial role in cytosolic and nuclear Fe/S protein biogenesis. They export via a mitochondrial ABC transporter (yeast ATM1, human ABCB7) a still unknown, sulfur-containing compound which is essential for Fe/S cluster assembly in the cytosol. The general cytosolic iron donor, the multi-domain monothiol glutaredoxin (human GRX3 or PICOT, yeast Grx3-Grx4) plays a crucial role in cytosolic-nuclear Fe/S protein biogenesis. The precise molecular function of the glutaredoxin is still unclear.

Evidence845
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/22609301
xref: http://identifiers.org/pubmed/20522543
xref: http://identifiers.org/pubmed/22382365
xref: http://identifiers.org/pubmed/16824008
comment: Iron-sulfur clusters containing 4 atoms of iron and 4 atoms of sulfur (4Fe-4S clusters) are assembled in the cytosol on a heterotetrameric scaffold composed of NUBP2 and NUBP1 subunits (reviewed in Lill et al. 2012, Rouault et al. 2012, Sharma et al. 2010, Lill and Mühlenhoff 2006). The sources of iron and sulfur are uncertain but the process requires a sulfur-containing compound exported from mitochondria via ABCB7 (ABC7). Newly synthesized 4Fe-4S are transferred to apoproteins such as XPD and POLD1 via the CIA targeting complex, composed of NARFL, CIAO1, FAM96B, and MMS19.

Evidence846
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Metabolic processes in human cells generate energy through the oxidation of molecules consumed in the diet and mediate the synthesis of diverse essential molecules not taken in the diet as well as the inactivation and elimination of toxic ones generated endogenously or present in the extracellular environment. The processes of energy metabolism can be classified into two groups according to whether they involve carbohydrate-derived or lipid-derived molecules, and within each group it is useful to distinguish processes that mediate the breakdown and oxidation of these molecules to yield energy from ones that mediate their synthesis and storage as internal energy reserves. Synthetic reactions are conveniently grouped by the chemical nature of the end products, such as nucleotides, amino acids and related molecules, and porphyrins. Detoxification reactions (biological oxidations) are likewise conveniently classified by the chemical nature of the toxin. At the same time, all of these processes are tightly integrated. Intermediates in reactions of energy generation are starting materials for biosyntheses of amino acids and other compounds, broad-specificity oxidoreductase enzymes can be involved in both detoxification reactions and biosyntheses, and hormone-mediated signaling processes function to coordinate the operation of energy-generating and energy-storing reactions and to couple these to other biosynthetic processes.

Evidence840
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1383219
comment: Cytosolic GUK1 (guanylate kinase 1) catalyzes the reaction of carbovir monophosphate and ATP to form carbovir diphosphate and ADP. The activity of human GUK1 is inferred from that of the corresponding pig protein (Miller et al. 1992).

Evidence841
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18479171
comment: Abacavir activation proceeds steps of phosphorylation, deamination to yield carbovir monophosphate, and phosphorylation of the latter compound to yield the triphosphate. In addition, abacavir can be conjugated with glucuronide or oxidized to its 5'-carboxylate derivative, the two major forms in which it is excreted from the body (Yuen et al. 2008).

Evidence842
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18479171
comment: Abacavir is a nucleoside analogue reverse transcriptase inhibitor with antiretroviral activity, widely used in combination with other drugs to treat HIV-1 infection (Yuen et al. 2008). Its uptake across the plasma membrane is mediated by organic cation transporters SLC22A1, 2, and 3; the transport proteins ABCB1 and ABCG2 mediate its efflux. Abacavir itself is a prodrug. Activation requires phosphorylation by a cytosolic adenosine phosphotransferase and deamination by ADAL deaminase to yield carbovir monophosphate. Cytosolic nucleotide kinases convert carbovir monophosphate to carbovir triphosphate, the active HIV reverse transcriptase inhibitor. Abacavir can be glucuronidated or oxidized to a 5'-carboxylate; these are the major forms in which it is excreted from the body.

(R)-2-hydroxyglutaric acid
type: SmallMoleculeReference
name: (R)-2-Hydroxyglutarate
name: ChEBI:32796 (R)-2-hydroxyglutaric acid
xref: UnificationXref3997

http://identifiers.org/pubmed/3208766
type: PublicationXref
id: 3208766
author: Day, IN
author: Fothergill, JE
author: McAleese, SM
author: Hinks, LJ
author: Dunbar, B
db: Pubmed
title: Complete amino acid sequence of the neurone-specific gamma isozyme of enolase (NSE) from human brain and comparison with the non-neuronal alpha form (NNE)
source: Eur J Biochem 178:413-7
year: 1988

Evidence858
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: At the beginning of this reaction, 1 molecule of 'dsRNA duplex', and 1 molecule of 'ADAR2 homodimer' are present. At the end of this reaction, 1 molecule of 'Editosome (ADAR2) complex' is present. This reaction takes place in the 'nucleus'.

Evidence859
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: It is still unclear how ADAR 1 and ADAR 2 proteins form the editosomes with the target RNA. Other components of these editosomes for A to I editing are unknown.

Evidence856
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: At the beginning of this reaction, 1 molecule of 'dsRNA duplex', and 1 molecule of 'ADAR1 homodimer ' are present. At the end of this reaction, 1 molecule of 'Editosome (ADAR1) complex' is present. This reaction takes place in the 'nucleus'.

Evidence857
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: At the beginning of this reaction, 2 molecules of 'ADAR2 protein' is present. At the end of this reaction, 1 molecule of 'ADAR2 homodimer' is present. This reaction takes place in the 'nucleus'.

Evidence854
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11017188
xref: http://identifiers.org/pubmed/11909521
xref: http://identifiers.org/pubmed/3326038
xref: http://identifiers.org/pubmed/10395561
comment: The 5'-ends of all eukaryotic pre-mRNAs studied thus far are converted to cap structures. The cap is thought to influence splicing of the first intron, and is bound by 'cap-binding' proteins, CBP80 and CBP20, in the nucleus. The cap is important for translation initiation, and it also interacts with the poly(A)terminus, via proteins, resulting in circularization of the mRNA to facilitate multiple rounds of translation. The cap is also important for mRNA stability, protecting it from 5' to 3' nucleases, and is required for mRNA export to the cytoplasm. The capping reaction usually occurs very rapidly on nascent transcripts; after the synthesis of only a few nucleotides by RNA polymerase II. The capping reaction involves the conversion of the 5'-end of the nascent transcript from a triphosphate to a diphosphate by a RNA 5'-triphosphatase, followed by the addition of a guanosine monophosphate by the mRNA guanylyltransferase, to form a 5'-5'-triphosphate linkage. This cap is then methylated by 2'-O-methyltransferases.

Evidence855
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: At the beginning of this reaction, 2 molecules of 'ADAR1 protein' is present. At the end of this reaction, 1 molecule of 'ADAR1 homodimer ' is present. This reaction takes place in the 'nucleus'.

http://identifiers.org/pubmed/20930137
type: PublicationXref
id: 20930137
author: Kull, FJ
author: Endow, SA
author: Liu, H
db: Pubmed
title: Kinesins at a glance
source: J Cell Sci 123:3420-4
year: 2010

Evidence852
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: The cap binding complex binds to the methylated GMP cap on the nascent mRNA transcript.

Evidence853
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: At the beginning of this reaction, 1 molecule of 'CBP80', and 1 molecule of 'CBP20' are present. At the end of this reaction, 1 molecule of 'Cap Binding Complex (CBC)' is present. This reaction takes place in the 'nucleus'.

Evidence850
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9512541
comment: The diphosphate 5'-end of the mRNA is joined to the GMP, releasing it from the enzyme. At this time, it is unclear how the RNA diphosphate end is transferred from the active site of the triphosphatase to the guanylyltransferase site. The covalent enzyme-GMP complex can form in the absence of RNA. Guanylyltransferase (GT) catalyzed second reaction can be represented as:ppN(pN)n + GTP -> GpppN(pN)n + PPi

Evidence851
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: GMP capped mRNA transcript dissociates from GT for further modification.

http://identifiers.org/pubmed/19540337
type: PublicationXref
id: 19540337
author: Masson, K
author: Rönnstrand, L
db: Pubmed
title: Oncogenic signaling from the hematopoietic growth factor receptors c-Kit and Flt3
source: Cell Signal 21:1717-26
year: 2009

http://identifiers.org/pubmed/9083101
type: PublicationXref
id: 9083101
author: Hosaka, K
author: Nikawa, J
author: Nakashima, A
db: Pubmed
title: Cloning of a human cDNA for CTP-phosphoethanolamine cytidylyltransferase by complementation in vivo of a yeast mutant
source: J Biol Chem 272:9567-72
year: 1997

Evidence860
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: At the beginning of this reaction, 1 molecule of 'Editosome (ADAR1) complex', and 1 molecule of 'H2O' are present. At the end of this reaction, 1 molecule of 'A to I edited RNA:Editosome (ADAR1) complex', and 1 molecule of 'NH3' are present. This reaction takes place in the 'nucleus' and is mediated by the 'double-stranded RNA adenosine deaminase activity' of 'ADAR1 homodimer '.

Evidence862
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7565688
xref: http://identifiers.org/pubmed/9111310
comment: Hydrolytic deamination of adenosine leads to inosine. Ammonia is presumed to be released during this reaction.

Evidence861
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: At the beginning of this reaction, 1 molecule of 'H2O', and 1 molecule of 'Editosome (ADAR2) complex' are present. At the end of this reaction, 1 molecule of 'NH3', and 1 molecule of 'A to I edited RNA:Editosome (ADAR2) complex' are present. This reaction takes place in the 'nucleus' and is mediated by the 'double-stranded RNA adenosine deaminase activity' of 'ADAR2 homodimer'.

Evidence864
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12139607
xref: http://identifiers.org/pubmed/11092837
comment: After transcription, some RNA molecules are altered to contain bases not encoded in the genome. Most often this involves the editing or modification of one base to another, but in some organisms can involve the insertion or deletion of a base. Such editing events alter the coding properties of mRNA. RNA editing can be generally defined as the co- or post transcriptional modification of the primary sequence of RNA from that encoded in the genome through nucleotide deletion, insertion, or base modification mechanisms. There are two pathways of RNA editing: the substitution/conversion pathway and the insertion/deletion pathway. The insertion/deletion editing occurs in protozoans like Trypanosoma, Leishmania; in slime molds like Physarum spp., and in some viral categories like paramyxoviruses, Ebola virus etc. To date, the substitution/conversion pathway has been observed in human along with other mammals, Drosophila, and some plants. The RNA editing processes are known to create diversity in proteins involved in various pathways like lipid transport, metabolism etc. and may act as potential targets for therapeutic intervention (Smith et al., 1997). The reaction mechanisms of cytidine and adenosine deaminases is represented below. In both these reactions, NH3 is presumed to be released:

Evidence863
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1747369
xref: http://identifiers.org/pubmed/11406411
xref: http://identifiers.org/pubmed/8943218
xref: http://identifiers.org/pubmed/12446660
xref: http://identifiers.org/pubmed/12045112
comment: In humans the deamination of adenosines to inosines is the most common editing event. It is particularly prevalent in the brain, where it leads to amino acid changes that affect the conductance of several ion channels. Inosines are recognized by the translation machinery as if they were guanosines. ADARs (Adenosine Deaminases Acting on RNA) modify pre-mRNA, acting as single peptides and recognize structural determinants in the RNA. To date 3 members of this deaminase family are known: ADAR 1, ADAR 2, and ADAR 3 that share a common modular domain structure. ADAR 1 and 2 contain a catalytic deaminase domain, a double-stranded RNA binding domain and exhibit RNA editing activity. ADAR1 activity is found in various mammalian tissues with the highest concentration in brain. An increasing number of mammalian genes have been found to undergo deamination by ADARs. Deamination by editing in pre-mRNAs encoding subunits of ionotropic glutamate receptors (GluRs) is another well studied example. An editing event at the Q/R site of the GluR2 (GluRB) subunit of AMPA ââ¬âreceptors converts a Gln codon CAG to an Arg codon CIG rendering the heteromeric receptor impermeable to Ca 2+ ions. Another example is the editing of 5-HT2C subtype serotonin receptor mRNA resulting in receptor isoforms with reduced G-protein coupling efficiency (reviewed by Gerber and Keller, 2001). In mice, the editosomes with ADAR proteins require some cis-acting elements like an intronic 'editing-site complementary sequence (ECS)'. Although evolutionarily conserved, the actual role of ECS is not yet elucidated in humans. The editing complex can be generally represented as:

Evidence866
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: At the beginning of this reaction, 1 molecule of 'ATAC B Complex' is present. At the end of this reaction, 1 molecule of 'U4 ATAC snRNP', and 1 molecule of 'ATAC C Complex' are present. This reaction takes place in the 'nucleus'.

Evidence865
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: The U4atac/U6atac enters the spliceosome and U6atac snRNA forms base pairing interactions with the 5' ss and also forms base pairing interactions with U12 and U4atac is partially displaced. U5 snRNP, the only snRNP common to both the major and minor splicing pathways, also joins the spliceosome to form the B complex and interacts with nucleotides within the 3' end of the exon flanking the 5' ss.

Evidence868
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: At the beginning of this reaction, 1 molecule of 'ATAC C Complex with lariat containing 5'-end cleaved mRNA' is present. At the end of this reaction, 1 molecule of 'U6 ATAC snRNP', 1 molecule of 'post exon ligation complex', 1 molecule of 'U12 snRNP', 1 molecule of 'U11 snRNP', and 1 molecule of 'U5 snRNP' are present. This reaction takes place in the 'nucleus'.

Evidence867
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: At the beginning of this reaction, 1 molecule of 'ATAC C Complex' is present. At the end of this reaction, 1 molecule of 'ATAC C Complex with lariat containing 5'-end cleaved mRNA' is present. This reaction takes place in the 'nucleus'.

Evidence869
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10207048
xref: http://identifiers.org/pubmed/9149533
comment: The splicing of a subset of pre-mRNA introns occurs by a second pathway, designated the AT-AC or U12-dependent splicing pathway. AT-AC introns have highly conserved, non-canonical splice sites that are removed by the AT-AC spliceosome, which contains distinct snRNAs (U11, U12, U4atac, U6atac) that are structurally and functionally analogous to the major spliceosome. U5 snRNA as well as many of the protein factors appear to be conserved between the two spliceosomes.

Evidence871
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Co-transcriptional pre-mRNA splicing is not obligatory. Pre-mRNA splicing begins co-transcriptionally and often continues post-transcriptionally. Human genes contain an average of nine introns per gene, which cannot serve as splicing substrates until both 5' and 3' ends of each intron are synthesized. Thus the time that it takes for pol II to synthesize each intron defines a minimal time and distance along the gene in which splicing factors can be recruited. The time that it takes for pol II to reach the end of the gene defines the maximal time in which splicing could occur co-transcriptionally. Thus, the kinetics of transcription can affect the kinetics of splicing.Any covalent change in a primary (nascent) mRNA transcript is mRNA Processing. For successful gene expression, the primary mRNA transcript needs to be converted to a mature mRNA prior to its translation into polypeptide. Eucaryotic mRNAs undergo a series of complex processing reactions; these begin on nascent transcripts as soon as a few ribonucleotides have been synthesized during transcription by RNA Polymerase II, through the export of the mature mRNA to the cytoplasm, and culminate with mRNA turnover in the cytoplasm.

Evidence870
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12226669
comment: The process in which excision of introns from the primary transcript of messenger RNA (mRNA) is followed by ligation of the two exon termini exposed by removal of each intron, is called mRNA splicing. Most of the mRNA is spliced by the major pathway, involving the U1, U2, U4, U5 and U6 snRNPs. A minor fraction, about 1 %, of the mRNAs are spliced via the U12 dependent pathway.

Evidence875
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15837794
xref: http://identifiers.org/pubmed/16937364
xref: http://identifiers.org/pubmed/11460167
xref: http://identifiers.org/pubmed/9851932
xref: http://identifiers.org/pubmed/8177321
xref: http://identifiers.org/pubmed/13130464
comment: C-Jun NH2 terminal kinases (JNKs) are an evolutionarily conserved family of serine/threonine protein kinases, that belong to mitogen activated protein kinase family (MAPKs - also known as stress-activated protein kinases, SAPKs). The JNK pathway is activated by heat shock, or inflammatory cytokines, or UV radiation. The JNKs are encoded by at least three genes: JNK1/SAPK-gamma, JNK2/SAPK-alpha and JNK3/ SAPK-beta. The first two are ubiquitously expressed, whereas the JNK3 protein is found mainly in brain and to a lesser extent in heart and testes. As a result of alternative gene splicing all cells express distinct active forms of JNK from 46 to 55 kDa in size. Sequence alignment of these different products shows homologies of >80%. In spite of this similarity, the multiple JNK isoforms differ in their ability to bind and phosphorylate different target proteins, thus leading to the distinctive cellular processes: induction of apoptosis, or enhancment of cell survival, or proliferation. Activation of JNKs is mediated by activated TAK1 which phosphorylates two dual specificity enzymes MKK4 (MAPK kinase 4) and MKK7(MAPK kinase 7).

Evidence874
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12193592
xref: http://identifiers.org/pubmed/9195981
xref: http://identifiers.org/pubmed/13130464
comment: c-Jun NH2 terminal kinase (JNK) plays a role in conveying signals from the cytosol to the nucleus, where they associate and activate their target transcription factors.

Evidence873
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11062067
xref: http://identifiers.org/pubmed/9162092
xref: http://identifiers.org/pubmed/18713996
xref: http://identifiers.org/pubmed/17875933
xref: http://identifiers.org/pubmed/16186825
xref: http://identifiers.org/pubmed/13130464
comment: Activated human JNK kinases (MKK4 and MKK7) phosphorylate Thr183 and Tyr185 residues in the characteristic Thr-Pro-Tyr phosphoacceptor loop of each JNK. JNK is differentially regulated by MKK4 and MKK7 depending on the stimulus. MKK7 is the primary activator of JNK in TNF, LPS, and PGN responses. However, TLR3 cascade requires both MKK4 and MKK7. Some studies reported that in three JNK isoforms tested MKK4 shows a striking preference for the tyrosine residue (Tyr-185), and MKK7 a striking preference for the threonine residue (Thr-183).

Evidence872
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Processing of mRNA encompasses the capping of mRNA, processing of mRNAs with and without introns, and also modification of mRNA, as in mRNA editing.

Evidence879
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15564374
xref: http://identifiers.org/pubmed/9069263
xref: http://identifiers.org/pubmed/19167516
xref: http://identifiers.org/pubmed/7622446
comment: Activator protein-1 (AP-1) is a collective term referring to a group of transcription factors that bind to promoters of target genes in a sequence-specific manner. AP-1 family consists of hetero- and homodimers of bZIP (basic region leucine zipper) proteins, mainly of Jun-Jun, Jun-Fos or Jun-ATF. AP-1 members are involved in the regulation of a number of cellular processes including cell growth, proliferation, survival, apoptosis, differentiation, cell migration. The ability of a single transcription factor to determine a cell fate critically depends on the relative abundance of AP-1 subunits, the composition of AP-1 dimers, the quality of stimulus, the cell type, the co-factor assembly. AP-1 activity is regulated on multiple levels; transcriptional, translational and post-translational control mechanisms contribute to the balanced production of AP-1 proteins and their functions. Briefly, regulation occurs through: effects on jun, fos, atf gene transcription and mRNA turnover. AP-1 protein members turnover. post-translational modifications of AP-1 proteins that modulate their transactivation potential (effect of protein kinases or phosphatases). interactions with other transcription factors that can either induce or interfere with AP-1 activity.

Evidence878
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10878576
comment: At the beginning of this reaction, 1 molecule of 'ATP', and 1 molecule of 'ATF-2' are present. At the end of this reaction, 1 molecule of 'ADP', and 1 molecule of 'ATF-2-P' are present. This reaction is mediated by the 'protein kinase activity' of 'MAPK1-P'.

Evidence877
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15837794
xref: http://identifiers.org/pubmed/10878576
xref: http://identifiers.org/pubmed/8622669
xref: http://identifiers.org/pubmed/8533096
comment: p38 mitogen-activated protein kinase (MAPK) belongs to a highly conserved family of serine/threonine protein kinases. The p38 MAPK-dependent signaling cascade is activated by pro-inflammatory or stressful stimuli such as ultraviolet radiation, oxidative injury, heat shock, cytokines, and other pro-inflammatory stimuli. p38 MAPK exists as four isoforms (alpha, beta, gamma, and delta). Of these, p38alpha and p38beta are ubiquitously expressed while p38gamma and p38delta are differentially expressed depending on tissue type. Each isoform is activated by upstream kinases including MAP kinase kinases (MKK) 3, 4, and 6, which in turn are phosphorylated by activated TAK1 at the typical Ser-Xaa-Ala-Xaa-Thr motif in their activation loops. Once p38 MAPK is phosphorylated it activates numerous downstream substrates, including MAPK-activated protein kinase-2 and 3 (MAPKAPK-2 or 3) and mitogen and stress-activated kinase-1/2 (MSK1/2). MAPKAPK-2/3 and MSK1/2 function to phosphorylate heat shock protein 27 (HSP27) and cAMP-response element binding protein transcriptional factor, respectively. Other transcription factors, including activating transcription factor 2, Elk, CHOP/GADD153, and myocyte enhancer factor 2, are known to be regulated by these kinases.

Evidence876
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9768359
xref: http://identifiers.org/pubmed/7535770
comment: The p38 activators MKK3 and MKK6 were present in both the nucleus and the cytoplasm, consistent with a role in activating p38 in the nucleus.

UniProt:Q12381
type: ProteinReference
xref: UnificationXref5710
organism: BioSource1

Evidence884
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7851425
comment: GABA is converted to succinate semialdehyde by 4-aminobutyrate aminotransferase

Evidence883
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15583024
comment: Active steroid hormones are produced from the precursor cholesterol.The steps involved in the biosynthesis of the adrenal steroid hormones, corticosterone, cortisol, and aldosterone; and the gonadal steroid hormones, progesterone, estradiol, and testosterone are annotated here. The enzymes that catalyze these reactions fall into two major classes of proteins: the cytochrome P450 heme-containing proteins and the hydroxysteroid dehydrogenases.

Evidence886
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16787421
xref: http://identifiers.org/pubmed/19428801
comment: GABA is a major inhibitory neurotransmitter in the mammalian central nervous system. GABA modulates neuronal excitability throughout the nervous system. Disruption of GABA neurotransmission leads to many neurological diseases including epilepsy and a general anxiety disorder. GABA is synthesized by two distinct enzymes GAD67 and GAD65 that differ in their cellular localization, functional properties and co-factor requirements. GABA synthesized by GAD65 is used for neurotransmission whereas GABA synthesized by GAD67 is used for processes other than neurotransmission such as synaptogenesis and protection against neuronal injury. GABA is loaded into synaptic vesicle with the help of vesicular inhibitory amino acid transporter or VGAT. GAD65 and VGAT are functionally linked at the synaptic vesicle membrane and GABA synthesized by GAD65 is preferentially loaded into the synaptic vesicle over GABA synthesized in cytoplasm by GAD67.The GABA loaded synaptic vesicles are docked at the plasma membrane with the help of the SNARE complexes and primed by interplay between various proteins including Munc18, complexin etc. Release of GABA loaded synaptic vesicle is initiated by the arrival of action potential at the presynaptic bouton and opening of N or P/Q voltage gated Ca2+ channels. Ca2+ influx results in Ca2+ binding by synaptobrevin, which is a part of the SNARE complex that also includes SNAP25 and syntaxin, leading to synaptic vesicle fusion. Release of GABA in the synaptic cleft leads to binding of GABA by the GABA receptors and post ligand binding events.

Evidence885
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19172412
comment: GABA is metabolized to succinated by the serial action of two enzymes, 4-aminobutyrate aminotransferase and suucinate semialdehyde dehydrogenase.

Evidence880
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12471242
xref: http://identifiers.org/pubmed/19767751
xref: http://identifiers.org/pubmed/17637696
xref: http://identifiers.org/pubmed/16393692
xref: http://identifiers.org/pubmed/17158707
comment: MAPKs are protein kinases that, once activated, phosphorylate their specific cytosolic or nuclear substrates at serine and/or threonine residues. Such phosphorylation events can either positively or negatively regulate substrate, and thus entire signaling cascade activity. The major cytosolic target of activated ERKs are RSKs (90 kDa Ribosomal protein S6 Kinase). Active RSKs translocates to the nucleus and phosphorylates such factors as c-Fos(on Ser362), SRF (Serum Response Factor) at Ser103, and CREB (Cyclic AMP Response Element-Binding protein) at Ser133. In the nucleus activated ERKs phosphorylate many other targets such as MSKs (Mitogen- and Stress-activated protein kinases), MNK (MAP interacting kinase) and Elk1 (on Serine383 and Serine389). ERK can directly phosphorylate CREB and also AP-1 components c-Jun and c-Fos. Another important target of ERK is NF-KappaB. Recent studies reveals that nuclear pore proteins are direct substrates for ERK (Kosako H et al, 2009). Other ERK nuclear targets include c-Myc, HSF1 (Heat-Shock Factor-1), STAT1/3 (Signal Transducer and Activator of Transcription-1/3), and many more transcription factors. Activated p38 MAPK is able to phosphorylate a variety of substrates, including transcription factors STAT1, p53, ATF2 (Activating transcription factor 2), MEF2 (Myocyte enhancer factor-2), protein kinases MSK1, MNK, MAPKAPK2/3, death/survival molecules (Bcl2, caspases), and cell cycle control factors (cyclin D1). JNK, once activated, phosphorylates a range of nuclear substrates, including transcription factors Jun, ATF, Elk1, p53, STAT1/3 and many other factors. JNK has also been shown to directly phosphorylate many nuclear hormone receptors. For example, peroxisome proliferator-activated receptor 1 (PPAR-1) and retinoic acid receptors RXR and RAR are substrates for JNK. Other JNK targets are heterogeneous nuclear ribonucleoprotein K (hnRNP-K) and the Pol I-specific transcription factor TIF-IA, which regulates ribosome synthesis. Oth…

Evidence882
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19112497
xref: http://identifiers.org/pubmed/19675569
xref: http://identifiers.org/pubmed/12609980
comment: In human, together with ubiquitin-conjugating E2-type enzymes UBC13 and UEV1A (also known as UBE2V1), TRAF6 catalyses Lys63-linked ubiquitination. It is believed that auto polyubiquitination and oligomerization of TRAF6 is followed by binding the ubiquitin receptors of TAB2 or TAB3 (TAK1 binding protein 2 and 3), which stimulates phosphorylation and activation of TGF beta-activated kinase 1(TAK1). TAK1 phosphorylates IKK alpha and IKK beta, which in turn phosphorylate NF-kB inhibitors - IkB and eventually results in IkB degradation and NF-kB translocation to the nucleus. Also TAK1 mediates JNK and p38 MAP kinases activation by phosphorylating MKK4/7 and MKK3/6 respectivly resulting in the activation of many transcription factors. The role of TRAF6 is somewhat controversial and probably cell type specific. TRAF6 autoubiquitination was found to be dispensable for TRAF6 function to activate TAK1 pathway. These findings are consistent with the new mechanism of TRAF6-mediated NF-kB activation that was suggested by Xia et al. (2009). TRAF6 generates unanchored Lys63-linked polyubiquitin chains that bind to the regulatory subunits of TAK1 (TAB2 or TAB3) and IKK(NEMO), leading to the activation of the kinases. Xia et al. (2009) demonstrated in vitro that unlike polyubiquitin chains covalently attached to TRAF6 or IRAK, TAB2 and NEMO-associated ubiquitin chains were found to be unanchored and susceptible to N-terminal ubiquitin cleavage. Only K63-linked polyubiquitin chains, but not monomeric ubiquitin, activated TAK1 in a dose-dependent manner. Optimal activation of the IKK complex was achieved using ubiquitin polymers containing both K48 and K63 linkages. Furthermore, the authors proposed that the TAK1 complexes might be brougt in close proximity by binding several TAB2/3 to a single polyubiquitin chain to facilitate TAK1 kinase trans-phosphorylation. Alternativly, the possibility that polyUb binding promotes allosteric activation of TAK1 complex should be considered (Wals…

Evidence881
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19196711
xref: http://identifiers.org/pubmed/11242034
xref: http://identifiers.org/pubmed/17637696
xref: http://identifiers.org/pubmed/11861597
comment: The mitogen activated protein kinase (MAPK) cascade, one of the most ancient and evolutionarily conserved signaling pathways, is involved in many processes of immune responses. The MAP kinases cascade transduces signals from the cell membrane to the nucleus in response to a wide range of stimuli (Chang and Karin, 2001; Johnson et al, 2002). There are three major groups of MAP kinases the extracellular signal-regulated protein kinases ERK1/2, the p38 MAP kinase and the c-Jun NH-terminal kinases JNK. ERK1 and ERK2 are activated in response to growth stimuli. Both JNKs and p38-MAPK are activated in response to a variety of cellular and environmental stresses. The MAP kinases are activated by dual phosphorylation of Thr and Tyr within the tripeptide motif Thr-Xaa-Tyr. The sequence of this tripeptide motif is different in each group of MAP kinases: ERK (Thr-Glu-Tyr); p38 (Thr-Gly-Tyr); and JNK (Thr-Pro-Tyr). MAPK activation is mediated by signal transduction in the conserved three-tiered kinase cascade: MAPKKKK (MAP4K or MKKKK or MAPKKK Kinase) activates the MAPKKK. The MAPKKKs then phosphorylates a dual-specificity protein kinase MAPKK, which in turn phosphorylates the MAPK. The dual specificity MAP kinase kinases (MAPKK or MKK) differ for each group of MAPK. The ERK MAP kinases are activated by the MKK1 and MKK2; the p38 MAP kinases are activated by MKK3, MKK4, and MKK6; and the JNK pathway is activated by MKK4 and MKK7. The ability of MAP kinase kinases (MKKs, or MEKs) to recognize their cognate MAPKs is facilitated by a short docking motif (the D-site) in the MKK N-terminus, which binds to a complementary region on the MAPK. MAPKs then recognize many of their targets using the same strategy, because many MAPK substrates also contain D-sites. The upstream signaling events in the TLR cascade that initiate and mediate the ERK signaling pathway remain unclear.

http://identifiers.org/pubmed/10958654
type: PublicationXref
id: 10958654
author: Vincent, MF
author: Marie, S
author: Van den Berghe, G
author: Race, V
db: Pubmed
title: Clinical, biochemical and molecular genetic correlations in adenylosuccinate lyase deficiency
source: Hum Mol Genet 9:2159-2165
year: 2000

Evidence888
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Dopamine in the cytosol is metabolized to 3-methoxytyramine by catecholamine o-methyltransferase (COMT), which uses s-adenosylmethionine as a methyl group donor.

Evidence887
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17880890
xref: http://identifiers.org/pubmed/16865347
xref: http://identifiers.org/pubmed/15217342
xref: http://identifiers.org/pubmed/16819626
comment: Neurotransmitter is stored in the synaptic vesicle in the pre-synaptic terminal prior to its release in the synaptic cleft upon depolarization of the pre-synaptic membrane. The release of the neurotransmitter is a multi-step process that is controlled by electrical signals passing through the axons in form of action potential. Neurotransmitters include glutamate, acetylcholine, nor-epinephrine, dopamine and seratonin. Each of the neurotransmitter cycle is independently described.

Evidence889
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17185601
comment: Dopamine once taken up by the dopamine transporter from the extracellular space into the cytosol is metabolized in a two step reaction to homovanillic acid.The first reaction is catalyzed by catecholamine o-methyl transferase and the subsequent reaction is catalyzed by monoamine oxidase A.

http://identifiers.org/pubmed/19767751
type: PublicationXref
id: 19767751
author: Kosako, H
author: Hattori, S
author: Taniguchi, H
author: Kose, S
author: Ushiyama, M
author: Nishida, E
author: Imamoto, N
author: Aranami, C
author: Yamaguchi, N
db: Pubmed
title: Phosphoproteomics reveals new ERK MAP kinase targets and links ERK to nucleoporin-mediated nuclear transport
source: Nat Struct Mol Biol 16:1026-35
year: 2009

Evidence897
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: In astrocytic glutamate-glutamine cycle, the excess glutamate released by the pre-synaptic neuron in the synaptic cleft is transported into the astrocyte by a family glutamate transporters called the excitatory amino acid transporters 1 and 2, EAAT1 and EAAT2. Astrocytes carrying these transporters exist in close apposition to the synapse to clear excess glutamate to prevent excessive activation of neurons and hence neuronal death. Glutamate in astrocytes is converted to glutamine by glutamine synthetase. Glutamine is then transported into the extracellular space by system N transporters. The glutamate in the extracellular space is available for neuronal uptake.

Evidence896
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Neurotransmitter released in the synaptic cleft binds to specific receptors on the post-synaptic cell and the excess of the neurotransmitter is cleared to prevent over activation of the post-synaptic cell. The neurotransmitter is cleared by either re-uptake by the pre-synaptic neuron, diffusion in the perisynaptic area, uptake by astrocytes surrounding the synaptic cleft or enzymatic degradation of the neurotransmitter. This topic will be annotated in a future release.

Evidence895
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Serotonergic neurotransmission affects a wide range of behaviors, from food intake and reproductive activity, to sensory processing and motor activity, to cognition and emotion. One such key regulator is the serotonin transporter (5-HTT), which is observed to remove serotonin released into the synaptic cleft.

Evidence894
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Serotonin is first metabolized to 5-hydroxyindole acetaldehyde by monoamine oxidase. 5-hydroxyindole acetaldehyde is then catalyzed by aldehyde dehydrogenase to form 5-hydroxyindole acetic acid.

Evidence893
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17010132
xref: http://identifiers.org/pubmed/8778744
comment: 5-hydroxyindole acetaldehyde is then catalyzed by aldehyde dehydrogenase to form 5-hydroxyindole acetic acid

Evidence892
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: The human gene SLC6A3 encodes the sodium-dependent dopamine transporter, DAT which mediates the re-uptake of dopamine from the synaptic cleft (Vandenbergh DJ et al, 2000). Dopamine can then be degraded by either COMT or monoamine oxidase.

Evidence891
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Alternately dopamine is metabolized to homovanillic acid in a two-step reaction in which dopamine is first oxidized to 3,4-dihydroxypheylacetic acid (DOPAC) and then converted to homovanillic acid by catecholamine o-methyltransferase.

Evidence890
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: 3,4-dihydroxyphenylacetic acid, generated after oxidation of dopamine by monoamineoxidase, is methylated by catecholamine o-methyltransferase to homovanillic acid.

http://identifiers.org/pubmed/12151002
type: PublicationXref
id: 12151002
author: Paiement, J
author: Desjardins, M
author: Bergeron, JJ
author: Cameron, PH
author: Duclos, S
author: Chevet, E
author: Gagnon, E
author: Steele-Mortimer, O
author: Rondeau, C
db: Pubmed
title: Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages
source: Cell 110:119-31
year: 2002

Evidence899
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref1428
comment: Chemical synapses are specialized junctions that are used for communication between neurons, neurons and muscle or gland cells. The synapse involves a pre-synaptic neuron and a post-synaptic neuron, muscle cell or glad cell. The pre and the post-synaptic cell are separated by a gap of 20nm called the synaptic cleft. The signals pass in a unidirection from pre-synaptic to post-synaptic. The pre-synaptic neuron communicates via the release of neurotransmitter which bind the receptors on the post-synaptic cell.

Evidence898
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Neuotransmitter uptake by astrocytes is mediated by specific transporter located on the astrocytic membrane. The imported neurotransmitter in the astrocytes is metabolized and transported back to the neuron via specialized transporters.

UnificationXref6316
type: UnificationXref
id: 428040
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428040

UnificationXref6317
type: UnificationXref
id: REACT_19520
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19520.1

UnificationXref6314
type: UnificationXref
id: 427984
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=427984

UnificationXref6315
type: UnificationXref
id: REACT_20346
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20346.1

UnificationXref6318
type: UnificationXref
id: 428003
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428003

UnificationXref6319
type: UnificationXref
id: REACT_20464
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20464.1

UnificationXref6312
type: UnificationXref
id: 427971
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=427971

UnificationXref6313
type: UnificationXref
id: REACT_19476
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19476.1

UnificationXref6310
type: UnificationXref
id: 427988
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=427988

UnificationXref6311
type: UnificationXref
id: REACT_20219
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20219.1

UnificationXref6325
type: UnificationXref
id: REACT_153144
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_153144.3

http://identifiers.org/pubmed/1717476
type: PublicationXref
id: 1717476
author: Hunter, T
author: Pines, J
db: Pubmed
title: Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport
source: J Cell Biol 115:1-17
year: 1991

UnificationXref6326
type: UnificationXref
id: 3665471
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665471

UnificationXref6327
type: UnificationXref
id: REACT_143218
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_143218.5

UnificationXref6328
type: UnificationXref
id: 3665466
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665466

UnificationXref6329
type: UnificationXref
id: REACT_98077
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_98077.9

UniProt:Q10208
type: ProteinReference
xref: UnificationXref2312
organism: BioSource1

UnificationXref6320
type: UnificationXref
id: GO:0005765
db: GENE ONTOLOGY

UnificationXref6321
type: UnificationXref
id: 3662632
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662632

UnificationXref6322
type: UnificationXref
id: 3662633
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662633

UnificationXref6323
type: UnificationXref
id: 3662634
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662634

UnificationXref6324
type: UnificationXref
id: 3662636
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662636

http://identifiers.org/pubmed/11347887
type: PublicationXref
id: 11347887
author: Hou, YM
author: King, MP
author: Davidson, E
author: Vitseva, O
author: Caffarella, J
db: Pubmed
title: Isolation of two cDNAs encoding functional human cytoplasmic cysteinyl-tRNA synthetase
source: Biol Chem 382:399-406
year: 2001

UnificationXref6338
type: UnificationXref
id: REACT_2577
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2577.2

UnificationXref6339
type: UnificationXref
id: CHEBI:42820
db: ChEBI

UnificationXref6336
type: UnificationXref
id: CHEBI:16737
db: ChEBI

UnificationXref6337
type: UnificationXref
id: 30733
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=30733

UnificationXref6334
type: UnificationXref
id: 446602
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=446602

UnificationXref6335
type: UnificationXref
id: REACT_21065
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21065.2

UnificationXref6332
type: UnificationXref
id: REACT_21137
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21137.2

UnificationXref6333
type: UnificationXref
id: CHEBI:3699
db: ChEBI

UnificationXref6330
type: UnificationXref
id: CHEBI:641
db: ChEBI

UnificationXref6331
type: UnificationXref
id: 446590
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=446590

http://identifiers.org/pubmed/10413847
type: PublicationXref
id: 10413847
author: Bläker, M
author: de Weerth, A
author: von Schrenck, T
db: Pubmed
title: [Receptors for cholecystokinin and gastrin]
source: Z Gastroenterol 37:389-401
year: 1999

UniProt:Q10205
type: ProteinReference
xref: UnificationXref1580
organism: BioSource1

UniProt:Q9C1X2
type: ProteinReference
xref: UnificationXref4000
organism: BioSource1

UniProt:P18296
type: ProteinReference
xref: UnificationXref7783
organism: BioSource1

UnificationXref6347
type: UnificationXref
id: REACT_21015
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21015.1

UnificationXref6348
type: UnificationXref
id: CHEBI:46020
db: ChEBI

UnificationXref6349
type: UnificationXref
id: 446599
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=446599

UnificationXref6343
type: UnificationXref
id: 446606
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=446606

UnificationXref6344
type: UnificationXref
id: REACT_21207
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21207.2

UnificationXref6345
type: UnificationXref
id: CHEBI:8428
db: ChEBI

UnificationXref6346
type: UnificationXref
id: 446598
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=446598

UnificationXref6340
type: UnificationXref
id: 446594
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=446594

UnificationXref6341
type: UnificationXref
id: REACT_21154
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21154.2

UnificationXref6342
type: UnificationXref
id: CHEBI:6801
db: ChEBI

http://identifiers.org/pubmed/19196647
type: PublicationXref
id: 19196647
author: McCrea, HJ
author: De Camilli, P
db: Pubmed
title: Mutations in phosphoinositide metabolizing enzymes and human disease
source: Physiology (Bethesda) 24:8-16
year: 2009

http://identifiers.org/pubmed/7962183
type: PublicationXref
id: 7962183
author: Tang, CJ
author: Chao, YJ
author: Tang, TK
author: Wu, CW
db: Pubmed
title: Nuclear mitotic apparatus protein (NuMA): spindle association, nuclear targeting and differential subcellular localization of various NuMA isoforms
source: J Cell Sci 107:1389-402
year: 1994

UniProt:Q9C1W5
type: ProteinReference
xref: UnificationXref8457
organism: BioSource1

UniProt:Q9C1W3
type: ProteinReference
xref: UnificationXref3002
organism: BioSource1

Fibroblast Growth Factor Receptor (FGFR) signaling
type: Pathway
data source: Provenance1
pathway component: p-ERK dimerizes
pathway component: REACT 114342.8
evidence: Evidence197
xref: UnificationXref1060
xref: RelationshipXref77
xref: UnificationXref1059
pathway order: PathwayStep194
pathway order: PathwayStep193
display name: Signaling by FGFR
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Regulation of gene expression in beta cells
type: Pathway
data source: Provenance1
pathway component: TemplateReaction35
pathway component: TemplateReaction5
evidence: Evidence1404
xref: RelationshipXref1108
xref: UnificationXref8702
xref: UnificationXref8701
pathway order: PathwayStep1377
pathway order: PathwayStep572
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/17637696
type: PublicationXref
id: 17637696
author: Gerondakis, S
author: Banerjee, A
db: Pubmed
title: Coordinating TLR-activated signaling pathways in cells of the immune system
source: Immunol Cell Biol 85:420-4
year: 2007

http://identifiers.org/pubmed/21029861
type: PublicationXref
id: 21029861
author: Hogg, JR
author: Goff, SP
db: Pubmed
title: Upf1 senses 3'UTR length to potentiate mRNA decay
source: Cell 143:379-89
year: 2010

http://identifiers.org/pubmed/11278511
type: PublicationXref
id: 11278511
author: Ding, WC
author: Berger, SH
author: Lebioda, L
author: Koli, S
author: Minor, W
author: Dunlap, RB
author: Phan, J
author: Steadman, DJ
db: Pubmed
title: Structure of human thymidylate synthase suggests advantages of chemotherapy with noncompetitive inhibitors
source: J Biol Chem 276:14170-7
year: 2001

Transport of vitamins, nucleosides, and related molecules
type: Pathway
data source: Provenance1
pathway component: REACT 143408.5
pathway component: BiochemicalReaction576
evidence: Evidence984
xref: UnificationXref6463
xref: UnificationXref6464
pathway order: PathwayStep963
pathway order: PathwayStep968
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/16143825
type: PublicationXref
id: 16143825
author: Briere, JJ
author: El Ghouzzi, V
author: Djouadi, F
author: Favier, J
author: Gimenez, AP
author: Benit, P
author: Rustin, P
db: Pubmed
title: Succinate dehydrogenase deficiency in human
source: Cell Mol Life Sci 62:2317â2324
year: 2005

UnificationXref6300
type: UnificationXref
id: 427993
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=427993

UnificationXref6302
type: UnificationXref
id: 428002
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428002

UnificationXref6301
type: UnificationXref
id: REACT_20456
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20456.2

UnificationXref6308
type: UnificationXref
id: 427960
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=427960

UnificationXref6307
type: UnificationXref
id: REACT_20460
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20460.2

UnificationXref6309
type: UnificationXref
id: REACT_19707
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19707.2

UnificationXref6304
type: UnificationXref
id: 427991
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=427991

UnificationXref6303
type: UnificationXref
id: REACT_20001
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20001.2

http://identifiers.org/pubmed/10536157
type: PublicationXref
id: 10536157
author: Wu, X
author: Zhang, Y
author: Xin, H
author: Lin, W
author: Yuan, F
db: Pubmed
title: The human REV1 gene codes for a DNA template-dependent dCMP transferase.
source: Nucleic Acids Res 27:4468-75
year: 1999

UnificationXref6306
type: UnificationXref
id: 427967
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=427967

UnificationXref6305
type: UnificationXref
id: REACT_20064
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20064.2

http://identifiers.org/pubmed/12947387
type: PublicationXref
id: 12947387
author: Valerie, K
author: Povirk, LF
db: Pubmed
title: Regulation and mechanisms of mammalian double-strand break repair.
source: Oncogene 22:5792-812
year: 2003

http://identifiers.org/pubmed/16483568
type: PublicationXref
id: 16483568
author: Da Silva, CA
author: Frossard, N
author: Reber, L
db: Pubmed
title: Stem cell factor and its receptor c-Kit as targets for inflammatory diseases
source: Eur J Pharmacol 533:327-40
year: 2006

(GlcNAc)2 (Man)8a
type: SmallMolecule
entity reference: CHEBI:60627
data source: Provenance1
xref: UnificationXref8322
xref: UnificationXref8323
cellular location: GO:0005829
comment: Reactome DB_ID: 1022112

Dolichyl phosphate
type: SmallMolecule
entity reference: dolichyl phosphate [ChEBI:16214]
data source: Provenance1
name: Dolichol phosphate
xref: UnificationXref8314
xref: UnificationXref8315
cellular location: GO:0044322
comment: Reactome DB_ID: 912287
display name: DOLP

http://identifiers.org/pubmed/13115431
type: PublicationXref
id: 13115431
author: Lieberman, I
author: Kornberg, A
db: Pubmed
title: Enzymic synthesis and breakdown of a pyrimidine, orotic acid. I. Dihydro-orotic dehydrogenase
source: Biochim Biophys Acta 12:223-234
year: 1953

(Glc)1 (GlcNAc)2 (Man)9
type: SmallMolecule
entity reference: CHEBI:59080
data source: Provenance1
xref: UnificationXref8312
xref: UnificationXref8311
cellular location: GO:0044322
comment: Reactome DB_ID: 912286

Dolichyl beta-D-glucosyl phosphate
type: SmallMolecule
entity reference: CHEBI:15812
data source: Provenance1
xref: UnificationXref8309
xref: UnificationXref8308
cellular location: GO:0044322
comment: Reactome DB_ID: 912292
display name: DbGP

Phosphatidylinositol-3,4,5-trisphosphate
type: SmallMolecule
entity reference: CHEBI:16618
data source: Provenance1
name: PI(3,4,5)P3
name: 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
xref: UnificationXref8764
xref: UnificationXref8765
cellular location: GO:0010008
comment: Reactome DB_ID: 917716
display name: PIP3

AMP
type: SmallMolecule
entity reference: CHEBI:16027
data source: Provenance1
xref: UnificationXref8638
xref: UnificationXref8637
cellular location: GO:0005654
comment: Reactome DB_ID: 164121

ADP
type: SmallMolecule
entity reference: CHEBI:16761
data source: Provenance1
xref: UnificationXref8517
xref: UnificationXref8516
cellular location: GO:0005789
comment: Reactome DB_ID: 211606

(GlcNAc)2 (Man)7aa
type: SmallMolecule
entity reference: CHEBI:60640
data source: Provenance1
xref: UnificationXref8329
xref: UnificationXref8328
cellular location: GO:0005829
comment: Reactome DB_ID: 1022111

http://identifiers.org/pubmed/20188572
type: PublicationXref
id: 20188572
author: von Lintig, Johannes
author: Palczewski, Krzysztof
author: Kiser, Philip D
author: Golczak, Marcin
db: Pubmed
title: The biochemical and structural basis for trans-to-cis isomerization of retinoids in the chemistry of vision
source: Trends Biochem. Sci. 35:400-10
year: 2010

(GlcNAc)2 (Man)8a
type: SmallMolecule
entity reference: CHEBI:60627
data source: Provenance1
xref: UnificationXref8298
xref: UnificationXref8297
cellular location: GO:0044322
comment: Reactome DB_ID: 912298

(GlcNAc)2 (Man)8c
type: SmallMolecule
entity reference: CHEBI:60629
data source: Provenance1
xref: UnificationXref8292
xref: UnificationXref8291
cellular location: GO:0044322
comment: Reactome DB_ID: 912294

(Glc)3 (GlcNAc)2 (Man)9 (PP-Dol)1
type: SmallMolecule
entity reference: (Glc)3 (GlcNAc)2 (Man)9 (PP-Dol)1
data source: Provenance1
xref: UnificationXref8250
xref: UnificationXref8251
cellular location: GO:0071556
comment: Reactome DB_ID: 449651

(Glc)2 (GlcNAc)2 (Man)9 (PP-Dol)1
type: SmallMolecule
entity reference: (Glc)2 (GlcNAc)2 (Man)9 (PP-Dol)1
data source: Provenance1
xref: UnificationXref8243
xref: UnificationXref8244
cellular location: GO:0071556
comment: Reactome DB_ID: 449638

(Glc)2 (GlcNAc)2 (Man)9 (Asn)1
type: SmallMolecule
entity reference: CHEBI:59082
data source: Provenance1
xref: UnificationXref8264
xref: UnificationXref8265
cellular location: GO:0005788
comment: Reactome DB_ID: 532677

(Glc)3 (GlcNAc)2 (Man)9 (Asn)1
type: SmallMolecule
entity reference: CHEBI:59084
data source: Provenance1
xref: UnificationXref8261
xref: UnificationXref8260
cellular location: GO:0071556
comment: Reactome DB_ID: 532673

(GlcNAc)2 (Man)9
type: SmallMolecule
entity reference: CHEBI:59092
data source: Provenance1
xref: UnificationXref8275
xref: UnificationXref8276
cellular location: GO:0044322
comment: Reactome DB_ID: 912288

alpha-D-glucose
type: SmallMolecule
entity reference: CHEBI:17925
data source: Provenance1
xref: UnificationXref8268
xref: UnificationXref8267
cellular location: GO:0005788
comment: Reactome DB_ID: 113780
display name: Glc

http://identifiers.org/pubmed/22952392
type: PublicationXref
id: 22952392
author: Nusse, Roel
author: Willert, Karl
db: Pubmed
title: Wnt proteins
source: Cold Spring Harb Perspect Biol 4:a007864
year: 2012

(GlcNAc)2 (Man)8b
type: SmallMolecule
entity reference: CHEBI:60628
data source: Provenance1
xref: UnificationXref8283
xref: UnificationXref8284
cellular location: GO:0044322
comment: Reactome DB_ID: 1018377

D-mannose
type: SmallMolecule
entity reference: CHEBI:4208
data source: Provenance1
xref: UnificationXref8281
xref: UnificationXref8280
cellular location: GO:0044322
comment: Reactome DB_ID: 912281
display name: Man

(GlcNAc)2 (Man)7aa
type: SmallMolecule
entity reference: CHEBI:60640
data source: Provenance1
xref: UnificationXref8304
xref: UnificationXref8303
cellular location: GO:0044322
comment: Reactome DB_ID: 912290

UniProt:Q10055
type: ProteinReference
xref: UnificationXref1775
organism: BioSource1

UniProt:Q10056
type: ProteinReference
xref: UnificationXref2131
organism: BioSource1

http://identifiers.org/pubmed/5324173
type: PublicationXref
id: 5324173
author: Berg, P
author: Baldwin, AN
db: Pubmed
title: Transfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetase
source: J Biol Chem 241:839-45
year: 1966

http://identifiers.org/pubmed/5324172
type: PublicationXref
id: 5324172
author: Berg, P
author: Baldwin, AN
db: Pubmed
title: Purification and properties of isoleucyl ribonucleic acid synthetase from Escherichia coli
source: J Biol Chem 241:831-8
year: 1966

UniProt:Q10066
type: ProteinReference
xref: UnificationXref5060
organism: BioSource1

UniProt:Q10061
type: ProteinReference
xref: UnificationXref8559
organism: BioSource1

UniProt:Q10062
type: ProteinReference
xref: UnificationXref5376
organism: BioSource1

http://identifiers.org/pubmed/15526160
type: PublicationXref
id: 15526160
author: Rönnstrand, L
db: Pubmed
title: Signal transduction via the stem cell factor receptor/c-Kit
source: Cell Mol Life Sci 61:2535-48
year: 2004

UniProt:Q10067
type: ProteinReference
xref: UnificationXref5895
organism: BioSource1

UnificationXref6398
type: UnificationXref
id: REACT_15863
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15863.2

UnificationXref6399
type: UnificationXref
id: 3662860
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662860

UnificationXref6394
type: UnificationXref
id: 3662857
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662857

UnificationXref6395
type: UnificationXref
id: 3662859
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662859

UnificationXref6396
type: UnificationXref
id: REACT_95882
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_95882.9

UnificationXref6397
type: UnificationXref
id: 216667
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=216667

mannose (a1-4) glucosaminyl-acyl-PI
type: SmallMolecule
entity reference: 6-O-[alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl]-O-acyl-1-phosphatidyl-1D-myo-inositols
data source: Provenance1
xref: UnificationXref8039
xref: UnificationXref8038
cellular location: GO:0005789
comment: Reactome DB_ID: 162793

mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI
type: SmallMolecule
entity reference: (GlcN)1 (Ino(acyl)-P)1 (Man)2 (EtN)1 (P)1
data source: Provenance1
xref: UnificationXref8053
xref: UnificationXref8054
cellular location: GO:0005789
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 162848

UnificationXref6392
type: UnificationXref
id: GO:0030667
db: GENE ONTOLOGY

dolichyl phosphate
type: SmallMolecule
entity reference: dolichyl phosphate [ChEBI:16214]
data source: Provenance1
xref: UnificationXref8057
xref: UnificationXref8056
cellular location: GO:0005789
comment: Reactome DB_ID: 162872

UnificationXref6393
type: UnificationXref
id: Q9HGQ3
db: UniProt

1,2-Diacylglyceroll
type: SmallMolecule
entity reference: SmallMoleculeReference19
data source: Provenance1
xref: UnificationXref8040
xref: UnificationXref8041
cellular location: GO:0005789
comment: Reactome DB_ID: 162777
display name: DAG

UnificationXref6390
type: UnificationXref
id: 216785
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=216785

dolichyl phosphate D-mannose
type: SmallMolecule
entity reference: SmallMoleculeReference488
data source: Provenance1
name: dolichyl D-mannosyl phosphate
xref: UnificationXref8051
xref: UnificationXref8050
cellular location: GO:0071458
comment: Reactome DB_ID: 162681
display name: DOLPman

UnificationXref6391
type: UnificationXref
id: REACT_16092
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_16092.3

Dolichyl phosphate
type: SmallMolecule
entity reference: dolichyl phosphate [ChEBI:16214]
data source: Provenance1
name: Dolichol phosphate
xref: UnificationXref8076
xref: UnificationXref8077
cellular location: GO:0071458
comment: Reactome DB_ID: 449299
display name: DOLP

D-glucosamine 6-phosphate
type: SmallMolecule
entity reference: CHEBI:15873
data source: Provenance1
xref: UnificationXref8086
xref: UnificationXref8085
cellular location: GO:0005829
comment: Reactome DB_ID: 449701
display name: GlcN6P

mannose (a1-2) mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI
type: SmallMolecule
entity reference: 6-O-{alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(1->6)-2-O-[(2-aminoethyl)phosphoryl]-alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl}-O-acyl-1-phosphatidyl-1D-myo-inositols
data source: Provenance1
xref: UnificationXref8063
xref: UnificationXref8064
cellular location: GO:0005789
comment: Reactome DB_ID: 162684

Dolichol
type: SmallMolecule
entity reference: CHEBI:16091
data source: Provenance1
xref: UnificationXref8075
xref: UnificationXref8074
cellular location: GO:0071458
comment: Reactome DB_ID: 449221

N-Acetyl-D-glucosamine 6-phosphate
type: SmallMolecule
entity reference: CHEBI:15784
data source: Provenance1
xref: UnificationXref8095
xref: UnificationXref8094
cellular location: GO:0005829
comment: Reactome DB_ID: 449703
display name: AcGlcN6P

ATM mediated phosphorylation of repair proteins
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction29
evidence: Evidence46
xref: UnificationXref202
xref: UnificationXref203
pathway order: PathwayStep45
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UnificationXref6386
type: UnificationXref
id: 3662851
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662851

UnificationXref6385
type: UnificationXref
id: O13918
db: UniProt

UnificationXref6384
type: UnificationXref
id: REACT_5883
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5883.3

UnificationXref6383
type: UnificationXref
id: 158417
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=158417

UnificationXref6389
type: UnificationXref
id: GO:0034774
db: GENE ONTOLOGY

UnificationXref6388
type: UnificationXref
id: REACT_85968
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_85968.9

UnificationXref6387
type: UnificationXref
id: 3662853
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662853

UnificationXref6380
type: UnificationXref
id: 3662845
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662845

UnificationXref6381
type: UnificationXref
id: 3662847
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662847

http://identifiers.org/pubmed/2462567
type: PublicationXref
id: 2462567
author: de Jong, WW
author: Stapel, SO
author: Lietman, T
author: Wistow, GJ
author: Piatigorsky, J
author: Williams, LA
author: Horwitz, J
db: Pubmed
title: Tau-crystallin/alpha-enolase: one gene encodes both an enzyme and a lens structural protein
source: J Cell Biol 107:2729-36
year: 1988

UnificationXref6382
type: UnificationXref
id: REACT_155581
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_155581.3

UniProt:P24488
type: ProteinReference
xref: UnificationXref2859
organism: BioSource1

UnificationXref6373
type: UnificationXref
id: Q10085
db: UniProt

UnificationXref6372
type: UnificationXref
id: 3662835
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662835

UnificationXref6375
type: UnificationXref
id: 3662840
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662840

UnificationXref6374
type: UnificationXref
id: 3662839
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662839

http://identifiers.org/pubmed/10496324
type: PublicationXref
id: 10496324
author: Dharmawardhane, S
author: Lennartz, M
author: Bokoch, GM
author: Brownson, D
db: Pubmed
title: Localization of p21-activated kinase 1 (PAK1) to pseudopodia, membrane ruffles, and phagocytic cups in activated human neutrophils
source: J Leukoc Biol 66:521-7
year: 1999

UnificationXref6377
type: UnificationXref
id: 3662842
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662842

UnificationXref6376
type: UnificationXref
id: 3662841
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662841

UnificationXref6379
type: UnificationXref
id: 3662844
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662844

UnificationXref6378
type: UnificationXref
id: 3662843
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662843

(GlcNAc)2 (Man)7 (PP-Dol)1
type: SmallMolecule
entity reference: CHEBI:59088
data source: Provenance1
xref: UnificationXref8215
xref: UnificationXref8216
cellular location: GO:0071556
comment: Reactome DB_ID: 449312

UnificationXref6370
type: UnificationXref
id: 3662831
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662831

(GlcNAc)2 (Man)8 (PP-Dol)1
type: SmallMolecule
entity reference: CHEBI:59091
data source: Provenance1
xref: UnificationXref8222
xref: UnificationXref8223
cellular location: GO:0071556
comment: Reactome DB_ID: 449365

UnificationXref6371
type: UnificationXref
id: Q9USK3
db: UniProt

Dolichyl phosphate
type: SmallMolecule
entity reference: dolichyl phosphate [ChEBI:16214]
data source: Provenance1
name: Dolichol phosphate
xref: UnificationXref8206
xref: UnificationXref8205
cellular location: GO:0071556
comment: Reactome DB_ID: 449311
display name: DOLP

(GlcNAc)2 (Man)6 (PP-Dol)1
type: SmallMolecule
entity reference: ChEBI:53023 (GlcNAc)2 (Man)6 (PP-Dol)1
data source: Provenance1
xref: UnificationXref8209
xref: UnificationXref8208
cellular location: GO:0071556
comment: Reactome DB_ID: 449315

(GlcNAc)2 (Man)5 (PP-Dol)1
type: SmallMolecule
entity reference: ChEBI:53022 (GlcNAc)2 (Man)5 (PP-Dol)1
data source: Provenance1
xref: UnificationXref8197
xref: UnificationXref8196
cellular location: GO:0071556
comment: Reactome DB_ID: 449298

Dolichyl phosphate D-mannose
type: SmallMolecule
entity reference: CHEBI:15809
data source: Provenance1
name: Dolichyl D-mannosyl phosphate
xref: UnificationXref8204
xref: UnificationXref8203
cellular location: GO:0071556
comment: Reactome DB_ID: 449229
display name: DOLPM

(GlcNAc)2 (Man)5 (PP-Dol)1
type: SmallMolecule
entity reference: ChEBI:53022 (GlcNAc)2 (Man)5 (PP-Dol)1
data source: Provenance1
xref: UnificationXref8190
xref: UnificationXref8189
cellular location: GO:0071458
comment: Reactome DB_ID: 449332

(Glc)1 (GlcNAc)2 (Man)9 (PP-Dol)1
type: SmallMolecule
entity reference: CHEBI:59081
data source: Provenance1
xref: UnificationXref8237
xref: UnificationXref8236
cellular location: GO:0071556
comment: Reactome DB_ID: 449649

(GlcNAc)2 (Man)9 (PP-Dol)1
type: SmallMolecule
entity reference: CHEBI:59093
data source: Provenance1
xref: UnificationXref8229
xref: UnificationXref8230
cellular location: GO:0071556
comment: Reactome DB_ID: 449371

Dolichyl beta-D-glucosyl phosphate
type: SmallMolecule
entity reference: CHEBI:15812
data source: Provenance1
xref: UnificationXref8234
xref: UnificationXref8233
cellular location: GO:0071556
comment: Reactome DB_ID: 532542
display name: DbGP

http://identifiers.org/pubmed/11533233
type: PublicationXref
id: 11533233
author: Fox, PL
author: Sonenberg, N
author: Imataka, H
author: Seshadri, V
author: Mazumder, B
db: Pubmed
title: Translational silencing of ceruloplasmin requires the essential elements of mRNA circularization: poly(A) tail, poly(A)-binding protein, and eukaryotic translation initiation factor 4G
source: Mol Cell Biol 21:6440-9
year: 2001

UnificationXref6369
type: UnificationXref
id: Q9UT92
db: UniProt

UnificationXref6368
type: UnificationXref
id: REACT_20849
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20849.1

http://identifiers.org/pubmed/9741684
type: PublicationXref
id: 9741684
author: Edwards, PA
author: Shell, BK
author: Greene, JM
author: Ericsson, J
author: Carter, KC
author: Florence, C
author: Duan, DR
db: Pubmed
title: Human geranylgeranyl diphosphate synthase: isolation of the cDNA, chromosomal mapping and tissue expression
source: J Lipid Res 39:1731-9
year: 1998

UnificationXref6367
type: UnificationXref
id: 446597
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=446597

UnificationXref6366
type: UnificationXref
id: REACT_20978
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20978.2

UnificationXref6365
type: UnificationXref
id: 446604
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=446604

UnificationXref6364
type: UnificationXref
id: REACT_20887
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20887.1

UnificationXref6363
type: UnificationXref
id: 446596
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=446596

UnificationXref6362
type: UnificationXref
id: REACT_20993
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20993.2

UnificationXref6361
type: UnificationXref
id: 446603
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=446603

D-Mannose 1-phosphate
type: SmallMolecule
entity reference: CHEBI:35374
data source: Provenance1
xref: UnificationXref8125
xref: UnificationXref8124
cellular location: GO:0005829
comment: Reactome DB_ID: 532531
display name: Man1P

GDP-alpha-D-mannose
type: SmallMolecule
entity reference: CHEBI:15820
data source: Provenance1
name: guanosine 5'-(3-(alpha-D-mannopyranosyl) dihydrogen diphosphate)
xref: UnificationXref8134
xref: UnificationXref8133
cellular location: GO:0005829
comment: Reactome DB_ID: 162860
display name: GDP-Man

Dolichyl beta-D-glucosyl phosphate
type: SmallMolecule
entity reference: CHEBI:15812
data source: Provenance1
xref: UnificationXref8145
xref: UnificationXref8146
cellular location: GO:0071458
comment: Reactome DB_ID: 532214
display name: DbGP

N-acetyl-D-glucosaminyl-diphosphodolichol
type: SmallMolecule
entity reference: CHEBI:18278
data source: Provenance1
xref: UnificationXref8156
xref: UnificationXref8157
cellular location: GO:0071458
comment: Reactome DB_ID: 449222
display name: GlcNAcDOLDP

UnificationXref6360
type: UnificationXref
id: REACT_21171
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21171.2

N-Acetyl-D-glucosamine 1-phosphate
type: SmallMolecule
entity reference: CHEBI:7125
data source: Provenance1
xref: UnificationXref8102
xref: UnificationXref8103
cellular location: GO:0005829
comment: Reactome DB_ID: 532204
display name: AcGlcN1P

D-Mannose 6-phosphate
type: SmallMolecule
entity reference: CHEBI:17369
data source: Provenance1
xref: UnificationXref8118
xref: UnificationXref8117
cellular location: GO:0005829
comment: Reactome DB_ID: 532562
display name: Man6P

http://identifiers.org/pubmed/9188776
type: PublicationXref
id: 9188776
author: Rider, MH
author: Veiga-da-Cunha, M
author: Gerin, I
author: Van Schaftingen, E
author: Collet, JF
db: Pubmed
title: Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate
source: FEBS Lett 408:281-4
year: 1997

N,N'-diacetylchitobiosyldiphosphodolichol
type: SmallMolecule
entity reference: N,N'-Diacetylchitobiosyldiphosphodolichol [ChEBI:7069]
data source: Provenance1
xref: UnificationXref8164
xref: UnificationXref8163
cellular location: GO:0071458
comment: Reactome DB_ID: 449293
display name: N,N'-DCDOLDP

beta-D-mannosyldiacetylchitobiosyldiphosphodolichol
type: SmallMolecule
entity reference: beta-D-Mannosyldiacetylchitobiosyldiphosphodolichol [ChEBI:10408]
data source: Provenance1
xref: UnificationXref8171
xref: UnificationXref8170
cellular location: GO:0071458
comment: Reactome DB_ID: 449283
display name: MDCDD

(GlcNAc)2 (Man)2 (PP-Dol)1
type: SmallMolecule
entity reference: CHEBI:59085
data source: Provenance1
xref: UnificationXref8178
xref: UnificationXref8177
cellular location: GO:0071458
comment: Reactome DB_ID: 449737

(GlcNAc)2 (Man)3 (PP-Dol)1
type: SmallMolecule
entity reference: CHEBI:53742
data source: Provenance1
xref: UnificationXref8184
xref: UnificationXref8185
cellular location: GO:0071458
comment: Reactome DB_ID: 449243

UnificationXref6359
type: UnificationXref
id: 446595
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=446595

UnificationXref6358
type: UnificationXref
id: REACT_21240
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21240.2

UnificationXref6355
type: UnificationXref
id: 446609
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=446609

UnificationXref6354
type: UnificationXref
id: REACT_20771
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20771.2

UnificationXref6357
type: UnificationXref
id: 446592
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=446592

UnificationXref6356
type: UnificationXref
id: REACT_21081
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21081.2

UnificationXref6351
type: UnificationXref
id: 446589
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=446589

UnificationXref6350
type: UnificationXref
id: REACT_20975
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20975.2

UnificationXref6353
type: UnificationXref
id: 446607
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=446607

UnificationXref6352
type: UnificationXref
id: REACT_21070
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21070.1

4-Trimethylammoniobutanal
type: SmallMoleculeReference
name: 4-Trimethylammoniobutanal [ChEBI:18020]
xref: UnificationXref5078

Recruitment of repair and signaling proteins to double-strand breaks
type: Pathway
data source: Provenance1
pathway component: REACT 38183.10
evidence: Evidence51
xref: UnificationXref217
xref: UnificationXref218
pathway order: PathwayStep50
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Phosphoenolpyruvic acid
type: SmallMoleculeReference
name: Phosphoenolpyruvate
name: Phosphoenolpyruvate [ChEBI:18021]
name: PEP
xref: UnificationXref2298

http://identifiers.org/pubmed/10101268
type: PublicationXref
id: 10101268
author: Heilmeyer LM, Jr
author: Gehrmann, T
author: Balla, A
author: Herberg, FW
author: Mayr, Georg W
author: Suer, S
author: Gülkan, H
author: Vereb, G
db: Pubmed
title: Functional expression and characterisation of a new human phosphatidylinositol 4-kinase PI4K230
source: Biochim Biophys Acta 1437:341-56
year: 1999

http://identifiers.org/pubmed/10615129
type: PublicationXref
id: 10615129
author: Mauro, T
author: Ikeda, S
author: Bonifas, JM
author: Beech, J
author: Bench, G
author: Ogawa, H
author: Hu, Z
author: Shigihara, T
author: Epstein EH, Jr
db: Pubmed
title: Mutations in ATP2C1, encoding a calcium pump, cause Hailey-Hailey disease
source: Nat Genet 24:61-5
year: 2000

diacylglycerols
type: SmallMoleculeReference
name: diacylglycerols [ChEBI:18035]
xref: UnificationXref967

http://identifiers.org/pubmed/15548136
type: PublicationXref
id: 15548136
author: Zhao, ZS
author: Manser, E
db: Pubmed
title: PAK and other Rho-associated kinases--effectors with surprisingly diverse mechanisms of regulation
source: Biochem J 386:201-14
year: 2005

L-Glutamine
type: SmallMoleculeReference
name: L-Glutamine [ChEBI:18050]
name: L-2-Aminoglutaramic acid
xref: UnificationXref4078

http://identifiers.org/pubmed/7678419
type: PublicationXref
id: 7678419
author: Smith, BL
author: Agre, P
author: Knepper, MA
author: Christensen, EI
author: Nielsen, S
db: Pubmed
title: CHIP28 water channels are localized in constitutively water-permeable segments of the nephron
source: J Cell Biol 120:371-83
year: 1993

SRP-dependent cotranslational protein targeting to membrane
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction671
pathway component: BiochemicalReaction670
evidence: Evidence1169
xref: UnificationXref7449
xref: UnificationXref7448
xref: RelationshipXref968
pathway order: PathwayStep1148
pathway order: PathwayStep1147
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UDPglucose
type: SmallMoleculeReference
name: UDP-D-glucose
name: UDPglucose [ChEBI:18066]
name: UDP-glucose
xref: UnificationXref2446

dTDP
type: SmallMoleculeReference
name: Deoxythymidine 5'-diphosphate
name: dTDP [ChEBI:18075]
xref: UnificationXref4439

TTP
type: SmallMoleculeReference
name: Deoxythymidine 5'-triphosphate
name: dTTP
name: Deoxythymidine triphosphate
name: dTTP [ChEBI:18077]
xref: UnificationXref6013

UniProt:Q10085
type: ProteinReference
xref: UnificationXref6373
organism: BioSource1

http://identifiers.org/pubmed/11459976
type: PublicationXref
id: 11459976
author: Bell, SP
author: Klemm, RD
db: Pubmed
title: ATP bound to the origin recognition complex is important for preRC formation.
source: Proc Natl Acad Sci U S A 98:8361-7
year: 2001

PI3K Cascade
type: Pathway
data source: Provenance1
pathway component: Activation of PKB
pathway component: PKB-mediated events
evidence: Evidence215
xref: UnificationXref1136
xref: UnificationXref1137
pathway order: PathwayStep210
pathway order: PathwayStep212
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/17189949
type: PublicationXref
id: 17189949
author: Maness, PF
author: Schachner, M
db: Pubmed
title: Neural recognition molecules of the immunoglobulin superfamily: signaling transducers of axon guidance and neuronal migration
source: Nat Neurosci 10:19-26
year: 2007

http://identifiers.org/pubmed/12121577
type: PublicationXref
id: 12121577
author: Safrany, ST
author: Leslie, NR
author: McLennan, AG
db: Pubmed
title: Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases
source: BMC Biochem 3:20
year: 2002

Evidence720
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19675644
xref: http://identifiers.org/pubmed/16261263
comment: Molybdenum cofactor (MoCo) is needed by three enzymes in humans: sulfite oxidase, xanthine oxidase and aldehyde oxidase. The pathway of its synthesis is so conserved that plants and bacteria can readily use human enzymes. Bacteria, however, diverge after the first three steps from this path and their final MoCo differs from that of the eukaryotes. Plants and animals have also developed a refinement of their MoCo which is needed for the function of their xanthine and aldehyde oxidases. This means, in humans we find sulfurated instead of desulfurated molybdenum cofactor on these two enzymes (Schwarz 2005; Schwarz, Mendel, Ribbe 2009).

Evidence721
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Vitamins are a diverse group of organic compounds, required in small amounts in the diet. They have distinct biochemical roles, often as coenzymes, and are either not synthesized or synthesized only in limited amounts by human cells. Vitamins are classified according to their solubility, either fat-soluble or water-soluble. The physiological processes dependent on vitamin-requiring reactions include many aspects of intermediary metabolism, vision, bone formation, and blood coagulation, and vitamin deficiencies are associated with a correspondingly diverse and severe group of diseases. Water-soluble vitamins include ascorbate (vitamin C) and the members of the B group: thiamin (vitamin B1), riboflavin (B2), niacin (B3), pantothenate (B5), pyridoxine (B6), biotin (B7), folate (B9), and cobalamin (B12). Metabolic processes annotated here include the synthesis of thiamin pyrophosphate (TPP) from thiamin (B1), the synthesis of FMN and FAD from riboflavin (B2), the synthesis of nicotinic acid (niacin - B3) from tryptophan, the synthesis of Coenzyme A from pantothenate (B5), and features of the metabolism of folate (B9).

Evidence726
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19360321
xref: http://identifiers.org/pubmed/11863375
comment: Glutamic-pyruvate transaminase 2 (alanine aminotransferase 2) (GPT2) catalyzes the reversible reaction of pyruvate and glutamate to form alanine and 2-oxoglutarate (alpha-ketoglutarate) (Yang et al. 2002). Unpublished crystallographic data are consistent with a homodimeric structure for the enzyme with one molecule of pyridoxal phosphate associated with each monomer (PDB 3IHJ). Recent studies of organelles purified from cultured human muscle cells suggest that GPT2 is localized to mitochondria (Glinghammar et al. 2009).

Evidence727
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/2241899
comment: Cytosolic aspartate aminotransferase (glutamate oxaloacetate transaminase 1 - GOT1) catalyzes the reversible reaction of oxaloacetate and glutamate to form aspartate and 2-oxoglutarate (alpha-ketoglutarate) (Doyle et al. 1990). Unpublished crystallographic data (PBD 3IIO) suggest the enzyme is a homodimer.

Evidence728
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/4052435
comment: Mitochondrial glutamate oxaloacetate transaminase 2 (aspartate aminotransferase 2 - GOT2) catalyzes the reversible reaction of aspartate and 2-oxoglutarate (alpha-ketoglutarate) to form oxaloacetate and glutamate (Martini et al. 1985). The active form of the enzyme is inferred to be a dimer with one molecule of pyridoxal phosphate associated with each monomer.

Evidence729
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9514741
xref: http://identifiers.org/pubmed/6819292
xref: PublicationXref1185
xref: http://identifiers.org/pubmed/1737786
comment: Mitochondrial ornithine aminotransferase (OAT) catalyzes the reversible reaction of ornithine and alpha-ketoglutarate to form glutamate semialdehyde and glutamate (Ohura et al. 1982). The active enzyme is a hexamer (Shen et al. 1998). Inherited OAT deficiency leads to ornithine accumulation in vivo and gyrate atrophy of the choroid and retina (Brody et al. 1992; Valle and Simell 2001).

Evidence722
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Vitamins are a diverse group of organic compounds, required in small amounts in the diet. They have distinct biochemical roles, often as coenzymes, and are either not synthesized or synthesized only in limited amounts by human cells. Vitamins are classified according to their solubility, either fat-soluble or water-soluble. The physiological processes dependent on vitamin-requiring reactions include many aspects of intermediary metabolism, vision, bone formation, and blood coagulation, and vitamin deficiencies are associated with a correspondingly diverse and severe group of diseases. The metabolism of water-soluble vitamins and of vitamin D are annotated in Reactome.

http://identifiers.org/pubmed/9556621
type: PublicationXref
id: 9556621
author: Riese DJ, 2nd
author: Stern, DF
author: Komurasaki, T
author: Plowman, GD
db: Pubmed
title: Activation of ErbB4 by the bifunctional epidermal growth factor family hormone epiregulin is regulated by ErbB2
source: J Biol Chem 273:11288-94
year: 1998

Evidence723
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1931970
xref: http://identifiers.org/pubmed/9119391
xref: http://identifiers.org/pubmed/11863375
comment: Cytosolic glutamic-pyruvate transaminase (alanine aminotransferase) (GPT) catalyzes the reversible reaction of alanine and 2-oxoglutarate (alpha-ketoglutarate) to form pyruvate and glutamate (Sohocki et al. 1997; Yang et al. 2002). The active form of the enzyme is a dimer (Ishiguro et al. 1991) and is inferred to have a molecule of pyridoxal phosphate associated with each monomer. This reaction allows the synthesis of alanine from intermediates of glucose metabolism in a well-fed person. Under fasting conditions, alanine, derived from protein breakdown, can be converted to pyruvate and used to synthesize glucose via the gluconeogenic pathway in liver, or fully oxidized via the TCA cycle in other tissues.

Evidence724
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1931970
xref: http://identifiers.org/pubmed/9119391
xref: http://identifiers.org/pubmed/11863375
comment: Cytosolic glutamic-pyruvate transaminase (alanine aminotransferase) (GPT) catalyzes the reversible reaction of pyruvate and glutamate to form alanine and 2-oxoglutarate (alpha-ketoglutarate) (Sohocki et al. 1997; Yang et al. 2002). The active form of the enzyme is a dimer (Ishiguro et al. 1991) and is inferred to have a molecule of pyridoxal phosphate associated with each monomer. This reaction allows the synthesis of alanine from intermediates of glucose metabolism in a well-fed person. Under fasting conditions, alanine, derived from protein breakdown, can be converted to pyruvate and used to synthesize glucose via the gluconeogenic pathway in liver, or fully oxidized via the TCA cycle in other tissues.

Evidence725
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19360321
xref: http://identifiers.org/pubmed/11863375
comment: Glutamic-pyruvate transaminase 2 (alanine aminotransferase 2) (GPT2) catalyzes the reversible reaction of alanine and 2-oxoglutarate (alpha-ketoglutarate) to form pyruvate and glutamate (Yang et al. 2002). Unpublished crystallographic data are consistent with a homodimeric structure for the enzyme with one molecule of pyridoxal phosphate associated with each monomer (PDB 3IHJ). Recent studies of organelles purified from cultured human muscle cells suggest that GPT2 is localized to mitochondria (Glinghammar et al. 2009).

http://identifiers.org/pubmed/9792662
type: PublicationXref
id: 9792662
author: Morgunov, I
author: Srere, PA
db: Pubmed
title: Interaction between citrate synthase and malate dehydrogenase. Substrate channeling of oxaloacetate
source: J Biol Chem 273:29540-29544
year: 1998

http://identifiers.org/pubmed/11459989
type: PublicationXref
id: 11459989
author: Paulusma, C
author: Wyman, C
author: Kanaar, R
author: Ristic, D
db: Pubmed
title: The architecture of the human Rad54-DNA complex provides evidence for protein translocation along DNA.
source: Proc Natl Acad Sci U S A 98:8454-60
year: 2001

Evidence731
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10037775
comment: Delta-1-pyrroline-5-carboxylate synthetase associated with the inner mitochondrial membrane catalyzes the two-step reaction that converts glutamate, ATP, and NADPH + H+ to L-glutamate gamma-semialdehyde, NADP+, ADP, and orthophosphate. Two P5CS isoforms have been identified; both are active when expressed in enzyme-deficient cells in culture (Hu et al. 1999). Unpublished crystallographic data (PDB 2H5G) indicate that the enzyme is a dimer.

Evidence732
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref1190
xref: http://identifiers.org/pubmed/2722838
xref: http://identifiers.org/pubmed/19648921
comment: Pyrroline-5-carboxylate reductase 1 (PYCR1) catalyzes the reaction of (S)-1-pyrroline-5-carboxylate with NADPH + H+ to form proline and NADP+ (Merrill et al. 1989). The active enzyme is a homodecamer (Meng et al. 2006). Recent immunofluoresence studies show that PYCR1 colocalizes with mitochondrial markers including pyrroline 5-carboxylate synthase in cultured human fibroblasts (Reversade et al. 2009).

Evidence730
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref1185
xref: http://identifiers.org/pubmed/1737786
comment: Mitochondrial ornithine aminotransferase (OAT) catalyzes the reversible reaction of glutamate semialdehyde and glutamate to form ornithine and alpha-ketoglutarate (Ohura et al. 1982). The active enzyme is a hexamer (Shen et al. 1998). Inherited OAT deficiency leads to ornithine accumulation in vivo and gyrate atrophy of the choroid and retina (Brody et al. 1992; Vallee and Simell 2001).

Evidence739
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15021249
comment: L-Serine is needed in human brain in large amounts as precursor to important biomolecules such as nucleotides, phospholipids and the neurotransmitters glycine and D-serine. The pathway for its synthesis starts with 3-phosphoglycerate and it later needs glutamate as an amination agent. Deficiencies in the participating enzymes lead to severe neurological symptoms that are treatable with serine if treatment starts early (de Koning & Klomp 2004).

Evidence737
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12633500
comment: The amino group needed for serine biosynthesis comes from glutamate. Its transfer onto 3-phosphonooxpyruvate is catalysed by the PSAT1 dimer which needs pyridoxal phosphate as cofactor. (Baek et al. 2003)

Evidence738
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9188776
comment: Dephosphorylation of O-phospho-L-serine to L-serine proceeds through a phospho-enzyme intermediate of the catalysing phosphatase PSP (Collet et al. 1997).

Evidence735
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7883047
xref: http://identifiers.org/pubmed/15364907
xref: http://identifiers.org/pubmed/8294935
xref: http://identifiers.org/pubmed/19338303
comment: CCBL1 (KAT 1) catalyzes the reaction of glutamine and pyruvate to form 2-oxoglutaramate and alanine. The active form of CCBL1 is a homodimer with one molecule of pyridoxal phosphate bound to each monomer (Baran et al. 1994; Han et al. 2009; Rossi et al. 2004). The enzyme's cytosolic localization is inferred from that of recombinant protein overexpressed in transfected cells (Perry et al. 1995).

Evidence736
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19235232
comment: Serine biosynthesis starts from 3-phosphoglycerate, a glycolysis intermediate. Its dehydrogenation is catalysed by tetrameric phosphoglycerate dehydrogenase PHGDH. (Tabatabaie et al. 2009).

Evidence733
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/2564390
comment: Cytosolic asparagine synthase (ASNS) catalyzes the reaction of aspartate, glutamine, and ATP to form asparagine, glutamate, AMP, and pyrophosphate. Studies of the recombinant protein expressed in E. coli suggest that the active form of the enzyme is a dimer (Van Heeke and Schuster 1989).

Evidence734
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16267323
xref: http://identifiers.org/pubmed/18005987
comment: Cytosolic glutamine synthetase (glutamate-ammonia ligase - GLUL) catalyzes the reaction of glutamate, ammonia, and ATP to form glutamine, ADP, and orthophosphate. The enzyme is a decamer (Krajewski et al. 2008). Mutations in the gene encoding GLUL cause glutamine deficiency in vivo (Haberle et al. 2005).

Evidence709
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8662720
xref: http://identifiers.org/pubmed/10978331
comment: SLC25A32 protein in the inner mitochondrial membrane mediates the reversible transport of tetrahydrofolate between the cytosol and the mitochondrial matrix. Retention of tetrahydrofolate within the mitochondrial matrix is dependent on mitochondrial polyglutamate addition (Titus and Moran 2000; Chen et al. 1996).

Evidence708
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1409616
xref: http://identifiers.org/pubmed/8662720
comment: Cytosolic folylpolyglutamate synthase catalyzes the reaction of 5-methylTHF-glutamate(n), L-glutamate, and ATP to form 5-methylTHF-glutamate(n+1), ADP, and orthophosphate. (The first glutamate residue is attached to the glutamate moiety of 5-methylTHF itself; for convenience the process is annotated here as if it proceeded in a single concerted step.) The extent of conjugation is variable, but the commonest cytosolic form of 5-methylTHF has five added glutamate residues. Although its properties as a donor of one-carbon units are not affected by glutamate addition, 5-methylTHF that lacks added glutamate residues cannot be retained in the cytosol so this reaction is needed for normal 5-methylTHF function under physiological conditions (Garrow et al. 1992; Chen et al. 1996).

Evidence700
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16326698
xref: http://identifiers.org/pubmed/22123817
xref: http://identifiers.org/pubmed/20952656
xref: http://identifiers.org/pubmed/16134170
xref: http://identifiers.org/pubmed/20153287
xref: http://identifiers.org/pubmed/12360400
xref: http://identifiers.org/pubmed/9630604
comment: Biotin (Btn) acts as a coenzyme to 4 carboxylases which exist in their inactive apo forms. In the cytosol, these apo carboxylases are biotinylated to their active halo forms by the activity of biotin-protein ligase (HCLS) (Ingaramo & Beckett 2012, Hiratsuka et al. 1998, Bailey et al. 2010). Defects in HLCS causes holocarboxylase synthetase deficiency (HLCS deficiency aka biotin-responsive multiple carboxylase deficiency; MIM:253270). HLCS deficiency is an autosomal recessive disorder whereby deficient HLCS activity results in reduced activity of multiple carboxylases. Symptoms include metabolic acidosis, organic aciduria, lethargy, hypotonia, convulsions and dermatitis (Suzuki et al. 2005). Acetyl-CoA carboxylases 1 and 2 (ACACA and ACACB) bind 2 Mn2+ and 1 Btn per subunit (Colbert et al. 2010). They can exist as either monomers, homodimers or homotetramers (latter two not shown in this reaction) (Magnard et al. 2002, Moreau et al. 2006). Unlike the other carboxylases acted upon by HCLS, ACACA and B are located in the cytosol (shown here) as well as the mitochondrial membrane. The exact order in which this complex is constructed is unknown.

Evidence701
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19319844
comment: Biotin (Btn) is an essential cofactor in a variety of carboxylation reactions (Zempleni et al. 2009). Humans cannot synthesize Btn but it is abundant in the human diet and can be taken up from the intestinal lumen by the SLC5A6 transporter. Its uptake, intracellular translocation, covalent conjugation to apoenzymes, and salvage are described here.

Evidence702
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11248244
xref: http://identifiers.org/pubmed/16118205
xref: http://identifiers.org/pubmed/17402747
xref: http://identifiers.org/pubmed/11788603
comment: NMNAT1 catalyzes the reaction of nicotinate D-ribonucleotide and ATP to form deamino-NAD+ (nicotinate adenine dinucleotide) and pyrophosphate (Schweiger et al. 2001). The active form of the enzyme in vitro is a hexamer (Zhou et al. 2002), and its activity is substantially greater in the presence of Zn++ than of Mg++ (Sorci et al. 2007). The predicted amino acid sequence of the enzyme contains a nuclear localization domain and the protein is observed to localize to the nucleus (Schweiger et al. 2001; Berger et al. 2005).

Evidence703
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/14516279
xref: http://identifiers.org/pubmed/16118205
xref: http://identifiers.org/pubmed/17402747
xref: http://identifiers.org/pubmed/12359228
comment: NMNAT2 catalyzes the reaction of nicotinate D-ribonucleotide and ATP to form deamino-NAD+ (nicotinate adenine dinucleotide) and pyrophosphate (Sorci et al. 2007). The active form of the enzyme is a monomer in vitro (Raffaelli et al. 2002). Although the predicted amino acid sequence of the enzyme lacks an obvious signal sequence or transmembrane domain (Yalowitz et al. 2004), recombinant FLAG-tagged protein expressed in HeLa cells localizes predominantly to the Golgi apparatus (Berger et al. 2005). Its localization within the Golgi apparatus is unknown and the annotation here is based on the plausible but speculative assumption that the enzyme is associated with the Gogi membrane and accessible from the cytosol. Immunostaining studies indicate that the protein is abundant in Islets of Langerhans and in several regions of the brain (Yalowitz et al. 2004).

Evidence704
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12574164
xref: http://identifiers.org/pubmed/16118205
xref: http://identifiers.org/pubmed/17402747
comment: NMNAT3 catalyzes the reaction of nicotinate D-ribonucleotide and ATP to form deamino-NAD+ (nicotinate adenine dinucleotide) and pyrophosphate (Sorci et al. 2007). The active form of the enzyme is a tetramer in vitro (Zhang et al. 2003). Recombinant FLAG-tagged protein expressed in HeLa cells localizes both to the cytosol and to mitochondria (Berger et al. 2005). The cytosolic protein is annotated here.

Evidence705
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12547821
comment: NAD synthase catalyzes the final step in the biosynthesis of NAD+, both in the de novo synthesis and in the salvage pathways. The enzyme makes use of glutamine as an amide donor in the reaction. NAD synthase exists as a homohexamer in the cytosol. There are two forms of NAD synthase in humans, NADsyn1 and NADsyn2. The major difference between the two forms is that NADsyn1 appears to be glutamine-dependent whereas NADsyn2 is strictly ammonia-dependent.

Evidence706
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/14704851
comment: Nicotinate (niacin) and nicotinamide are precursors of the coenzymes nicotinamide-adenine dinucleotide (NAD+) and nicotinamide-adenine dinucleotide phosphate (NADP+). When NAD+ and NADP+ are interchanged in a reaction with their reduced forms, NADH and NADPH respectively, they are important cofactors in several hundred redox reactions. Nicotinate is synthesized from 2-amino-3-carboxymuconate semialdehyde, an intermediate in the catabolism of the essential amino acid tryptophan.

Evidence707
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1409616
xref: http://identifiers.org/pubmed/8662720
comment: Cytosolic folylpolyglutamate synthase catalyzes the reaction of THF-glutamate(n), L-glutamate, and ATP to form THF-glutamate(n+1), ADP, and orthophosphate. (The first glutamate residue is attached to the glutamate moiety of THF itself; for convenience the process is annotated here as if it proceeded in a single concerted step.) The extent of conjugation is variable, but the commonest cytosolic form of THF has five added glutamate residues. Although its properties as a donor of one-carbon units are not affected by glutamate addition, THF that lacks added glutamate residues cannot be retained in the cytosol so this reaction is needed for normal THF function under physiological conditions (Garrow et al. 1992; Chen et al. 1996).

Evidence719
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18650437
comment: In order to get a sulfur atom for subsequent sulfuration reactions, cysteine is first desulfurated by NFS1 which transfers it onto a cysteine of MOCS3, yielding a protein persulfide (Marelja et al, 2008).

PKB-mediated events
type: Pathway
data source: Provenance1
pathway component: REACT 110168.9
evidence: Evidence212
xref: UnificationXref1127
xref: UnificationXref1126
pathway order: PathwayStep209
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Evidence710
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8662720
xref: http://identifiers.org/pubmed/10978331
comment: SLC25A32 protein in the inner mitochondrial membrane mediates the reversible transport of tetrahydrofolate between the cytosol and the mitochondrial matrix. Retention of tetrahydrofolate within the mitochondrial matrix is dependent on mitochondrial polyglutamate addition (Titus and Moran 2000; Chen et al. 1996).

Evidence713
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3871768
xref: http://identifiers.org/pubmed/3053686
comment: The methenyltetrahydrofolate cyclohydrolase activity of the trifunctional MTHFD1 enzyme catalyzes the reversible reaction of 10-formylTHF polyglutamate to form 5,10-methenylTHF polyglutamate and H2O. MTHFD1 is cytosolic and occurs as a dimer. The human enzyme has been identified and partially characterized biochemically (Hum et al. 1988); additional reaction details can be inferred from the properties of the well-studied homologous rabbit enzyme (Villar et al. 1985).

Evidence714
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3871768
xref: http://identifiers.org/pubmed/3053686
comment: The methylenetetrahydrofolate dehydrogenase activity of the trifunctional MTHFD1 enzyme catalyzes the reversible reaction of 5,10-methenylTHF polyglutamate, NADPH, and H+ to form 5,10-methyleneTHF polyglutamate and NADP+. MTHFD1 is cytosolic and occurs as a dimer. The human enzyme has been identified and partially characterized biochemically (Hum et al. 1988); additional reaction details can be inferred from the properties of the well-studied homologous rabbit enzyme (Villar et al. 1985).

Evidence711
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1409616
xref: http://identifiers.org/pubmed/8662720
comment: Mitochondrial folylpolyglutamate synthase catalyzes the reaction of THF-glutamate(n), L-glutamate, and ATP to form THF-glutamate(n+1), ADP, and orthophosphate. (The first glutamate residue is attached to the glutamate moiety of THF itself; for convenience the process is annotated here as if it proceeded in a single concerted step.) The extent of conjugation is variable, but the commonest mitochondrial form of THF has six added glutamate residues. Although its properties as a donor of one-carbon units are not affected by glutamate addition, THF that lacks added glutamate residues cannot be retained in the mitochondrial matrix so this reaction is needed for normal THF function under physiological conditions. The mitochondrial and cytosolic forms of folylpolyglutamate synthase are encoded by the same gene - alternative splicing generates mRNA with or without an initial exon encoding a mitochondrial targeting sequence (Garrow et al. 1992; Chen et al. 1996).

Evidence712
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3871768
xref: http://identifiers.org/pubmed/3053686
comment: The formate-tetrahydrofolate ligase activity of the trifunctional MTHFD1 enzyme catalyzes the reaction of THF polyglutamate, formate, and ATP to form 10-formylTHF polyglutamate, ADP, and orthophosphate. MTHFD1 is cytosolic and occurs as a dimer. The human enzyme has been identified and partially characterized biochemically (Hum et al. 1988); additional reaction details can be inferred from the properties of the well-studied homologous rabbit enzyme (Villar et al. 1985).

Evidence717
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3871768
xref: http://identifiers.org/pubmed/3053686
comment: The methenyltetrahydrofolate cyclohydrolase activity of the trifunctional MTHFD1 enzyme catalyzes the reversible reaction of 5,10-methenylTHF polyglutamate and H2O to form 10-formylTHF polyglutamate. MTHFD1 is cytosolic and occurs as a dimer. The human enzyme has been identified and partially characterized biochemically (Hum et al. 1988); additional reaction details can be inferred from the properties of the well-studied homologous rabbit enzyme (Villar et al. 1985).

Evidence718
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10466189
xref: http://identifiers.org/pubmed/11001804
comment: Folates are essential cofactors that provide one-carbon moieties in various states of reduction for biosynthetic reactions. Processes annotated here include transport reactions by which folates are taken up by cells and moved intracellularly, folate conjugation with glutamate (required for folate retention within a cell), and some of the key reactions in the generation of reduced folates and one-carbon derivatives of folate.

Evidence715
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7726158
comment: Cytosolic MTHFR dimer catalyzes the reaction of 5,10-methyleneTHF polyglutamate, NADPH, and H+ to form 5-methylTHF polyglutamate and NADP+. The specificity and importance of this reaction in vivo have been established through the study of patients deficient in the enzyme (Goyette et al. 1995).

Evidence716
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3871768
xref: http://identifiers.org/pubmed/3053686
comment: The methylenetetrahydrofolate dehydrogenase activity of the trifunctional MTHFD1 enzyme catalyzes the reversible reaction of 5,10-methyleneTHF polyglutamate and NADP+ to form 5,10-methenylTHF polyglutamate, NADPH, and H+. MTHFD1 is cytosolic and occurs as a dimer. The human enzyme has been identified and partially characterized biochemically (Hum et al. 1988); additional reaction details can be inferred from the properties of the well-studied homologous rabbit enzyme (Villar et al. 1985).

http://identifiers.org/pubmed/19196711
type: PublicationXref
id: 19196711
author: Frankson, E
author: Bardwell, L
author: Bardwell, AJ
db: Pubmed
title: Selectivity of docking sites in MAPK kinases
source: J Biol Chem 284:13165-73
year: 2009

http://identifiers.org/pubmed/8633070
type: PublicationXref
id: 8633070
author: Ullrich, A
author: Giot, JF
author: Møller, NP
author: Zahalka, MA
author: Lechner, C
db: Pubmed
title: ERK6, a mitogen-activated protein kinase involved in C2C12 myoblast differentiation
source: Proc Natl Acad Sci U S A 93:4355-9
year: 1996

Evidence767
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16141327
xref: http://identifiers.org/pubmed/7649538
comment: Cytosolic Arginase 1 (ARG1) trimer catalyzes the hydrolysis of arginine to yield ornithine and urea (DiCostanzo et al. 2005). Patients expressing mutated forms of the enzyme with diminished in vitro arginase activity can accumulate arginine to pathogenic levels in the blood (e.g., Uchino et al. 1995).

Evidence766
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/2263616
xref: http://identifiers.org/pubmed/9256435
comment: Cytosolic argininosuccinate lyase (ASL) catalyzes the reversible reaction of argininosuccinate to form fumarate and arginine. The enzyme is a homotetramer (Turner et al. 1997). The function of the human enzyme in vivo is inferred from the defective argininosuccinate lyase enzyme activity observed in patients with mutant forms of the ASL gene (e.g., Walker et al. 1990).

Evidence769
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref1244
comment: The urea cycle yields urea, the major form in which excess nitrogen is excreted from the human body, and the amino acid arginine (Brusilow and Horwich 2001). It consists of four reactions: that of ornithine and carbamoyl phosphate to form citrulline, of citrulline and aspartate to form argininosuccinate, the cleavage of argininosuccinate to yield fumarate and arginine, and the cleavage of arginine to yield urea and re-form ornithine. The carbamoyl phosphate consumed in this cycle is synthesized in the mitochondria from bicarbonate and ammonia, and this synthesis in turn is dependent on the presence of N-acetylglutamate, which allosterically activates carbamoyl synthetase I enzyme. The synthesis of N-acetylglutamate is stimulated by high levels of arginine. Increased levels of free amino acids, indicated by elevated arginine levels, thus stimulate urea synthesis. Two enzymes catalyze the hydrolysis of arginine to yield ornithine and urea. Cytosolic ARG1 is the canonical urea cycle enzyme. Mitochondrial ARG2 likewise catalyzes urea production from arginine and may have a substantial sparing effect in patients lacking ARG1 enzyme, so its reaction is annotated here although the role of ARG2 under normal physiological conditions remains unclear.

Evidence768
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12859189
xref: http://identifiers.org/pubmed/8898077
xref: http://identifiers.org/pubmed/9686347
comment: Arginase 2 (ARG2) trimer catalyzes the hydrolysis of arginine to form urea and ornithine (Cama et al. 2003). ARG2 is localized to the mitochondrion (Gotoh ea 1996). The enzyme is expressed in many tissues in addition to liver and while its function appears to mitigate the effects of ARG1 deficiency on urea synthesis, its normal physiological roles have not been fully defined (Iyer et al. 1998).

Evidence763
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/6249820
comment: At the beginning of this reaction, 1 molecule of 'NH4+', 1 molecule of 'HCO3-', and 1 molecule of 'ATP' are present. At the end of this reaction, 1 molecule of 'Carbamoyl phosphate', 1 molecule of 'ADP', and 1 molecule of 'Orthophosphate' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'carbamoyl-phosphate synthase (ammonia) activity' of 'carbamoyl-phosphate synthetase I dimer'.

Evidence762
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12459178
xref: http://identifiers.org/pubmed/15050968
comment: Mitochondrial N acetylglutamate synthetase (NAGS) catalyzes the reaction of glutamate and acetyl-CoA to form N-acetylglutamate and CoA. NAGS is activated by arginine and the N-acetylglutamate produced in the reaction in turn is required to activate carbamoyl synthetase I. Consistent with this regulatory role in urea synthesis, NAGS mutations in humans are associated with hyperammonemia (Caldovic et al. 2002; Morizono et al. 2004).

Evidence765
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/518841
xref: http://identifiers.org/pubmed/19006241
xref: http://identifiers.org/pubmed/18323623
comment: Cytosolic argininosuccinate synthase catalyzes the reaction of aspartate, citrulline, and ATP to form argininosuccinate, AMP, and pyrophosphate. The function of the human enzyme in vivo is inferred from the hypercitrullinemia observed in patients with defective forms of the enzyme (e.g., Engel et al. 2009). The enzyme is active as a homotetramer (OâBrien 1980; Karlberg et al. 2008).

Evidence764
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/6372096
xref: http://identifiers.org/pubmed/11237854
comment: Mitochondrial ornithine transcarbamoylase (OTC) catalyzes the reaction of ornithine and carbamoyl phosphate to form citrulline (Horwich et al. 1984). The enzyme is a homotrimer (Shi et al. 2001).

http://identifiers.org/pubmed/15153429
type: PublicationXref
id: 15153429
author: Berezin, V
author: Bock, E
author: Kiryushko, D
db: Pubmed
title: Regulators of neurite outgrowth: role of cell adhesion molecules
source: Ann N Y Acad Sci 1014:140-54
year: 2004

UniProt:P00046
type: ProteinReference
xref: UnificationXref2120
organism: BioSource1

Evidence761
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1772073
comment: Tryptophan is catabolized in seven steps to yield aminomuconate. Intermedistes in this process are used as well for the synthesis of serotonin and kynurenine (Peters 1991).

Evidence760
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16376499
comment: CCBL2 (KAT 3) catalyzes the reaction of kynurenine and pyruvate to form 4-(2-aminophenyl)-2,4-dioxobutanoate and alanine. CCBL2 is known only as the predicted protein product of a cloned human gene closely homologous to CCBL1 (Yu et al. 2006) and all of the structural and catalytic properties annotated here are inferred from those of CCBL1.

http://identifiers.org/pubmed/11124962
type: PublicationXref
id: 11124962
author: Wilson, GM
author: Brewer, G
author: Chuang, Ky
author: Sutphen, K
db: Pubmed
title: Folding of A+U-rich RNA elements modulates AUF1 binding. Potential roles in regulation of mRNA turnover
source: J Biol Chem 276:8695-704
year: 2001

Signaling by Wnt
type: Pathway
data source: Provenance1
pathway component: REACT 167633.1
evidence: Evidence279
xref: UnificationXref1466
xref: UnificationXref1467
pathway order: PathwayStep276
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Evidence779
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19620624
comment: Equilibrium between 5'-methylthio ribose-1-phosphate and 5'-methylthio ribulose-1-phosphate is catalyzed by 5'-methylthio ribose-1-phosphate isomerase. (Kabuyama et al, 2009)

Evidence778
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19620624
comment: Equilibrium between 5'-methylthio ribose-1-phosphate and 5'-methylthio ribulose-1-phosphate is catalyzed by 5'-methylthio ribose-1-phosphate isomerase. (Kabuyama et al, 2009)

Evidence777
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3091600
xref: http://identifiers.org/pubmed/6785752
xref: http://identifiers.org/pubmed/22464254
comment: MTA phosphorylase catalyzes the cleavage of adenine from S-methylthioadenosine (MTA) and subsequent phosphorylation of the product, yielding 5'-methylthio ribose-1-phosphate (Kamatani et al. 1981). The active form of the enzyme is a homotrimer (Della Ragione et al. 1985). Mutations in the gene are associated with a rare bone dysplasia and cancer syndrome, DMS-MFH (Camacho-Vanegas et al. 2012).

Evidence776
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/2069720
comment: Spermidine synthase is one of four enzymes in the polyamine-biosynthetic pathway and carries out the final step of spermidine biosynthesis. This enzyme catalyzes the conversion of putrescine to spermidine using decarboxylated S-adenosylmethionine as the cofactor.

Evidence775
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10029540
xref: http://identifiers.org/pubmed/11583147
comment: S-Adenosylmethionine decarboxylase belongs to a small class of amino acid decarboxylases that use a covalently bound pyruvate as a prosthetic group. It is an essential enzyme for polyamine biosynthesis and provides an important target for the design of anti-parasitic and cancer chemotherapeutic agents. It catalyzes the formation of the aminopropyl group donor in the biosynthesis of the polyamines spermidine and spermine. These pyruvoyl-dependent decarboxylases also form amines such as histamine, decarboxylated S-adenosylmethionine, phosphatidylethanolamine (a component of membrane phospholipids), and -alanine (a precursor of coenzyme A), which are all of critical importance in cellular physiology and provide important targets for drug design.

Evidence774
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref1185
comment: L-ornithine is converted into putrescine by ODC holoenzyme complex.Putrescine is subsequent used for polyamine synthesis.

Evidence773
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17025265
xref: http://identifiers.org/pubmed/15784477
xref: http://identifiers.org/pubmed/15028568
xref: http://identifiers.org/pubmed/15028567
comment: Agmatine is an amine that is formed by decarboxylation of L-arginine by the enzyme arginine decarboxylase (ADC) and hydrolyzed by the enzyme agmatinase to putrescine. Agmatine binds to several target receptors in the brain and has been proposed as a novel neuromodulator (Reghunathan 2006). Agmatine has the potential to serve in the coordination of the early and repair phase pathways of arginine in inflammation (Satriano, 2003).

Evidence772
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/14738999
comment: Agmatine is polyamine formed by decarboxylation of L-arginine by arginine decarboxylase (ADC). Human ADC is a 460-amino acid protein that shows about 48% identity to mammalian ornithine decarboxylase (ODC) but has no ODC activity.

Evidence771
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9706223
comment: Carnitine is synthesized in four steps from trimethyllysine (generated in turn by the S-adenosyl-methionine-mediated methylation of lysine residues in proteins, followed by protein hydrolysis). The enzymes that catalyze the first three steps of carnitine synthesis, converting trimethyllysine to gamma-butyrobetaine, are widely distributed in human tissues. The enzyme that catalyzes the last reaction, converting gamma-butyrobetaine to carnitine, is found only in liver and kidney cells, and at very low levels in brain tissues. Other tissues that require carnitine, such as muscle, are dependent on transport systems that mediate its export from the liver and uptake by other tissues (Kerner and Hoppel 1998).

Evidence770
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10702312
xref: http://identifiers.org/pubmed/2925663
comment: Cytosolic 4-trimethylaminobutyraldehyde dehydrogenase tetramer (ALDH9A1) catalyzes the reaction of NAD+', and 4-trimethylammoniobutanal to form 4-Trimethylammoniobutanoate and NADH + H+ (Kurys et al. 1989; Vaz et al. 2000).

http://identifiers.org/pubmed/20861159
type: PublicationXref
id: 20861159
author: Nilius, B
author: Colsoul, B
author: Gees, M
db: Pubmed
title: The role of transient receptor potential cation channels in Ca2+ signaling
source: Cold Spring Harb Perspect Biol 2:a003962
year: 2010

Evidence745
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17371050
comment: Mitochondrial acetyl-CoA acetyltransferase (ACAT1) catalyzes the reaction of alpha-methyl-acetoacetyl-CoA and CoA to form propionyl-CoA and acetyl-CoA. Structural studies have shown the active enzyme to be a tetramer of ACAT1 polypeptides whose aminoterminal 34 residues, a mitochondrial targeting sequence, have been removed (Haapalainen et al. 2007).

2,6-diaminohexanoic acid
type: SmallMoleculeReference
name: Lysine acid
name: L-Lysine [ChEBI:18019]
name: L-Lysine
xref: UnificationXref4927

Evidence744
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12269802
xref: http://identifiers.org/pubmed/11264579
xref: http://identifiers.org/pubmed/9165094
comment: Mitochondrial branched-chain-amino-acid aminotransferase (BCAT2) catalyzes the reversible reactions of alpha-ketoisocaproate, alpha-keto-beta-methylvalerate, or a-ketoisovalerate with glutamate to form leucine, isoleucine, or valine, respectively, and alpha-ketoglutarate (Bledsoe et al. 1997). The active enzyme is a homodimer (Yennawar et al. 2001, 2002). In the body, this enzyme is widely expressed but is especially abundant in muscle tissue.

Evidence747
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref1209
xref: PublicationXref1210
comment: The branched-chain amino acids, leucine, isoleucine, and valine, are all essential amino acids (i.e., ones required in the diet). They are major constituents of muscle protein. The breakdown of these amino acids starts with two common steps catalyzed by enzymes that act on all three amino acids: reversible transamination by branched-chain amino acid aminotransferase, and irreversible oxidative decarboxylation by the branched-chain ketoacid dehydrogenase complex. Isovaleryl-CoA is produced from leucine by these two reactions, alpha-methylbutyryl-CoA from isoleucine, and isobutyryl-CoA from valine. These acyl-CoA's undergo dehydrogenation, catalyzed by three different but related enzymes, and the breakdown pathways then diverge. Leucine is ultimately converted to acetyl-CoA and acetoacetate; isoleucine to acetyl-CoA and succinyl-CoA; and valine to succinyl-CoA. Under fasting conditions, substantial amounts of all three amino acids are generated by protein breakdown. In muscle, the final products of leucine, isoleucine, and valine catabolism can be fully oxidized via the citric acid cycle; in liver they can be directed toward the synthesis of ketone bodies (acetoacetate and acetyl-CoA) and glucose (succinyl-CoA) (Chuang & Shih 2001, Sweetman & Williams 2001).

Evidence746
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8824301
comment: Mitochondrial 3-hydroxyisobutyryl-CoA hydrolase (HIBCH) catalyzes the hydrolysis of beta-hydroxyisobutyryl-CoA to form beta-hydroxyisobutyrate (3-hydroxy-2-methylpropanoate) and CoA (Hawes et al. 1996).

Evidence749
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10775527
xref: http://identifiers.org/pubmed/6434529
comment: The saccharopine dehydrogenase activity of lysine-ketoglutarate reductase / saccharopine dehydrogenase homotetramer in the mitochondrial matrix catalyzes the reaction of saccharopine (N6-(L-1,3-Dicarboxypropyl)-L-lysine), H2O, and NAD+ to form 'L-2-Aminoadipate 6-semialdehyde, glutamate, and NADH + H+ (Markovitz et al. 1984; Sacksteder et al. 2001).

Evidence748
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10775527
xref: http://identifiers.org/pubmed/6434529
comment: The saccharopine dehydrogenase activity of lysine-ketoglutarate reductase / saccharopine dehydrogenase homotetramer in the mitochondrial matrix catalyzes the reaction of lysine, alpha-ketoglutarate, and NADPH + H+ to form saccharopine, NADP+, and H2O (Markovitz et al. 1984; Sacksteder et al. 2001).

Fumaric acid
type: SmallMoleculeReference
name: ChEBI:18012 Fumaric acid
name: Trans-butenedioic acid
xref: UnificationXref3969

Evidence741
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16141215
comment: Cytosolic branched-chain-amino-acid aminotransferase (BCAT1) catalyzes the reversible reactions of leucine, isoleucine, or valine with alpha-ketoglutarate (2-oxoglutarate) to form alpha-ketoisocaproate, alpha-keto-beta-methylvalerate, or a-ketoisovalerate, respectively, and glutamate. The active enzyme is a homodimer. Hutson and colleagues have argues that cytosolic BCAT1 plays a major role in the generation of glutamate involved in synaptic transmission in neural tissue (Goto et al. 2005).

Evidence740
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: These reactions mediate the synthesis of aspartate, asparagine, glutamate, and glutamine from ammonia and intermediates of glycolysis, and allow the utilization of the carbon atoms from these four amino acids for glucose synthesis under fasting conditions. These reactions also provide a means to collect nitrogen, both as ammonia and as amino groups, and direct it towards urea synthesis. Transamination, the conversion of an amino acid to the corresponding alpha-keto acid coupled to the conversion of a molecule of alpha-ketoglutarate to glutamate, is the first step in the catabolism of most amino acids. Transamination reactions are freely reversible so they also provide a means to balance concentrations of various amino acids and alpha-keto (2-oxo) acids in the cytosol.

Evidence743
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12269802
xref: http://identifiers.org/pubmed/11264579
xref: http://identifiers.org/pubmed/9165094
comment: Mitochondrial branched-chain-amino-acid aminotransferase (BCAT2) catalyzes the reversible reactions of leucine, isoleucine, or valine with alpha-ketoglutarate (2-oxoglutarate) to form alpha-ketoisocaproate, alpha-keto-beta-methylvalerate, or a-ketoisovalerate, respectively, and glutamate (Bledsoe et al. 1997). The active enzyme is a homodimer (Yennawar et al. 2001, 2002). In the body, this enzyme is widely expressed but is especially abundant in muscle tissue.

Evidence742
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16141215
comment: Cytosolic branched-chain-amino-acid aminotransferase (BCAT1) catalyzes the reversible reactions of alpha-ketoisocaproate, alpha-keto-beta-methylvalerate, or a-ketoisovalerate with glutamate to form leucine, isoleucine, or valine, respectively, and alpha-ketoglutarate (2-oxoglutarate). The active enzyme is a homodimer (Goto et al. 2005).

http://identifiers.org/pubmed/17555404
type: PublicationXref
id: 17555404
author: Alp, NJ
author: Schmidt, TS
db: Pubmed
title: Mechanisms for the role of tetrahydrobiopterin in endothelial function and vascular disease
source: Clin Sci (Lond) 113:47-63
year: 2007

Evidence758
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref1190
comment: Proline is catabolized in two steps to yield L-glutamate gamma-semialdehyde, which can react further with glutamate to yield ornithine and alpha-ketoglutarate (annotated as a reaction of amino acid synthesis and interconversion) or with NAD+ to yield glutamate and NADH + H+ (Phang et al. 2001).

Evidence757
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3944130
xref: http://identifiers.org/pubmed/9700195
xref: http://identifiers.org/pubmed/8621661
comment: Mitochondrial delta-1-pyrroline-5-carboxylate dehydrogenase (ALDH4A1) catalyzes the reaction of L-glutamate gamma-semialdehyde and NAD+ to form glutamate and NADH + H+ (Hu et al. 1996). The enzyme is a dimer (Forte-McRobbie and Pietruszko 1986). ALDH4A1 mutations cause type II hyperprolinemia in vivo (Geraghty et al. 1998).

NADP+
type: SmallMoleculeReference
name: TPN
name: NADP+ [ChEBI:18009]
name: beta-Nicotinamide adenine dinucleotide phosphate
name: Nicotinamide adenine dinucleotide phosphate
name: Triphosphopyridine nucleotide
name: NADP
xref: UnificationXref1485

Evidence756
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15662599
comment: The dehydrogenation of proline to L-1-pyrroline-5-carboxylate coupled to the conversion of FAD to FADH2 is the first step in proline breakdown (Bender et al. 2005). Proline dehydrogenase (PRODH), the enzyme that catalyzes this reaction, is found in liver, kidney, and brain cells, where it is tightly bound to the inner mitochondrial membrane.

Evidence755
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref1221
xref: PublicationXref1220
comment: The first reaction in this pathway converts phenylalanine to tyrosine, coupled to the conversion of tetrahydrobiopterin to 4a-hydroxytetrahydrobiopterin, catalyzed by phenylalanine hydroxylase. (Deficiencies in this enzyme are responsible for the commonest form of phenylketonuria (PKU) in humans.) This reaction functions both as the first step in the pathway by which the body disposes of excess phenylalanine, and as a source of the amino acid tyrosine. The next two reactions are responsible for the regeneration of tetrahydrobiopterin from 4a-hydroxytetrahydrobiopterin. The following five reactions convert tyrosine to fumarate, an intermediate in the citric acid cycle, and acetoacetate, a ketone body.

3-phenyl-2-oxopropanoate
type: SmallMoleculeReference
name: keto-phenylpyruvate
name: keto-phenylpyruvate [ChEBI:18005]
name: 3-(4-hydroxyphenyl)pyruvate
xref: UnificationXref6956

Evidence759
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/13069505
xref: http://identifiers.org/pubmed/7883047
xref: http://identifiers.org/pubmed/15364907
xref: http://identifiers.org/pubmed/8294935
xref: http://identifiers.org/pubmed/19338303
comment: CCBL1 (KAT 1) catalyzes the reaction of kynurenine and pyruvate to form 4-(2-aminophenyl)-2,4-dioxobutanoate and alanine. The active form of CCBL1 is a homodimer with one molecule of pyridoxal phosphate bound to each monomer (Baran et al. 1994; Han et al. 2009; Rossi et al. 2004). The enzyme's cytosolic localization is inferred from that of recombinant protein overexpressed in transfected cells (Perry et al. 1995). The pH optimum observed for CCBL1 in vitro is 9.5 - 10.0, so its role in kynurenine metabolism in vivo is not clear (Baran et al. 1994). Biochemical studies of CCBL1 activity in vitro (e.g., Baren et al. 1994) invariably measure kynurenic acid as the reaction product, not 4-(2-aminophenyl)-2,4-dioxobutanoate, the product to be expected from transamination of kynurenine. The condensation of 4-(2-aminophenyl)-2,4-dioxobutanoate and elimination of a water molecule to form kynurenic acid has not been demonstrated directly. As noted by Miller et al. (1953), discussing their characterization of a bacterial form of the enzyme, "The keto acid assumed to be formed prior to ring closure in the conversion of kynurenine to kynurenic acid has not yet been detected. In principle, such detection should be possible, since it is sufficiently stable to have been synthesized. It also remains to be established whether ring closure is spontaneous, enzymatic, or both. The formation of kynurenic acid from L-kynurenine by the L-amino acid oxidase of Neurospora suggests, however, that ring closure can be spontaneous, unless the somewhat improbable assumption is made that Neurospora filtrate contained the ring-closing enzyme."

Evidence750
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11083877
comment: SLC25A21, the mitochondrial 2-oxodicarboxylate carrier, mediates the exchange of 2-oxoadipate and 2-oxoglutarate across the inner mitochondrial membrane. While the exchange is reversible, under physiological conditions it proceeds in the direction of 2-oxoadipate import into the mitochondrial matrix and 2-oxoglutarate export (Fiermonte et al. 2001).

Evidence754
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8444860
xref: http://identifiers.org/pubmed/7744010
xref: http://identifiers.org/pubmed/8352282
comment: Cytosolic pterin-4-alpha-carbinolamine dehydratase (PCDB1) catalyzes the reaction of 4a-hydroxytetrahydrobiopterin to form q-dihydrobiopterin and water (Hauer et al. 1993. The active enzyme is a homotetramer (Ficner et al. 1995); mutations in the PCDB1 gene are associated with mild hyperphenylalanemia in vivo (Citron et al. 1993).

Evidence753
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7883047
xref: http://identifiers.org/pubmed/15364907
xref: http://identifiers.org/pubmed/8294935
xref: http://identifiers.org/pubmed/19338303
comment: CCBL1 (KAT 1) catalyzes the reaction of phenylalanine and pyruvate to form 3-(indol-3-yl)pyruvate and alanine. The active form of CCBL1 is a homodimer with one molecule of pyridoxal phosphate bound to each monomer (Baran et al. 1994; Han et al. 2009; Rossi et al. 2004). The enzyme's cytosolic localization is inferred from that of recombinant protein overexpressed in transfected cells (Perry et al. 1995).

Evidence752
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref1216
xref: http://identifiers.org/pubmed/12126930
xref: PublicationXref1214
xref: http://identifiers.org/pubmed/6434529
comment: In humans, most catabolism of L-lysine normally proceeds via a sequence of seven reactions which feeds into the pathway for fatty acid catabolism. In the first two reactions, catalyzed by a single enzyme complex, lysine is combined with alpha-ketoglutarate to form saccharopine, which in turn is cleaved and oxidized to yield glutamate and alpha-ketoadipic semialdehyde. The latter molecule is further oxidized to alpha-ketoadipate. Alpha-ketoadipate is oxidatively decarboxylated by the alpha-ketoglutarate dehydrogenase complex (the same enzyme complex responsible for the conversion of alpha-ketoglutarate to succinyl-CoA in the citric acid cycle), yielding glutaryl-CoA. Glutaryl-CoA is converted to crotonyl-CoA, crotonyl-CoA is converted to beta-hydroxybutyryl-CoA, and beta-hydroxybutyryl-CoA is converted to acetoacetyl-CoA. The products of lysine catabolism are thus exclusively ketogenic; i.e., under starvation conditions they can be used for the synthesis of ketone bodies, beta-hydroxybutyrate and acetoacetate, but not for the net synthesis of glucose (Cox 2001; Goodman and Freeman 2001).

Evidence751
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11752427
xref: http://identifiers.org/pubmed/2188967
xref: http://identifiers.org/pubmed/9727038
xref: http://identifiers.org/pubmed/15946682
comment: The mitochondrial alpha-ketoglutarate dehydrogenase complex catalyzes the reaction of alpha-ketoadipate, CoASH, and NAD+ to form glutaryl-CoA, CO2, and NADH. The enzyme complex contains multiple copies of three different proteins, E1 (OGDH), E2 (DLST), and E3 (DLD), each with distinct catalytic activities (Reed and Hackert 1990; Zhou et al 2001). The reaction starts with the oxidative decarboxylation of alpha-ketoadipate catalyzed by E1alpha and beta (alpha ketoglutarate dehydrogenase). Lipoamide cofactor associated with E1 is reduced at the same time. Next, the glutaryl group derived from alpha ketoglutarate is transferred to coenzyme A in two steps catalyzed E2 (dihydrolipolyl transacetylase). Finally, the oxidized form of lipoamide is regenerated and electrons are transferred to NAD+ in two steps catalyzed by E3 (dihydrolipoyl dehydrogenase). The biochemical details of this reaction have been worked out with alpha ketoglutarate dehydrogenase complex and subunits purified from bovine tissue (McCartney et al. 1998). While all of the human proteins are known as predicted protein products of cloned genes, direct experimental evidence for their functions is available only for E3 (DLD) (Brautigam et al. 2005).

UnificationXref6455
type: UnificationXref
id: 205683
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=205683

UnificationXref6456
type: UnificationXref
id: REACT_22654
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22654.2

UnificationXref6453
type: UnificationXref
id: 742368
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=742368

UnificationXref6454
type: UnificationXref
id: REACT_23055
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_23055.2

UnificationXref6451
type: UnificationXref
id: REACT_129261
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_129261.5

UnificationXref6452
type: UnificationXref
id: CHEBI:17009
db: ChEBI

UnificationXref6450
type: UnificationXref
id: 3663322
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663322

UnificationXref6459
type: UnificationXref
id: 3663316
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663316

http://identifiers.org/pubmed/15893380
type: PublicationXref
id: 15893380
author: Jackowski, S
author: Zhang, YM
author: Rock, CO
author: Leonardi, R
db: Pubmed
title: Coenzyme A: back in action
source: Prog Lipid Res 44:125-53
year: 2005

UnificationXref6457
type: UnificationXref
id: Q9UUI8
db: UniProt

UnificationXref6458
type: UnificationXref
id: 3663314
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663314

http://identifiers.org/pubmed/9083049
type: PublicationXref
id: 9083049
author: Lee, PT
author: Shepherd, JA
author: Tzagoloff, A
author: Myles, DC
author: Clarke, CF
author: Shtanko, A
author: Barkovich, RJ
db: Pubmed
title: Characterization of the COQ5 gene from Saccharomyces cerevisiae. Evidence for a C-methyltransferase in ubiquinone biosynthesis
source: J Biol Chem 272:9182-8
year: 1997

UnificationXref6464
type: UnificationXref
id: REACT_129013
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_129013.5

UnificationXref6465
type: UnificationXref
id: 3665079
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665079

UnificationXref6466
type: UnificationXref
id: REACT_89376
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_89376.9

UnificationXref6467
type: UnificationXref
id: Q9P7T9
db: UniProt

UnificationXref6460
type: UnificationXref
id: REACT_134390
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_134390.5

UnificationXref6461
type: UnificationXref
id: 3665509
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665509

UnificationXref6462
type: UnificationXref
id: REACT_143408
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_143408.5

UnificationXref6463
type: UnificationXref
id: 3665508
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665508

UnificationXref6468
type: UnificationXref
id: 3662943
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662943

UnificationXref6469
type: UnificationXref
id: 3662944
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662944

http://identifiers.org/pubmed/21682741
type: PublicationXref
id: 21682741
author: Minnicozzi, M
author: Fenton, MJ
author: Sawyer, RT
db: Pubmed
title: Innate immunity in allergic disease
source: Immunol Rev 242:106-27
year: 2011

UnificationXref6470
type: UnificationXref
id: 3662810
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662810

Evidence782
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17786183
comment: Acireducone (1,2-Dihydroxy-3-oxo-5'-methylthiopentene) is oxidized using acireductone dioxygenase and dioxygen. There are two reactions possible, dependent on the metal cofactor: the alternative product 3-methylthiopropionate using nickel was confirmed in Klebsiella. In eukaryotes using iron(II) the result is 4-methylthio-2-oxobutanoate (MOB). (Ju et al, 2006)

Evidence783
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11443076
comment: In the last step MOB gets transaminated to methionine. The reaction was confirmed in yeast, where several transaminases catalyze it, which appears to be also the case in rat. At the moment, the human enzymes involved are unknown but due to homology to the respective enzyme in the parasite Crithidia fasciculata we feel supported to state that human GOT is probably one of the involved transaminases. (Berger et al, 2001)

UnificationXref6430
type: UnificationXref
id: 727815
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=727815

Evidence780
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: The human enzyme with 5'-methylthio ribulose-1-phosphate isomerase activity is probably produced from the APIP gene, according to its orthology with the yeast Mde1p enzyme.

Evidence781
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15843022
comment: Acireductone synthase (also: enolase-phosphatase E1) catalyzes the dephosphorylation and conversion to enolate of 2,3-dioxo-5'-methylthiopentane-1-phosphate, yielding acireductone. (Wang et al, 2005)

Evidence786
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17088322
xref: http://identifiers.org/pubmed/16616139
comment: Peroxisomal D-amino-acid oxidase catalyzes the reaction of glycine, water, and O2 to form glyoxylate, H2O2, and NH4+. The active form of the enzyme is a homodimer and has FAD as a cofactor (Kawazoe et al. 2006; Molla et al. 2006).

UnificationXref6433
type: UnificationXref
id: 3663308
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663308

Evidence787
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15956068
comment: Glyoxylate is generated in the course of glycine and hydroxyproline catabolism and can be converted to oxalate. In humans, this process takes place in the liver. Defects in two enzymes of glyoxylate metabolism, alanine:glyoxylate aminotransferase (AGXT) and glycerate dehydrogenase/glyoxylate reductase (GRHPR), are associated with pathogenic overproduction of oxalate (Danpure 2005). The reactions that interconvert glycine, glycolate, and glyoxylate and convert glyoxylate to oxalate have been characterized in molecular detail in humans. A reaction sequence for the conversion of hydroxyproline to glyoxylate has been inferred from studies of partially purified extracts of rat and bovine liver but the enzymes involved in the corresponding human reactions have not been identified.

UnificationXref6434
type: UnificationXref
id: 3663310
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663310

Evidence784
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19946895
xref: http://identifiers.org/pubmed/18625006
comment: Methionine salvage is a sequential pathway of six reactions that create methionine from 5'-methylthioadenosine (MTA) which is a byproduct of polyamine biosynthesis in nearly all organisms. The process happens completely in the cytosol. It is important in humans for recycling of sulphur that has to be assimilated using energy. (Pirkov et al, 2008; Albers, 2009)

UnificationXref6431
type: UnificationXref
id: REACT_22966
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22966.2

Evidence785
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15784477
xref: http://identifiers.org/pubmed/12686127
xref: http://identifiers.org/pubmed/11564948
comment: Polyamines is a family of molecules (i.e. putrescine, spermine, spermidine) derived from ornithine according to a decarboxylation/condensative process. More recently, it has been demonstrated that arginine can be metabolised according to the same pathway leading to agmatine formation. Polyamines are essential for the growth, the maintenance and the function of normal cells. The complexity of their metabolism and the fact that polyamines homeostasis is tightly regulated support the idea that polyamines are essential to cell survival. Multiple abnormalities in the control of polyamines metabolism might be implicated in several pathological processes (Moinard et al., 2005). Legend for the following figure:

UnificationXref6432
type: UnificationXref
id: P87041
db: UniProt

UnificationXref6437
type: UnificationXref
id: 742353
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=742353

UnificationXref6438
type: UnificationXref
id: REACT_22644
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22644.2

Evidence788
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9175157
xref: http://identifiers.org/pubmed/12163696
comment: S-adenosylmethionine (SAM) is an essential metabolite in all cells. SAM is a precursor in the synthesis of polyamines. Methionine adenosyltransferase (MAT; EC 2.5.1.6) catalyzes the only known SAM biosynthetic reaction from methionine and ATP. In mammalian tissues, three different forms of MAT (MAT I, MAT III and MAT II) have been identified that are the product of two different genes (MAT1A and MAT2A). A third gene MAT2B has been identified and is known to be a part of MAT II heterotetramer complex.

UnificationXref6435
type: UnificationXref
id: REACT_156861
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_156861.3

Evidence789
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: At the beginning of this reaction, 1 molecule of 'S-adenosylhomocysteine', and 1 molecule of 'H2O' are present. At the end of this reaction, 1 molecule of 'adenosine', and 1 molecule of 'Homocysteine' are present. This reaction takes place in the 'cytosol' and is mediated by the 'adenosylhomocysteinase activity' of 'SAH hydrolase homotetramer'.

UnificationXref6436
type: UnificationXref
id: CHEBI:16082
db: ChEBI

UnificationXref6439
type: UnificationXref
id: 742361
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=742361

http://identifiers.org/pubmed/12438414
type: PublicationXref
id: 12438414
author: Michael, WM
author: Van Hatten, RA
author: Holway, AH
author: Tutter, AV
author: Khederian, AM
author: Walter, JC
db: Pubmed
title: The Xenopus Xmus101 protein is required for the recruitment of Cdc45 to origins of DNA replication.
source: J Cell Biol 159:541-7
year: 2002

UniProt:Q10101
type: ProteinReference
xref: UnificationXref1892
organism: BioSource1

Evidence790
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10212249
xref: http://identifiers.org/pubmed/19261609
comment: Cystathionine is cleaved to cysteine, oxobutanoate, and ammonia by the alpha,gamma-elimination activity of cystathionine gamma-lyase (CTH) (Chiku et al. 2009, Steegborn et al. 1999).

Evidence791
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15497768
xref: http://identifiers.org/pubmed/20817827
comment: Transsulfuration is the interconversion of homocysteine and cysteine, and it fully takes place in bacteria and some plants and fungi. Animals however have only one direction of this bidirectional path, the synthesis of cysteine from homocysteine via cystathionine. Because excess cysteine is degraded to hydrogen sulfide, which is now known as a neuromodulator and smooth muscle relaxant, this pathway is also the main source of its production, which takes place in the cytosol, as well as in extracellular space (Dominy & Stipanuk 2004, Bearden et al. 2010).

Evidence792
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7826375
xref: http://identifiers.org/pubmed/9675072
comment: The first step in the formation of glutathione is the ligation of glutamate with cysteine, catalyzed by the dimeric protein glutamate-cysteine ligase (Gipp et al, 1995; Misra and Griffith, 1998).

Evidence793
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12473676
comment: A cytosolic, non-specific peptidase can hydrolyze cysteinylglycine to release cysteine and glycine (Tuefel et al, 2003).

UnificationXref6440
type: UnificationXref
id: REACT_22899
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22899.2

Evidence794
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10212249
xref: http://identifiers.org/pubmed/19261609
comment: Excess homocysteine will change the enzymatic activity of CBS such that other reactions than transsulfuration take place. In these reactions, oxobutanoate, lanthionine, and homolanthionine are produced by cystathionine gamma-lyase (CTH) (Chiku et al. 2009, Steegborn et al. 1999)

UnificationXref6441
type: UnificationXref
id: O74750
db: UniProt

Evidence795
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10212249
xref: http://identifiers.org/pubmed/19261609
comment: alpha,beta-elimination activity of cystathionine-gamma-lyase (CTH) replaces the sulfur in cysteine with oxygen from water, resulting in serine and toxic hydrogen sulfide, which is further oxidized in mitochondria (Chiku et al. 2009, Steegborn et al. 1999).

UnificationXref6442
type: UnificationXref
id: 3663320
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663320

Evidence796
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10212249
xref: http://identifiers.org/pubmed/19261609
comment: Excess homocysteine will change the enzymatic activity of CBS such that other reactions than transsulfuration take place. In these reactions, oxobutanoate, lanthionine, and homolanthionine are produced by cystathionine gamma-lyase (CTH) (Chiku et al. 2009, Steegborn et al. 1999)

UnificationXref6443
type: UnificationXref
id: 3663324
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663324

Evidence797
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10212249
xref: http://identifiers.org/pubmed/19261609
comment: Excess homocysteine will change the enzymatic activity of CBS such that other reactions than transsulfuration take place. In these reactions, oxobutanoate, lanthionine, and homolanthionine are produced by cystathionine gamma-lyase (CTH) (Chiku et al. 2009, Steegborn et al. 1999)

UnificationXref6444
type: UnificationXref
id: REACT_142511
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_142511.5

Evidence798
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12832624
xref: http://identifiers.org/pubmed/18494801
comment: When SQR is in the oxidized state, it can bind hydrogen sulfide as persulfide to one of its own cysteine residue, the electrons being transferred to ubiquinone. After that the additional sulfur is dioxygenated by another enzyme (ETHE1). The activity of human SQR was deduced from the orthologue in Arenicola marina (Theissen et al. 2003, Hildebrandt & Grieshaber 2008).

UnificationXref6445
type: UnificationXref
id: CHEBI:16264
db: ChEBI

Evidence799
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18494801
comment: The main reaction catalyzed by rhodanase is not the name-giving detoxification of cyanide to thiocyanate, but the transfer of a sulfur atom from SQR-S-SH onto sulfite yielding thiosulfate during sulfide oxidation. The activity of human rhodanase was inferred from the rat orthologue by Hildebrandt & Grieshaber, 2008.

UnificationXref6446
type: UnificationXref
id: 741437
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=741437

UnificationXref6447
type: UnificationXref
id: REACT_22968
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22968.1

UnificationXref6448
type: UnificationXref
id: 914003
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=914003

UnificationXref6449
type: UnificationXref
id: REACT_26828
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_26828.2

Import of palmitoyl-CoA into the mitochondrial matrix
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction214
evidence: Evidence423
xref: UnificationXref2814
xref: UnificationXref2815
xref: RelationshipXref245
pathway order: PathwayStep414
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/19428801
type: PublicationXref
id: 19428801
author: Buddhala, C
author: Wu, Jer-Yuarn
author: Hsu, CC
db: Pubmed
title: A novel mechanism for GABA synthesis and packaging into synaptic vesicles
source: Neurochem Int 55:9-12
year: 2009

http://identifiers.org/pubmed/11752427
type: PublicationXref
id: 11752427
author: McCarthy, DB
author: Stoops, JK
author: O'Connor, CM
author: Reed, LJ
author: Zhou, ZH
db: Pubmed
title: The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes.
source: Proc Natl Acad Sci U S A 98:14802-7
year: 2001

http://identifiers.org/pubmed/16854592
type: PublicationXref
id: 16854592
author: Wu, Y
author: Feder, JN
author: Cheng, D
author: Mintier, GA
author: Tamura, JK
author: Chu, CH
author: Harpel, MR
author: Locke, GA
author: An, Y
author: Cook, JW
author: Chen, L
db: Pubmed
title: Expression, purification, and characterization of human and rat acetyl coenzyme A carboxylase (ACC) isozymes
source: Protein Expr Purif 51:11-21
year: 2007

UnificationXref6419
type: UnificationXref
id: 727753
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=727753

UnificationXref6418
type: UnificationXref
id: REACT_128889
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_128889.5

UnificationXref6417
type: UnificationXref
id: 3665482
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665482

CHEBI:71956
type: SmallMoleculeReference
name: CHEBI:71956 [ChEBI:71956]
xref: UnificationXref6890

UnificationXref6416
type: UnificationXref
id: REACT_145297
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_145297.5

UnificationXref6415
type: UnificationXref
id: 3665486
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665486

UnificationXref6414
type: UnificationXref
id: REACT_144433
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_144433.5

UnificationXref6413
type: UnificationXref
id: 3662871
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662871

UnificationXref6412
type: UnificationXref
id: 3662869
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662869

UnificationXref6411
type: UnificationXref
id: Q9USV7
db: UniProt

UnificationXref6410
type: UnificationXref
id: REACT_20939
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20939.2

http://identifiers.org/pubmed/10411507
type: PublicationXref
id: 10411507
author: McGarry, TJ
author: Zou, H
author: Bernal, T
author: Kirschner, MW
db: Pubmed
title: Identification of a vertebrate sister-chromatid separation inhibitor involved in transformation and tumorigenesis
source: Science 285:418-22
year: 1999

http://identifiers.org/pubmed/9593753
type: PublicationXref
id: 9593753
author: Jackowski, S
author: Lykidis, A
author: Murti, KG
db: Pubmed
title: Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase
source: J Biol Chem 273:14022-9
year: 1998

UnificationXref6429
type: UnificationXref
id: REACT_22669
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22669.2

UnificationXref6428
type: UnificationXref
id: 727803
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=727803

UnificationXref6425
type: UnificationXref
id: 727810
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=727810

UnificationXref6424
type: UnificationXref
id: REACT_127597
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_127597.5

UnificationXref6427
type: UnificationXref
id: CHEBI:16556
db: ChEBI

UnificationXref6426
type: UnificationXref
id: REACT_22895
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22895.2

UnificationXref6421
type: UnificationXref
id: Q9USW4
db: UniProt

UnificationXref6420
type: UnificationXref
id: REACT_23184
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_23184.2

UnificationXref6423
type: UnificationXref
id: 3663304
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663304

UnificationXref6422
type: UnificationXref
id: 3663302
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663302

UnificationXref6403
type: UnificationXref
id: REACT_126830
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_126830.5

UnificationXref6402
type: UnificationXref
id: 3665484
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665484

UnificationXref6405
type: UnificationXref
id: REACT_93104
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_93104.9

UnificationXref6404
type: UnificationXref
id: 3665485
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665485

UnificationXref6407
type: UnificationXref
id: 437295
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=437295

UniProt:Q9C106
type: ProteinReference
xref: UnificationXref685
organism: BioSource1

UnificationXref6406
type: UnificationXref
id: CHEBI:29036
db: ChEBI

UnificationXref6409
type: UnificationXref
id: 209799
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=209799

UniProt:Q9C104
type: ProteinReference
xref: UnificationXref3266
organism: BioSource1

UnificationXref6408
type: UnificationXref
id: REACT_21200
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21200.2

UnificationXref6401
type: UnificationXref
id: REACT_130232
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_130232.5

UnificationXref6400
type: UnificationXref
id: 3662862
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662862

UnificationXref6005
type: UnificationXref
id: 3657634
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657634

UnificationXref6004
type: UnificationXref
id: 3657632
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657632

UnificationXref6003
type: UnificationXref
id: REACT_3288
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3288.1

UnificationXref6002
type: UnificationXref
id: 68422
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=68422

UnificationXref6001
type: UnificationXref
id: REACT_108209
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_108209.9

UnificationXref6000
type: UnificationXref
id: 3665038
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665038

UnificationXref6009
type: UnificationXref
id: REACT_5885
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5885.1

UnificationXref6008
type: UnificationXref
id: 30185
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=30185

UnificationXref6007
type: UnificationXref
id: CHEBI:16311
db: ChEBI

UnificationXref6006
type: UnificationXref
id: REACT_102769
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_102769.9

http://identifiers.org/pubmed/15157936
type: PublicationXref
id: 15157936
author: Bertinato, J
author: L'Abbé, MR
db: Pubmed
title: Maintaining copper homeostasis: regulation of copper-trafficking proteins in response to copper deficiency or overload
source: J Nutr Biochem 15:316-22
year: 2004

ATP6V1C1
type: Protein
entity reference: Q9HDW6
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1169
feature: FragmentFeature188
cellular location: GO:0005829
comment: Reactome DB_ID: 3659697
display name: Q9HDW6

ATP6V1C
type: Protein
data source: Provenance1
member physical entity: ATP6V1C1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1171
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659699

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43046
data source: Provenance1
name: ATP6V1F
xref: UnificationXref1167
feature: FragmentFeature187
cellular location: GO:0005829
comment: Reactome DB_ID: 3659713
display name: O43046

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P31411
data source: Provenance1
name: ATP6V1B2
xref: UnificationXref1174
feature: FragmentFeature191
cellular location: GO:0005829
comment: Reactome DB_ID: 3659691
display name: P31411

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P31411
data source: Provenance1
name: ATP6V1B1
xref: UnificationXref1173
feature: FragmentFeature190
cellular location: GO:0005829
comment: Reactome DB_ID: 3659690
display name: P31411

ATP6V1B
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1175
cellular location: GO:0005829
comment: Reactome DB_ID: 3659692
comment: Converted from EntitySet in Reactome

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9HDW6
data source: Provenance1
name: ATP6V1C2
xref: UnificationXref1170
feature: FragmentFeature189
cellular location: GO:0005829
comment: Reactome DB_ID: 3659698
display name: Q9HDW6

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O13687
data source: Provenance1
name: ATP6V1E2
xref: UnificationXref1179
feature: FragmentFeature193
cellular location: GO:0005829
comment: Reactome DB_ID: 3659708
display name: O13687

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O13687
data source: Provenance1
name: ATP6V1E1(2-226)
name: ATP6V1E1
xref: UnificationXref1178
feature: FragmentFeature192
cellular location: GO:0005829
comment: Reactome DB_ID: 3659707
display name: O13687

ATP6V1E
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1180
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659709

http://identifiers.org/pubmed/20147624
type: PublicationXref
id: 20147624
author: Pellegrini-Calace, M
author: Oliva, R
author: Calamita, G
author: Thornton, JM
db: Pubmed
title: Electrostatics of aquaporin and aquaglyceroporin channels correlates with their transport selectivity
source: Proc Natl Acad Sci U S A 107:4135-40
year: 2010

Uroporphyrinogen I
type: SmallMoleculeReference
name: Uroporphyrinogen I [ChEBI:9904]
xref: UnificationXref5347

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O59823
data source: Provenance1
name: ATP6V1D
xref: UnificationXref1184
feature: FragmentFeature195
cellular location: GO:0005829
comment: Reactome DB_ID: 3659703
display name: O59823

http://identifiers.org/pubmed/16533814
type: PublicationXref
id: 16533814
author: Kang, KR
author: McPhie, P
author: Bell, JK
author: Park, MH
author: Wolff, EC
author: Kim, YS
db: Pubmed
title: Deoxyhypusine hydroxylase is a Fe(II)-dependent, HEAT-repeat enzyme. Identification of amino acid residues critical for Fe(II) binding and catalysis [corrected].
source: J Biol Chem 281:13217-25
year: 2006

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14265
data source: Provenance1
name: ATP6V1H
xref: UnificationXref1182
feature: FragmentFeature194
cellular location: GO:0005829
comment: Reactome DB_ID: 3659724
display name: O14265

ATP6V1G
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1191
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659719

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P31406
data source: Provenance1
name: ATP6V1A
xref: UnificationXref1186
feature: FragmentFeature196
cellular location: GO:0005829
comment: Reactome DB_ID: 3659685
display name: P31406

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74174
data source: Provenance1
name: ATP6V1G2
xref: UnificationXref1190
feature: FragmentFeature198
cellular location: GO:0005829
comment: Reactome DB_ID: 3659718
display name: O74174

http://identifiers.org/pubmed/18481987
type: PublicationXref
id: 18481987
author: Sandler, H
author: Stoecklin, G
db: Pubmed
title: Control of mRNA decay by phosphorylation of tristetraprolin
source: Biochem Soc Trans 36:491-6
year: 2008

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74174
data source: Provenance1
name: ATP6V1G1
xref: UnificationXref1189
feature: FragmentFeature197
cellular location: GO:0005829
comment: Reactome DB_ID: 3659717
display name: O74174

phospho-p-T,Y-MAPK8
type: Protein
entity reference: Q09892
data source: Provenance1
xref: UnificationXref1203
feature: ModificationFeature42
feature: FragmentFeature200
feature: ModificationFeature43
cellular location: GO:0005654
comment: Reactome DB_ID: 3660839

phospho-p-T,Y-MAPK8
type: Protein
entity reference: Q09892
data source: Provenance1
xref: UnificationXref1202
feature: ModificationFeature42
feature: FragmentFeature199
feature: ModificationFeature43
cellular location: GO:0005829
comment: Reactome DB_ID: 3660854

Homologues of RHOA
type: Protein
data source: Provenance1
member physical entity: RHOA_HUMAN
xref: UnificationXref1232
cellular location: GO:0005886
comment: Reactome DB_ID: 3661371
comment: Converted from EntitySet in Reactome

O74369
type: Protein
entity reference: O74369
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: NSMA_HUMAN
name: Sphingomyelin phosphodiesterase 2
xref: UnificationXref1223
feature: FragmentFeature201
cellular location: GO:0005886
comment: Reactome DB_ID: 3661355
display name: SMPD2

http://identifiers.org/pubmed/10212249
type: PublicationXref
id: 10212249
author: Sondermann, P
author: Steegborn, C
author: Wahl, MC
author: Huber, R
author: Marinkovic, S
author: Jacob, U
author: Worbs, M
author: Clausen, T
db: Pubmed
title: Kinetics and inhibition of recombinant human cystathionine gamma-lyase. Toward the rational control of transsulfuration
source: J Biol Chem 274:12675-84
year: 1999

UnificationXref6023
type: UnificationXref
id: 3665046
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665046

UnificationXref6022
type: UnificationXref
id: REACT_101578
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_101578.9

UnificationXref6021
type: UnificationXref
id: 3657883
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657883

UnificationXref6020
type: UnificationXref
id: 3657881
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657881

UnificationXref6027
type: UnificationXref
id: 3657726
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657726

UnificationXref6026
type: UnificationXref
id: 3657722
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657722

phospho-p-S1387-TSC2
type: Protein
entity reference: Q9UUG9
data source: Provenance1
xref: UnificationXref1116
feature: ModificationFeature41
feature: FragmentFeature178
cellular location: GO:0005829
comment: Reactome DB_ID: 3662439

UnificationXref6025
type: UnificationXref
id: 3657717
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657717

UnificationXref6024
type: UnificationXref
id: REACT_94747
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_94747.9

UnificationXref6029
type: UnificationXref
id: 3657728
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657728

UnificationXref6028
type: UnificationXref
id: 3657727
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657727

Homologues of RPS6
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1094
cellular location: GO:0005829
comment: Reactome DB_ID: 3658803
comment: Converted from EntitySet in Reactome

http://identifiers.org/pubmed/20952656
type: PublicationXref
id: 20952656
author: Fitzgerald, Kevin
author: Palnitkar, Maya
author: Kwon, Hyock Joo
author: Horton, JD
author: Deisenhofer, Johann
author: Henry, Lisa
author: Kim, Chai-Wan
author: McKean, William B
author: Moon, YA
author: Colbert, Christopher L
db: Pubmed
title: Crystal structure of Spot 14, a modulator of fatty acid synthesis
source: Proc. Natl. Acad. Sci. U.S.A. 107:18820-5
year: 2010

Q09778
type: Protein
entity reference: Q09778
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1114
feature: FragmentFeature177
cellular location: GO:0005829
comment: Reactome DB_ID: 3660740
display name: TSC1

phospho-p-S422-EIF4B
type: Protein
entity reference: O14369
data source: Provenance1
xref: UnificationXref1102
feature: ModificationFeature40
feature: FragmentFeature176
cellular location: GO:0005829
comment: Reactome DB_ID: 3660798

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14369
data source: Provenance1
name: EIF4B(2-118)
name: O14369
name: eIF-4B
name: Eukaryotic translation initiation factor 4B
name: eukaryotic translation initiation factor 4B
xref: UnificationXref1101
feature: FragmentFeature175
cellular location: GO:0005829
comment: Reactome DB_ID: 3658917
display name: eIF4B

phospho-p-5S-RPS6
type: Protein
entity reference: P05752
data source: Provenance1
xref: UnificationXref1096
feature: ModificationFeature36
feature: ModificationFeature35
feature: ModificationFeature38
feature: ModificationFeature37
feature: FragmentFeature174
feature: ModificationFeature39
cellular location: GO:0005829
comment: Reactome DB_ID: 3660793

phospho-p-5S-RPS6
type: Protein
entity reference: UniProt:Q9C0Z7
data source: Provenance1
xref: UnificationXref1095
feature: ModificationFeature31
feature: FragmentFeature173
feature: ModificationFeature33
feature: ModificationFeature32
feature: ModificationFeature34
feature: ModificationFeature30
cellular location: GO:0005829
comment: Reactome DB_ID: 3660787

Homologues of p-5S-RPS6
type: Protein
data source: Provenance1
member physical entity: phospho-p-5S-RPS6
xref: UnificationXref1097
cellular location: GO:0005829
comment: Reactome DB_ID: 3660794
comment: Converted from EntitySet in Reactome

UnificationXref6030
type: UnificationXref
id: 3657729
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657729

Phenyllactate [ChEBI:8100]
type: SmallMoleculeReference
name: Phenyllactate
xref: UnificationXref6961

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P05752
data source: Provenance1
name: P10660
name: P05752
name: Phosphoprotein NP33
name: 40S ribosomal protein S6
name: 40S small ribosomal protein 6
xref: UnificationXref1093
feature: FragmentFeature172
cellular location: GO:0005829
comment: Reactome DB_ID: 3658802
display name: RPS6

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q9C0Z7
data source: Provenance1
name: Q9C0Z7
name: P10660
name: Phosphoprotein NP33
name: 40S ribosomal protein S6
name: 40S small ribosomal protein 6
xref: UnificationXref1091
feature: FragmentFeature171
cellular location: GO:0005829
comment: Reactome DB_ID: 3658798
display name: RPS6

UnificationXref6010
type: UnificationXref
id: CHEBI:16497
db: ChEBI

UnificationXref6012
type: UnificationXref
id: REACT_4670
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4670.1

UnificationXref6011
type: UnificationXref
id: 29892
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29892

UnificationXref6014
type: UnificationXref
id: 30187
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=30187

UnificationXref6013
type: UnificationXref
id: CHEBI:18077
db: ChEBI

UnificationXref6016
type: UnificationXref
id: 29604
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29604

UnificationXref6015
type: UnificationXref
id: REACT_2773
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2773.1

UnificationXref6018
type: UnificationXref
id: 68424
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=68424

http://identifiers.org/pubmed/15581572
type: PublicationXref
id: 15581572
author: Xia, Z
author: Massiah, M A
author: Mildvan, A S
author: Kang, L-W
author: Gabelli, S B
author: Bianchet, M A
author: Amzel, L Mario
author: Azurmendi, H F
author: Legler, P M
author: Saraswat, V
db: Pubmed
title: Structures and mechanisms of Nudix hydrolases
source: Arch. Biochem. Biophys. 433:129-43
year: 2005

UnificationXref6017
type: UnificationXref
id: REACT_5621
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5621.1

UnificationXref6019
type: UnificationXref
id: REACT_2531
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2531.1

http://identifiers.org/pubmed/16856888
type: PublicationXref
id: 16856888
author: Tomer, A
author: Deutsch, VR
db: Pubmed
title: Megakaryocyte development and platelet production
source: Br J Haematol 134:453-66
year: 2006

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O13742
data source: Provenance1
name: ATP6V0A1
xref: UnificationXref1150
feature: FragmentFeature179
cellular location: GO:0010008
comment: Reactome DB_ID: 3659660
display name: O13742

ATP6V0A
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1154
cellular location: GO:0010008
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659664

UniProt:Q10361
type: ProteinReference
xref: UnificationXref5405
organism: BioSource1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O13753
data source: Provenance1
name: ATP6V0D2
xref: UnificationXref1157
feature: FragmentFeature184
cellular location: GO:0010008
comment: Reactome DB_ID: 3659678
display name: O13753

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O13753
data source: Provenance1
name: ATP6V0D1
xref: UnificationXref1156
feature: FragmentFeature183
cellular location: GO:0010008
comment: Reactome DB_ID: 3659677
display name: O13753

ATP6V0C
type: Protein
entity reference: P50515
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1162
feature: FragmentFeature186
cellular location: GO:0010008
comment: Reactome DB_ID: 3659672
display name: P50515

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14046
data source: Provenance1
name: ATP6V0B
xref: UnificationXref1160
feature: FragmentFeature185
cellular location: GO:0010008
comment: Reactome DB_ID: 3659668
display name: O14046

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O13742
data source: Provenance1
name: ATP6V0A4
xref: UnificationXref1152
feature: FragmentFeature181
cellular location: GO:0010008
comment: Reactome DB_ID: 3659662
display name: O13742

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O13742
data source: Provenance1
name: ATP6V0A2
xref: UnificationXref1151
feature: FragmentFeature180
cellular location: GO:0010008
comment: Reactome DB_ID: 3659661
display name: O13742

ATP6V0D
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1158
cellular location: GO:0010008
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659679

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O13742
data source: Provenance1
name: O13742
xref: UnificationXref1153
feature: FragmentFeature182
cellular location: GO:0010008
comment: Reactome DB_ID: 3659663
display name: TCIRG1

UniProt:P0C016
type: ProteinReference
xref: UnificationXref1859
organism: BioSource1

UnificationXref6048
type: UnificationXref
id: REACT_138301
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_138301.5

5'-Methylthio-ribose-1P (2-)
type: SmallMolecule
entity reference: CHEBI:58533
data source: Provenance1
xref: UnificationXref5125
xref: UnificationXref5124
cellular location: GO:0005829
comment: Reactome DB_ID: 1237165

UnificationXref6049
type: UnificationXref
id: 3665055
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665055

UnificationXref6046
type: UnificationXref
id: 3657893
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657893

UnificationXref6047
type: UnificationXref
id: 3657894
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657894

UnificationXref6044
type: UnificationXref
id: REACT_54065
db: Reactome
id version: 10
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_54065.10

UnificationXref6045
type: UnificationXref
id: 3657892
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657892

UnificationXref6042
type: UnificationXref
id: 3657890
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657890

UnificationXref6043
type: UnificationXref
id: 3657891
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657891

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7U6
data source: Provenance1
name: ARHGEF18
name: p114/Arhgef18
xref: UnificationXref1325
feature: FragmentFeature226
cellular location: GO:0005829
comment: Reactome DB_ID: 3661486
display name: Q9Y7U6

Decarboxylated AdoMet
type: SmallMolecule
entity reference: CHEBI:15625
data source: Provenance1
name: S-Adenosylmethioninamine
xref: UnificationXref5108
xref: UnificationXref5107
cellular location: GO:0005829
comment: Reactome DB_ID: 353113
display name: SAM

UnificationXref6052
type: UnificationXref
id: 3657896
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657896

1,4-Butanediamine
type: SmallMolecule
entity reference: CHEBI:17148
data source: Provenance1
name: Tetramethylenediamine
name: 1,4-Diaminobutane
xref: UnificationXref5101
xref: UnificationXref5102
cellular location: GO:0005829
comment: Reactome DB_ID: 29610
display name: Putrescine

UnificationXref6051
type: UnificationXref
id: 3657895
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657895

Homologues of ARHGEF18
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1327
cellular location: GO:0005829
comment: Reactome DB_ID: 3661488
comment: Converted from EntitySet in Reactome

Agmatine
type: SmallMolecule
entity reference: CHEBI:17431
data source: Provenance1
xref: UnificationXref5093
xref: UnificationXref5092
cellular location: GO:0005829
comment: Reactome DB_ID: 351164
display name: AGM

UnificationXref6050
type: UnificationXref
id: REACT_87534
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_87534.9

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7U5
data source: Provenance1
name: ARHGEF18
name: p114/Arhgef18
xref: UnificationXref1324
feature: FragmentFeature225
cellular location: GO:0005829
comment: Reactome DB_ID: 3661485
display name: Q9Y7U5

4-Trimethylammoniobutanoate
type: SmallMolecule
entity reference: 4-Trimethylammoniobutanoate
data source: Provenance1
xref: UnificationXref5083
xref: UnificationXref5082
cellular location: GO:0005829
comment: Reactome DB_ID: 31369
display name: TEABT

4-Trimethylammoniobutanal
type: SmallMolecule
entity reference: 4-Trimethylammoniobutanal
data source: Provenance1
xref: UnificationXref5079
xref: UnificationXref5080
cellular location: GO:0005829
comment: Reactome DB_ID: 31311
display name: TEABL

Carbamide
type: SmallMolecule
entity reference: Urea [ChEBI:16199]
data source: Provenance1
xref: UnificationXref5069
xref: UnificationXref5068
cellular location: GO:0005759
comment: Reactome DB_ID: 374061
display name: Urea

Carbamide
type: SmallMolecule
entity reference: Urea [ChEBI:16199]
data source: Provenance1
xref: UnificationXref5059
xref: UnificationXref5058
cellular location: GO:0005829
comment: Reactome DB_ID: 29514
display name: Urea

(S)-2,5-Diaminopentanoate
type: SmallMolecule
entity reference: CHEBI:15729
data source: Provenance1
name: (S)-2,5-Diaminopentanoic acid
name: (S)-2,5-diaminovaleric acid
name: L-Ornithine
xref: UnificationXref5055
xref: UnificationXref5056
cellular location: GO:0005829
comment: Reactome DB_ID: 29498
display name: L-Orn

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7U6
data source: Provenance1
name: ARHGEF2
name: Arhgef2
name: Q9Y7U6
xref: UnificationXref1317
feature: FragmentFeature220
cellular location: GO:0005829
comment: Reactome DB_ID: 3661478
display name: Gef-h1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTR5
data source: Provenance1
name: ARHGEF2
name: Q9UTR5
name: Arhgef2
xref: UnificationXref1318
feature: FragmentFeature221
cellular location: GO:0005829
comment: Reactome DB_ID: 3661479
display name: Gef-h1

http://identifiers.org/pubmed/9799232
type: PublicationXref
id: 9799232
author: Wagner, H
author: Mischak, H
author: Sparwasser, T
author: Lipford, GB
author: Schmid, R
author: Heeg, K
author: Miethke, T
author: Hacker, H
author: Liptay, S
db: Pubmed
title: CpG-DNA-specific activation of antigen-presenting cells requires stress kinase activity and is preceded by non-specific endocytosis and endosomal maturation
source: EMBO J 17:6230-40
year: 1998

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7U5
data source: Provenance1
name: ARHGEF2
name: Arhgef2
name: Q9Y7U5
xref: UnificationXref1316
feature: FragmentFeature219
cellular location: GO:0005829
comment: Reactome DB_ID: 3661477
display name: Gef-h1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7U6
data source: Provenance1
name: PDZ-RhoGEF
name: ARHGEF11
xref: UnificationXref1321
feature: FragmentFeature223
cellular location: GO:0005829
comment: Reactome DB_ID: 3661482
display name: Q9Y7U6

http://identifiers.org/pubmed/9799231
type: PublicationXref
id: 9799231
author: Guillemot, JC
author: Chavrier, P
author: Montcourrier, P
author: Massol, P
db: Pubmed
title: Fc receptor-mediated phagocytosis requires CDC42 and Rac1
source: EMBO J 17:6219-29
year: 1998

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTR5
data source: Provenance1
name: PDZ-RhoGEF
name: ARHGEF11
xref: UnificationXref1322
feature: FragmentFeature224
cellular location: GO:0005829
comment: Reactome DB_ID: 3661483
display name: Q9UTR5

http://identifiers.org/pubmed/19010255
type: PublicationXref
id: 19010255
author: Neu-Yilik, G
author: Kulozik, AE
db: Pubmed
title: NMD: multitasking between mRNA surveillance and modulation of gene expression
source: Adv Genet 62:185-243
year: 2008

Activation of PKB
type: Pathway
data source: Provenance1
pathway component: PDK1 attachment to plasma membrane
evidence: Evidence214
xref: UnificationXref1135
xref: UnificationXref1134
pathway order: PathwayStep211
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Homologues of ARHGEF11
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1323
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3661484

S-methylthio adenosine
type: SmallMolecule
entity reference: CHEBI:17509
data source: Provenance1
xref: UnificationXref5117
xref: UnificationXref5118
cellular location: GO:0005829
comment: Reactome DB_ID: 353106
display name: MTAD

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7U5
data source: Provenance1
name: PDZ-RhoGEF
name: ARHGEF11
xref: UnificationXref1320
feature: FragmentFeature222
cellular location: GO:0005829
comment: Reactome DB_ID: 3661481
display name: Q9Y7U5

Spermidine
type: SmallMolecule
entity reference: CHEBI:16610
data source: Provenance1
xref: UnificationXref5114
xref: UnificationXref5115
cellular location: GO:0005829
comment: Reactome DB_ID: 204635
display name: SPM

UnificationXref6039
type: UnificationXref
id: REACT_138728
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_138728.5

ARHGEF4
type: Protein
entity reference: P40995
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: ARHG4_HUMAN
name: Rho guanine nucleotide exchange factor 4
xref: UnificationXref1338
feature: FragmentFeature235
cellular location: GO:0005829
comment: Reactome DB_ID: 3661501
display name: P40995

UnificationXref6035
type: UnificationXref
id: REACT_134203
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_134203.5

UnificationXref6036
type: UnificationXref
id: 3657880
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657880

http://identifiers.org/pubmed/7685356
type: PublicationXref
id: 7685356
author: Weiner, KX
author: Maley, F
author: Weiner, RS
author: Maley, GF
db: Pubmed
title: Primary structure of human deoxycytidylate deaminase and overexpression of its functional protein in Escherichia coli
source: J Biol Chem 268:12983-9
year: 1993

UnificationXref6037
type: UnificationXref
id: REACT_129614
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_129614.5

UnificationXref6038
type: UnificationXref
id: 3665052
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665052

UnificationXref6031
type: UnificationXref
id: REACT_133187
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_133187.5

UnificationXref6032
type: UnificationXref
id: 3657733
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657733

UnificationXref6033
type: UnificationXref
id: 3657734
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657734

UnificationXref6034
type: UnificationXref
id: 3657735
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657735

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7U6
data source: Provenance1
name: ARHGEF3
name: Rho guanine nucleotide exchange factor 3
name: ARHG3_HUMAN
xref: UnificationXref1335
feature: FragmentFeature233
cellular location: GO:0005829
comment: Reactome DB_ID: 3661498
display name: Q9Y7U6

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTR5
data source: Provenance1
name: ARHGEF3
name: Rho guanine nucleotide exchange factor 3
name: ARHG3_HUMAN
xref: UnificationXref1336
feature: FragmentFeature234
cellular location: GO:0005829
comment: Reactome DB_ID: 3661499
display name: Q9UTR5

UnificationXref6041
type: UnificationXref
id: REACT_87222
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_87222.9

UnificationXref6040
type: UnificationXref
id: 3657888
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657888

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTR5
data source: Provenance1
name: ARHGEF18
name: p114/Arhgef18
xref: UnificationXref1326
feature: FragmentFeature227
cellular location: GO:0005829
comment: Reactome DB_ID: 3661487
display name: Q9UTR5

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10164
data source: Provenance1
name: Active breakpoint cluster region-related protein
name: Q10164
name: ABR_HUMAN
xref: UnificationXref1329
feature: FragmentFeature228
cellular location: GO:0005829
comment: Reactome DB_ID: 3661492
display name: ABR

Homologues of AKAP13
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1333
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3661496

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7U5
data source: Provenance1
name: AKP13_HUMAN
name: Q9Y7U5
name: A-kinase anchor protein 13
xref: UnificationXref1330
feature: FragmentFeature229
cellular location: GO:0005829
comment: Reactome DB_ID: 3661493
display name: AKAP13

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7U6
data source: Provenance1
name: AKP13_HUMAN
name: Q9Y7U6
name: A-kinase anchor protein 13
xref: UnificationXref1331
feature: FragmentFeature230
cellular location: GO:0005829
comment: Reactome DB_ID: 3661494
display name: AKAP13

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTR5
data source: Provenance1
name: AKP13_HUMAN
name: Q9UTR5
name: A-kinase anchor protein 13
xref: UnificationXref1332
feature: FragmentFeature231
cellular location: GO:0005829
comment: Reactome DB_ID: 3661495
display name: AKAP13

Homologues of ARHGEF3
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1337
cellular location: GO:0005829
comment: Reactome DB_ID: 3661500
comment: Converted from EntitySet in Reactome

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7U5
data source: Provenance1
name: ARHGEF3
name: Rho guanine nucleotide exchange factor 3
name: ARHG3_HUMAN
xref: UnificationXref1334
feature: FragmentFeature232
cellular location: GO:0005829
comment: Reactome DB_ID: 3661497
display name: Q9Y7U5

http://identifiers.org/pubmed/12040175
type: PublicationXref
id: 12040175
author: Iyengar, R
author: Ram, PT
author: Neves, SR
db: Pubmed
title: G protein pathways
source: Science 296:1636-9
year: 2002

UnificationXref6066
type: UnificationXref
id: 3661118
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661118

UnificationXref6067
type: UnificationXref
id: O94329
db: UniProt

UnificationXref6064
type: UnificationXref
id: Q9P7C8
db: UniProt

UnificationXref6065
type: UnificationXref
id: 3661122
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661122

UnificationXref6068
type: UnificationXref
id: 3661117
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661117

UnificationXref6069
type: UnificationXref
id: 3661123
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661123

UnificationXref6070
type: UnificationXref
id: 3661124
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661124

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10133
data source: Provenance1
name: Q10133
name: RhoB
xref: UnificationXref1300
feature: FragmentFeature209
cellular location: GO:0005886
comment: Reactome DB_ID: 3661426
display name: RHOB

Homologues of RHOB
type: Protein
data source: Provenance1
member physical entity: Q09914
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1302
cellular location: GO:0005886
comment: Reactome DB_ID: 3661428
comment: Converted from EntitySet in Reactome

UnificationXref6074
type: UnificationXref
id: REACT_85564
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_85564.9

Q09914
type: Protein
entity reference: UniProt:Q09914
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: RhoB
xref: UnificationXref1299
feature: FragmentFeature208
cellular location: GO:0005886
comment: Reactome DB_ID: 3661425
display name: RHOB

UnificationXref6073
type: UnificationXref
id: 3665357
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665357

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7U6
data source: Provenance1
name: ARHGEF1
name: ARH1_HUMAN
name: Rho guanine nucleotide exchange factor 1
xref: UnificationXref1242
feature: FragmentFeature206
cellular location: GO:0005886
comment: Reactome DB_ID: 3661381
display name: Q9Y7U6

UnificationXref6072
type: UnificationXref
id: REACT_80707
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_80707.9

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTR5
data source: Provenance1
name: ARHGEF1
name: ARH1_HUMAN
name: Rho guanine nucleotide exchange factor 1
xref: UnificationXref1244
feature: FragmentFeature207
cellular location: GO:0005886
comment: Reactome DB_ID: 3661385
display name: Q9UTR5

UnificationXref6071
type: UnificationXref
id: 3661125
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661125

Homologues of ARHGEF1
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1245
cellular location: GO:0005886
comment: Reactome DB_ID: 3661386
comment: Converted from EntitySet in Reactome

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7U5
data source: Provenance1
name: ARHGEF1
name: ARH1_HUMAN
name: Rho guanine nucleotide exchange factor 1
xref: UnificationXref1240
feature: FragmentFeature205
cellular location: GO:0005886
comment: Reactome DB_ID: 3661377
display name: Q9Y7U5

RHOA_HUMAN
type: Protein
entity reference: UniProt:Q10133
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Q10133
name: RhoA
name: Transforming protein RhoA
xref: UnificationXref1230
feature: FragmentFeature203
cellular location: GO:0005886
comment: Reactome DB_ID: 3661366
display name: RHOA

RHOA_HUMAN
type: Protein
entity reference: Q9HE04
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Q9HE04
name: RhoA
name: Transforming protein RhoA
xref: UnificationXref1231
feature: FragmentFeature204
cellular location: GO:0005886
comment: Reactome DB_ID: 3661370
display name: RHOA

RHOA_HUMAN
type: Protein
entity reference: UniProt:Q09914
data source: Provenance1
name: Q09914
name: Note: the coordinates are copied over from Homo sapiens.
name: RhoA
name: Transforming protein RhoA
xref: UnificationXref1229
feature: FragmentFeature202
cellular location: GO:0005886
comment: Reactome DB_ID: 3661362
display name: RHOA

UnificationXref6053
type: UnificationXref
id: REACT_30035
db: Reactome
id version: 10
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_30035.10

UnificationXref6054
type: UnificationXref
id: 3665053
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665053

UnificationXref6055
type: UnificationXref
id: REACT_90801
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_90801.9

UnificationXref6056
type: UnificationXref
id: 169515
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=169515

UnificationXref6057
type: UnificationXref
id: REACT_7812
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_7812.1

UnificationXref6058
type: UnificationXref
id: 169509
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=169509

UnificationXref6059
type: UnificationXref
id: REACT_7610
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_7610.1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P40995
data source: Provenance1
name: Collybistin/Pem2
name: Rho guanine nucleotide exchange factor 9
name: gephrin
name: ARHGEF9
xref: UnificationXref1313
feature: FragmentFeature216
cellular location: GO:0005829
comment: Reactome DB_ID: 3661474
display name: P40995

UnificationXref6061
type: UnificationXref
id: REACT_108654
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_108654.9

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P40995
data source: Provenance1
name: TIAM2_HUMAN
name: T-lymphoma invasion and metastasis-inducing protein 2
name: TIAM2(2-1701)
name: P40995
xref: UnificationXref1314
feature: FragmentFeature217
cellular location: GO:0005829
comment: Reactome DB_ID: 3661475
display name: TIAM2

UnificationXref6060
type: UnificationXref
id: 3660895
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660895

TIAM1(2-1591)
type: Protein
entity reference: P40995
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: P40995
xref: UnificationXref1315
feature: FragmentFeature218
cellular location: GO:0005829
comment: Reactome DB_ID: 3661476
display name: Tiam1

UnificationXref6063
type: UnificationXref
id: 3661113
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661113

Homologues of ARHGEF2
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1319
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3661480

UnificationXref6062
type: UnificationXref
id: Q9P7X6
db: UniProt

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O59781
data source: Provenance1
name: Mitochondrial Rho GTPase 1
name: O59781
name: MIRO1_HUMAN
xref: UnificationXref1306
feature: FragmentFeature212
cellular location: GO:0005886
comment: Reactome DB_ID: 3661436
display name: RHOT1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P40995
data source: Provenance1
name: Guanine nucleotide exchange factor VAV3
name: VAV3_HUMAN
name: P40995
xref: UnificationXref1310
feature: FragmentFeature213
cellular location: GO:0005829
comment: Reactome DB_ID: 3661471
display name: VAV3

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P40995
data source: Provenance1
name: ARHGEF6
name: Alpha-Pix
name: PIX alpha
name: P40995
xref: UnificationXref1311
feature: FragmentFeature214
cellular location: GO:0005829
comment: Reactome DB_ID: 3661472
display name: Cool-2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P40995
data source: Provenance1
name: PLEKHG2
name: Plekhg-2/Clg
xref: UnificationXref1312
feature: FragmentFeature215
cellular location: GO:0005829
comment: Reactome DB_ID: 3661473
display name: P40995

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9HE04
data source: Provenance1
name: Q9HE04
name: RhoB
xref: UnificationXref1301
feature: FragmentFeature210
cellular location: GO:0005886
comment: Reactome DB_ID: 3661427
display name: RHOB

Q01112
type: Protein
entity reference: Q01112
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Cell division control protein 42 homolog
name: CDC42_HUMAN
xref: UnificationXref1304
feature: FragmentFeature211
cellular location: GO:0005886
comment: Reactome DB_ID: 3661432
display name: CDC42

Protoporphyrin IX
type: SmallMolecule
entity reference: CHEBI:15430
data source: Provenance1
xref: UnificationXref5373
xref: UnificationXref5372
cellular location: GO:0005758
comment: Reactome DB_ID: 189463
display name: PRIN9

UnificationXref6093
type: UnificationXref
id: 3657927
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657927

Flavin adenine dinucleotide
type: SmallMolecule
entity reference: FAD [ChEBI:16238]
data source: Provenance1
xref: UnificationXref5374
xref: UnificationXref5375
cellular location: GO:0005758
comment: Reactome DB_ID: 189484
display name: FAD

UnificationXref6094
type: UnificationXref
id: 3657928
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657928

UnificationXref6095
type: UnificationXref
id: REACT_90761
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_90761.9

UnificationXref6096
type: UnificationXref
id: O59835
db: UniProt

http://identifiers.org/pubmed/7000367
type: PublicationXref
id: 7000367
author: Kozak, M
db: Pubmed
title: Evaluation of the "scanning model" for initiation of protein synthesis in eucaryotes.
source: Cell 22:7-8
year: 1981

Coproporphyrinogen III
type: SmallMolecule
entity reference: CHEBI:15439
data source: Provenance1
xref: UnificationXref5357
xref: UnificationXref5358
cellular location: GO:0005758
comment: Reactome DB_ID: 189411
display name: COPRO3

Protoporphyrinogen IX
type: SmallMolecule
entity reference: CHEBI:15435
data source: Provenance1
xref: UnificationXref5360
xref: UnificationXref5361
cellular location: GO:0005758
comment: Reactome DB_ID: 189478
display name: PPGEN9

UnificationXref6090
type: UnificationXref
id: 3657925
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657925

Carbon dioxide
type: SmallMolecule
entity reference: CHEBI:16526
data source: Provenance1
xref: UnificationXref5362
xref: UnificationXref5363
cellular location: GO:0005758
comment: Reactome DB_ID: 189480
display name: CO2

UnificationXref6091
type: UnificationXref
id: 3657926
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657926

Hydrogen peroxide
type: SmallMolecule
entity reference: H2O2
data source: Provenance1
xref: UnificationXref5364
xref: UnificationXref5365
cellular location: GO:0005758
comment: Reactome DB_ID: 189481
display name: H2O2

UnificationXref6092
type: UnificationXref
id: REACT_87725
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_87725.9

Pb++
type: SmallMolecule
entity reference: CHEBI:27889
data source: Provenance1
xref: UnificationXref5394
xref: UnificationXref5393
cellular location: GO:0005759
comment: Reactome DB_ID: 391232
display name: Pb2+

iron (ferrous)
type: SmallMolecule
entity reference: CHEBI:18248
data source: Provenance1
name: Fe(II)
xref: UnificationXref5384
xref: UnificationXref5383
cellular location: GO:0005759
comment: Reactome DB_ID: 113531
display name: Fe2+

heme A
type: SmallMolecule
entity reference: CHEBI:24479
data source: Provenance1
xref: UnificationXref5403
xref: UnificationXref5404
cellular location: GO:0005759
comment: Reactome DB_ID: 2995348

heme O
type: SmallMolecule
entity reference: CHEBI:24480
data source: Provenance1
xref: UnificationXref5397
xref: UnificationXref5396
cellular location: GO:0005759
comment: Reactome DB_ID: 2995328

UnificationXref6087
type: UnificationXref
id: 3657919
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657919

http://identifiers.org/pubmed/2332429
type: PublicationXref
id: 2332429
author: Vance, JE
db: Pubmed
title: Phospholipid synthesis in a membrane fraction associated with mitochondria
source: J Biol Chem 265:7248-56
year: 1990

UnificationXref6086
type: UnificationXref
id: 3657918
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657918

Protoporphyrin IX
type: SmallMolecule
entity reference: CHEBI:15430
data source: Provenance1
xref: UnificationXref5382
xref: UnificationXref5381
cellular location: GO:0005759
comment: Reactome DB_ID: 189487
display name: PRIN9

UnificationXref6089
type: UnificationXref
id: 3657924
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657924

UnificationXref6088
type: UnificationXref
id: REACT_87606
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_87606.9

http://identifiers.org/pubmed/16682955
type: PublicationXref
id: 16682955
author: Hays, S
author: Westbrook, L
author: Qu, Z
author: Kern, FG
author: Thottassery, JV
author: Rentz, SS
author: Manuvakhova, M
db: Pubmed
title: Expression of the SNT-1/FRS2 phosphotyrosine binding domain inhibits activation of MAP kinase and PI3-kinase pathways and antiestrogen resistant growth induced by FGF-1 in human breast carcinoma cells
source: Oncogene 25:6003-14
year: 2006

Uroporphyrinogen III
type: SmallMolecule
entity reference: CHEBI:15437
data source: Provenance1
xref: UnificationXref5334
xref: UnificationXref5333
cellular location: GO:0005829
comment: Reactome DB_ID: 189407
display name: URO3

UnificationXref6084
type: UnificationXref
id: 3657908
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657908

UnificationXref6085
type: UnificationXref
id: 3657917
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657917

Hydroxymethylbilane
type: SmallMolecule
entity reference: CHEBI:16645
data source: Provenance1
name: preuroporphyrinogen
xref: UnificationXref5323
xref: UnificationXref5322
cellular location: GO:0005829
comment: Reactome DB_ID: 189449
display name: HMBL

UnificationXref6082
type: UnificationXref
id: 3657900
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657900

dipyrromethane
type: SmallMolecule
entity reference: CHEBI:36319
data source: Provenance1
xref: UnificationXref5328
xref: UnificationXref5327
cellular location: GO:0005829
comment: Reactome DB_ID: 189447
display name: DIPY

UnificationXref6083
type: UnificationXref
id: O94697
db: UniProt

delta-Aminolevulinic acid
type: SmallMolecule
entity reference: CHEBI:17549
data source: Provenance1
name: 5-aminolevulinate
xref: UnificationXref5315
xref: UnificationXref5314
cellular location: GO:0005829
comment: Reactome DB_ID: 189489
display name: dALA

UnificationXref6080
type: UnificationXref
id: 3657912
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657912

Porphobilinogen
type: SmallMolecule
entity reference: CHEBI:17381
data source: Provenance1
xref: UnificationXref5318
xref: UnificationXref5317
cellular location: GO:0005829
comment: Reactome DB_ID: 189464
display name: PBG

UnificationXref6081
type: UnificationXref
id: O14003
db: UniProt

protoheme
type: SmallMolecule
entity reference: CHEBI:17627
data source: Provenance1
xref: UnificationXref5303
xref: UnificationXref5304
cellular location: GO:0005759
comment: Reactome DB_ID: 189444
display name: heme

Pb++
type: SmallMolecule
entity reference: CHEBI:27889
data source: Provenance1
xref: UnificationXref5307
xref: UnificationXref5306
cellular location: GO:0005829
comment: Reactome DB_ID: 190173
display name: Pb2+

Oxygen
type: SmallMolecule
entity reference: CHEBI:15379
data source: Provenance1
xref: UnificationXref5355
xref: UnificationXref5356
cellular location: GO:0005758
comment: Reactome DB_ID: 189461
display name: O2

Coproporphyrinogen I
type: SmallMolecule
entity reference: Coproporphyrinogen I
data source: Provenance1
xref: UnificationXref5351
xref: UnificationXref5352
cellular location: GO:0005829
comment: Reactome DB_ID: 190128
display name: COPRO1

Uroporphyrinogen I
type: SmallMolecule
entity reference: Uroporphyrinogen I
data source: Provenance1
xref: UnificationXref5349
xref: UnificationXref5348
cellular location: GO:0005829
comment: Reactome DB_ID: 190157
display name: URO1

Coproporphyrinogen III
type: SmallMolecule
entity reference: CHEBI:15439
data source: Provenance1
xref: UnificationXref5341
xref: UnificationXref5340
cellular location: GO:0005829
comment: Reactome DB_ID: 189455
display name: COPRO3

UnificationXref6079
type: UnificationXref
id: O94449
db: UniProt

UnificationXref6078
type: UnificationXref
id: 3657904
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657904

UnificationXref6077
type: UnificationXref
id: Q09843
db: UniProt

UnificationXref6076
type: UnificationXref
id: 3657916
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657916

UnificationXref6075
type: UnificationXref
id: O60182
db: UniProt

2-Ketobutyrate
type: SmallMolecule
entity reference: CHEBI:30831
data source: Provenance1
xref: UnificationXref5216
xref: UnificationXref5215
cellular location: GO:0005829
comment: Reactome DB_ID: 936714
display name: 2-oxobutanoate

gamma-glutamyl-L-cysteine
type: SmallMolecule
entity reference: CHEBI:17515
data source: Provenance1
xref: UnificationXref5226
xref: UnificationXref5225
cellular location: GO:0005829
comment: Reactome DB_ID: 174393
display name: gGluCys

cysteine-glycine
type: SmallMolecule
entity reference: CHEBI:4047
data source: Provenance1
name: cysteinylglycine
xref: UnificationXref5235
xref: UnificationXref5236
cellular location: GO:0005829
comment: Reactome DB_ID: 1247904
display name: Cys-Gly

H2S
type: SmallMolecule
entity reference: Hydrogen sulfide [ChEBI:5787]
data source: Provenance1
xref: UnificationXref5244
xref: UnificationXref5243
cellular location: GO:0005829
comment: Reactome DB_ID: 1614532

L-Homolanthionine
type: SmallMolecule
entity reference: CHEBI:62856
data source: Provenance1
xref: UnificationXref5251
xref: UnificationXref5250
cellular location: GO:0005829
comment: Reactome DB_ID: 1614594

L-Lanthionine
type: SmallMolecule
entity reference: CHEBI:21347
data source: Provenance1
xref: UnificationXref5257
xref: UnificationXref5256
cellular location: GO:0005829
comment: Reactome DB_ID: 1614582

H+
type: SmallMolecule
entity reference: CHEBI:15378
data source: Provenance1
xref: UnificationXref5265
xref: UnificationXref5264
cellular location: GO:0005743
comment: Reactome DB_ID: 1614597

sulfite(2-)
type: SmallMolecule
entity reference: CHEBI:17359
data source: Provenance1
xref: UnificationXref5271
xref: UnificationXref5272
cellular location: GO:0005759
comment: Reactome DB_ID: 1614538

thiosulfate(2-)
type: SmallMolecule
entity reference: CHEBI:16094
data source: Provenance1
xref: UnificationXref5275
xref: UnificationXref5276
cellular location: GO:0005759
comment: Reactome DB_ID: 1614595
display name: S2O3(2-)

delta-Aminolevulinic acid
type: SmallMolecule
entity reference: CHEBI:17549
data source: Provenance1
name: 5-aminolevulinate
xref: UnificationXref5293
xref: UnificationXref5292
cellular location: GO:0005759
comment: Reactome DB_ID: 189466
display name: dALA

Glycine
type: SmallMolecule
entity reference: CHEBI:15428
data source: Provenance1
name: Aminoacetic acid
xref: UnificationXref5289
xref: UnificationXref5290
cellular location: GO:0005759
comment: Reactome DB_ID: 159549
display name: Gly

FAD
type: SmallMolecule
entity reference: FAD [ChEBI:16238]
data source: Provenance1
xref: UnificationXref5186
xref: UnificationXref5187
cellular location: GO:0005782
comment: Reactome DB_ID: 141335

1,2-Dihydroxy-3-oxo-methylthiopentene (1-)
type: SmallMolecule
entity reference: CHEBI:58795
data source: Provenance1
xref: UnificationXref5150
xref: UnificationXref5149
cellular location: GO:0005829
comment: Reactome DB_ID: 1237155
display name: Acireductone

4-Methylthio-2-oxobutanoate (1-)
type: SmallMolecule
entity reference: CHEBI:16723
data source: Provenance1
xref: UnificationXref5158
xref: UnificationXref5157
cellular location: GO:0005829
comment: Reactome DB_ID: 1237122

5'-Methylthio-ribulose-1P (2-)
type: SmallMolecule
entity reference: CHEBI:58548
data source: Provenance1
xref: UnificationXref5133
xref: UnificationXref5132
cellular location: GO:0005829
comment: Reactome DB_ID: 1237107

2,3-Dioxo-methiopentane-1P (2-)
type: SmallMolecule
entity reference: CHEBI:58828
data source: Provenance1
xref: UnificationXref5142
xref: UnificationXref5141
cellular location: GO:0005829
comment: Reactome DB_ID: 1237176

NH4+
type: SmallMolecule
entity reference: NH4+
data source: Provenance1
xref: UnificationXref5180
xref: UnificationXref5179
cellular location: GO:0005782
comment: Reactome DB_ID: 389843

Glyoxylate
type: SmallMolecule
entity reference: CHEBI:16891
data source: Provenance1
xref: UnificationXref5183
xref: UnificationXref5182
cellular location: GO:0005782
comment: Reactome DB_ID: 389678

L-Methionine
type: SmallMolecule
entity reference: CHEBI:16643
data source: Provenance1
xref: UnificationXref5170
xref: UnificationXref5169
cellular location: GO:0005829
comment: Reactome DB_ID: 174390
display name: L-Met

glycine
type: SmallMolecule
entity reference: CHEBI:15428
data source: Provenance1
name: Aminoacetic acid
xref: UnificationXref5177
xref: UnificationXref5178
cellular location: GO:0005782
comment: Reactome DB_ID: 193446
display name: Gly

http://identifiers.org/pubmed/18395510
type: PublicationXref
id: 18395510
author: Bigotti, MG
author: Clarke, AR
db: Pubmed
title: Chaperonins: The hunt for the Group II mechanism
source: Arch Biochem Biophys 474:331-9
year: 2008

UnificationXref6099
type: UnificationXref
id: 3657932
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657932

UnificationXref6098
type: UnificationXref
id: P87324
db: UniProt

UnificationXref6097
type: UnificationXref
id: 3657937
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657937

L-Cystathionine
type: SmallMolecule
entity reference: CHEBI:17482
data source: Provenance1
xref: UnificationXref5213
xref: UnificationXref5212
cellular location: GO:0005829
comment: Reactome DB_ID: 1614518

Homocysteine
type: SmallMolecule
entity reference: CHEBI:17230
data source: Provenance1
xref: UnificationXref5204
xref: UnificationXref5203
cellular location: GO:0005829
comment: Reactome DB_ID: 174369
display name: HCYS

early endosome membrane
type: CellularLocationVocabulary
xref: UnificationXref1447

late endosome membrane
type: CellularLocationVocabulary
xref: UnificationXref3518

early endosome lumen
type: CellularLocationVocabulary
xref: UnificationXref6205

late endosome lumen
type: CellularLocationVocabulary
xref: UnificationXref6225

endosome lumen
type: CellularLocationVocabulary
xref: UnificationXref1146

http://identifiers.org/pubmed/8163536
type: PublicationXref
id: 8163536
author: Sidorenko, SP
author: Chandran, KA
author: Clark, EA
author: Disteche, CM
author: Edelhoff, S
author: Law, CL
author: Weiss, A
author: Chan, AC
author: Draves, KE
db: Pubmed
title: Molecular cloning of human Syk. A B cell protein-tyrosine kinase associated with the surface immunoglobulin M-B cell receptor complex
source: J Biol Chem 269:12310-9
year: 1994

(2Fe-2S)(1+)
type: SmallMolecule
entity reference: CHEBI:33738
data source: Provenance1
xref: UnificationXref5591
xref: UnificationXref5590
cellular location: GO:0005829
comment: Reactome DB_ID: 2564757

(2Fe-2S)(2+)
type: SmallMolecule
entity reference: CHEBI:33737
data source: Provenance1
xref: UnificationXref5585
xref: UnificationXref5586
cellular location: GO:0005829
comment: Reactome DB_ID: 2564759

Sulfur atom
type: SmallMolecule
entity reference: CHEBI:26833
data source: Provenance1
xref: UnificationXref5597
xref: UnificationXref5598
cellular location: GO:0005829
comment: Reactome DB_ID: 2566513
display name: S

GABA
type: SmallMolecule
entity reference: CHEBI:16865
data source: Provenance1
xref: UnificationXref5834
xref: UnificationXref5833
cellular location: GO:0005759
comment: Reactome DB_ID: 916850

Dopamine
type: SmallMolecule
entity reference: CHEBI:18243
data source: Provenance1
xref: UnificationXref5847
xref: UnificationXref5848
cellular location: GO:0005829
comment: Reactome DB_ID: 159362
display name: DA

1-chloro-2,4-dinitrobenzene
type: SmallMolecule
entity reference: 2,4-Dinitro-1-chlorobenzene
data source: Provenance1
xref: UnificationXref5850
xref: UnificationXref5851
cellular location: GO:0005829
comment: Reactome DB_ID: 176044
display name: CDNB

5-hydroxytryptamine N-methyl conjugate
type: SmallMolecule
entity reference: CHEBI:3210
data source: Provenance1
xref: UnificationXref5861
xref: UnificationXref5860
cellular location: GO:0005829
comment: Reactome DB_ID: 159363
display name: 5HT-N-CH3

iron (oxidation state not specified)
type: SmallMolecule
entity reference: CHEBI:18248
data source: Provenance1
xref: UnificationXref5600
xref: UnificationXref5599
cellular location: GO:0005829
comment: Reactome DB_ID: 71160
display name: Fe

Guanosine monophosphate
type: SmallMolecule
entity reference: CHEBI:17345
data source: Provenance1
name: Guanosine 5'-phosphate
name: Guanylic acid
name: Guanosine 5'-monophosphate
xref: UnificationXref5627
xref: UnificationXref5626
cellular location: GO:0005654
comment: Reactome DB_ID: 29626
display name: GMP

GDP
type: SmallMolecule
entity reference: CHEBI:17552
data source: Provenance1
xref: UnificationXref5631
xref: UnificationXref5630
cellular location: GO:0005654
comment: Reactome DB_ID: 111349

http://identifiers.org/pubmed/8670417
type: PublicationXref
id: 8670417
author: Tarakhovsky, A
author: Guinamard, R
author: Stabel, S
author: Schaal, S
author: Davoust, J
author: Leitges, M
author: Schmedt, C
db: Pubmed
title: Immunodeficiency in protein kinase cbeta-deficient mice
source: Science 273:788-91
year: 1996

NH3
type: SmallMolecule
entity reference: Ammonia
data source: Provenance1
xref: UnificationXref5667
xref: UnificationXref5668
cellular location: GO:0005654
comment: Reactome DB_ID: 76230

L-2-amino-3-mercaptopropionic acid
type: SmallMolecule
entity reference: CHEBI:17561
data source: Provenance1
name: L-cysteine
xref: UnificationXref5508
xref: UnificationXref5507
cellular location: GO:0005576
comment: Reactome DB_ID: 352016
display name: Cys

2-Amino-3-methylbutyric acid
type: SmallMolecule
entity reference: CHEBI:16414
data source: Provenance1
name: L-Valine
xref: UnificationXref5505
xref: UnificationXref5506
cellular location: GO:0005576
comment: Reactome DB_ID: 351992
display name: L-Val

(S)-2-Amino-3-(p-hydroxyphenyl)propionic acid
type: SmallMolecule
entity reference: CHEBI:17895
data source: Provenance1
name: L-Tyrosine
name: (S)-3-(p-Hydroxyphenyl)alanine
xref: UnificationXref5503
xref: UnificationXref5504
cellular location: GO:0005576
comment: Reactome DB_ID: 352030
display name: L-Tyr

carbovir diphosphate
type: SmallMolecule
entity reference: CHEBI:64172
data source: Provenance1
xref: UnificationXref5569
xref: UnificationXref5568
cellular location: GO:0005829
comment: Reactome DB_ID: 2162075
display name: xenobiotic

4Fe-4S cluster
type: SmallMolecule
entity reference: CHEBI:49883
data source: Provenance1
xref: UnificationXref5580
xref: UnificationXref5581
cellular location: GO:0005829
comment: Reactome DB_ID: 2564758

Pyridoxal 5'-phosphate
type: SmallMolecule
entity reference: Pyridoxal 5'-phosphate
data source: Provenance1
name: Pyridoxal 5-phosphate
name: Pyridoxal phosphate
xref: UnificationXref5544
xref: UnificationXref5543
cellular location: GO:0005759
comment: Reactome DB_ID: 113583
display name: PXLP

carbovir monophosphate
type: SmallMolecule
entity reference: CHEBI:64116
data source: Provenance1
xref: UnificationXref5566
xref: UnificationXref5565
cellular location: GO:0005829
comment: Reactome DB_ID: 2161176
display name: xenobiotic

cysteine-glycine
type: SmallMolecule
entity reference: CHEBI:4047
data source: Provenance1
name: cysteinylglycine
xref: UnificationXref5519
xref: UnificationXref5518
cellular location: GO:0005576
comment: Reactome DB_ID: 1247934
display name: Cys-Gly

iron (ferrous)
type: SmallMolecule
entity reference: CHEBI:18248
data source: Provenance1
xref: UnificationXref5532
xref: UnificationXref5531
cellular location: GO:0005758
comment: Reactome DB_ID: 1362385
display name: Fe2+

L-serine
type: SmallMolecule
entity reference: CHEBI:17115
data source: Provenance1
xref: UnificationXref5509
xref: UnificationXref5510
cellular location: GO:0005576
comment: Reactome DB_ID: 352002
display name: L-Ser

gamma-glutamyl group
type: SmallMolecule
entity reference: CHEBI:24190
data source: Provenance1
xref: UnificationXref5515
xref: UnificationXref5514
cellular location: GO:0005576
comment: Reactome DB_ID: 1247930

L-Glutamine
type: SmallMolecule
entity reference: L-Glutamine
data source: Provenance1
name: L-2-Aminoglutaramic acid
xref: UnificationXref5479
xref: UnificationXref5480
cellular location: GO:0005576
comment: Reactome DB_ID: 212615
display name: L-Gln

2-aminosuccinic acid
type: SmallMolecule
entity reference: CHEBI:17053
data source: Provenance1
name: L-Aspartate
name: L-Aspartic acid
xref: UnificationXref5477
xref: UnificationXref5478
cellular location: GO:0005576
comment: Reactome DB_ID: 351973
display name: L-Asp

L-Isoleucine
type: SmallMolecule
entity reference: CHEBI:17191
data source: Provenance1
name: 2-Amino-3-methylvaleric acid
xref: UnificationXref5485
xref: UnificationXref5484
cellular location: GO:0005576
comment: Reactome DB_ID: 352001
display name: L-Ile

(S)-alpha-Amino-1H-imidazole-4-propionic acid
type: SmallMolecule
entity reference: CHEBI:15971
data source: Provenance1
name: L-Histidine
xref: UnificationXref5483
xref: UnificationXref5482
cellular location: GO:0005576
comment: Reactome DB_ID: 351970
display name: L-His

PublicationXref692
type: PublicationXref
author: Agarwal, AK
title: Lysophospholipid acyltransferases: 1-acylglycerol-3-phosphate O-acyltransferases (AGPATs) From discovery to disease
source: Curr Op Lipidology
year: 2012

L-Leucine
type: SmallMolecule
entity reference: CHEBI:15603
data source: Provenance1
name: (2S)-alpha-2-Amino-4-methylvaleric acid
name: (2S)-alpha-Leucine
name: 2-amino-4-methylvaleric acid
xref: UnificationXref5487
xref: UnificationXref5486
cellular location: GO:0005576
comment: Reactome DB_ID: 351964
display name: L-Leu

2,6-diaminohexanoic acid
type: SmallMolecule
entity reference: 2,6-diaminohexanoic acid
data source: Provenance1
name: Lysine acid
name: L-Lysine
xref: UnificationXref5489
xref: UnificationXref5488
cellular location: GO:0005576
comment: Reactome DB_ID: 351991
display name: L-Lys

half cystine
type: SequenceModificationVocabulary
xref: UnificationXref5262

L-Methionine
type: SmallMolecule
entity reference: CHEBI:16643
data source: Provenance1
xref: UnificationXref5490
xref: UnificationXref5491
cellular location: GO:0005576
comment: Reactome DB_ID: 351966
display name: L-Met

L-Phenylalanine
type: SmallMolecule
entity reference: CHEBI:17295
data source: Provenance1
name: (S)-alpha-amino-beta-phenylpropionic acid
xref: UnificationXref5492
xref: UnificationXref5493
cellular location: GO:0005576
comment: Reactome DB_ID: 351993
display name: L-Phe

2-Pyrrolidinecarboxylic acid
type: SmallMolecule
entity reference: CHEBI:17203
data source: Provenance1
name: L-Proline
xref: UnificationXref5494
xref: UnificationXref5495
cellular location: GO:0005576
comment: Reactome DB_ID: 352033
display name: L-Pro

L-Threonine
type: SmallMolecule
entity reference: CHEBI:16857
data source: Provenance1
xref: UnificationXref5498
xref: UnificationXref5497
cellular location: GO:0005576
comment: Reactome DB_ID: 352000
display name: L-Thr

http://identifiers.org/pubmed/7559569
type: PublicationXref
id: 7559569
author: Buhl, AM
author: Dhanasekaran, N
author: Johnson, NL
author: Johnson, GL
db: Pubmed
title: G alpha 12 and G alpha 13 stimulate Rho-dependent stress fiber formation and focal adhesion assembly
source: J Biol Chem 270:24631-4
year: 1995

(S)-alpha-amino-beta-(3-indolyl)-propionic acid
type: SmallMolecule
entity reference: CHEBI:16828
data source: Provenance1
name: L-Tryptophan
xref: UnificationXref5500
xref: UnificationXref5501
cellular location: GO:0005576
comment: Reactome DB_ID: 352006
display name: L-Trp

Acetate
type: SmallMolecule
entity reference: CHEBI:15366
data source: Provenance1
name: Ethanoic acid
name: Acetic acid
xref: UnificationXref5435
xref: UnificationXref5434
cellular location: GO:0005829
comment: Reactome DB_ID: 29416
display name: CH3COO-

Ethanal
type: SmallMolecule
entity reference: CHEBI:15343
data source: Provenance1
name: Acetaldehyde
xref: UnificationXref5433
xref: UnificationXref5432
cellular location: GO:0005829
comment: Reactome DB_ID: 29510
display name: CH3CHO

Acetate
type: SmallMolecule
entity reference: CHEBI:15366
data source: Provenance1
name: Ethanoic acid
name: Acetic acid
xref: UnificationXref5422
xref: UnificationXref5421
cellular location: GO:0005759
comment: Reactome DB_ID: 113539
display name: CH3COO-

Ethanal
type: SmallMolecule
entity reference: CHEBI:15343
data source: Provenance1
name: Acetaldehyde
xref: UnificationXref5418
xref: UnificationXref5419
cellular location: GO:0005759
comment: Reactome DB_ID: 113532
display name: CH3CHO

3,4-dihydroxybenzoate
type: SmallMolecule
entity reference: CHEBI:36062
data source: Provenance1
xref: UnificationXref5450
xref: UnificationXref5449
cellular location: GO:0005829
comment: Reactome DB_ID: 175977
display name: protocatechuate

3-hydroxy 4-methoxybenzoate
type: SmallMolecule
entity reference: CHEBI:63797
data source: Provenance1
xref: UnificationXref5453
xref: UnificationXref5452
cellular location: GO:0005829
comment: Reactome DB_ID: 175978

gamma-L-Glutamyl-L-cysteinyl-glycine
type: SmallMolecule
entity reference: CHEBI:16856
data source: Provenance1
name: 5-L-Glutamyl-L-cysteinylglycine
name: N-(N-gamma-L-Glutamyl-L-cysteinyl)glycine
name: Reduced glutathione
name: Glutathione
xref: UnificationXref5469
xref: UnificationXref5470
cellular location: GO:0005576
comment: Reactome DB_ID: 1247892
display name: GSH

(S)-2-Amino-5-guanidinovaleric acid
type: SmallMolecule
entity reference: CHEBI:16467
data source: Provenance1
name: L-Arginine
xref: UnificationXref5473
xref: UnificationXref5474
cellular location: GO:0005576
comment: Reactome DB_ID: 351977
display name: L-Arg

L-Asparagine
type: SmallMolecule
entity reference: CHEBI:17196
data source: Provenance1
name: 2-Aminosuccinamic acid
xref: UnificationXref5476
xref: UnificationXref5475
cellular location: GO:0005576
comment: Reactome DB_ID: 351980
display name: L-Asn

L-Amino Acids
type: SmallMolecule
data source: Provenance1
member physical entity: 2-Amino-3-methylbutyric acid
member physical entity: 2-Pyrrolidinecarboxylic acid
member physical entity: L-Asparagine
member physical entity: L-Isoleucine
member physical entity: L-Leucine
member physical entity: (S)-alpha-amino-beta-(3-indolyl)-propionic acid
member physical entity: 2-aminosuccinic acid
member physical entity: (S)-2-Amino-5-guanidinovaleric acid
member physical entity: L-Methionine
member physical entity: L-Threonine
member physical entity: 2,6-diaminohexanoic acid
member physical entity: L-Phenylalanine
member physical entity: (S)-alpha-Amino-1H-imidazole-4-propionic acid
member physical entity: Glycine
member physical entity: L-Glutamine
member physical entity: (S)-2-Amino-3-(p-hydroxyphenyl)propionic acid
member physical entity: L-Glutaminic acid
member physical entity: L-serine
member physical entity: L-alpha-Alanine
member physical entity: L-2-amino-3-mercaptopropionic acid
xref: UnificationXref5511
xref: UnificationXref5512
cellular location: GO:0005576
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 428009

L-alpha-Alanine
type: SmallMolecule
entity reference: CHEBI:16977
data source: Provenance1
name: L-Alanine
name: L-2-Aminopropionic acid
xref: UnificationXref5471
xref: UnificationXref5472
cellular location: GO:0005576
comment: Reactome DB_ID: 352036
display name: L-Ala

3-(indol-3-yl)pyruvic acid
type: SmallMolecule
entity reference: CHEBI:29750
data source: Provenance1
xref: UnificationXref4961
xref: UnificationXref4960
cellular location: GO:0005829
comment: Reactome DB_ID: 893599

glutaryl-CoA
type: SmallMolecule
entity reference: CHEBI:15524
data source: Provenance1
xref: UnificationXref4954
xref: UnificationXref4953
cellular location: GO:0005759
comment: Reactome DB_ID: 70955
display name: GL-CoA

6,7-dihydrobiopterin
type: SmallMolecule
entity reference: 6,7-dihydrobiopterin [ChEBI:20680]
data source: Provenance1
name: q-dihydrobiopterin
xref: UnificationXref4968
xref: UnificationXref4969
cellular location: GO:0005829
comment: Reactome DB_ID: 71129
display name: qDHB

4a-hydroxytetrahydrobiopterin
type: SmallMolecule
entity reference: CHEBI:15374
data source: Provenance1
xref: UnificationXref4966
xref: UnificationXref4965
cellular location: GO:0005829
comment: Reactome DB_ID: 71112

L-2-Aminoadipate 6-semialdehyde
type: SmallMolecule
entity reference: CHEBI:17917
data source: Provenance1
xref: UnificationXref4940
xref: UnificationXref4939
cellular location: GO:0005759
comment: Reactome DB_ID: 113556
display name: 2AMAS

L-Saccharopine
type: SmallMolecule
entity reference: CHEBI:16927
data source: Provenance1
name: N6-(L-1,3-Dicarboxypropyl)-L-lysine
name: saccharopine
xref: UnificationXref4931
xref: UnificationXref4932
cellular location: GO:0005759
comment: Reactome DB_ID: 30176
display name: SACN

alpha-ketoadipate
type: SmallMolecule
entity reference: CHEBI:15753
data source: Provenance1
name: 2-oxoadipic acid
name: alpha-ketoadipic acid
xref: UnificationXref4946
xref: UnificationXref4947
cellular location: GO:0005759
comment: Reactome DB_ID: 70951
display name: 2-oxoadipate

alpha-ketoadipate
type: SmallMolecule
entity reference: CHEBI:15753
data source: Provenance1
name: 2-oxoadipic acid
name: alpha-ketoadipic acid
xref: UnificationXref4945
xref: UnificationXref4944
cellular location: GO:0005829
comment: Reactome DB_ID: 113577
display name: 2-oxoadipate

2,6-diaminohexanoic acid
type: SmallMolecule
entity reference: 2,6-diaminohexanoic acid
data source: Provenance1
name: Lysine acid
name: L-Lysine
xref: UnificationXref4929
xref: UnificationXref4928
cellular location: GO:0005759
comment: Reactome DB_ID: 29444
display name: L-Lys

3-hydroxyisobutyryl-CoA
type: SmallMolecule
entity reference: CHEBI:28259
data source: Provenance1
name: beta-hydroxyisobutyryl-CoA
xref: UnificationXref4917
xref: UnificationXref4916
cellular location: GO:0005759
comment: Reactome DB_ID: 71847
display name: bHIB-CoA

beta-hydroxyisobutyrate
type: SmallMolecule
entity reference: CHEBI:11805
data source: Provenance1
name: 3-hydroxy-2-methylpropanoate
xref: UnificationXref4920
xref: UnificationXref4919
cellular location: GO:0005759
comment: Reactome DB_ID: 573404
display name: bHIBA

N(omega)-(L-Arginino)succinate
type: SmallMolecule
entity reference: CHEBI:15682
data source: Provenance1
name: L-Argininosuccinic acid
name: N-(L-Arginino)succinate
name: L-Arginosuccinic acid
xref: UnificationXref5041
xref: UnificationXref5040
cellular location: GO:0005829
comment: Reactome DB_ID: 34575
display name: L-Argininosuccinate

2-Amino-5-ureidovaleric acid
type: SmallMolecule
entity reference: CHEBI:16349
data source: Provenance1
name: L-Citrulline
xref: UnificationXref5037
xref: UnificationXref5038
cellular location: GO:0005829
comment: Reactome DB_ID: 29968
display name: L-Cit

PLC-gamma1 signalling
type: Pathway
data source: Provenance1
pathway component: REACT 80694.9
evidence: Evidence238
xref: UnificationXref1266
xref: UnificationXref1267
xref: RelationshipXref98
pathway order: PathwayStep173
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

2-Amino-5-ureidovaleric acid
type: SmallMolecule
entity reference: CHEBI:16349
data source: Provenance1
name: L-Citrulline
xref: UnificationXref5031
xref: UnificationXref5030
cellular location: GO:0005759
comment: Reactome DB_ID: 113567
display name: L-Cit

Carbamoyl phosphate
type: SmallMolecule
entity reference: CHEBI:17672
data source: Provenance1
xref: UnificationXref5022
xref: UnificationXref5021
cellular location: GO:0005759
comment: Reactome DB_ID: 29676
display name: CAP

Hydrogencarbonate
type: SmallMolecule
entity reference: CHEBI:17544
data source: Provenance1
name: Bicarbonate
name: Acid carbonate
xref: UnificationXref5019
xref: UnificationXref5020
cellular location: GO:0005759
comment: Reactome DB_ID: 29896
display name: HCO3-

NH4+
type: SmallMolecule
entity reference: NH4+
data source: Provenance1
xref: UnificationXref5018
xref: UnificationXref5017
cellular location: GO:0005759
comment: Reactome DB_ID: 113561

(S)-2-Amino-5-guanidinovaleric acid
type: SmallMolecule
entity reference: CHEBI:16467
data source: Provenance1
name: L-Arginine
xref: UnificationXref5015
xref: UnificationXref5016
cellular location: GO:0005759
comment: Reactome DB_ID: 374064
display name: L-Arg

(S)-2-Amino-5-guanidinovaleric acid
type: SmallMolecule
entity reference: CHEBI:16467
data source: Provenance1
name: L-Arginine
xref: UnificationXref5011
xref: UnificationXref5010
cellular location: GO:0005829
comment: Reactome DB_ID: 29468
display name: L-Arg

N-Acetyl-L-glutamic acid
type: SmallMolecule
entity reference: CHEBI:17533
data source: Provenance1
name: N-Acetyl-L-glutamate
xref: UnificationXref5004
xref: UnificationXref5005
cellular location: GO:0005759
comment: Reactome DB_ID: 30471
display name: NAcGlu

4-(2-aminophenyl)-2,4-dioxobutanoic acid
type: SmallMolecule
entity reference: CHEBI:17442
data source: Provenance1
xref: UnificationXref4993
xref: UnificationXref4992
cellular location: GO:0005829
comment: Reactome DB_ID: 893615

Gap-filling DNA repair synthesis and ligation in GG-NER
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction42
evidence: Evidence76
xref: UnificationXref355
xref: RelationshipXref34
xref: UnificationXref354
pathway order: PathwayStep75
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

3-Anthraniloyl-L-alanine
type: SmallMolecule
entity reference: CHEBI:16946
data source: Provenance1
name: L-Kynurenine
xref: UnificationXref4990
xref: UnificationXref4989
cellular location: GO:0005829
comment: Reactome DB_ID: 29970
display name: L-KYN

Ceramide signalling
type: Pathway
data source: Provenance1
pathway component: Production of ceramide which can activate JNK and other targets
evidence: Evidence227
xref: UnificationXref1228
xref: RelationshipXref87
xref: UnificationXref1227
pathway order: PathwayStep224
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/11863375
type: PublicationXref
id: 11863375
author: Yang, RZ
author: Shuldiner, AR
author: Gong, DW
author: Blaileanu, G
author: Hansen, BC
db: Pubmed
title: cDNA cloning, genomic structure, chromosomal mapping, and functional expression of a novel human alanine aminotransferase
source: Genomics 79:445-50
year: 2002

PublicationXref621
type: PublicationXref
author: Tyfield, LA
author: Walter, JH
author: Holton, JB
title: Galactosemia
source: The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Scriver CR, et al., editors) 1:1553-1587
year: 2001

http://identifiers.org/pubmed/16543383
type: PublicationXref
id: 16543383
author: Pollard, JW
author: Pollack, SE
author: Cohen, PE
db: Pubmed
title: Genetic analysis of chromosome pairing, recombination, and cell cycle control during first meiotic prophase in mammals
source: Endocr Rev 27:398-426
year: 2006

Assembly of the RAD50-MRE11-NBS1 complex at DNA double-strand breaks
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction30
evidence: Evidence49
xref: UnificationXref213
xref: UnificationXref214
pathway order: PathwayStep48
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

phospho-p-S722,S792-RPTOR-1
type: Protein
entity reference: P87141
data source: Provenance1
xref: UnificationXref1089
feature: ModificationFeature28
feature: FragmentFeature170
feature: ModificationFeature29
cellular location: GO:0005829
comment: Reactome DB_ID: 3660779

phospho-p-S371,T389-RPS6KB1
type: Protein
entity reference: UniProt:Q12706
data source: Provenance1
xref: UnificationXref1085
feature: ModificationFeature27
feature: FragmentFeature169
feature: ModificationFeature26
cellular location: GO:0005829
comment: Reactome DB_ID: 3660775

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q12706
data source: Provenance1
name: RPS6KB1
name: Q12706
xref: UnificationXref1084
feature: FragmentFeature168
cellular location: GO:0005829
comment: Reactome DB_ID: 3660772
display name: S6K1

P87141
type: Protein
entity reference: P87141
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Regulatory-associated protein of mTOR
name: RPTOR_HUMAN
xref: UnificationXref1079
feature: FragmentFeature167
cellular location: GO:0005829
comment: Reactome DB_ID: 3660762
display name: RPTOR

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7K2
data source: Provenance1
name: Q9Y7K2
name: mTOR
xref: UnificationXref1076
feature: FragmentFeature166
cellular location: GO:0005829
comment: Reactome DB_ID: 3660757
display name: MTOR

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14356
data source: Provenance1
name: O14356
name: mTOR
xref: UnificationXref1074
feature: FragmentFeature165
cellular location: GO:0005829
comment: Reactome DB_ID: 3660753
display name: MTOR

Homologues of MTOR
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1077
cellular location: GO:0005829
comment: Reactome DB_ID: 3660758
comment: Converted from EntitySet in Reactome

Pyridoxine phosphate [ChEBI:8672]
type: SmallMoleculeReference
name: Pyridoxine 5-phosphate
name: Pyridoxine phosphate
name: Pyridoxine 5'-phosphate
xref: UnificationXref4592

UniProt:Q10421
type: ProteinReference
xref: UnificationXref1819
organism: BioSource1

http://identifiers.org/pubmed/11498013
type: PublicationXref
id: 11498013
author: Sorkin, A
db: Pubmed
title: Internalization of the epidermal growth factor receptor: role in signalling
source: Biochem Soc Trans 29:480-4
year: 2001

dITP
type: SmallMoleculeReference
name: 2'-Deoxyinosine 5'-triphosphate
name: dITP [ChEBI:10499]
name: 2'-Deoxyinosine-5'-triphosphate
xref: UnificationXref4482

UniProt:Q10425
type: ProteinReference
xref: UnificationXref7295
organism: BioSource1

2'-Deoxyinosine 5'-phosphate [ChEBI:28806]
type: SmallMoleculeReference
name: 2'-Deoxyinosine 5'-phosphate
name: dIMP
xref: UnificationXref4485

http://identifiers.org/pubmed/11278778
type: PublicationXref
id: 11278778
author: Trimble, RB
author: Cipollo, JF
author: Yan, Q
author: Dean, N
author: Chi, JH
db: Pubmed
title: The yeast ALG11 gene specifies addition of the terminal alpha 1,2-Man to the Man5GlcNAc2-PP-dolichol N-glycosylation intermediate formed on the cytosolic side of the endoplasmic reticulum
source: J Biol Chem 276:21828-40
year: 2001

Homologues of PDPK1
type: Protein
data source: Provenance1
member physical entity: 3-phosphoinositide dependent protein kinase-1
xref: UnificationXref1034
cellular location: GO:0005886
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3660159

3-phosphoinositide dependent protein kinase-1
type: Protein
entity reference: Q9Y7J6
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: PDPK1
name: Q9Y7J6
xref: UnificationXref1030
feature: FragmentFeature160
cellular location: GO:0005829
comment: Reactome DB_ID: 3661824
display name: PDK1

3-phosphoinositide dependent protein kinase-1
type: Protein
entity reference: Q9Y7J6
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: PDPK1
name: Q9Y7J6
xref: UnificationXref1033
feature: FragmentFeature162
cellular location: GO:0005886
comment: Reactome DB_ID: 3660158
display name: PDK1

3-phosphoinositide dependent protein kinase-1
type: Protein
entity reference: UniProt:Q12701
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: PDPK1
name: Q12701
xref: UnificationXref1032
feature: FragmentFeature161
cellular location: GO:0005886
comment: Reactome DB_ID: 3660154
display name: PDK1

phospho-p-T185,Y187-MAPK1
type: Protein
entity reference: P27638
data source: Provenance1
xref: UnificationXref1013
feature: FragmentFeature158
feature: ModificationFeature25
feature: ModificationFeature24
cellular location: GO:0005654
comment: Reactome DB_ID: 3660181

phospho-p-T185,Y187-MAPK1
type: Protein
entity reference: P27638
data source: Provenance1
xref: UnificationXref1009
feature: FragmentFeature157
feature: ModificationFeature25
feature: ModificationFeature24
cellular location: GO:0005829
comment: Reactome DB_ID: 3660175

3-phosphoinositide dependent protein kinase-1
type: Protein
entity reference: UniProt:Q12701
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: PDPK1
name: Q12701
xref: UnificationXref1028
feature: FragmentFeature159
cellular location: GO:0005829
comment: Reactome DB_ID: 3661823
display name: PDK1

Homologues of PDPK1
type: Protein
data source: Provenance1
member physical entity: 3-phosphoinositide dependent protein kinase-1
xref: UnificationXref1031
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3661825

http://identifiers.org/pubmed/15272052
type: PublicationXref
id: 15272052
author: Dinh, TP
author: Piomelli, D
author: Kathuria, S
db: Pubmed
title: RNA interference suggests a primary role for monoacylglycerol lipase in the degradation of the endocannabinoid 2-arachidonoylglycerol
source: Mol Pharmacol 66:1260-4
year: 2004

Phospho-ERK
type: Protein
data source: Provenance1
member physical entity: phospho-p-T202,Y204-MAPK3
member physical entity: phospho-p-T185,Y187-MAPK1
xref: UnificationXref1055
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3663725

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94363
data source: Provenance1
name: O94363
name: Rheb
xref: UnificationXref1066
feature: FragmentFeature163
cellular location: GO:0005829
comment: Reactome DB_ID: 3660746
display name: RHEB

O74184
type: Protein
entity reference: O74184
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: mLst8
xref: UnificationXref1072
feature: FragmentFeature164
cellular location: GO:0005829
comment: Reactome DB_ID: 3660766
display name: MLST8

phospho-p-T566,T710,S729-PRKCE
type: Protein
entity reference: UniProt:P36583
data source: Provenance1
xref: UnificationXref961
feature: ModificationFeature20
feature: FragmentFeature150
feature: ModificationFeature21
feature: ModificationFeature19
cellular location: GO:0005886
comment: Reactome DB_ID: 3661654

phospho-p-T566,T710,S729-PRKCE
type: Protein
entity reference: UniProt:P36582
data source: Provenance1
xref: UnificationXref960
feature: ModificationFeature17
feature: ModificationFeature18
feature: FragmentFeature149
feature: ModificationFeature16
cellular location: GO:0005886
comment: Reactome DB_ID: 3661650

Homologues of p-T566,T710,S729-PRKCE
type: Protein
data source: Provenance1
member physical entity: phospho-p-T566,T710,S729-PRKCE
xref: UnificationXref962
cellular location: GO:0005886
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3661655

phospho-p-T507,S645,S664-PRKCD(1-676)
type: Protein
entity reference: UniProt:P36583
data source: Provenance1
xref: UnificationXref958
feature: FragmentFeature148
feature: ModificationFeature14
feature: ModificationFeature15
feature: ModificationFeature13
cellular location: GO:0005886
comment: Reactome DB_ID: 3661645

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P40376
data source: Provenance1
name: P40376
name: cAMP-dependent protein kinase, alpha-catalytic subunit
name: PKA C-alpha
xref: UnificationXref978
feature: FragmentFeature153
cellular location: GO:0005829
comment: Reactome DB_ID: 3660351
display name: PRKACA

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36600
data source: Provenance1
name: PRKAR2B
name: cAMP-dependent protein kinase type II-beta regulatory chain
xref: UnificationXref975
feature: FragmentFeature152
cellular location: GO:0005829
comment: Reactome DB_ID: 3660358
display name: P36600

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36600
data source: Provenance1
name: PRKAR2A
name: cAMP-dependent protein kinase type II-alpha regulatory chain
xref: UnificationXref974
feature: FragmentFeature151
cellular location: GO:0005829
comment: Reactome DB_ID: 3660357
display name: P36600

PKA regulatory subunit
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref976
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3660359

http://identifiers.org/pubmed/18802471
type: PublicationXref
id: 18802471
author: Jefferies, WA
author: Seipp, RP
author: Basha, G
author: Omilusik, KD
author: Lizée, G
author: Reinicke, AT
db: Pubmed
title: MHC class I endosomal and lysosomal trafficking coincides with exogenous antigen loading in dendritic cells
source: PLoS One 3:e3247
year: 2008

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P40376
data source: Provenance1
name: P40376
name: cAMP-dependent protein kinase, alpha-catalytic subunit
name: PKA C-alpha
xref: UnificationXref985
feature: FragmentFeature154
cellular location: GO:0005654
comment: Reactome DB_ID: 3660352
display name: PRKACA

http://identifiers.org/pubmed/17177598
type: PublicationXref
id: 17177598
author: DeBiasi, RM
author: Leahy, DJ
author: Paez, JG
author: Yoshimoto, K
author: O'Neill, K
author: Thomas, RK
author: Cloughesy, T
author: Greulich, H
author: Yuza, Y
author: Ziaugra, L
author: Vivanco, I
author: Levine, RL
author: Rao, PN
author: Xu, Q
author: Gabriel, S
author: Onofrio, R
author: Lee, JC
author: Glatt, KA
author: Nghiemphu, P
author: Peck, TC
author: Liau, LM
author: Huang, JHY
author: Beroukhim, R
author: King, JC
author: Linhart, DJ
author: Kawaguchi, T
author: Sellers, WR
author: Mellinghoff, IK
author: Meyerson, M
author: Feng, WL
author: Getz, G
author: Nelson, SF
author: Mischel, P
author: Sawyers, CL
author: Pieper, RO
author: Khan, H
db: Pubmed
title: Epidermal growth factor receptor activation in glioblastoma through novel missense mutations in the extracellular domain
source: PLoS Med 3:e485
year: 2006

phospho-p-T202,Y204-MAPK3
type: Protein
entity reference: P27638
data source: Provenance1
xref: UnificationXref999
feature: ModificationFeature23
feature: ModificationFeature22
feature: FragmentFeature155
cellular location: GO:0005829
comment: Reactome DB_ID: 3660170

phospho-p-T202,Y204-MAPK3
type: Protein
entity reference: P27638
data source: Provenance1
xref: UnificationXref1003
feature: ModificationFeature23
feature: FragmentFeature156
feature: ModificationFeature22
cellular location: GO:0005654
comment: Reactome DB_ID: 3660178

http://identifiers.org/pubmed/19338303
type: PublicationXref
id: 19338303
author: Han, Q
author: Robinson, H
author: Tagle, DA
author: Cai, T
author: Li, J
db: Pubmed
title: Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K
source: J Med Chem 52:2786-93
year: 2009

P24339
type: Protein
entity reference: UniProt:P24339
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: KIF11_HUMAN
name: KIF11
name: Kinesin-5
name: Kinesin-like protein KIF11
xref: UnificationXref920
feature: FragmentFeature141
cellular location: GO:0005829
comment: Reactome DB_ID: 3663675
display name: EG5

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O13786
data source: Provenance1
name: ZFYVE20(2-784)
name: Rabenosyn-5
xref: UnificationXref915
feature: FragmentFeature140
cellular location: GO:0010008
comment: Reactome DB_ID: 3663708
display name: O13786

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q1MTQ7
data source: Provenance1
name: Kinesin-like protein KIF23
name: MKLP1
name: Q1MTQ7
xref: UnificationXref925
feature: FragmentFeature142
cellular location: GO:0005829
comment: Reactome DB_ID: 3663678
display name: KIF23

Kinesin-6
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref926
cellular location: GO:0005829
comment: Reactome DB_ID: 3663679
comment: Converted from EntitySet in Reactome

Q1MTQ1
type: Protein
entity reference: Q1MTQ1
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: CENP-E
xref: UnificationXref933
feature: FragmentFeature144
cellular location: GO:0005829
comment: Reactome DB_ID: 3663685
display name: CENPE

http://identifiers.org/pubmed/1968462
type: PublicationXref
id: 1968462
author: Edwards, PA
author: Kutsunai, SY
author: Wilkin, DJ
db: Pubmed
title: Isolation and sequence of the human farnesyl pyrophosphate synthetase cDNA. Coordinate regulation of the mRNAs for farnesyl pyrophosphate synthetase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, and 3-hydroxy-3-methylglutaryl coenzyme A synthase by phorbol ester
source: J Biol Chem 265:4607-14
year: 1990

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94466
data source: Provenance1
name: MgcRacGAP
name: RACGAP1
xref: UnificationXref928
feature: FragmentFeature143
cellular location: GO:0005829
comment: Reactome DB_ID: 3661539
display name: O94466

KLP5_SCHPO
type: Protein
entity reference: O14343
data source: Provenance1
name: Kinesin-like protein 5
xref: UnificationXref938
xref: UnificationXref939
feature: FragmentFeature145
cellular location: GO:0005829
comment: Reactome DB_ID: 984724
display name: klp5

Kinesin-8 monomers
type: Protein
data source: Provenance1
member physical entity: KLP6_SCHPO
member physical entity: KLP5_SCHPO
xref: UnificationXref943
xref: UnificationXref944
cellular location: GO:0005829
comment: Reactome DB_ID: 984594
comment: Converted from EntitySet in Reactome

Homologues of p-T507,S645,S664-PRKCD(1-676)
type: Protein
data source: Provenance1
member physical entity: phospho-p-T507,S645,S664-PRKCD(1-676)
xref: UnificationXref959
cellular location: GO:0005886
comment: Reactome DB_ID: 3661646
comment: Converted from EntitySet in Reactome

KLP6_SCHPO
type: Protein
entity reference: O59751
data source: Provenance1
name: Kinesin-like protein 6
xref: UnificationXref941
xref: UnificationXref942
feature: FragmentFeature146
cellular location: GO:0005829
comment: Reactome DB_ID: 984634
display name: klp6

Toll Like Receptor 9 (TLR9) Cascade
type: Pathway
data source: Provenance1
pathway component: REACT 91130.9
evidence: Evidence1044
xref: RelationshipXref879
xref: UnificationXref6678
xref: UnificationXref6679
pathway order: PathwayStep1024
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/7874169
type: PublicationXref
id: 7874169
author: Pulleyn, LJ
author: Schinzel, A
author: Losken, HW
author: Malcolm, S
author: Muenke, M
author: Schell, U
author: Reardon, W
author: Rutland, P
author: Robin, NH
author: Hehr, A
db: Pubmed
title: A common mutation in the fibroblast growth factor receptor 1 gene in Pfeiffer syndrome
source: Nat Genet 8:269-74
year: 1994

http://identifiers.org/pubmed/18653779
type: PublicationXref
id: 18653779
author: Sandahl, MA
author: Miraglia, L
author: Hunter, D
author: Earp HS, 3rd
author: Muraoka-Cook, RS
db: Pubmed
title: Prolactin and ErbB4/HER4 signaling interact via Janus kinase 2 to induce mammary epithelial cell gene expression differentiation
source: Mol Endocrinol 22:2307-21
year: 2008

phospho-p-T507,S645,S664-PRKCD(1-676)
type: Protein
entity reference: UniProt:P36582
data source: Provenance1
xref: UnificationXref957
feature: ModificationFeature11
feature: FragmentFeature147
feature: ModificationFeature12
feature: ModificationFeature10
cellular location: GO:0005886
comment: Reactome DB_ID: 3661641

http://identifiers.org/pubmed/2241899
type: PublicationXref
id: 2241899
author: Doyle, JM
author: Bossa, F
author: Doonan, S
author: Schinina, ME
db: Pubmed
title: The amino acid sequence of cytosolic aspartate aminotransferase from human liver
source: Biochem J 270:651-7
year: 1990

dCDP
type: SmallMoleculeReference
name: dCDP [ChEBI:28846]
name: 2'-Deoxycytidine diphosphate
name: 2'-Deoxycytidine 5'-diphosphate
xref: UnificationXref4407

http://identifiers.org/pubmed/17463226
type: PublicationXref
id: 17463226
author: Puggioni, EM
author: Cesareni, G
author: Gulino, A
author: Santangelo, L
author: Belleudi, F
author: Palumbo, C
author: Frati, L
author: Marrocco, J
author: Omerovic, J
author: Torrisi, MR
author: Di Marcotullio, L
author: Alimandi, M
author: Dall'Armi, C
db: Pubmed
title: The E3 ligase Aip4/Itch ubiquitinates and targets ErbB-4 for degradation
source: FASEB J 21:2849-62
year: 2007

UniProt:P24865
type: ProteinReference
xref: UnificationXref7538
organism: BioSource1

5'-Phosphoribosyl-5-aminoimidazole [ChEBI:28843]
type: SmallMoleculeReference
name: 5'-Phosphoribosyl-5-aminoimidazole
name: Aminoimidazole ribotide
name: 1-(5'-Phosphoribosyl)-5-aminoimidazole
name: 1-(5-Phospho-D-ribosyl)-5-aminoimidazole
name: AIR
xref: UnificationXref4115

http://identifiers.org/pubmed/17170135
type: PublicationXref
id: 17170135
author: Li, JL
author: Gimeno, RE
author: Li, D
author: Tobin, JF
author: Cao, J
db: Pubmed
title: Molecular identification of microsomal acyl-CoA:glycerol-3-phosphate acyltransferase, a key enzyme in de novo triacylglycerol synthesis
source: Proc Natl Acad Sci U S A 103:19695-700
year: 2006

UniProt:Q10452
type: ProteinReference
xref: UnificationXref8555
organism: BioSource1

http://identifiers.org/pubmed/8567683
type: PublicationXref
id: 8567683
author: Beardsley, GP
author: Moroson, BA
author: Rayl, EA
db: Pubmed
title: The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase
source: J Biol Chem 271:2225-2233
year: 1996

dUDP [ChEBI:28850]
type: SmallMoleculeReference
name: 2'-Deoxyuridine 5'-diphosphate
name: dUDP
xref: UnificationXref4436

UniProt:Q10445
type: ProteinReference
xref: UnificationXref275
organism: BioSource1

http://identifiers.org/pubmed/18762715
type: PublicationXref
id: 18762715
author: Ohta, KY
author: Yuasa, H
author: Inoue, K
author: Ishii, M
author: Katano, T
author: Watanabe, J
author: Ohgusu, Y
author: Urano, K
db: Pubmed
title: Functional characterization of human aquaporin 9 as a facilitative glycerol carrier
source: Drug Metab Pharmacokinet 23:279-84
year: 2008

http://identifiers.org/pubmed/21540551
type: PublicationXref
id: 21540551
author: Matejas, V
author: Kispert, A
author: Casarin, A
author: Faul, C
author: Pertegato, V
author: Akman, S
author: Kusakabe, T
author: Wang, S
author: Santos-Ocaña, C
author: Krick, S
author: Doimo, M
author: Hildebrandt, F
author: Chernin, G
author: Vega-Warner, V
author: McLaughlin, HM
author: Nürnberg, G
author: Navas, P
author: Chaki, M
author: Schoeb, DS
author: Becker, C
author: Saisawat, P
author: Heeringa, SF
author: Varpizen, S
author: Prokisch, H
author: Wiggins, RC
author: Nürnberg, P
author: Beissert, A
author: Zhou, W
author: Bakkaloglu, A
author: Ji, Z
author: Xie, LX
author: Hinkes, B
author: Bakkaloglu, SA
author: Salviati, L
author: Reiser, J
author: Vlangos, CN
author: Mir, S
author: Airik, R
author: Topaloglu, R
author: Sloan, AJ
author: Rötig, A
author: Trevisson, E
author: Gbadegesin, R
author: Raphael, Y
author: Zenker, M
author: Clarke, CF
author: Ozaltin, F
author: Soliman, NA
author: Müller, D
author: Berdeli, A
author: Ashraf, S
author: Killen, PD
author: Mundel, P
author: Hurd, TW
author: Giorgi, G
author: Ovunc, B
db: Pubmed
title: COQ6 mutations in human patients produce nephrotic syndrome with sensorineural deafness
source: J Clin Invest 121:2013-24
year: 2011

UniProt:Q10434
type: ProteinReference
xref: UnificationXref902
organism: BioSource1

http://identifiers.org/pubmed/12855817
type: PublicationXref
id: 12855817
author: Sato, S
author: Takeda, K
author: Takeuchi, O
author: Sanjo, H
author: Sugiyama, M
author: Hoshino, K
author: Kaisho, T
author: Hemmi, H
author: Okabe, M
author: Yamamoto, M
db: Pubmed
title: Role of adaptor TRIF in the MyD88-independent toll-like receptor signaling pathway
source: Science 301:640-3
year: 2003

UnificationXref6109
type: UnificationXref
id: 3657945
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657945

UnificationXref6105
type: UnificationXref
id: 3657944
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657944

UnificationXref6106
type: UnificationXref
id: REACT_97393
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_97393.9

UnificationXref6107
type: UnificationXref
id: 3665056
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665056

UnificationXref6108
type: UnificationXref
id: REACT_104214
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_104214.9

UnificationXref6101
type: UnificationXref
id: 3657941
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657941

UnificationXref6102
type: UnificationXref
id: 3657933
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657933

UnificationXref6103
type: UnificationXref
id: 3657942
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657942

UnificationXref6104
type: UnificationXref
id: 3657943
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657943

UniProt:Q10429
type: ProteinReference
xref: UnificationXref7750
organism: BioSource1

UniProt:Q10428
type: ProteinReference
xref: UnificationXref8567
organism: BioSource1

UnificationXref6100
type: UnificationXref
id: P30316
db: UniProt

UnificationXref6149
type: UnificationXref
id: 3665047
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665047

UnificationXref6144
type: UnificationXref
id: REACT_32076
db: Reactome
id version: 10
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_32076.10

UnificationXref6143
type: UnificationXref
id: 3665060
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665060

UnificationXref6142
type: UnificationXref
id: REACT_125903
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_125903.5

http://identifiers.org/pubmed/7641697
type: PublicationXref
id: 7641697
author: Nasmyth, K
author: Lengauer, C
author: Piatti, S
db: Pubmed
title: Cdc6 is an unstable protein whose de novo synthesis in G1 is important for the onset of S phase and for preventing a 'reductional' anaphase in the budding yeast Saccharomyces cerevisiae.
source: EMBO J 14:3788-99
year: 1995

UnificationXref6141
type: UnificationXref
id: 3657972
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657972

UnificationXref6148
type: UnificationXref
id: REACT_100837
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_100837.9

UnificationXref6147
type: UnificationXref
id: 3665058
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665058

UnificationXref6146
type: UnificationXref
id: REACT_87057
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_87057.9

UnificationXref6145
type: UnificationXref
id: 3665059
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665059

UniProt:Q10233
type: ProteinReference
xref: UnificationXref676
organism: BioSource1

UniProt:Q10232
type: ProteinReference
xref: UnificationXref1977
organism: BioSource1

UnificationXref6150
type: UnificationXref
id: REACT_98675
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_98675.9

UnificationXref6151
type: UnificationXref
id: 3665043
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665043

UniProt:Q10231
type: ProteinReference
xref: UnificationXref3012
organism: BioSource1

UnificationXref6139
type: UnificationXref
id: 69172
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=69172

UnificationXref6138
type: UnificationXref
id: REACT_99674
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_99674.9

UnificationXref6131
type: UnificationXref
id: 3657959
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657959

UnificationXref6130
type: UnificationXref
id: REACT_4584
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4584.1

2'-Deoxyguanosine 5'-diphosphate
type: SmallMoleculeReference
name: dGDP [ChEBI:28862]
name: dGDP
xref: UnificationXref4423

UnificationXref6133
type: UnificationXref
id: REACT_2427
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2427.1

UnificationXref6132
type: UnificationXref
id: 68469
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=68469

UnificationXref6135
type: UnificationXref
id: 3657966
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657966

UnificationXref6134
type: UnificationXref
id: 3657960
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657960

UnificationXref6137
type: UnificationXref
id: 3665061
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665061

UnificationXref6136
type: UnificationXref
id: REACT_82521
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_82521.9

UniProt:Q10243
type: ProteinReference
xref: UnificationXref1450
organism: BioSource1

UnificationXref6140
type: UnificationXref
id: REACT_4394
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4394.1

http://identifiers.org/pubmed/11429702
type: PublicationXref
id: 11429702
author: Colombo, G
author: Dell'Era, P
author: Neri, A
author: Lombardi, L
author: Greco, A
author: Otsuki, T
author: Ronchetti, D
author: Compasso, S
db: Pubmed
title: Deregulated FGFR3 mutants in multiple myeloma cell lines with t(4;14): comparative analysis of Y373C, K650E and the novel G384D mutations
source: Oncogene 20:3553-62
year: 2001

UnificationXref6129
type: UnificationXref
id: 68467
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=68467

UnificationXref6128
type: UnificationXref
id: REACT_84911
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_84911.9

UnificationXref6127
type: UnificationXref
id: 3657958
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657958

UnificationXref6126
type: UnificationXref
id: 3657957
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657957

UnificationXref6125
type: UnificationXref
id: 3657952
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657952

UnificationXref6124
type: UnificationXref
id: 3657956
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657956

UnificationXref6123
type: UnificationXref
id: Q9URU2
db: UniProt

UnificationXref6122
type: UnificationXref
id: REACT_81429
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_81429.9

UnificationXref6121
type: UnificationXref
id: 3657950
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657950

DNA replication initiation
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction542
pathway component: BiochemicalReaction541
evidence: Evidence919
xref: UnificationXref6023
xref: RelationshipXref803
xref: UnificationXref6024
pathway order: PathwayStep904
pathway order: PathwayStep903
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UnificationXref6120
type: UnificationXref
id: 3657949
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657949

Q09914
type: Protein
entity reference: UniProt:Q09914
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: RhoB
xref: UnificationXref743
feature: FragmentFeature97
cellular location: GO:0005829
comment: Reactome DB_ID: 3661456
display name: RHOB

UniProt:Q10258
type: ProteinReference
xref: UnificationXref4727
organism: BioSource1

Homologues of RHOB
type: Protein
data source: Provenance1
member physical entity: Q09914
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref746
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3661459

RHOA_HUMAN
type: Protein
entity reference: Q9HE04
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Q9HE04
name: RhoA
name: Transforming protein RhoA
xref: UnificationXref741
feature: FragmentFeature96
cellular location: GO:0005829
comment: Reactome DB_ID: 3661454
display name: RHOA

RHOA_HUMAN
type: Protein
entity reference: UniProt:Q10133
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Q10133
name: RhoA
name: Transforming protein RhoA
xref: UnificationXref739
feature: FragmentFeature95
cellular location: GO:0005829
comment: Reactome DB_ID: 3661453
display name: RHOA

phospho-p-Y173-VAV3
type: Protein
entity reference: P40995
data source: Provenance1
xref: UnificationXref760
feature: ModificationFeature8
feature: FragmentFeature101
cellular location: GO:0005829
comment: Reactome DB_ID: 3662882

UniProt:Q10254
type: ProteinReference
xref: UnificationXref8252
organism: BioSource1

phospho-p-Y172-VAV2
type: Protein
entity reference: P40995
data source: Provenance1
xref: UnificationXref755
feature: ModificationFeature7
feature: FragmentFeature100
cellular location: GO:0005829
comment: Reactome DB_ID: 3662876

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9HE04
data source: Provenance1
name: Q9HE04
name: RhoB
xref: UnificationXref745
feature: FragmentFeature99
cellular location: GO:0005829
comment: Reactome DB_ID: 3661458
display name: RHOB

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10133
data source: Provenance1
name: Q10133
name: RhoB
xref: UnificationXref744
feature: FragmentFeature98
cellular location: GO:0005829
comment: Reactome DB_ID: 3661457
display name: RHOB

UniProt:Q10251
type: ProteinReference
xref: UnificationXref7372
organism: BioSource1

UniProt:Q10252
type: ProteinReference
xref: UnificationXref3753
organism: BioSource1

RHOA_HUMAN
type: Protein
entity reference: UniProt:Q09914
data source: Provenance1
name: Q09914
name: Note: the coordinates are copied over from Homo sapiens.
name: RhoA
name: Transforming protein RhoA
xref: UnificationXref737
feature: FragmentFeature94
cellular location: GO:0005829
comment: Reactome DB_ID: 3661452
display name: RHOA

http://identifiers.org/pubmed/12702875
type: PublicationXref
id: 12702875
author: Milton, SC
author: McIntire, TM
author: Glabe, CG
author: Cotman, CW
author: Head, E
author: Kayed, R
author: Thompson, JL
db: Pubmed
title: Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
source: Science 300:486-9
year: 2003

Homologues of RHOA
type: Protein
data source: Provenance1
member physical entity: RHOA_HUMAN
xref: UnificationXref742
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3661455

Cytosolic tRNA aminoacylation
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction632
pathway component: BiochemicalReaction633
pathway component: BiochemicalReaction630
pathway component: BiochemicalReaction629
pathway component: BiochemicalReaction628
pathway component: pyrophosphate + H2O => 2 orthophosphate [cytosolic]
pathway component: BiochemicalReaction626
pathway component: BiochemicalReaction625
pathway component: BiochemicalReaction631
pathway component: BiochemicalReaction627
evidence: Evidence1115
xref: UnificationXref7071
xref: RelationshipXref927
xref: UnificationXref7072
pathway order: PathwayStep1088
pathway order: PathwayStep1094
pathway order: PathwayStep1086
pathway order: PathwayStep1087
pathway order: PathwayStep1090
pathway order: PathwayStep1093
pathway order: PathwayStep1089
pathway order: PathwayStep1092
pathway order: PathwayStep287
pathway order: PathwayStep1091
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UnificationXref6117
type: UnificationXref
id: REACT_68438
db: Reactome
id version: 10
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_68438.10

UnificationXref6116
type: UnificationXref
id: 3657948
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657948

UnificationXref6119
type: UnificationXref
id: REACT_3907
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3907.1

UnificationXref6118
type: UnificationXref
id: 68454
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=68454

UnificationXref6113
type: UnificationXref
id: 68452
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=68452

UnificationXref6112
type: UnificationXref
id: REACT_129158
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_129158.5

UnificationXref6115
type: UnificationXref
id: 3657946
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3657946

UnificationXref6114
type: UnificationXref
id: REACT_4386
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4386.1

UnificationXref6111
type: UnificationXref
id: 3665057
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665057

UnificationXref6110
type: UnificationXref
id: REACT_144983
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_144983.5

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36582
data source: Provenance1
name: Protein kinase C, delta type
name: nPKC-delta
name: PRKCD(1-676)
name: P36582
xref: UnificationXref785
feature: FragmentFeature104
cellular location: GO:0005829
comment: Reactome DB_ID: 3661631
display name: PRKCD

Homologues of PRKCD(1-676)
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref788
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3661633

Homologues of PRKCE
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref791
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3661636

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36583
data source: Provenance1
name: Protein kinase C, delta type
name: nPKC-delta
name: PRKCD(1-676)
name: P36583
xref: UnificationXref787
feature: FragmentFeature105
cellular location: GO:0005829
comment: Reactome DB_ID: 3661632
display name: PRKCD

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36583
data source: Provenance1
name: nPKC-epsilon
name: Protein kinase C, epsilon type
name: P36583
xref: UnificationXref790
feature: FragmentFeature107
cellular location: GO:0005829
comment: Reactome DB_ID: 3661635
display name: PRKCE

UniProt:Q10267
type: ProteinReference
xref: UnificationXref1778
organism: BioSource1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36582
data source: Provenance1
name: nPKC-epsilon
name: Protein kinase C, epsilon type
name: P36582
xref: UnificationXref789
feature: FragmentFeature106
cellular location: GO:0005829
comment: Reactome DB_ID: 3661634
display name: PRKCE

Homologues of PRKCH
type: Protein
data source: Provenance1
member physical entity: Protein kinase C, eta type
xref: UnificationXref794
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3662605

VAV family
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref765
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3662823

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P40995
data source: Provenance1
name: P40995
xref: UnificationXref764
feature: FragmentFeature103
cellular location: GO:0005829
comment: Reactome DB_ID: 3661470
display name: VAV2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P40995
data source: Provenance1
name: P40995
xref: UnificationXref763
feature: FragmentFeature102
cellular location: GO:0005829
comment: Reactome DB_ID: 3661469
display name: VAV1

UnificationXref6187
type: UnificationXref
id: 3664040
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664040

UnificationXref6188
type: UnificationXref
id: 3664042
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664042

UnificationXref6185
type: UnificationXref
id: 3664038
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664038

UnificationXref6186
type: UnificationXref
id: 3664039
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664039

UnificationXref6189
type: UnificationXref
id: REACT_154258
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_154258.3

Homologues of PRKCQ
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref797
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3661800

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36582
data source: Provenance1
name: nPKC-theta
name: Protein kinase C, theta type
name: P36582
xref: UnificationXref795
feature: FragmentFeature110
cellular location: GO:0005829
comment: Reactome DB_ID: 3661798
display name: PRKCQ

organic anion
type: SmallMolecule
entity reference: CHEBI:25696
data source: Provenance1
xref: UnificationXref6180
xref: UnificationXref6179
cellular location: GO:0005576
comment: Reactome DB_ID: 1454919

Protein kinase C, eta type
type: Protein
entity reference: UniProt:P36582
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: PKC-L
name: nPKC-eta
name: P36582
xref: UnificationXref792
feature: FragmentFeature108
cellular location: GO:0005829
comment: Reactome DB_ID: 3662603
display name: PRKCH

organic anion
type: SmallMolecule
entity reference: CHEBI:25696
data source: Provenance1
xref: UnificationXref6177
xref: UnificationXref6178
cellular location: GO:0005829
comment: Reactome DB_ID: 1454930

Protein kinase C, eta type
type: Protein
entity reference: UniProt:P36583
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: PKC-L
name: nPKC-eta
name: P36583
xref: UnificationXref793
feature: FragmentFeature109
cellular location: GO:0005829
comment: Reactome DB_ID: 3662604
display name: PRKCH

porphyrin
type: SmallMolecule
entity reference: Porphyrin
data source: Provenance1
xref: UnificationXref6167
xref: UnificationXref6168
cellular location: GO:0005759
comment: Reactome DB_ID: 1369027

2'-deoxyguanosine 5'-triphosphate
type: SmallMolecule
entity reference: CHEBI:16497
data source: Provenance1
name: Deoxyguanosine 5'-triphosphate
name: Deoxyguanosine triphosphate
xref: UnificationXref6012
xref: UnificationXref6011
cellular location: GO:0005654
comment: Reactome DB_ID: 29892
display name: dGTP

UnificationXref6191
type: UnificationXref
id: REACT_80848
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_80848.9

deoxycytidine 5'-triphosphate
type: SmallMolecule
entity reference: CHEBI:16311
data source: Provenance1
name: Deoxycytidine triphosphate
name: 2'-Deoxycytidine 5'-triphosphate
xref: UnificationXref6008
xref: UnificationXref6009
cellular location: GO:0005654
comment: Reactome DB_ID: 30185
display name: dCTP

UnificationXref6190
type: UnificationXref
id: 3665447
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665447

http://identifiers.org/pubmed/1976634
type: PublicationXref
id: 1976634
author: Hurwitz, J
author: Lee, SH
author: Kwong, AD
db: Pubmed
title: The in vitro replication of DNA containing the SV40 origin.
source: J Biol Chem 265:18043-6
year: 1990

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36583
data source: Provenance1
name: Protein kinase C, alpha type
name: PKC-A
name: PKC-alpha
name: P36583
xref: UnificationXref829
feature: FragmentFeature114
cellular location: GO:0005829
comment: Reactome DB_ID: 3660492
display name: PRKCA

5-Hydroxyindole acetic acid
type: SmallMolecule
entity reference: CHEBI:27823
data source: Provenance1
xref: UnificationXref5872
xref: UnificationXref5873
cellular location: GO:0005759
comment: Reactome DB_ID: 380593
display name: HIAA

Homologues of PRKCB
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref833
cellular location: GO:0005829
comment: Reactome DB_ID: 3660496
comment: Converted from EntitySet in Reactome

Homologues of PRKCA
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref830
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3660493

porphyrin
type: SmallMolecule
entity reference: Porphyrin
data source: Provenance1
xref: UnificationXref6166
xref: UnificationXref6165
cellular location: GO:0005829
comment: Reactome DB_ID: 1369066

UnificationXref6195
type: UnificationXref
id: 74112
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=74112

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36582
data source: Provenance1
name: Protein kinase C, alpha type
name: PKC-A
name: P36582
name: PKC-alpha
xref: UnificationXref828
feature: FragmentFeature113
cellular location: GO:0005829
comment: Reactome DB_ID: 3660488
display name: PRKCA

heme (ferrous)
type: SmallMolecule
entity reference: CHEBI:17627
data source: Provenance1
xref: UnificationXref6159
xref: UnificationXref6160
cellular location: GO:0005829
comment: Reactome DB_ID: 71185
display name: heme

UnificationXref6194
type: UnificationXref
id: REACT_19724
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19724.1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36583
data source: Provenance1
name: nPKC-theta
name: Protein kinase C, theta type
name: P36583
xref: UnificationXref796
feature: FragmentFeature111
cellular location: GO:0005829
comment: Reactome DB_ID: 3661799
display name: PRKCQ

2'-deoxyadenosine 5'-triphosphate
type: SmallMolecule
entity reference: 2'-deoxyadenosine 5'-triphosphate
data source: Provenance1
name: Deoxyadenosine 5'-triphosphate
name: Deoxyadenosine triphosphate
xref: UnificationXref6017
xref: UnificationXref6016
cellular location: GO:0005654
comment: Reactome DB_ID: 29604
display name: dATP

UnificationXref6193
type: UnificationXref
id: 425815
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=425815

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94305
data source: Provenance1
name: O94305
name: Monoglyceride lipase
xref: UnificationXref818
feature: FragmentFeature112
cellular location: GO:0005886
comment: Reactome DB_ID: 3662621
display name: MGLL

Deoxythymidine 5'-triphosphate
type: SmallMolecule
entity reference: TTP
data source: Provenance1
name: dTTP
name: Deoxythymidine triphosphate
xref: UnificationXref6015
xref: UnificationXref6014
cellular location: GO:0005654
comment: Reactome DB_ID: 30187
display name: TTP

UnificationXref6192
type: UnificationXref
id: CHEBI:49713
db: ChEBI

UnificationXref6174
type: UnificationXref
id: 3665446
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665446

UnificationXref6175
type: UnificationXref
id: REACT_114366
db: Reactome
id version: 8
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_114366.8

UnificationXref6176
type: UnificationXref
id: CHEBI:25696
db: ChEBI

UnificationXref6177
type: UnificationXref
id: 1454930
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1454930

UnificationXref6178
type: UnificationXref
id: REACT_111889
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_111889.1

UnificationXref6179
type: UnificationXref
id: 1454919
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1454919

http://identifiers.org/pubmed/7913309
type: PublicationXref
id: 7913309
author: Rokosz, LL
author: Cueto, MA
author: Butkiewicz, EA
author: Hermes, JD
author: Boulton, DA
author: Sanyal, G
author: Lachance, PA
db: Pubmed
title: Human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme A synthase: expression, purification, and characterization of recombinant wild-type and Cys129 mutant enzymes
source: Arch Biochem Biophys 312:1-13
year: 1994

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36583
data source: Provenance1
name: Protein kinase C, beta type
name: PKC-beta
name: PKC-B
name: P36583
xref: UnificationXref832
feature: FragmentFeature116
cellular location: GO:0005829
comment: Reactome DB_ID: 3660495
display name: PRKCB

Homologues of PRKCG
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref836
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3660499

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36582
data source: Provenance1
name: PKC-gamma
name: P36582
name: Protein kinase C, gamma type
xref: UnificationXref834
feature: FragmentFeature117
cellular location: GO:0005829
comment: Reactome DB_ID: 3660497
display name: PRKCG

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36583
data source: Provenance1
name: PKC-gamma
name: P36583
name: Protein kinase C, gamma type
xref: UnificationXref835
feature: FragmentFeature118
cellular location: GO:0005829
comment: Reactome DB_ID: 3660498
display name: PRKCG

UniProt:Q10283
type: ProteinReference
xref: UnificationXref2867
organism: BioSource1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36582
data source: Provenance1
name: Protein kinase C, beta type
name: PKC-beta
name: PKC-B
name: P36582
xref: UnificationXref831
feature: FragmentFeature115
cellular location: GO:0005829
comment: Reactome DB_ID: 3660494
display name: PRKCB

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36582
data source: Provenance1
name: Protein kinase C, beta type
name: PKC-beta
name: PKC-B
name: P36582
xref: UnificationXref847
feature: FragmentFeature121
cellular location: GO:0005886
comment: Reactome DB_ID: 3660505
display name: PRKCB

UnificationXref6180
type: UnificationXref
id: REACT_111412
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_111412.1

Homologues of PRKCA
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref843
cellular location: GO:0005886
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3660503

UnificationXref6182
type: UnificationXref
id: 3664035
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664035

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36582
data source: Provenance1
name: Protein kinase C, alpha type
name: PKC-A
name: P36582
name: PKC-alpha
xref: UnificationXref841
feature: FragmentFeature119
cellular location: GO:0005886
comment: Reactome DB_ID: 3660501
display name: PRKCA

UnificationXref6181
type: UnificationXref
id: 3664034
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664034

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36583
data source: Provenance1
name: Protein kinase C, alpha type
name: PKC-A
name: PKC-alpha
name: P36583
xref: UnificationXref842
feature: FragmentFeature120
cellular location: GO:0005886
comment: Reactome DB_ID: 3660502
display name: PRKCA

UnificationXref6184
type: UnificationXref
id: 3664037
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664037

Homologues of PRKCB
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref849
cellular location: GO:0005886
comment: Reactome DB_ID: 3660507
comment: Converted from EntitySet in Reactome

UnificationXref6183
type: UnificationXref
id: 3664036
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664036

UnificationXref6169
type: UnificationXref
id: Q02592
db: UniProt

L-alpha-Alanine
type: SmallMolecule
entity reference: CHEBI:16977
data source: Provenance1
name: L-Alanine
name: L-2-Aminopropionic acid
xref: UnificationXref6273
xref: UnificationXref6272
cellular location: GO:0043202
comment: Reactome DB_ID: 428020
display name: L-Ala

(S)-2-Amino-5-guanidinovaleric acid
type: SmallMolecule
entity reference: CHEBI:16467
data source: Provenance1
name: L-Arginine
xref: UnificationXref6274
xref: UnificationXref6275
cellular location: GO:0043202
comment: Reactome DB_ID: 428011
display name: L-Arg

UnificationXref6167
type: UnificationXref
id: 1369027
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1369027

UnificationXref6168
type: UnificationXref
id: REACT_111818
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_111818.1

UnificationXref6165
type: UnificationXref
id: 1369066
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1369066

UnificationXref6166
type: UnificationXref
id: REACT_111450
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_111450.1

UnificationXref6163
type: UnificationXref
id: REACT_110174
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_110174.9

UnificationXref6164
type: UnificationXref
id: CHEBI:8337
db: ChEBI

http://identifiers.org/pubmed/19244215
type: PublicationXref
id: 19244215
author: Buczynski, MW
author: Dumlao, DS
author: Dennis, EA
db: Pubmed
title: Thematic Review Series: Proteomics. An integrated omics analysis of eicosanoid biology
source: J Lipid Res 50:1015-38
year: 2009

Activation of Chaperones by ATF6-alpha
type: Pathway
data source: Provenance1
pathway component: REACT 141651.5
evidence: Evidence1349
xref: UnificationXref8506
xref: UnificationXref8505
xref: RelationshipXref1095
pathway order: PathwayStep1327
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36583
data source: Provenance1
name: Protein kinase C, beta type
name: PKC-beta
name: PKC-B
name: P36583
xref: UnificationXref848
feature: FragmentFeature122
cellular location: GO:0005886
comment: Reactome DB_ID: 3660506
display name: PRKCB

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94590
data source: Provenance1
name: Platelet SEC1 protein
name: O94590
xref: UnificationXref857
feature: FragmentFeature123
cellular location: GO:0005829
comment: Reactome DB_ID: 3660516
display name: STXBP3

Platelet releasate cytosolic proteins
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
member physical entity: O74759
xref: UnificationXref877
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3663203

http://identifiers.org/pubmed/12648452
type: PublicationXref
id: 12648452
author: Buttgereit, F
author: Qian, SB
author: Finzi, D
author: Princiotta, MF
author: Yewdell, JW
author: Gibbs, J
author: Bennink, JR
author: Schuchmann, S
db: Pubmed
title: Quantitating protein synthesis, degradation, and endogenous antigen processing
source: Immunity 18:343-54
year: 2003

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14301
data source: Provenance1
name: WD repeat-containing protein 1
name: WDR1_HUMAN
name: O14301
xref: UnificationXref872
feature: FragmentFeature126
cellular location: GO:0005829
comment: Reactome DB_ID: 3663194
display name: WDR1

phospho-p-STXBP3
type: Protein
entity reference: O94590
data source: Provenance1
xref: UnificationXref860
feature: FragmentFeature124
feature: ModificationFeature9
cellular location: GO:0005829
comment: Reactome DB_ID: 3660518

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9USH7
data source: Provenance1
name: Q9USH7
name: Syntaxin 4
xref: UnificationXref866
feature: FragmentFeature125
cellular location: GO:0005829
comment: Reactome DB_ID: 3660524
display name: STX4

L-Amino Acids
type: SmallMolecule
data source: Provenance1
member physical entity: (S)-2-Amino-3-(p-hydroxyphenyl)propionic acid
member physical entity: L-Methionine
member physical entity: 2-aminosuccinic acid
member physical entity: L-serine
member physical entity: L-Threonine
member physical entity: L-alpha-Alanine
member physical entity: L-2-amino-3-mercaptopropionic acid
member physical entity: 2-Amino-3-methylbutyric acid
member physical entity: (S)-alpha-Amino-1H-imidazole-4-propionic acid
member physical entity: 2,6-diaminohexanoic acid
member physical entity: Glycine
member physical entity: L-Glutaminic acid
member physical entity: L-Phenylalanine
member physical entity: L-Isoleucine
member physical entity: L-Leucine
member physical entity: L-Glutamine
member physical entity: 2-Pyrrolidinecarboxylic acid
member physical entity: L-Asparagine
member physical entity: (S)-alpha-amino-beta-(3-indolyl)-propionic acid
member physical entity: (S)-2-Amino-5-guanidinovaleric acid
xref: UnificationXref6311
xref: UnificationXref6310
cellular location: GO:0043202
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 427988

Platelet releasate cytosolic proteins
type: Protein
data source: Provenance1
member physical entity: O74759
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref882
cellular location: GO:0005576
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3663207

UnificationXref6173
type: UnificationXref
id: REACT_146916
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_146916.5

(S)-alpha-Amino-1H-imidazole-4-propionic acid
type: SmallMolecule
entity reference: CHEBI:15971
data source: Provenance1
name: L-Histidine
xref: UnificationXref6270
xref: UnificationXref6271
cellular location: GO:0043202
comment: Reactome DB_ID: 428038
display name: L-His

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14301
data source: Provenance1
name: WD repeat-containing protein 1
name: WDR1_HUMAN
name: O14301
xref: UnificationXref879
feature: FragmentFeature129
cellular location: GO:0005576
comment: Reactome DB_ID: 3663204
display name: WDR1

UnificationXref6172
type: UnificationXref
id: 3664019
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664019

(S)-2-Amino-3-(p-hydroxyphenyl)propionic acid
type: SmallMolecule
entity reference: CHEBI:17895
data source: Provenance1
name: L-Tyrosine
name: (S)-3-(p-Hydroxyphenyl)alanine
xref: UnificationXref6254
xref: UnificationXref6253
cellular location: GO:0005829
comment: Reactome DB_ID: 29506
display name: L-Tyr

O74759
type: Protein
entity reference: O74759
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Bromodomain and PHD finger-containing protein 3
xref: UnificationXref874
feature: FragmentFeature127
cellular location: GO:0005829
comment: Reactome DB_ID: 3663198
display name: BRPF3

UnificationXref6171
type: UnificationXref
id: 3664017
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664017

(S)-alpha-amino-beta-(3-indolyl)-propionic acid
type: SmallMolecule
entity reference: CHEBI:16828
data source: Provenance1
name: L-Tryptophan
xref: UnificationXref6252
xref: UnificationXref6251
cellular location: GO:0005829
comment: Reactome DB_ID: 29500
display name: L-Trp

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:O42914
data source: Provenance1
name: Intracellular hyaluronan-binding protein 4
name: O42914
xref: UnificationXref876
feature: FragmentFeature128
cellular location: GO:0005829
comment: Reactome DB_ID: 3663202
display name: HABP4

UnificationXref6170
type: UnificationXref
id: 3664016
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664016

L-Threonine
type: SmallMolecule
entity reference: CHEBI:16857
data source: Provenance1
xref: UnificationXref6250
xref: UnificationXref6249
cellular location: GO:0005829
comment: Reactome DB_ID: 351990
display name: L-Thr

http://identifiers.org/pubmed/17371050
type: PublicationXref
id: 17371050
author: Kondo, N
author: Fukao, T
author: Haapalainen, AM
author: Wierenga, RK
author: Meriläinen, G
author: Pirilä, PL
db: Pubmed
title: Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase: the importance of potassium and chloride ions for its structure and function
source: Biochemistry 46:4305-21
year: 2007

2-Pyrrolidinecarboxylic acid
type: SmallMolecule
entity reference: CHEBI:17203
data source: Provenance1
name: L-Proline
xref: UnificationXref6247
xref: UnificationXref6248
cellular location: GO:0005829
comment: Reactome DB_ID: 113538
display name: L-Pro

2,6-diaminohexanoic acid
type: SmallMolecule
entity reference: 2,6-diaminohexanoic acid
data source: Provenance1
name: Lysine acid
name: L-Lysine
xref: UnificationXref6245
xref: UnificationXref6246
cellular location: GO:0005829
comment: Reactome DB_ID: 351979
display name: L-Lys

(S)-alpha-Amino-1H-imidazole-4-propionic acid
type: SmallMolecule
entity reference: CHEBI:15971
data source: Provenance1
name: L-Histidine
xref: UnificationXref6243
xref: UnificationXref6244
cellular location: GO:0005829
comment: Reactome DB_ID: 29612
display name: L-His

L-Amino Acids
type: SmallMolecule
data source: Provenance1
member physical entity: L-Glutamine
member physical entity: L-serine
member physical entity: SmallMolecule95
member physical entity: (S)-alpha-Amino-1H-imidazole-4-propionic acid
member physical entity: L-Leucine
member physical entity: L-Threonine
member physical entity: L-Phenylalanine
member physical entity: SmallMolecule97
member physical entity: L-glycine
member physical entity: L-2-amino-3-mercaptopropionic acid
member physical entity: L-alpha-Alanine
member physical entity: L-Methionine
member physical entity: 2-Pyrrolidinecarboxylic acid
member physical entity: (S)-2-Amino-3-(p-hydroxyphenyl)propionic acid
member physical entity: (S)-2-Amino-5-guanidinovaleric acid
member physical entity: L-Asparagine
member physical entity: L-Isoleucine
member physical entity: 2,6-diaminohexanoic acid
member physical entity: 2-Amino-3-methylbutyric acid
member physical entity: (S)-alpha-amino-beta-(3-indolyl)-propionic acid
xref: UnificationXref6256
xref: UnificationXref6255
cellular location: GO:0005829
comment: Reactome DB_ID: 400144
comment: Converted from EntitySet in Reactome

UnificationXref6156
type: UnificationXref
id: REACT_103462
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_103462.9

UnificationXref6157
type: UnificationXref
id: 3665041
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665041

UnificationXref6158
type: UnificationXref
id: REACT_77135
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_77135.9

UnificationXref6159
type: UnificationXref
id: 71185
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=71185

H+
type: SmallMolecule
entity reference: CHEBI:15378
data source: Provenance1
xref: UnificationXref6235
xref: UnificationXref6236
cellular location: GO:0005576
comment: Reactome DB_ID: 351626

UnificationXref6152
type: UnificationXref
id: REACT_103522
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_103522.9

UnificationXref6153
type: UnificationXref
id: 3665054
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665054

UnificationXref6154
type: UnificationXref
id: REACT_81203
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_81203.9

UnificationXref6155
type: UnificationXref
id: 3665044
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665044

http://identifiers.org/pubmed/9852097
type: PublicationXref
id: 9852097
author: Kerr, TA
author: Russell, DW
author: Li, WP
author: Sakai, J
author: Lund, EG
db: Pubmed
title: cDNA cloning of mouse and human cholesterol 25-hydroxylases, polytopic membrane proteins that synthesize a potent oxysterol regulator of lipid metabolism
source: J Biol Chem 273:34316-27
year: 1998

O74759
type: Protein
entity reference: O74759
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Bromodomain and PHD finger-containing protein 3
xref: UnificationXref880
feature: FragmentFeature130
cellular location: GO:0005576
comment: Reactome DB_ID: 3663205
display name: BRPF3

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:O42914
data source: Provenance1
name: Intracellular hyaluronan-binding protein 4
name: O42914
xref: UnificationXref881
feature: FragmentFeature131
cellular location: GO:0005576
comment: Reactome DB_ID: 3663206
display name: HABP4

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P78929
data source: Provenance1
name: COF1_HUMAN
name: P78929
name: Cofilin-1
xref: UnificationXref886
feature: FragmentFeature132
cellular location: GO:0005829
comment: Reactome DB_ID: 3662550
display name: CFL1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P78929
data source: Provenance1
name: COF1_HUMAN
name: P78929
name: Cofilin-1
xref: UnificationXref887
feature: FragmentFeature133
cellular location: GO:0005576
comment: Reactome DB_ID: 3663209
display name: CFL1

Sodium ion
type: SmallMolecule
entity reference: CHEBI:29101
data source: Provenance1
xref: UnificationXref6228
xref: UnificationXref6229
cellular location: late endosome lumen
comment: Reactome DB_ID: 425977
display name: Na+

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36604
data source: Provenance1
name: 78 kDa glucose-regulated protein
name: GRP78
name: HSPA5
name: P36604
xref: UnificationXref892
feature: FragmentFeature134
cellular location: GO:0005789
comment: Reactome DB_ID: 3662221
display name: BiP

H+
type: SmallMolecule
entity reference: CHEBI:15378
data source: Provenance1
xref: UnificationXref6227
xref: UnificationXref6226
cellular location: late endosome lumen
comment: Reactome DB_ID: 425999

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36604
data source: Provenance1
name: 78 kDa glucose-regulated protein
name: P36604
xref: UnificationXref893
feature: FragmentFeature135
cellular location: GO:0005576
comment: Reactome DB_ID: 3662222
display name: HSPA5

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10434
data source: Provenance1
name: F-actin-capping protein subunit alpha-1
name: CAZA1_HUMAN
name: Q10434
xref: UnificationXref903
feature: FragmentFeature136
cellular location: GO:0005829
comment: Reactome DB_ID: 3663361
display name: CAPZA1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9HGP5
data source: Provenance1
name: Q9HGP5
name: CAPZB_HUMAN
name: F-actin-capping protein subunit beta
xref: UnificationXref905
feature: FragmentFeature137
cellular location: GO:0005829
comment: Reactome DB_ID: 3663365
display name: CAPZB

UnificationXref6160
type: UnificationXref
id: REACT_2784
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2784.3

Sodium ion
type: SmallMolecule
entity reference: CHEBI:29101
data source: Provenance1
xref: UnificationXref6211
xref: UnificationXref6212
cellular location: early endosome lumen
comment: Reactome DB_ID: 425971
display name: Na+

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P36586
data source: Provenance1
name: RAB5A_HUMAN
name: P36586
name: Ras-related protein Rab-5A
name: RAB5A(2-215)
xref: UnificationXref911
feature: FragmentFeature138
cellular location: GO:0010008
comment: Reactome DB_ID: 3663704
display name: RAB5A

Sodium
type: SmallMolecule
entity reference: CHEBI:29101
data source: Provenance1
name: sodium ion
xref: UnificationXref6210
xref: UnificationXref6209
cellular location: GO:0005829
comment: Reactome DB_ID: 83910
display name: Na+

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09805
data source: Provenance1
name: Vacuolar protein sorting-associated protein 45
name: Q09805
name: VPS45_HUMAN
xref: UnificationXref913
feature: FragmentFeature139
cellular location: GO:0010008
comment: Reactome DB_ID: 3663712
display name: VPS45

UnificationXref6162
type: UnificationXref
id: 3662472
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662472

Sodium
type: SmallMolecule
entity reference: CHEBI:29101
data source: Provenance1
name: sodium ion
xref: UnificationXref6221
xref: UnificationXref6220
cellular location: GO:0005796
comment: Reactome DB_ID: 425958
display name: Na+

UnificationXref6161
type: UnificationXref
id: 3662470
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662470

H+
type: SmallMolecule
entity reference: CHEBI:15378
data source: Provenance1
xref: UnificationXref6218
xref: UnificationXref6219
cellular location: GO:0005796
comment: Reactome DB_ID: 425969

http://identifiers.org/pubmed/11698644
type: PublicationXref
id: 11698644
author: Kabashima, T
author: Uyeda, K
author: Kawaguchi, T
author: Takenoshita, M
db: Pubmed
title: Glucose and cAMP regulate the L-type pyruvate kinase gene by phosphorylation/dephosphorylation of the carbohydrate response element binding protein
source: Proc Natl Acad Sci U S A 98:13710-5
year: 2001

Calcium
type: SmallMolecule
entity reference: CHEBI:29108
data source: Provenance1
xref: UnificationXref6196
xref: UnificationXref6195
cellular location: GO:0005576
comment: Reactome DB_ID: 74112
display name: Ca2+

Lithium ion
type: SmallMolecule
entity reference: CHEBI:49713
data source: Provenance1
xref: UnificationXref6194
xref: UnificationXref6193
cellular location: GO:0005576
comment: Reactome DB_ID: 425815
display name: Li+

H+
type: SmallMolecule
entity reference: CHEBI:15378
data source: Provenance1
xref: UnificationXref6207
xref: UnificationXref6206
cellular location: early endosome lumen
comment: Reactome DB_ID: 425978

Lithium ion
type: SmallMolecule
entity reference: CHEBI:49713
data source: Provenance1
xref: UnificationXref6197
xref: UnificationXref6198
cellular location: GO:0005829
comment: Reactome DB_ID: 425810
display name: Li+

(S)-alpha-amino-beta-(3-indolyl)-propionic acid
type: SmallMolecule
entity reference: CHEBI:16828
data source: Provenance1
name: L-Tryptophan
xref: UnificationXref6299
xref: UnificationXref6298
cellular location: GO:0043202
comment: Reactome DB_ID: 427978
display name: L-Trp

(S)-2-Amino-3-(p-hydroxyphenyl)propionic acid
type: SmallMolecule
entity reference: CHEBI:17895
data source: Provenance1
name: L-Tyrosine
name: (S)-3-(p-Hydroxyphenyl)alanine
xref: UnificationXref6300
xref: UnificationXref6301
cellular location: GO:0043202
comment: Reactome DB_ID: 427993
display name: L-Tyr

2-Amino-3-methylbutyric acid
type: SmallMolecule
entity reference: CHEBI:16414
data source: Provenance1
name: L-Valine
xref: UnificationXref6302
xref: UnificationXref6303
cellular location: GO:0043202
comment: Reactome DB_ID: 428002
display name: L-Val

L-2-amino-3-mercaptopropionic acid
type: SmallMolecule
entity reference: CHEBI:17561
data source: Provenance1
name: L-cysteine
xref: UnificationXref6305
xref: UnificationXref6304
cellular location: GO:0043202
comment: Reactome DB_ID: 427991
display name: L-Cys

L-serine
type: SmallMolecule
entity reference: CHEBI:17115
data source: Provenance1
xref: UnificationXref6307
xref: UnificationXref6306
cellular location: GO:0043202
comment: Reactome DB_ID: 427967
display name: L-Ser

Glycine
type: SmallMolecule
entity reference: CHEBI:15428
data source: Provenance1
name: Aminoacetic acid
xref: UnificationXref6309
xref: UnificationXref6308
cellular location: GO:0043202
comment: Reactome DB_ID: 427960
display name: Gly

H+
type: SmallMolecule
entity reference: CHEBI:15378
data source: Provenance1
xref: UnificationXref6317
xref: UnificationXref6316
cellular location: GO:0043202
comment: Reactome DB_ID: 428040

Evidence939
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9191022
xref: http://identifiers.org/pubmed/7378348
xref: http://identifiers.org/pubmed/2175912
comment: The processive complex is responsible for synthesizing at least 5-10 kb of DNA in a continuous manner during leading strand synthesis. The incorporation of nucleotides by pol delta is quite accurate. However, incorporation of an incorrect nucleotide does occur occasionally. Misincorporated nucleotides are removed by the 3' to 5' exonucleolytic proofreading capability of pol delta.

Evidence932
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15707891
xref: http://identifiers.org/pubmed/10834843
comment: DNA Replication is regulated accurately and precisely by various protein complexes. Many members of the MCM protein family are assembled into the pre-Replication Complexes (pre-RC) at the end of M phase of the cell cycle. DNA helicase activity of some of the MCM family proteins are important for the unwinding of DNA and initiation of replication processes. This section contains four events which have been proved in different eukaryotic experimental systems to involve various proteins for this essential step during DNA Replication.

Cytosolic Iron-sulfur Cluster Assembly
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction505
pathway component: BiochemicalReaction506
evidence: Evidence845
xref: UnificationXref5613
xref: UnificationXref5612
pathway order: PathwayStep834
pathway order: PathwayStep835
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Evidence931
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16483939
comment: By applying the chromatin immunoprecipitation technique to paused forks, certain proteins like DNA pol alpha, DNA pol delta, DNA pol epsilon, MCM2-7, CDC45, GINS and MCM10 were identified. By uncoupling a helicase at the site using a polymerase inhibitor, MCM2-7, GINS complex and CDC45 alone were found to be enriched at the paused fork suggesting these proteins may form a part of an "unwindosome" at the replicating fork.

Evidence934
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/2165567
xref: http://identifiers.org/pubmed/9660172
comment: The binding of the primer recognition complex involves the loading of proliferating cell nuclear antigen (PCNA). Replication Factor C transiently opens the PCNA toroid in an ATP-dependent reaction, and then allows PCNA to re-close around the double helix adjacent to the primer terminus. This leads to the formation of the "sliding clamp".

Evidence933
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1671046
xref: http://identifiers.org/pubmed/10656792
xref: http://identifiers.org/pubmed/10656791
comment: Once the RNA-DNA primer is synthesized, replication factor C (RFC) initiates a reaction called "polymerase switching"; pol delta, the processive enzyme replaces pol alpha, the priming enzyme. RFC binds to the 3'-end of the RNA-DNA primer on the Primosome, to displace the pol alpha primase complex. The binding of RFC triggers the binding of the primer recognition complex.

Evidence936
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7713898
xref: http://identifiers.org/pubmed/1974050
xref: http://identifiers.org/pubmed/1682322
xref: http://identifiers.org/pubmed/8104944
comment: The loading of proliferating cell nuclear antigen (PCNA) leads to recruitment of pol delta. Human PCNA is a homotrimer of 36 kDa subunits that form a toroidal structure. The loading of PCNA by RFC is a key event in the transition from the priming mode to the extension mode of DNA synthesis. The processive complex is composed of the pol delta holoenzyme and PCNA.

Evidence935
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9822671
comment: Replication factor C is proposed to dissociate from PCNA following sliding clamp formation, and the DNA toroid alone tethers pol delta to the DNA.

Evidence938
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9191022
xref: http://identifiers.org/pubmed/1671046
xref: http://identifiers.org/pubmed/7378348
xref: http://identifiers.org/pubmed/10751307
comment: Polymerase switching is a key event that allows the processive synthesis of DNA by the pol delta and PCNA complex. Polymerase delta possesses polymerization and proofreading activities, which increases the overall fidelity of DNA replication. The pol delta holoenzyme is a heterotetrameric complex that contains p125, p66, p50, and p12 subunits, in human cells.

Evidence937
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1671046
xref: http://identifiers.org/pubmed/1967833
xref: http://identifiers.org/pubmed/1670772
comment: After the primers are synthesized, Replication Factor C binds to the 3'-end of the initiator DNA to trigger polymerase switching. The non-processive nature of pol alpha catalytic activity and the tight binding of Replication Factor C to the primer-template junction presumably lead to the turnover of the pol alpha:primase complex. After the Pol alpha-primase primase complex is displaced from the primer, the proliferating cell nuclear antigen (PCNA) binds to form a "sliding clamp" structure. Replication Factor C then dissociates, and DNA polymerase delta binds and catalyzes the processive synthesis of DNA.

http://identifiers.org/pubmed/17656326
type: PublicationXref
id: 17656326
author: Ardehali, H
author: Burke, MA
db: Pubmed
title: Mitochondrial ATP-binding cassette proteins
source: Transl Res 150:73-80
year: 2007

1-methyl-4-phenyl-pyridinium
type: SmallMolecule
entity reference: CHEBI:641
data source: Provenance1
xref: UnificationXref6332
xref: UnificationXref6331
cellular location: GO:0005829
comment: Reactome DB_ID: 446590
display name: MPP

MATE substrates
type: SmallMolecule
data source: Provenance1
member physical entity: Tetramethylammonium
member physical entity: Cimetidine
member physical entity: 1-methyl-4-phenyl-pyridinium
member physical entity: Guanidine
member physical entity: Procainamide
member physical entity: Creatinine
member physical entity: Metformin
xref: UnificationXref6352
xref: UnificationXref6351
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 446589

Evidence930
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10834843
comment: In budding yeast, all MCM proteins have been proved to be essential for elongation. The active form of this protein complex may be a heterohexamer. A subcomplex of MCM proteins consisting fo MCM4,6, and -7 has a weak helicase activity that may contribute to DNA unwinding.

Creatinine
type: SmallMolecule
entity reference: CHEBI:16737
data source: Provenance1
name: 1-Methylglycocyamidine
xref: UnificationXref6337
xref: UnificationXref6338
cellular location: GO:0005829
comment: Reactome DB_ID: 30733
display name: CREAT

Cimetidine
type: SmallMolecule
entity reference: CHEBI:3699
data source: Provenance1
xref: UnificationXref6334
xref: UnificationXref6335
cellular location: GO:0005829
comment: Reactome DB_ID: 446602
display name: CIM

PublicationXref545
type: PublicationXref
id: 0079130356
author: Mantei, N
author: Auricchio, S
author: Semenza, G
db: ISBN
title: Small-intestinal disaccharidases
source: The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1623-1650
year: 2001

L-Glutaminic acid
type: SmallMolecule
entity reference: CHEBI:16015
data source: Provenance1
name: L-Glutamic acid
name: L-Glutamate
xref: UnificationXref6280
xref: UnificationXref6281
cellular location: GO:0043202
comment: Reactome DB_ID: 428017
display name: L-Glu

L-Glutamine
type: SmallMolecule
entity reference: L-Glutamine
data source: Provenance1
name: L-2-Aminoglutaramic acid
xref: UnificationXref6283
xref: UnificationXref6282
cellular location: GO:0043202
comment: Reactome DB_ID: 428006
display name: L-Gln

L-Asparagine
type: SmallMolecule
entity reference: CHEBI:17196
data source: Provenance1
name: 2-Aminosuccinamic acid
xref: UnificationXref6276
xref: UnificationXref6277
cellular location: GO:0043202
comment: Reactome DB_ID: 428042
display name: L-Asn

2-aminosuccinic acid
type: SmallMolecule
entity reference: CHEBI:17053
data source: Provenance1
name: L-Aspartate
name: L-Aspartic acid
xref: UnificationXref6278
xref: UnificationXref6279
cellular location: GO:0043202
comment: Reactome DB_ID: 427963
display name: L-Asp

2,6-diaminohexanoic acid
type: SmallMolecule
entity reference: 2,6-diaminohexanoic acid
data source: Provenance1
name: Lysine acid
name: L-Lysine
xref: UnificationXref6288
xref: UnificationXref6289
cellular location: GO:0043202
comment: Reactome DB_ID: 428004
display name: L-Lys

L-Methionine
type: SmallMolecule
entity reference: CHEBI:16643
data source: Provenance1
xref: UnificationXref6291
xref: UnificationXref6290
cellular location: GO:0043202
comment: Reactome DB_ID: 428001
display name: L-Met

L-Isoleucine
type: SmallMolecule
entity reference: CHEBI:17191
data source: Provenance1
name: 2-Amino-3-methylvaleric acid
xref: UnificationXref6284
xref: UnificationXref6285
cellular location: GO:0043202
comment: Reactome DB_ID: 427955
display name: L-Ile

L-Leucine
type: SmallMolecule
entity reference: CHEBI:15603
data source: Provenance1
name: (2S)-alpha-2-Amino-4-methylvaleric acid
name: (2S)-alpha-Leucine
name: 2-amino-4-methylvaleric acid
xref: UnificationXref6286
xref: UnificationXref6287
cellular location: GO:0043202
comment: Reactome DB_ID: 427983
display name: L-Leu

Evidence928
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11454864
xref: http://identifiers.org/pubmed/10834843
xref: http://identifiers.org/pubmed/10611290
xref: http://identifiers.org/pubmed/10677495
xref: http://identifiers.org/pubmed/12364596
xref: http://identifiers.org/pubmed/10872463
xref: http://identifiers.org/pubmed/11282021
xref: http://identifiers.org/pubmed/10567526
xref: http://identifiers.org/pubmed/10748114
xref: http://identifiers.org/pubmed/9335335
xref: http://identifiers.org/pubmed/9305914
xref: http://identifiers.org/pubmed/10884341
comment: At the start of the elongation phase of DNA replication, the Mcm2-7 complex may re-arrange to function as the replicative helicase associated with the replication fork. In general, a replicative helicase is associated with the replication fork and unwinds DNA ahead of the polymerase. In yeast, the Mcm proteins associate with origin DNA in G1 phase and then exit the origin upon replication initiation, consistent with moving out of the origin with the replication fork. The Mcm2-7 complex is a ring-shaped hexamer. Complexes of Mcm4, Mcm6 and Mcm7 proteins from humans or S. pombe display a modest ATP-dependent helicase activity in vitro. Consistent with the hypothesis that eukaryotic Mcm complexes function as helicases, an archaeal Mcm homolog is a ring-shaped double hexamer that has a processive DNA unwinding activity. Mcm proteins may have additional functions during elongation, as uninterrupted function of all six is required for replication fork progression in budding yeast. Mcm4,6,7 helicase activity may be negatively regulated in two ways. Mcm2, Mcm4, Mcm6, and Mcm7 also form a stable complex which, however, has no helicase activity, suggesting that Mcm2 inhibits DNA unwinding by Mcm4,6,7. In addition, phosphorylation of human Mcm4,6,7 complex by CDK inhibits its helicase activity.

Evidence922
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11931757
comment: At the beginning of this reaction, 1 molecule of 'ubiquitinated Orc1' is present. At the end of this reaction, 1 molecule of 'ubiquitin' is present. This reaction takes place in the 'cytosol' and is mediated by the 'endopeptidase activity' of '26S proteasome'.

Evidence921
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11931757
comment: In this reaction, 1 molecule of 'ubiquitinated Orc1' is translocated from nucleoplasm to cytosol. This movement of the molecule occurs through the 'nuclear pore'.

Evidence920
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11931757
comment: At the beginning of this reaction, 1 molecule of 'ubiquitin', and 1 molecule of 'phosphorylated Orc1' are present. At the end of this reaction, 1 molecule of 'ubiquitinated Orc1' is present. This reaction takes place in the 'nucleus'.

Evidence927
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12045100
xref: http://identifiers.org/pubmed/11046155
comment: As cells enter S phase, HsCdc6p is phosphorylated by CDK promoting its export from the nucleus (see Bell and Dutta 2002).

Evidence926
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11046155
comment: At the beginning of this reaction, 1 molecule of 'ubiquitinated Cdc6' is present. At the end of this reaction, 1 molecule of 'ubiquitin' is present. This reaction takes place in the 'cytosol' and is mediated by the 'endopeptidase activity' of '26S proteasome'.

Evidence925
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10339564
comment: In this reaction, 1 molecule of 'phosphorylated Cdc6' is translocated from nucleoplasm to cytosol. This movement of the molecule occurs through the 'nuclear pore'.

Evidence924
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10339564
comment: At the beginning of this reaction, 1 molecule of 'CDC6', and 1 molecule of 'ATP' are present. At the end of this reaction, 1 molecule of 'ADP', and 1 molecule of 'phosphorylated Cdc6' are present. This reaction takes place in the 'nucleus' and is mediated by the 'kinase activity' of 'CDK'.

http://identifiers.org/pubmed/11719186
type: PublicationXref
id: 11719186
author: Gherzi, R
author: Chan, EL
author: Pruijn, GJ
author: Stoecklin, G
author: Moroni, C
author: Karin, M
author: Mann, M
author: Raijmakers, R
author: Ong, SE
author: Chen, CY
db: Pubmed
title: AU binding proteins recruit the exosome to degrade ARE-containing mRNAs
source: Cell 107:451-64
year: 2001

L-Threonine
type: SmallMolecule
entity reference: CHEBI:16857
data source: Provenance1
xref: UnificationXref6297
xref: UnificationXref6296
cellular location: GO:0043202
comment: Reactome DB_ID: 427964
display name: L-Thr

2-Pyrrolidinecarboxylic acid
type: SmallMolecule
entity reference: CHEBI:17203
data source: Provenance1
name: L-Proline
xref: UnificationXref6294
xref: UnificationXref6295
cellular location: GO:0043202
comment: Reactome DB_ID: 427962
display name: L-Pro

L-Phenylalanine
type: SmallMolecule
entity reference: CHEBI:17295
data source: Provenance1
name: (S)-alpha-amino-beta-phenylpropionic acid
xref: UnificationXref6293
xref: UnificationXref6292
cellular location: GO:0043202
comment: Reactome DB_ID: 427949
display name: L-Phe

Copper
type: SmallMolecule
entity reference: CHEBI:29036
data source: Provenance1
xref: UnificationXref6407
xref: UnificationXref6408
cellular location: GO:0005576
comment: Reactome DB_ID: 437295
display name: Cu2+

Tetramethylammonium
type: SmallMolecule
entity reference: CHEBI:46020
data source: Provenance1
xref: UnificationXref6366
xref: UnificationXref6365
cellular location: GO:0005576
comment: Reactome DB_ID: 446604
display name: TMAM

http://identifiers.org/pubmed/15068804
type: PublicationXref
id: 15068804
author: Lima, CD
author: Kiledjian, M
author: Fabrega, C
author: Liu, SW
author: Gu, M
author: Liu, H
db: Pubmed
title: Insights into the structure, mechanism, and regulation of scavenger mRNA decapping activity
source: Mol Cell 14:67-80
year: 2004

Zn(II)
type: SmallMolecule
entity reference: CHEBI:29105
data source: Provenance1
name: Zn++
name: Zinc ion
xref: UnificationXref6384
xref: UnificationXref6383
cellular location: GO:0005576
comment: Reactome DB_ID: 158417
display name: Zn2+

Zinc 2+
type: SmallMolecule
entity reference: CHEBI:29105
data source: Provenance1
xref: UnificationXref6390
xref: UnificationXref6391
cellular location: GO:0034774
comment: Reactome DB_ID: 216785
display name: Zn2+

Zinc 2+
type: SmallMolecule
entity reference: CHEBI:29105
data source: Provenance1
xref: UnificationXref6397
xref: UnificationXref6398
cellular location: GO:0005796
comment: Reactome DB_ID: 216667
display name: Zn2+

Evidence917
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/6693436
comment: At the beginning of this reaction, 1 molecule of 'DNA polymerase alpha:primase:DNA polymerase alpha:origin complex', and 1 molecule of 'NTP' are present. At the end of this reaction, 1 molecule of 'DNA polymerase epsilon', and 1 molecule of 'RNA primer:origin duplex:DNA polymerase alpha:primase complex' are present. This reaction takes place in the 'nucleus' and is mediated by the 'DNA-directed RNA polymerase activity' of 'DNA polymerase alpha:primase'.

Evidence918
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: At the beginning of this reaction, 1 molecule of 'dTTP', 1 molecule of 'dGTP', 1 molecule of 'dATP', 1 molecule of 'RNA primer:origin duplex:DNA polymerase alpha:primase complex', and 1 molecule of 'dCTP' are present. At the end of this reaction, 1 molecule of 'RNA primer-DNA primer:origin duplex' is present. This reaction takes place in the 'nucleus' and is mediated by the 'DNA-directed DNA polymerase activity' of 'DNA polymerase alpha:primase'.

Evidence919
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11395402
xref: http://identifiers.org/pubmed/6693436
comment: DNA polymerases are not capable of de novo DNA synthesis and require synthesis of a primer, usually by a DNA-dependent RNA polymerase (primase) to begin DNA synthesis. In eukaryotic cells, the primer is synthesized by DNA polymerase alpha:primase. First, the DNA primase portion of this complex synthesizes approximately 6-10 nucleotides of RNA primer and then the DNA polymerase portion synthesizes an additional 20 nucleotides of DNA (Frick & Richardson 2002; Wang et al 1984).

Evidence914
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10402192
xref: http://identifiers.org/pubmed/9829972
xref: http://identifiers.org/pubmed/10970868
xref: http://identifiers.org/pubmed/10801458
xref: http://identifiers.org/pubmed/11395502
xref: http://identifiers.org/pubmed/9038340
xref: http://identifiers.org/pubmed/7502077
xref: http://identifiers.org/pubmed/9765232
xref: http://identifiers.org/pubmed/11459976
xref: http://identifiers.org/pubmed/12169736
xref: http://identifiers.org/pubmed/9353276
xref: http://identifiers.org/pubmed/11779870
xref: http://identifiers.org/pubmed/11323433
comment: In S. cerevisiae, two ORC subunits, Orc1 and Orc5, both bind ATP, and Orc1 in addition has ATPase activity. Both ATP binding and ATP hydrolysis appear to be essential functions in vivo. ATP binding by Orc1 is unaffected by the association of ORC with origin DNA (ARS) sequences, but ATP hydrolysis is ARS-dependent, being suppressed by associated double-stranded DNA and stimulated by associated single-stranded DNA. These data are consistent with the hypothesis that ORC functions as an ATPase switch, hydrolyzing bound ATP and changing state as DNA unwinds at the origin immediately before replication. It is attractive to speculate that ORC likewise functions as a switch as human pre-replicative complexes are activated, but human Orc proteins are not well enough characterized to allow the model to be critically tested. mRNAs encoding human orthologs of all six Orc proteins have been cloned, and ATP-binding amino acid sequence motifs have been identified in Orc1, Orc4, and Orc5. Interactions among proteins expressed from the cloned genes have been characterized, but the ATP-binding and hydrolyzing properties of these proteins and complexes of them have not been determined.

Evidence913
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12045100
comment: At the beginning of this reaction, 1 molecule of 'origin of replication', and 1 molecule of 'DNA polymerase epsilon' are present. At the end of this reaction, 1 molecule of 'DNA polymerase epsilon:origin complex' is present.

Evidence916
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Finally, progression out of mitosis and division of the cell into two daughters (cytokinesis) requires the inactivation of Cyclin B - Cdc2 by ubiquitin-dependent proteolysis of Cyclin A and B, which is regulated by a large E3 ubiquitin ligase complex known as the Anaphase Promoting Complex (APC). The detailed annotation of the M/G1 transition will be completed in a later version of GK.

Evidence915
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Although, DNA replication occurs in the S phase of the cell cycle, the formation of the DNA replication pre-initiation complex begins during G1 phase.

Evidence910
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9554851
xref: http://identifiers.org/pubmed/9660782
xref: http://identifiers.org/pubmed/7708676
xref: http://identifiers.org/pubmed/10757793
xref: http://identifiers.org/pubmed/11296242
xref: http://identifiers.org/pubmed/10430907
xref: http://identifiers.org/pubmed/12438414
xref: http://identifiers.org/pubmed/10790374
xref: http://identifiers.org/pubmed/10518787
xref: http://identifiers.org/pubmed/9335335
xref: http://identifiers.org/pubmed/11756551
comment: Once the Mcm2-7 complex has been assembled onto the origin of replication, the next step is the assembly of Cdc45, an essential replication protein, in late G1. The assembly of Cdc45 onto origins of replication forms a complex distinct from the pre-replicative complex, sometimes called the pre-initiation complex. The assembly of Cdc45 onto origins correlates with the time of initiation. Like the Mcm2-7 proteins, Cdc45 binds specifically to origins in the G1 phase of the cell cycle and then to non-origin DNA during S phase and is therefore thought to travel with the replication fork. Indeed, S. cerevisiae Cdc45 is required for DNA replication elongation as well as replication initiation. Cdc45 is required for the association of alpha DNA polymerase:primase with chromatin. Based on this observation and the observation that in S. cerevisiae, cCdc45 has been found in large complexes with some components of Mcm2-7 complex, it has been suggested that Cdc45 plays a scaffolding role at the replication fork, coupling Pol-alpha:primase to the replication fork through the helicase. Association of Cdc45 with origin DNA is regulated in the cell cycle and its association is dependent on the activity of cyclin-dependent kinases but not the Cdc7/Dbf4 kinase. In Xenopus egg extracts, association of Cdc45 with chromatin is dependent on Xmus101. TopBP1, the human homolog of Xmus1, is essential for DNA replication and interacts with DNA polymerase epsilon, one of the polymerases involved in replicating the genome. TopBP1 homologs have been found in S. cerevisiae and S. pombe. Sld3, an additional protein required for Cdc45 association with chromatin in S. cerevisiae and S. pombe, has no known human homolog.

Evidence912
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12045100
xref: http://identifiers.org/pubmed/8253737
xref: http://identifiers.org/pubmed/10757793
xref: http://identifiers.org/pubmed/10882098
xref: http://identifiers.org/pubmed/11395402
comment: DNA polymerase alpha:primase is comprised of four subunits, p180, p70, p58, and p49. The two primase subunits, p58 and p49, form a tight complex. The p49 subunit contains the DNA primase activity and one role of p58 appears to be tethering p49 to p180, the DNA polymerase catalytic subunit. The fourth subunit, p70, binds p180 and may tether the DNA polymerase alpha:primase complex to Cdc45.

Evidence911
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10473346
xref: http://identifiers.org/pubmed/1311258
xref: http://identifiers.org/pubmed/10757793
xref: http://identifiers.org/pubmed/9242902
xref: http://identifiers.org/pubmed/2200738
xref: http://identifiers.org/pubmed/10882098
comment: After pre-RC assembly and Cdc45 association with the origin of replication, Replication Protein A (RPA) also associates with chromatin. RPA is a heterotrimeric complex containing p70, p34, and p11 subunits, and also is required for DNA recombination and DNA repair. The p70 subunit of RPA binds to the primase subunits of Pol alpha:primase. The p70 and p34 subunits of RPA are phosphorylated in a cell cycle-dependent manner. RPA is a single-strand DNA (ssDNA) binding protein and its association with chromatin at this stage suggests that DNA is partially unwound. This suggestion has been confirmed by detection of ssDNA in budding yeast origins of replication using chemical methods.

CMP-sialic acid
type: SmallMolecule
entity reference: CHEBI:16556
data source: Provenance1
xref: UnificationXref6429
xref: UnificationXref6428
cellular location: GO:0005829
comment: Reactome DB_ID: 727803
display name: CMP-SA

Cytidine-5'-monophosphate
type: SmallMolecule
entity reference: CHEBI:17361
data source: Provenance1
name: cytidine 5'-monophosphate
name: cytidylic acid
xref: UnificationXref6426
xref: UnificationXref6425
cellular location: GO:0005796
comment: Reactome DB_ID: 727810
display name: CMP

UDP-xylose
type: SmallMolecule
entity reference: CHEBI:16082
data source: Provenance1
xref: UnificationXref6437
xref: UnificationXref6438
cellular location: GO:0005829
comment: Reactome DB_ID: 742353
display name: UDP-Xyl

CMP-sialic acid
type: SmallMolecule
entity reference: CHEBI:16556
data source: Provenance1
xref: UnificationXref6430
xref: UnificationXref6431
cellular location: GO:0005796
comment: Reactome DB_ID: 727815
display name: CMP-SA

Acetyl coenzyme A
type: SmallMolecule
entity reference: CHEBI:15351
data source: Provenance1
name: Acetyl-CoA
xref: UnificationXref6420
xref: UnificationXref6419
cellular location: GO:0005796
comment: Reactome DB_ID: 727753
display name: Ac-CoA

Copper
type: SmallMolecule
entity reference: CHEBI:29036
data source: Provenance1
xref: UnificationXref6410
xref: UnificationXref6409
cellular location: GO:0005829
comment: Reactome DB_ID: 209799
display name: Cu2+

MATE substrates
type: SmallMolecule
data source: Provenance1
member physical entity: Cimetidine
member physical entity: 1-methyl-4-phenyl-pyridinium
member physical entity: Procainamide
member physical entity: Tetramethylammonium
member physical entity: Creatinine
member physical entity: Metformin
member physical entity: Guanidine
xref: UnificationXref6367
xref: UnificationXref6368
cellular location: GO:0005576
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 446597

1-methyl-4-phenyl-pyridinium
type: SmallMolecule
entity reference: CHEBI:641
data source: Provenance1
xref: UnificationXref6354
xref: UnificationXref6353
cellular location: GO:0005576
comment: Reactome DB_ID: 446607
display name: MPP

Procainamide
type: SmallMolecule
entity reference: Procainamide [ChEBI:8428]
data source: Provenance1
xref: UnificationXref6346
xref: UnificationXref6347
cellular location: GO:0005829
comment: Reactome DB_ID: 446598

Tetramethylammonium
type: SmallMolecule
entity reference: CHEBI:46020
data source: Provenance1
xref: UnificationXref6350
xref: UnificationXref6349
cellular location: GO:0005829
comment: Reactome DB_ID: 446599
display name: TMAM

Guanidine
type: SmallMolecule
entity reference: CHEBI:42820
data source: Provenance1
xref: UnificationXref6340
xref: UnificationXref6341
cellular location: GO:0005829
comment: Reactome DB_ID: 446594
display name: Gu

Metformin
type: SmallMolecule
entity reference: CHEBI:6801
data source: Provenance1
xref: UnificationXref6344
xref: UnificationXref6343
cellular location: GO:0005829
comment: Reactome DB_ID: 446606
display name: MTF

Evidence908
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9927482
xref: http://identifiers.org/pubmed/9288745
xref: http://identifiers.org/pubmed/9829972
xref: http://identifiers.org/pubmed/9407030
xref: http://identifiers.org/pubmed/11801723
xref: http://identifiers.org/pubmed/11046155
xref: http://identifiers.org/pubmed/9335335
comment: DNA replication pre-initiation in eukaryotic cells begins with the formation of the pre-replicative complex (pre-RC) during the late M phase and continues in the G1 phase of the mitotic cell cycle, a process also called DNA replication origin licensing. The association of initiation proteins (ORC, Cdc6, Cdt1, Mcm2-7) with the origin of replication in both S. cerevisiae and humans has been demonstrated by chromatin immunoprecipitation experiments. In S. cerevisiae, pre-replicative complexes are assembled from late M to G1. In mammalian cells as well, pre-replicative complexes are assembled from late M to G1, as shown by biochemical fractionation and immunostaining. There are significant sequence similarities among some of the proteins in the pre-replicative complex. The ORC subunits Orc1, Orc4 and Orc5 are homologous to one another and to Cdc6. The six subunits of the Mcm2-7 complex are homologous to one another. In addition, Orc1, Orc4, Orc5, Cdc6, and the Mcm2-7 subunits, are members of the AAA+ superfamily of ATPases. Since the initial identification of these pre-RC components other factors that participate in this complex have been found, including Cdt1 in human, Xenopus, S. pombe, and S. cerevisiae cells.

Evidence909
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/14766746
xref: http://identifiers.org/pubmed/11864598
xref: http://identifiers.org/pubmed/10783164
xref: http://identifiers.org/pubmed/12604790
xref: http://identifiers.org/pubmed/11282021
xref: http://identifiers.org/pubmed/11095689
xref: http://identifiers.org/pubmed/9154825
xref: http://identifiers.org/pubmed/9745018
xref: http://identifiers.org/pubmed/15494305
xref: http://identifiers.org/pubmed/15201046
comment: MCM10 is required for human DNA replication. In S. cerevisiae, Mcm10, like Mcm2-7, is required for minichromosome maintenance, but Mcm10 has no sequence homology with these other proteins (Merchant et al., 1997). Genetic studies have demonstrated that Mcm10 is required for DNA replication in S. pombe (Aves et al., 1998) and S. cerevisiae cells (Homesley et al., 2000) and immunodepletion of XlMcm10 interferes with DNA replication in Xenopus egg extracts (Wohlschlegel et al., 2002). Human Mcm10 interacts with chromatin in G1 phase and then dissociates during G2 phase. In S. cerevisiae, Mcm10 has been shown to localize to origins during G1 (Ricke and Bielinsky, 2004), and it may stabilize the association of Mcm2-7 with the pre-replicative complex (Sawyer et al., 2004). This timing of association is consistent with studies that demonstrate that, in Xenopus egg extracts, Mcm10 is required for association of Cdc45, but not Mcm2-7 with chromatin. Biochemical evidence that Mcm10 plays a direct role in the activation of the pre-replicative complex includes the requirement for SpMcm10 in the phosphorylation of the Mcm2-7 complex by DDK (Lee et al., 2004) and the fact that SpMcm10 binds and stimulates DNA polymerase alpha activity (Fien et al., 2004).

Evidence906
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9778043
xref: http://identifiers.org/pubmed/9520412
comment: At the end of this reaction, 1 molecule of 'Cdc6' is present.

Evidence907
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11532947
xref: http://identifiers.org/pubmed/7641697
xref: http://identifiers.org/pubmed/9566895
xref: http://identifiers.org/pubmed/9312054
xref: http://identifiers.org/pubmed/10995389
xref: http://identifiers.org/pubmed/10712901
xref: http://identifiers.org/pubmed/10339564
xref: http://identifiers.org/pubmed/9520412
xref: http://identifiers.org/pubmed/11046155
xref: http://identifiers.org/pubmed/10801458
xref: http://identifiers.org/pubmed/9889196
comment: Cdc6 is a regulator of DNA replication initiation in both yeasts and human cells, but its mechanism of action differs between the two systems. Genetic studies in budding yeast (S. cerevisiae) and fission yeast (S. pombe) indicate that the normal function of Cdc6 protein is required to restrict DNA replication to once per cell cycle. Specifically, Cdc6 may function as an ATPase switch linked to Mcm2-7 association with the Cdt1:Cdc6:ORC:origin complex. In S. cerevisiae, Cdc6 protein is expressed late in the M phase of the cell cycle and, in cells with a prolonged G1 phase, late in G1. This protein has a short half-life, and is destroyed by ubiquitin-mediated proteolysis, mediated by the SCF complex. Human Cdc6 protein levels are reduced early in G1 but otherwise are constant throughout the cell cycle. Some reports have suggested that after cells enter S phase, Cdc6 is phosphorylated, excluded from the nucleus and subject to ubiquitination and degradation. Replenishing Cdc6 protein levels during G1 appears to be regulated by E2F transcription factors.

http://identifiers.org/pubmed/11470505
type: PublicationXref
id: 11470505
author: Langin, D
author: Reue, K
author: Xia, YR
author: Holm, C
author: Karlsson, M
author: Tornqvist, H
author: Lusis, AJ
db: Pubmed
title: Exon-intron organization and chromosomal localization of the mouse monoglyceride lipase gene
source: Gene 272:11-8
year: 2001

Evidence905
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11395502
xref: http://identifiers.org/pubmed/11739726
xref: http://identifiers.org/pubmed/9372948
xref: http://identifiers.org/pubmed/8044842
xref: http://identifiers.org/pubmed/1579162
xref: http://identifiers.org/pubmed/11278932
xref: http://identifiers.org/pubmed/1110244
xref: http://identifiers.org/pubmed/10438470
xref: http://identifiers.org/pubmed/11323433
comment: In Saccharomyces cerevisiae, the entire ORC complex is constitutively bound to the origin of replication. However, in mammalian cells, Orc1, and possibly other Orc subunits, dissociate from origins of replication, while Orc2 remains stably associated with chromatin across the cell cycle. The first step in formation of the pre-RC is assembly of the hexameric Origin Recognition Complex (ORC) at the origin of replication. Recent work on human (Hs) ORC has suggested that the heterohexamer assembles in an ordered manner. HsOrc2 appears to be constitutively bound to origins of replication. HsOrc2 and HsOrc3 form a complex that interacts with HsOrc4 and HsOrc5. Recruitment of HsOrc5 into the complex is important for the association of HsOrc1. HsOrc6 is also capable of interacting with the core HsOrc2:3:4:5 complex, but not smaller complexes. Interestingly, HsOrc1 and a subunit of the Mcm2-7 complex (HsMcm2) interact with a histone acetyltransferase, HsHBO1 (Bell & Stillman 1992; Diffley et al. 1994; Lee & Bell 1997; Wenger et al. 1975; Li & DePamphili;s 2001; Dhar et al. 2001; Vashee et al, 2001; Iizuka & Stillman 1999 Burke et al. 2001).

http://identifiers.org/pubmed/9207791
type: PublicationXref
id: 9207791
author: Bergsagel, PL
author: Nardini, E
author: Ried, T
author: Schröck, E
author: Brents, LA
author: Kuehl, WM
author: Chesi, M
db: Pubmed
title: Frequent translocation t(4;14)(p16.3;q32.3) in multiple myeloma is associated with increased expression and activating mutations of fibroblast growth factor receptor 3
source: Nat Genet 16:260-4
year: 1997

Evidence904
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11395502
xref: http://identifiers.org/pubmed/11739726
xref: http://identifiers.org/pubmed/11046155
xref: http://identifiers.org/pubmed/11323433
comment: At the beginning of this reaction, 1 molecule of 'Orc4:Orc5:Orc3:Orc2:origin', and 1 molecule of 'Orc1' are present. At the end of this reaction, 1 molecule of 'Orc1:Orc4:Orc5:Orc3:Orc2:origin' is present. This reaction takes place in the 'nucleus'.

Evidence903
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11395502
xref: http://identifiers.org/pubmed/11323433
comment: At the beginning of this reaction, 1 molecule of 'Orc4', and 1 molecule of 'Orc5:Orc3:Orc2:origin' are present. At the end of this reaction, 1 molecule of 'Orc4:Orc5:Orc3:Orc2:origin' is present. This reaction takes place in the 'nucleus'.

Evidence902
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11395502
xref: http://identifiers.org/pubmed/9765232
xref: http://identifiers.org/pubmed/11323433
comment: At the beginning of this reaction, 1 molecule of 'Orc3:Orc2:origin', and 1 molecule of 'Orc5' are present. At the end of this reaction, 1 molecule of 'Orc5:Orc3:Orc2:origin' is present. This reaction takes place in the 'nucleus'.

Evidence901
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11395502
xref: http://identifiers.org/pubmed/11046155
xref: http://identifiers.org/pubmed/11323433
xref: http://identifiers.org/pubmed/9733749
comment: At the beginning of this reaction, 1 molecule of 'Orc2:origin', and 1 molecule of 'Orc3' are present. At the end of this reaction, 1 molecule of 'Orc3:Orc2:origin' is present. This reaction takes place in the 'nucleus'.

Evidence900
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref1428
comment: The human brain contains at least 100 billion neurons, each with the ability to influence many other cells. Clearly, highly sophisticated and efficient mechanisms are needed to enable communication among this astronomical number of elements. This communication occurs across synapses, the functional connection between neurons. Synapses can be divided into two general classes: electrical synapses and chemical synapses. Electrical synapses permit direct, passive flow of electrical current from one neuron to another. The current flows through gap junctions, specialized membrane channels that connect the two cells. Chemical synapses enable cell-to-cell communication using neurotransmitter release. Neurotransmitters are chemical agents released by presynaptic neurons that trigger a secondary current flow in postsynaptic neurons by activating specific receptor molecules. Neurotransmitter secretion is triggered by the influx of Ca2+ through voltage-gated channels, which gives rise to a transient increase in Ca2+ concentration within the presynaptic terminal. The rise in Ca2+ concentration causes synaptic vesicles (the presynaptic organelles that store neurotransmitters) to fuse with the presynaptic plasma membrane and release their contents into the space between the pre- and postsynaptic cells.

Procainamide
type: SmallMolecule
entity reference: Procainamide [ChEBI:8428]
data source: Provenance1
xref: UnificationXref6364
xref: UnificationXref6363
cellular location: GO:0005576
comment: Reactome DB_ID: 446596

Metformin
type: SmallMolecule
entity reference: CHEBI:6801
data source: Provenance1
xref: UnificationXref6362
xref: UnificationXref6361
cellular location: GO:0005576
comment: Reactome DB_ID: 446603
display name: MTF

Guanidine
type: SmallMolecule
entity reference: CHEBI:42820
data source: Provenance1
xref: UnificationXref6359
xref: UnificationXref6360
cellular location: GO:0005576
comment: Reactome DB_ID: 446595
display name: Gu

Creatinine
type: SmallMolecule
entity reference: CHEBI:16737
data source: Provenance1
name: 1-Methylglycocyamidine
xref: UnificationXref6357
xref: UnificationXref6358
cellular location: GO:0005576
comment: Reactome DB_ID: 446592
display name: CREAT

http://identifiers.org/pubmed/12807903
type: PublicationXref
id: 12807903
author: Nagai, M
author: Sudol, M
author: Navin, NE
author: Komuro, A
db: Pubmed
title: WW domain-containing protein YAP associates with ErbB-4 and acts as a co-transcriptional activator for the carboxyl-terminal fragment of ErbB-4 that translocates to the nucleus
source: J Biol Chem 278:33334-41
year: 2003

UnificationXref6199
type: UnificationXref
id: P87122
db: UniProt

Cimetidine
type: SmallMolecule
entity reference: CHEBI:3699
data source: Provenance1
xref: UnificationXref6355
xref: UnificationXref6356
cellular location: GO:0005576
comment: Reactome DB_ID: 446609
display name: CIM

UnificationXref6198
type: UnificationXref
id: REACT_20181
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20181.1

UnificationXref6197
type: UnificationXref
id: 425810
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=425810

UnificationXref6196
type: UnificationXref
id: REACT_5668
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5668.2

phosphatidylethanolamine
type: SmallMolecule
entity reference: SmallMoleculeReference160
data source: Provenance1
xref: UnificationXref6532
xref: UnificationXref6531
cellular location: GO:0009898
comment: Reactome DB_ID: 939760
display name: PE

aminophospholipids
type: SmallMolecule
data source: Provenance1
member physical entity: phosphatidylserine
member physical entity: phosphatidylethanolamine
xref: UnificationXref6536
xref: UnificationXref6535
cellular location: GO:0009898
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 947588
display name: APLs

phosphatidylserine
type: SmallMolecule
entity reference: ChEBI:18303 phosphatidyl-L-serine
data source: Provenance1
xref: UnificationXref6534
xref: UnificationXref6533
cellular location: GO:0009898
comment: Reactome DB_ID: 947592
display name: PS

PIP3, PI(3,4)P2
type: SmallMolecule
data source: Provenance1
member physical entity: 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphates
member physical entity: SmallMolecule19
xref: UnificationXref6563
xref: UnificationXref6564
cellular location: GO:0005886
comment: Reactome DB_ID: 202277
comment: Converted from EntitySet in Reactome

1-phosphatidyl-1D-myo-inositol 3,4-bisphosphates
type: SmallMolecule
entity reference: ChEBI:16152 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphates
data source: Provenance1
xref: UnificationXref6561
xref: UnificationXref6562
cellular location: GO:0005886
comment: Reactome DB_ID: 202247
display name: PI(3,4)P2

AGE adducts
type: SmallMolecule
data source: Provenance1
member physical entity: N(6)-carboxymethyl-lysine
member physical entity: N-epsilon-(1-(1-carboxy)ethyl)lysine
xref: UnificationXref6734
xref: UnificationXref6733
cellular location: GO:0005576
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 879487

N(6)-carboxymethyl-lysine
type: SmallMolecule
entity reference: ChEBI:53014 N(6)-carboxymethyl-L-lysine
data source: Provenance1
xref: UnificationXref6729
xref: UnificationXref6728
cellular location: GO:0005576
comment: Reactome DB_ID: 879473
display name: NECML

N-epsilon-(1-(1-carboxy)ethyl)lysine
type: SmallMolecule
entity reference: CHEBI:60125
data source: Provenance1
xref: UnificationXref6731
xref: UnificationXref6732
cellular location: GO:0005576
comment: Reactome DB_ID: 938699

Peptide
type: SmallMolecule
entity reference: CHEBI:16670
data source: Provenance1
xref: UnificationXref6737
xref: UnificationXref6736
cellular location: GO:0005576
comment: Reactome DB_ID: 879484

Phosphatidyl choline
type: SmallMolecule
entity reference: Phosphatidyl-N-trimethylethanolamine
data source: Provenance1
xref: UnificationXref6803
xref: UnificationXref6802
cellular location: GO:0005886
comment: Reactome DB_ID: 429802
display name: PC

Phosphatidic acid
type: SmallMolecule
entity reference: CHEBI:16337
data source: Provenance1
xref: UnificationXref6805
xref: UnificationXref6804
cellular location: GO:0005886
comment: Reactome DB_ID: 1602448
display name: PA

http://identifiers.org/pubmed/17698633
type: PublicationXref
id: 17698633
author: Chase, A
author: Grand, FH
author: Cross, NC
db: Pubmed
title: Activity of TKI258 against primary cells and cell lines with FGFR1 fusion genes associated with the 8p11 myeloproliferative syndrome
source: Blood 110:3729-34
year: 2007

GDP-L-fucose
type: SmallMolecule
entity reference: CHEBI:17009
data source: Provenance1
xref: UnificationXref6454
xref: UnificationXref6453
cellular location: GO:0005829
comment: Reactome DB_ID: 742368
display name: GDP-Fuc

UDP-N-acetylglucosamine
type: SmallMolecule
entity reference: UDP-N-acetyl-D-glucosamine
data source: Provenance1
name: UDP-N-acetyl-D-glucosamine
xref: UnificationXref6448
xref: UnificationXref6449
cellular location: GO:0005796
comment: Reactome DB_ID: 914003
display name: UDP-GlcNAc

UDP-GlcNAc
type: SmallMolecule
entity reference: UDP-N-acetyl-D-glucosamine
data source: Provenance1
xref: UnificationXref6447
xref: UnificationXref6446
cellular location: GO:0005829
comment: Reactome DB_ID: 741437

UDP-xylose
type: SmallMolecule
entity reference: CHEBI:16082
data source: Provenance1
xref: UnificationXref6440
xref: UnificationXref6439
cellular location: GO:0005796
comment: Reactome DB_ID: 742361
display name: UDP-xyl

glycerol
type: SmallMolecule
entity reference: CHEBI:17754
data source: Provenance1
xref: UnificationXref6481
xref: UnificationXref6482
cellular location: GO:0005576
comment: Reactome DB_ID: 192438
display name: Glycerol

Urea
type: SmallMolecule
entity reference: Urea [ChEBI:16199]
data source: Provenance1
xref: UnificationXref6487
xref: UnificationXref6488
cellular location: GO:0005576
comment: Reactome DB_ID: 432019

GDP-L-fucose
type: SmallMolecule
entity reference: CHEBI:17009
data source: Provenance1
xref: UnificationXref6455
xref: UnificationXref6456
cellular location: GO:0005796
comment: Reactome DB_ID: 205683
display name: GDP-Fuc

phosphatidylethanolamine
type: SmallMolecule
entity reference: SmallMoleculeReference160
data source: Provenance1
xref: UnificationXref6525
xref: UnificationXref6524
cellular location: GO:0009897
comment: Reactome DB_ID: 947595
display name: PE

phosphatidylserine
type: SmallMolecule
entity reference: ChEBI:18303 phosphatidyl-L-serine
data source: Provenance1
xref: UnificationXref6526
xref: UnificationXref6527
cellular location: GO:0009897
comment: Reactome DB_ID: 939747
display name: PS

Calcium
type: SmallMolecule
entity reference: CHEBI:29108
data source: Provenance1
xref: UnificationXref6515
xref: UnificationXref6514
cellular location: GO:0005796
comment: Reactome DB_ID: 167012
display name: Ca2+

aminophospholipids
type: SmallMolecule
data source: Provenance1
member physical entity: phosphatidylethanolamine
member physical entity: phosphatidylserine
xref: UnificationXref6528
xref: UnificationXref6529
cellular location: GO:0009897
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 947594
display name: APLs

PublicationXref558
type: PublicationXref
id: 0121227022
author: Noltmann, EA
db: ISBN
title: Aldose-ketose isomerases
source: The Enzymes, 3rd ed (Book): 271-354
year: 1972

PublicationXref569
type: PublicationXref
author: Slein, MW
author: Cori, CF
author: Cori, GT
title: Crystalline D-glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle
source: J Biol Chem 173:605-618
year: 1948

PublicationXref561
type: PublicationXref
id: 0121227022
author: Lardy, HA
author: Bloxham, DP
db: ISBN
title: Phosphofructokinase
source: The Enzymes, 3rd ed (Book): 239-278
year: 1973

H+
type: SmallMolecule
entity reference: CHEBI:15378
data source: Provenance1
xref: UnificationXref6852
xref: UnificationXref6851
cellular location: GO:0097013
comment: Reactome DB_ID: 1470067

http://identifiers.org/pubmed/19501527
type: PublicationXref
id: 19501527
author: Cassel, SL
author: Sutterwala, FS
author: Joly, S
db: Pubmed
title: The NLRP3 inflammasome: a sensor of immune danger signals
source: Semin Immunol 21:194-8
year: 2009

phys-ent-participant97857
type: SmallMolecule
entity reference: CHEBI:15354
data source: Provenance1
name: phys-ent-participant35962
name: phys-ent-participant92341
name: phys-ent-participant36724
name: phys-ent-participant59676
name: phys-ent-participant36150
xref: UnificationXref6807
xref: UnificationXref6808
cellular location: GO:0005829
comment: Reactome DB_ID: 2263486
display name: choline

PublicationXref570
type: PublicationXref
author: Slein, MW
author: Taylor, JF
author: Cori, CF
author: Velick, SF
author: Cori, GT
title: The prosthetic group of crystalline D-glyceraldehyde-3-phosphate dehydrogenase
source: J Biol Chem 173:619-626
year: 1948

5-hydroxyindole acetaldehyde
type: SmallMolecule
entity reference: CHEBI:50157
data source: Provenance1
xref: UnificationXref5869
xref: UnificationXref5870
cellular location: GO:0005759
comment: Reactome DB_ID: 380598
display name: HIALD

http://identifiers.org/pubmed/16100110
type: PublicationXref
id: 16100110
author: Jigami, Y
author: Sato, T
author: Gao, XD
author: Tachikawa, H
author: Dean, N
db: Pubmed
title: Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation
source: J Biol Chem 280:36254-62
year: 2005

http://identifiers.org/pubmed/14567916
type: PublicationXref
id: 14567916
author: DiCorleto, PE
author: Maitra, RK
author: Fox, PL
author: Sampath, P
author: Seshadri, V
author: Mazumder, B
db: Pubmed
title: Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control
source: Cell 115:187-98
year: 2003

http://identifiers.org/pubmed/15692562
type: PublicationXref
id: 15692562
author: Sagata, N
db: Pubmed
title: The Polo-like kinase Plx1 interacts with and inhibits Myt1 after fertilization of Xenopus eggs
source: EMBO J 24:1057-67
year: 2005

http://identifiers.org/pubmed/11136719
type: PublicationXref
id: 11136719
author: Kimura, Keiji
author: Cuvier, Olivier
author: Hirano, T
db: Pubmed
title: Chromosome condensation by a human condensin complex in Xenopus egg extracts
source: J. Biol. Chem. 276:5417-20
year: 2001

Presynaptic phase of homologous DNA pairing and strand exchange
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction31
pathway component: REACT 104366.9
evidence: Evidence56
xref: UnificationXref239
xref: UnificationXref240
pathway order: PathwayStep55
pathway order: PathwayStep52
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/16100120
type: PublicationXref
id: 16100120
author: Lahiri, S
author: Futerman, AH
db: Pubmed
title: LASS5 is a bona fide dihydroceramide synthase that selectively utilizes palmitoyl-CoA as acyl donor
source: J Biol Chem 280:33735-8
year: 2005

Metal ion SLC transporters
type: Pathway
data source: Provenance1
pathway component: REACT 93104.9
pathway component: BiochemicalReaction575
evidence: Evidence976
xref: UnificationXref6416
xref: UnificationXref6415
pathway order: PathwayStep960
pathway order: PathwayStep959
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Evidence987
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18948439
xref: http://identifiers.org/pubmed/8621489
xref: http://identifiers.org/pubmed/15948717
xref: http://identifiers.org/pubmed/7530250
xref: http://identifiers.org/pubmed/18202181
xref: http://identifiers.org/pubmed/20147624
xref: http://identifiers.org/pubmed/9829975
xref: http://identifiers.org/pubmed/18501347
xref: http://identifiers.org/pubmed/19857466
xref: http://identifiers.org/pubmed/1510932
xref: http://identifiers.org/pubmed/19590626
xref: http://identifiers.org/pubmed/18762715
xref: http://identifiers.org/pubmed/3049610
xref: http://identifiers.org/pubmed/14514735
xref: http://identifiers.org/pubmed/21251984
xref: http://identifiers.org/pubmed/11573934
xref: http://identifiers.org/pubmed/11952783
xref: http://identifiers.org/pubmed/18768791
xref: http://identifiers.org/pubmed/9806845
xref: http://identifiers.org/pubmed/11231887
xref: http://identifiers.org/pubmed/19170255
xref: http://identifiers.org/pubmed/19144687
xref: http://identifiers.org/pubmed/10564231
xref: http://identifiers.org/pubmed/17178220
xref: http://identifiers.org/pubmed/12801959
xref: http://identifiers.org/pubmed/12084581
xref: http://identifiers.org/pubmed/9405233
xref: http://identifiers.org/pubmed/16596446
xref: http://identifiers.org/pubmed/8855281
xref: http://identifiers.org/pubmed/7510718
xref: http://identifiers.org/pubmed/18555844
xref: http://identifiers.org/pubmed/11532455
xref: http://identifiers.org/pubmed/15703994
xref: http://identifiers.org/pubmed/17374283
xref: http://identifiers.org/pubmed/7678419
xref: http://identifiers.org/pubmed/16325777
xref: http://identifiers.org/pubmed/11001937
xref: http://identifiers.org/pubmed/8140421
xref: http://identifiers.org/pubmed/11034202
xref: http://identifiers.org/pubmed/18678926
xref: http://identifiers.org/pubmed/19383790
xref: http://identifiers.org/pubmed/17920625
xref: http://identifiers.org/pubmed/18511455
xref: http://identifiers.org/pubmed/7535000
xref: http://identifiers.org/pubmed/14592814
xref: http://identifiers.org/pubmed/9369468
xref: http://identifiers.org/pubmed/1373524
xref: http://identifiers.org/pubmed/11076974
xref: http://identifiers.org/pubmed/11027599
xref: http://identifiers.org/pubmed/14701836
xref: http://identifiers.org/pubmed/10510269
comment: Aquaporin-0 (AQP0, also known as MIP), AQP1, AQP2, AQP3, AQP4, AQP5, AQP7, AQP8, AQP9, and AQP10 are 6-pass transmembrane proteins that passively transport water across the plasma membrane according to the concentration gradient. Each molecule contains a water channel and subunits assemble into homotetramers. In principle water can move in either direction through an aquaporin, however in vivo flow may occur in only one direction. Conductance of water by AQP0 and AQP11 are low relative to other aquaporins.

Evidence986
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18948439
xref: http://identifiers.org/pubmed/8621489
xref: http://identifiers.org/pubmed/15948717
xref: http://identifiers.org/pubmed/7530250
xref: http://identifiers.org/pubmed/18202181
xref: http://identifiers.org/pubmed/20147624
xref: http://identifiers.org/pubmed/9829975
xref: http://identifiers.org/pubmed/18501347
xref: http://identifiers.org/pubmed/19857466
xref: http://identifiers.org/pubmed/1510932
xref: http://identifiers.org/pubmed/19590626
xref: http://identifiers.org/pubmed/18762715
xref: http://identifiers.org/pubmed/3049610
xref: http://identifiers.org/pubmed/14514735
xref: http://identifiers.org/pubmed/21251984
xref: http://identifiers.org/pubmed/11573934
xref: http://identifiers.org/pubmed/11952783
xref: http://identifiers.org/pubmed/18768791
xref: http://identifiers.org/pubmed/9806845
xref: http://identifiers.org/pubmed/11231887
xref: http://identifiers.org/pubmed/19170255
xref: http://identifiers.org/pubmed/19144687
xref: http://identifiers.org/pubmed/10564231
xref: http://identifiers.org/pubmed/17178220
xref: http://identifiers.org/pubmed/12801959
xref: http://identifiers.org/pubmed/12084581
xref: http://identifiers.org/pubmed/9405233
xref: http://identifiers.org/pubmed/16596446
xref: http://identifiers.org/pubmed/16407156
xref: http://identifiers.org/pubmed/8855281
xref: http://identifiers.org/pubmed/7510718
xref: http://identifiers.org/pubmed/18555844
xref: http://identifiers.org/pubmed/11532455
xref: http://identifiers.org/pubmed/15703994
xref: http://identifiers.org/pubmed/17374283
xref: http://identifiers.org/pubmed/7678419
xref: http://identifiers.org/pubmed/16325777
xref: http://identifiers.org/pubmed/11001937
xref: http://identifiers.org/pubmed/8140421
xref: http://identifiers.org/pubmed/11034202
xref: http://identifiers.org/pubmed/19383790
xref: http://identifiers.org/pubmed/18678926
xref: http://identifiers.org/pubmed/17920625
xref: http://identifiers.org/pubmed/18511455
xref: http://identifiers.org/pubmed/7535000
xref: http://identifiers.org/pubmed/14592814
xref: http://identifiers.org/pubmed/9369468
xref: http://identifiers.org/pubmed/19574955
xref: http://identifiers.org/pubmed/1373524
xref: http://identifiers.org/pubmed/11076974
xref: http://identifiers.org/pubmed/11027599
xref: http://identifiers.org/pubmed/14701836
xref: http://identifiers.org/pubmed/10510269
comment: Aquaporin-0 (AQP0, also known as MIP), AQP1, AQP2, AQP3, AQP4, AQP5, AQP7, AQP8, AQP9, and AQP10 are 6-pass transmembrane proteins that passively transport water across the plasma membrane according to the concentration gradient. Each molecule contains a water channel and subunits assemble into homotetramers. In principle water can move in either direction through an aquaporin, however in vivo flow may occur in only one direction. Conductance of water by AQP0 and AQP11 are low relative to other aquaporins.

Evidence989
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12084581
xref: http://identifiers.org/pubmed/11573934
xref: http://identifiers.org/pubmed/11952783
xref: http://identifiers.org/pubmed/9405233
xref: http://identifiers.org/pubmed/16596446
xref: http://identifiers.org/pubmed/18678926
xref: http://identifiers.org/pubmed/10564231
xref: http://identifiers.org/pubmed/18555844
xref: http://identifiers.org/pubmed/9369468
xref: http://identifiers.org/pubmed/19590626
xref: http://identifiers.org/pubmed/18762715
xref: http://identifiers.org/pubmed/11027599
xref: http://identifiers.org/pubmed/16325777
xref: http://identifiers.org/pubmed/10510269
comment: Aquaporin-3 (AQP3), AQP7, AQP9, and AQP10 are 6-pass transmembrane proteins that passively transport glycerol across the plasma membrane through a pore in each subunit of a homotetramer.

Evidence988
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12084581
xref: http://identifiers.org/pubmed/11573934
xref: http://identifiers.org/pubmed/11952783
xref: http://identifiers.org/pubmed/9405233
xref: http://identifiers.org/pubmed/16596446
xref: http://identifiers.org/pubmed/18678926
xref: http://identifiers.org/pubmed/10564231
xref: http://identifiers.org/pubmed/18555844
xref: http://identifiers.org/pubmed/9369468
xref: http://identifiers.org/pubmed/19590626
xref: http://identifiers.org/pubmed/18762715
xref: http://identifiers.org/pubmed/11027599
xref: http://identifiers.org/pubmed/16325777
xref: http://identifiers.org/pubmed/10510269
comment: Aquaporin-3 (AQP3), AQP7, AQP9, and AQP10 are 6-pass transmembrane proteins that passively transport glycerol across the plasma membrane through a pore in each subunit of a homotetramer.

Evidence981
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15911612
comment: The human gene SLC35B4 encodes the bifunctional UDP-xylose and UDP-N-acetylglucosamine transporter YEA4. YEA4 resides on the Golgi membrane and mediates the influx of UDP-N-acetylglucosamine into the lumen (Ashikov A et al, 2005).

Evidence980
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15911612
comment: The human gene SLC35B4 encodes the bifunctional UDP-xylose and UDP-N-acetylglucosamine transporter YEA4. YEA4 resides on the Golgi membrane and mediates the influx of UDP-xylose into the lumen (Ashikov A et al, 2005).

Evidence983
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16981043
xref: http://identifiers.org/pubmed/19164095
xref: http://identifiers.org/pubmed/12759756
comment: Nucleotide sugars are used as sugar donors by glycosyltransferases to create the sugar chains for glycoconjugates such as glycoproteins, polysaccharides and glycolipids. Glycosyltransferases reside mainly in the lumen of the Golgi apparatus and endoplasmic reticulum (ER) whereas nucleotide sugars are synthesized in the cytosol. The human solute carrier family SLC35 encode nucleotide sugar transporters (NSTs) which can mediate the antiport of nucleotide sugars in exchange for the corresponding nucleoside monophosphates (eg. UMP for UDP-sugars). Owing to their function, NSTs are primarily located on Golgi and ER membranes (He L et al, 2009; Handford M et al, 2006; Ishida N and Kawakita M, 2004).

Evidence982
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11326280
comment: The human gene SLC35C1 encodes the GDP-fucose transporter FUCT1. It resides on the Golgi membrane and mediates the transport of UDP-fucose into the Golgi lumen. Defects in SLC35C1 causes the congenital disorder of glycosylation type 2C, also known as leukocyte adhesion deficiency type II (LAD2) (Lubke T et al, 2001).

http://identifiers.org/pubmed/18690016
type: PublicationXref
id: 18690016
author: Schnetkamp, PP
author: Altimimi, HF
db: Pubmed
title: Na+/Ca2+-K+ exchangers (NCKX): functional properties and physiological roles
source: Channels (Austin) 1:62-9
year: 2007

Evidence985
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19164095
xref: http://identifiers.org/pubmed/14624363
comment: Proteins with transporting functions can be roughly classified into 3 categories: ATP-powered pumps, ion channels, and transporters. Pumps utilize the energy released by ATP hydrolysis to power the movement of the substrates across the membrane, against their electrochemical gradient. Channels at the open state can transfer the substrates (ions or water) down their electrochemical gradient, at an extremely high efficiency (up to 108 s-1). Transporters facilitate the movement of a specific substrate âeither against or following their concentration gradient, at a lower speed (about 102 -104 s-1); as generally believed, conformational change of the transporter protein is involved in the transfer process. According to the Human Genome Organization (HUGO) Gene Nomenclature Committee, all human transporters can be grouped into the solute-carrier (SLC) superfamily. Currently, there are 55 SLC families in the superfamily, with a total of at least 362 putatively functional protein-coding genes (Hediger et al, 2004; He et al., 2009). At least 20-25% amino-acid sequence identity is shared by members belonging to the same SLC family. No homology is shared between different SLC families. While the HUGO nomenclature system by definition only includes human genes, the nomenclature system has been informally extended to include rodent species through the use of lower cases letters (e.g., Slc1a1 denotes the rodent ortholog of the human SLC1A1 gene). And it's worthwhile to mention that pumps, channels and aquporins are not included in SLC superfamily.

Evidence984
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: This pathway groups the processes mediated by SLC transporters, by which vitamins and cofactors, as well as nucleosides, nucleotides, nucleobases, and related molecules cross lipid bilayer membranes.

UniProt:P34208 chk1
type: ProteinReference
name: chk1
name: rad27
name: SPCC1259.13
xref: UnificationXref7510
comment: FUNCTION 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. Binds to and phosphorylates CDC25. This leads to negative regulation of CDC25 and prevents mitotic entry.CATALYTIC ACTIVITY ATP + a protein = ADP + a phosphoprotein.SUBUNIT Interacts with rfp1.PTM Phosphorylated.SIMILARITY Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. NIM1 subfamily.SIMILARITY Contains 1 protein kinase domain.
organism: BioSource1

Evidence999
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17662945
comment: The function of V-type proton pumping ATPases is basically the same as that of F-type ATPases, except that V-ATPases cannot synthesize ATP from the proton motive force, the reverse reaction of pumping. When pumping, ATP hydrolysis drives a 120 degree rotation of the rotor which leads to movement of three protons into the phagosome (Adachi et al. 2007).

Evidence998
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11773613
xref: http://identifiers.org/pubmed/17222168
xref: http://identifiers.org/pubmed/17961083
xref: http://identifiers.org/pubmed/15340377
xref: http://identifiers.org/pubmed/15924268
xref: http://identifiers.org/pubmed/15901243
xref: http://identifiers.org/pubmed/16650285
xref: http://identifiers.org/pubmed/19448080
xref: http://identifiers.org/pubmed/20224213
xref: http://identifiers.org/pubmed/15809071
xref: http://identifiers.org/pubmed/19096770
xref: http://identifiers.org/pubmed/16107722
comment: Aquaporins (AQP's) are six-pass transmembrane proteins that form channels in membranes. Each monomer contains a central channel formed in part by two asparagine-proline-alanine motifs (NPA boxes) that confer selectivity for water and/or solutes. The monomers assemble into tetramers. Most aquaporins (i.e. AQP0/MIP, AQP1, AQP2, AQP3, AQP4, AQP5, AQP7, AQP8, AQP9, AQP10) passively transport water into and out of cells according to the osmotic gradient across the membrane. Four aquaporins (the aquaglyceroporins AQP3, AQP7, AQP9, AQP10) conduct glycerol, three aquaporins (AQP7, AQP9, AQP10) conduct urea, and one aquaporin (AQP6) conducts anions, especially nitrate. AQP8 also conducts ammonia in addition to water. AQP11 and AQP12, classified as group III aquaporins, were identified as a result of the genome sequencing project and are characterized by having variations in the first NPA box when compared to more traditional aquaporins. Additionally, a conserved cysteine residue is present about 9 amino acids downstream from the second NPA box and this cysteine is considered indicative of group III aquaporins. Purified AQP11 incorporated into liposomes showed water transport. Knockout mice lacking AQP11 had fatal cyst formation in the proximal tubule of the kidney. Exogenously expressed AQP12 showed intracellular localization. AQP12 is expressed exclusively in pancreatic acinar cells. Aquaporins are important in fluid and solute transport in various tissues. In adipocytes, glycerol generated by triglyceride hydrolysis is exported by AQP7 and is imported by liver cells via AQP9. AQP1 plays a role in forming cerebrospinal fluid and AQP1, AQP4, and AQP9 appear to be important in maintaining fluid balance in the brain. AQP0, AQP1, AQP3, AQP4, AQP8, AQP9, and AQP11 play roles in the physiology of the hepatobiliary tract. In the kidney, water and solutes are passed out of the bloodstream and into the proximal tubule via the slit-like structure formed by nephrin in the glomerulus. …

Evidence997
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19096781
xref: http://identifiers.org/pubmed/16764946
comment: Triglycerides stored in adipocytes are hydrolyzed to yield fatty acids and glycerol. The glycerol is passively transported out of the adipocyte and into the bloodstream by Aquaporin-7 (AQP7) located in the plasma membrane of adipocytes. Glycerol in the bloodstream is passively transported into liver cells by AQP9 located in the plasma membrane of hepatocytes. Once inside the liver cell the glycerol is a substrate for gluconeogenesis.

Evidence992
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17961083
xref: http://identifiers.org/pubmed/17222168
xref: http://identifiers.org/pubmed/15924268
xref: http://identifiers.org/pubmed/19096781
xref: http://identifiers.org/pubmed/15901243
xref: http://identifiers.org/pubmed/16764946
xref: http://identifiers.org/pubmed/19448080
xref: http://identifiers.org/pubmed/11773613
xref: http://identifiers.org/pubmed/17513417
xref: http://identifiers.org/pubmed/15340377
xref: http://identifiers.org/pubmed/18173545
xref: http://identifiers.org/pubmed/19096775
xref: http://identifiers.org/pubmed/18566824
xref: http://identifiers.org/pubmed/19096770
comment: Aquaporins (AQP's) are six-pass transmembrane proteins that form channels in membranes. Each monomer contains a central channel formed in part by two asparagine-proline-alanine motifs (NPA boxes) that confer selectivity for water and/or solutes. The monomers assemble into tetramers. Most aquaporins (i.e. AQP0/MIP, AQP1, AQP2, AQP3, AQP4, AQP5, AQP7, AQP8, AQP9, AQP10) passively transport water into and out of cells according to the osmotic gradient across the membrane. Four aquaporins (the aquaglyceroporins AQP3, AQP7, AQP9, AQP10) conduct glycerol, three aquaporins (AQP7, AQP9, AQP10) conduct urea, and one aquaporin (AQP6) conducts anions, especially nitrate. AQP8 also conducts ammonia in addition to water. AQP11 and AQP12, classified as group III aquaporins, were identified as a result of the genome sequencing project and are characterized by having variations in the first NPA box when compared to more traditional aquaporins. Additionally, a conserved cysteine residue is present about 9 amino acids downstream from the second NPA box and this cysteine is considered indicative of group III aquaporins. Purified AQP11 incorporated into liposomes showed water transport. Knockout mice lacking AQP11 had fatal cyst formation in the proximal tubule of the kidney. Exogenously expressed AQP12 showed intracellular localization. AQP12 is expressed exclusively in pancreatic acinar cells. Aquaporins are important in fluid and solute transport in various tissues. In adipocytes, glycerol generated by triglyceride hydrolysis is exported by AQP7 and is imported by liver cells via AQP9. AQP1 plays a role in forming cerebrospinal fluid and AQP1, AQP4, and AQP9 appear to be important in maintaining fluid balance in the brain. AQP0, AQP1, AQP3, AQP4, AQP8, AQP9, and AQP11 play roles in the physiology of the hepatobiliary tract. In the kidney, water and solutes are passed out of the bloodstream and into the proximal tubule via the slit-like structure formed by nephrin in the glomerulus. …

Evidence991
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12084581
xref: http://identifiers.org/pubmed/11573934
xref: http://identifiers.org/pubmed/18762715
xref: http://identifiers.org/pubmed/19590626
xref: http://identifiers.org/pubmed/11027599
xref: http://identifiers.org/pubmed/10564231
comment: Aquaporin-9 (AQP9) and AQP10 are 6-pass transmembrane proteins that passively transport urea across the plasma membrane through a pore in each subunit of a homotetramer.

MicroRNA (miRNA) Biogenesis
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction652
pathway component: BiochemicalReaction653
pathway component: TemplateReaction10
evidence: Evidence1139
xref: UnificationXref7279
xref: UnificationXref7278
pathway order: PathwayStep1116
pathway order: PathwayStep1117
pathway order: PathwayStep1118
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Evidence990
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12084581
xref: http://identifiers.org/pubmed/11573934
xref: http://identifiers.org/pubmed/18762715
xref: http://identifiers.org/pubmed/19590626
xref: http://identifiers.org/pubmed/18678926
xref: http://identifiers.org/pubmed/11027599
xref: http://identifiers.org/pubmed/10564231
comment: Aquaporin-9 (AQP9) and AQP10 are 6-pass transmembrane proteins that passively transport urea across the plasma membrane through a pore in each subunit of a homotetramer.

Evidence996
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17961083
xref: http://identifiers.org/pubmed/18762715
xref: http://identifiers.org/pubmed/19590626
xref: http://identifiers.org/pubmed/11027599
xref: http://identifiers.org/pubmed/10564231
comment: Aquaporin-9 (AQP9) passively transports water, glycerol, urea, and some other small neutral solutes across the plasma membrane according to the osmotic gradient. AQP9 is expressed in the sinusoidal plasma membrane in the liver facing the portal vein where it is believed to be responsible for glycerol uptake as part of gluconeogenesis. AQP9 is also expressed in glia, neurons, and peripheral leukocytes.

Evidence995
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18555844
xref: http://identifiers.org/pubmed/17961083
xref: http://identifiers.org/pubmed/11952783
xref: http://identifiers.org/pubmed/9405233
xref: http://identifiers.org/pubmed/16325777
comment: Aquaporin-7 (AQP7) passively transports glycerol and water across the plasma membrane according to the osmotic gradient. AQP7 is expressed in adipocytes under the direct control of the PPARG and RXRA nuclear receptors. Expression of AQP7 correlates with release of glycerol from adipocytes. AQP7 is seen to translocate from the nuclear periphery to the plasma membrane during adrenaline-stimulated lipolysis. In rat AQP7 also transports urea.

Evidence994
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11773613
xref: http://identifiers.org/pubmed/17222168
xref: http://identifiers.org/pubmed/15924268
xref: http://identifiers.org/pubmed/19096775
xref: http://identifiers.org/pubmed/18566824
comment: In the kidney water and solutes are passed out of the bloodstream and into the proximal tubule via the slit-like structure formed by nephrin in the glomerulus. Water is reabsorbed from the filtrate during its transit through the proximal tubule, the descending loop of Henle, the distal convoluted tubule, and the collecting duct. Aquaporin-1 (AQP1) in the proximal tubule and the descending thin limb of Henle is responsible for about 90% of reabsorption (as estimated from mouse knockouts of AQP1). AQP1 is located on both the apical and basolateral surface of epithelial cells and thus transports water through the epithelium and back into the bloodstream. In the collecting duct epithelial cells have AQP2 on their apical surface and AQP3 and AQP4 on their basolateral surface to transport water across the epithelium. The permeability of the epithelium is regulated by vasopressin, which activates the phosphorylation and subsequent translocation of AQP2 from intracellular vesicles to the plasma membrane.

Evidence993
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7538665
xref: http://identifiers.org/pubmed/9374640
xref: http://identifiers.org/pubmed/15703994
xref: http://identifiers.org/pubmed/9369468
xref: http://identifiers.org/pubmed/18678926
xref: http://identifiers.org/pubmed/9374639
xref: http://identifiers.org/pubmed/7503232
xref: http://identifiers.org/pubmed/7526388
xref: http://identifiers.org/pubmed/8063828
comment: Aquaporin-3 (AQP3) passively transports water and glycerol across the plasma membrane according to the osmotic gradient. AQP3 is expressed in airway epithelia, secretory glands, skin, the collecting ducts of the kidney, and the basolateral surface of intestinal epithelium..

Evidence960
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17716241
xref: http://identifiers.org/pubmed/12734757
xref: http://identifiers.org/pubmed/14770312
comment: Calcium ions are used by cells as ubiquitous signalling molecules that control diverse physiological events. Three mammalian gene families control Ca2+ transport across plasma membranes and intracellular compartments (Lytton J, 2007). They are the Na+/Ca2+ exchanger family designated NCX (SLC8) (three members NCX1-3) (Quednau BD et al, 2004), the Na+/Ca2+-K+ exchanger family designated NCKX (SLC24) (five members NCKX1-5) (Schnetkamp PP, 2004) and a Ca2+/cation exchanger (NCKX6, NCLX) whose physiological function remains unclear.

Evidence961
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15522866
xref: http://identifiers.org/pubmed/11940519
comment: NHE6 (SLC9A6) (Brett CL et al, 2002; Nakamura N et al, 2005) is expressed ubiquitously and thought to play a housekeeping role in pH homeostasis in early endosomes.

Evidence962
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15522866
xref: http://identifiers.org/pubmed/11279194
comment: NHE7 and 8 (SLC9A7,8) (Nakamura N et al, 2005) are expressed ubiquitously and thought to play a housekeeping role in pH homeostasis in the trans-golgi network.

Evidence963
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15522866
comment: NHE9 (SLC9A9) (Nakamura N et al, 2005) is expressed ubiquitously and thought to play a housekeeping role in pH homeostasis in the late endosome membrane.

http://identifiers.org/pubmed/10940339
type: PublicationXref
id: 10940339
author: Laurell, H
author: Holm, C
author: Osterlund, T
author: Contreras, JA
db: Pubmed
title: Molecular mechanisms regulating hormone-sensitive lipase and lipolysis
source: Annu Rev Nutr 20:365-93
year: 2000

Evidence968
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16461757
xref: http://identifiers.org/pubmed/17581921
xref: http://identifiers.org/pubmed/17693766
xref: http://identifiers.org/pubmed/18690016
xref: http://identifiers.org/pubmed/12759754
xref: http://identifiers.org/pubmed/12739168
xref: http://identifiers.org/pubmed/18195086
xref: http://identifiers.org/pubmed/12845533
xref: http://identifiers.org/pubmed/19164095
xref: http://identifiers.org/pubmed/18400693
xref: http://identifiers.org/pubmed/12734757
xref: http://identifiers.org/pubmed/16955105
comment: Teleologically, one might argue that inorganic cation and anion transport would be evolutionarily among the oldest transport functions. Eight families comprise the group that transports exclusively inorganic cations and anions across membranes : SLC4 plays a pivotal role in mediating Na+- and/or Clâ-dependent transport of basic anions [e.g. HCO3â, (CO3)2â] in various tissues and cell types (in addition to pH regulation, specific members of this family also contribute to vectorial trans-epithelial base transport in several organ systems including the kidney, pancreas, and eye) (Pushkin A and Kurtz I, 2006); SLC8 is a group of Na+/Ca2+ exchangers (SLC8A1 is involved in cardiac contractility) (Quednau BD et al, 2004); SLC24 is a group of Na+/Ca2+ or Na+/K+ exchangers (Altimimi HF and Schnetkamp PP, 2007); SLC9 comprises Na+/H+ exchanger proteins involved in the electroneutral exchange of sodium ion and protons (Orlowski J and Grinstein S, 2004); SLC12 functions as Na+, K+ and Clâ ion electroneutral symporters (Hebert SC et al, 2004); SLC26 is the trans-epithelial multifunctional anion (e.g. sulfate, oxalate, HCO3â, Clâ) exchanger family, important in cartilage development, production of thyroid hormone, sound amplification in the cochlea etc (Sindic A et al, 2007; Dorwart MR et al, 2008; Ashmore J, 2008). SLC34 is an important Type II Na+/(HPO4)2â symporter (Forster IC et al, 2006; Virkki LV et al, 2007); SLC20 was originally identified as a viral receptor, and functions as a Type III Na+/(H2PO4)â symporter (Collins JF et al, 2004; Virkki LV et al, 2007). Eight SLC gene families are involved in the transport of amino acids and oligopeptides.

Evidence969
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17509534
xref: http://identifiers.org/pubmed/16807400
xref: http://identifiers.org/pubmed/16330770
comment: The human gene family SLC47 encodes 2 multidrug and toxin extrusion (MATE) proteins. Mammalian MATE-type transporters are responsible for the final step in the excretion of metabolic waste and xenobiotic organic cations in the kidney and liver through electroneutral exchange of H(+). MATE1 is primarily expressed in the kidney and liver, where it is localized to the luminal membranes of the urinary tubules and bile canaliculi. When expressed in HEK293 cells, MATE1 mediates H(+)-coupled electroneutral exchange of various drugs (Otsuka M et al, 2005). MATE2 is a human kidney-specific H+/organic cation antiporter that is responsible for the tubular secretion of cationic drugs across the brush border membranes (Masuda S et al, 2006). Substrates for both MATEs include tetraethylammonium, 1-methyl-4-phenylpyridinium, cimetidine, metformin, creatinine, guanidine and procainamide (Tanihara Y et al, 2007).

Evidence964
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11279194
xref: http://identifiers.org/pubmed/15522866
xref: http://identifiers.org/pubmed/12845533
comment: The SLC9 gene family encode proteins (sodium/proton exchangers, NHE or NHX) which exchange sodium (influx) for protons (efflux) electroneutrally. This mechanism is important because many metabolic processes generate acids which need to be removed to maintain pH. This is the major proton extruding system in cells, driven by the inward sodium ion chemical gradient. To date, there are eleven NHE genes, NHE1-11. NHE1-5 exchange cations at the cell membrane. NHE6-9 exchange cations at endosomal membranes or the trans-golgi network membranes.

Evidence965
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9299407
xref: http://identifiers.org/pubmed/7896779
xref: http://identifiers.org/pubmed/7756356
comment: The prototypical transporters of the SLC15 gene family are PEPT1 and PEPT2, which mediate the uptake of every possible di- and tri-peptide. PEPT1 (PTR1) is expressed mainly in the intestine (Liang R et al, 1995; Saito H et al, 1997) while PEPT2 (PTR2) is expressed in the kidney (Liu W et al, 1995).

Evidence966
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11741232
comment: A bioinformatics approach identified two further human transporters, PHT1 and PHT2 (Botka CW et al, 2000). These two transporters may be located on the lysosomal membrane for the proton-coupled export of histidine and di-peptides from lysosomal protein degradation.

Evidence967
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12905028
comment: The human SLC15 gene family encode four proton-coupled oligopeptide transporters; PEPT1 (SLC15A1), PEPT2 (SLC15A2), PHT2 (SLC15A3) and PHT1 (SLC15A4). These cotransporters are part of the Proton-coupled Oligopeptide Transporter (POT) superfamily (also called Peptide Transporter (PTR) family) (Daniel H and Kottra G, 2004).

http://identifiers.org/pubmed/9153422
type: PublicationXref
id: 9153422
author: Batelier, G
author: Soulié, S
author: Melki, R
author: Williams RC, Jr
db: Pubmed
title: Cytoplasmic chaperonin containing TCP-1: structural and functional characterization
source: Biochemistry 36:5817-26
year: 1997

Evidence973
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12748859
comment: The human SLC30 gene family of solute carriers is thought to participate in the homeostasis of zinc ions and facilitate zinc transport into specialized compartments of the cell such as endosomes, golgi network and synaptic vesicles. There are 10 members of this family, named ZnT1-10. ZnT4, ZnT9 and ZnT10 have no function determined as of yet (Palmiter RD and Huang L, 2004).

Evidence974
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16675045
xref: http://identifiers.org/pubmed/18754861
xref: http://identifiers.org/pubmed/17374385
comment: Zinc is an essential element for all organisms because it serves as a catalytic or structural cofactor for many different proteins. Cellular zinc homoeostasis is co-ordinated through Zn2+-specific transporters which are members of two distinct gene families. Members of the SLC39 gene family (ZRTL-like import proteins1â14, ZIP1-14) are responsible for Zn2+ import into the cytoplasm, either across the plasma membrane or out of intracellular organelles. In contrast, members of the SLC30 gene family (zinc transporters 1â10, ZnT1-10) export Zn2+ from the cytoplasm, either across the plasma membrane into the extracellular space or into intracellular organelles (Murakami M and Hirano T, 2008; Devirgiliis C et al, 2007; Eide DJ, 2006)

Evidence971
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11904301
comment: The human gene SLC30A5 encodes the zinc transporter ZnT5. This protein is widely expressed but is most abundant in pancreatic beta cells (Kambe T et al, 2002). In these cells, ZnT5 mediates the transport of zinc into secretory granules that contain insulin.

Evidence972
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12446736
comment: The human gene SLC30A7 encodes the zinc transporter ZnT7. It is thought to be present in the small intestine and lung in humans (Kirschke CP and Huang L, 2003). Functional properties assigned to ZnT7 are based on studies conducted with mouse experiments.

Evidence970
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15276077
comment: The human gene SLC30A1 encodes the zinc transporter ZnT1. It is widely expressed throughout the body and it's expression is regulated by zinc. ZnT1 is the only member of the SLC30 gene family that is located on the plasma membrane and mediates the transport of zinc out of the cell (Devergnas S et al, 2004).

Evidence979
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9010752
xref: http://identifiers.org/pubmed/15576474
comment: The human gene SLC35A1 encodes the CMP-sialic acid transporter which mediates the antiport of CMP-sialic acid into the Golgi lumen in exchange for CMP (Ishida N et al, 1996). Defects in SLC35A1 are the cause of congenital disorder of glycosylation type 2F (CDG2F). CDGs are a family of severe inherited diseases caused by a defect in protein N-glycosylation (Martinez-Duncker I et al, 2005).

Evidence977
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12748858
xref: http://identifiers.org/pubmed/12811562
xref: http://identifiers.org/pubmed/12750891
xref: http://identifiers.org/pubmed/19164095
comment: Hexoses like glucose, galactose and fructose serve as basic fuel molecules for eukaryotic cells. Indeed, glucose is the main energy source for mammalian cells. These sugars are unable to diffuse across cellular membranes, and require transporter proteins for entry into and exit out of cells. Four gene families encode hexose transporter proteins (He et al, 2009). SLC2 family contains 14 genes and encode facilitative glucose transporters (GLUTs) (Uldry M and Thorens B, 2004). SLC5 family contains 12 genes and encode Na+/glucose symporters (Wright EM and Turk E, 2004). SLC37 family contains 4 members and encode sugar-phosphate/phosphate exchangers (Bartoloni L and Antonarakis SE, 2004). SLC45 family has 4 members and encode putative sugar/H+ symporters.

Evidence978
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9096318
xref: http://identifiers.org/pubmed/19061983
comment: The human gene SLC33A1 encodes acetyl-CoA transporter AT1 (Kanamori A et al, 1997).Acetyl-CoA is transported to the lumen of the Golgi apparatus, where it serves as the substrate of acetyltransferases that modify the sialyl residues of gangliosides and glycoproteins. Defects in SLC33A1 are the cause of spastic paraplegia autosomal dominant type 42 (SPG42) which is a neurodegenerative disorder (Lin P et al, 2008).

Evidence975
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9207117
xref: http://identifiers.org/pubmed/17211682
xref: http://identifiers.org/pubmed/11734551
comment: Copper (Cu2+) is essential for many important biological processes such as mitochondrial oxidative phosphorylation, detoxification of free radicals, iron metabolism and neurotransmiter synthesis. Too much influx results in cell poisoning. In humans, there are two member of the SLC31 gene family that are implicated in copper transport. The human gene SLC31A1 encodes human copper transporter 1, hCTR1 and is ubiquitiously expressed, with highest levels seen in the liver.. It was first identified by functional complementation in ctr1-deficient yeast (Zhou B and Gitschier J, 1997). hCTR1 exists as a homotrimer at the plasma membrane of cells (De Feo CJ et al, 2007) and is responsible for high-affinity copper uptake (Lee J et al, 2002). The second gene product, hCTR2, has not be characterized yet.

http://identifiers.org/pubmed/17712357
type: PublicationXref
id: 17712357
author: Hardie, DG
db: Pubmed
title: AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy
source: Nat Rev Mol Cell Biol 8:774-85
year: 2007

Evidence976
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16720382
xref: http://identifiers.org/pubmed/16825786
xref: http://identifiers.org/pubmed/17439925
xref: http://identifiers.org/pubmed/16675045
xref: http://identifiers.org/pubmed/12748861
xref: http://identifiers.org/pubmed/14530973
xref: http://identifiers.org/pubmed/12827356
xref: http://identifiers.org/pubmed/15157936
xref: http://identifiers.org/pubmed/16908340
xref: http://identifiers.org/pubmed/12836025
xref: http://identifiers.org/pubmed/19164095
xref: http://identifiers.org/pubmed/17215883
xref: http://identifiers.org/pubmed/17374385
comment: Six SLC gene families encode proteins which mediate transport of metals. The families are SLC11, SLC30, SLC31, SLC39, SLC40 and SLC41 (He L et al, 2009; Bressler JP et al, 2007).

Gene Expression
type: Pathway
data source: Provenance1
pathway component: REACT 107708.9
pathway component: REACT 110265.9
pathway component: REACT 132581.5
pathway component: REACT 128867.5
pathway component: REACT 127779.5
pathway component: REACT 114358.8
pathway component: REACT 83961.9
pathway component: REACT 84003.9
pathway component: REACT 34720.10
pathway component: REACT 93223.9
pathway component: RNA Polymerase I, RNA Polymerase III, and Mitochondrial Transcription
pathway component: REACT 81734.9
evidence: Evidence1179
xref: RelationshipXref974
xref: UnificationXref7507
xref: UnificationXref7506
pathway order: PathwayStep1158
pathway order: PathwayStep844
pathway order: PathwayStep118
pathway order: PathwayStep861
pathway order: PathwayStep305
pathway order: PathwayStep854
pathway order: PathwayStep1120
pathway order: PathwayStep310
pathway order: PathwayStep138
pathway order: PathwayStep314
pathway order: PathwayStep1115
pathway order: PathwayStep297
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Evidence940
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1671046
xref: http://identifiers.org/pubmed/1974050
xref: http://identifiers.org/pubmed/9081985
xref: http://identifiers.org/pubmed/8104944
xref: http://identifiers.org/pubmed/8144677
xref: http://identifiers.org/pubmed/1328683
comment: After RFC initiates the assembly of the primer recognition complex, the complex of pol delta and PCNA is responsible for incorporating the additional nucleotides prior to the position of the next downstream initiator RNA primer. On the lagging strand, short discontinuous segments of DNA, called Okazaki fragments, are synthesized on RNA primers. The average length of the Okazaki fragments is 100 nucleotides. Polymerase switching is a key event that allows the processive synthesis of DNA by the pol delta and PCNA complex.

Evidence941
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11473323
xref: http://identifiers.org/pubmed/7711022
xref: http://identifiers.org/pubmed/11724925
comment: When the polymerase delta:PCNA complex reaches a downstream Okazaki fragment, strand displacement synthesis occurs. The primer containing 5'-terminus of the downstream Okazaki fragment is folded into a single-stranded flap.

Evidence942
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11473323
comment: After RPA binds the long flap, it recruits the Dna2 endonuclease. Dna2 endonuclease removes most of the flap, but the job of complete removal of the flap is then completed by FEN-1.

Evidence943
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9080773
xref: http://identifiers.org/pubmed/8824221
xref: http://identifiers.org/pubmed/10806216
xref: http://identifiers.org/pubmed/10409700
xref: http://identifiers.org/pubmed/11825897
xref: http://identifiers.org/pubmed/7876218
xref: http://identifiers.org/pubmed/8131753
comment: The remaining flap, which is too short to support RPA binding, is then processed by FEN-1. There is evidence that binding of RPA to the displaced end of the RNA-containing Okazaki fragment prevents FEN-1 from accessing the substrate. FEN-1 is a structure-specific endonuclease that cleaves near the base of the flap at a position one nucleotide into the annealed region. Biochemical studies have shown that the preferred substrate for FEN-1 consists of a one-nucleotide 3'-tail on the upstream primer in addition to the 5'-flap of the downstream primer.

Evidence944
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8131753
xref: http://identifiers.org/pubmed/7926735
xref: http://identifiers.org/pubmed/7644470
comment: Two endonucleases, Dna2 and flap endonuclease 1 (FEN-1), are responsible for resolving the nascent flap structure (Tsurimoto and Stillman 1991). The Dna2 endonuclease/helicase in yeast is a monomer of approximately 172 kDa. Human FEN-1 is a single polypeptide of approximately 42 kDa. Replication Protein A regulates the switching of endonucleases during the removal of the displaced flap.

Evidence945
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9759502
xref: http://identifiers.org/pubmed/10959839
xref: http://identifiers.org/pubmed/9081985
xref: http://identifiers.org/pubmed/8392066
comment: Removal of the flap by FEN-1 leads to the generation of a nick between the 3'-end of the upstream Okazaki fragment and the 5'-end of the downstream Okazaki fragment. DNA ligase I then seals the nicks between adjacent processed Okazaki fragments to generate intact double-stranded DNA.

Evidence946
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1671046
comment: The key event that allows the processive synthesis on the lagging strand, is polymerase switching from pol alpha to pol delta, as on the leading strand. However, the processive synthesis on the lagging strand proceeds very differently. DNA synthesis is discontinuous, and involves the formation of short fragments called the Okazaki fragments. During the synthesis of Okazaki fragments, the RNA primer is folded into a single-stranded flap, which is removed by endonucleases. This is followed by the ligation of adjacent Okazaki fragments.

Metabolism of nitric oxide
type: Pathway
data source: Provenance1
pathway component: REACT 131084.5
evidence: Evidence590
xref: UnificationXref3858
xref: UnificationXref3859
xref: RelationshipXref428
pathway order: PathwayStep580
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Evidence947
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9081985
comment: Due to the antiparallel nature of DNA, DNA polymerization is unidirectional, and one strand is synthesized discontinuously. This strand is called the lagging strand. Although the polymerase switching on the lagging strand is very similar to that on the leading strand, the processive synthesis on the two strands proceeds quite differently. Short DNA fragments, about 100 bases long, called Okazaki fragments are synthesized on the RNA-DNA primers first. Strand-displacement synthesis occurs, whereby the primer-containing 5'-terminus of the adjacent Okazaki fragment is folded into a single-stranded flap structure. This flap structure is removed by endonucleases, and the adjacent Okazaki fragments are joined by DNA ligase.

Evidence948
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1976634
xref: http://identifiers.org/pubmed/1536007
xref: http://identifiers.org/pubmed/7623835
xref: http://identifiers.org/pubmed/9081985
xref: http://identifiers.org/pubmed/8594377
comment: Accurate and efficient genome duplication requires coordinated processes to replicate two template strands at eucaryotic replication forks. Knowledge of the fundamental reactions involved in replication fork progression is derived largely from biochemical studies of the replication of simian virus and from yeast genetic studies. Since duplex DNA forms an anti-parallel structure, and DNA polymerases are unidirectional, one of the new strands is synthesized continuously in the direction of fork movement. This strand is designated as the leading strand. The other strand grows in the direction away from fork movement, and is called the lagging strand. Several specific interactions among the various proteins involved in DNA replication underlie the mechanism of DNA synthesis, on both the leading and lagging strands, at a DNA replication fork. These interactions allow the replication enzymes to cooperate in the replication process (Hurwitz et al 1990; Brush et al 1996; Ayyagari et al 1995; Budd & Campbell 1997; Bambara et al 1997).

Evidence949
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: The actual synthesis of DNA occurs in the S phase of the cell cycle. This includes the initiation of DNA replication, when the first nucleotide of the new strand is laid down during the synthesis of the primer. The DNA replication preinitiation events begin in late M or early G1 phase.

http://identifiers.org/pubmed/9914500
type: PublicationXref
id: 9914500
author: di Padova, F
author: Freuler, F
author: Heilker, R
author: Eder, J
author: Pulfer, R
db: Pubmed
title: All three IkappaB isoforms and most Rel family members are stably associated with the IkappaB kinase 1/2 complex
source: Eur J Biochem 259:253-61
year: 1999

Evidence951
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Licensing factors are removed from the origin by various means like biochemical modification (phosphorylation) or by physical association with other proteins. This pathway includes the annotations of events in which the fates of different proteins at the origin are outlined.

Evidence952
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: DNA replication is regulated at various levels via ORC proteins. This pathway includes annotation of individual events that lead to the regulation of replication.

Evidence950
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: The eukaryotic six-subunit origin recognition complex (ORC) governs the initiation site of DNA replication and formation of the prereplication complex.

Evidence955
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17006453
xref: http://identifiers.org/pubmed/10837493
comment: The human gene ABCB6 encodes a mitochondrial half-type ATP-binding cassette (ABC) protein MTABC3 which is uniquely located on the outer mitochondrial membrane and is functional as a homodimer (Krishnamurthy et al. 2006). It plays a crucial role in heme synthesis by mediating porphyrin uptake into mitochondria (Mitsuhashi et al. 2000, Krishnamurthy et al. 2006).

Evidence956
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17656326
comment: Mammalian ABC transporters are usually found on the plasma membrane and on organelles such as the ER and peroxisome but a small number are also located on the mitochondria. Here they are thought to play roles in heme biosynthesis and iron-sulphur cluster synthesis (Burke & Ardehali 2007).

Evidence953
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1536007
xref: http://identifiers.org/pubmed/12045100
xref: http://identifiers.org/pubmed/11257218
xref: http://identifiers.org/pubmed/8223461
xref: http://identifiers.org/pubmed/10966477
xref: http://identifiers.org/pubmed/1579437
comment: Studies in the past decade have suggested that the basic mechanism of DNA replication initiation is conserved in all kingdoms of life. Initiation in unicellular eukaryotes, in particular Saccharomyces cerevisiae (budding yeast), is well understood, and has served as a model for studies of DNA replication initiation in multicellular eukaryotes, including humans. In general terms, the first step of initiation is the binding of the replication initiator to the origin of replication. The replicative helicase is then assembled onto the origin, usually by a helicase assembly factor. Either shortly before or shortly after helicase assembly, some local unwinding of the origin of replication occurs in a region rich in adenine and thymine bases (often termed a DNA unwinding element, DUE). The unwound region provides the substrate for primer synthesis and initiation of DNA replication. The best-defined eukaryotic origins are those of S. cerevisiae, which have well-conserved sequence elements for initiator binding, DNA unwinding and binding of accessory proteins. In multicellular eukaryotes, unlike S. cerevisiae, these loci appear not to be defined by the presence of a DNA sequence motif. Indeed, choice of replication origins in a multicellular eukaryote may vary with developmental stage and tissue type. In cell-free models of metazoan DNA replication, such as the one provided by Xenopus egg extracts, there are only limited DNA sequence specificity requirements for replication initiation (Kelly & Brown 2000; Bell & Dutta 2002; Marahrens & Stillman 1992; Cimbora & Groudine 2001; Mahbubani et al 1992, Hyrien & Mechali 1993).

Evidence954
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12892562
xref: http://identifiers.org/pubmed/9878413
xref: http://identifiers.org/pubmed/10196363
xref: http://identifiers.org/pubmed/10922475
xref: http://identifiers.org/pubmed/15225610
xref: http://identifiers.org/pubmed/9883897
xref: http://identifiers.org/pubmed/15215243
comment: Mitochondrial ABC transporters are thought to play a key role in iron metabolism and heme biosynthesis. All mitochondrial ABC transporters described to date are of the half-transporter type and would probably function as dimers (Ramjeesingh et al. 2003) but their dimerization partners have not yet been identified. ABC7 is the functional human orthologue of yeast Atm1p (Csere et al. 1998), is predicted to dimerize in the same way as Atm1p (Chloupková et al. 2004) and is probably involved in iron homeostasis. Defects in ABCB7 are the cause of X-linked sideroblastic anemia with ataxia (ASAT) [MIM:301310] (Allikmets et al. 1999). Human genes ABCB8 and ABCB10 encode mABC1 and mABC2 respectively (Hogue et al. 1999, Zhang et al 2000 respectively). They would be expected to dimerize, as demonstrated for mABC2 (Graf et al. 2004). Both are believed to have similar functionality to ABC7 although this has not been demonstrated yet.

Evidence959
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15060069
xref: http://identifiers.org/pubmed/14625281
comment: SLC24A6 (NCKX6, NCLX) (Palty R et al, 2004) encodes a protein which can transport Li+ or Na+ in exchange for Ca2+ in an K+-independent manner (Cai X and Lytton J, 2004). Lithium exchange with calcium is shown here.

Evidence957
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16816140
comment: The multidrug resistance associated protein (MRPs) subfamily of the ABC transporter family can transport a wide and diverse range of organic anions that can be endogenous compounds and xenobiotics and their metabolites. All human MRPs (except MRP9) can mediate these transport reactions (Deeley et al. 2006). Separately, specific reactions have also been annotated to describe the roles of ABCC4 in platelet dense granule assembly, of ABCC1 in LTC4 export (an aspect of leukotriene synthesis), and of ABCC3 in bile salt efflux.

Evidence958
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15209530
xref: http://identifiers.org/pubmed/11435397
xref: http://identifiers.org/pubmed/12045106
xref: http://identifiers.org/pubmed/19234479
comment: The ATP-binding cassette (ABC) superfamily of active transporters involves a large number of functionally diverse transmembrane proteins. They transport a variety of compounds through membranes against steep concentration gradients at the cost of ATP hydrolysis. These substrates include amino acids, lipids, inorganic ions, peptides, saccharides, peptides for antigen presentation, metals, drugs, and proteins. The ABC transporters not only move a variety of substrates into and out of the cell, but are also involved in intracellular compartmental transport. Energy derived from the hydrolysis of ATP is used to transport the substrate across the membrane against a concentration gradient. Human genome contains 48 ABC genes; 16 of these have a known function and 14 are associated with a defined human disease (Dean et al. 2001, Borst and Elferink 2002, Rees et al. 2009).

cobalamin(III)
type: SmallMoleculeReference
name: cob(III)alamin [ChEBI:28911]
name: alpha-(5,6-dimethylbenzimidazolyl)cobamide
name: Cobalamin (III)
name: cobalamin(1+)
name: cob(III)alamin
name: Cbl
xref: UnificationXref4608

http://identifiers.org/pubmed/10987144
type: PublicationXref
id: 10987144
author: Kwon, OS
author: Choi, SY
author: Moon, BJ
author: Lee, HS
db: Pubmed
title: Human pyridoxal kinase: overexpression and properties of the recombinant enzyme
source: Mol Cells 10:452-9
year: 2000

1-acyl-sn-glycero-3-phospho-D-myo-inositol
type: SmallMoleculeReference
name: 1-Acyl-sn-glycero-3-phosphoinositol
name: 1-acyl-sn-glycero-3-phospho-D-myo-inositol [ChEBI:28914]
xref: UnificationXref3353

http://identifiers.org/pubmed/17335080
type: PublicationXref
id: 17335080
author: Li, HY
author: Zhou, XF
db: Pubmed
title: Roles of glial p75NTR in axonal regeneration
source: J Neurosci Res 85:1601-5
year: 2007

UniProt:Q10305
type: ProteinReference
xref: UnificationXref1388
organism: BioSource1

http://identifiers.org/pubmed/8672512
type: PublicationXref
id: 8672512
author: Horiuchi, S
author: Sano, H
author: Yoshida, M
author: Jinnouchi, Y
author: Higashi, T
author: Ikeda, K
author: Araki, T
author: Ueda, S
db: Pubmed
title: N (epsilon)-(carboxymethyl)lysine protein adduct is a major immunological epitope in proteins modified with advanced glycation end products of the Maillard reaction
source: Biochemistry 35:8075-83
year: 1996

http://identifiers.org/pubmed/20576942
type: PublicationXref
id: 20576942
author: Kühl, Michael
author: Rao, Tata Purushothama
db: Pubmed
title: An updated overview on Wnt signaling pathways: a prelude for more
source: Circ. Res. 106:1798-806
year: 2010

2-acyl-sn-glycero-3-phosphoethanolamine [ChEBI:28936]
type: SmallMoleculeReference
name: 2-acyl-sn-glycero-3-phosphoethanolamine
xref: UnificationXref3251

NH4+
type: SmallMoleculeReference
name: NH4+ [ChEBI:28938]
xref: UnificationXref4193

UniProt:P14068
type: ProteinReference
xref: UnificationXref7677
organism: BioSource1

MASTL Facilitates Mitotic Progression
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction696
evidence: Evidence1228
xref: UnificationXref7741
xref: UnificationXref7740
pathway order: PathwayStep1207
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UnificationXref6213
type: UnificationXref
id: O13726
db: UniProt

UnificationXref6214
type: UnificationXref
id: 3662615
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662615

IRS-mediated signalling
type: Pathway
data source: Provenance1
pathway component: REACT 143809.5
pathway component: PI3K Cascade
evidence: Evidence217
xref: UnificationXref1141
xref: UnificationXref1140
pathway order: PathwayStep214
pathway order: PathwayStep213
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UnificationXref6211
type: UnificationXref
id: 425971
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=425971

UnificationXref6212
type: UnificationXref
id: REACT_20087
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20087.2

Destabilization of mRNA by Tristetraprolin (TTP)
type: Pathway
data source: Provenance1
pathway component: Tristetraproline (TTP) Binds AU-rich Elements in 3' UTR of Target mRNAs
evidence: Evidence309
xref: UnificationXref1751
xref: UnificationXref1750
pathway order: PathwayStep303
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UnificationXref6210
type: UnificationXref
id: REACT_3923
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3923.2

UnificationXref6219
type: UnificationXref
id: REACT_19508
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19508.1

UnificationXref6217
type: UnificationXref
id: GO:0005796
db: GENE ONTOLOGY

UnificationXref6218
type: UnificationXref
id: 425969
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=425969

UnificationXref6215
type: UnificationXref
id: 3662617
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662617

UnificationXref6216
type: UnificationXref
id: REACT_108681
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_108681.9

http://identifiers.org/pubmed/20593814
type: PublicationXref
id: 20593814
author: Thorpe, C
author: Bahnson, BJ
author: Daithankar, VN
author: Schaefer, SA
author: Dong, M
db: Pubmed
title: Structure of the human sulfhydryl oxidase augmenter of liver regeneration and characterization of a human mutation causing an autosomal recessive myopathy
source: Biochemistry 49:6737-45
year: 2010

UniProt:Q10311
type: ProteinReference
xref: UnificationXref1693
organism: BioSource1

UnificationXref6222
type: UnificationXref
id: 3662618
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662618

UnificationXref6223
type: UnificationXref
id: 3662620
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662620

UnificationXref6224
type: UnificationXref
id: REACT_92389
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_92389.9

UnificationXref6225
type: UnificationXref
id: GO:0031906
db: GENE ONTOLOGY

UnificationXref6220
type: UnificationXref
id: 425958
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=425958

UniProt:Q10306
type: ProteinReference
xref: UnificationXref3920
organism: BioSource1

UnificationXref6221
type: UnificationXref
id: REACT_19769
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19769.2

UnificationXref6226
type: UnificationXref
id: 425999
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=425999

UnificationXref6227
type: UnificationXref
id: REACT_20336
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20336.1

UnificationXref6228
type: UnificationXref
id: 425977
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=425977

UnificationXref6229
type: UnificationXref
id: REACT_19873
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19873.2

UniProt:Q10349
type: ProteinReference
xref: UnificationXref4842
organism: BioSource1

http://identifiers.org/pubmed/11175906
type: PublicationXref
id: 11175906
author: Burden, A
author: Wu, CK
author: Wang, BC
author: Dailey, HA
author: Rose, JP
author: Sellers, VM
db: Pubmed
title: The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis.
source: Nat Struct Biol 8:156-60
year: 2001

2,4-Dinitro-1-chlorobenzene
type: SmallMoleculeReference
name: 1-chloro-2,4-dinitrobenzene [ChEBI:34718]
name: DNCB
name: 1-Chloro-2,4-dinitrobenzol
name: 1-chloro-2,4-dinitrobenzene
name: Dncb
name: 6-Chloro-1,3-dinitrobenzene
name: Dinitrochlorobenzene
name: 1,3-Dinitro-4-chlorobenzene
name: Chlorodinitrobenzene
name: 2,4-Dinitrophenyl chloride
name: Cdnb
name: 4-Chloro-1,3-dinitrobenzene
name: 2,4-Dinitrochlorobenzene
xref: UnificationXref5849

UniProt:Q10330
type: ProteinReference
xref: UnificationXref1985
organism: BioSource1

UniProt:Q10333
type: ProteinReference
xref: UnificationXref2883
organism: BioSource1

UniProt:Q10334
type: ProteinReference
xref: UnificationXref4759
organism: BioSource1

http://identifiers.org/pubmed/12671646
type: PublicationXref
id: 12671646
author: Chao, MV
db: Pubmed
title: Neurotrophins and their receptors: a convergence point for many signalling pathways
source: Nat Rev Neurosci 4:299-309
year: 2003

UniProt:Q10329
type: ProteinReference
xref: UnificationXref1657
organism: BioSource1

UnificationXref6200
type: UnificationXref
id: 3662600
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662600

UnificationXref6201
type: UnificationXref
id: 3662602
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662602

UnificationXref6202
type: UnificationXref
id: REACT_83166
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_83166.9

UnificationXref6203
type: UnificationXref
id: 3665465
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665465

UnificationXref6204
type: UnificationXref
id: REACT_86924
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_86924.9

UnificationXref6205
type: UnificationXref
id: GO:0031905
db: GENE ONTOLOGY

UnificationXref6206
type: UnificationXref
id: 425978
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=425978

UnificationXref6207
type: UnificationXref
id: REACT_19509
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19509.1

http://identifiers.org/pubmed/18760361
type: PublicationXref
id: 18760361
author: Maness, PF
author: Schmid, RS
db: Pubmed
title: L1 and NCAM adhesion molecules as signaling coreceptors in neuronal migration and process outgrowth
source: Curr Opin Neurobiol 18:245-50
year: 2008

UnificationXref6208
type: UnificationXref
id: CHEBI:29101
db: ChEBI

UnificationXref6209
type: UnificationXref
id: 83910
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=83910

UniProt:P36600
type: ProteinReference
xref: UnificationXref973
organism: BioSource1

UniProt:P36601
type: ProteinReference
xref: UnificationXref229
organism: BioSource1

UniProt:P36604
type: ProteinReference
xref: UnificationXref891
organism: BioSource1

P87140
type: Protein
entity reference: P87140
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Coatomer gamma subunit
xref: UnificationXref8716
feature: FragmentFeature1345
cellular location: GO:0005829
comment: Reactome DB_ID: 3661722
display name: COPG1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:O42937
data source: Provenance1
name: O42937
name: Coatomer beta' subunit
xref: UnificationXref8718
feature: FragmentFeature1346
cellular location: GO:0005829
comment: Reactome DB_ID: 3661710
display name: COPB2

Evidence459
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11969204
xref: http://identifiers.org/pubmed/12829805
comment: 4-methylcholesta-8(9),24-dien-3-one and NADPH + H+ react to form 4-methylcholesta-8(9),24-dien-3beta-ol and NADP+. This reaction takes place in the endoplasmic reticulum, catalyzed by HSD17B7. Two isoforms of the enzyme due to alternative splicing have been identified but only the first has been tested for enzymatic activity (Marijanovic et al. 2003). The human enzyme has not been studied extensively; molecular details of the reaction are inferred from those worked out in studies of material from rat liver (Gaylor 2002).

UniProt:P36603
type: ProteinReference
xref: UnificationXref7604
organism: BioSource1

Evidence458
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/4401584
xref: http://identifiers.org/pubmed/14506130
xref: http://identifiers.org/pubmed/10710235
comment: 4-methyl,4-carboxycholesta-8(9),24-dien-3beta-ol and NAD+ react to form 4-methylcholesta-8(9),24-dien-3-one, CO2, and NADH + H+. This reaction occurs in the endoplasmic reticulum, catalyzed by NSDHL (Caldas and Herman 2003). Defects in this enzyme are associated with CHILD syndrome (Congenital Hemidysplasia with Ichthyosiform nevus and Limb Defects) (Konig et al. 2000), but cholesterol biosynthesis in cells and tissues from affected individuals has not been characterized. Instead, the mechanism and stoichiometry of the reaction are inferred from biochemical studies of partially purified rat enzyme (Rahimtula and Gaylor 1972).

Q9P7F7
type: Protein
entity reference: Q9P7F7
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: CHM4A_HUMAN
name: Charged multivesicular body protein 4a
xref: UnificationXref8745
feature: FragmentFeature1348
cellular location: GO:0005829
comment: Reactome DB_ID: 3663442
display name: CHMP4A

Evidence457
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/240818
xref: http://identifiers.org/pubmed/7228857
xref: http://identifiers.org/pubmed/8663358
comment: 4,4-dimethylcholesta-8(9),24-dien-3beta-ol, NADPH + H+, and O2 react to form 4-methyl,4-carboxycholesta-8(9),24-dien-3beta-ol, NADP+, and H2O. This reaction, in the endoplasmic reticulum, is catalyzed by SC4MOL (C-4 methylsterol oxidase). The human enzyme has been identified based on its sequence similarity to yeast methyl sterol oxidase (ERG25) and the ability of the cloned human gene to rescue ERG25-deficient yeast cells (Li and Kaplan 1996). The mechanism and stoichiometry of the reaction have been inferred from studies of partially purified rat enzyme (Gaylor et al. 1975; Fukushima et al. 1981).

Q9P7F7
type: Protein
entity reference: Q9P7F7
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: CHM4B_HUMAN
name: Charged multivesicular body protein 4b
xref: UnificationXref8746
feature: FragmentFeature1349
cellular location: GO:0005829
comment: Reactome DB_ID: 3663443
display name: CHMP4B

Evidence456
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12618959
xref: http://identifiers.org/pubmed/16784888
comment: 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol and NADPH + H+ react to form 4,4-dimethylcholesta-8(9),24-dien-3beta-ol and NADP+, catalyzed by TM7SF2 in the endoplasmic reticulum. TM7SF2 protein has sterol delta14-reductase activity in vitro, and expression of the gene is induced by sterol starvation in human cells, as expected for a gene involved in sterol biosynthesis (Bennati et al. 2006). However, molecular studies of material from an individual with HEM/Greenberg skeletal dysplasia indicate that LBR, a protein that spans the inner nuclear membrane and has both laminin receptor and sterol delta14-reductase activities, is required for normal sterol 14delta-reductase activity in human cells. It remains to be determined whether both LBR and TM7SF2 catalyze this reaction in vivo, and whether the role of TM7SF2 is essential (Waterham et al. 2003).

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74767
data source: Provenance1
name: O74767
name: Coatomer epsilon subunit
xref: UnificationXref8721
feature: FragmentFeature1347
cellular location: GO:0005829
comment: Reactome DB_ID: 3661718
display name: COPE

Evidence455
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12618959
xref: http://identifiers.org/pubmed/16784888
xref: http://identifiers.org/pubmed/9878250
comment: 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol and NADPH + H+ react to form 4,4-dimethylcholesta-8(9),24-dien-3beta-ol and NADP+, catalyzed by LBR in the nuclear envelope. LBR protein spans the inner nuclear envelope, has an aminoterminal region with properties of a laminin receptor and a carboxyterminal domain with sequence similarity to sterol delta14-reductases (Holmer et al. 1998). Studies of material from an individual with HEM/Greenberg skeletal dysplasia indicate that LBR catalyzes the sterol delta14-reductase step of cholesterol biosynthesis in vivo. DNA sequencing revealed homozygosity for a mutant LBR allele encoding a truncated protein in the affected individual, and cells from the individual accumulated cholesta-8,14-dien-3beta-ol in culture. Transfection of wild-type LBR into the cultured cells reversed the accumulation of cholesta-8,14-dien-3beta-ol (Waterham et al. 2003). This observation is surprising because a second gene, TM7SF2, encodes an efficient sterol delta14-reductase that is localized to the endoplasmic reticulum whose expression is up-regulated in response to sterol depletion (Bennati et al. 2006). The physiological roles of LBR and TM7SF2 in vivo remain to be determined.

CHMP4
type: Protein
data source: Provenance1
member physical entity: Q9P7F7
xref: UnificationXref8748
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3663445

Evidence454
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3771545
xref: http://identifiers.org/pubmed/11969204
xref: http://identifiers.org/pubmed/2007571
xref: http://identifiers.org/pubmed/8619637
comment: Lanosterol, NADPH + H+, and O2 react to form 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, NADP+, H2O and formate. This oxidative demethylation reaction, in the endoplasmic reticulum, is catalyzed by lanosterol 14alpha-demethylase (CYP51A1). Although the reaction is annotated here as a single concerted event, studies with purified rat enzyme indicate that the methyl group is converted successively to an alcohol and an aldehyde before being released as formate (Trzaskos et al. 1986; Fischer et al. 1991; Gaylor 2002).

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14177
data source: Provenance1
name: O14177
name: CHM2A_HUMAN
name: Charged multivesicular body protein 2a
xref: UnificationXref8752
feature: FragmentFeature1352
cellular location: GO:0005829
comment: Reactome DB_ID: 3663434
display name: CHMP2A

Evidence453
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/14766201
xref: http://identifiers.org/pubmed/8593458
xref: http://identifiers.org/pubmed/5918048
comment: Lanosterol synthase (LS) catalyzes the cyclization of squalene 2,3-epoxide to lanosterol, a reaction that forms the sterol nucleus.LS is located on the ER membrane and is active as the monomer (Ruf et al, 2004).

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94318
data source: Provenance1
name: Charged multivesicular body protein 6
name: O94318
name: CHMP6_HUMAN
name: CHMP6(2-201)
xref: UnificationXref8754
feature: FragmentFeature1353
cellular location: GO:0005829
comment: Reactome DB_ID: 3663449
display name: CHMP6

Evidence452
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10666321
comment: Squalene monooxygenase (squalene epoxidase, SE) is located on the endoplamic reticulum. It catalyzes the oxidation of squalene to squalene 2,3-epoxide. SE seems to be an important rate-limiting enzyme in cholesterol biosynthesis.

Q9P7F7
type: Protein
entity reference: Q9P7F7
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Charged multivesicular body protein 4c
name: CHM4C_HUMAN
xref: UnificationXref8747
feature: FragmentFeature1350
cellular location: GO:0005829
comment: Reactome DB_ID: 3663444
display name: CHMP4C

Evidence451
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10896663
comment: In the second step, FDFT catalyzes the reduction of presqualene diphosphate to squalene (Pandit et al. 2000).

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14296
data source: Provenance1
name: Charged multivesicular body protein 3
name: CHMP3_HUMAN
name: CHMP3(2-222)
name: O14296
xref: UnificationXref8750
feature: FragmentFeature1351
cellular location: GO:0005829
comment: Reactome DB_ID: 3663438
display name: VPS24

Evidence450
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10896663
comment: Farnesyl diphosphate farnesyltransferase (FDFT; squalene synthase) catalyzes the reductive dimerization of two farnesyl diphosphate (FPP) molecules to form squalene. This happens in two distinct steps. The first step of dimerization forms presqualene diphosphate (Pandit et al. 2000).

Evidence460
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/240818
xref: http://identifiers.org/pubmed/7228857
xref: http://identifiers.org/pubmed/8663358
comment: 4-methylcholesta-8(9),24-dien-3beta-ol, NADPH + H+, and O2 react to form 4-carboxycholesta-8(9),24-dien-3beta-ol, NADP+, and H2O. This reaction, in the endoplasmic reticulum, is catalyzed by SC4MOL (C-4 methylsterol oxidase). The human enzyme has been identified based on its sequence similarity to yeast methyl sterol oxidase (ERG25) and the ability of the cloned human gene to rescue ERG25-deficient yeast cells (Li and Kaplan 1996). The mechanism and stoichiometry of the reaction have been inferred from studies of partially purified rat enzyme (Gaylor et al. 1975; Fukushima et al. 1981).

http://identifiers.org/pubmed/15189140
type: PublicationXref
id: 15189140
author: de Lange, T
author: Smogorzewska, A
db: Pubmed
title: Regulation of telomerase by telomeric proteins
source: Annu Rev Biochem 73:177-208
year: 2004

http://identifiers.org/pubmed/8682198
type: PublicationXref
id: 8682198
author: Hagerhall, C
author: Hederstedt, L
db: Pubmed
title: A structural model for the membrane-integral domain of succinate: quinone
source: FEBS Lett 389:25-31
year: 1996

UniProt:P36611
type: ProteinReference
xref: UnificationXref2861
organism: BioSource1

UniProt:P36612
type: ProteinReference
xref: UnificationXref1707
organism: BioSource1

Nucleotide-binding domain, leucine rich repeat containing receptor (NLR) signaling pathways
type: Pathway
data source: Provenance1
pathway component: REACT 138777.5
pathway component: REACT 154885.3
evidence: Evidence1058
xref: UnificationXref6726
xref: RelationshipXref887
xref: UnificationXref6725
pathway order: PathwayStep1036
pathway order: PathwayStep1039
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UniProt:P36613
type: ProteinReference
xref: UnificationXref315
organism: BioSource1

Evidence448
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16684881
xref: http://identifiers.org/pubmed/9741684
xref: http://identifiers.org/pubmed/10026212
comment: The family of enzymes called prenyltransferases is involved in the biosynthesis of isoprenoids. Two members of this family are known to catalyse the sequential condensation of isopentenyl pyrophosphate to DMAPP: farnesyl pyrophosphate synthase (FPPS) and geranylgeranyl pyrophosphate synthetase (GGPPS) (Kavanaugh et al, 2006).

Evidence447
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8806705
comment: Cytosolic isopentenyl diphosphate isomerase (IPP isomerase) catalyzes an essential activation step in the isoprenoid biosynthetic pathway. It rearranges isopentenyl pyrophosphate into its highly electrophilic isomer, dimethylallyl pyrophosphate (DMAPP). IPP isomerase may also be located in human peroxisomes but it's function there is not clear.

Evidence449
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16684881
xref: http://identifiers.org/pubmed/9741684
xref: http://identifiers.org/pubmed/10026212
comment: Further condensation of an isopentenyl pyrophosphate with geranyl pyrophosphate to form farnesyl pyrophosphate is catalyzed by the prenyltransferases FPP synthase and GGPP synthase. (Kavanagh et al, 2006)

Evidence444
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1967820
xref: http://identifiers.org/pubmed/10698924
comment: 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) catalyzes the four-electron reduction of HMG-CoA to mevalonate. Mevalonate concentrations in the cell are tightly controlled through the activity of HMGR, which is one of the most highly regulated enzymes known (Goldstein and Brown 1990).

Evidence443
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7913309
comment: 3-hydroxy-3-methylglutaryl Coenzyme A synthase (HMG-CoA synthase) catalyzes the condensation of acetyl CoA with acetoacetyl CoA to produce HMG-CoA. There are two forms of this enzyme, cytosolic and mitochondrial. The cytosolic form is ubiquitous in the body and is involved in cholesterol biosynthesis and synthesis of other isoprenoid products. The mitochondrial form, found solely in the liver and kidney, is involved in the ketogenic pathway.

Evidence446
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8626466
comment: Mevalonate pyrophosphate decarboxylase (MPD) decarboxylates mevalonate-5-pyrophosphate into isopentenyl pyrophosphate while hydrolysing ATP to ADP and orthophosphate.

http://identifiers.org/pubmed/9536209
type: PublicationXref
id: 9536209
author: Clarke, D
author: Cunningham, SK
author: Fearon, U
author: McKenna, TJ
db: Pubmed
title: A critical review of the origin and control of adrenal androgens
source: Baillieres Clin Obstet Gynaecol 11:229-48
year: 1997

Evidence445
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1377680
xref: http://identifiers.org/pubmed/11111075
xref: http://identifiers.org/pubmed/14730012
comment: Mevalonate kinase (MK) catalyzes the phosphorylation of mevalonate to mevalonate-5-phosphate.

Evidence440
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9166898
xref: http://identifiers.org/pubmed/10468558
comment: Peroxisomal HACL1 catalyzes the reaction of 2-hydroxyphytanoyl-CoA to form pristanal and formyl-CoA. The active form of the enzyme is a homotetramer, with one Mg++ and one molecule of thiamin pyrophosphate bound to each monomer (Croes et al. 1997; Foulon et al. 1999).

Evidence442
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16756494
comment: In humans, the catabolism of phytanate, pristanate, and very long chain fatty acids as well as the first four steps of the biosynthesis of plasmalogens are catalyzed by peroxisomal enzymes. Defects in any of these enzymes or in the assembly of peroxisomes are associated with severe developmental disorders (Wanders and Watherham 2006).

Evidence441
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12633678
xref: http://identifiers.org/pubmed/4177872
comment: Phytanic acid arises through ruminant metabolism of chlorophyll and enters the human diet as a constituent of dairy products (Baxter 1968). It can act as an agonist for PPAR and other nuclear hormone receptors, but its normal role in human physiology, if any, is unclear. It is catabolized via a five-step alpha-oxidation reaction sequence that yields pristanoyl-CoA, which is turn is a substrate for beta-oxidation. These reactions take place in the peroxisomal matrix and their failure is associated with Refsum disease (Wanders et al. 2003).

Evidence439
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: The reactions involved in the metabolism of fatty acids and of the triacylglycerols and ketone bodies derived from them form a closely interrelated, coordinately regulated module that plays a central role in human energy metabolism.

Evidence438
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18288277
xref: http://identifiers.org/pubmed/16476485
xref: http://identifiers.org/pubmed/10529898
xref: http://identifiers.org/pubmed/16503871
comment: Peroxisome proliferator-activated receptor alpha (PPAR-alpha) is the major regulator of fatty acid oxidation in the liver. PPARalpha is also the target of fibrate drugs used to treat abnormal plasma lipid levels. PPAR-alpha is a type II nuclear receptor (its subcellular location does not depend on ligand binding). PPAR-alpha forms heterodimers with Retinoid X receptor alpha (RXR-alpha), another type II nuclear receptor. PPAR-alpha is activated by binding fatty acid ligands, especially polyunsaturated fatty acids having 18-22 carbon groups and 2-6 double bonds. The PPAR-alpha:RXR-alpha heterodimer binds peroxisome proliferator receptor elements (PPREs) in and around target genes. Binding of fatty acids and synthetic ligands causes a conformational change in PPAR-alpha such that it releases the corepressors and binds coactivators (CBP-SRC-HAT complex, ASC complex, and TRAP-Mediator complex) which initiate transcription of the target genes. Target genes of PPAR-alpha participate in fatty acid transport, fatty acid oxidation, triglyceride clearance, lipoprotein production, and cholesterol homeostasis.

Evidence437
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/20936127
xref: http://identifiers.org/pubmed/14999402
xref: http://identifiers.org/pubmed/18288277
xref: http://identifiers.org/pubmed/10529898
xref: http://identifiers.org/pubmed/11330046
comment: The set of genes regulated by PPAR-alpha is not fully known in humans, however many examples have been found in mice. Genes directly activated by PPAR-alpha contain peroxisome proliferator receptor elements (PPREs) in their promoters and include: 1) genes involved in fatty acid oxidation and ketogenesis (Acox1, Cyp4a, Acadm, Hmgcs2); 2) genes involved in fatty acid transport (Cd36, , Slc27a1, Fabp1, Cpt1a, Cpt2); 3) genes involved in producing fatty acids and very low density lipoproteins (Me1, Scd1); 4) genes encoding apolipoproteins (Apoa1, Apoa2, Apoa5); 5) genes involved in triglyceride clearance ( Angptl4); 6) genes involved in glycerol metabolism (Gpd1 in mouse); 7) genes involved in glucose metabolism (Pdk4); 8) genes involved in peroxisome proliferation (Pex11a); 9) genes involved in lipid storage (Plin, Adfp). Many other genes are known to be regulated by PPAR-alpha but whether their regulation is direct or indirect remains to be found. These genes include: ACACA, FAS, SREBP1, FADS1, DGAT1, ABCA1, PLTP, ABCB4, UGT2B4, SULT2A1, Pnpla2, Acsl1, Slc27a4, many Acot genes, and others (reviewed in Rakhshandehroo et al. 2010).

Evidence436
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/20110263
comment: The TIAM2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.

Evidence431
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8647822
comment: The HMGCR gene is transcribed to yield mRNA and the mRNA is translated to yield protein.

Evidence430
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref711
xref: http://identifiers.org/pubmed/8687421
xref: http://identifiers.org/pubmed/7821823
xref: http://identifiers.org/pubmed/8163052
comment: FAD-linked mitochondrial glycerol 3-phosphate dehydrogenase (GPD2, alias: mGPDH) and its NAD-linked cytosolic isoform (GPD1, alias:cGPDH) constitute glycerol phosphate shuttle. GPD2 catalyzes the unidirectional conversion of glycerol-3-phosphate (G-3-P) to dihydroxyacetone phosphate (DHAP) with concomitant reduction of the enzyme-bound FAD. Impaired activity of GPD2 has been suggested to be one of the primary causes of insulin secretory defects in beta-cells and thus it is a candidate gene for type 2 diabetes.

Evidence435
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/20110263
comment: The RGL1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.

Evidence434
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19710929
comment: The PEX11A gene is transcribed to yield mRNA and the mRNA is translated to yield protein.

Evidence433
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19710929
comment: The HMGCS2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.

http://identifiers.org/pubmed/15189156
type: PublicationXref
id: 15189156
author: Lorsch, JR
author: Kapp, LD
db: Pubmed
title: The molecular mechanics of eukaryotic translation
source: Annu Rev Biochem 73:657-704
year: 2004

Evidence432
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19088433
xref: http://identifiers.org/pubmed/12177166
comment: The HMGCS1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.

Evidence426
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/21479626
comment: In a healthy, well-nourished individual, the production of ketone bodies occurs at a relatively low rate. During periods of normal physiological responses to carbohydrate shortages, the liver increases the production of ketone bodies from acetyl-CoA generated from fatty acid oxidation. This allows heart and skeletal muscle to use ketone bodies as the primary source of energy, thereby preserving the limited glucose supply for use in brain tissue. In untreated diabetes mellitus, a huge buildup of ketone bodies occurs due to an increase in fatty acid oxidation. The production of ketone bodies exceeds the ability of peripheral tissues to oxidize them, and results in lowering the pH of blood. Blood acidification is dangerous, chiefly as it impairs the ability of hemoglobin to bind oxygen. Ketone body synthesis proceeds via the synthesis of ccetoacetic acid in three steps from acetyl CoA, followed by the reduction of acetoacetic acid to beta-hydroxybutyrate. In the body, these reactions occur in the mitochondria of liver cells (Sass 2011).

UnificationXref6799
type: UnificationXref
id: REACT_162207
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_162207.2

Evidence425
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11479731
comment: Hydroxymethylglutaryl-CoA synthase tetramer (HMGCS2) in the mitochondrial matrix catalyzes the reaction of acetoacetyl-CoA and acetyl-CoA to form beta-hydroxy-beta-methylglutaryl coenzyme A (HMG CoA) and CoA (Aledo et al. 2001).

UnificationXref6798
type: UnificationXref
id: 3664677
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664677

Evidence428
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/21479626
comment: The levels of acetone in ketone bodies are much lower than those of acetoacetic acid and beta-hydroxybutyric acid. Acetone cannot be converted back to acetyl-CoA, and is excreted in urine, or breathed out through the lungs. Extrahepatic tissues utilize ketone bodies by converting the beta-hydroxybutyrate successively to acetoacetate, acetoacetatyl-CoA, finally to acetyl-CoA (Sass 2011).

Evidence427
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3709573
comment: Acetyl-CoA acetyltransferase tetramer (ACAT1) in the mitochondrial matrix catalyzes the reversible reaction of acetoacetyl-CoA and CoA to form two molecules of acetyl-CoA (Middleton et al. 1986).

Evidence429
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/21479626
comment: Acetoacetate, beta-hydroxybutyrate, and acetone collectively are called ketone bodies. The first two are synthesized from acetyl-CoA, in the mitochondria of liver cells; acetone is formed by spontaneous decarboxylation of acetoacetate. Ketone body synthesis in liver is effectively irreversible because the enzyme that catalyzes the conversion of acetoacetate to acetoacetyl-CoA is not present in liver cells. Ketone bodies, unlike fatty acids and triglycerides, are water-soluble. They are exported from the liver, and are taken up by other tissues, notably brain and skeletal and cardiac muscle. There, they are broken down to acetyl-CoA which is oxidized via the TCA cycle to yield energy. In a normal person, this pathway of ketone body synthesis and utilization is most active during extended periods of fasting. Under these conditions, mobilization and breakdown of stored fatty acids generates abundant acetyl-CoA acetyl-CoA in liver cells for synthesis of ketone bodies, and their utilization in other tissues minimizes the demand of these tissues for glucose (Sass 2011).

UnificationXref6791
type: UnificationXref
id: 3664667
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664667

UnificationXref6790
type: UnificationXref
id: 3664666
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664666

Evidence420
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18694939
xref: http://identifiers.org/pubmed/17158099
comment: Lipin proteins LPIN1, 2, and 3, associated with the endoplasmic reticulum membrane, can each catalyze the hydrolysis of phosphatidate to yield 1,2-diacyl-glycerol and orthophosphate. The activities of LPIN1 and LPIN2 have been established experimentally (Grimsey et al. 2008); that of LPIN3 is inferred from its structural similarities both to its human paralogues and to its mouse ortholog (Donkor et al. 2007). Only LPIN1 has been shown to be stably associated with the endoplasmic reticulum, but all three enzymes appear to be catalytically active at that location (Grimsey et al. 2008; Donkor et al. 2007).

UnificationXref6793
type: UnificationXref
id: REACT_163281
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_163281.2

UnificationXref6792
type: UnificationXref
id: 3664678
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664678

Evidence422
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17223360
xref: http://identifiers.org/pubmed/10677481
xref: http://identifiers.org/pubmed/9099716
comment: Cytosolic acetyl-CoA carboxylase 1 (ACACA) catalyzes the reaction of bicarbonate, ATP, and acetyl-CoA to form malonyl-CoA, ADP, and orthophosphate. The reaction is positively regulated by citrate. The human ACACA cDNA has been cloned (Abu-Elheiga et al. 1995) and the biochemical properties of the human enzyme have recently been described (Cheng et al. 2007; Locke et al. 2008). Four ACACA isoforms generated by alternative splicing have been identified as mRNAs - the protein product of the first has been characterized experimentally.

UnificationXref6795
type: UnificationXref
id: 3664673
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664673

Evidence421
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8944226
comment: The overall process of triglyceride (triacylglycerol) biosynthesis consists of four biochemical pathways: fatty acyl-CoA biosynthesis, conversion of fatty acyl-CoA to phosphatidic acid, conversion of phosphatidic acid to diacylglycerol, and conversion fo diacylglycerol to triacylglycerol.

UnificationXref6794
type: UnificationXref
id: 3664670
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664670

Evidence424
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3709573
comment: Acetyl-CoA acetyltransferase tetramer (ACAT1) in the mitochondrial matrix catalyzes the reversible reaction of two molecules of acetyl-CoA to form acetoacetyl-CoA and CoA (Middleton et al. 1986).

UnificationXref6797
type: UnificationXref
id: 3664675
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664675

Evidence423
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11257506
xref: http://identifiers.org/pubmed/10856709
comment: The mitochondrial carnitine system catalyzes the transport of long-chain fatty acids into the mitochondrial matrix where they undergo beta oxidation. This transport system consists of the malonyl-CoA sensitive carnitine palmitoyltransferase I (CPT-I) localized in the mitochondrial outer membrane, the carnitine:acylcarnitine translocase, an integral inner membrane protein, and carnitine palmitoyltransferase II localized on the matrix side of the inner membrane. (Kerner and Hoppel, 2000).

UnificationXref6796
type: UnificationXref
id: 3664674
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664674

ARFGAP1
type: Protein
entity reference: O94601
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: O94601
xref: UnificationXref8546
feature: FragmentFeature1310
cellular location: GO:0005829
comment: Reactome DB_ID: 3661728
display name: GAP

UnificationXref6785
type: UnificationXref
id: 3662889
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662889

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94625
data source: Provenance1
name: DNAJB11
name: O94625
name: ERdj3
xref: UnificationXref8540
feature: FragmentFeature1309
cellular location: GO:0005788
comment: Reactome DB_ID: 3664378
display name: HEDJ

UnificationXref6786
type: UnificationXref
id: 3662890
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662890

Evidence498
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/14702039
comment: In the cytosol, glycerophosphocholine phosphodiesterase (GPCPD1, also known as GDE5) hydrolyzes glycerophosphocholine (GPCho) to produce choline (Cho) and glycerol-3-phosphate (G3P). This event has been inferred from mice. GPCPD1 has also been characterized in humans (Ota et al. 2004).

UnificationXref6783
type: UnificationXref
id: O36027
db: UniProt

Evidence499
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19501189
xref: http://identifiers.org/pubmed/20705608
xref: http://identifiers.org/pubmed/15944408
comment: Lysophosphatidylcholine (LPC) is hydrolyzed by phospholipases to produce glycerophosphocholine (GPCho) which is in turn hydrolyzed by glycerophosphocholine phosphodiesterase to produce choline (Cho) and glycerol-3-phosphate (G3P) (Yamashita et al. 2009, Yamashita et al. 2005, Ghomashchi et al. 2010).

UnificationXref6784
type: UnificationXref
id: 3662888
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662888

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94270
data source: Provenance1
name: ERD23_HUMAN
name: ER lumen protein retaining receptor 3
name: O94270
xref: UnificationXref8564
feature: FragmentFeature1314
cellular location: GO:0005789
comment: Reactome DB_ID: 3664406
display name: KDELR3

Evidence496
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16864775
xref: http://identifiers.org/pubmed/18195019
xref: http://identifiers.org/pubmed/18772128
xref: http://identifiers.org/pubmed/18458083
xref: http://identifiers.org/pubmed/16243729
xref: http://identifiers.org/pubmed/16704971
xref: http://identifiers.org/pubmed/17182612
comment: At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferases acylate 2-acyl lysophosphatidylcholine (LPC) to form phosphatidylcholine (PC). The lysophospholipid acyltransferases involved are: lysophosphatidylcholine acyltransferase 1 (LPCAT1) (Nakanishi et al. 2006, Chen et al. 2006); lysophosphatidylcholine acyltransferase 2 (LPCAT2) (Shindou et al. 2006); lysophospholipid acyltransferase 5 (LPCAT3) (Hishikawa et al. 2008, Zhao et al. 2008, Gijon et al. 2008, Jain et al. 2009, Kazachkov et al. 2008); lysophospholipid acyltransferase LPCAT4 (LPCAT4) aka LPEAT2 (Cao et al. 2008, Ye et al. 2005); or lysophospholipid acyltransferase 2 (MBOAT2) aka LPCAT4 (Hishikawa et al. 2008, Gijon et al. 2008).

UnificationXref6781
type: UnificationXref
id: 3664665
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664665

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10061
data source: Provenance1
name: HYOU1_HUMAN
name: Hypoxia up-regulated protein 1
name: Q10061
xref: UnificationXref8560
feature: FragmentFeature1313
cellular location: GO:0005788
comment: Reactome DB_ID: 3664373
display name: HYOU1

Evidence497
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18195019
xref: http://identifiers.org/pubmed/12359733
xref: http://identifiers.org/pubmed/18458083
xref: http://identifiers.org/pubmed/20705608
comment: In the acyl chain remodelling pathway (Lands cycle), phosphatidylcholine (PC) is hydrolysed by phopholipases and subsequently reacylated by acyltransferases. These cycles modify the fatty acid composition of glycerophospholipids to generate diverse molecules asymmetrically distributed in the cell membrane (Ghomashchi et al. 2010, Singer et al. 2002, Cao et al. 2008, Zhao et al. 2008).

UnificationXref6782
type: UnificationXref
id: REACT_163280
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_163280.2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10452
data source: Provenance1
name: Q10452
name: Glycogen synthase kinase-3 alpha
name: KG3A_HUMAN
name: GSK3A(1-483)
xref: UnificationXref8556
feature: FragmentFeature1312
cellular location: GO:0005829
comment: Reactome DB_ID: 3661663
display name: GSK3A

Evidence494
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12216837
xref: http://identifiers.org/pubmed/12221122
comment: De novo (Kennedy pathway) synthesis of phosphatidylcholine (PC) involves phosphorylation of choline (Cho) to phosphocholine (PCho) followed by condensing with cytidine triphosphate (CTP) to form CDP-choline (CDP-Cho). Diacylglycerol (DAG) and CDP-ETA together then form PC. Alternatively, PC is formed when phosphatidylethanolamine (PE) is methylated by phosphatidylethanolamine N-methyltransferase (PEMT) (Henneberry et al. 2002; Wright & McMaster 2002).

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9P7G5
data source: Provenance1
name: Golgi SNAP receptor complex member 2
name: Q9P7G5
name: GOSR2_HUMAN
xref: UnificationXref8552
feature: FragmentFeature1311
cellular location: GO:0000139
comment: Reactome DB_ID: 3664429
display name: GOSR2

Evidence495
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16864775
xref: http://identifiers.org/pubmed/18195019
xref: http://identifiers.org/pubmed/18772128
xref: http://identifiers.org/pubmed/18458083
xref: http://identifiers.org/pubmed/16243729
xref: http://identifiers.org/pubmed/16704971
xref: http://identifiers.org/pubmed/17182612
comment: At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferases acylate 1-acyl lysophosphatidylcholine (LPC) to form phosphatidylcholine (PC). The lysophospholipid acyltransferases involved are: lysophosphatidylcholine acyltransferase 1 (LPCAT1) (Nakanishi et al. 2006, Chen et al. 2006); lysophosphatidylcholine acyltransferase 2 (LPCAT2) (Shindou et al. 2006); lysophospholipid acyltransferase 5 (LPCAT3) (Hishikawa et al. 2008, Zhao et al. 2008, Gijon et al. 2008, Jain et al. 2009, Kazachkov et al. 2008); lysophospholipid acyltransferase LPCAT4 (LPCAT4) aka LPEAT2 (Cao et al. 2008, Ye et al. 2005); or lysophospholipid acyltransferase 2 (MBOAT2) aka LPCAT4 (Hishikawa et al. 2008, Gijon et al. 2008).

UnificationXref6780
type: UnificationXref
id: 3662473
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662473

UnificationXref6789
type: UnificationXref
id: REACT_161704
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_161704.2

Molybdenum cofactor biosynthesis
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction419
evidence: Evidence720
xref: RelationshipXref603
xref: UnificationXref4753
xref: UnificationXref4754
pathway order: PathwayStep710
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UnificationXref6787
type: UnificationXref
id: 3662891
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662891

UnificationXref6788
type: UnificationXref
id: 3662892
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662892

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P78759
data source: Provenance1
name: 2A5B_HUMAN
name: PPP2R5B
name: Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform
xref: UnificationXref8570
feature: FragmentFeature1316
cellular location: GO:0005829
comment: Reactome DB_ID: 3664394
display name: P78759

E3 ubiquitin-protein ligase synoviolin
type: Protein
entity reference: O74757
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: O74757
name: SYVN1_HUMAN
name: SYVN1(1-617)
xref: UnificationXref8579
feature: FragmentFeature1317
cellular location: GO:0005789
comment: Reactome DB_ID: 3664384
display name: SYVN1

Homologues of PPP2R5B
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref8571
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3664395

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q10428
data source: Provenance1
name: 2A5B_HUMAN
name: PPP2R5B
name: Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform
xref: UnificationXref8568
feature: FragmentFeature1315
cellular location: GO:0005829
comment: Reactome DB_ID: 3664390
display name: Q10428

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9HDZ7
data source: Provenance1
name: Q9HDZ7
name: WIPI1_HUMAN
name: WD repeat domain phosphoinositide-interacting protein 1
xref: UnificationXref8585
feature: FragmentFeature1318
cellular location: GO:0000139
comment: Reactome DB_ID: 3664445
display name: WIPI1

Evidence487
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18195019
xref: http://identifiers.org/pubmed/18772128
xref: http://identifiers.org/pubmed/18287005
xref: http://identifiers.org/pubmed/18781350
xref: http://identifiers.org/pubmed/19351971
xref: http://identifiers.org/pubmed/18458083
comment: At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferases acylate 1-acyl lysophosphatidylethanolamine (LPE) to form phosphatidylethanolamine (PE). The lysophospholipid acyltransferases involved are: lysophospholipid acyltransferase 1 (MBOAT1) aka LPEAT1 (Gijon et al. 2008, Hishikawa et al. 2008); lysophospholipid acyltransferase LPCAT4 (LPCAT4) aka LPEAT2 (Cao et al. 2008, Ye et al., 2005); lysophospholipid acyltransferase 2 (MBOAT2) aka LPCAT4 (Hishikawa et al. 2008, Gijon et al. 2008); lysophospholipid acyltransferase 5 (LPCAT3) (Hishikawa et al. 2008, Zhao et al. 2008, Gijon et al. 2008, Jain et al. 2009, Kazachkov et al. 2008).

UnificationXref6772
type: UnificationXref
id: 3664615
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664615

Evidence488
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18195019
xref: http://identifiers.org/pubmed/18772128
xref: http://identifiers.org/pubmed/18287005
xref: http://identifiers.org/pubmed/18781350
xref: http://identifiers.org/pubmed/19351971
xref: http://identifiers.org/pubmed/18458083
comment: At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferases acylate 2-acyl lysophosphatidylethanolamine (LPE) to form phosphatidylethanolamine (PE). The lysophospholipid acyltransferases involved are: lysophospholipid acyltransferase 1 (MBOAT1) aka LPEAT1 (Gijon et al. 2008, Hishikawa et al. 2008); lysophospholipid acyltransferase LPCAT4 (LPCAT4) aka LPEAT2 (Cao et al. 2008, Ye et al. 2005); lysophospholipid acyltransferase 2 (MBOAT2) aka LPCAT4 (Hishikawa et al. 2008, Gijon et al. 2008); lysophospholipid acyltransferase 5 (LPCAT3) (Hishikawa et al. 2008, Zhao et al. 2008, Gijon et al. 2008, Jain et al. 2009, Kazachkov et al. 2008).

UnificationXref6773
type: UnificationXref
id: 3664616
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664616

http://identifiers.org/pubmed/20060739
type: PublicationXref
id: 20060739
author: Sheftel, Alex
author: Stehling, Oliver
author: Lill, R
db: Pubmed
title: Iron-sulfur proteins in health and disease
source: Trends Endocrinol. Metab. 21:302-14
year: 2010

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9HGM9
data source: Provenance1
name: p58IPK
name: Q9HGM9
xref: UnificationXref8593
feature: FragmentFeature1320
cellular location: GO:0005788
comment: Reactome DB_ID: 3664435
display name: DNAJC3

Evidence489
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18195019
xref: http://identifiers.org/pubmed/12359733
xref: http://identifiers.org/pubmed/18287005
xref: http://identifiers.org/pubmed/18458083
xref: http://identifiers.org/pubmed/20705608
comment: In the acyl chain remodelling pathway (Lands cycle), phosphatidylethanolamine (PE) is hydrolyzed by phopholipases and subsequently reacylated by acyltransferases. These cycles modify the fatty acid composition of glycerophospholipids to generate diverse molecules asymmetrically distributed in the cell membrane (Ghomashchi et al. 2010, Singer et al. 2002, Cao et al. 2008, Zhao et al. 2008, Hishikawa et al. 2008).

UnificationXref6774
type: UnificationXref
id: 3664617
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664617

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P87148
data source: Provenance1
name: Protein YIF1A
name: YIF1A(1-293)
name: YIF1A_HUMAN
name: P87148
xref: UnificationXref8589
feature: FragmentFeature1319
cellular location: GO:0005789
comment: Reactome DB_ID: 3664422
display name: YIF1A

UnificationXref6775
type: UnificationXref
id: 3664618
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664618

O13351
type: Protein
entity reference: O13351
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: SUMO1_HUMAN
name: Small ubiquitin-related modifier 1
xref: UnificationXref8612
feature: FragmentFeature1322
cellular location: GO:0005654
comment: Reactome DB_ID: 3664940
display name: SUMO1

Evidence483
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18583706
xref: http://identifiers.org/pubmed/9083101
comment: At the endoplasmic reticulum (ER) membrane, active membrane-bound ethanolamine-phosphate cytidylyltransferase (PCY2) dimer condenses phosphoethanolamine (PETA) and cytidine triphosphate (CTP) to produce CDP-ethanolamine (CDP-ETA) (Zhu et al. 2008, Nakashima et al. 1997).

O13351
type: Protein
entity reference: O13351
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: proSUMO1
name: SUMO1(2-101)
name: SUMO1_HUMAN
name: Small ubiquitin-related modifier 1
xref: UnificationXref8611
feature: FragmentFeature1321
cellular location: GO:0005654
comment: Reactome DB_ID: 3664946
display name: SUMO1

Evidence484
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18694939
xref: http://identifiers.org/pubmed/17158099
comment: At the endoplasmic reticulum (ER) membrane, phosphatidate phosphatase 1-3 (LPIN) dephosphorylates phosphatidic acid (PA) to form diacylglycerol (DAG) (Grimsey et al. 2008, Donkor et al. 2007).

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:O42957
data source: Provenance1
name: Sentrin-specific protease 1 ecNumber3.4.22.68/ecNumber
name: O42957
name: SENP1_HUMAN
xref: UnificationXref8614
feature: FragmentFeature1323
cellular location: GO:0005654
comment: Reactome DB_ID: 3664950
display name: SENP1

Evidence485
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17478478
comment: At the inner mitochondrial (IM) membrane, phosphatidylserine decarboxylase proenzyme (heterodimer of two chains from the same protein) (PISD) decarboxylates phosphatidylserine (PS) to phosphatidylethanolamine (PE). This event has been inferred from rats and limited data for a human PISD (Forbes et al. 2007).

UnificationXref6770
type: UnificationXref
id: 3664599
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664599

SENP1/2/5
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref8616
cellular location: GO:0005654
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3664952

Evidence486
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/2332429
xref: http://identifiers.org/pubmed/1898727
xref: http://identifiers.org/pubmed/12221122
comment: De novo (Kennedy pathway) synthesis of phosphatidylethanolamine (PE) involves phosphorylation of ethanolamine (ETA) to phosphoethanolamine (PETA) followed by condensing with cytidine triphosphate (CTP) to form CDP-ethanolamine (CDP-ETA). Diacylglycerol (DAG) and CDP-ETA together then form PE. Alternatively, PE is formed when phosphatidylserine (PS) is decarboxylated by phosphatidylserine decarboxylase proenzyme (PISD) (Henneberry et al. 2002, Vance 1991, Vance 1990).

UnificationXref6771
type: UnificationXref
id: 3664601
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664601

UnificationXref6776
type: UnificationXref
id: 3664620
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664620

UnificationXref6777
type: UnificationXref
id: REACT_166353
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_166353.1

UnificationXref6778
type: UnificationXref
id: 3665595
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665595

UnificationXref6779
type: UnificationXref
id: REACT_166877
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_166877.1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:O42957
data source: Provenance1
name: SENP2_HUMAN
name: O42957
name: Sentrin-specific protease 2 ecNumber3.4.22.68/ecNumber
xref: UnificationXref8615
feature: FragmentFeature1324
cellular location: GO:0005654
comment: Reactome DB_ID: 3664951
display name: SENP2

Evidence491
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19501189
xref: http://identifiers.org/pubmed/15944408
comment: Lysophosphatidylethanolamine (LPE) is hydrolyzed by phospholipases to produce glycerophosphoethanolamine (GPETA) which is in turn hydrolyzed by glycerophosphocholine phosphodiesterase to produce ethanolamine (ETA) and glycerol-3-phosphate (G3P) (Yamashita et al. 2009, Yamashita et al. 2005).

Small ubiquitin-related modifier 2
type: Protein
entity reference: O13351
data source: Provenance1
name: O13351
name: Note: the coordinates are copied over from Homo sapiens.
name: proSUMO2
name: SUMO2_HUMAN
name: SUMO2(1-95)
xref: UnificationXref8619
feature: FragmentFeature1325
cellular location: GO:0005654
comment: Reactome DB_ID: 3664955
display name: SUMO2

Evidence490
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/14702039
comment: In the cytosol, glycerophosphocholine phosphodiesterase (GPCPD1, also known as GDE5) hydrolyzes glycerophosphoethanolamine (GPETA) to produce ethanolamine (ETA) and glycerol-3-phosphate (G3P). This event has been inferred from mice. GPCPD1 has also been characterized in humans (Ota et al. 2004).

Small ubiquitin-related modifier 2
type: Protein
entity reference: O13351
data source: Provenance1
name: O13351
name: Note: the coordinates are copied over from Homo sapiens.
name: SUMO2_HUMAN
xref: UnificationXref8620
feature: FragmentFeature1326
cellular location: GO:0005654
comment: Reactome DB_ID: 3664956
display name: SUMO2

Evidence493
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9593753
comment: At the endoplasmic reticulum (ER) membrane, active membrane-bound choline-phosphate cytidylyltransferase A (PCYT1A) or B (PCYT1B) homodimer condenses phosphocholine (PCho) and cytidine triphosphate (CTP) to produce CDP-choline (CDP-Cho) (Lykidis et al. 1998).

Evidence492
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10100195
xref: http://identifiers.org/pubmed/11420179
xref: http://identifiers.org/pubmed/3057511
comment: At the endoplasmic reticulum (ER) membrane, phosphatidylethanolamine N-methyltransferase (PEMT) methylates phosphatidylethanolamine (PE) and produces phosphatidylcholine (PC) (Vance & Ridgway 1998, Shields et al. 2001, Guan et al. 1999).

Homologues of SH3GL2
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref8667
cellular location: GO:0005886
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3661160

Evidence474
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9536209
xref: http://identifiers.org/pubmed/9208814
xref: http://identifiers.org/pubmed/2339109
xref: http://identifiers.org/pubmed/17986282
xref: http://identifiers.org/pubmed/1944596
comment: The conversion of testosterone to the most potent androgen, 5-alpha-dihydrotestosterone (DHT), is catalyzed by the microsomal 5alpha-steroid reductase enzymes, of which there are three reported types in humans to date (SRD5A1-3) (Andersson S and Russell DW, 1990; Andersson S et al, 1991; Uemura M et al, 2008 respectively). These enzymes are expressed in the prostate and other androgen target sites. Defects in SRD5A2 are the cause of pseudovaginal perineoscrotal hypospadias, also known as male pseudohermaphroditism (Anwar R et al, 1997). Corticotropin (Adrenocorticotropic hormone, ACTH) acts through the ACTH receptor called melanocortin receptor type 2 (MC2R) to stimulate steroidogenesis, increasing the production of androgens (McKenna et al, 1997).

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P40984
data source: Provenance1
name: SUMO-conjugating enzyme UBC9
name: SUMO3 S-glycyl-cys93 UBE2I
name: SUMO3-C93-UBE2I
name: UBC9_HUMAN
xref: UnificationXref8649
feature: FragmentFeature1333
feature: ModificationFeature214
cellular location: GO:0005654
comment: Reactome DB_ID: 3664966
display name: P40984

Evidence475
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12428201
comment: Androgens are the determining factors for male development and behaviour in vertebrates (Miller 2002).

UnificationXref6760
type: UnificationXref
id: 3664609
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664609

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P40984
data source: Provenance1
name: P40984
name: SUMO-conjugating enzyme UBC9
name: UBC9_HUMAN
name: UBE2I (UBC9)
xref: UnificationXref8648
feature: FragmentFeature1332
cellular location: GO:0005654
comment: Reactome DB_ID: 3664964
display name: UBE2I

Evidence472
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11969205
xref: http://identifiers.org/pubmed/12543708
comment: In a healthy adult human, about 500 mg of cholesterol is converted to bile salts daily (Russell 2003). The major pathway for bile salt synthesis in the liver begins with the conversion of cholesterol to 7alpha-hydroxycholesterol. Bile salt synthesis can also begin with the synthesis of an oxysterol - 24-hydroxycholesterol or 27-hydroxycholesterol. In the body, the initial steps of these two pathways occur in extrahepatic tissues, generating intermediates that are transported to the liver and converted to bile salts via the 7alpha-hydroxycholesterol pathway. These extrahepatic pathways contribute little to the total synthesis of bile salts, but are thought to play important roles in cholesterol homeostasis (Javitt 2002).

SUMO1-C173-UBA2
type: Protein
entity reference: UniProt:O42939
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: SAE2_HUMAN
name: SUMO-activating enzyme subunit 2
name: SUMO1 S-glycyl-cys173 UBA2
xref: UnificationXref8635
feature: ModificationFeature213
feature: FragmentFeature1331
cellular location: GO:0005654
comment: Reactome DB_ID: 3664942
display name: O42939

Evidence473
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/14699511
xref: http://identifiers.org/pubmed/12663868
xref: http://identifiers.org/pubmed/11969205
xref: http://identifiers.org/pubmed/12543708
comment: In a healthy adult human, about 500 mg of cholesterol is converted to bile salts daily. Newly synthesized bile salts are secreted into the bile and released into the small intestine where they emulsify dietary fats (Russell 2003). About 95% of the bile salts in the intestine are recovered and returned to the liver (Kullak-Ublick et al. 2004; Trauner and Boyer 2002). The major pathway for bile salt synthesis in the liver begins with the conversion of cholesterol to 7alpha-hydroxycholesterol. Bile salt synthesis can also begin with the synthesis of an oxysterol - 24-hydroxycholesterol or 27-hydroxycholesterol. In the body, the initial steps of these two pathways occur in extrahepatic tissues, generating intermediates that are transported to the liver and converted to bile salts via the 7alpha-hydroxycholesterol pathway. These extrahepatic pathways contribute little to the total synthesis of bile salts, but are thought to play important roles in extrahepatic cholesterol homeostasis (Javitt 2002).

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P79064
data source: Provenance1
name: P79064
name: SUMO-activating enzyme subunit 1
name: SAE1_HUMAN
xref: UnificationXref8632
feature: FragmentFeature1330
cellular location: GO:0005654
comment: Reactome DB_ID: 3664931
display name: SAE1

Evidence478
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15583024
comment: Steroid hormones are synthesized primarily in the adrenal gland and gonads. They regulate energy metabolism and stress responses (glucocorticoids), salt balance (mineralocorticoids), and sexual development and function (androgens and estrogens). All steroids are synthesized from cholesterol. Steroid hormone synthesis is largely regulated at the initial steps of cholesterol mobilization and transport into the mitochondrial matrix for conversion to pregnenolone. In the body, the fate of pregnenolone is tissue-specific: in the zona fasciculata of the adrenal cortex it is converted to cortisol, in the zona glomerulosa to aldosterone, and in the gonads to testosterone and then to estrone and estradiol. These pathways are outlined in the figure below, which also details the sites on the cholesterol molecule that undergo modification in the course of these reactions. Vitamin D3 (cholecalciferol) is a steroid hormone that plays a role in regulating calcium and bone metabolism. The processes by which it is synthesized, modified, and transported in the body are annotated here.

UnificationXref6763
type: UnificationXref
id: 3664603
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664603

O42939
type: Protein
entity reference: UniProt:O42939
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: SAE2_HUMAN
name: SUMO-activating enzyme subunit 2
xref: UnificationXref8630
feature: FragmentFeature1329
cellular location: GO:0005654
comment: Reactome DB_ID: 3664935
display name: UBA2

Evidence479
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8530346
xref: http://identifiers.org/pubmed/9582313
comment: Phosphatidylcholine (PC) is hydrolyzed to phosphatidic acid (PA) and choline (Cho) by the enzymes phospholipase D1/2 (PLD1/2), at the endoplasmic reticulum (ER) membrane (Lopez et al. 1998, Hammond et al. 1995).

UnificationXref6764
type: UnificationXref
id: 3664605
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664605

http://identifiers.org/pubmed/9202389
type: PublicationXref
id: 9202389
author: Compton, DA
author: Howard, L
author: Saredi, A
db: Pubmed
title: Phosphorylation regulates the assembly of NuMA in a mammalian mitotic extract
source: J Cell Sci 110:1287-97
year: 1997

O13351
type: Protein
entity reference: O13351
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Small ubiquitin-related modifier 3
name: SUMO3_HUMAN
xref: UnificationXref8624
feature: FragmentFeature1328
cellular location: GO:0005654
comment: Reactome DB_ID: 3664959
display name: SUMO3

Evidence476
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19027824
comment: Expression of HSD17B1 which is the main enzyme that catalyzes the hydrogenation of estrone is strongly restricted to placenta, ovaries, endometrium and breast tissue (Moeller and Adamski, 2009).

UnificationXref6761
type: UnificationXref
id: 3664608
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664608

O13351
type: Protein
entity reference: O13351
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Small ubiquitin-related modifier 3
name: proSUMO3
name: SUMO3_HUMAN
name: SUMO3(1-103)
xref: UnificationXref8623
feature: FragmentFeature1327
cellular location: GO:0005654
comment: Reactome DB_ID: 3664958
display name: SUMO3

Evidence477
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15583024
comment: In female vertebrates, estrogens control reproductive system development and reproductive functions (Payne AH and Hales DB, 2004).

UnificationXref6762
type: UnificationXref
id: 3664610
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664610

Catalysis12
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction23
control type: ACTIVATION
xref: RelationshipXref14
xref: RelationshipXref10
controller: Pol eta:lesioned DNA template inserted with correct base complement (name copied from entity in Homo sapiens)

UnificationXref6767
type: UnificationXref
id: 3664602
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664602

Catalysis13
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction26
control type: ACTIVATION
xref: RelationshipXref10
xref: RelationshipXref15
controller: Pol zeta:damaged DNA template complex (name copied from entity in Homo sapiens)

UnificationXref6768
type: UnificationXref
id: 3664604
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664604

Catalysis10
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction20
control type: ACTIVATION
xref: RelationshipXref10
xref: RelationshipXref12
controller: REV1:lesioned DNA template with misinserted bases (name copied from entity in Homo sapiens)

UnificationXref6765
type: UnificationXref
id: 3664600
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664600

Catalysis11
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction22
control type: ACTIVATION
xref: RelationshipXref10
xref: RelationshipXref13
controller: Pol eta:damaged DNA template complex (name copied from entity in Homo sapiens)

UnificationXref6766
type: UnificationXref
id: 3664607
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664607

UnificationXref6769
type: UnificationXref
id: 3664598
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664598

Catalysis19
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction42
control type: ACTIVATION
xref: RelationshipXref21
xref: RelationshipXref20
controller: Protein24

Catalysis18
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction41
control type: ACTIVATION
xref: RelationshipXref31
xref: RelationshipXref30
controller: incision complex for GG-NER (name copied from entity in Homo sapiens)

Catalysis17
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction38
control type: ACTIVATION
xref: RelationshipXref27
xref: RelationshipXref26
controller: pre-incision complex in GG-NER (name copied from entity in Homo sapiens)

Catalysis16
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction34
control type: ACTIVATION
xref: RelationshipXref21
xref: RelationshipXref20
controller: Protein24

UniProt:P36617
type: ProteinReference
xref: UnificationXref329
organism: BioSource1

Catalysis15
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction29
control type: ACTIVATION
xref: RelationshipXref17
xref: RelationshipXref16
controller: Protein11

Catalysis14
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction27
control type: ACTIVATION
xref: RelationshipXref17
xref: RelationshipXref16
controller: Protein11

http://identifiers.org/pubmed/11435397
type: PublicationXref
id: 11435397
author: Allikmets, R
author: Dean, M
author: Rzhetsky, A
db: Pubmed
title: The human ATP-binding cassette (ABC) transporter superfamily
source: Genome Res 11:1156-66
year: 2001

Evidence482
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15364929
comment: Acyl chain remodeling of triacylglycerol (TAG) and diacylglycerol (DAG) progresses through their hydrolysis by patatin-like phospholipase domain-containing proteins 2/3 (PNPLA2/3). DAG is reacylated back to TAG by acylglycerol O-acyltransferase 1/2 (DGAT1/2), while DAG and its hydrolysis product 2-monoacylglycerol (2-MAG) are transacylated back to TAG by PNPLA2/3. In addition, the DAG hydrolysis product 2-MAG is subsequently hydrolyzed to fatty acid and glycerol by monoglyceride lipase (MGLL) (Jenkins et al. 2004).

Evidence481
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18452279
xref: http://identifiers.org/pubmed/15272052
xref: http://identifiers.org/pubmed/19962385
xref: http://identifiers.org/pubmed/19957260
comment: At the endoplasmic reticulum (ER) membrane, monoglyceride lipase (MGLL) hydrolyzes 2-monoacylglycerol (2-MAG) to form a fatty acid and glycerol (Dinh et al. 2004, Zvonok et al. 2008, Bertrand et al. 2010, Labar et al. 2010).

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UUD0
data source: Provenance1
name: Endophilin
name: Q9UUD0
xref: UnificationXref8664
feature: FragmentFeature1334
cellular location: GO:0005886
comment: Reactome DB_ID: 3661155
display name: SH3GL2

Evidence480
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/21173190
xref: http://identifiers.org/pubmed/17170135
xref: http://identifiers.org/pubmed/12359733
xref: http://identifiers.org/pubmed/18718904
xref: http://identifiers.org/pubmed/20705608
comment: In the de novo synthesis of phosphatidic acid (PA), lysophosphatidic acid (LPA) is initially formed by the esterification of sn-1 by glycerol 3-phosphate acyltransferase (GPAT) from glycerol 3-phosphate (G3P). Next, LPA is converted to PA by a LPA acyltransferase (AGPAT, also known as LPAAT). In addition to this, PA is also formed when phosphatidylcholine (PC) is hydrolyzed by phospholipase D1/2 (PLD1/2). PA is involved in acyl chain remodeling via cleavage by phospholipases followed by reacylation by acyltransferases (Ghomashchi et al. 2010, Singer et al. 2002, Prasad et al. 2011, Shindou & Shimizu 2009, Cao et al. 2006).

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94478
data source: Provenance1
name: O94478
name: Endophilin
xref: UnificationXref8666
feature: FragmentFeature1335
cellular location: GO:0005886
comment: Reactome DB_ID: 3661159
display name: SH3GL2

Q09718
type: Protein
entity reference: Q09718
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: AP-2 clathrin coat assembly protein
name: Clathrin -coated Pit Adapter Protein
xref: UnificationXref8680
feature: FragmentFeature1341
cellular location: GO:0005886
comment: Reactome DB_ID: 3661134
display name: AP2M1

Evidence461
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/4401584
xref: http://identifiers.org/pubmed/14506130
xref: http://identifiers.org/pubmed/10710235
comment: 4-carboxycholesta-8(9),24-dien-3beta-ol and NAD+ react to form zymosterone (cholesta-8(9),24-dien-3-one), CO2, and NADH + H+. This reaction occurs in the endoplasmic reticulum, catalyzed by NSDHL (Caldas and Herman 2003). Defects in this enzyme are associated with CHILD syndrome (Congenital Hemidysplasia with Ichthyosiform nevus and Limb Defects) (Konig et al. 2000), but cholesterol biosynthesis in cells and tissues from affceted individuals has not been characterized. Instead, the mechanism and stoichiometry of the reaction are inferred from biochemical studies of partially purified rat enzyme (Rahimtula and Gaylor 1972).

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43005
data source: Provenance1
name: AP-2 beta 2
name: O43005
xref: UnificationXref8678
feature: FragmentFeature1340
cellular location: GO:0005886
comment: Reactome DB_ID: 3661130
display name: AP2B1

Evidence462
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11969204
xref: http://identifiers.org/pubmed/12829805
comment: Zymosterone (cholesta-8(9),24-dien-3-one) and NADPH + H+ react to form zymosterol (cholesta-8(9),24-dien-3beta-ol) and NADP+. This reaction takes place in the endoplasmic reticulum, catalyzed by HSD17B7. Two isoforms of the enzyme due to alternative splicing have been identified but only the first has been tested for enzymatic activity (Marijanovic et al. 2003). The human enzyme has not been studied extensively; molecular details of the reaction are inferred from those worked out in studies of material from rat liver (Gaylor 2002).

UniProt:P36630
type: ProteinReference
xref: UnificationXref7536
organism: BioSource1

http://identifiers.org/pubmed/183598
type: PublicationXref
id: 183598
author: Clark, P
author: Edwards, YH
author: Harris, H
db: Pubmed
title: Isozymes of glyceraldehyde-3-phosphate dehydrogenase in man and other mammals.
source: Ann Hum Genet 40:67-77
year: 1976

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74496
data source: Provenance1
name: Coatomer delta subunit
name: O74496
xref: UnificationXref8712
feature: FragmentFeature1343
cellular location: GO:0005829
comment: Reactome DB_ID: 3661714
display name: ARCN1

Evidence463
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12812989
xref: http://identifiers.org/pubmed/3997841
xref: http://identifiers.org/pubmed/12189593
comment: Cholesta-7,24-dien-3beta-ol, NADPH + H+, and O2 react to form cholesta-5,7,24-trien-3beta-ol, NADP+, and 2 H2O, catalyzed by SC5D. This reaction takes place in the endoplasmic reticulum. Its biochemical details are inferred from those of the reaction catalyzed by the purified rat protein (Kawata et al. 1985). The role of human SC5D in catalyzing this reaction in vivo is established from studies of patients in whom the enzyme is defective (Brunetti-Pierri et al. 2002; Krakowiak et al. 2003).

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UUF7
data source: Provenance1
name: Q9UUF7
name: Coatomer beta subunit
xref: UnificationXref8710
feature: FragmentFeature1342
cellular location: GO:0005829
comment: Reactome DB_ID: 3661706
display name: COPB1

Evidence464
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16054061
xref: http://identifiers.org/pubmed/11969204
xref: http://identifiers.org/pubmed/1390320
xref: http://identifiers.org/pubmed/12668600
xref: http://identifiers.org/pubmed/3524618
comment: Cholesterol is synthesized de novo from from acetyl CoA. The overall synthetic process is outlined in the figure below. Enzymes whose regulation plays a major role in determining the rate of cholesterol synthesis in the body are highlighted in red, and connections to other metabolic processes are indicated. The transformation of lanosterol into cholesterol requires multiple steps, including the removal of three methyl groups, the reduction of one double bond and the migration of another. These reactions may not occur in a single fixed order in the body, so the linear pathway laid out here following the work of Gaylor and colleagues (Gaylor 2002) is an oversimplification of the process that occurs in vivo. Defects in several of the enzymes involved in this process are associated with human disease and have provided useful insights into the regulatory roles of cholesterol and its synthetic intermediates in human development (Herman 2003; Song et al. 2005).

Adaptor protein complex 2 (AP-2) large adaptins
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref8676
cellular location: GO:0005886
comment: Reactome DB_ID: 3661144
comment: Converted from EntitySet in Reactome

Evidence465
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1968462
comment: The FDPS gene is transcribed to yield mRNA and the mRNA is translated to yield protein.

UnificationXref6750
type: UnificationXref
id: 3508918
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3508918

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9Y7L6
data source: Provenance1
name: AP-2 complex subunit sigma
name: Plasma membrane adapto AP-2 17 kDa protein
name: Q9Y7L6
name: Adaptor protein complex AP-2 subunit sigma
xref: UnificationXref8672
feature: FragmentFeature1337
cellular location: GO:0005886
comment: Reactome DB_ID: 3661138
display name: AP2S1

Evidence466
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8976377
comment: The SC5D gene is transcribed to yield mRNA and the mRNA is translated to yield protein.

UnificationXref6751
type: UnificationXref
id: REACT_164270
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_164270.1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q9C0W7
data source: Provenance1
name: AP2A2(1-939)
name: Adaptor protein AP2A2
xref: UnificationXref8675
feature: FragmentFeature1339
cellular location: GO:0005886
comment: Reactome DB_ID: 3661143
display name: Q9C0W7

Evidence467
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8626488
comment: The SQLE gene is transcribed to yield mRNA and the mRNA is translated to yield protein.

UnificationXref6752
type: UnificationXref
id: 3650579
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650579

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q9C0W7
data source: Provenance1
name: Q9C0W7
name: Adaptor protein AP2A1
xref: UnificationXref8674
feature: FragmentFeature1338
cellular location: GO:0005886
comment: Reactome DB_ID: 3661142
display name: AP2A1

Evidence468
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/20138239
comment: The TM7SF2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.

UnificationXref6753
type: UnificationXref
id: 1964477
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1964477

Evidence469
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15457548
xref: http://identifiers.org/pubmed/15589694
xref: http://identifiers.org/pubmed/9748295
comment: After transiting to the nucleus SREBPs (SREBP1A/1C/2, SREBFs) bind short sequences, sterol regulatory elements (SREs), in the promoters of target genes (reviewed in Eberle et al. 2004, Weber et al. 2004). SREBPs alone are relatively weak activators of transcription, with SREBP1C being significantly weaker than SREBP1A or SREBP2. In combination with other transcription factors such as SP1 and NF-Y the SREBPs are much stronger activators. SREBP1C seems to more specifically target genes involved in fatty acid synthesis while SREBP2 seems to target genes involved in cholesterol synthesis (Pai et al. 1998).

UnificationXref6754
type: UnificationXref
id: REACT_164072
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_164072.1

UnificationXref6755
type: UnificationXref
id: 3664606
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664606

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9USP6
data source: Provenance1
name: Q9USP6
name: CLCA_HUMAN
name: Clathrin light chain A
xref: UnificationXref8669
feature: FragmentFeature1336
cellular location: GO:0005886
comment: Reactome DB_ID: 3661149
display name: CLTA

UnificationXref6756
type: UnificationXref
id: 3664612
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664612

UnificationXref6757
type: UnificationXref
id: 3664613
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664613

UnificationXref6758
type: UnificationXref
id: 3664611
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664611

http://identifiers.org/pubmed/183599
type: PublicationXref
id: 183599
author: Hers, HG
db: Pubmed
title: The control of glycogen metabolism in the liver
source: Annu Rev Biochem 45:167-89
year: 1976

UnificationXref6759
type: UnificationXref
id: 3664614
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664614

S6K1 signalling
type: Pathway
data source: Provenance1
pathway component: Phosphorylation and activation of eIF4B by activated S6K1
pathway component: Phosphorylation of Ribosomal protein S6 by activated S6K1
evidence: Evidence205
xref: UnificationXref1105
xref: UnificationXref1106
pathway order: PathwayStep202
pathway order: PathwayStep201
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/12440953
type: PublicationXref
id: 12440953
author: Kruys, V
author: Huez, G
author: Gueydan, C
author: Zhang, T
db: Pubmed
title: AU-rich element-mediated translational control: complexity and multiple activities of trans-activating factors
source: Biochem Soc Trans 30:952-8
year: 2002

Q96WV5
type: Protein
entity reference: Q96WV5
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Coatomer alpha subunit
xref: UnificationXref8714
feature: FragmentFeature1344
cellular location: GO:0005829
comment: Reactome DB_ID: 3661702
display name: COPA

Evidence471
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9852097
comment: The microsomal enzyme cholesterol 25-hydroxylase is a member of a lipid metabolizing enzyme family that utilizes oxygen and diiron-oxygen cofactor to hydroxylate, desaturate, epoxidate and acetylate substrates.

Evidence470
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15457548
xref: http://identifiers.org/pubmed/18974038
xref: http://identifiers.org/pubmed/19933148
comment: Sterol regulatory element binding proteins (SREBPs, SREBFs) respond to low cholesterol concentrations by transiting to the nucleus and activating genes involved in cholesterol and lipid biosynthesis (reviewed in Brown and Goldstein 2009, Osborne and Espenshade 2009, Weber et al. 2004). Newly synthesized SREBPs are transmembrane proteins that bind SCAP in the endoplasmic reticulum (ER) membrane. SCAP binds cholesterol which causes a conformational change that allows SCAP to interact with INSIG, retaining the SCAP:SREBP complex in the ER. INSIG binds oxysterols, which cause INSIG to bind SCAP and retain SCAP:SREBP in the endoplasmic reticulum. In low cholesterol (below about 5 mol%) SCAP no longer interacts with cholesterol or INSIG and binds Sec24 of the CopII coat complex instead. Thus SCAP:SREBP transits with the CopII complex from the ER to the Golgi. In the Golgi SREBP is cleaved by S1P and then by S2P, releasing the N-terminal fragment of SREBP into the cytosol. The N-terminal fragment is imported to the nucleus by importin-beta and then acts with other factors, such as SP1 and NF-Y, to activate transcription of target genes. Targets of SREBP include the genes encoding all enzymes of cholesterol biosynthesis and several genes involved in lipogenesis. SREBP2 most strongly activates cholesterol biosynthesis while SREBP1C most strongly activates lipogenesis.

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P87059
data source: Provenance1
name: MIA40_HUMAN
name: CHCHD4 (MIA40)
name: P87059
name: Mitochondrial intermembrane space import and assembly protein 40
xref: UnificationXref8433
feature: FragmentFeature1278
cellular location: GO:0005758
comment: Reactome DB_ID: 3663982
display name: CHCHD4

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9P7K0
data source: Provenance1
name: TIM9_HUMAN
name: TIMM9 (disulfide-bonded)
name: 4xHC-TIMM9(2-89)
name: Mitochondrial import inner membrane translocase subunit Tim9
name: Q9P7K0
xref: UnificationXref8430
feature: ModificationFeature210
feature: FragmentFeature1277
feature: ModificationFeature209
feature: ModificationFeature208
feature: ModificationFeature211
cellular location: GO:0005743
comment: Reactome DB_ID: 3663935
display name: TIMM9

TIMM17
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref8443
cellular location: GO:0005743
comment: Reactome DB_ID: 3663849
comment: Converted from EntitySet in Reactome

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14144
data source: Provenance1
name: ALR_HUMAN
name: GFER (ERV1)
name: FAD-linked sulfhydryl oxidase ALR
name: O14144
xref: UnificationXref8435
feature: FragmentFeature1279
cellular location: GO:0005758
comment: Reactome DB_ID: 3663986
display name: GFER

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P87130
data source: Provenance1
name: TIMM17B
name: Mitochondrial import inner membrane translocase subunit Tim17-B
name: TI17B_HUMAN
xref: UnificationXref8442
feature: FragmentFeature1281
cellular location: GO:0005743
comment: Reactome DB_ID: 3663848
display name: P87130

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P87130
data source: Provenance1
name: TI17A_HUMAN
name: TIMM17A
name: Mitochondrial import inner membrane translocase subunit Tim17-A
xref: UnificationXref8441
feature: FragmentFeature1280
cellular location: GO:0005743
comment: Reactome DB_ID: 3663847
display name: P87130

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O13636
data source: Provenance1
name: TIM50_HUMAN
name: O13636
name: Mitochondrial import inner membrane translocase subunit TIM50
xref: UnificationXref8447
feature: FragmentFeature1283
cellular location: GO:0005743
comment: Reactome DB_ID: 3663839
display name: TIMM50

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9USM7
data source: Provenance1
name: Q9USM7
name: TIM23_HUMAN
name: Mitochondrial import inner membrane translocase subunit Tim23
xref: UnificationXref8445
feature: FragmentFeature1282
cellular location: GO:0005743
comment: Reactome DB_ID: 3663843
display name: TIMM23

UDP-D-galactose [ChEBI:18307]
type: SmallMoleculeReference
name: UDP-D-galactopyranose
name: UDPgalactose
name: UDP-D-galactose
xref: UnificationXref2468

phytoceramide
type: SmallMolecule
entity reference: CHEBI:31998
data source: Provenance1
xref: UnificationXref3658
xref: UnificationXref3659
cellular location: GO:0005789
comment: Reactome DB_ID: 428204

UnificationXref6748
type: UnificationXref
id: 3665514
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665514

ceramide
type: SmallMolecule
entity reference: CHEBI:17761
data source: Provenance1
xref: UnificationXref3651
xref: UnificationXref3652
cellular location: GO:0005789
comment: Reactome DB_ID: 428256
display name: CERA

UnificationXref6747
type: UnificationXref
id: REACT_140326
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_140326.5

dihydrosphingosine 1-phosphate
type: SmallMolecule
entity reference: CHEBI:16893
data source: Provenance1
name: sphinganine 1-phosphate
xref: UnificationXref3697
xref: UnificationXref3696
cellular location: GO:0005829
comment: Reactome DB_ID: 428275
display name: SPAP

L-serine
type: SmallMolecule
entity reference: CHEBI:17115
data source: Provenance1
xref: UnificationXref3663
xref: UnificationXref3664
cellular location: GO:0005829
comment: Reactome DB_ID: 200736
display name: L-Ser

UnificationXref6749
type: UnificationXref
id: REACT_141306
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_141306.5

UnificationXref6744
type: UnificationXref
id: 3663354
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663354

UnificationXref6743
type: UnificationXref
id: 3663353
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663353

Deamido-NAD+
type: SmallMoleculeReference
name: Deamino-NAD+
name: Deamino-NAD+ [ChEBI:4340]
xref: UnificationXref4645

UnificationXref6746
type: UnificationXref
id: 3663356
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663356

ChEBI:18303 phosphatidyl-L-serine
type: SmallMoleculeReference
name: phosphatidyl-L-serine
xref: UnificationXref3217

UnificationXref6745
type: UnificationXref
id: 3663355
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663355

Choline phosphate
type: SmallMolecule
entity reference: Choline phosphate [ChEBI:3667]
data source: Provenance1
name: Phosphocholine
xref: UnificationXref3721
xref: UnificationXref3720
cellular location: GO:0005886
comment: Reactome DB_ID: 1610735
display name: ChoP

UnificationXref6740
type: UnificationXref
id: O59866
db: UniProt

ceramide
type: SmallMolecule
entity reference: CHEBI:17761
data source: Provenance1
xref: UnificationXref3719
xref: UnificationXref3718
cellular location: GO:0005886
comment: Reactome DB_ID: 429807
display name: CERA

UnificationXref6742
type: UnificationXref
id: Q9USH8
db: UniProt

UnificationXref6741
type: UnificationXref
id: 3663349
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663349

Sphingosine-1-phosphate
type: SmallMolecule
entity reference: CHEBI:37550
data source: Provenance1
name: SPGP
xref: UnificationXref3707
xref: UnificationXref3708
cellular location: GO:0005829
comment: Reactome DB_ID: 428203
display name: S1P

sphinganine
type: SmallMolecule
entity reference: CHEBI:16566
data source: Provenance1
name: dihydrosphingosine
xref: UnificationXref3699
xref: UnificationXref3698
cellular location: GO:0005829
comment: Reactome DB_ID: 428694
display name: SPA

http://identifiers.org/pubmed/10744726
type: PublicationXref
id: 10744726
author: Corfas, G
author: Buxbaum, JD
author: Rio, C
author: Peschon, JJ
db: Pubmed
title: Tumor necrosis factor-alpha-converting enzyme is required for cleavage of erbB4/HER4
source: J Biol Chem 275:10379-87
year: 2000

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09783
data source: Provenance1
name: TIMM8A (disulfide-bonded)
name: TIM8A_HUMAN
name: Q09783
name: Mitochondrial import inner membrane translocase subunit Tim8 A
name: 4xHC-TIMM8A
xref: UnificationXref8428
feature: ModificationFeature202
feature: FragmentFeature1275
feature: ModificationFeature200
feature: ModificationFeature201
feature: ModificationFeature203
cellular location: GO:0005758
comment: Reactome DB_ID: 3663972
display name: TIMM8A

ceramide phosphocholines
type: SmallMolecule
entity reference: CHEBI:17636
data source: Provenance1
name: sphingomyelins
xref: UnificationXref3716
xref: UnificationXref3717
cellular location: GO:0005886
comment: Reactome DB_ID: 429776
display name: SPHM

Mitochondrial import inner membrane translocase subunit Tim8 B
type: Protein
entity reference: Q09783
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: TIMM8B (disulfide-bonded)
name: Q09783
name: TIM8B_HUMAN
name: 4xHC-TIMM8B(2-83)
xref: UnificationXref8429
feature: ModificationFeature206
feature: ModificationFeature204
feature: ModificationFeature205
feature: FragmentFeature1276
feature: ModificationFeature207
cellular location: GO:0005758
comment: Reactome DB_ID: 3663977
display name: TIMM8B

sphingosine
type: SmallMolecule
entity reference: CHEBI:16393
data source: Provenance1
xref: UnificationXref3710
xref: UnificationXref3711
cellular location: GO:0005829
comment: Reactome DB_ID: 428682
display name: SPG

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9P7X1
data source: Provenance1
name: Mitochondrial-processing peptidase subunit beta
name: Q9P7X1
name: MPPB_HUMAN
xref: UnificationXref8466
feature: FragmentFeature1289
cellular location: GO:0005759
comment: Reactome DB_ID: 3663905
display name: PMPCB

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:Q9C1W5
data source: Provenance1
name: TIM16_HUMAN
name: PAM16 (TIM16)
name: Q9C1W5
name: Mitochondrial import inner membrane translocase subunit TIM16
xref: UnificationXref8458
feature: FragmentFeature1288
cellular location: GO:0005743
comment: Reactome DB_ID: 3663855
display name: PAM16

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43047
data source: Provenance1
name: GRPE2_HUMAN
name: GrpE protein homolog 2, mitochondrial
name: O43047
xref: UnificationXref8455
feature: FragmentFeature1287
cellular location: GO:0005743
comment: Reactome DB_ID: 3663868
display name: GRPEL2

PublicationXref1221
type: PublicationXref
id: 0079130356
author: Tanguay, RM
author: Mitchell, GA
author: Grompe, M
author: Lambert, M
db: ISBN
title: Hypertyrosinemia
source: The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1777-1805
year: 2001

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43047
data source: Provenance1
name: GRPE1_HUMAN
name: O43047
name: GrpE protein homolog 1, mitochondrial
xref: UnificationXref8454
feature: FragmentFeature1286
cellular location: GO:0005743
comment: Reactome DB_ID: 3663867
display name: GRPEL1

PublicationXref1220
type: PublicationXref
id: 0079130356
author: Thony, B
author: Blau, N
author: Cotton, RG
author: Hyland, K
db: ISBN
title: Disorders of tetrahydrobiopterin and related biogenic amines
source: The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1725-1776
year: 2001

O74831
type: Protein
entity reference: O74831
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: FRDA_HUMAN
name: FXN(1-210)
name: Frataxin precursor
xref: UnificationXref8472
feature: FragmentFeature1291
cellular location: GO:0005758
comment: Reactome DB_ID: 3663915
display name: FXN

Precursors Imported to the Matrix by TIMM23 PAM
type: Protein
data source: Provenance1
member physical entity: O74831
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref8477
cellular location: GO:0005758
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3663918
display name: Precursor Cargo of TIMM23 PAM

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94745
data source: Provenance1
name: Mitochondrial-processing peptidase subunit alpha
name: O94745
name: MPPA_HUMAN
xref: UnificationXref8468
feature: FragmentFeature1290
cellular location: GO:0005759
comment: Reactome DB_ID: 3663901
display name: PMPCA

1-(5'-Phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole
type: SmallMoleculeReference
name: 5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide
name: SAICAR
name: 5'-Phosphoribosyl-4-(N-succinocarboxamide)-5-aminoimidazole
name: 1-(5'-Phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole [ChEBI:18319]
name: (S)-2-[5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
name: 1-(5'-Phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole
xref: UnificationXref4120

L-Glutaminic acid
type: SmallMolecule
entity reference: CHEBI:16015
data source: Provenance1
name: L-Glutamic acid
name: L-Glutamate
xref: UnificationXref3592
xref: UnificationXref3591
cellular location: GO:0005576
comment: Reactome DB_ID: 210382
display name: Glu

UnificationXref6739
type: UnificationXref
id: REACT_24245
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_24245.1

Leukotriene D4
type: SmallMolecule
entity reference: Leukotriene D4 [ChEBI:6423]
data source: Provenance1
xref: UnificationXref3589
xref: UnificationXref3590
cellular location: GO:0005576
comment: Reactome DB_ID: 266074
display name: LTD4

UnificationXref6738
type: UnificationXref
id: 879479
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=879479

Leukotriene C4
type: SmallMolecule
entity reference: CHEBI:16978
data source: Provenance1
xref: UnificationXref3579
xref: UnificationXref3580
cellular location: GO:0005576
comment: Reactome DB_ID: 266013
display name: LTC4

UnificationXref6737
type: UnificationXref
id: REACT_24248
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_24248.2

UnificationXref6736
type: UnificationXref
id: 879484
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=879484

UnificationXref6735
type: UnificationXref
id: CHEBI:16670
db: ChEBI

UnificationXref6734
type: UnificationXref
id: REACT_24863
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_24863.1

UnificationXref6733
type: UnificationXref
id: 879487
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=879487

UnificationXref6732
type: UnificationXref
id: REACT_24806
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_24806.1

UnificationXref6731
type: UnificationXref
id: 938699
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=938699

pyridine nucleotides, oxidized
type: SmallMolecule
data source: Provenance1
member physical entity: SmallMolecule46
member physical entity: SmallMolecule71
name: NAD+, NADP+
xref: UnificationXref3648
xref: UnificationXref3649
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 428218
display name: NAD(P)+

UnificationXref6730
type: UnificationXref
id: CHEBI:60125
db: ChEBI

dihydroceramide
type: SmallMolecule
entity reference: CHEBI:31488
data source: Provenance1
xref: UnificationXref3646
xref: UnificationXref3647
cellular location: GO:0005789
comment: Reactome DB_ID: 428126
display name: DHCE

NADH, NADPH
type: SmallMolecule
data source: Provenance1
member physical entity: SmallMolecule44
member physical entity: SmallMolecule72
name: pyridine nucleotides, reduced
xref: UnificationXref3644
xref: UnificationXref3643
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 428206
display name: NAD(P)H

Mitotic Spindle Checkpoint
type: Pathway
data source: Provenance1
pathway component: REACT 110681.9
evidence: Evidence1198
xref: UnificationXref7600
xref: UnificationXref7599
xref: RelationshipXref979
pathway order: PathwayStep1176
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O60084
data source: Provenance1
name: TIM44_HUMAN
name: O60084
name: Mitochondrial import inner membrane translocase subunit TIM44
name: TIMM44(?-452)
xref: UnificationXref8452
feature: FragmentFeature1285
cellular location: GO:0005743
comment: Reactome DB_ID: 3663859
display name: TIMM44

sphinganine
type: SmallMolecule
entity reference: CHEBI:16566
data source: Provenance1
name: dihydrosphingosine
xref: UnificationXref3637
xref: UnificationXref3638
cellular location: GO:0005789
comment: Reactome DB_ID: 428163
display name: SPA

GRPEL1 or GRPEL2
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref8456
cellular location: GO:0005743
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3663869

3-dehydrosphinganine
type: SmallMolecule
entity reference: CHEBI:17862
data source: Provenance1
xref: UnificationXref3635
xref: UnificationXref3634
cellular location: GO:0005789
comment: Reactome DB_ID: 428182
display name: 3-ketosphinganine

Leukotriene E4
type: SmallMolecule
entity reference: CHEBI:15650
data source: Provenance1
xref: UnificationXref3617
xref: UnificationXref3616
cellular location: GO:0005576
comment: Reactome DB_ID: 266033
display name: LTE4

Stress-70 protein, mitochondrial
type: Protein
entity reference: UniProt:P22774
data source: Provenance1
name: HSPA9 (mtHsp70)
name: Note: the coordinates are copied over from Homo sapiens.
name: P22774
name: GRP75_HUMAN
xref: UnificationXref8450
feature: FragmentFeature1284
cellular location: GO:0005743
comment: Reactome DB_ID: 3663863
display name: HSPA9

Glycine
type: SmallMolecule
entity reference: CHEBI:15428
data source: Provenance1
name: Aminoacetic acid
xref: UnificationXref3613
xref: UnificationXref3614
cellular location: GO:0005576
comment: Reactome DB_ID: 266029
display name: Gly

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09864
data source: Provenance1
name: 60 kDa heat shock protein, mitochondrial
name: HSP60
name: Q09864
name: CH60_HUMAN
xref: UnificationXref8487
feature: FragmentFeature1299
cellular location: GO:0005743
comment: Reactome DB_ID: 3663834
display name: HSPD1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTL6
data source: Provenance1
name: Q9UTL6
name: HSC20_HUMAN
name: Iron-sulfur cluster co-chaperone protein HscB, mitochondrial
xref: UnificationXref8486
feature: FragmentFeature1298
cellular location: GO:0005743
comment: Reactome DB_ID: 3663830
display name: HSCB

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09864
data source: Provenance1
name: 60 kDa heat shock protein, mitochondrial
name: HSPD1(1-573)
name: HSP60 precursor
name: Q09864
name: CH60_HUMAN
xref: UnificationXref8480
feature: FragmentFeature1296
cellular location: GO:0005743
comment: Reactome DB_ID: 3663911
display name: HSPD1

PublicationXref1210
type: PublicationXref
id: 0079130356
author: Williams, JC
author: Sweetman, L
db: ISBN
title: Branched chain organic acidurias
source: The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 2125-2163
year: 2001

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTL6
data source: Provenance1
name: Q9UTL6
name: HSCB(1-235)
name: HSCB precursor
name: HSC20_HUMAN
name: Iron-sulfur cluster co-chaperone protein HscB, mitochondrial
xref: UnificationXref8479
feature: FragmentFeature1295
cellular location: GO:0005743
comment: Reactome DB_ID: 3663910
display name: HSCB

O74831
type: Protein
entity reference: O74831
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: FRDA_HUMAN
name: FXN(42-210)
name: Frataxin, intermediate
xref: UnificationXref8485
feature: FragmentFeature1297
cellular location: GO:0005743
comment: Reactome DB_ID: 3663826
display name: FXN

Proteins Imported to the Matrix by TIMM23 PAM
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
member physical entity: O74831
xref: UnificationXref8488
cellular location: GO:0005743
comment: Reactome DB_ID: 3663835
comment: Converted from EntitySet in Reactome
display name: Cargo of TIMM23 PAM

UnificationXref6729
type: UnificationXref
id: REACT_24449
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_24449.1

http://identifiers.org/pubmed/14624363
type: PublicationXref
id: 14624363
author: Bruford, EA
author: Hediger, MA
author: Rolfs, A
author: Romero, MF
author: Takanaga, H
author: Peng, JB
db: Pubmed
title: The ABCs of solute carriers: physiological, pathological and therapeutic implications of human membrane transport proteinsIntroduction
source: Pflugers Arch 447:465-8
year: 2004

pyruvate kinase tetramer
type: Complex
data source: Provenance1
member physical entity: pyruvate kinase complex, liver and RBC (name copied from entity in Homo sapiens)
member physical entity: pyruvate kinase M1 complex (name copied from entity in Homo sapiens)
xref: UnificationXref2320
cellular location: GO:0005829
comment: Reactome DB_ID: 3658494
comment: Converted from EntitySet in Reactome

UnificationXref6722
type: UnificationXref
id: REACT_145521
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_145521.5

pyruvate kinase M1 complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry707
component stoichiometry: Stoichiometry709
component stoichiometry: Stoichiometry708
component: SmallMolecule49
component: Note: the coordinates are copied over from Homo sapiens.
component: SmallMolecule78
xref: UnificationXref2317
cellular location: GO:0005829
comment: Reactome DB_ID: 3658491

UnificationXref6721
type: UnificationXref
id: 3665511
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665511

phosphoglycerate kinase 1 complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry704
component stoichiometry: Stoichiometry703
component: SmallMolecule49
component: O60101
xref: UnificationXref2292
cellular location: GO:0005829
comment: Reactome DB_ID: 3658125

UnificationXref6724
type: UnificationXref
id: REACT_138777
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_138777.5

enolase 1 dimer, (alpha) (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry706
component stoichiometry: Stoichiometry705
component: Homologues of ENO1
component: SmallMolecule49
xref: UnificationXref2306
cellular location: GO:0005829
comment: Reactome DB_ID: 3658137

UnificationXref6723
type: UnificationXref
id: 3665512
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665512

glyceraldehyde-3-phosphate dehydrogenase tetramer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry701
component: Homologues of GAPDH
xref: UnificationXref2279
cellular location: GO:0005829
comment: Reactome DB_ID: 3658067

UnificationXref6726
type: UnificationXref
id: REACT_129962
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_129962.5

glyceraldehyde-3-phosphate dehydrogenase, testis-specific, tetramer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry702
component: Homologues of GAPDHS
xref: UnificationXref2283
cellular location: GO:0005829
comment: Reactome DB_ID: 3658071

UnificationXref6725
type: UnificationXref
id: 3665513
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665513

triosephosphate isomerase dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry700
component: P07669
xref: UnificationXref2262
cellular location: GO:0005829
comment: Reactome DB_ID: 3658079

UnificationXref6728
type: UnificationXref
id: 879473
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=879473

glyceraldehyde-3-phosphate dehydrogenase tetramer
type: Complex
data source: Provenance1
member physical entity: glyceraldehyde-3-phosphate dehydrogenase, testis-specific, tetramer (name copied from entity in Homo sapiens)
member physical entity: glyceraldehyde-3-phosphate dehydrogenase tetramer (name copied from entity in Homo sapiens)
xref: UnificationXref2284
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658072

UnificationXref6727
type: UnificationXref
id: CHEBI:53014
db: ChEBI

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTL6
data source: Provenance1
name: Q9UTL6
name: HSCB(1-235)
name: HSCB precursor
name: HSC20_HUMAN
name: Iron-sulfur cluster co-chaperone protein HscB, mitochondrial
xref: UnificationXref8474
feature: FragmentFeature1292
cellular location: GO:0005758
comment: Reactome DB_ID: 3663916
display name: HSCB

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09864
data source: Provenance1
name: 60 kDa heat shock protein, mitochondrial
name: HSPD1(1-573)
name: HSP60 precursor
name: Q09864
name: CH60_HUMAN
xref: UnificationXref8476
feature: FragmentFeature1293
cellular location: GO:0005758
comment: Reactome DB_ID: 3663917
display name: HSPD1

PublicationXref1214
type: PublicationXref
id: 0079130356
author: Cox, RP
db: ISBN
title: Errors of lysine metabolism
source: The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1965-1970
year: 2001

Precursors Imported to the Matrix by TIMM23 PAM
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
member physical entity: O74831
xref: UnificationXref8481
cellular location: GO:0005743
comment: Reactome DB_ID: 3663912
comment: Converted from EntitySet in Reactome
display name: Precursor Cargo of TIMM23 PAM

O74831
type: Protein
entity reference: O74831
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: FRDA_HUMAN
name: FXN(1-210)
name: Frataxin precursor
xref: UnificationXref8478
feature: FragmentFeature1294
cellular location: GO:0005743
comment: Reactome DB_ID: 3663909
display name: FXN

pyruvate kinase complex, liver and RBC (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry712
component stoichiometry: Stoichiometry710
component stoichiometry: Stoichiometry711
component: SmallMolecule49
component: Note: the coordinates are copied over from Homo sapiens.
component: SmallMolecule78
xref: UnificationXref2319
cellular location: GO:0005829
comment: Reactome DB_ID: 3658493

UnificationXref6720
type: UnificationXref
id: REACT_145214
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_145214.5

pyruvate carboxylase holoenzyme (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry713
component stoichiometry: Stoichiometry714
component stoichiometry: Stoichiometry715
component: Note: the coordinates are copied over from Homo sapiens.
component: SmallMolecule85
component: SmallMolecule86
xref: UnificationXref2351
cellular location: GO:0005759
comment: Reactome DB_ID: 3658144

PublicationXref1216
type: PublicationXref
id: 0079130356
author: Goodman, SI
author: Frerman, FE
db: ISBN
title: Organic acidemias due to defects in lysine oxidation: 2-ketoadipic acidemia and glutaric acidemia
source: The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 2195-2204
year: 2001

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O14147
data source: Provenance1
name: DDX11_HUMAN
name: Probable ATP-dependent RNA helicase DDX11
name: O14147
xref: UnificationXref8536
feature: FragmentFeature1308
cellular location: GO:0005654
comment: Reactome DB_ID: 3664400
display name: DDX11

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74508
data source: Provenance1
name: CXXC1_HUMAN
name: CpG-binding protein
name: O74508
xref: UnificationXref8532
feature: FragmentFeature1307
cellular location: GO:0005654
comment: Reactome DB_ID: 3664440
display name: CXXC1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09695
data source: Provenance1
name: Q09695
name: Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2
name: CTDS2_HUMAN
xref: UnificationXref8528
feature: FragmentFeature1306
cellular location: GO:0005654
comment: Reactome DB_ID: 3664411
display name: CTDSP2

Adducin alpha
type: Protein
entity reference: Q7LKY2
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Q7LKY2
name: Alpha adducin
xref: UnificationXref8522
feature: FragmentFeature1305
cellular location: GO:0005829
comment: Reactome DB_ID: 3661810
display name: ADD1

phospho-p-S724-ERN1
type: Protein
entity reference: O94537
data source: Provenance1
xref: UnificationXref8512
feature: FragmentFeature1304
feature: ModificationFeature212
cellular location: GO:0005789
comment: Reactome DB_ID: 3662449

Stoichiometry8
type: Stoichiometry
physical entity: PhysicalEntity4
stoichiometric coefficient: 1.0

Stoichiometry7
type: Stoichiometry
physical entity: Protein2
stoichiometric coefficient: 1.0

Stoichiometry6
type: Stoichiometry
physical entity: PhysicalEntity3
stoichiometric coefficient: 1.0

UnificationXref6718
type: UnificationXref
id: 3663344
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663344

Stoichiometry5
type: Stoichiometry
physical entity: Protein2
stoichiometric coefficient: 1.0

UnificationXref6719
type: UnificationXref
id: 3663345
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663345

Stoichiometry9
type: Stoichiometry
physical entity: Protein2
stoichiometric coefficient: 1.0

UnificationXref6713
type: UnificationXref
id: REACT_154885
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_154885.3

PublicationXref1209
type: PublicationXref
id: 0079130356
author: Shih, VE
author: Chuang, DT
db: ISBN
title: Maple syrup urine disease (branched-chain ketoaciduria)
source: The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1971-2005
year: 2001

UnificationXref6712
type: UnificationXref
id: 3665549
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665549

UnificationXref6711
type: UnificationXref
id: REACT_131593
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_131593.5

UnificationXref6710
type: UnificationXref
id: 3663800
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663800

Stoichiometry3
type: Stoichiometry
physical entity: PhysicalEntity2
stoichiometric coefficient: 1.0

UnificationXref6717
type: UnificationXref
id: 3663342
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663342

Stoichiometry4
type: Stoichiometry
physical entity: Protein1
stoichiometric coefficient: 1.0

UnificationXref6716
type: UnificationXref
id: O59709
db: UniProt

Pyridoxamine phosphate [ChEBI:8670]
type: SmallMoleculeReference
name: Pyridoxamine 5-phosphate
name: Pyridoxamine phosphate
name: Pyridoxamine 5'-phosphate
xref: UnificationXref4584

Stoichiometry1
type: Stoichiometry
physical entity: Protein1
stoichiometric coefficient: 1.0

UnificationXref6715
type: UnificationXref
id: 3663343
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663343

Stoichiometry2
type: Stoichiometry
physical entity: PhysicalEntity1
stoichiometric coefficient: 1.0

UnificationXref6714
type: UnificationXref
id: P41887
db: UniProt

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09864
data source: Provenance1
name: 60 kDa heat shock protein, mitochondrial
name: HSP60
name: Q09864
name: CH60_HUMAN
xref: UnificationXref8494
feature: FragmentFeature1302
cellular location: GO:0005759
comment: Reactome DB_ID: 3663875
display name: HSPD1

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94537
data source: Provenance1
name: IRE1
name: O94537
xref: UnificationXref8508
feature: FragmentFeature1303
cellular location: GO:0005789
comment: Reactome DB_ID: 3662446
display name: ERN1

O74831
type: Protein
entity reference: O74831
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: FRDA_HUMAN
name: FXN(42-210)
name: Frataxin, intermediate
name: FXN (42-210)
xref: UnificationXref8492
feature: FragmentFeature1300
cellular location: GO:0005759
comment: Reactome DB_ID: 3663873
display name: FXN

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTL6
data source: Provenance1
name: Q9UTL6
name: HSC20_HUMAN
name: Iron-sulfur cluster co-chaperone protein HscB, mitochondrial
xref: UnificationXref8493
feature: FragmentFeature1301
cellular location: GO:0005759
comment: Reactome DB_ID: 3663874
display name: HSCB

Proteins Imported to the Matrix by TIMM23 PAM
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
member physical entity: O74831
xref: UnificationXref8495
cellular location: GO:0005759
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3663876
display name: Cargo of TIMM23 PAM

UnificationXref6708
type: UnificationXref
id: 3663797
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663797

UnificationXref6707
type: UnificationXref
id: 3663796
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663796

UnificationXref6709
type: UnificationXref
id: 3663798
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663798

http://identifiers.org/pubmed/19644473
type: PublicationXref
id: 19644473
author: Zhao, Jean J
author: Roberts, Thomas M
author: Liu, Pixu
author: Cheng, Hailing
db: Pubmed
title: Targeting the phosphoinositide 3-kinase pathway in cancer
source: Nat Rev Drug Discov 8:627-44
year: 2009

2-acyl lysophosphatidylinositol
type: SmallMolecule
entity reference: CHEBI:62746
data source: Provenance1
name: 2-acyl-sn-glycero-3-phospho-D-myo-inositol
xref: UnificationXref3360
xref: UnificationXref3361
cellular location: GO:0005789
comment: Reactome DB_ID: 1498737
display name: 2-acyl LPI

1-Acylglycerophosphoinositol
type: SmallMolecule
entity reference: 1-acyl-sn-glycero-3-phospho-D-myo-inositol
data source: Provenance1
name: 1-Acyl-sn-glycero-3-phosphoinositol
name: 1-acyl lysophosphatidylinositol
xref: UnificationXref3354
xref: UnificationXref3355
cellular location: GO:0005789
comment: Reactome DB_ID: 1498733
display name: 1-acyl LPI

Phosphatidylglycerol
type: SmallMolecule
entity reference: CHEBI:17517
data source: Provenance1
xref: UnificationXref3368
xref: UnificationXref3367
cellular location: GO:0005789
comment: Reactome DB_ID: 1483256
display name: PG

cardiolipin
type: SmallMolecule
entity reference: Diphosphatidylglycerol
data source: Provenance1
xref: UnificationXref3388
xref: UnificationXref3389
cellular location: GO:0005789
comment: Reactome DB_ID: 1524081
display name: CL

Evidence410
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Processes annotated here include the digestion of dietary lipids, sterol uptake, the formation and turnover of lipoproteins (chylomicrons, VLDL, LDL, and HDL), and the mobilization of fatty acids through the action of hormone-sensitive lipase.

Dilysocardiolipin
type: SmallMolecule
entity reference: 2,2'-dilyso diphosphatidyl glycerol
data source: Provenance1
xref: UnificationXref3394
xref: UnificationXref3393
cellular location: GO:0005789
comment: Reactome DB_ID: 1524080
display name: DLCL

Evidence411
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: SLC25A1, in the inner mitochondrial membrane, mediates the exchange of mitochondrial citrate for cytosolic malate.

1-phosphatidyl-1D-myo-inositol 4-phosphate
type: SmallMolecule
entity reference: CHEBI:17526
data source: Provenance1
xref: UnificationXref3402
xref: UnificationXref3403
cellular location: GO:0005789
comment: Reactome DB_ID: 1806234
display name: PI4P

Evidence412
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1371749
comment: While fatty acid synthesis from acetyl CoA proceeds in the cytosol, most acetyl CoA in the cell is generated within the mitochondria, by oxidative decarboxylation of the pyruvate derived from glycolysis, as well as from a number of reactions of amino acid catabolism. Mitochondrial Acetyl-CoA is transported to cytoplasm as citrate to participate in fatty acid biosynthesis. Mitochondrial citrate synthase, a tricarboxylic acid transporter in the inner mitochondrial membrane, and cytosolic citrate lyase are involved in this transport.

Phosphatidyl 1D-myo-inositol
type: SmallMolecule
entity reference: SmallMoleculeReference177
data source: Provenance1
xref: UnificationXref3420
xref: UnificationXref3421
cellular location: GO:0000139
comment: Reactome DB_ID: 1524146
display name: PI

Evidence413
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18455495
xref: http://identifiers.org/pubmed/16854592
xref: http://identifiers.org/pubmed/7732023
comment: Cytosolic acetyl-CoA carboxylase 1 (ACACA) catalyzes the reaction of bicarbonate, ATP, and acetyl-CoA to form malonyl-CoA, ADP, and orthophosphate. The reaction is positively regulated by citrate. The human ACACA cDNA has been cloned (Abu-Elheiga et al. 1995) and the biochemical properties of the human enzyme have recently been described (Cheng et al. 2007; Locke et al. 2008). Four ACACA isoforms generated by alternative splicing have been identified as mRNAs - the protein product of the first has been characterized experimentally.

N,N'-Diacetylchitobiosyldiphosphodolichol [ChEBI:7069]
type: SmallMoleculeReference
name: N,N'-Diacetylchitobiosyldiphosphodolichol
name: Chitobiosyldiphosphodolichol
xref: UnificationXref8162

Cytidine diphosphate diacylglycerol
type: SmallMolecule
entity reference: CHEBI:17962
data source: Provenance1
xref: UnificationXref3372
xref: UnificationXref3371
cellular location: GO:0005743
comment: Reactome DB_ID: 1524064
display name: CDP-DAG

Phosphatidylglycerophosphate
type: SmallMolecule
entity reference: CHEBI:37393
data source: Provenance1
xref: UnificationXref3374
xref: UnificationXref3375
cellular location: GO:0005743
comment: Reactome DB_ID: 1524059
display name: PGP

Cytidine-5'-monophosphate
type: SmallMolecule
entity reference: CHEBI:17361
data source: Provenance1
name: cytidine 5'-monophosphate
name: cytidylic acid
xref: UnificationXref3377
xref: UnificationXref3376
cellular location: GO:0005759
comment: Reactome DB_ID: 1524067
display name: CMP

Monolysocardiolipin
type: SmallMolecule
entity reference: MLCL
data source: Provenance1
xref: UnificationXref3386
xref: UnificationXref3385
cellular location: GO:0005789
comment: Reactome DB_ID: 1524069
display name: MLCL

Evidence418
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Fatty acyl-CoA biosynthesis involves following steps: -Palmitate synthesis catalyzed by Acetyl-CoA carboxylase and Fatty acid synthase -Conversion of palmitic acid to long chain fatty acids and -Conversion of long chain fatty acids to fatty acyl-CoA by acyl-CoA synthases.

UnificationXref6703
type: UnificationXref
id: 3660986
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660986

Evidence419
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16864775
xref: http://identifiers.org/pubmed/17707131
xref: http://identifiers.org/pubmed/16495223
xref: http://identifiers.org/pubmed/16620771
xref: http://identifiers.org/pubmed/9212163
xref: http://identifiers.org/pubmed/18718904
xref: PublicationXref692
xref: http://identifiers.org/pubmed/15367102
xref: http://identifiers.org/pubmed/19336658
xref: http://identifiers.org/pubmed/16704971
xref: http://identifiers.org/pubmed/9461603
comment: At the endoplasmic reticulum (ER) membrane, 1-acyl-lysophosphatidic acid (LPA) is acylated to phosphatidic acid (PA) by the enzymes 1-acyl-sn-glycerol-3-phosphate acyltransferases (AGPAT1 through 11), and lysophosphatidylcholine acyltransferase (LPCAT1) (Aguado and Campbell 1998). See recent review by Agarwal (2012, in press). AGPAT1, 2, 3 and LPCAT1 have been characterized biochemically (AGPAT1, 2: Yamashita et al. 2007, West et al. 1997, Aguado and Campbell 1998, Gale et al. 2006; AGPAT3: Agarwal et al. 2006; LPCAT1: Nakanishi et al. 2006, Chen et al. 2006). Two additional proteins, AGPAT4 and AGPAT5, are inferred to have such activity based on studies of homologous mouse enzymes (Lu et al. 2005). These enzymes differ in their tissue specific patterns of expression in the body and in their preferences for specific acyl CoA molecules (Shindou and Shimizu 2009; Takeuchi and Reue 2009).

UnificationXref6704
type: UnificationXref
id: 3663795
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663795

UnificationXref6705
type: UnificationXref
id: 3660990
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660990

UnificationXref6706
type: UnificationXref
id: 3660989
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660989

5-phosphoribosylglycinamide [ChEBI:18349]
type: SmallMoleculeReference
name: Glycinamide ribonucleotide
name: GAR
name: 5-phosphoribosylglycinamide
name: N1-(5-Phospho-D-ribosyl)glycinamide
xref: UnificationXref4090

Evidence414
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17379924
comment: Membrane-associated acyl-CoA synthetase long-chain family member 3 (ACSL3) catalyzes the reaction of palmitate, CoASH, and ATP to form palmitoyl-CoA, AMP, pyrophosphate, and water. The enzyme is probably associated specifically with the endoplasmic reticulum membrane, and can also associate with lipid droplets. It is active on oleic acid as well as on palmitic acid (Fujimoto ea 2007).

Evidence415
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12525535
xref: http://identifiers.org/pubmed/11889465
comment: Acyl-CoA synthetase long-chain family member 4 (ACSL4) associated with the endoplasmic reticulum membrane catalyzes the reaction of arachidonate, CoASH, and ATP to form arachidonyl-CoA, AMP, pyrophosphate, and water (Longo et al. 2003; Meloni et al. 2003).

UnificationXref6700
type: UnificationXref
id: 3660983
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660983

Evidence416
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12482854
comment: Trans-2,3-enoyl-CoA reductase (TECR) catalyzes the reaction of trans-octadec-2-enoyl-CoA and NADPH + H+ to form stearoyl-CoA and NADP+. This activity of TECR protein and its localization to the endoplasmic reticulum membrane was established in studies of transfected cells expressing the protein (Moon and Horton 2003).

UnificationXref6701
type: UnificationXref
id: 3660984
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660984

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
type: SmallMoleculeReference
name: ChEBI:18348 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
name: PIP2
xref: UnificationXref773

Evidence417
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/4379659
xref: http://identifiers.org/pubmed/16564093
comment: Very long-chain fatty acyl-CoA molecules are synthesized from palmitic acid (C16) or other fatty acids that are synthesized de novo or obtained from the diet. Before they can be elongated, these fatty acids are activated by conversion to fatty acyl-CoAs in reactions catalyzed by the five members of the ACSL (acyl-CoA synthetase long-chain) enzyme family. Elongation proceeds by a four-step reaction sequence parallel to that responsible for the synthesis of palmitate (C16) from acetyl-CoA and malonyl-CoA: a molecule of malonyl-CoA condenses with the long chain fatty acyl-CoA forming a 3-oxoacyl-CoA containing two more carbon atoms than the starting long chain fatty acyl-CoA and CO2. This reaction is catalyzed by one of the seven members of the ELOVL (Elongation of very long chain fatty acids protein) enzyme family. The 3-oxoacyl-CoA is reduced to a 3-hydroxyacyl-CoA by HSD17B12 (hydroxysteroid (17-beta) dehydrogenase 12), 3-hydroxyacyl-CoA is dehydrated to a trans-2,3-enoyl-CoA, and the trans-2,3-enoyl-CoA is reduced to a fatty acid two carbon atoms longer than the input one by TECR (trans-2,3-enoyl-CoA reductase) enzyme. All of these enzyme activities are associated with separate polypeptides associated with the endoplasmic reticulum membrane, unlike the multifunctional and cytosolic FAS complex responsible for synthesis of palmitic acid (Jakobsson ea 2006; Nugteren 1965). The specific reactions annotated here mediate the synthesis of stearoyl-CoA (3-hydroxyoctadecanoyl-CoA) from palmitate, as well as the activation and condensation with malonyl-CoA of arachidonic acid, a 20-carbon unsaturated fatty acid that plays a central role in the synthesis of prostaglandins and related hormones. Human cells contain a wide range of very long chain fatty acids, and the enzymes involved in these reactions are believed to have broader substrate specificities than are shown in these annotations, but few direct experimental data are available to support more extensive annotations.

UnificationXref6702
type: UnificationXref
id: 3660985
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660985

http://identifiers.org/pubmed/19234479
type: PublicationXref
id: 19234479
author: Johnson, E
author: Lewinson, O
author: Rees, DC
db: Pubmed
title: ABC transporters: the power to change
source: Nat Rev Mol Cell Biol 10:218-27
year: 2009

1-Acyl-sn-glycero-3-phosphoserine
type: SmallMolecule
entity reference: CHEBI:52603
data source: Provenance1
name: 1-acyl lysophosphatidylserine
xref: UnificationXref3319
xref: UnificationXref3320
cellular location: GO:0005789
comment: Reactome DB_ID: 1498724
display name: 1-acyl LPS

Glycerol 3-phosphocholine
type: SmallMolecule
entity reference: CHEBI:16870
data source: Provenance1
name: glycerophosphocholine
xref: UnificationXref3313
xref: UnificationXref3312
cellular location: GO:0005829
comment: Reactome DB_ID: 1498750
display name: GPCho

2-acyl-sn-glycero-3-phosphocholine
type: SmallMolecule
entity reference: CHEBI:16728
data source: Provenance1
xref: UnificationXref3305
xref: UnificationXref3306
cellular location: GO:0005789
comment: Reactome DB_ID: 975614
display name: 2-acyl LPC

1-acyl-sn-glycero-3-phosphocholines
type: SmallMolecule
entity reference: CHEBI:17504
data source: Provenance1
name: 2-lysophosphatidylcholine
xref: UnificationXref3299
xref: UnificationXref3300
cellular location: GO:0005789
comment: Reactome DB_ID: 1524028
display name: 1-acyl LPC

Mg2+/Mn2+
type: SmallMolecule
data source: Provenance1
member physical entity: SmallMolecule222
member physical entity: Mn(III)
xref: UnificationXref3346
xref: UnificationXref3347
cellular location: GO:0005789
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 1500591

Evidence401
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12105228
xref: http://identifiers.org/pubmed/10585413
xref: http://identifiers.org/pubmed/12121577
xref: http://identifiers.org/pubmed/10419486
xref: http://identifiers.org/pubmed/10777568
xref: http://identifiers.org/pubmed/9822604
comment: Diphosphoinositol polyphosphate phosphohydrolases (DIPP), also known as nucleoside diphosphate-linked moiety X motif (NUDT) proteins, dephosphorylate inositol bisdiphospho-tetrakisphosphate ((PP)2-IP4) to inositol 5-diphospho-1,2,3,4,6-pentakisphosphate (5-PP-IP5). The NUDT proteins involved are: nucleoside diphosphate-linked moiety X motif 3 (NUDT3), 4 (NUDT4), 10 (NUDT10), and 11 (NUDT11). The reactants consumed are: inositol 1,5-bisdiphospho-2,3,4,6-tetrakisphosphate (1,5-(PP)2-IP4) and inositol 3,5-bisdiphospho-1,2,4,6-tetrakisphosphate (3,5-(PP)2-IP4). The following lists the above proteins with their corresponding literature references: NUDT3 (Safrany et al. 1999, Safrany et al. 1998, Yang et al. 1999, Caffrey et al. 2000), NUDT4 (Caffrey et al. 2000), NUDT10 (Leslie et al. 2002, Hidaka et al. 2002) and NUDT11 (Leslie et al. 2002, Hidaka et al. 2002).

Mn(III)
type: SmallMolecule
entity reference: CHEBI:18291
data source: Provenance1
name: Mn(II)
name: Manganese
xref: UnificationXref3344
xref: UnificationXref3345
cellular location: GO:0005789
comment: Reactome DB_ID: 1500595
display name: Mn2+

Evidence402
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11502751
xref: http://identifiers.org/pubmed/17412958
comment: Inositol hexakisphosphate kinase 1 (IP6K1) and 3 (IP6K3) phosphorylate 1-diphospho-2,3,4,5,6-pentakisphosphate (1-PP-IP5) to form inositol 1,5-bisdiphospho-2,3,4,6-tetrakisphosphate (1,5-(PP)2-IP4) (Saiardi et al. 2001, Mulugu et al. 2007).

Cytidine diphosphate diacylglycerol
type: SmallMolecule
entity reference: CHEBI:17962
data source: Provenance1
xref: UnificationXref3337
xref: UnificationXref3338
cellular location: GO:0005789
comment: Reactome DB_ID: 426955
display name: CDP-DAG

Phosphatidyl 1D-myo-inositol
type: SmallMolecule
entity reference: SmallMoleculeReference177
data source: Provenance1
xref: UnificationXref3340
xref: UnificationXref3341
cellular location: GO:0005789
comment: Reactome DB_ID: 426639
display name: PI

Evidence400
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18355727
xref: http://identifiers.org/pubmed/11502751
comment: Inositol hexakisphosphate kinase 1 (IP6K1) and 3 (IP6K3) phosphorylate inositol 5-diphospho-1,2,3,4,6-pentakisphosphate (5-PP-IP5) to inositol 5-triphospho- 1,2,3,4,6-pentakisphosphate (5-PPP-IP5). The following lists the above proteins with their corresponding literature references: IP6K1 (Saiardi et al. 2001, Draskovic et al. 2008) and IP6K3 (Saiardi et al. 2001, Draskovic et al. 2008).

2-acyl lysophosphatidylserine
type: SmallMolecule
entity reference: CHEBI:37646
data source: Provenance1
name: 2-Acyl-sn-glycero-3-phosphoserine
xref: UnificationXref3327
xref: UnificationXref3328
cellular location: GO:0005789
comment: Reactome DB_ID: 1498722
display name: 2-acyl LPS

Inositol
type: SmallMolecule
entity reference: CHEBI:17268
data source: Provenance1
name: Myo-inositol
xref: UnificationXref3335
xref: UnificationXref3334
cellular location: GO:0005829
comment: Reactome DB_ID: 426910
display name: Ins

phosphatidylserine
type: SmallMolecule
entity reference: ChEBI:18303 phosphatidyl-L-serine
data source: Provenance1
xref: UnificationXref3322
xref: UnificationXref3321
cellular location: GO:0005789
comment: Reactome DB_ID: 1500646
display name: PS

Evidence409
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12364542
xref: http://identifiers.org/pubmed/10940339
xref: http://identifiers.org/pubmed/15337753
comment: Triacylglycerol is a major energy store in the body and its hydrolysis to yield fatty acids and glycerol is a tightly regulated part of energy metabolism. A central part in this regulation is played by hormone-sensitive lipase (HSL), a neutral lipase abundant in adipocytes and skeletal and cardiac muscle, but also abundant in ovarian and adrenal tissue, where it mediates cholesterol ester hydrolysis, yielding cholesterol for steroid biosynthesis. The hormones to which it is sensitive include catecholamines (e.g., epinephrine), ACTH, and glucagon, all of which trigger signaling cascades that lead to its phosphorylation and activation, and insulin, which sets off events leading to its dephosphorylation and inactivation (Holm et al. 2000; Kraemer and Shen 2002). The processes of triacylglycerol and cholesterol ester hydrolysis are also regulated by subcellular compartmentalization: these lipids are packaged in cytosolic particles and the enzymes responsible for their hydrolysis, and perhaps for additional steps in their metabolism, are organized at the surfaces of these particles (e.g., Brasaemle et al. 2004). This organization is dynamic: the inactive form of HSL is not associated with the particles, but is translocated there after being phosphorylated. Conversely, perilipin, a major constituent of the particle surface, appears to block access of enzymes to the lipids within the particle; its phosphorylation allows greater access. Here, HSL-mediated triacylglycerol hydrolysis is described as a pathway containing twelve reactions. The first six of these involve activation: phosphorylation of HSL, dimerization of HSL, disruption of CGI-58:perilipin complexes at the surfaces of cytosolic lipid particles, phosphorylation of perilipin, association of phosphorylated HSL with FABP, and translocation of HSL from the cytosol to the surfaces of lipid particles. The next four reactions are the hydrolysis reactions themselves: the hydrolysis of cholesterol esters, and the success…

Evidence407
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/20359876
xref: http://identifiers.org/pubmed/17943301
xref: http://identifiers.org/pubmed/11331907
xref: http://identifiers.org/pubmed/16781889
xref: http://identifiers.org/pubmed/20414202
comment: Inositol phosphates (IPs) are molecules involves in signalling processes in eukaryotes. myo-Inositol consists of a six-carbon cyclic alcohol with an axial 2-hydroxy and five equatorial hydroxyls. Mono-, di-, and triphosphorylation of the inositol ring generates a wide variety of stereochemically distinct signalling entities. Inositol 1,4,5-trisphosphate (I(1,4,5)P3), is formed when the phosphoinositide phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) is hydrolysed by a phospholipase C isozyme. An array of inositol trisphosphate (IP3) and tetrakisphosphate (IP4) molecules are synthesised by the action of various kinases and phosphatases in the cytosol. These species then transport between the cytosol and the nucleus where they are acted on by inositol polyphosphate multikinase (IPMK), inositol-pentakisphosphate 2-kinase (IPPK), inositol hexakisphosphate kinase 1 (IP6K1) and 2 (IP6K2), to produce IP5, IP6, IP7, and IP8 molecules. Some of these nuclear produced IPs transport back to the cytosol where they are converted to an even wider variety of IPs, by kinases and phosphatases, including the di- and triphospho inositol phosphates aka pyrophosphates (Irvine & Schell 2001, Bunney & Katan 2010, Alcazar-Romain & Wente 2008, York 2006, Monserrate and York 2010).

Evidence408
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3955067
xref: http://identifiers.org/pubmed/1249056
comment: Rat monoacylglycerol lipase (MGLL) catalyzes the hydrolysis of 2-acylglycerol to yield glycerol + fatty acid (Tornqvist and Belfrage 1976; Fredrikson et al. 1986). Localization of the enzyme to lipid particles is plausible, given its low solubility and its involvement in acylglycerol metabolism, but this localization has not been directly experimentally verified. The human reaction is inferred from the well-studied rat one.

Evidence405
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7761412
xref: http://identifiers.org/pubmed/10593988
xref: http://identifiers.org/pubmed/9430698
xref: http://identifiers.org/pubmed/15474001
comment: A group of inositol phosphatases dephosphorylate inositol 1,4,5-trisphosphate (I(1,4,5)P3) to inositol 1,4-bisphosphate (I(1,4)P2). The group of inositol phosphatases involved are: inositol polyphosphate 5-phosphatase OCRL-1 (OCRL), phosphatidylinositol 4,5-bisphosphate 5-phosphatase A (INPP5J), and synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1 (SYNJ1). The following lists the above proteins with their corresponding literature references: OCRL (Zhang et al. 1995, Zhang et al. 1998, Schmid et al. 2004); INPP5J (Mochizuki & Thompson 1999); SYNJ1 (Schmid et al. 2004).

Evidence406
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17068342
xref: http://identifiers.org/pubmed/11331907
xref: http://identifiers.org/pubmed/20414202
xref: http://identifiers.org/pubmed/15024000
comment: Inositol phosphates IP2, IP and the six-carbon cyclic alcohol inositol (Ins) are produced by various phosphatases and the inositol-3-phosphate synthase 1 (ISYNA1) (Ju et al. 2004, Ohnishi et al. 2007, Irvine & Schell 2001, Bunney & Katan 2010).

Evidence403
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12105228
xref: http://identifiers.org/pubmed/10585413
xref: http://identifiers.org/pubmed/12121577
xref: http://identifiers.org/pubmed/10419486
xref: http://identifiers.org/pubmed/10777568
xref: http://identifiers.org/pubmed/9822604
comment: Diphosphoinositol polyphosphate phosphohydrolases (DIPP), also known as nucleoside diphosphate-linked moiety X motif (NUDT) proteins, dephosphorylate inositol bisdiphospho-tetrakisphosphate ((PP)2-IP4) to inositol diphospho-pentakisphosphate (PP-IP5). The NUDT proteins involved are: nucleoside diphosphate-linked moiety X motif 3 (NUDT3), 4 (NUDT4), 10 (NUDT10), and 11 (NUDT11). The reactants consumed are: inositol 1,5-bisdiphospho-2,3,4,6-tetrakisphosphate (1,5-(PP)2-IP4) and inositol 3,5-bisdiphospho-1,2,4,6-tetrakisphosphate (3,5-(PP)2-IP4). The products made are: inositol 1-diphospho-2,3,4,5,6-pentakisphosphate (1-PP-IP5) and 3-diphospho-1,2,4,5,6-pentakisphosphate (3-PP-IP5). The following lists the above proteins with their corresponding literature references: NUDT3 (Safrany et al. 1999, Safrany et al. 1998, Yang et al. 1999, Caffrey et al. 2000), NUDT4 (Caffrey et al. 2000), NUDT10 (Leslie et al. 2002, Hidaka et al. 2002) and NUDT11 (Leslie et al. 2002, Hidaka et al. 2002).

Evidence404
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/20359876
xref: http://identifiers.org/pubmed/18355727
xref: http://identifiers.org/pubmed/17943301
xref: http://identifiers.org/pubmed/11331907
xref: http://identifiers.org/pubmed/16781889
xref: http://identifiers.org/pubmed/11502751
xref: http://identifiers.org/pubmed/17702752
xref: http://identifiers.org/pubmed/12121577
xref: http://identifiers.org/pubmed/11909533
xref: http://identifiers.org/pubmed/10777568
comment: Inositol phosphates such as IP4, IP5 and IP6 are converted to an even wider variety of IPs including the di- and triphospho inositol phosphates, also known as pyrophosphates (Irvine & Schell 2001, Alcazar-Romain & Wente 2008, York 2006, Monserrate and York 2010, Ho et al. 2002, Saiardi et al. 2001, Draskovic et al. 2008, Choi et al. 2007, Caffrey et al. 2000, Leslie et al. 2002).

http://identifiers.org/pubmed/10053006
type: PublicationXref
id: 10053006
author: Wasmuth, JJ
author: Thompson, LM
author: Tavormina, PL
author: Jabs, EW
author: Bellus, GA
author: Donoghue, DJ
author: Szabo, J
author: Webster, MK
author: Jiang, W
author: Wilcox, WR
author: Bamshad, MJ
author: Francomano, CA
author: Fraley, AE
author: McIntosh, I
db: Pubmed
title: A novel skeletal dysplasia with developmental delay and acanthosis nigricans is caused by a Lys650Met mutation in the fibroblast growth factor receptor 3 gene
source: Am J Hum Genet 64:722-31
year: 1999

1-phosphatidyl-1D-myo-inositol 4-phosphates
type: SmallMolecule
entity reference: CHEBI:17526
data source: Provenance1
name: Phosphatidylinositol 4-phosphate
xref: UnificationXref3512
xref: UnificationXref3513
cellular location: early endosome membrane
comment: Reactome DB_ID: 1806180
display name: PI4P

http://identifiers.org/pubmed/12419251
type: PublicationXref
id: 12419251
author: Wuarin, J
author: Nurse, P
author: Buck, V
author: Millar, JB
db: Pubmed
title: Stable association of mitotic cyclin B/Cdc2 to replication origins prevents endoreduplication.
source: Cell 111:419-31
year: 2002

1-phosphatidyl-1D-myo-inositol 5-phosphate
type: SmallMolecule
entity reference: CHEBI:16500
data source: Provenance1
xref: UnificationXref3531
xref: UnificationXref3532
cellular location: late endosome membrane
comment: Reactome DB_ID: 1806212
display name: PI5P

4,4-Dimethyl-5alpha-cholesta-8,24-dien-3beta-ol
type: SmallMoleculeReference
name: 14-Demethyllanosterol
name: 14-Demethyllanosterol [ChEBI:755]
xref: UnificationXref3033

Phosphatidyl 1D-myo-inositol
type: SmallMolecule
entity reference: SmallMoleculeReference177
data source: Provenance1
xref: UnificationXref3537
xref: UnificationXref3536
cellular location: late endosome membrane
comment: Reactome DB_ID: 1806195
display name: PI

(5Z,13E)-(15S)-9alpha,11alpha-Epidioxy-15-hydroxyprosta-5,13-dienoate
type: SmallMolecule
entity reference: CHEBI:15554
data source: Provenance1
name: Prostaglandin H2
xref: UnificationXref3552
xref: UnificationXref3551
cellular location: GO:0005829
comment: Reactome DB_ID: 265283
display name: PGH2

Prostaglandin E2
type: SmallMolecule
entity reference: CHEBI:15551
data source: Provenance1
xref: UnificationXref3555
xref: UnificationXref3554
cellular location: GO:0005829
comment: Reactome DB_ID: 265287
display name: PGE2

Leukotriene A4
type: SmallMolecule
entity reference: CHEBI:15651
data source: Provenance1
xref: UnificationXref3564
xref: UnificationXref3563
cellular location: GO:0005829
comment: Reactome DB_ID: 265281
display name: LTA4

Leukotriene-B(4) omega-hydroxylase
type: SmallMolecule
entity reference: CHEBI:15647
data source: Provenance1
name: Leukotriene B4
name: Leukotriene-B(4) 20-monooxygenase
xref: UnificationXref3567
xref: UnificationXref3566
cellular location: GO:0005829
comment: Reactome DB_ID: 266056
display name: LTB4

Zn(II)
type: SmallMolecule
entity reference: CHEBI:29105
data source: Provenance1
name: Zn++
name: Zinc ion
xref: UnificationXref3569
xref: UnificationXref3570
cellular location: GO:0005829
comment: Reactome DB_ID: 29426
display name: Zn2+

Leukotriene C4
type: SmallMolecule
entity reference: CHEBI:16978
data source: Provenance1
xref: UnificationXref3578
xref: UnificationXref3577
cellular location: GO:0005829
comment: Reactome DB_ID: 266066
display name: LTC4

Phosphate
type: SmallMoleculeReference
name: Orthophosphate
name: Orthophosphate [ChEBI:18367]
name: Inorganic Phosphate
xref: UnificationXref525

http://identifiers.org/pubmed/11257506
type: PublicationXref
id: 11257506
author: Gandour, RD
author: van der Leij, FR
author: Ramsay, RR
db: Pubmed
title: Molecular enzymology of carnitine transfer and transport
source: Biochim Biophys Acta 1546:21-43
year: 2001

1-phosphatidyl-1D-myo-inositol 3-phosphate
type: SmallMolecule
entity reference: CHEBI:17283
data source: Provenance1
xref: UnificationXref3520
xref: UnificationXref3519
cellular location: late endosome membrane
comment: Reactome DB_ID: 1806198
display name: PI3P

Arg-tRNA(Arg)
type: SmallMoleculeReference
name: ChEBI:18366 Arg-tRNA(Arg)
xref: UnificationXref7083

1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
type: SmallMolecule
entity reference: CHEBI:16851
data source: Provenance1
xref: UnificationXref3521
xref: UnificationXref3522
cellular location: late endosome membrane
comment: Reactome DB_ID: 1806289
display name: PI(3,5)P2

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q10481
data source: Provenance1
name: TIMM13 (disulfide-bonded)
name: 4xHC-TIMM13
name: TIM13_HUMAN
name: Mitochondrial import inner membrane translocase subunit Tim13
name: Q10481
xref: UnificationXref8427
feature: ModificationFeature198
feature: ModificationFeature199
feature: ModificationFeature197
feature: ModificationFeature196
feature: FragmentFeature1274
cellular location: GO:0005758
comment: Reactome DB_ID: 3663967
display name: TIMM13

COX17_HUMAN
type: Protein
entity reference: Q9P7Z7
data source: Provenance1
name: COX17 (disulfide-bonded)
name: Note: the coordinates are copied over from Homo sapiens.
name: 4xHC-COX17(2-63)
name: Cytochrome c oxidase copper chaperone
name: Q9P7Z7
xref: UnificationXref8425
feature: FragmentFeature1272
feature: ModificationFeature189
feature: ModificationFeature188
feature: ModificationFeature191
feature: ModificationFeature190
cellular location: GO:0005758
comment: Reactome DB_ID: 3663962
display name: COX17

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTE9
data source: Provenance1
name: TIMM10 (disulfide-bonded)
name: TIM10_HUMAN
name: Mitochondrial import inner membrane translocase subunit Tim10
name: Q9UTE9
name: 4xHC-TIMM10
xref: UnificationXref8426
feature: ModificationFeature194
feature: ModificationFeature193
feature: FragmentFeature1273
feature: ModificationFeature195
feature: ModificationFeature192
cellular location: GO:0005743
comment: Reactome DB_ID: 3663927
display name: TIMM10

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9P7K0
data source: Provenance1
name: TIM9_HUMAN
name: TIMM9(2-89)
name: Mitochondrial import inner membrane translocase subunit Tim9
name: Q9P7K0
xref: UnificationXref8423
feature: FragmentFeature1271
cellular location: GO:0005758
comment: Reactome DB_ID: 3663956
display name: TIMM9

1-phosphatidyl-1D-myo-inositol 3-phosphate
type: SmallMolecule
entity reference: CHEBI:17283
data source: Provenance1
xref: UnificationXref3435
xref: UnificationXref3434
cellular location: GO:0000139
comment: Reactome DB_ID: 1806159
display name: PI3P

Products of MIA40:ERV1
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
member physical entity: COX17_HUMAN
member physical entity: Mitochondrial import inner membrane translocase subunit Tim8 B
xref: UnificationXref8431
cellular location: GO:0005758
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3663978

1-phosphatidyl-1D-myo-inositol 4-phosphate
type: SmallMolecule
entity reference: CHEBI:17526
data source: Provenance1
xref: UnificationXref3422
xref: UnificationXref3423
cellular location: GO:0000139
comment: Reactome DB_ID: 1806217
display name: PI4P

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q09783
data source: Provenance1
name: TIM8A_HUMAN
name: Q09783
name: Mitochondrial import inner membrane translocase subunit Tim8 A
xref: UnificationXref8420
feature: FragmentFeature1269
cellular location: GO:0005758
comment: Reactome DB_ID: 3663954
display name: TIMM8A

Mitochondrial import inner membrane translocase subunit Tim8 B
type: Protein
entity reference: Q09783
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: TIMM8B(2-83)
name: Q09783
name: TIM8B_HUMAN
xref: UnificationXref8421
feature: FragmentFeature1270
cellular location: GO:0005758
comment: Reactome DB_ID: 3663955
display name: TIMM8B

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q9UTE9
data source: Provenance1
name: TIM10_HUMAN
name: Mitochondrial import inner membrane translocase subunit Tim10
name: Q9UTE9
xref: UnificationXref8416
feature: FragmentFeature1267
cellular location: GO:0005758
comment: Reactome DB_ID: 3663946
display name: TIMM10

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: Q10481
data source: Provenance1
name: TIM13_HUMAN
name: Mitochondrial import inner membrane translocase subunit Tim13
name: Q10481
xref: UnificationXref8418
feature: FragmentFeature1268
cellular location: GO:0005758
comment: Reactome DB_ID: 3663950
display name: TIMM13

6-(L-erythro-1,2-Dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
type: SmallMoleculeReference
name: 7,8-dihydroneopterin 3'-triphosphate [ChEBI:18372]
name: 6-[(1S,2R)-1,2-Dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin
name: 6-(L-erythro-1,2-dihydroxy-3-triphosphooxypropyl)-7,8-dihydropterin
name: 2-Amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
name: 7,8-dihydroneopterin 3'-triphosphate
xref: UnificationXref3837

COX17_HUMAN
type: Protein
entity reference: Q9P7Z7
data source: Provenance1
name: Note: the coordinates are copied over from Homo sapiens.
name: Cytochrome c oxidase copper chaperone
name: COX17(2-63)
name: Q9P7Z7
xref: UnificationXref8414
feature: FragmentFeature1266
cellular location: GO:0005758
comment: Reactome DB_ID: 3663945
display name: COX17

Phosphatidyl 1D-myo-inositol
type: SmallMolecule
entity reference: SmallMoleculeReference177
data source: Provenance1
xref: UnificationXref3474
xref: UnificationXref3473
cellular location: GO:0005886
comment: Reactome DB_ID: 426658
display name: PI

1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
type: SmallMolecule
entity reference: CHEBI:16851
data source: Provenance1
xref: UnificationXref3481
xref: UnificationXref3480
cellular location: GO:0005886
comment: Reactome DB_ID: 1806224
display name: PI(3,5)P2

PublicationXref1244
type: PublicationXref
id: 0079130356
author: Horwich, AL
author: Brusilow, SW
db: ISBN
title: Urea cycle enzymes
source: The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1909-1963
year: 2001

1-phosphatidyl-1D-myo-inositol 4-phosphates
type: SmallMolecule
entity reference: CHEBI:17526
data source: Provenance1
name: Phosphatidylinositol 4-phosphate
xref: UnificationXref3464
xref: UnificationXref3463
cellular location: GO:0005886
comment: Reactome DB_ID: 392417
display name: PI4P

1-phosphatidyl-1D-myo-inositol 3-phosphate
type: SmallMolecule
entity reference: CHEBI:17283
data source: Provenance1
xref: UnificationXref3472
xref: UnificationXref3471
cellular location: GO:0005886
comment: Reactome DB_ID: 1806276
display name: PI3P

1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
type: SmallMolecule
entity reference: CHEBI:16851
data source: Provenance1
xref: UnificationXref3499
xref: UnificationXref3498
cellular location: early endosome membrane
comment: Reactome DB_ID: 1806205
display name: PI(3,5)P2

Phosphatidyl 1D-myo-inositol
type: SmallMolecule
entity reference: SmallMoleculeReference177
data source: Provenance1
xref: UnificationXref3509
xref: UnificationXref3508
cellular location: early endosome membrane
comment: Reactome DB_ID: 1806199
display name: PI

1-phosphatidyl-1D-myo-inositol 5-phosphate
type: SmallMolecule
entity reference: CHEBI:16500
data source: Provenance1
xref: UnificationXref3486
xref: UnificationXref3485
cellular location: GO:0005886
comment: Reactome DB_ID: 1806240
display name: PI5P

http://identifiers.org/pubmed/11711427
type: PublicationXref
id: 11711427
author: Wang, X
db: Pubmed
title: The expanding role of mitochondria in apoptosis.
source: Genes Dev 15:2922-33
year: 2001

1-phosphatidyl-1D-myo-inositol 3-phosphate
type: SmallMolecule
entity reference: CHEBI:17283
data source: Provenance1
xref: UnificationXref3496
xref: UnificationXref3497
cellular location: early endosome membrane
comment: Reactome DB_ID: 1806200
display name: PI3P

1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
type: SmallMolecule
entity reference: CHEBI:16851
data source: Provenance1
xref: UnificationXref3449
xref: UnificationXref3448
cellular location: GO:0000139
comment: Reactome DB_ID: 1806290
display name: PI(3,5)P2

PIKFYVE:VAC14:FIG4 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry841
component stoichiometry: Stoichiometry843
component stoichiometry: Stoichiometry842
component: Protein765
component: Protein763
component: Protein764
xref: UnificationXref3526
cellular location: late endosome membrane
comment: Reactome DB_ID: 3664299

LTA4H:Zn2+ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry844
component stoichiometry: Stoichiometry845
component: Protein768
component: Zn(II)
xref: UnificationXref3573
cellular location: GO:0005829
comment: Reactome DB_ID: 3662200

PIKFYVE:VAC14:FIG4 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry836
component stoichiometry: Stoichiometry835
component stoichiometry: Stoichiometry837
component: Protein752
component: Protein753
component: Protein754
xref: UnificationXref3456
cellular location: GO:0000139
comment: Reactome DB_ID: 3664307

UnificationXref4559
type: UnificationXref
id: 3661588
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661588

Ammonia
type: SmallMoleculeReference
name: NH3 [ChEBI:16134]
name: NH3
xref: UnificationXref4251

PIKFYVE:VAC14:FIG4 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry838
component stoichiometry: Stoichiometry839
component stoichiometry: Stoichiometry840
component: Protein761
component: Protein762
component: Protein760
xref: UnificationXref3503
cellular location: early endosome membrane
comment: Reactome DB_ID: 3664351

UnificationXref4558
type: UnificationXref
id: 3661587
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661587

UnificationXref4557
type: UnificationXref
id: Q9USK7
db: UniProt

Hydrogen sulfide [ChEBI:5787]
type: SmallMoleculeReference
name: H2S
name: Hydrogen-sulfide
name: Hydrogen sulfide
xref: UnificationXref5242

UnificationXref4556
type: UnificationXref
id: REACT_11378
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11378.2

UnificationXref4555
type: UnificationXref
id: 196834
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=196834

UnificationXref4554
type: UnificationXref
id: CHEBI:15769
db: ChEBI

UnificationXref4553
type: UnificationXref
id: REACT_11705
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11705.2

beta-D-Mannosyldiacetylchitobiosyldiphosphodolichol [ChEBI:10408]
type: SmallMoleculeReference
name: Man-beta1->4GlcNAc-beta1->4GlcNAc-PP-Dol
name: beta-1,4-D-Mannosylchitobiosyldiphosphodolichol
name: beta-D-Mannosyldiacetylchitobiosyldiphosphodolichol
xref: UnificationXref8169

UnificationXref4552
type: UnificationXref
id: 196786
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=196786

SPTLC1:SPTLC2 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry850
component stoichiometry: Stoichiometry851
component: Protein793
component: Protein792
xref: UnificationXref3669
cellular location: GO:0005789
comment: Reactome DB_ID: 3662652

UnificationXref4551
type: UnificationXref
id: CHEBI:15905
db: ChEBI

http://identifiers.org/pubmed/9278442
type: PublicationXref
id: 9278442
author: Shiba, K
author: Musier-Forsyth, K
author: Stello, T
author: Noda, T
author: Motegi, H
author: Schimmel, P
db: Pubmed
title: Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant
source: J Biol Chem 272:22809-16
year: 1997

SPTLC1:SPTLC3 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry853
component stoichiometry: Stoichiometry852
component: Protein794
component: Protein793
xref: UnificationXref3671
cellular location: GO:0005789
comment: Reactome DB_ID: 3662655

UnificationXref4550
type: UnificationXref
id: REACT_7424
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_7424.3

GGT5 dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry848
component stoichiometry: Stoichiometry849
component: Protein781
component: Protein778
xref: UnificationXref3608
cellular location: GO:0005886
comment: Reactome DB_ID: 3662181

L-Lactic acid
type: SmallMolecule
entity reference: CHEBI:422
data source: Provenance1
name: L-Lactate
name: (S)-Lactate
xref: UnificationXref3862
xref: UnificationXref3861
cellular location: GO:0005829
comment: Reactome DB_ID: 29708
display name: LACT

serine palymitoyltransferase
type: Complex
data source: Provenance1
member physical entity: SPTLC1:SPTLC3 (name copied from entity in Homo sapiens)
member physical entity: SPTLC1:SPTLC2 (name copied from entity in Homo sapiens)
xref: UnificationXref3672
cellular location: GO:0005789
display name: SPTLC 2 or 3 complexes
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3662656

L-Phenylalanine
type: SmallMolecule
entity reference: CHEBI:17295
data source: Provenance1
name: (S)-alpha-amino-beta-phenylpropionic acid
xref: UnificationXref3853
xref: UnificationXref3852
cellular location: GO:0005829
comment: Reactome DB_ID: 29502
display name: L-Phe

Apoptosis
type: Pathway
data source: Provenance1
pathway component: Intrinsic Pathway for Apoptosis
pathway component: REACT 131152.5
pathway component: REACT 40104.10
evidence: Evidence335
xref: UnificationXref2174
xref: UnificationXref2175
xref: RelationshipXref136
pathway order: PathwayStep324
pathway order: PathwayStep318
pathway order: PathwayStep327
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

GGT1/5 dimer
type: Complex
data source: Provenance1
member physical entity: GGT5 dimer (name copied from entity in Homo sapiens)
member physical entity: GGT1 dimer (name copied from entity in Homo sapiens)
xref: UnificationXref3609
cellular location: GO:0005886
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3662182

1-Hydroxytricarballylic acid
type: SmallMolecule
entity reference: CHEBI:151
data source: Provenance1
name: 1-Hydroxypropane-1,2,3-tricarboxylic acid
name: D-erythro-Isocitric acid
name: D-threo-Isocitric acid
name: Isocitric acid
name: Isocitrate
name: (1R,2S)-1-Hydroxypropane-1,2,3-tricarboxylate
xref: UnificationXref3926
xref: UnificationXref3927
cellular location: GO:0005759
comment: Reactome DB_ID: 29938
display name: ISCIT

GGT1 dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry846
component stoichiometry: Stoichiometry847
component: Protein775
component: Protein772
xref: UnificationXref3601
cellular location: GO:0005886
comment: Reactome DB_ID: 3662174

Thiamin diphosphate
type: SmallMolecule
entity reference: CHEBI:18290
data source: Provenance1
name: ThPP
name: Thiamin pyrophosphate
name: TPP
name: Thiamine diphosphate
xref: UnificationXref3896
xref: UnificationXref3895
cellular location: GO:0005759
comment: Reactome DB_ID: 113547
display name: TDP

http://identifiers.org/pubmed/14699511
type: PublicationXref
id: 14699511
author: Meier, PJ
author: Kullak-Ublick, GA
author: Stieger, B
db: Pubmed
title: Enterohepatic bile salt transporters in normal physiology and liver disease
source: Gastroenterology 126:322-42
year: 2004

MDMQ10H2
type: SmallMolecule
entity reference: CHEBI:64180
data source: Provenance1
xref: UnificationXref3785
xref: UnificationXref3786
cellular location: GO:0005759
comment: Reactome DB_ID: 2162205

DMQ10H2
type: SmallMolecule
entity reference: CHEBI:64181
data source: Provenance1
xref: UnificationXref3789
xref: UnificationXref3788
cellular location: GO:0005759
comment: Reactome DB_ID: 2162204

http://identifiers.org/pubmed/8806705
type: PublicationXref
id: 8806705
author: Poulter, CD
author: Hahn, FM
author: Chambers, AF
author: Xuan, JW
db: Pubmed
title: Human isopentenyl diphosphate: dimethylallyl diphosphate isomerase: overproduction, purification, and characterization
source: Arch Biochem Biophys 332:30-4
year: 1996

DeMQ10H2
type: SmallMolecule
entity reference: CHEBI:64182
data source: Provenance1
xref: UnificationXref3796
xref: UnificationXref3795
cellular location: GO:0005759
comment: Reactome DB_ID: 2162212

iron (ferrous)
type: SmallMolecule
entity reference: CHEBI:18248
data source: Provenance1
name: Fe(II)
xref: UnificationXref3799
xref: UnificationXref3800
cellular location: GO:0005743
comment: Reactome DB_ID: 352605
display name: Fe2+

Q10H2
type: SmallMolecule
entity reference: CHEBI:64183
data source: Provenance1
xref: UnificationXref3805
xref: UnificationXref3806
cellular location: GO:0005759
comment: Reactome DB_ID: 2162198

Dihydroneopterin trisphosphate
type: SmallMolecule
entity reference: 6-(L-erythro-1,2-Dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
data source: Provenance1
xref: UnificationXref3839
xref: UnificationXref3838
cellular location: GO:0005829
comment: Reactome DB_ID: 1474124
display name: DHNTP

5,6,7,8-Tetrahydrobiopterin
type: SmallMolecule
entity reference: CHEBI:15372
data source: Provenance1
name: 2-Amino-6-(1,2-dihydroxypropyl)-5,6,7,8-tetrahydoro-4(1H)-pteridinone
name: Tetrahydrobiopterin
xref: UnificationXref3848
xref: UnificationXref3849
cellular location: GO:0005829
comment: Reactome DB_ID: 29870
display name: BH4

http://identifiers.org/pubmed/14681208
type: PublicationXref
id: 14681208
author: Qin, Y
author: Macara, IG
author: Yi, R
author: Cullen, BR
db: Pubmed
title: Exportin-5 mediates the nuclear export of pre-microRNAs and short hairpin RNAs
source: Genes Dev 17:3011-6
year: 2003

LPIN2:Mg2+ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry816
component stoichiometry: Stoichiometry817
component: SmallMolecule222
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref3211
cellular location: GO:0005789
comment: Reactome DB_ID: 3664139

UnificationXref4569
type: UnificationXref
id: REACT_101098
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_101098.9

UniProt:O42984
type: ProteinReference
xref: UnificationXref1841
organism: BioSource1

LPIN3:Mg2+ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry819
component stoichiometry: Stoichiometry818
component: SmallMolecule222
component: Protein719
xref: UnificationXref3213
cellular location: GO:0005789
comment: Reactome DB_ID: 3664141

PISD:Pyruvoyl (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry821
component stoichiometry: Stoichiometry822
component stoichiometry: Stoichiometry820
component: SmallMolecule225
component: Protein720
component: Protein723
xref: UnificationXref3234
cellular location: GO:0005743
comment: Reactome DB_ID: 3664157

UnificationXref4566
type: UnificationXref
id: 3665387
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665387

UnificationXref4565
type: UnificationXref
id: REACT_126726
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_126726.5

UnificationXref4568
type: UnificationXref
id: 3665388
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665388

UnificationXref4567
type: UnificationXref
id: REACT_97175
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_97175.9

PIK3C3:Mn2+:PIK3R4:Mn2+ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry831
component stoichiometry: Stoichiometry834
component: PIK3C3:Mn2+ (name copied from entity in Homo sapiens)
component: PIK3R4:Mn2+ (name copied from entity in Homo sapiens)
xref: UnificationXref3442
cellular location: GO:0005829
comment: Reactome DB_ID: 3664312

Zn(II)
type: SmallMolecule
entity reference: CHEBI:29105
data source: Provenance1
name: Zn++
name: Zinc ion
xref: UnificationXref4010
xref: UnificationXref4011
cellular location: GO:0005759
comment: Reactome DB_ID: 880067
display name: Zn2+

UnificationXref4562
type: UnificationXref
id: O13805
db: UniProt

PIK3R4:Mn2+ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry829
component stoichiometry: Stoichiometry830
component: SmallMolecule134
component: Protein750
xref: UnificationXref3438
cellular location: GO:0005829
comment: Reactome DB_ID: 3664311

UnificationXref4561
type: UnificationXref
id: REACT_98050
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_98050.9

PIK3C3:Mn2+ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry833
component stoichiometry: Stoichiometry832
component: SmallMolecule134
component: Protein751
xref: UnificationXref3441
cellular location: GO:0005829
comment: Reactome DB_ID: 3664310

UnificationXref4564
type: UnificationXref
id: 3661685
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661685

UnificationXref4563
type: UnificationXref
id: 3661683
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661683

PCYT1 dimer
type: Complex
data source: Provenance1
member physical entity: PCYT1B dimer (name copied from entity in Homo sapiens)
member physical entity: PCYT1A dimer (name copied from entity in Homo sapiens)
xref: UnificationXref3293
cellular location: GO:0005789
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3664106

Coenzyme Q
type: SmallMolecule
entity reference: CHEBI:16389
data source: Provenance1
name: CoQ
name: ubiquinone
xref: UnificationXref4034
xref: UnificationXref4033
cellular location: GO:0005743
comment: Reactome DB_ID: 73663
display name: Q

PCYT1A dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry825
component: Protein732
xref: UnificationXref3290
cellular location: GO:0005789
comment: Reactome DB_ID: 3664103

FADH2
type: SmallMolecule
entity reference: CHEBI:17877
data source: Provenance1
xref: UnificationXref4028
xref: UnificationXref4029
cellular location: GO:0005743
comment: Reactome DB_ID: 164934

PCYT1B dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry826
component: Protein733
xref: UnificationXref3292
cellular location: GO:0005789
comment: Reactome DB_ID: 3664105

4-hydroxybutyrate
type: SmallMolecule
entity reference: CHEBI:16724
data source: Provenance1
xref: UnificationXref4017
xref: UnificationXref4016
cellular location: GO:0005759
comment: Reactome DB_ID: 880041
display name: HBUT

UnificationXref4560
type: UnificationXref
id: 3661590
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661590

http://identifiers.org/pubmed/7543319
type: PublicationXref
id: 7543319
author: Hameister, H
author: Poustka, A
author: Bachner, D
author: Korn, B
author: Sedlacek, Z
db: Pubmed
title: Expression patterns of two human genes coding for different rab GDP-dissociation inhibitors (GDIs), extremely conserved proteins involved in cellular transport
source: Hum Mol Genet 4:701-8
year: 1995

5'-phosphoribosyl-5-formaminoimidazole-4-carboxamide
type: SmallMoleculeReference
name: ChEBI:18381 5'-phosphoribosyl-5-formaminoimidazole-4-carboxamide
xref: UnificationXref4134

CDIPT:Mg2+/Mn2+ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry828
component stoichiometry: Stoichiometry827
component: Mg2+/Mn2+
component: Protein736
xref: UnificationXref3348
cellular location: GO:0005789
comment: Reactome DB_ID: 3664096

succinate semialdehyde
type: SmallMolecule
entity reference: Succinic semialdehyde
data source: Provenance1
xref: UnificationXref4014
xref: UnificationXref4013
cellular location: GO:0005759
comment: Reactome DB_ID: 880046
display name: SUCCSA

Ethylenesuccinic acid
type: SmallMolecule
entity reference: CHEBI:15741
data source: Provenance1
name: Butanedionic acid
name: Succinate
name: Succinic acid
xref: UnificationXref3961
xref: UnificationXref3960
cellular location: GO:0005759
comment: Reactome DB_ID: 113536
display name: SUCCA

Fumaric acid
type: SmallMolecule
entity reference: Fumaric acid
data source: Provenance1
name: Trans-butenedioic acid
name: Fumarate
xref: UnificationXref3971
xref: UnificationXref3970
cellular location: GO:0005759
comment: Reactome DB_ID: 113588
display name: FUMA

Succinyl-CoA
type: SmallMolecule
entity reference: CHEBI:15380
data source: Provenance1
name: Succinyl coenzyme A
xref: UnificationXref3944
xref: UnificationXref3945
cellular location: GO:0005759
comment: Reactome DB_ID: 70958
display name: SUCC-CoA

Lipoamide
type: SmallMolecule
entity reference: CHEBI:17460
data source: Provenance1
xref: UnificationXref3950
xref: UnificationXref3949
cellular location: GO:0005759
comment: Reactome DB_ID: 29824
display name: LIPAM

(R)-2-hydroxyglutaric acid
type: SmallMolecule
entity reference: (R)-2-hydroxyglutaric acid
data source: Provenance1
name: (R)-2-hydroxyglutarate
xref: UnificationXref3998
xref: UnificationXref3999
cellular location: GO:0005759
comment: Reactome DB_ID: 879997
display name: 2HG

http://identifiers.org/pubmed/16650285
type: PublicationXref
id: 16650285
author: Gorelick, DA
author: Agre, P
author: Tsunenari, T
author: Nielsen, S
author: Praetorius, J
db: Pubmed
title: Aquaporin-11: a channel protein lacking apparent transport function expressed in brain
source: BMC Biochem 7:14
year: 2006

cobalt
type: SmallMolecule
entity reference: CHEBI:27638
data source: Provenance1
xref: UnificationXref4008
xref: UnificationXref4007
cellular location: GO:0005759
comment: Reactome DB_ID: 880069
display name: Co2+

UniProt:O42978
type: ProteinReference
xref: UnificationXref1615
organism: BioSource1

UnificationXref4535
type: UnificationXref
id: 3661608
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661608

UnificationXref4534
type: UnificationXref
id: 3661607
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661607

UnificationXref4533
type: UnificationXref
id: O74866
db: UniProt

UnificationXref4532
type: UnificationXref
id: REACT_3399
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3399.2

SREBP1A/1C/2:NF-Y:FDPS gene (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry799
component stoichiometry: Stoichiometry797
component stoichiometry: Stoichiometry798
component: NF-Y (name copied from entity in Homo sapiens)
component: SREBP1A/1C/2 Dimer (name copied from entity in Homo sapiens)
component: PhysicalEntity130
xref: UnificationXref3099
cellular location: GO:0005654
comment: Reactome DB_ID: 3664214

UnificationXref4539
type: UnificationXref
id: 3661594
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661594

SREBP1A/2:NF-Y:SC5DL gene (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry801
component stoichiometry: Stoichiometry802
component stoichiometry: Stoichiometry800
component: SREBP1A/2 Dimer (name copied from entity in Homo sapiens)
component: PhysicalEntity131
component: NF-Y (name copied from entity in Homo sapiens)
xref: UnificationXref3104
cellular location: GO:0005654
comment: Reactome DB_ID: 3664248

UnificationXref4538
type: UnificationXref
id: O74841
db: UniProt

UnificationXref4537
type: UnificationXref
id: REACT_80178
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_80178.9

UnificationXref4536
type: UnificationXref
id: 3661610
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661610

CH25H (Fe2+ cofactor) (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry809
component stoichiometry: Stoichiometry810
component: Protein709
component: SmallMolecule209
xref: UnificationXref3133
cellular location: GO:0005789
comment: Reactome DB_ID: 3661348

10-formyltetrahydrofolate
type: SmallMolecule
entity reference: CHEBI:15637
data source: Provenance1
xref: UnificationXref4099
xref: UnificationXref4098
cellular location: GO:0005829
comment: Reactome DB_ID: 419151
display name: 10-formyl-THF

HSD17B1 dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry811
component: Protein711
xref: UnificationXref3161
cellular location: GO:0005829
comment: Reactome DB_ID: 3663336

Glycinamide ribonucleotide
type: SmallMolecule
entity reference: 5-phosphoribosylglycinamide [ChEBI:18349]
data source: Provenance1
name: 5-phosphoribosylglycinamide
name: PRGA
name: N1-(5-Phospho-D-ribosyl)glycinamide
xref: UnificationXref4092
xref: UnificationXref4091
cellular location: GO:0005829
comment: Reactome DB_ID: 111338
display name: GAR

SREBP1A/2:SQLE gene (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry803
component stoichiometry: Stoichiometry804
component stoichiometry: Stoichiometry805
component: SREBP1A/2 Dimer (name copied from entity in Homo sapiens)
component: NF-Y (name copied from entity in Homo sapiens)
component: PhysicalEntity132
xref: UnificationXref3109
cellular location: GO:0005654
comment: Reactome DB_ID: 3664240

5,6,7,8-tetrahydrofolate
type: SmallMolecule
entity reference: CHEBI:15635
data source: Provenance1
name: Tetrahydrofolate
name: tetrahydrofolic acid
xref: UnificationXref4105
xref: UnificationXref4104
cellular location: GO:0005829
comment: Reactome DB_ID: 111355
display name: THF

ChEBI:16152 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphates
type: SmallMoleculeReference
name: ChEBI:16152 ChEBI:16152 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphates
xref: UnificationXref6560

SREBP1A/1C/2:NF-Y:TM7SF2 gene (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry806
component stoichiometry: Stoichiometry808
component stoichiometry: Stoichiometry807
component: PhysicalEntity133
component: NF-Y (name copied from entity in Homo sapiens)
component: SREBP1A/1C/2 Dimer (name copied from entity in Homo sapiens)
xref: UnificationXref3114
cellular location: GO:0005654
comment: Reactome DB_ID: 3664224

N2-Formyl-N1-(5-phospho-D-ribosyl)glycinamide
type: SmallMolecule
entity reference: CHEBI:18272
data source: Provenance1
name: N-Formylglycinamide ribonucleotide
name: 5'-phosphoribosyl-N-formylglycinamide
xref: UnificationXref4102
xref: UnificationXref4101
cellular location: GO:0005829
comment: Reactome DB_ID: 111354
display name: N-Formyl-GAR

LPIN
type: Complex
data source: Provenance1
member physical entity: LPIN3:Mg2+ (name copied from entity in Homo sapiens)
member physical entity: LPIN1:Mg2+ (name copied from entity in Homo sapiens)
member physical entity: LPIN2:Mg2+ (name copied from entity in Homo sapiens)
xref: UnificationXref3214
cellular location: GO:0005789
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3664142

UnificationXref4531
type: UnificationXref
id: 73524
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=73524

LPIN1:Mg2+ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry815
component stoichiometry: Stoichiometry814
component: SmallMolecule222
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref3210
cellular location: GO:0005789
comment: Reactome DB_ID: 3664138

UnificationXref4530
type: UnificationXref
id: REACT_11530
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11530.2

MGLL dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry812
component: Protein717
xref: UnificationXref3188
cellular location: GO:0005789
comment: Reactome DB_ID: 3664062

L-glycine
type: SmallMolecule
entity reference: CHEBI:15428
data source: Provenance1
name: Aminoacetic acid
xref: UnificationXref4088
xref: UnificationXref4089
cellular location: GO:0005829
comment: Reactome DB_ID: 29424
display name: Gly

PCYT2 dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry813
component: Protein718
xref: UnificationXref3203
cellular location: GO:0005789
comment: Reactome DB_ID: 3664135

5-phosphoribosylamine
type: SmallMolecule
entity reference: CHEBI:17284
data source: Provenance1
name: 5-phospho-D-ribosylamine
name: 5-phosphoribosyl-1-amine
name: 5-phospho-beta-D-ribosylamine
xref: UnificationXref4082
xref: UnificationXref4083
cellular location: GO:0005829
comment: Reactome DB_ID: 111292
display name: PRA

L-Glutamine
type: SmallMolecule
entity reference: L-Glutamine
data source: Provenance1
name: L-2-Aminoglutaramic acid
xref: UnificationXref4080
xref: UnificationXref4079
cellular location: GO:0005829
comment: Reactome DB_ID: 29472
display name: L-Gln

SQLE:FAD (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry780
component stoichiometry: Stoichiometry779
component: Q9C1W3
component: SmallMolecule189
xref: UnificationXref3006
cellular location: GO:0005789
comment: Reactome DB_ID: 3661274

Coenzyme QH2
type: SmallMolecule
entity reference: CHEBI:17976
data source: Provenance1
name: CoQH2
name: ubiquinol
xref: UnificationXref4036
xref: UnificationXref4037
cellular location: GO:0005743
comment: Reactome DB_ID: 76633
display name: QH2

5'-Adenylic acid
type: SmallMolecule
entity reference: CHEBI:16027
data source: Provenance1
name: Adenylate
name: Adenosine 5'-phosphate
name: 5'-AMP
name: 5'-Adenosine monophosphate
name: adenosine 5'-monophosphate
name: Adenylic acid
xref: UnificationXref4043
xref: UnificationXref4042
cellular location: GO:0005759
comment: Reactome DB_ID: 159448
display name: AMP

http://identifiers.org/pubmed/8752212
type: PublicationXref
id: 8752212
author: Hubbard, SR
author: Schlessinger, J
author: Mohammadi, M
db: Pubmed
title: Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism
source: Cell 86:577-87
year: 1996

sulfur
type: SmallMolecule
entity reference: CHEBI:17909
data source: Provenance1
xref: UnificationXref4061
xref: UnificationXref4062
cellular location: GO:0005829
comment: Reactome DB_ID: 111284
display name: S

Inosine 5'-phosphate
type: SmallMolecule
entity reference: CHEBI:17202
data source: Provenance1
name: Inosine monophosphate
name: 5'-Inosine monophosphate
name: 5'-Inosinic acid
name: 5'-Inosinate
name: Inosinic acid
name: Inosine 5'-monophosphate
xref: UnificationXref4074
xref: UnificationXref4073
cellular location: GO:0005829
comment: Reactome DB_ID: 29602
display name: IMP

Arachidonate production from DAG
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction85
evidence: Evidence148
xref: UnificationXref822
xref: UnificationXref821
pathway order: PathwayStep145
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UnificationXref4544
type: UnificationXref
id: 3661603
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661603

UnificationXref4543
type: UnificationXref
id: 3661601
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661601

UnificationXref4546
type: UnificationXref
id: 3665391
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665391

UnificationXref4545
type: UnificationXref
id: REACT_105775
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_105775.9

Serine biosynthesis
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction435
pathway component: BiochemicalReaction433
pathway component: BiochemicalReaction434
evidence: Evidence739
xref: UnificationXref4853
xref: RelationshipXref627
xref: UnificationXref4852
pathway order: PathwayStep727
pathway order: PathwayStep728
pathway order: PathwayStep729
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UnificationXref4548
type: UnificationXref
id: CHEBI:17561
db: ChEBI

UnificationXref4547
type: UnificationXref
id: REACT_86951
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_86951.9

HACL1 tetramer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry764
component: HACL1 holoenzyme monomer (name copied from entity in Homo sapiens)
xref: UnificationXref2920
cellular location: GO:0005782
comment: Reactome DB_ID: 3662479

UnificationXref4549
type: UnificationXref
id: 111707
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111707

HACL1 holoenzyme monomer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry761
component stoichiometry: Stoichiometry763
component stoichiometry: Stoichiometry762
component: SmallMolecule175
component: 2-hydroxyphytanoyl-CoA lyase
component: SmallMolecule174
xref: UnificationXref2919
cellular location: GO:0005782
comment: Reactome DB_ID: 3662478

2'-deoxyadenosine
type: SmallMolecule
entity reference: CHEBI:17256
data source: Provenance1
name: deoxyadenosine
xref: UnificationXref4183
xref: UnificationXref4182
cellular location: GO:0005829
comment: Reactome DB_ID: 83925
display name: dA

HMGCR dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry768
component: 3-hydroxy-3-methylglutaryl-coenzyme A reductase-1
xref: UnificationXref2936
cellular location: GO:0005789
comment: Reactome DB_ID: 3661299

adenosine
type: SmallMolecule
entity reference: CHEBI:16335
data source: Provenance1
name: ADENOCARD (TN)
xref: UnificationXref4180
xref: UnificationXref4179
cellular location: GO:0005829
comment: Reactome DB_ID: 83909
display name: Ade-Rib

MVK dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry769
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2944
cellular location: GO:0005829
comment: Reactome DB_ID: 3661312

adenosine, deoxyadenosine
type: SmallMolecule
data source: Provenance1
member physical entity: 2'-deoxyadenosine
member physical entity: adenosine
xref: UnificationXref4185
xref: UnificationXref4184
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 500173

MVD dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry770
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2955
cellular location: GO:0005829
comment: Reactome DB_ID: 3661334

N6-(1,2-Dicarboxyethyl)-AMP
type: SmallMolecule
entity reference: CHEBI:15919
data source: Provenance1
name: adenylosuccinate
name: Adenylosuccinic acid
xref: UnificationXref4159
xref: UnificationXref4158
cellular location: GO:0005829
comment: Reactome DB_ID: 35141
display name: ADS

IDI1 or 2 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry771
component stoichiometry: Stoichiometry772
component: SmallMolecule49
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2963
cellular location: GO:0005829
comment: Reactome DB_ID: 3661319

xanthosine 5'-monophosphate
type: SmallMolecule
entity reference: CHEBI:15652
data source: Provenance1
name: xanthylic acid
xref: UnificationXref4145
xref: UnificationXref4146
cellular location: GO:0005829
comment: Reactome DB_ID: 111584
display name: XMP

UnificationXref4540
type: UnificationXref
id: 3661596
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661596

holo-FDPS dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry775
component: FDPS:3Mg++ (name copied from entity in Homo sapiens)
xref: UnificationXref2975
cellular location: GO:0005829
comment: Reactome DB_ID: 3661287

5'-phosphoribosyl-5-formaminoimidazole-4-carboxamide
type: SmallMolecule
entity reference: 5'-phosphoribosyl-5-formaminoimidazole-4-carboxamide
data source: Provenance1
xref: UnificationXref4136
xref: UnificationXref4135
cellular location: GO:0005829
comment: Reactome DB_ID: 111427
display name: FAICAR

Stimulation of the cell death response by PAK-2p34
type: Pathway
data source: Provenance1
pathway component: Proteolytic PAK-2p34 fragment translocates to the nucleus
pathway component: Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197
pathway component: Autophosphorylation of PAK-2p34 in the activation loop
evidence: Evidence329
xref: UnificationXref2152
xref: UnificationXref2153
pathway order: PathwayStep319
pathway order: PathwayStep320
pathway order: PathwayStep321
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

FDPS:3Mg++ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry774
component stoichiometry: Stoichiometry773
component: SmallMolecule49
component: Homologues of FDPS
xref: UnificationXref2974
cellular location: GO:0005829
comment: Reactome DB_ID: 3661286

5'-phosphoribosyl-5-aminoimidazole-4-carboxamide
type: SmallMolecule
entity reference: 5'-Phosphoribosyl-5-amino-4-imidazolecarboxamide
data source: Provenance1
xref: UnificationXref4128
xref: UnificationXref4127
cellular location: GO:0005829
comment: Reactome DB_ID: 111409
display name: AICAR

UnificationXref4542
type: UnificationXref
id: 3661600
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661600

FDFT (Mg2+ cofactor) (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry778
component stoichiometry: Stoichiometry777
component: SmallMolecule49
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2988
cellular location: GO:0005789
comment: Reactome DB_ID: 3661326

UnificationXref4541
type: UnificationXref
id: REACT_89710
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_89710.9

SREBP1A/1C/2 Dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry759
component: PhysicalEntity129
xref: UnificationXref2874
cellular location: GO:0005654
comment: Reactome DB_ID: 3664200

SREBP1A/1C/2:NF-Y:HMGCS1 gene (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry758
component stoichiometry: Stoichiometry760
component stoichiometry: Stoichiometry757
component: PhysicalEntity128
component: NF-Y (name copied from entity in Homo sapiens)
component: SREBP1A/1C/2 Dimer (name copied from entity in Homo sapiens)
xref: UnificationXref2875
cellular location: GO:0005654
comment: Reactome DB_ID: 3664244

5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide
type: SmallMolecule
entity reference: 1-(5'-Phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole
data source: Provenance1
xref: UnificationXref4121
xref: UnificationXref4122
cellular location: GO:0005829
comment: Reactome DB_ID: 111399
display name: SAICAR

Fumarate
type: SmallMolecule
entity reference: CHEBI:37154
data source: Provenance1
xref: UnificationXref4124
xref: UnificationXref4125
cellular location: GO:0005829
comment: Reactome DB_ID: 29586
display name: FUMA

http://identifiers.org/pubmed/8855281
type: PublicationXref
id: 8855281
author: Lu, M
author: Verdijk, MA
author: Smith, BL
author: Agre, P
author: Jung, JS
author: Lee, MD
author: Deen, PM
author: Rijss, JP
author: Merkx, G
db: Pubmed
title: The human AQP4 gene: definition of the locus encoding two water channel polypeptides in brain
source: Proc Natl Acad Sci U S A 93:10908-12
year: 1996

2-(Formamido)-N1-(5-phospho-D-ribosyl)acetamidine
type: SmallMolecule
entity reference: 5'-Phosphoribosylformylglycinamidine
data source: Provenance1
name: 1-(5'-Phosphoribosyl)-N-formylglycinamidine
name: 2-(Formamido)-N1-(5'-phosphoribosyl)acetamidine
name: 5'-Phosphoribosyl-N-formylglycinamidine
name: 5'-phosphoribosylformylglycinamidine
xref: UnificationXref4110
xref: UnificationXref4109
cellular location: GO:0005829
comment: Reactome DB_ID: 111369
display name: FGAM

5'-phosphoribosyl-5-aminoimidazole
type: SmallMolecule
entity reference: 5'-Phosphoribosyl-5-aminoimidazole [ChEBI:28843]
data source: Provenance1
name: Aminoimidazole ribotide
name: 1-(5'-Phosphoribosyl)-5-aminoimidazole
name: 1-(5-Phospho-D-ribosyl)-5-aminoimidazole
xref: UnificationXref4117
xref: UnificationXref4116
cellular location: GO:0005829
comment: Reactome DB_ID: 111370
display name: AIR

UniProt:O42952
type: ProteinReference
xref: UnificationXref1786
organism: BioSource1

UniProt:O42957
type: ProteinReference
xref: UnificationXref8613
organism: BioSource1

2'-deoxyadenosine 5'-diphosphate
type: SmallMoleculeReference
name: 2'-deoxyadenosine 5'-diphosphate [ChEBI:16174]
name: dADP
xref: UnificationXref4384

UnificationXref4516
type: UnificationXref
id: REACT_11493
db: Reactome
id version: 4
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11493.4

UnificationXref4517
type: UnificationXref
id: CHEBI:29073
db: ChEBI

UnificationXref4514
type: UnificationXref
id: CHEBI:16504
db: ChEBI

UnificationXref4515
type: UnificationXref
id: 198803
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=198803

UnificationXref4512
type: UnificationXref
id: REACT_11824
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11824.1

UnificationXref4513
type: UnificationXref
id: 3661677
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661677

UnificationXref4510
type: UnificationXref
id: 3661675
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661675

UnificationXref4511
type: UnificationXref
id: 198842
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=198842

UnificationXref4519
type: UnificationXref
id: REACT_11772
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11772.3

UnificationXref4518
type: UnificationXref
id: 198816
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=198816

Mitotic G2-G2/M phases
type: Pathway
data source: Provenance1
pathway component: REACT 103766.9
evidence: Evidence1226
xref: UnificationXref7729
xref: UnificationXref7728
pathway order: PathwayStep1205
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

UnificationXref4520
type: UnificationXref
id: CHEBI:36144
db: ChEBI

Succinate dehydrogenase flavoprotein (subunit A), oxidised (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry913
component stoichiometry: Stoichiometry912
component: Flavin adenine dinucleotide
component: Protein847
xref: UnificationXref3975
cellular location: GO:0005743
comment: Reactome DB_ID: 3658370

Succinate dehydrogenase complex (oxidised) (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry911
component stoichiometry: Stoichiometry914
component stoichiometry: Stoichiometry918
component stoichiometry: Stoichiometry917
component: Succinate dehydrogenase flavoprotein (subunit A), oxidised (name copied from entity in Homo sapiens)
component: PhysicalEntity138
component: Protein849
component: Succinate dehydrogenase Iron Sulphur (subunit B) (name copied from entity in Homo sapiens)
xref: UnificationXref3983
cellular location: GO:0005743
comment: Reactome DB_ID: 3658381

Succinate dehydrogenase Iron Sulphur (subunit B) (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry915
component stoichiometry: Stoichiometry916
component: PhysicalEntity139
component: Protein848
xref: UnificationXref3980
cellular location: GO:0005743
comment: Reactome DB_ID: 3658375

alpha-ketoglutarate dehydrogenase E1 homodimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry907
component: alpha-ketoglutarate dehydrogenase E1 holoenzyme (name copied from entity in Homo sapiens)
xref: UnificationXref3955
cellular location: GO:0005759
comment: Reactome DB_ID: 3658400

UnificationXref4525
type: UnificationXref
id: REACT_157580
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_157580.3

alpha-ketoglutarate dehydrogenase E2 holoenzyme (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry903
component stoichiometry: Stoichiometry902
component: Protein843
component: Lipoamide
xref: UnificationXref3951
cellular location: GO:0005759
comment: Reactome DB_ID: 3658406

UnificationXref4526
type: UnificationXref
id: 3665396
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665396

Succinyl-CoA synthetase heterodimer (ADP-forming) (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry909
component stoichiometry: Stoichiometry910
component: Protein846
component: Protein845
xref: UnificationXref3966
cellular location: GO:0005759
comment: Reactome DB_ID: 3658392

UnificationXref4527
type: UnificationXref
id: REACT_158047
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_158047.3

alpha-ketoglutarate dehydrogenase E1 holoenzyme (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry905
component stoichiometry: Stoichiometry906
component: Thiamin diphosphate
component: Protein844
xref: UnificationXref3954
cellular location: GO:0005759
comment: Reactome DB_ID: 3658399

UnificationXref4528
type: UnificationXref
id: CHEBI:17015
db: ChEBI

Citrate Synthase Holoenzyme (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry896
component: Protein838
xref: UnificationXref3922
cellular location: GO:0005759
comment: Reactome DB_ID: 3658349

UnificationXref4521
type: UnificationXref
id: 198853
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=198853

UnificationXref4522
type: UnificationXref
id: REACT_11277
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11277.2

alpha-ketoglutarate dehydrogenase complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry901
component stoichiometry: Stoichiometry904
component stoichiometry: Stoichiometry908
component: alpha-ketoglutarate dehydrogenase E2 holoenzyme (name copied from entity in Homo sapiens)
component: alpha-keto acid dehydrogenase E3 homodimer (name copied from entity in Homo sapiens)
component: alpha-ketoglutarate dehydrogenase E1 homodimer (name copied from entity in Homo sapiens)
xref: UnificationXref3956
cellular location: GO:0005759
comment: Reactome DB_ID: 3658413

UnificationXref4523
type: UnificationXref
id: 3661676
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661676

IDH3 complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry898
component stoichiometry: Stoichiometry900
component stoichiometry: Stoichiometry897
component stoichiometry: Stoichiometry899
component: Protein841
component: Protein842
component: SmallMolecule86
component: Protein840
xref: UnificationXref3939
cellular location: GO:0005759
comment: Reactome DB_ID: 3658335

UnificationXref4524
type: UnificationXref
id: 3661679
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661679

UniProt:O42935
type: ProteinReference
xref: UnificationXref1908
organism: BioSource1

UniProt:O42937
type: ProteinReference
xref: UnificationXref8717
organism: BioSource1

UniProt:O42931
type: ProteinReference
xref: UnificationXref1688
organism: BioSource1

UnificationXref4529
type: UnificationXref
id: 196931
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=196931

UniProt:O42939
type: ProteinReference
xref: UnificationXref8629
organism: BioSource1

UniProt:O42938
type: ProteinReference
xref: UnificationXref2232
organism: BioSource1

http://identifiers.org/pubmed/15231747
type: PublicationXref
id: 15231747
author: Lehner, B
author: Sanderson, CM
db: Pubmed
title: A protein interaction framework for human mRNA degradation
source: Genome Res 14:1315-23
year: 2004

phosphorylated pyruvate dehydrogenase E1 complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry888
component stoichiometry: Stoichiometry889
component: pyruvate dehydrogenase E1 complex (name copied from entity in Homo sapiens)
component: Thiamin diphosphate
xref: UnificationXref3903
cellular location: GO:0005759
comment: Reactome DB_ID: 3661889

phosphorylated pyruvate dehydrogenase complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry891
component stoichiometry: Stoichiometry890
component stoichiometry: Stoichiometry893
component stoichiometry: Stoichiometry892
component stoichiometry: Stoichiometry894
component: pyruvate dehydrogenase E1 complex (name copied from entity in Homo sapiens)
component: phosphorylated pyruvate dehydrogenase E1 complex (name copied from entity in Homo sapiens)
component: pyruvate dehydrogenase E2 trimer (name copied from entity in Homo sapiens)
component: Protein829
component: alpha-keto acid dehydrogenase E3 homodimer (name copied from entity in Homo sapiens)
xref: UnificationXref3904
cellular location: GO:0005759
comment: Reactome DB_ID: 3661890

FPP
type: SmallMolecule
entity reference: CHEBI:17407
data source: Provenance1
xref: UnificationXref3732
xref: UnificationXref3733
cellular location: GO:0005759
comment: Reactome DB_ID: 2162257

pyruvate dehydrogenase E1 complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry885
component stoichiometry: Stoichiometry884
component stoichiometry: Stoichiometry883
component: Protein831
component: Protein832
component: Thiamin diphosphate
xref: UnificationXref3899
cellular location: GO:0005759
comment: Reactome DB_ID: 3658470

IPPP
type: SmallMolecule
entity reference: CHEBI:16584
data source: Provenance1
xref: UnificationXref3734
xref: UnificationXref3735
cellular location: GO:0005759
comment: Reactome DB_ID: 2162256

pyruvate dehydrogenase E2 trimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry881
component: Protein830
xref: UnificationXref3892
cellular location: GO:0005759
comment: Reactome DB_ID: 3658477

dGMP
type: SmallMoleculeReference
name: Deoxyguanylic acid
name: 2'-Deoxyguanosine 5'-phosphate
name: 2'-Deoxyguanosine 5'-monophosphate
name: dGMP [ChEBI:16192]
name: Deoxyguanosine monophosphate
xref: UnificationXref4418

lactate dehydrogenase B4 complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry873
component: Protein825
xref: UnificationXref3870
cellular location: GO:0005829
comment: Reactome DB_ID: 3658157

lactate dehydrogenase AB3 complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry872
component stoichiometry: Stoichiometry871
component: Protein824
component: Protein825
xref: UnificationXref3869
cellular location: GO:0005829
comment: Reactome DB_ID: 3658156

alpha-keto acid dehydrogenase E3 holoenzyme (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry876
component stoichiometry: Stoichiometry877
component: SmallMolecule167
component: Protein828
xref: UnificationXref3885
cellular location: GO:0005759
comment: Reactome DB_ID: 3658411

Urea [ChEBI:16199]
type: SmallMoleculeReference
name: Carbamide
name: Urea
xref: UnificationXref5057

alpha-keto acid dehydrogenase E3 homodimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry878
component: alpha-keto acid dehydrogenase E3 holoenzyme (name copied from entity in Homo sapiens)
xref: UnificationXref3886
cellular location: GO:0005759
comment: Reactome DB_ID: 3658412

pyruvate dehydrogenase complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry882
component stoichiometry: Stoichiometry880
component stoichiometry: Stoichiometry879
component stoichiometry: Stoichiometry886
component: pyruvate dehydrogenase E1 complex (name copied from entity in Homo sapiens)
component: pyruvate dehydrogenase E2 trimer (name copied from entity in Homo sapiens)
component: Protein829
component: alpha-keto acid dehydrogenase E3 homodimer (name copied from entity in Homo sapiens)
xref: UnificationXref3900
cellular location: GO:0005759
comment: Reactome DB_ID: 3658482

MPC1:MPC2 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry874
component stoichiometry: Stoichiometry875
component: Protein826
component: Protein827
xref: UnificationXref3880
cellular location: GO:0005743
comment: Reactome DB_ID: 3662238

UniProt:O42900
type: ProteinReference
xref: UnificationXref3436
organism: BioSource1

http://identifiers.org/pubmed/12030331
type: PublicationXref
id: 12030331
author: Badner, JA
author: Baysal, BE
author: Willett-Brozick, JE
author: Corona, W
author: Nimgaonkar, VL
author: Ferrell, RE
author: Detera-Wadleigh, SD
db: Pubmed
title: A mannosyltransferase gene at 11q23 is disrupted by a translocation breakpoint that co-segregates with bipolar affective disorder in a small family
source: Neurogenetics 4:43-53
year: 2002

UniProt:O42905
type: ProteinReference
xref: UnificationXref223
organism: BioSource1

S-adenosyl-L-homocysteine
type: SmallMolecule
entity reference: CHEBI:16680
data source: Provenance1
xref: UnificationXref3776
xref: UnificationXref3775
cellular location: GO:0005759
comment: Reactome DB_ID: 2162252

lactate dehydrogenase complex
type: Complex
data source: Provenance1
member physical entity: lactate dehydrogenase A4 complex (name copied from entity in Homo sapiens)
member physical entity: lactate dehydrogenase A3B complex (name copied from entity in Homo sapiens)
member physical entity: lactate dehydrogenase B4 complex (name copied from entity in Homo sapiens)
member physical entity: lactate dehydrogenase A2B2 complex (name copied from entity in Homo sapiens)
member physical entity: lactate dehydrogenase AB3 complex (name copied from entity in Homo sapiens)
xref: UnificationXref3871
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658158

MHDB
type: SmallMolecule
entity reference: CHEBI:50776
data source: Provenance1
xref: UnificationXref3778
xref: UnificationXref3779
cellular location: GO:0005759
comment: Reactome DB_ID: 2162215

GCH1 dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry864
component: Protein823
xref: UnificationXref3842
cellular location: GO:0005829
comment: Reactome DB_ID: 3664047

lactate dehydrogenase A3B complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry868
component stoichiometry: Stoichiometry869
component: Protein824
component: Protein825
xref: UnificationXref3867
cellular location: GO:0005829
comment: Reactome DB_ID: 3658154

S-adenosyl-L-methionine
type: SmallMolecule
entity reference: CHEBI:15414
data source: Provenance1
xref: UnificationXref3773
xref: UnificationXref3774
cellular location: GO:0005759
comment: Reactome DB_ID: 2162265

lactate dehydrogenase A2B2 complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry866
component stoichiometry: Stoichiometry867
component: Protein824
component: Protein825
xref: UnificationXref3866
cellular location: GO:0005829
comment: Reactome DB_ID: 3658153

lactate dehydrogenase A4 complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry870
component: Protein824
xref: UnificationXref3868
cellular location: GO:0005829
comment: Reactome DB_ID: 3658155

UnificationXref4500
type: UnificationXref
id: Q9P791
db: UniProt

PDSS1/2 tetramer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry858
component stoichiometry: Stoichiometry859
component: Protein815
component: PDSS1:Mg2+ (name copied from entity in Homo sapiens)
xref: UnificationXref3744
cellular location: GO:0005759
comment: Reactome DB_ID: 3664741

UnificationXref4501
type: UnificationXref
id: 3664771
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664771

UnificationXref4502
type: UnificationXref
id: 3664772
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664772

COQ6:FAD (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry860
component stoichiometry: Stoichiometry861
component: Protein817
component: Flavin adenine dinucleotide
xref: UnificationXref3770
cellular location: GO:0005743
comment: Reactome DB_ID: 3664712

UnificationXref4503
type: UnificationXref
id: 3664774
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664774

PDSS1:Mg2+ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry857
component stoichiometry: Stoichiometry856
component: SmallMolecule53
component: Protein814
xref: UnificationXref3741
cellular location: GO:0005759
comment: Reactome DB_ID: 3664736

UnificationXref4504
type: UnificationXref
id: REACT_152920
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_152920.3

GCH1 decamer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry865
component: GCH1 dimer (name copied from entity in Homo sapiens)
xref: UnificationXref3843
cellular location: GO:0005829
comment: Reactome DB_ID: 3664048

UnificationXref4505
type: UnificationXref
id: 3665606
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665606

COQ7:Fe2+ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry863
component stoichiometry: Stoichiometry862
component: iron (ferrous)
component: Protein820
xref: UnificationXref3801
cellular location: GO:0005743
comment: Reactome DB_ID: 3664729

UnificationXref4506
type: UnificationXref
id: REACT_158608
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_158608.3

UnificationXref4508
type: UnificationXref
id: REACT_111960
db: Reactome
id version: 8
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_111960.8

UnificationXref4507
type: UnificationXref
id: 3665102
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665102

UnificationXref4509
type: UnificationXref
id: Q9USM6
db: UniProt

UniProt:O42912
type: ProteinReference
xref: UnificationXref5650
organism: BioSource1

UniProt:O42914
type: ProteinReference
xref: UnificationXref875
organism: BioSource1

UniProt:O42917
type: ProteinReference
xref: UnificationXref142
organism: BioSource1

Flavin adenine dinucleotide
type: SmallMolecule
entity reference: FAD [ChEBI:16238]
data source: Provenance1
xref: UnificationXref3768
xref: UnificationXref3769
cellular location: GO:0005743
comment: Reactome DB_ID: 113597
display name: FAD

UniProt:O42916
type: ProteinReference
xref: UnificationXref3244
organism: BioSource1

NADP+
type: SmallMolecule
entity reference: NADP+
data source: Provenance1
name: beta-Nicotinamide adenine dinucleotide phosphate
name: Nicotinamide adenine dinucleotide phosphate
name: Triphosphopyridine nucleotide
name: NADP
xref: UnificationXref3765
xref: UnificationXref3764
cellular location: GO:0005759
comment: Reactome DB_ID: 113563
display name: TPN

DHDB
type: SmallMolecule
entity reference: CHEBI:50775
data source: Provenance1
xref: UnificationXref3762
xref: UnificationXref3763
cellular location: GO:0005759
comment: Reactome DB_ID: 2162209

Oxygen
type: SmallMolecule
entity reference: CHEBI:15379
data source: Provenance1
xref: UnificationXref3760
xref: UnificationXref3759
cellular location: GO:0005759
comment: Reactome DB_ID: 113533
display name: O2

NADPH
type: SmallMolecule
entity reference: CHEBI:16474
data source: Provenance1
xref: UnificationXref3758
xref: UnificationXref3757
cellular location: GO:0005759
comment: Reactome DB_ID: 113600
display name: TPNH

DHB
type: SmallMolecule
entity reference: CHEBI:64136
data source: Provenance1
xref: UnificationXref3751
xref: UnificationXref3752
cellular location: GO:0005759
comment: Reactome DB_ID: 2162207

PHB
type: SmallMolecule
entity reference: CHEBI:30763
data source: Provenance1
xref: UnificationXref3748
xref: UnificationXref3749
cellular location: GO:0005759
comment: Reactome DB_ID: 2162213

all-E-10PrP2
type: SmallMolecule
entity reference: CHEBI:61011
data source: Provenance1
xref: UnificationXref3738
xref: UnificationXref3737
cellular location: GO:0005759
comment: Reactome DB_ID: 2162214

http://identifiers.org/pubmed/10224048
type: PublicationXref
id: 10224048
author: Guo, S
author: York, JD
author: Lemrow, SM
author: Stolz, LE
db: Pubmed
title: SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases
source: J Biol Chem 274:12990-5
year: 1999

http://identifiers.org/pubmed/8068008
type: PublicationXref
id: 8068008
author: Rödl, W
author: Rücknagel, KP
author: Werner, T
author: Bacher, A
author: Jaeger, E
author: Ziegler, I
author: Gütlich, M
db: Pubmed
title: Human GTP cyclohydrolase I: only one out of three cDNA isoforms gives rise to the active enzyme
source: Biochem J 302:215-21
year: 1994

Evidence393
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/20359876
xref: http://identifiers.org/pubmed/18355727
xref: http://identifiers.org/pubmed/17943301
xref: http://identifiers.org/pubmed/11331907
xref: http://identifiers.org/pubmed/16781889
xref: http://identifiers.org/pubmed/11502751
xref: http://identifiers.org/pubmed/12027805
xref: http://identifiers.org/pubmed/10827188
xref: http://identifiers.org/pubmed/17412958
xref: http://identifiers.org/pubmed/12223481
xref: http://identifiers.org/pubmed/16293229
comment: Within the nucleus, inositol polyphosphate multikinase (IPMK), inositol-pentakisphosphate 2-kinase (IPPK), inositol hexakisphosphate kinase 1 (IP6K1) and 2 (IP6K2) produce IP5, IP6, IP7, and IP8 inositol phosphate molecules (Irvine & Schell 2001, Alcazar-Romain & Wente 2008, York 2006, Monserrate and York 2010, Nalaskowski et al. 2002, Chang et al. 2002, Chang & Majerus 2006, Saiardi et al. 2001, Saiardi et al. 2000, Draskovic et al. 2008, Mulugu et al. 2007).

Evidence394
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18355727
xref: http://identifiers.org/pubmed/11502751
xref: http://identifiers.org/pubmed/10827188
comment: Inositol hexakisphosphate kinase 1 (IP6K1) and 3 (IP6K3) phosphorylate inositol 1,3,4,5,6-pentakisphosphate (I(1,3,4,5,6)P5) to inositol 5-diphospho-(1,3,4,6)-tetrakisphosphate (5-PP-IP4) (Saiardi et al. 2001, Saiardi et al. 2000, Draskovic et al. 2008).

Evidence391
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18355727
xref: http://identifiers.org/pubmed/11502751
comment: In the nucleus, inositol hexakisphosphate kinase 1 (IP6K1) and 2 (IP6K2) phosphorylate inositol 5-diphospho-1,2,3,4,6-pentakisphosphate (5-PP-IP5) to inositol 5-triphospho- 1,2,3,4,6-pentakisphosphate (5-PPP-IP5) (Saiardi et al. 2001, Draskovic et al. 2008) and IP6K2 (Saiardi et al. 2001, Draskovic et al. 2008). While this reaction has been demonstrated to occur in vitro, the extent to which it occurs in vivo is less clear.

Evidence392
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11502751
xref: http://identifiers.org/pubmed/17412958
comment: In the nucleus, inositol hexakisphosphate kinase 1 (IP6K1) and 2 (IP6K2) phosphorylate 1-diphospho-2,3,4,5,6-pentakisphosphate (1-PP-IP5) to make inositol 1,5-bisdiphospho-2,3,4,6-tetrakisphosphate (1,5-(PP)2-IP4) (Saiardi et al. 2001, Mulugu et al. 2007).

Evidence390
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18355727
xref: http://identifiers.org/pubmed/11502751
xref: http://identifiers.org/pubmed/17412958
comment: In the nucleus, inositol hexakisphosphate kinase 1 (IP6K1) and 2 (IP6K2) phosphorylate inositol 1,2,3,4,5,6-hexakisphosphate (IP6) to inositol 5-diphospho-1,2,3,4,6-pentakisphosphate (5-PP-IP5). The following lists the above proteins with their corresponding literature references: IP6K1 (Saiardi et al. 2001, Mulugu et al. 2007, Draskovic et al. 2008) and IP6K2 (Saiardi et al. 2001, Mulugu et al. 2007, Draskovic et al. 2008).

http://identifiers.org/pubmed/15761154
type: PublicationXref
id: 15761154
author: Pack, M
author: Chang, H
author: Delamarre, L
author: Trombetta, ES
author: Mellman, I
db: Pubmed
title: Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate
source: Science 307:1630-4
year: 2005

http://identifiers.org/pubmed/18048764
type: PublicationXref
id: 18048764
author: Eizirik, DL
author: Cnop, M
author: Cardozo, AK
db: Pubmed
title: The role for endoplasmic reticulum stress in diabetes mellitus
source: Endocr Rev 29:42-61
year: 2008

Evidence389
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18355727
xref: http://identifiers.org/pubmed/11502751
xref: http://identifiers.org/pubmed/10827188
comment: In the nucleus, inositol hexakisphosphate kinase 1 (IP6K1) and 2 (IP6K2) phosphorylate5-diphospho-1,3,4,6-tetrakisphosphate (5-PP-IP4) to inositol 1,5-bisdiphospho-3,4,6-trisphosphate (1,5-(PP)2-IP3) (Saiardi et al. 2001, Saiardi et al. 2000, Draskovic et al. 2008).

Evidence388
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18355727
xref: http://identifiers.org/pubmed/11502751
xref: http://identifiers.org/pubmed/10827188
comment: In the nucleus, inositol hexakisphosphate kinase 1 (IP6K1) and 2 (IP6K2) phosphorylate inositol 1,3,4,5,6-pentakisphosphate (I(1,3,4,5,6)P5) to inositol 5-diphospho-(1,3,4,6)-tetrakisphosphate (5-PP-IP4) (Saiardi et al. 2001, Saiardi et al. 2000, Draskovic et al. 2008).

Evidence387
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11331907
xref: http://identifiers.org/pubmed/20414202
comment: An array of inositol trisphosphate (IP3) and tetrakisphosphate (IP4) molecules are synthesised by the action of various kinases and phosphatases in the cytosol (Irvine & Schell 2001, Bunney & Katan 2010).

Evidence386
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7761412
xref: http://identifiers.org/pubmed/8769125
xref: http://identifiers.org/pubmed/8723348
xref: http://identifiers.org/pubmed/15316017
xref: http://identifiers.org/pubmed/10593988
xref: http://identifiers.org/pubmed/9430698
xref: http://identifiers.org/pubmed/15474001
xref: http://identifiers.org/pubmed/11909533
xref: http://identifiers.org/pubmed/12223481
comment: A group of inositol phosphatases and the broad specificity enzyme inositol-tetrakisphosphate 1-kinase (ITPK1) dephosphorylate inositol 1,3,4,5-tetrakisphosphate (I(1,3,4,5)P4) to inositol 1,3,4-trisphosphate (I(1,3,4)P3). The group of inositol phosphatases involved are: inositol polyphosphate 5-phosphatase OCRL-1 (OCRL), phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) aka SHIP1, phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2 (INPPL1) aka SHIP2, phosphatidylinositol 4,5-bisphosphate 5-phosphatase A (INPP5J) aka PIPP, and synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1 (SYNJ1). The following lists the above proteins with their corresponding literature references: OCRL (Chang et al. 2002, Zhang et al. 1995, Zhang et al. 1998, Schmid et al. 2004); INPP5D (Drayer et al. 1996, Kavanaugh et al. 1996); INPPL1 (Chi et al. 2004); INPP5J (Mochizuki & Thompson 1999); SYNJ1 (Schmid et al. 2004); ITPK1 (Ho et al. 2002).

Evidence385
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: These pathways together are responsible for: 1) the extraction of energy and carbon skeletons for biosyntheses from dietary sugars and related molecules; 2) the short-term storage of glucose in the body (as glycogen) and its mobilization during a short fast; and 3) the synthesis of glucose from pyruvate during extended fasts.

Evidence384
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8702702
xref: http://identifiers.org/pubmed/4358634
xref: http://identifiers.org/pubmed/14392173
xref: http://identifiers.org/pubmed/8253776
xref: http://identifiers.org/pubmed/2444588
xref: http://identifiers.org/pubmed/4328836
xref: http://identifiers.org/pubmed/2537655
xref: http://identifiers.org/pubmed/2168892
comment: 5-Phospho-alpha-D-ribose 1-diphosphate (PRPP) is a key intermediate in both the de novo and salvage pathways of purine and pyrimidine synthesis. PRPP and the enzymatic activity responsible for its synthesis were first described by Kornberg et al. (1955). The enzyme, phosphoribosyl pyrophosphate synthetase 1, has been purified from human erythrocytes and characterized biochemically. The purified enzyme readily forms multimers; its smallest active form appears to be a dimer and for simplicity it is annotated as a dimer here. It specifically catalyzes the transfer of pyrophosphate from ATP or dATP to D-ribose 5-phosphate, and has an absolute requirement for Mg++ and orthophosphate (Fox and Kelley 1971; Roth et al. 1974). The significance of the reaction with dATP in vivo is unclear, as the concentration of cytosolic dATP is normally much lower than that of ATP. The importance of this enzyme for purine synthesis in vivo has been established by demonstrating excess phosphoribosyl pyrophosphate synthetase activity, correlated with elevated enzyme levels or altered enzyme properties, in individuals whose rates of uric acid production are constitutively abnormally high (Becker and Kim 1987; Roessler et al. 1993). Molecular cloning studies have revealed the existence of two additional genes that encode phosphoribosyl pyrophosphate synthetase-like proteins, one widely expressed (phosphoribosyl pyrophosphate synthetase 2) and one whose expression appears to be confined to the testis (phosphoribosyl pyrophosphate synthetase 1-like 1) (Taira et al. 1989; 1991). Neither of these proteins has been purified and characterized enzymatically, nor have variations in the abundance or sequence of either protein been associated with alterations in human nucleotide metabolism (Roessler et al. 1993; Becker et al. 1996), so their dimerization and ability to catalyze the synthesis of PRPP from D-ribose 5-phosphate are inferred here on the basis of their predicted amino acid sequence similarit…

http://identifiers.org/pubmed/16543958
type: PublicationXref
id: 16543958
author: Hirsch, E
author: Rommel, C
author: Barberis, L
author: Montrucchio, G
author: Lembo, G
author: Costa, C
db: Pubmed
title: Signaling through PI3Kgamma: a common platform for leukocyte, platelet and cardiovascular stress sensing
source: Thromb Haemost 95:29-35
year: 2006

Evidence399
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12105228
xref: http://identifiers.org/pubmed/10585413
xref: http://identifiers.org/pubmed/12121577
xref: http://identifiers.org/pubmed/10419486
xref: http://identifiers.org/pubmed/10777568
xref: http://identifiers.org/pubmed/9822604
comment: Diphosphoinositol polyphosphate phosphohydrolases, also known as nucleoside diphosphate-linked moiety X motif (NUDT) proteins, dephosphorylate inositol diphospho-pentakisphosphate (PP-IP5) to inositol 1,2,3,4,5,6-hexakisphosphate (IP6). The NUDT proteins involved are: nucleoside diphosphate-linked moiety X motif 3 (NUDT3), 4 (NUDT4), 10 (NUDT10), and 11 (NUDT11). The reactants consumed are: inositol 1-diphospho-2,3,4,5,6-pentakisphosphate (1-PP-IP5) and 3-diphospho-1,2,4,5,6-pentakisphosphate (3-PP-IP5). The following lists the above proteins with their corresponding literature references: NUDT3 (Safrany et al. 1999, Safrany et al. 1998, Yang et al. 1999, Caffrey et al. 2000), NUDT4 (Caffrey et al. 2000), NUDT10 (Leslie et al. 2002, Hidaka et al. 2002) and NUDT11 (Leslie et al. 2002, Hidaka et al. 2002).

Evidence396
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18355727
xref: http://identifiers.org/pubmed/11502751
xref: http://identifiers.org/pubmed/10827188
comment: Inositol hexakisphosphate kinase 1 (IP6K1) and 3 (IP6K3) phosphorylate inositol 1-diphospho-3,4,5,6-tetrakisphosphate (1-PP-IP4) to form inositol 1,5-bisdiphospho-3,4,6-trisphosphate (1,5-(PP)2-IP3) (Saiardi et al. 2001, Saiardi et al. 2000, Draskovic et al. 2008).

Evidence395
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11502751
xref: http://identifiers.org/pubmed/10827188
comment: Diphosphoinositol polyphosphate phosphohydrolase 2, also known as nucleoside diphosphate-linked moiety X motif 4 (NUDT4), dephosphorylates diphospho- tetrakisphosphate (PP-IP4) to inositol 1,3,4,5,6-pentakisphosphate (I(1,3,4,5,6)P5). The products made are: inositol 5-diphospho-1,3,4,6-tetrakisphosphate (5-PP-IP4); inositol 1-diphospho-3,4,5,6-tetrakisphosphate (1-PP-IP4); and inositol 3-diphospho-1,4,5,6-tetrakisphosphate (3-PP-IP4). The following lists the above protein with its corresponding literature references: NUDT4 (Saiardi et al. 2001, Saiardi et al. 2000).

Evidence398
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12105228
xref: http://identifiers.org/pubmed/10585413
xref: http://identifiers.org/pubmed/12121577
xref: http://identifiers.org/pubmed/10419486
xref: http://identifiers.org/pubmed/10777568
xref: http://identifiers.org/pubmed/9822604
comment: Diphosphoinositol polyphosphate phosphohydrolases (DIPP), also known as nucleoside diphosphate-linked moiety X motif (NUDT) proteins, dephosphorylate inositol 5-diphospho-1,2,3,4,6-pentakisphosphate (5-PP-IP5) to inositol 1,2,3,4,5,6-hexakisphosphate (IP6). The NUDT proteins involved are: nucleoside diphosphate-linked moiety X motif 3 (NUDT3), 4 (NUDT4), 10 (NUDT10), and 11 (NUDT11). The following lists the above proteins with their corresponding literature references: NUDT3 (Safrany et al. 1999, Safrany et al. 1998, Yang et al. 1999, Caffrey et al. 2000), NUDT4 (Caffrey et al. 2000), NUDT10 (Leslie et al. 2002, Hidaka et al. 2002) and NUDT11 (Leslie et al. 2002, Hidaka et al. 2002).

Evidence397
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18355727
xref: http://identifiers.org/pubmed/11502751
xref: http://identifiers.org/pubmed/18981179
xref: http://identifiers.org/pubmed/17412958
comment: Inositol hexakisphosphate kinase 1 (IP6K1) and 3 (IP6K3) phosphorylate inositol 1,2,3,4,5,6-hexakisphosphate (IP6) to inositol 5-diphospho-1,2,3,4,6-pentakisphosphate (5-PP-IP5). The following lists the above proteins with their corresponding literature references: IP6K1 (Saiardi et al. 2001, Mulugu et al. 2007, Draskovic et al. 2008; Lin et al. 2009) and IP6K3 (Saiardi et al. 2001, Draskovic et al. 2008).

http://identifiers.org/pubmed/9748295
type: PublicationXref
id: 9748295
author: Brown, MS
author: Guryev, O
author: Goldstein, JL
author: Pai, JT
db: Pubmed
title: Differential stimulation of cholesterol and unsaturated fatty acid biosynthesis in cells expressing individual nuclear sterol regulatory element-binding proteins
source: J Biol Chem 273:26138-48
year: 1998

phosphoribosyl pyrophosphate synthetase holoenzyme
type: Complex
data source: Provenance1
member physical entity: phosphoribosyl pyrophosphate synthetase 1 holoenzyme (name copied from entity in Homo sapiens)
xref: UnificationXref2561
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3659325

NUDT4:Mg2+/Mn2+ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry738
component stoichiometry: Stoichiometry739
component: Note: the coordinates are copied over from Homo sapiens.
component: SmallMolecule133
xref: UnificationXref2646
cellular location: GO:0005829
comment: Reactome DB_ID: 3664568

NUDT(1)
type: Complex
data source: Provenance1
member physical entity: NUDT10:Mg2+/Mn2+ (name copied from entity in Homo sapiens)
member physical entity: NUDT4:Mg2+/Mn2+ (name copied from entity in Homo sapiens)
member physical entity: NUDT3:Mg2+ (name copied from entity in Homo sapiens)
xref: UnificationXref2663
cellular location: GO:0005829
display name: DIPP
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3664571

SREBP1A/2:NF-Y:HMGCR gene (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry754
component stoichiometry: Stoichiometry750
component stoichiometry: Stoichiometry756
component: PhysicalEntity126
component: SREBP1A/2 Dimer (name copied from entity in Homo sapiens)
component: NF-Y (name copied from entity in Homo sapiens)
xref: UnificationXref2866
cellular location: GO:0005654
comment: Reactome DB_ID: 3664220

UnificationXref4594
type: UnificationXref
id: REACT_26668
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_26668.2

ACAT1 tetramer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry748
component: Q9UQW6
xref: UnificationXref2823
cellular location: GO:0005759
comment: Reactome DB_ID: 3658308

UnificationXref4595
type: UnificationXref
id: 3663599
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663599

SREBP1A/2 Dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry755
component: PhysicalEntity127
xref: UnificationXref2865
cellular location: GO:0005654
comment: Reactome DB_ID: 3664219

UnificationXref4596
type: UnificationXref
id: REACT_110784
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_110784.9

NF-Y (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry753
component stoichiometry: Stoichiometry751
component stoichiometry: Stoichiometry752
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2863
cellular location: GO:0005654
comment: Reactome DB_ID: 3664213

UnificationXref4597
type: UnificationXref
id: 29408
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29408

NUDT10:Mg2+/Mn2+ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry743
component stoichiometry: Stoichiometry742
component: SmallMolecule133
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2662
cellular location: GO:0005829
comment: Reactome DB_ID: 3664570

UnificationXref4590
type: UnificationXref
id: 965053
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=965053

NUDT3:Mg2+ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry741
component stoichiometry: Stoichiometry740
component: Note: the coordinates are copied over from Homo sapiens.
component: SmallMolecule49
xref: UnificationXref2660
cellular location: GO:0005829
comment: Reactome DB_ID: 3664566

UnificationXref4591
type: UnificationXref
id: REACT_26765
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_26765.2

Btn-ACACA:2Mn2+ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry745
component stoichiometry: Stoichiometry746
component: SmallMolecule134
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2811
cellular location: GO:0005829
comment: Reactome DB_ID: 3659959

UnificationXref4592
type: UnificationXref
id: CHEBI:28803
db: ChEBI

Citrate lyase homotetramer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry744
component: ATP citrate lyase
xref: UnificationXref2729
cellular location: GO:0005829
comment: Reactome DB_ID: 3659941

UnificationXref4593
type: UnificationXref
id: 964952
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=964952

UnificationXref4598
type: UnificationXref
id: REACT_3714
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3714.1

UnificationXref4599
type: UnificationXref
id: Q9UTQ1
db: UniProt

http://identifiers.org/pubmed/9706223
type: PublicationXref
id: 9706223
author: Kerner, J
author: Hoppel, C
db: Pubmed
title: Genetic disorders of carnitine metabolism and their nutritional management.
source: Annu Rev Nutr 18:179-206
year: 1998

PGM2:Mg++ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry727
component stoichiometry: Stoichiometry726
component: Note: the coordinates are copied over from Homo sapiens.
component: SmallMolecule49
xref: UnificationXref2440
cellular location: GO:0005829
comment: Reactome DB_ID: 3657996

8xUGP2 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry728
component: Homologues of UGP2(2-508)
xref: UnificationXref2454
cellular location: GO:0005829
comment: Reactome DB_ID: 3658009

phosphoglucomutase
type: Complex
data source: Provenance1
member physical entity: PGM1:Mg++ (name copied from entity in Homo sapiens)
member physical entity: PGM2:Mg++ (name copied from entity in Homo sapiens)
xref: UnificationXref2441
cellular location: GO:0005829
display name: PGM1, PGM2
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3657997

PGM1:Mg++ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry725
component stoichiometry: Stoichiometry724
component: SmallMolecule49
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2437
cellular location: GO:0005829
comment: Reactome DB_ID: 3657991

monomethylated residue
type: SequenceModificationVocabulary
xref: UnificationXref5688

phosphoribosyl pyrophosphate synthetase 1 holoenzyme (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry737
component: O94413
xref: UnificationXref2556
cellular location: GO:0005829
comment: Reactome DB_ID: 3659324

RPE dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry736
component: O14105
xref: UnificationXref2517
cellular location: GO:0005829
comment: Reactome DB_ID: 3658447

PGD dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry735
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2509
cellular location: GO:0005829
comment: Reactome DB_ID: 3658440

G6PD tetramer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry733
component stoichiometry: Stoichiometry734
component: SmallMolecule46
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2491
cellular location: GO:0005829
comment: Reactome DB_ID: 3658035

G6PD dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry731
component stoichiometry: Stoichiometry732
component: SmallMolecule46
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2490
cellular location: GO:0005829
comment: Reactome DB_ID: 3658034

G6PD dimer and tetramer
type: Complex
data source: Provenance1
member physical entity: G6PD dimer (name copied from entity in Homo sapiens)
member physical entity: G6PD tetramer (name copied from entity in Homo sapiens)
xref: UnificationXref2492
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658036

GALE dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry729
component stoichiometry: Stoichiometry730
component: Homologues of GALE
component: SmallMolecule71
xref: UnificationXref2480
cellular location: GO:0005829
comment: Reactome DB_ID: 3658027

UniProt:P36592
type: ProteinReference
xref: UnificationXref221
organism: BioSource1

GOT2 dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry717
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2383
cellular location: GO:0005759
comment: Reactome DB_ID: 3658237

UnificationXref4570
type: UnificationXref
id: CHEBI:17310
db: ChEBI

UniProt:P36590
type: ProteinReference
xref: UnificationXref4444
organism: BioSource1

Intrinsic Pathway for Apoptosis
type: Pathway
data source: Provenance1
pathway component: REACT 131602.5
evidence: Evidence325
xref: RelationshipXref130
xref: UnificationXref2127
xref: UnificationXref2128
pathway order: PathwayStep317
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

malate dehydrogenase 2 dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry716
component: Q9Y7R8
xref: UnificationXref2368
cellular location: GO:0005759
comment: Reactome DB_ID: 3658356

UnificationXref4571
type: UnificationXref
id: 965131
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=965131

fructose-1,6-bisphosphatase isoforms
type: Complex
data source: Provenance1
member physical entity: FBP2 tetramer (name copied from entity in Homo sapiens)
member physical entity: FBP1 tetramer (name copied from entity in Homo sapiens)
xref: UnificationXref2424
cellular location: GO:0005829
display name: FBP tetramer
comment: Reactome DB_ID: 3658115
comment: Converted from EntitySet in Reactome

UnificationXref4572
type: UnificationXref
id: REACT_25477
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_25477.2

UniProt:P36596
type: ProteinReference
xref: UnificationXref2986
organism: BioSource1

GOT1 dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry719
component stoichiometry: Stoichiometry718
component: Note: the coordinates are copied over from Homo sapiens.
component: SmallMolecule99
xref: UnificationXref2399
cellular location: GO:0005829
comment: Reactome DB_ID: 3658228

UnificationXref4573
type: UnificationXref
id: O74860
db: UniProt

UniProt:P36595
type: ProteinReference
xref: UnificationXref378
organism: BioSource1

FBP2 tetramer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry722
component stoichiometry: Stoichiometry723
component: SmallMolecule49
component: P09202
xref: UnificationXref2423
cellular location: GO:0005829
comment: Reactome DB_ID: 3658114

UnificationXref4574
type: UnificationXref
id: 3663590
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663590

UniProt:P36594
type: ProteinReference
xref: UnificationXref368
organism: BioSource1

FBP1 tetramer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry721
component stoichiometry: Stoichiometry720
component: P09202
component: SmallMolecule49
xref: UnificationXref2421
cellular location: GO:0005829
comment: Reactome DB_ID: 3658112

UnificationXref4575
type: UnificationXref
id: O14242
db: UniProt

UnificationXref4576
type: UnificationXref
id: 3663594
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663594

UnificationXref4577
type: UnificationXref
id: 3663595
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663595

UnificationXref4578
type: UnificationXref
id: 3663596
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663596

UniProt:O42991
type: ProteinReference
xref: UnificationXref1970
organism: BioSource1

UnificationXref4579
type: UnificationXref
id: 3663600
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663600

cholest-5-en-3beta-ol
type: SmallMoleculeReference
name: cholesterol
name: cholesterol [ChEBI:16113]
xref: UnificationXref3122

Phosphatidyl-N-trimethylethanolamine
type: SmallMoleculeReference
name: Choline phosphatide
name: 1,2-diacyl-sn-glycero-3-phosphocholine
name: Phosphatidylcholine
name: Lecithin
name: lecithins
name: L-alpha-phosphatidylcholine
name: 1,2-diacyl-sn-glycero-3-phosphocholines
name: PC
name: (3-sn-phosphatidyl)choline
name: 1,2-diacyl-sn-glycero-3-phosphocholine [ChEBI:16110]
xref: UnificationXref3168

Dihydroxyacetone phosphate
type: SmallMoleculeReference
name: Glycerone phosphate
name: Dihydroxyacetone phosphate [ChEBI:16108]
xref: UnificationXref2254

UnificationXref4581
type: UnificationXref
id: CHEBI:16410
db: ChEBI

UnificationXref4582
type: UnificationXref
id: 964945
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=964945

UniProt:P36582
type: ProteinReference
xref: UnificationXref784
organism: BioSource1

UnificationXref4580
type: UnificationXref
id: REACT_88519
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_88519.9

UniProt:P36584
type: ProteinReference
xref: UnificationXref1941
organism: BioSource1

UnificationXref4585
type: UnificationXref
id: 965146
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=965146

UniProt:P36583
type: ProteinReference
xref: UnificationXref786
organism: BioSource1

UnificationXref4586
type: UnificationXref
id: REACT_26021
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_26021.2

UniProt:P36586
type: ProteinReference
xref: UnificationXref910
organism: BioSource1

UnificationXref4583
type: UnificationXref
id: REACT_26830
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_26830.2

UniProt:P36585
type: ProteinReference
xref: UnificationXref2011
organism: BioSource1

UnificationXref4584
type: UnificationXref
id: CHEBI:18335
db: ChEBI

UnificationXref4589
type: UnificationXref
id: CHEBI:16709
db: ChEBI

UnificationXref4587
type: UnificationXref
id: 3663598
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663598

UnificationXref4588
type: UnificationXref
id: REACT_140311
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_140311.5

Evidence310
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16391004
xref: http://identifiers.org/pubmed/15460540
xref: http://identifiers.org/pubmed/12704645
xref: http://identifiers.org/pubmed/12440953
comment: RNA elements rich in adenine and uracil residues (AU-rich elements) bind specific proteins which either target the RNA for degradation or, more rarely, stabilize the RNA. The activity of the AU-element binding proteins is regulated, usually by phosphorylation but also by subcellular localization.

Evidence314
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17352659
xref: http://identifiers.org/pubmed/18447580
xref: http://identifiers.org/pubmed/17531985
xref: http://identifiers.org/pubmed/20795950
xref: http://identifiers.org/pubmed/19359157
xref: http://identifiers.org/pubmed/18256688
xref: http://identifiers.org/pubmed/19859661
xref: http://identifiers.org/pubmed/17671086
xref: http://identifiers.org/pubmed/18447585
comment: Nonsense-mediated decay has been observed with mRNAs that do not have an exon junction complex (EJC) downstream of the termination codon (reviewed in Isken and Maquat 2007, Chang et al. 2007, Behm-Ansmant et al. 2007, Rebbapragada and Lykke-Andersen 2009, Nicholson et al. 2010). In these cases the trigger is unknown but a correlation with the length of the 3' UTR has sometimes been seen. The current model posits a competition between PABP and UPF1 for access to eRF3 at the terminating ribosome (Ivanov et al. 2008, Singh et al. 2008, reviewed in Bhuvanagiri et al. 2010). Abnormally long 3' UTRs may prevent PABP from efficiently interacting with eRF3 and allow UPF1 to bind eRF3 instead. Long UTRs with hairpin loops may bring PABP closer to eRF3 and help evade NMD (Eberle et al. 2008). The pathway of degradation taken during EJC-independent NMD has not been elucidated. It is thought that phosphorylation of UPF1 by SMG1 and recruitment of SMG6 or SMG5 and SMG7 are involved, as with EJC-enhanced NMD, but this has not yet been shown.

Evidence313
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18447580
xref: http://identifiers.org/pubmed/18230761
xref: http://identifiers.org/pubmed/16622410
xref: http://identifiers.org/pubmed/21029861
xref: http://identifiers.org/pubmed/18256688
xref: http://identifiers.org/pubmed/18447585
comment: Nonsense-mediated decay of an mRNA can be triggered even if the termination codon does not precede an exon junction (Buhler et al. 2006, Eberle et al. 2008, Silva et al. 2008, Singh et al. 2008, Ivanov et al. 2008). UPF1 and PABP seem to modulate the efficiency of translation termination and PABP in the proximity of a termination codon prevents NMD likely by outcompeting UPF1 for interaction with eRF3 (Singh et al. 2008, Ivanov et al. 2008, Silva et al. 2008). Factors in the competition may be the length and secondary structure of the 3' UTR (Buhler et al. 2006, Eberle et al. 2008). UPF1 preferentially binds some but not all longer UTRs (Hogg and Goff 2010). Interaction of eRF3 with PABP stimulates ribosome dissociation and initiation of a new round of translation on the mRNA. Interaction of eRF3 with UPF1 appears to promote nonsense-mediated decay. It is possible but not yet demonstrated that all components of the SURF complex (SMG1, UPF1, eRF1, eRF3) are assembled on an mRNA without an exon junction complex and that UPF1 is phosphorylated by SMG1.

Evidence312
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17352659
xref: http://identifiers.org/pubmed/17531985
xref: http://identifiers.org/pubmed/19410547
xref: http://identifiers.org/pubmed/20795950
xref: http://identifiers.org/pubmed/19359157
xref: http://identifiers.org/pubmed/19859661
xref: http://identifiers.org/pubmed/21496649
xref: http://identifiers.org/pubmed/17671086
comment: During normal translation termination eRF3 associates with the ribosome and then interacts with PABP bound to the polyadenylate tail of the mRNA to release the ribosome and allow a new round of translation to commence. Nonsense-mediated decay (NMD) is triggered if eRF3 at the ribosome interacts with UPF1, which may compete with PABP (reviewed in Isken and Maquat 2007, Chang et al. 2007, Behm-Ansmant et al. 2007, Rebbapragada and Lykke-Andersen 2009, Bhuvanagiri et al. 2010, Nicholson et al. 2010, Durand and Lykke-Andersen 2011). An exon junction located 50-55 nt downstream of a termination codon is observed to enhance NMD. Exon-junction complexes (EJCs) are deposited on the mRNA during splicing in the nucleus, remain on mRNAs after transport to the cytosol, and are dislodged by the ribosome as it progresses along the mRNA during the pioneer round of translation (Gehring et al. 2009). EJCs contain the core factors eIF4A-III, Magoh-Y14, and CASC3 as well as the peripheral factors RNPS1, UPF2, and UPF3. UPF2 and UPF3 recruit UPF1 to eRF3 at the terminating ribosome. Thus an EJC downstream of a termination codon will not have been dislodged during translation and will recruit UPF1, triggering NMD. UPF1 is believed to form a complex containing SMG1, SMG8, and SMG9. In the key regulatory step of NMD SMG1 phosphorylates UPF1. The phosphorylated UPF1 then recruits either SMG6 or SMG5 and SMG7. SMG6 is itself an endoribonuclease that cleaves the mRNA. SMG5 and SMG7 do not have endoribonuclease activty, but are thought to recruit ribonucleases. Nonsense-mediated decay has been observed to involve deadenlyation, decapping, and both 5' to 3' and 3' to 5' exonuclease activities, but the exact degradative pathways taken by a given mRNA are not yet known. UPF1 also plays roles in Staufen-mediated decay, histone mRNA decay, telomere maintenance, genome integrity, and may play a role in normal termination of translation.

Evidence311
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/20817927
xref: http://identifiers.org/pubmed/14636577
xref: http://identifiers.org/pubmed/11544179
xref: http://identifiers.org/pubmed/19359157
xref: http://identifiers.org/pubmed/19417104
xref: http://identifiers.org/pubmed/16452507
xref: http://identifiers.org/pubmed/11331269
comment: SMG1 phosphorylates UPF1 in vitro and in vivo (Denning et al. 2001, Yamashita et al. 2001, Kashima et al. 2006). Serines 1073, 1078, 1096, and 1116 in isoform 2 (Serines 1084, 1089, 1107, 1127 in isoform 1) are phosphorylated in vitro and phosphorylation at serines 1078 and 1096 has been confirmed in vivo (Yamashita et al. 2001, Ohnishi et al. 2003, Kashima et al. 2006). UPF1 also contains additional serine and threonine residues that could be phosphorylated. SMG8 and SMG9 associate with SMG1 and regulate the kinase activity of SMG1 (Yamashita et al. 2009). The phosphorylation reaction is rate-limiting in nonsense-mediated decay and is therefore regarded as a licensing step (reviewed in Rebbapragada and Lykke-Andersen 2009). Phosphorylation is enhanced by the exon junction complex, which can interact with UPF1 via UPF2 and/or UPF3 (Kashima et al. 2006, Ivanov et al. 2008) or via Y14:Magoh (Ivanov et al. 2008). SMG8 and SMG9 bind SMG1 and regulate its kinase activity (Yamashita et al. 2009, Fernandez et al. 2011).

Evidence318
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/2408761
comment: Poly(A) polymerase has no specificity for any particular RNA sequence, as well as a very low affinity for the RNA. Under physiological conditions, the activity of poly(A) polymerase depends on two auxiliary factors, both of which bind to specific RNA sequences and recruit the poly(A) polymerase by a direct contact. One of these proteins is the heterotetrameric CPSF, which binds the AAUAAA sequence and is also essential for 3' cleavage.

Evidence317
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: RNA metabolism consists of both mRNA degradative pathways and non-coding RNA metabolism. Non-coding RNA metabolism includes the processing and packaging of the small nuclear ribonucleoproteins (snRNPs).

Evidence316
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Once synthesized mRNA can be utilized until degraded. Degradation itself is the final mode of gene expression regulation.

Evidence315
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17352659
xref: http://identifiers.org/pubmed/17531985
xref: http://identifiers.org/pubmed/20795950
xref: http://identifiers.org/pubmed/19010255
xref: http://identifiers.org/pubmed/19359157
xref: http://identifiers.org/pubmed/19859661
xref: http://identifiers.org/pubmed/18524595
xref: http://identifiers.org/pubmed/21496649
xref: http://identifiers.org/pubmed/17671086
comment: The Nonsense-Mediated Decay (NMD) pathway activates the destruction of mRNAs containing premature termination codons (PTCs) (reviewed in Isken and Maquat 2007, Chang et al. 2007, Behm-Ansmant et al. 2007, Neu-Yilik and Kulozik 2008, Rebbapragada and Lykke-Andersen 2009, Bhuvanagiri et al. 2010, Nicholson et al. 2010, Durand and Lykke-Andersen 2011). In mammalian cells a termination codon can be recognized as premature if it precedes an exon-exon junction by at least 50-55 nucleotides or if it is followed by an abnormal 3' untranslated region (UTR). While length of the UTR may play a part, the qualifications for being "abnormal" have not been fully elucidated. Also, some termination codons preceding exon junctions are not degraded by NMD so the criteria for triggering NMD are not yet fully known (reviewed in Rebbapragada and Lykke-Andersen 2009). While about 30% of disease-associated mutations in humans activate NMD, about 10% of normal human transcripts are also degraded by NMD (reviewed in Stalder and Muhlemann 2008, Neu-Yilik and Kulozik 2008, Bhuvanagiri et al. 2010, Nicholson et al. 2010). Thus NMD is a normal physiological process controlling mRNA stability in unmutated cells. Exon junction complexes (EJCs) are deposited on an mRNA during splicing in the nucleus and are displaced by ribosomes during the first round of translation. When a ribosome terminates translation the A site encounters the termination codon and the eRF1 factor enters the empty A site and recruits eRF3. Normally, eRF1 cleaves the translated polypeptide from the tRNA in the P site and eRF3 interacts with Polyadenylate-binding protein (PABP) bound to the polyadenylated tail of the mRNA. During activation of NMD eRF3 interacts with UPF1 which is contained in a complex with SMG1, SMG8, and SMG9. NMD can arbitrarily be divided into EJC-enhanced and EJC-independent pathways. In EJC-enhanced NMD, an exon junction is located downstream of the PTC and the EJC remains on the mRNA after termination of…

Evidence319
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11909521
comment: The 3' ends of eukaryotic mRNAs are generated by posttranscriptional processing of an extended primary transcript. For almost all RNAs, 3' processing consists of two steps: The mRNA is first cleaved at a particular phosphodiester bond downstream of the coding sequence. The upstream fragment then receives a poly(A) tail of approximately 250 adenylate residues whereas the downstream fragment is degraded. The two partial reactions are coupled so that reaction intermediates are usually undetectable. While 3' processing can be studied as an isolated event in vitro, it appears to be connected to transcription, splicing and transcription termination in vivo.

Evidence301
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19239894
xref: http://identifiers.org/pubmed/17245413
xref: http://identifiers.org/pubmed/20584987
xref: http://identifiers.org/pubmed/11283721
xref: http://identifiers.org/pubmed/16141059
xref: http://identifiers.org/pubmed/14749774
xref: http://identifiers.org/pubmed/15475613
comment: Degradation of mRNA from 5' to 3' occurs in three steps. First, the mRNA is bound at its 3' end by the Lsm1-7 complex. The bound Lsm1-7 may prevent nucleases from accessing the 3' end. Second, the 7-methylguanosine cap of the mRNA is hydrolyzed by the DCP1-DCP2 complex. Third, the 5' end of the decapped mRNA is attacked by the XRN1 exoribonuclease which digests the remainder of the mRNA from 5' to 3'. These processes may be physically connected by PATL1, the homolog of yeast Pat1, which stably binds the Lsm1-7 complex and interacts with the DCP1-DCP2 decapping complex and the Ccr4-NOT deadenylation complex (Ozgur et al. 2010).

Evidence300
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19239894
xref: http://identifiers.org/pubmed/17245413
xref: http://identifiers.org/pubmed/11283721
xref: http://identifiers.org/pubmed/12515382
xref: http://identifiers.org/pubmed/16141059
xref: http://identifiers.org/pubmed/14749774
xref: http://identifiers.org/pubmed/15475613
xref: http://identifiers.org/pubmed/16299471
comment: The XRN1 exoribonuclease hydrolyzes decapped mRNA from 5' to 3' and yields ribonucleotides having 5'-monophosphates. In yeast Xrn1 associates with the Lsm1-7 complex.

Evidence303
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12819195
xref: http://identifiers.org/pubmed/8246982
xref: http://identifiers.org/pubmed/11124962
xref: http://identifiers.org/pubmed/15257295
xref: http://identifiers.org/pubmed/18240226
xref: http://identifiers.org/pubmed/12819194
xref: http://identifiers.org/pubmed/10559216
xref: http://identifiers.org/pubmed/9346902
xref: http://identifiers.org/pubmed/14976220
xref: http://identifiers.org/pubmed/17486099
xref: http://identifiers.org/pubmed/19074427
xref: http://identifiers.org/pubmed/18573886
xref: http://identifiers.org/pubmed/12944492
comment: AUF1 monomers form dimers which bind the U-rich sequences in AU-rich elements of mRNAs. Binding of the mRNA causes the dimers of AUF1 to form tetramers. Nonphosphorylated AUF1 isoform p40 causes the mRNA to form a rigid structure whereas p40 that is phosphorylated at serines 83 and 87 does not. This difference may cause nonphosphorylated p40 to fail to destabilize the bound mRNA.

Evidence302
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19239894
xref: http://identifiers.org/pubmed/17245413
xref: http://identifiers.org/pubmed/11283721
xref: http://identifiers.org/pubmed/16141059
xref: http://identifiers.org/pubmed/14749774
xref: http://identifiers.org/pubmed/15475613
comment: After undergoing rounds of translation, mRNA is normally destroyed by the deadenylation-dependent pathway. Though the trigger is unclear, deadenylation likely proceeds in two steps: one catalyzed by the PAN2-PAN3 complex that shortens the poly(A) tail from about 200 adenosine residues to about 80 residues and one catalyzed by the CCR4-NOT complex or by the PARN enzyme that shortens the tail to about 10-15 residues. After deadenylation the mRNA is then hydrolyzed by either the 5' to 3' pathway or the 3' to 5' pathway. It is unknown what determinants target a mRNA to one pathway or the other. The 5' to 3' pathway is initiated by binding of the Lsm1-7 complex to the 3' oligoadenylate tail followed by decapping by the DCP1-DCP2 complex. The 5' to 3' exoribonuclease XRN1 then hydrolyzes the remaining RNA. The 3' to 5' pathway is initiated by the exosome complex at the 3' end of the mRNA. The exosome processively hydrolyzes the mRNA from 3' to 5', leaving only a capped oligoribonucleotide. The cap is then removed by the scavenging decapping enzyme DCPS.

Evidence305
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12819195
xref: http://identifiers.org/pubmed/16391004
xref: http://identifiers.org/pubmed/12704645
xref: http://identifiers.org/pubmed/10205060
xref: http://identifiers.org/pubmed/18573886
xref: http://identifiers.org/pubmed/12440953
comment: AUF1 (hnRNP D0) dimers bind U-rich regions of AU-rich elements (AREs) in the 3' untranslated regions of mRNAs. The binding causes AUF1 dimers to assemble into higher order tetrameric complexes. Diphosphorylated AUF1 bound to RNA recruits additional proteins, including eIF4G, polyA-binding protein, Hsp, Hsc70, Hsp27, NSEP-1, NSAP-1, and IMP-2 which target the mRNA and AUF1 for degradation. Unphosphorylated AUF1 is thought to be less able to recruit additional proteins. AUF1 also interacts directly or indirectly with HuR and the RNA-induced silencing complex (RISC). AUF1 complexed with RNA and other proteins is ubiquitinated and targeted for destruction by the proteasome while the bound mRNA is degraded. Inhibition of ubiquitin addition to AUF1 blocks mRNA degradation. The mechanism by which ubiquitin-dependent proteolysis is coupled to mRNA degradation is unknown. At least 4 isoforms of AUF1 exist: p45 (45 kDa) contains all exons, p42 lacks exon 2, p40 lacks exon 7, and p37 lacks exons 2 and 7. The presence of exon 7 in p42 and p45 seems to block ubiquitination while the absence of exon 7 (p37 and p40) targets AUF1 for ubiquitination and destabilizes bound RNAs. Lack of exon 2 (p37 and p42) is associated with higher affinity for RNA and 14-3-3sigma. AUF1 binds and destabilizes mRNAs encoding Interleukin-1 beta (IL1B), Tumor Necrosis Factor alpha (TNFA), Cyclin-dependent kinase inhibitor 1 (CDNK1A, p21), Cyclin-D1 (CCND1), Granulocyte-macrophage colony stimulating factor (GM-CSF, CSF2), inducible Nitric oxide synthase (iNOS, NOS2), Proto-oncogene cFos (FOS), Myc proto-oncogene (MYC), Apoptosis regulator Bcl-2 (BCL2).

Evidence304
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11842200
xref: http://identifiers.org/pubmed/15257295
xref: http://identifiers.org/pubmed/10205060
xref: http://identifiers.org/pubmed/12136087
comment: Ubiquitin-dependent proteolysis of AUF1 and nuclease-dependent destruction of AUF1-bound mRNA are coupled in an unknown way. It is possible that ubiquitinated AUF1 targets other members of the AUF1 and signal transduction regulated complex (ASTRC), such as polyA-binding protein, for degradation and this renders the mRNA susceptible to nucleases.

Evidence307
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16391004
xref: http://identifiers.org/pubmed/15687258
xref: http://identifiers.org/pubmed/12704645
xref: http://identifiers.org/pubmed/12440953
xref: http://identifiers.org/pubmed/11719186
comment: Butyrate Response Factor 1 (BRF1, ZFP36L1, not to be confused with transcription factor IIIB) binds AU-rich elements in the 3' region of mRNAs. After binding, BRF1 recruits exonucleases (XRN1 and the exosome) and decapping enzymes (DCP1a and DCP2) to hydrolyze the RNA. The ability of BRF1 to direct RNA degradation is controlled by phosphorylation of BRF1. Protein kinase B/AKT1 phosphorylates BRF1 at serines 92 and 203. Phosphorylated BRF1 can still bind RNA but is sequestered by binding 14-3-3 protein, preventing BRF1 from destabilizing RNA. BRF1 is also phosphorylated by MK2 at serines 54, 92, 203, and at an unknown site in the C-terminus. It is unknown if this particular phosphorylated form of BRF1 binds 14-3-3.

Evidence306
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17030608
xref: http://identifiers.org/pubmed/18326031
xref: http://identifiers.org/pubmed/15538381
xref: http://identifiers.org/pubmed/12198173
comment: Butyrate response factor 1 (BRF1) binds AU-rich elements in the 3' untranslated region of mRNAs.

Evidence309
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16391004
xref: http://identifiers.org/pubmed/18481987
xref: http://identifiers.org/pubmed/12704645
xref: http://identifiers.org/pubmed/12440953
comment: Tristetraproline (TTP) binds RNAs that contain AU-rich elements and recruits enzymes that degrade RNA. TTP interacts with the exosome (3' to 5' exonuclease), XRN1 (5' to 3' exonuclease), and the decapping enzymes DCP1 and DCP2a. The activity of TTP is regulated by phosphorylation. MK2 phosphorylates TTP, which then binds 14-3-3.The interaction with 14-3-3 prevents phosphorylated TTP from entering stress granules and stabilizes mRNA bound by phosphorylated TTP. Tristetraproline is known to bind AU-rich elements in the following mRNAs: Tumor necrosis factor alpha (TNFA), Granulocyte-macrophage colony stimulating factor (CSF2, GM-CSF), Interleukin-2 (IL-2), and Proto-oncogene C-FOS (FOS, c-fos). Mice deficient in TTP exhibit arthritis, weight loss, skin lesions, autoimmunity, and myeloid hyperplasia.

Evidence308
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17133347
xref: http://identifiers.org/pubmed/12324455
xref: http://identifiers.org/pubmed/18367721
xref: http://identifiers.org/pubmed/12639954
xref: http://identifiers.org/pubmed/12705825
xref: http://identifiers.org/pubmed/17369404
xref: http://identifiers.org/pubmed/10330172
xref: http://identifiers.org/pubmed/12646273
xref: http://identifiers.org/pubmed/19729507
xref: http://identifiers.org/pubmed/15117938
comment: Tristetraprolin (TTP) binds UUAUUUAUU motifs in the AU-rich elements of mRNAs. TTP binds Transportin-1 (Importin beta-2) which plays a role in shuttling TTP between P-bodies and stress granules.

Glucuronidation
type: Pathway
data source: Provenance1
pathway component: REACT 77971.9
evidence: Evidence826
xref: RelationshipXref755
xref: UnificationXref5446
xref: UnificationXref5447
pathway order: PathwayStep816
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Evidence336
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/6466686
xref: http://identifiers.org/pubmed/1697585
xref: http://identifiers.org/pubmed/9427547
comment: Extracellular trehalose, a disaccharide, is cleaved by trehalase associated with the plasma membrane to yield two molecules of glucose. Trehalase has been purified to homogeneity from rabbit intestine and shown to be a monomer attached to the plasma membrane by a GPI anchor (Galand 1984; Ruf et al. 1990). A human cDNA encoding a closely homologous protein has been cloned and the protein product of the clone has been shown to have trehalase activity in vitro (Ishihara et al. 1997). The human enzyme has not been characterized further, and so both the posttranslational modifications of the human enzyme and its activity in vivo have been inferred from the properties of the well studied rabbit enzyme.

Evidence335
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/14561771
xref: http://identifiers.org/pubmed/12209154
xref: http://identifiers.org/pubmed/12505355
xref: http://identifiers.org/pubmed/15218528
xref: http://identifiers.org/pubmed/12189384
xref: http://identifiers.org/pubmed/4561027
xref: http://identifiers.org/pubmed/14634621
comment: Apoptosis is a distinct form of cell death that is functionally and morphologically different from necrosis. Nuclear chromatin condensation, cytoplasmic shrinking, dilated endoplasmic reticulum, and membrane blebbing characterize apoptosis in general. Mitochondria remain morphologically unchanged. In 1972 Kerr et al introduced the concept of apoptosis as a distinct form of "cell-death", and the mechanisms of various apoptotic pathways are still being revealed today. The two principal pathways of apoptosis are (1) the Bcl-2 inhibitable or intrinsic pathway induced by various forms of stress like intracellular damage, developmental cues, and external stimuli and (2) the caspase 8/10 dependent or extrinsic pathway initiated by the engagement of death receptors The caspase 8/10 dependent or extrinsic pathway is a death receptor mediated mechanism that results in the activation of caspase-8 and caspase-10. Activation of death receptors like Fas/CD95, TNFR1, and the TRAIL receptor is promoted by the TNF family of ligands including FASL (APO1L OR CD95L), TNF, LT-alpha, LT-beta, CD40L, LIGHT, RANKL, BLYS/BAFF, and APO2L/TRAIL. These ligands are released in response to microbial infection, or as part of the cellular, humoral immunity responses during the formation of lymphoid organs, activation of dendritic cells, stimulation or survival of T, B, and natural killer (NK) cells, cytotoxic response to viral infection or oncogenic transformation. The Bcl-2 inhibitable or intrinsic pathway of apoptosis is a stress-inducible process, and acts through the activation of caspase-9 via Apaf-1 and cytochrome c. The rupture of the mitochondrial membrane, a rapid process involving some of the Bcl-2 family proteins, releases these molecules into the cytoplasm. Examples of cellular processes that may induce the intrinsic pathway in response to various damage signals include: auto reactivity in lymphocytes, cytokine deprivation, calcium flux or cellular damage by cytotoxic drugs like taxol,…

Evidence334
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11432772
xref: http://identifiers.org/pubmed/12724336
comment: A regulated balance between cell survival and apoptosis is essential for normal development and homeostasis of multicellular organisms (see Matsuzawa, 2001). Defects in control of this balance may contribute to autoimmune disease, neurodegeneration and cancer. Protein ubiquitination and degradation is one of the major mechanisms that regulate apoptotic cell death (reviewed in Yang and Yu 2003).

Evidence333
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12853446
xref: http://identifiers.org/pubmed/9786869
comment: Stimulation of cell death by PAK-2 requires the generation and stabilization of the caspase-activated form, PAK-2p34 (Walter et al., 1998;Jakobi et al., 2003). Levels of proteolytically activated PAK-2p34 protein are controlled by ubiquitin-mediated proteolysis. PAK-2p34 but not full-length PAK-2 is degraded by the 26 S proteasome (Jakobi et al., 2003). It is not known whether ubiquitination and degradation of PAK-2p34 occurs in the cytoplasm or in the nucleus.

Evidence332
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12853446
comment: Proteolytically activated PAK-2p34, but not full-length PAK-2, is degraded rapidly by the proteasome (Jakobi et al., 2003). Here, degradation of PAK-2p34 is described as occurring in the cytosol. However, to date it is not known whether this occurs in the nucleus or in the cytoplasm.

Evidence331
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12655297
comment: In the execution phase of apoptosis, effector caspases cleave vital cellular proteins leading to the morphological changes that characterize apoptosis. These changes include destruction of the nucleus and other organelles, DNA fragmentation, chromatin condensation, cell shrinkage and cell detachment and membrane blebbing (reviewed in Fischer et al., 2003).

Evidence330
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12668660
comment: Adenoviral expression of the BAP31 cleavage product, p20 causes early release of Ca2+ from the ER, concomitant uptake of Ca2+ into mitochondria, and recruitment of Drp1 to the mitochondria (Breckenridge et al., 2003) . Drp1 mediates scission of the outer mitochondrial membrane, resulting in dramatic fragmentation and fission of the mitochondrial network .

Evidence339
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10601273
comment: Free glucokinase (GCK1) leaves the nucleus via the nuclear pore. While the GCK1 protein contains a nuclear export sequence motif, the molecular details of the GCK1 export process remain to be worked out (Shiota et al. 1999).

Evidence338
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9493266
xref: http://identifiers.org/pubmed/7150652
xref: http://identifiers.org/pubmed/8325892
xref: http://identifiers.org/pubmed/11780755
xref: http://identifiers.org/pubmed/8786021
xref: http://identifiers.org/pubmed/1871135
comment: Cytosolic glucokinase and the three isoforms of hexokinase catalyze the irreversible reaction of glucose and ATP to form glucose 6 phosphate and ADP. In the body glucokinase is found only in hepatocytes and pancreatic beta cells. Glucokinase and the hexokinase enzymes differ in that glucokinase has a higher Km than the hexokinases and is less readily inhibited by the reaction product. As a result, glucokinase should be inactive in the fasting state when glucose concentrations are low but in the fed state should have an activity proportional to glucose concentration. These features are thought to enable efficient glucose uptake and retention in the liver, and to function as a sensor of glucose concentration coupled to insulin release in pancreatic beta cells (Thorens 2001). Glucokinase mutations are associated with MODY2, a heritable early onset form of type II diabetes (Tanizawa et al. 1991; Takeda et al. 1993). Three human hexokinase enzymes have been characterized, HK1 (Aleshin et al. 1998), HK2 (Lehto et al. 1995), and HK3 (Rijksen at al. 1982).

Evidence337
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref545
comment: Carbohydrate is a major component of the human diet, and includes starch (amylose and amylopectin) and disaccharides such as sucrose, lactose, maltose and, in small amounts, trehalose. The digestion of starch begins with the action of amylase enzymes secreted in the saliva and small intestine, which convert it to maltotriose, maltose, limit dextrins, and some glucose. Digestion of the limit dextrins and disaccharides, both dietary and starch-derived, to monosaccharides - glucose, galactose, and fructose - is accomplished by enzymes located on the luminal surfaces of enterocytes lining the microvilli of the small intestine (Semenza et al. 2001).

Evidence323
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12941691
xref: http://identifiers.org/pubmed/12660240
comment: Permeabilization of the outer mitochondrial membrane by pro-apoptotic BCL2 family proteins, such as BAK and BAX, allows cytochrome c eflux from the mitochondrial intermembrane space into the cytosol (Arnoult et al. 2003).

Evidence322
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Post-transcriptional splicing of introns is affected neither by the elongating properties of RNA polymerase II, nor by the binding of splicing regulatory factors to the enzyme. It is only affected by the relative abundance of constitutive and/or regulatory splicing factors at the sites where splicing takes place. Nevertheless it is important to point out that cytological evidence indicates that unspliced or partially spliced pre-mRNAs do not diffuse in the nucleoplasm far from the transcription sites. Therefore, recruitment of splicing factors to transcription sites would still favor the post-transcriptional splicing of introns.

Evidence325
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12042762
xref: http://identifiers.org/pubmed/14561771
xref: http://identifiers.org/pubmed/11711427
xref: http://identifiers.org/pubmed/15077149
xref: http://identifiers.org/pubmed/14634621
comment: The intrinsic (Bcl-2 inhibitable or mitochondrial) pathway of apoptosis functions in response to various types of intracellular stress including growth factor withdrawal, DNA damage, unfolding stresses in the endoplasmic reticulum and death receptor stimulation. Following the reception of stress signals, proapoptotic BCL-2 family proteins are activated and subsequently interact with and inactivate antiapoptotic BCL-2 proteins. This interaction leads to the destabilization of the mitochondrial membrane and release of apoptotic factors. These factors induce the caspase proteolytic cascade, chromatin condensation, and DNA fragmentation, ultimately leading to cell death. The key players in the Intrinsic pathway are the Bcl-2 family of proteins that are critical death regulators residing immediately upstream of mitochondria. The Bcl-2 family consists of both anti- and proapoptotic members that possess conserved alpha-helices with sequence conservation clustered in BCL-2 Homology (BH) domains. Proapoptotic members are organized as follows: 1. "Multidomain" BAX family proteins such as BAX, BAK etc. that display sequence conservation in their BH1-3 regions. These proteins act downstream in mitochondrial disruption. 2. "BH3-only" proteins such as BID,BAD, NOXA, PUMA,BIM, and BMF have only the short BH3 motif. These act upstream in the pathway, detecting developmental death cues or intracellular damage. Anti-apoptotic members like Bcl-2, Bcl-XL and their relatives exhibit homology in all segments BH1-4. One of the critical functions of BCL-2/BCL-XL proteins is to maintain the integrity of the mitochondrial outer membrane.

Evidence324
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10913597
xref: http://identifiers.org/pubmed/12941691
xref: http://identifiers.org/pubmed/12660240
xref: http://identifiers.org/pubmed/15077149
comment: Apoptotic factors released from the mitochondria promote apoptosis through several different mechanisms. Cytochrome C participates in Apoptosome driven effector caspase activation while SMAC relieves IAP mediated caspase inhibition.

Evidence320
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11031238
xref: http://identifiers.org/pubmed/10571029
xref: http://identifiers.org/pubmed/12242288
xref: http://identifiers.org/pubmed/12408966
xref: http://identifiers.org/pubmed/7597053
comment: Co-transcriptional pre-mRNA splicing is not obligatory. Pre-mRNA splicing begins co-transcriptionally and often continues post-transcriptionally. Human genes contain an average of nine introns per gene, which cannot serve as splicing substrates until both 5' and 3' ends of each intron are synthesized. Thus the time that it takes for pol II to synthesize each intron defines a minimal time and distance along the gene in which splicing factors can be recruited. The time that it takes for pol II to reach the end of the gene defines the maximal time in which splicing could occur co-transcriptionally. Thus, the kinetics of transcription can affect the kinetics of splicing. There are two classes of intronless pre-mRNAs (mRNAs expressed from genes that lack introns). The first class encodes the replication dependent histone mRNAs. These mRNAs have unique 3' ends that do not have a polyA tail. The replication dependent histone mRNAs in all metazoans, as well as Chlamydomonas and Volvox fall into this class. The second class of mRNAs end in polyA tails, which are formed by a mechanism similar to that which poly-adenylate pre-mRNAs containing introns. In the intronless genes there is a different method of replacing the 3' splice site that activates polyadenylation.

Evidence327
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12853446
comment: The subcellular localization of PAK-2 is controlled by nuclear localization and nuclear export signal motifs (Jakobi et al.,2003). The regulatory domain contains a nuclear export signal motif that prevents the nuclear accumulation of full-length PAK-2. The activating proteolytic cleavage disrupts the nuclear export signal in PAK-2 and removes most its regulatory domain. The resulting activated PAK-2p34 fragment contains a nuclear localization signal and translocates to and is retained in the nucleus (Jakobi et al.,2003).

Evidence326
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9786869
comment: Activation of PAK-2p34 coincides with autophosphorylation of Thr 402 in the the catalytic domain (Walter et al., 1998).

Evidence329
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15471851
xref: http://identifiers.org/pubmed/12853446
xref: http://identifiers.org/pubmed/15234964
xref: http://identifiers.org/pubmed/9786869
comment: In response to stress signals, the p21-activated protein kinase PAK-2 stimulates a cell death response characterized by increased cell rounding and apoptotic chromatin condensation (see Jakobi et al., 2003). PAK-2 is proteolytically cleaved by caspase-3 producing a constitutively active fragment, PAK-2p34. Following cleavage, PAK-2p34 is autophosphorylated at Thr 402 and transported to the nucleus where it accumulates due to the loss of its nuclear export signal motif (Jakobi et al., 2003). The activity of PAK-2p34 appears to be regulated both by proteosomal degradation (Jakobi et al., 2003) and by association with the GTPase-activating protein PS-GAP/ RHG-10. This interaction inhibits the kinase activity of PAK-2p34 and changes the localization of PAK-2p34 from the nucleus to the perinuclear region (Koeppel et al., 2004). PAK-2p34 may function in the down-regulation of translation initiation in apoptosis through phosphorylation of Mnk1 (Orton et al.,2004).

Evidence328
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10075701
xref: http://identifiers.org/pubmed/16204230
comment: Inactive PAK-2 can be partially autophosphorylated in the regulatory region without being activated (Gatti et al. 1999).

http://identifiers.org/pubmed/12450384
type: PublicationXref
id: 12450384
author: Zhang, Y
author: Desharnais, J
author: Beardsley, GP
author: Wilson, IA
author: Greasley, SE
author: Boger, DL
db: Pubmed
title: Crystal structures of human GAR Tfase at low and high pH and with substrate beta-GAR
source: Biochemistry 41:14206-14215
year: 2002

http://identifiers.org/pubmed/2780561
type: PublicationXref
id: 2780561
author: Moyzis, RK
author: Ratliff, RL
author: Meyne, J
db: Pubmed
title: Conservation of the human telomere sequence (TTAGGG)n among vertebrates
source: Proc Natl Acad Sci U S A 86:7049-53
year: 1989

http://identifiers.org/pubmed/12721290
type: PublicationXref
id: 12721290
author: Maness, PF
author: Richter, M
author: Midkiff, BR
author: Buhusi, M
author: Gates, AM
author: Schachner, M
db: Pubmed
title: Close homolog of L1 is an enhancer of integrin-mediated cell migration
source: J Biol Chem 278:25024-31
year: 2003

UnificationXref6888
type: UnificationXref
id: 1217510
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1217510

UnificationXref6889
type: UnificationXref
id: REACT_117054
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_117054.2

Evidence359
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8571957
xref: http://identifiers.org/pubmed/6434534
comment: The reversible conversion of glyceraldehyde-3-phosphate to dihydroxyacetone phosphate is catalyzed by cytosolic triose phosphate isomerase (Watanabe et al. 1996; Lu et al. 1984).

UnificationXref6886
type: UnificationXref
id: REACT_117645
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_117645.1

Pyridoxal 5'-phosphate
type: SmallMoleculeReference
name: Pyridoxal 5-phosphate
name: Pyridoxal phosphate
name: Pyridoxal phosphate [ChEBI:18405]
xref: UnificationXref2396

UnificationXref6887
type: UnificationXref
id: CHEBI:5674
db: ChEBI

Evidence353
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/4052435
comment: Mitochondrial aspartate aminotransferase catalyzes the reversible reaction of oxaloacetate and glutamate to form aspartate and 2-oxoglutarate (alpha-ketoglutarate) (Martini et al. 1985). The active form of the enzyme is inferred to be a dimer with one molecule of pyridoxal phosphate associated with each monomer.

UnificationXref6880
type: UnificationXref
id: REACT_116266
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_116266.1

Evidence354
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/2241899
comment: Cytosolic aspartate aminotransferase (glutamate oxaloacetate transaminase 1 - GOT1) catalyzes the reversible reaction of aspartate and 2-oxoglutarate (alpha-ketoglutarate) to form oxaloacetate and glutamate (Doyle et al. 1990). Unpublished crystallographic data (PBD 3IIO) suggest the enzyme is a homodimer).

UnificationXref6881
type: UnificationXref
id: CHEBI:65324
db: ChEBI

Evidence351
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10229653
xref: http://identifiers.org/pubmed/12437512
comment: The carboxylation of pyruvate to form oxaloacetate, catalyzed by mitochondrial pyruvate carboxylase, is an irreversible and allosterically regulated reaction (Jitrapakdee and Wallace 1999).

Evidence352
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16740313
xref: http://identifiers.org/pubmed/9792106
comment: Mitochondrial malate dehydrogenase catalyzes the reversible reaction of oxaloacetate and NADH + H+ to form malate and NAD+ (Luo et al. 2006). Unpublished crystallographic data indicate that the protein is a dimer (PDB 3E04).

Evidence357
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7391027
xref: http://identifiers.org/pubmed/6771269
comment: Cytosolic phosphoglycerate kinase complexed with magnesium catalyzes the reversible phosphorylation of 3-phosphoglycerate to form 1,3-bisphosphoglycerate (Huang et al. 1980a, 1980b).

UnificationXref6884
type: UnificationXref
id: CHEBI:5292
db: ChEBI

Evidence358
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10714828
xref: http://identifiers.org/pubmed/7144574
xref: http://identifiers.org/pubmed/183598
xref: http://identifiers.org/pubmed/3170585
comment: The reversible reduction of 1,3-bisphosphoglycerate to form glyceraldehyde-3-phosphate is catalyzed by cytosolic glyceraldehyde-3-phosphate dehydrogenase tetramer. There are multiple human glyceraldehyde 3-phosphate dehydrogenase-like pseudogenes, but only one glyceraldehyde 3-phosphate dehydrogenase gene expressed in somatic tissue (Benham and Povey 1989). Consistent with this conclusion, the homogeneous enzymes purified from various human tissues had indistinguishable physical and immunochemical properties (Heinz and Freimuller 1982), and studies of human erythrocytes of various ages suggested that variant forms of the enzyme arise as a result of post-translational modifications (Edwards et al. 1976). There is, however, an authentic second isoform of glyceraldehyde 3-phosphate dehydrogenase whose expression is confined to spermatogenic cells of the testis (Welch et al. 2000).

UnificationXref6885
type: UnificationXref
id: 1217505
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1217505

Evidence355
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8666394
xref: http://identifiers.org/pubmed/11945784
xref: http://identifiers.org/pubmed/11946196
xref: http://identifiers.org/pubmed/9254007
xref: http://identifiers.org/pubmed/4719206
comment: SLC25A1, in the inner mitochondrial membrane, mediates the exchange of cytosolic citrate for mitochondrial phosphoenolpyruvate. The exchange is physiologically irreversible because of the potential of the inner mitochondrial membrane. The gene encoding human SLC25A1 has been cloned and its expression pattern has been characterized (Heisterkamp et al. 1995; Iacobazzi et al. 1997), but the biochemical details of the transport process are inferred from those worked out for the well-characterized rat system (Robinson 1971; Soling et al. 1971; Kleineke et al. 1973).

UnificationXref6882
type: UnificationXref
id: 1217507
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1217507

http://identifiers.org/pubmed/12766759
type: PublicationXref
id: 12766759
author: Inohara, N
author: Nunez, G
db: Pubmed
title: NODs: intracellular proteins involved in inflammation and apoptosis
source: Nat Rev Immunol 3:371-82
year: 2003

Evidence356
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7689884
xref: http://identifiers.org/pubmed/11506403
xref: http://identifiers.org/pubmed/3208766
xref: http://identifiers.org/pubmed/3529090
xref: http://identifiers.org/pubmed/2462567
comment: Cytosolic enolase dimer catalyzes the reversible reaction of phosphoenolpyruvate and water to form 2-phosphoglycerate. Three enolase isozymes have been purified and biochemically characterized. The alpha isoform is widely expressed (Giallongo et al. 1986). The beta isoform is expressed in muscle. Evidence for its function in vivo in humans comes from studies of a patient in whom a point mutation in the gene encoding the enzyme was associated specifically with reduced enolase activity in muscle extracts, and with other symptoms consistent with a defect in glycolysis (Comi et al. 2001). The gamma isoform of human enolase is normally expressed in neural tissue. It is not known to have distinctive biochemical functions, but is of possible clinical interest as a marker of some types of neuroendocrine and lung tumors (McAleese et al. 1988). Verma and Kurl (1993) identifed a possible fourth isoform, a "lung-specific" enolase whose expression is increased in response to dexamethasone treatment. The protein has not been biochemically characterized, however, nor have the levels of mRNA and protein in other tissues been examined. Thus, the observation that this protein is particularly similar in its predicted amino acid sequence to a duck crystallin (Wistow et al. 1988) raises the possibility that its normal function is unrelated to glycolysis.

UnificationXref6883
type: UnificationXref
id: REACT_116852
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_116852.3

http://identifiers.org/pubmed/10441588
type: PublicationXref
id: 10441588
author: Li, TK
author: Chen, CC
author: Wang, MF
author: Chen, YC
author: Chang, YC
author: Yin, SJ
author: Lu, RB
db: Pubmed
title: Interaction between the functional polymorphisms of the alcohol-metabolism genes in protection against alcoholism.
source: Am J Hum Genet 65:795-807
year: 1999

Evidence361
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/13538944
xref: http://identifiers.org/pubmed/7989588
xref: PublicationXref558
comment: The reversible isomerization of fructose-6-phosphate to form glucose-6-phosphate is catalyzed by cytosolic phosphoglucose isomerase (Noltman 1972; Xu and Beutler 1994; Tsuboi et al. 1958).

UniProt:Q09926
type: ProteinReference
xref: UnificationXref5807
organism: BioSource1

Evidence360
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9678974
xref: http://identifiers.org/pubmed/9382095
comment: Cytosolic fructose-1,6-bisphosphatase catalyzes the physiologically irreversible hydrolysis of fructose-1,6-bisphosphate to form fructose-6-phosphate and orthophosphate. In the body, two isoforms of the enzyme are expressed, one ubiquitous and one muscle-specific (Kikawa et al. 1997; Tillmann and Eschrich 1998).

UniProt:Q09925
type: ProteinReference
xref: UnificationXref3665
organism: BioSource1

UniProt:Q09924
type: ProteinReference
xref: UnificationXref7385
organism: BioSource1

5'-Phosphoribosyl-5-amino-4-imidazolecarboxamide
type: SmallMoleculeReference
name: 5-Phosphoribosyl-4-carbamoyl-5-aminoimidazole
name: 5-Aminoimidazole-4-carboxamide ribotide
name: 1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide [ChEBI:18406]
name: 5'-Phospho-ribosyl-5-amino-4-imidazole carboxamide
name: 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
name: 1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide
name: AICAR
name: 5'-phosphoribosyl-5-aminoimidazole-4-carboxamide
xref: UnificationXref4126

Evidence348
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/4413246
xref: http://identifiers.org/pubmed/11506403
xref: http://identifiers.org/pubmed/3529090
xref: http://identifiers.org/pubmed/3208766
xref: http://identifiers.org/pubmed/2462567
comment: Cytosolic enolase catalyzes the reversible reaction of 2 phosphoglycerate to form phosphoenolpyruvate and water, elevating the transfer potential of the phosphoryl group. Enolase is a homodimer and requires Mg++ for activity. Three isozymes have been purified and biochemically characterized. The alpha isoform is expressed in many normal human tissues (Giallongo et al. 1986). The beta isoform is expressed in muscle. Evidence for its function in vivo in humans comes from studies of a patient in whom a point mutation in the gene encoding the enzyme was associated specifically with reduced enolase activity in muscle extracts and with other symptoms consistent with a defect in glycolysis (Comi et al. 2001). The gamma isoform of human enolase is normally expressed in neural tissue and is of possible clinical interest as a marker of some types of neuroendocrine and lung tumors (McAleese et al. 1988). Biochemical studies of the homologous rat proteins indicate that both homo- and heterodimers of enolase form and are enzymatically active (Rider and Taylor 1974).

UnificationXref6875
type: UnificationXref
id: REACT_145271
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_145271.5

Evidence349
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3126495
xref: http://identifiers.org/pubmed/1896471
xref: http://identifiers.org/pubmed/18191611
xref: http://identifiers.org/pubmed/11960989
xref: http://identifiers.org/pubmed/2040271
xref: http://identifiers.org/pubmed/15982340
xref: http://identifiers.org/pubmed/15996096
comment: Cytosolic pyruvate kinase catalyzes the transfer of a high-energy phosphate from phosphoenolpyruvate to ADP, forming pyruvate and ATP. This reaction, an instance of substrate-level phosphorylation, is essentially irreversible under physiological conditions. Four isozymes of human pyruvate kinase have been described, L, R, M1 and M2. Isozymes L and R are encoded by alternatively spliced transcripts of the PKLR gene; isozymes M1 and M2 are encoded by alternatively spliced transcripts of PKM2. In the body, L pyruvate kinase is found in liver (Tani et al. 1988), R in red blood cells (Kanno et al. 1991), M1 in muscle, heart and brain (Takenaka et al. 1991), and M2 in early fetal tissues and tumors (e.g., Lee et al. 2008). In all cases, the active form of the enzyme is a homotetramer, activated by fructose 1,6-bisphosphate (Valentini et al. 2002; Dombrauckas et al. 2005). Mutations in PKLR have been associated with hemolytic anemias (e.g., Zanella et al. 2005).

UnificationXref6876
type: UnificationXref
id: 3661822
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661822

5'-Phosphoribosylformylglycinamidine
type: SmallMoleculeReference
name: 2-(Formamido)-N1-(5-phospho-D-ribosyl)acetamidine
name: 1-(5'-Phosphoribosyl)-N-formylglycinamidine
name: 2-(Formamido)-N1-(5'-phosphoribosyl)acetamidine
name: 5'-Phosphoribosylformylglycinamidine [ChEBI:18413]
name: 5'-Phosphoribosyl-N-formylglycinamidine
xref: UnificationXref4108

UnificationXref6877
type: UnificationXref
id: 3663726
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663726

UnificationXref6878
type: UnificationXref
id: CHEBI:64153
db: ChEBI

UnificationXref6879
type: UnificationXref
id: 1217506
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1217506

Evidence340
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10601273
xref: http://identifiers.org/pubmed/14627435
comment: Glucokinase (GCK1) is negatively regulated by glucokinase regulatory protein (GKRP), which reversibly binds the enzyme to form an inactive complex. Binding is stimulated by fructose 6-phosphate and sorbitol 6-phosphate (hence high concentrations of these molecules tend to reduce GCK1 activity) and inhibited by fructose 1-phosphate (hence a high concentration of this molecule tends to increase GCK1 activity). Once formed, the complex is translocated to the nucleus. In the presence of high glucose concentrations, the nuclear GCK1:GKRP complex dissociates, freeing GCK1 to return to the cytosol. The free GKRP is thought also to return to the cytosol under these conditions, but this return has not been confirmed experimentally. Possible physiological roles for this sequestration process are to decrease futile cycling between glucose and glucose 6 phosphate in hepatocytes under low-glucose conditions, and to decrease the lag between a rise in intracellular glucose levels and the onset of glucose phosphorylation in both hepatocytes and pancreatic beta cells (Brocklehurst et al. 2004; Shiota et al. 1999).

Evidence341
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11780753
comment: Cells take up glucose by facilitated diffusion, via glucose transporters (GLUTs) associated with the plasma membrane, a reversible reaction (Joost and Thorens 2001). Four tissue-specific GLUT isoforms are known. Glucose in the cytosol is phosphorylated by tissue-specific kinases to yield glucose 6-phosphate, which cannot cross the plasma membrane because of its negative charge. In the liver, this reaction is catalyzed by glucokinase which has a low affinity for glucose (Km about 10 mM) but is not inhibited by glucose 6-phosphate. In other tissues, this reaction is catalyzed by isoforms of hexokinase. Hexokinases are feedback-inhibited by glucose 6-phosphate and have a high affinity for glucose (Km about 0.1 mM). Liver cells can thus accumulate large amounts of glucose 6-phosphate but only when blood glucose concentrations are high, while most other tissues can take up glucose even when blood glucose concentrations are low but cannot accumulate much intracellular glucose 6-phosphate. These differences are consistent with the view that that the liver functions to buffer blood glucose concentrations, while most other tissues take up glucose to meet immediate metabolic needs. Glucose 6-phosphatase, expressed in liver and kidney, allows glucose 6-phosphate generated by gluconeogenesis (both tissues) and glycogen breakdown (liver) to leave the cell. The absence of glucose 6-phosphatase from other tissues makes glucose uptake by these tissues essentially irreversible, consistent with the view that cells in these tissues take up glucose for local metabolic use.

Evidence342
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16186415
xref: http://identifiers.org/pubmed/15546855
comment: Hexoses, notably fructose, glucose, and galactose, generated in the lumen of the small intestine by breakdown of dietary carbohydrate are taken up by enterocytes lining the microvilli of the small intestine and released from them into the blood. Uptake into enterocytes is mediated by two transporters localized on the lumenal surfaces of the cells, SGLT1 (glucose and galactose, together with sodium ions) and GLUT5 (fructose). GLUT2, localized on the basolateral surfaces of enterocytes, mediates the release of these hexoses into the blood (Wright et al. 2004). GLUT2 may also play a role in hexose uptake from the gut lumen into enterocytes when the lumenal content of monosaccharides is very high (e.g., Kellet and Brot-Laroche, 2005) and GLUT5 mediates fructose uptake from the blood into cells of the body, notably hepatocytes. Cells take up glucose by facilitated diffusion, via glucose transporters (GLUTs) associated with the plasma membrane, a reversible reaction. Four tissue-specific GLUT isoforms are known. Glucose in the cytosol is phosphorylated by tissue-specific kinases to yield glucose 6-phosphate, which cannot cross the plasma membrane because of its negative charge. In the liver, this reaction is catalyzed by glucokinase which has a low affinity for glucose (Km about 10 mM) but is not inhibited by glucose 6-phosphate. In other tissues, this reaction is catalyzed by isoforms of hexokinase. Hexokinases are feedback-inhibited by glucose 6-phosphate and have a high affinity for glucose (Km about 0.1 mM). Liver cells can thus accumulate large amounts of glucose 6-phosphate but only when blood glucose concentrations are high, while most other tissues can take up glucose even when blood glucose concentrations are low but cannot accumulate much intracellular glucose 6-phosphate. These differences are consistent with the view that that the liver functions to buffer blood glucose concentrations, while most other tissues take up glucose to meet immediate metabolic needs.…

Evidence343
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/13538944
xref: http://identifiers.org/pubmed/7989588
xref: PublicationXref561
xref: http://identifiers.org/pubmed/11371164
xref: PublicationXref558
comment: Cytosolic phosphoglucose isomerase catalyzes the reversible interconversion of glucose 6-phosphate and fructose 6-phosphate (Tsuboi et al. 1958; Noltmann 1972; Bloxham and Lardy 1973). The active form of the enzyme is a homodimer (Read et al. 2001). Mutations in the enzyme are associated with hemolytic anemia (Xu and Beutler 1994).

UnificationXref6870
type: UnificationXref
id: 3663746
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663746

Evidence344
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/6451249
xref: http://identifiers.org/pubmed/7825568
xref: http://identifiers.org/pubmed/6444721
xref: http://identifiers.org/pubmed/2960695
xref: http://identifiers.org/pubmed/8117307
comment: Cytosolic phosphofructokinase 1 catalyzes the reaction of fructose 6-phosphate and ATP to form fructose 1,6-bisphosphate and ADP. This reaction, irreversible under physiological conditions, is the rate limiting step of glycolysis. Phosphofructokinase 1 activity is allosterically regulated by ATP, citrate, and fructose 2,6-bisphosphate. Phosphofructokinase 1 is active as a tetramer (although higher order multimers, not annotated here, may form in vivo). Two isoforms of phosphofructokinase 1 monomer, L and M, are widely expressed in human tissues. Different tissues can contain different homotetramers or heterotetramers: L4 in liver, M4 in muscle, and all possible heterotetramers, L4, L3M, L2M2, LM3, and M4, in red blood cells, for example (Raben et al. 1995; Vora et al. 1980, 1987; Vora 1981). A third isoform, P, is abundant in platelets, where it is found in P4, P3L, P2L2, and PL3 tetramers (Eto et al. 1994; Vora et al. 1987).

UnificationXref6871
type: UnificationXref
id: REACT_128949
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_128949.5

Evidence345
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16511037
xref: http://identifiers.org/pubmed/6434534
comment: Cytosolic triose phosphate isomerase catalyzes the freely reversible interconversion of dihydroxyacetone phosphate and glyceraldehyde 3-phosphate (Lu et al. 1984). The active form of the enzyme is a homodimer (Kinoshita et al. 2005).

UnificationXref6872
type: UnificationXref
id: 3665543
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665543

Evidence346
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref570
xref: http://identifiers.org/pubmed/10714828
xref: http://identifiers.org/pubmed/7144574
xref: http://identifiers.org/pubmed/183598
xref: http://identifiers.org/pubmed/2793178
xref: http://identifiers.org/pubmed/3170585
xref: PublicationXref569
comment: Cytosolic glyceraldehyde 3-phosphate dehydrogenase catalyzes the reversible reaction of glyceraldehyde 3-phosphate, orthophosphate, and NAD+ to form NADH + H+ and 1,3-bisphosphoglycerate, the first energy rich intermediate of glycolysis. The biochemical details of this reaction were worked out by C and G Cori and their colleagues (Taylor et al. 1948; Cori et al. 1948). While there are multiple human glyceraldehyde 3-phosphate dehydrogenase-like pseudogenes, there is only one glyceraldehyde 3-phosphate dehydrogenase gene expressed in somatic tissue (Benham and Povey 1989; Heinz and Freimuller 1982; Ercolani et al. 1988), and studies of aged human erythrocytes suggest that variant forms of the enzyme arise as a result of post-translational modifications (Edwards et al. 1976). There is, however, an authentic second isoform of glyceraldehyde 3-phosphate dehydrogenase whose expression is confined to spermatogenic cells of the testis (Welch et al. 2000).

UnificationXref6873
type: UnificationXref
id: REACT_147435
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_147435.5

Evidence347
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7391027
xref: http://identifiers.org/pubmed/6771269
xref: http://identifiers.org/pubmed/5009693
comment: Cytosolic phosphoglycerate kinase catalyzes the reaction of ADP and 1,3-bisphosphoglycerate to form D glyceraldehyde 3-phosphate and ATP. The active form of the enzyme is a monomer and requires Mg++ (Yoshida and Watanabe 1972; Huang et al. 1980a,b). This is the first substrate level phosphorylation reaction in glycolysis.

UnificationXref6874
type: UnificationXref
id: 3665544
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665544

http://identifiers.org/pubmed/15809071
type: PublicationXref
id: 15809071
author: Ishibashi, K
author: Uchida, S
author: Ko, SB
author: Sasaki, S
author: Kuwahara, M
author: Rai, T
author: Itoh, T
db: Pubmed
title: Identification of a novel aquaporin, AQP12, expressed in pancreatic acinar cells
source: Biochem Biophys Res Commun 330:832-8
year: 2005

Evidence350
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16051738
comment: The reactions of glycolysis (e.g., van Wijk and van Solinge 2005) convert glucose 6-phosphate to pyruvate. The entire process is cytosolic. Glucose 6-phosphate is reversibly isomerized to form fructose 6-phosphate. Phosphofructokinase 1 catalyzes the physiologically irreversible phosphorylation of fructose 6-phosphate to form fructose 1,6-bisphosphate. In six reversible reactions, fructose 1,6-bisphosphate is converted to two molecules of phosphoenolpyruvate and two molecules of NAD+ are reduced to NADH + H+. Each molecule of phosphoenolpyruvate reacts with ADP to form ATP and pyruvate in a physiologically irreversible reaction. Under aerobic conditions the NADH +H+ can be reoxidized to NAD+ via electron transport to yield additional ATP, while under anaerobic conditions or in cells lacking mitochondria NAD+ can be regenerated via the reduction of pyruvate to lactate.

Evidence379
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/14988808
comment: The reversible interconversion of ribulose 5-phosphate and ribose 5-phosphate is catalyzed by cytosolic ribose 5-phosphate isomerase (Huck et al. 2004).

Evidence377
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8300619
xref: http://identifiers.org/pubmed/11283793
comment: Cytosolic transaldolase (TALDO1) catalyzes the reversible reaction of D-glyceraldehyde 3-phosphate and sedoheptulose 7-phosphate to form D-erythrose 4-phosphate and D-fructose 6-phosphate. Protein expressed from the cloned gene has been characterized biochemically (Banki et al. 1994) and transaldolase deficiency in a patient has been correlated with a mutation in the TALDO1 gene (Verhoeven et al. 2001).

Evidence378
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8300619
xref: http://identifiers.org/pubmed/11283793
comment: Cytosolic transaldolase (TALDO1) catalyzes the reversible reaction of D-erythrose 4-phosphate and D-fructose 6-phosphate to form D-glyceraldehyde 3-phosphate and sedoheptulose 7-phosphate. Protein expressed from the cloned gene has been characterized biochemically (Banki et al. 1994) and transaldolase deficiency in a patient has been correlated with a mutation in the TALDO1 gene (Verhoeven et al. 2001).

Evidence375
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/2581946
xref: http://identifiers.org/pubmed/7396409
comment: Cytosolic ribulose-5-phosphate-3-epimerase (RPE) catalyzes the reversible interconversion of D-ribulose 5-phosphate and D-xylulose 5-phosphate (Bose and 1985). The electrophoretic properties of RPE activity detected in extracts of mouse-human somatic cell hybrids suggest that the active form of the enzyme is a homodimer (Spencer and Hopkinson 1980).

Evidence376
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/2581946
xref: http://identifiers.org/pubmed/7396409
comment: Cytosolic ribulose-5-phosphate-3-epimerase (RPE) catalyzes the reversible interconversion of D-xylulose 5-phosphate and D-ribulose 5-phosphate (Bose and 1985). The electrophoretic properties of RPE activity detected in extracts of mouse-human somatic cell hybrids suggest that the active form of the enzyme is a homodimer (Spencer and Hopkinson 1980).

Evidence373
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3932573
xref: http://identifiers.org/pubmed/10518023
comment: Cytosolic 6-phosphogluconolactonase (PGLS) catalyzes the hydrolysis of D-glucono-1,5-lactone 6-phosphate to form 6-phospho-D-gluconate (Beutler and Kuhl 1985; Collard et al. 1999).

Evidence374
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3994686
xref: http://identifiers.org/pubmed/3932573
xref: http://identifiers.org/pubmed/9920387
comment: Cytosolic phosphogluconate dehydrogenase (PGD) catalyzes the reaction of 6-phospho-D-gluconate and NADP+ to form D-ribulose 5-phosphate, CO2, and NADPH + H+ (Beutler and Kuhl 1985; Rippa et al. 1998). The PGD enzyme is dimeric (Dallocchio et al. 1985).

Evidence383
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/4328836
comment: Cytosolic phophoribosyl pyrophosphate synthetase catalyzes the reaction of D-ribose 5-phosphate and ATP to form 5-phospho-alpha-D-ribose and AMP. Three isoforms of the enzyme have been described. The first has been purified and characterized biochemically (Fox and Kelley 1971). The others are known only as inferred protein products of cloned genes; their catalytic properties have not been determined.

http://identifiers.org/pubmed/17996737
type: PublicationXref
id: 17996737
author: Chacinska, A
author: Guiard, B
author: Milenkovic, D
author: Stojanovski, D
author: Müller, JM
author: Pfanner, N
db: Pubmed
title: The MIA system for protein import into the mitochondrial intermembrane space
source: Biochim Biophys Acta 1783:610-7
year: 2008

Evidence382
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/4328836
comment: Cytosolic phosphoribosyl pyrophosphate synthetase 1 catalyzes the reaction of D-ribose 5-phosphate and dATP to form 5-phospho-alpha-D-ribose 1-diphosphate and 2'-deoxyadenosine 5'-monophosphate. While phosphoribosyl pyrophosphate synthetase 1 works well with either ATP or dATP as a substrate in vitro, the extent of the dATP reaction in vivo is unclear, as cellular dATP concentrations are normally very low (Fox and Kelley 1971).

Evidence381
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3790084
xref: http://identifiers.org/pubmed/18987987
xref: http://identifiers.org/pubmed/5666113
comment: The pentose phosphate pathway is responsible for the generation of a substantial fraction of the cytoplasmic NADPH required for biosynthetic reactions, and for the generation of ribose 5-phosphate for nucleotide synthesis. Although the pentose phosphate pathway and glycolysis are distinct, they involve three common intermediates, glucose 6-phosphate, glyceraldehyde 3-phosphate, and fructose 6-phosphate, so the two pathways are interconnected. The pentose phosphate pathway consists of eight reactions:1. Conversion glucose 6-phosphate to D-glucono-1,5-lactone 6-phosphate, with the formation of NADPH; 2. Conversion of D-glucono-1,5-lactone 6-phosphate to 6-phospho-D-gluconate; 3. Conversion of 6-phospho-D-gluconate to ribulose 5-phosphate, with the formation of NADPH; 4. Conversion of ribulose 5-phosphate to xylulose 5-phosphate; 5. Conversion of ribulose 5-phosphate to ribose 5-phosphate; 6. Rearrangement of ribose 5-phosphate and xylulose 5-phosphate to form sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate; 7. Rearrangement of sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate to form erythrose 4-phosphate and fructose 6-phosphate; and 8. Rearrangement of xylulose 5-phosphate and erythrose 4-phosphate to form glyceraldehyde 3-phosphate and fructose-6-phosphate. The oxidative branch of the pentose phosphate pathway, reactions 1-3, generates NADPH and pentose 5-phosphate. The non-oxidative branch of the pathway, reactions 4-8, converts pentose 5-phosphate to other sugars. The overall pathway can operate to generate only NADPH (glucose 6-phosphate is converted to pentose 5-phosphates, which are directed to the synthesis of fructose 6-phosphate and glyceraldehyde 3-phosphate, which in turn are converted back to glucose 6-phosphate). The reactions of the non-oxidative branch can operate to generate net amounts of ribose 5-phosphate with no production of NADPH. Net flux through this network of reactions appears to depend on the metabolic state of the cell and…

Evidence380
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/14988808
comment: The reversible interconversion of ribose 5-phosphate and ribulose 5-phosphate is catalyzed by cytosolic ribose 5-phosphate isomerase (Huck et al. 2004).

UnificationXref6897
type: UnificationXref
id: REACT_131263
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_131263.5

UnificationXref6898
type: UnificationXref
id: 3665542
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665542

UnificationXref6899
type: UnificationXref
id: REACT_145098
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_145098.5

Evidence366
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7902568
comment: Cytosolic phosphoglucomutase (PGM) catalyzes the reversible conversion of glucose 1-phosphate to glucose 6-phosphate. Two PGM isoenzymes, both monomers, have been identified. PGM1 is the major form found in most tissues except erythrocytes, where PGM2 is abundant (March et al. 1993; Parrington et al. 1968; Putt et al. 1993). PGM2 also has substantial phosphopentomutase activity and its primary physiological in normal tissues in vivo is not clear.

UnificationXref6893
type: UnificationXref
id: 1217511
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1217511

Evidence367
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/4320262
xref: http://identifiers.org/pubmed/183599
comment: Glycogen breakdown occurs via the same chemical steps in all tissues but is separately regulated via tissue specific isozymes and signaling pathways that enable distinct physiological fates for liver glycogen and that in other tissues. Glycogen phosphorylase, which can be activated by phosphorylase kinase, catalyzes the removal of glucose residues as glucose 1-phosphate from the ends of glycogen branches. The final four residues of each branch are removed in two steps catalyzed by debranching enzyme, and further glycogen phosphorylase activity completes the process of glycogen breakdown. The figure shows the actions of phosphorylase and debranching enzyme. The first glucose residue in each branch is released as free glucose; all other residues are released as glucose 1-phosphate. The latter molecule can be converted to glucose 6-phosphate in a step shared with other pathways (Villar-Palasi and Larner 1970; Hers 1976).

UnificationXref6894
type: UnificationXref
id: REACT_117275
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_117275.1

Evidence368
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Glucose is the major form in which dietary sugars are made available to cells of the human body. Its breakdown is a major source of energy for all cells, and is essential for the brain and red blood cells. Glucose utilization begins with its uptake by cells and conversion to glucose 6-phosphate, which cannot traverse the cell membrane. Fates open to cytosolic glucose 6-phosphate include glycolysis to yield pyruvate, glycogen synthesis, and the pentose phosphate pathway. In some tissues, notably the liver and kidney, glucose 6-phosphate can be synthesized from pyruvate by the pathway of gluconeogenesis.

UnificationXref6895
type: UnificationXref
id: 3663727
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663727

Evidence369
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1897530
comment: Cytosolic galactose-1-phosphate uridylyltransferase (GALT) catalyzes the reaction of alpha-D-galactose 1-phosphate and UDP glucose to form D-glucose 1-phosphate and UDP galactose (Reichardt et al. 1991).

UnificationXref6896
type: UnificationXref
id: 3663728
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663728

Evidence362
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8379904
comment: The reactions of gluconeogenesis convert mitochondrial pyruvate to cytosolic glucose 6-phosphate which in turn can be hydrolyzed to glucose and exported from the cell. Gluconeogenesis is confined to cells of the liver and kidney and enables glucose synthesis from molecules such as lactate and alanine and other amino acids when exogenous glucose is not available (reviewed, e.g., by Gerich 1993). The process of gluconeogenesis as diagrammed below occurs in two parts: a network of reactions converts mitochondrial pyruvate to cytosolic phosphoenolpyruvate; then phosphoenolpyruvate is converted to glucose 6-phosphate in a single sequence of cytosolic reactions. Three variants of the first part of the process are physiologically important. 1) A series of transport and transamination reactions convert mitochondrial oxaloacetate to cytosolic oxaloacetate which is converted to phosphoenolpyruvate by a hormonally regulated, cytosolic isoform of phosphoenolpyruvate carboxykinase. This variant allows regulated glucose synthesis from lactate. 2) Mitochondrial oxaloacetate is reduced to malate, which is exported to the cytosol and re-oxidized to oxaloacetate. This variant provides reducing equivalents to the cytosol, needed for glucose synthesis from amino acids such as alanine and glutamine. 3) Constitutively expressed mitochondrial phosphoenolpyruvate carboxykinase catalyzes the conversion of mitochondrial oxaloacetate to phosphoenolpyruvate which is then transported to the cytosol. The exact path followed by any one molecule of pyruvate through this reaction network is determined by the tissue in which the reactions are occurring, the source of the pyruvate, and the physiological stress that triggered gluconeogenesis. In all cases, the synthesis of glucose from two molecules of pyruvate requires the generation and consumption of two reducing equivalents as cytosolic NADH + H+. For pyruvate derived from lactate (variants 1 and 3), NADH + H+ is generated with the oxidation of la…

Evidence363
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17804405
xref: http://identifiers.org/pubmed/8257433
xref: http://identifiers.org/pubmed/7902568
xref: http://identifiers.org/pubmed/1840235
comment: Cytosolic phosphoglucomutase (PGM) catalyzes the reversible conversion of glucose 6-phosphate to glucose 1-phosphate (Drago et al. 1991). Two PGM isoenzymes, both monomers, have been identified. PGM1 is the major form found in most tissues except erythrocytes, where PGM2 is abundant (March et al. 1993; Parrington et al. 1968; Putt et al. 1993). PGM2 also has substantial phosphopentomutase activity and its primary physiological in normal tissues in vivo is not clear.

UnificationXref6890
type: UnificationXref
id: CHEBI:71956
db: ChEBI

Evidence364
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8631325
xref: http://identifiers.org/pubmed/5348606
xref: http://identifiers.org/pubmed/5427280
comment: Cytosolic UDP-glucose pyrophosphorylase 2 (UGP2) catalyzes the reaction of UTP and glucose 1-phosphate to form UDP glucose and pyrophosphate (Knop and Hansen 1970; Duggleby et al. 1996). UGP2 is inferred to occur in the cell as a homooctamer from studies of its bovine homologue (Levine et al. 1969).

UnificationXref6891
type: UnificationXref
id: 1217514
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1217514

Evidence365
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/4320262
xref: http://identifiers.org/pubmed/15238248
xref: http://identifiers.org/pubmed/183599
comment: Glycogen, a highly branched glucose polymer, is formed and broken down in most human tissues, but is most abundant in liver and muscle, where it serves as a major stored fuel. Glycogen metabolism has been studied in most detail in muscle, although considerable experimental data are available concerning these reactions in liver as well. Glycogen metabolism in other tissues has not been studied as extensively, and is thought to resemble the muscle process (Hers 1976; Lomako et al. 2004; Villar-Palasi and Larner 1970). Glycogen synthesis involves five reactions. The first two, conversion of glucose 6-phosphate to glucose 1-phosphate and synthesis of UDP-glucose from glucose 1-phosphate and UTP, are shared with several other pathways. The next three reactions, the auto-catalyzed synthesis of a glucose oligomer on glycogenin, the linear extension of the glucose oligomer catalyzed by glycogen synthase, and the formation of branches catalyzed by glycogen branching enzyme, are unique to glycogen synthesis. These reactions are shown in the figure. Repetition of the last two reactions generates large, extensively branched glycogen polymers. The catalysis of several of these reactions by distinct isozymes in liver and muscle allows them to be regulated independently in the two tissues.

UnificationXref6892
type: UnificationXref
id: REACT_117607
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_117607.3

Evidence370
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15175331
xref: http://identifiers.org/pubmed/10801319
comment: Cytosolic UDP-galactose 4-epimerase catalyzes the interconversion of UDP-D-galactose and UDPglucose (Schulz et al. 2004). The active form of the enzyme is a homodimer with one molecule of bound NAD per monomer (Thoden et al. 2000).

Evidence372
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10745013
xref: http://identifiers.org/pubmed/5666113
comment: Cytosolic glucose-6-phosphate dehydrogenase (G6PD) catalyzes the reaction of glucose 6-phosphate and NADP+ to form D-glucono-1,5-lactone 6-phosphate and , and NADPH + H+. Biochemical studies indicate that both G6PD dimers and tetramers are catalytically active and capable or forming under physiological conditions in vivo (Au et al. 2000). Mutations that reduce the catalytic efficientcy of G6PD are remarkably common in human populations; these appear to have a protective effect against malaria (e.g., Luzzatto and Afolayan 1968).

Evidence371
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11261429
xref: PublicationXref621
comment: The main sources of galactose in the human diet are milk and milk products. The disaccharide lactose from these sources is hydrolyzed in the intestine to its constituent monosaccharides, glucose and galactose. Galactose is metabolized primarily in the liver in a sequence of three reactions that yield one molecule of glucose 1-phosphate per molecule of galactose. First, it is phosphorylated to yield galactose 1-phosphate. Then, galactose 1-phosphate and UDP-glucose react to form UDP-galactose and glucose 1-phosphate, and UDP-galactose undergoes epimerization to form UDP-glucose. In a reaction shared with other pathways, glucose 1-phosphate can be converted into glucose 6-phosphate (Holton et al. 2001; Elsas and Lai 2001).

UniProt:Q02592
type: ProteinReference
xref: UnificationXref6169
organism: BioSource1

http://identifiers.org/pubmed/18721752
type: PublicationXref
id: 18721752
author: Lane, WS
author: Kaushansky, A
author: MacBeath, G
author: Rush, J
author: Budnik, BA
author: Gordus, A
db: Pubmed
title: System-wide investigation of ErbB4 reveals 19 sites of Tyr phosphorylation that are unusually selective in their recruitment properties
source: Chem Biol 15:808-17
year: 2008

http://identifiers.org/pubmed/8682206
type: PublicationXref
id: 8682206
author: Authier, F
author: Bergeron, JJ
author: Posner, BI
db: Pubmed
title: Endosomal proteolysis of internalized proteins.
source: FEBS Lett 389:55-60
year: 1996

http://identifiers.org/pubmed/20494131
type: PublicationXref
id: 20494131
author: Welin, M
author: Nordlund, P
db: Pubmed
title: Understanding specificity in metabolic pathways--structural biology of human nucleotide metabolism
source: Biochem Biophys Res Commun 396:157-63
year: 2010

PublicationXref1332
type: PublicationXref
author: Parkinson, A
title: Casarett and Doull's Toxicology 5th Edn
source: 113-186
year: 1995

http://identifiers.org/pubmed/17567461
type: PublicationXref
id: 17567461
author: Lemasters, JJ
db: Pubmed
title: Modulation of mitochondrial membrane permeability in pathogenesis, autophagy and control of metabolism
source: J Gastroenterol Hepatol 22:S31-7
year: 2007

UnificationXref6841
type: UnificationXref
id: REACT_90753
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_90753.9

UnificationXref6840
type: UnificationXref
id: 3665243
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665243

UnificationXref6843
type: UnificationXref
id: REACT_142761
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_142761.5

UnificationXref6842
type: UnificationXref
id: 3665229
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665229

UnificationXref6845
type: UnificationXref
id: REACT_146142
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_146142.5

UnificationXref6844
type: UnificationXref
id: 3665230
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665230

UnificationXref6847
type: UnificationXref
id: REACT_137149
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_137149.5

UnificationXref6846
type: UnificationXref
id: 3665231
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665231

http://identifiers.org/pubmed/14624239
type: PublicationXref
id: 14624239
author: Ellison, V
author: Stillman, B
db: Pubmed
title: Biochemical characterization of DNA damage checkpoint complexes: clamp loader and clamp complexes with specificity for 5' recessed DNA
source: PLoS Biol 1:E33
year: 2003

UnificationXref6849
type: UnificationXref
id: REACT_130379
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_130379.5

UnificationXref6848
type: UnificationXref
id: 3665232
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665232

UnificationXref6839
type: UnificationXref
id: REACT_167179
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_167179.1

UnificationXref6830
type: UnificationXref
id: 3664923
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664923

PublicationXref1327
type: PublicationXref
author: Oesch, F
author: Arand, M
title: Toxicology
source: 83-107
year: 1999

UnificationXref6834
type: UnificationXref
id: 3665620
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665620

UnificationXref6833
type: UnificationXref
id: REACT_165765
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_165765.1

UnificationXref6832
type: UnificationXref
id: 3664925
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664925

UnificationXref6831
type: UnificationXref
id: 3664924
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664924

UnificationXref6838
type: UnificationXref
id: 3665245
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665245

UnificationXref6837
type: UnificationXref
id: REACT_168839
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_168839.1

UnificationXref6836
type: UnificationXref
id: 3665403
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665403

http://identifiers.org/pubmed/3594573
type: PublicationXref
id: 3594573
author: Rothman, JE
author: Gleason, ML
author: Serafini, TA
author: Wieland, FT
db: Pubmed
title: The rate of bulk flow from the endoplasmic reticulum to the cell surface
source: Cell 50:289-300
year: 1987

UnificationXref6835
type: UnificationXref
id: REACT_168232
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_168232.1

UnificationXref4608
type: UnificationXref
id: CHEBI:28911
db: ChEBI

UnificationXref4609
type: UnificationXref
id: 3000241
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3000241

UnificationXref4606
type: UnificationXref
id: 3665533
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665533

UnificationXref4607
type: UnificationXref
id: REACT_134129
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_134129.5

UnificationXref6861
type: UnificationXref
id: 3663735
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663735

UnificationXref6860
type: UnificationXref
id: 3663739
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663739

UnificationXref6863
type: UnificationXref
id: 3663731
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663731

UnificationXref6862
type: UnificationXref
id: 3663736
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663736

UnificationXref4601
type: UnificationXref
id: 3663605
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663605

UnificationXref6869
type: UnificationXref
id: 3663744
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663744

UnificationXref4600
type: UnificationXref
id: 3663604
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663604

UnificationXref6868
type: UnificationXref
id: 3663743
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663743

http://identifiers.org/pubmed/19531029
type: PublicationXref
id: 19531029
author: Kawamukai, Makoto
db: Pubmed
title: Biosynthesis and bioproduction of coenzyme Q10 by yeasts and other organisms
source: Biotechnol. Appl. Biochem. 53:217-26
year: 2009

Mg++
type: SmallMoleculeReference
name: Magnesium [ChEBI:18420]
name: Mg2+
name: Magnesium
xref: UnificationXref1219

UnificationXref4605
type: UnificationXref
id: REACT_126163
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_126163.5

UnificationXref6865
type: UnificationXref
id: 3663732
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663732

UnificationXref4604
type: UnificationXref
id: 3663607
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663607

UnificationXref6864
type: UnificationXref
id: 3663729
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663729

UnificationXref4603
type: UnificationXref
id: REACT_125943
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_125943.5

UnificationXref6867
type: UnificationXref
id: 3663733
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663733

UnificationXref4602
type: UnificationXref
id: 3663608
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663608

UnificationXref6866
type: UnificationXref
id: 3663730
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663730

http://identifiers.org/pubmed/15102545
type: PublicationXref
id: 15102545
author: Lewis, DF
db: Pubmed
title: 57 varieties: the human cytochromes P450
source: Pharmacogenomics 5:305-18
year: 2004

UnificationXref6852
type: UnificationXref
id: REACT_111691
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_111691.1

UnificationXref6851
type: UnificationXref
id: 1470067
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1470067

UnificationXref6850
type: UnificationXref
id: GO:0097013
db: GENE ONTOLOGY

UnificationXref6859
type: UnificationXref
id: 3663738
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663738

UnificationXref6858
type: UnificationXref
id: 3663737
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663737

http://identifiers.org/pubmed/16141215
type: PublicationXref
id: 16141215
author: Hutson, SM
author: Conway, ME
author: Goto, M
author: Islam, MM
author: Miyahara, I
author: Hirotsu, K
author: Yennawar, NH
db: Pubmed
title: Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin
source: J Biol Chem 280:37246-56
year: 2005

UnificationXref6857
type: UnificationXref
id: 3663734
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663734

2,2'-dilyso diphosphatidyl glycerol
type: SmallMoleculeReference
name: 2,2'-dilyso-1,3-diphosphatidylglycerol
name: 2,2'-dilyso cardiolipin [ChEBI:60431]
name: 2,2'-dilyso diphosphatidylglycerol
name: 2,2'-dilysocardiolipin
name: 2,2'-dilyso DPG
name: 2,2'-dilyso cardiolipin
name: dilyso cardiolipin
xref: UnificationXref3392

UnificationXref6856
type: UnificationXref
id: 3663742
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663742

MLCL
type: SmallMoleculeReference
name: lysoDPG
name: Monolysocardiolipin
name: monolyso cardiolipin [ChEBI:60430]
name: monolysoDPG
name: monolyso cardiolipin
xref: UnificationXref3384

UnificationXref6855
type: UnificationXref
id: 3663740
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663740

UnificationXref6854
type: UnificationXref
id: 3663741
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663741

UnificationXref6853
type: UnificationXref
id: GO:0030670
db: GENE ONTOLOGY

http://identifiers.org/pubmed/3539386
type: PublicationXref
id: 3539386
author: Wood, T
db: Pubmed
title: Physiological functions of the pentose phosphate pathway
source: Cell Biochem Funct 4:241-7
year: 1986

UnificationXref6807
type: UnificationXref
id: 2263486
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2263486

UnificationXref6806
type: UnificationXref
id: CHEBI:15354
db: ChEBI

UnificationXref6809
type: UnificationXref
id: 3664687
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664687

UnificationXref6808
type: UnificationXref
id: REACT_160541
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_160541.1

UnificationXref6800
type: UnificationXref
id: 3665487
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665487

http://identifiers.org/pubmed/10798271
type: PublicationXref
id: 10798271
author: Heindl, B
author: Zahler, S
author: Kupatt, C
author: Becker, BF
db: Pubmed
title: Endothelial function and hemostasis
source: Z Kardiol 89:160-7
year: 2000

UnificationXref6801
type: UnificationXref
id: REACT_163031
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_163031.2

UnificationXref6802
type: UnificationXref
id: 429802
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=429802

Deoxythymidylic acid
type: SmallMolecule
entity reference: CHEBI:17013
data source: Provenance1
name: dTMP
name: thymidylic acid
name: Thymidylate
name: 5'-Thymidylic acid
name: Thymidine 5'-phosphate
name: Deoxythymidine 5'-phosphate
name: thymidine 5'-monophosphate
name: Thymidine monophosphate
xref: UnificationXref4350
xref: UnificationXref4351
cellular location: GO:0005829
comment: Reactome DB_ID: 109366
display name: TMP

UnificationXref6803
type: UnificationXref
id: REACT_20271
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20271.2

(deoxy)cytidine
type: SmallMolecule
data source: Provenance1
member physical entity: Deoxycytidine
member physical entity: cytidine
xref: UnificationXref4365
xref: UnificationXref4366
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 500829

UnificationXref6804
type: UnificationXref
id: 1602448
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1602448

cytidine
type: SmallMolecule
entity reference: CHEBI:17562
data source: Provenance1
xref: UnificationXref4360
xref: UnificationXref4361
cellular location: GO:0005829
comment: Reactome DB_ID: 83949
display name: Cyt-Rib

UnificationXref6805
type: UnificationXref
id: REACT_123209
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_123209.1

Deoxycytidine
type: SmallMolecule
entity reference: CHEBI:15698
data source: Provenance1
name: 2'-deoxycytidine
xref: UnificationXref4364
xref: UnificationXref4363
cellular location: GO:0005829
comment: Reactome DB_ID: 109379
display name: dC

(deoxy)uridine
type: SmallMolecule
data source: Provenance1
member physical entity: 2-Deoxyuridine
member physical entity: uridine
xref: UnificationXref4373
xref: UnificationXref4374
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 500430

uridine
type: SmallMolecule
entity reference: CHEBI:16704
data source: Provenance1
xref: UnificationXref4369
xref: UnificationXref4368
cellular location: GO:0005829
comment: Reactome DB_ID: 83929
display name: Ura-Rib

2-Deoxyuridine
type: SmallMolecule
entity reference: CHEBI:16450
data source: Provenance1
name: 2'-deoxyuridine
name: Deoxyuridine
xref: UnificationXref4371
xref: UnificationXref4372
cellular location: GO:0005829
comment: Reactome DB_ID: 109383
display name: dU

(d)ADP
type: SmallMolecule
data source: Provenance1
member physical entity: 2'-deoxyadenosine 5'-diphosphate
member physical entity: SmallMolecule31
xref: UnificationXref4388
xref: UnificationXref4387
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 500087

2'-deoxyadenosine 5'-diphosphate
type: SmallMolecule
entity reference: 2'-deoxyadenosine 5'-diphosphate
data source: Provenance1
xref: UnificationXref4385
xref: UnificationXref4386
cellular location: GO:0005829
comment: Reactome DB_ID: 110090
display name: dADP

AMP, dAMP, CMP, dCMP
type: SmallMolecule
data source: Provenance1
member physical entity: SmallMolecule116
member physical entity: 2'-deoxycytidine 5'-monophosphate
member physical entity: SmallMolecule55
member physical entity: SmallMolecule54
xref: UnificationXref4402
xref: UnificationXref4403
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 500062
display name: (d)AMP, (d)CMP

N-carbamoyl-L-aspartate
type: SmallMolecule
entity reference: CHEBI:15859
data source: Provenance1
xref: UnificationXref4293
xref: UnificationXref4294
cellular location: GO:0005829
comment: Reactome DB_ID: 111628

(S)-4,5-dihydroorotate
type: SmallMolecule
entity reference: CHEBI:17025
data source: Provenance1
name: L-dihydroorotic acid
name: dihydro-L-orotic acid
name: (S)-dihydroorotate
xref: UnificationXref4299
xref: UnificationXref4298
cellular location: GO:0005829
comment: Reactome DB_ID: 76630
display name: L-dihydroorotate

uracil-6-carboxylic acid
type: SmallMolecule
entity reference: CHEBI:16742
data source: Provenance1
name: orotic acid
xref: UnificationXref4303
xref: UnificationXref4304
cellular location: GO:0005829
comment: Reactome DB_ID: 76632
display name: orotate

2'-deoxycytidine 5'-monophosphate
type: SmallMolecule
entity reference: CHEBI:15918
data source: Provenance1
name: Deoxycytidine monophosphate
name: Deoxycytidylate
name: deoxycytidylic acid
xref: UnificationXref4324
xref: UnificationXref4325
cellular location: GO:0005829
comment: Reactome DB_ID: 109378
display name: dCMP

http://identifiers.org/pubmed/10851172
type: PublicationXref
id: 10851172
author: Miller, FD
author: Kaplan, DR
db: Pubmed
title: Neurotrophin signal transduction in the nervous system
source: Curr Opin Neurobiol 10:381-91
year: 2000

2'-Deoxyuridine 5'-phosphate
type: SmallMolecule
entity reference: CHEBI:17622
data source: Provenance1
name: Deoxyuridine monophosphate
name: Deoxyuridine 5'-phosphate
name: 2'-deoxyuridine 5'-monophosphate
name: deoxyuridylic acid
xref: UnificationXref4327
xref: UnificationXref4328
cellular location: GO:0005829
comment: Reactome DB_ID: 109382
display name: dUMP

flavin mononucleotide
type: SmallMolecule
entity reference: CHEBI:17621
data source: Provenance1
name: riboflavin-5-phosphate
xref: UnificationXref4307
xref: UnificationXref4306
cellular location: GO:0005743
comment: Reactome DB_ID: 76629
display name: FMN

orotidine 5'-monophosphate
type: SmallMolecule
entity reference: CHEBI:15842
data source: Provenance1
name: orotidine 5'-phosphate
xref: UnificationXref4315
xref: UnificationXref4314
cellular location: GO:0005829
comment: Reactome DB_ID: 111629
display name: orotidylic acid

2'-Deoxyuridine 5'-phosphate
type: SmallMolecule
entity reference: CHEBI:17622
data source: Provenance1
name: Deoxyuridine monophosphate
name: Deoxyuridine 5'-phosphate
name: 2'-deoxyuridine 5'-monophosphate
name: deoxyuridylic acid
xref: UnificationXref4339
xref: UnificationXref4340
cellular location: GO:0005654
comment: Reactome DB_ID: 500742
display name: dUMP

7,8-Dihydrofolic acid
type: SmallMolecule
entity reference: CHEBI:15633
data source: Provenance1
name: Dihydrofolic acid
name: Dihydrofolate
name: 7,8-Dihydrofolate
xref: UnificationXref4348
xref: UnificationXref4347
cellular location: GO:0005829
comment: Reactome DB_ID: 73604
display name: DHF

2'-deoxyuridine 5'-triphosphate
type: SmallMolecule
entity reference: CHEBI:17625
data source: Provenance1
xref: UnificationXref4335
xref: UnificationXref4336
cellular location: GO:0005654
comment: Reactome DB_ID: 500739
display name: dUTP

Water
type: SmallMolecule
entity reference: CHEBI:15377
data source: Provenance1
xref: UnificationXref4337
xref: UnificationXref4338
cellular location: GO:0005654
comment: Reactome DB_ID: 113518
display name: H2O

2'-deoxyinosine
type: SmallMolecule
entity reference: 2'-deoxyinosine
data source: Provenance1
name: deoxyinosine
xref: UnificationXref4232
xref: UnificationXref4231
cellular location: GO:0005829
comment: Reactome DB_ID: 109331
display name: dI

inosine
type: SmallMolecule
entity reference: CHEBI:17596
data source: Provenance1
xref: UnificationXref4228
xref: UnificationXref4229
cellular location: GO:0005829
comment: Reactome DB_ID: 83927
display name: Ino

http://identifiers.org/pubmed/15509595
type: PublicationXref
id: 15509595
author: Elsässer, Hans-Peter
author: Mühlenhoff, Ulrich
author: Stehling, Oliver
author: Lill, R
author: Brückel, Bernd
db: Pubmed
title: Iron-sulfur protein maturation in human cells: evidence for a function of frataxin
source: Hum. Mol. Genet. 13:3007-15
year: 2004

UnificationXref6829
type: UnificationXref
id: 3664922
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664922

UnificationXref6828
type: UnificationXref
id: 3664920
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664920

UnificationXref6824
type: UnificationXref
id: 3665242
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665242

UnificationXref6825
type: UnificationXref
id: REACT_149800
db: Reactome
id version: 4
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_149800.4

UnificationXref6826
type: UnificationXref
id: 3665244
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665244

6-aminopurine
type: SmallMolecule
entity reference: CHEBI:16708
data source: Provenance1
name: adenine
xref: UnificationXref4239
xref: UnificationXref4238
cellular location: GO:0005829
comment: Reactome DB_ID: 83951
display name: Ade

UnificationXref6827
type: UnificationXref
id: REACT_168264
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_168264.1

UnificationXref6820
type: UnificationXref
id: 3665395
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665395

UnificationXref6821
type: UnificationXref
id: REACT_161975
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_161975.2

UnificationXref6822
type: UnificationXref
id: 3665241
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665241

UnificationXref6823
type: UnificationXref
id: REACT_127523
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_127523.5

http://identifiers.org/pubmed/18678926
type: PublicationXref
id: 18678926
author: Rajnarayanan, RV
author: Cohly, HH
author: Isokpehi, R
db: Pubmed
title: Compartmentalization of aquaporins in the human intestine
source: Int J Environ Res Public Health 5:115-9
year: 2008

Oxygen
type: SmallMolecule
entity reference: CHEBI:15379
data source: Provenance1
xref: UnificationXref4268
xref: UnificationXref4267
cellular location: GO:0005782
comment: Reactome DB_ID: 113535
display name: O2

NADPH
type: SmallMolecule
entity reference: CHEBI:16474
data source: Provenance1
xref: UnificationXref4270
xref: UnificationXref4269
cellular location: GO:0005782
comment: Reactome DB_ID: 113602
display name: TPNH

protoheme
type: SmallMolecule
entity reference: CHEBI:17627
data source: Provenance1
xref: UnificationXref4272
xref: UnificationXref4273
cellular location: GO:0005782
comment: Reactome DB_ID: 113569
display name: heme

carbamoyl phosphate
type: SmallMolecule
entity reference: CHEBI:17672
data source: Provenance1
xref: UnificationXref4286
xref: UnificationXref4285
cellular location: GO:0005829
comment: Reactome DB_ID: 111647
display name: CAP

Ammonia
type: SmallMolecule
entity reference: Ammonia
data source: Provenance1
xref: UnificationXref4253
xref: UnificationXref4252
cellular location: GO:0005829
comment: Reactome DB_ID: 29382
display name: NH3

Xanthine
type: SmallMolecule
entity reference: CHEBI:17712
data source: Provenance1
xref: UnificationXref4256
xref: UnificationXref4255
cellular location: GO:0005829
comment: Reactome DB_ID: 30064
display name: XAN

Hydrogen peroxide
type: SmallMolecule
entity reference: H2O2
data source: Provenance1
xref: UnificationXref4264
xref: UnificationXref4263
cellular location: GO:0005782
comment: Reactome DB_ID: 113575
display name: H2O2

H2O
type: SmallMolecule
entity reference: CHEBI:15377
data source: Provenance1
xref: UnificationXref4266
xref: UnificationXref4265
cellular location: GO:0005782
comment: Reactome DB_ID: 141343

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O94663
data source: Provenance1
name: SNF8_HUMAN
name: Vacuolar-sorting protein SNF8
name: O94663
name: VPS22
xref: UnificationXref8762
feature: FragmentFeature1356
cellular location: GO:0005829
comment: Reactome DB_ID: 3663460
display name: SNF8

Homologues of RPS27A(1-76)
type: Protein
data source: Provenance1
member physical entity: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref8768
cellular location: GO:0010008
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3663454

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O74967
data source: Provenance1
name: VPS25_HUMAN
name: Vacuolar protein-sorting-associated protein 25
name: O74967
xref: UnificationXref8758
feature: FragmentFeature1354
cellular location: GO:0005829
comment: Reactome DB_ID: 3663464
display name: VPS25

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: O43038
data source: Provenance1
name: VPS36_HUMAN
name: Vacuolar protein-sorting-associated protein 36
name: O43038
xref: UnificationXref8760
feature: FragmentFeature1355
cellular location: GO:0005829
comment: Reactome DB_ID: 3663468
display name: VPS36

ribose 1-phosphate, deoxyribose 1-phosphate
type: SmallMolecule
data source: Provenance1
member physical entity: D-ribose 1-phosphate
member physical entity: 2-deoxy-D-ribose 1-phosphate
xref: UnificationXref4207
xref: UnificationXref4206
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 500244

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: P0C8R3
data source: Provenance1
name: RPS27A(1-76)
name: P0C8R3
name: ubiquitin (RPS27A)
xref: UnificationXref8766
feature: FragmentFeature1357
cellular location: GO:0010008
comment: Reactome DB_ID: 3663452
display name: RPS27A

NH4+
type: SmallMolecule
entity reference: NH4+
data source: Provenance1
xref: UnificationXref4195
xref: UnificationXref4194
cellular location: GO:0005829
comment: Reactome DB_ID: 31633

Note: the coordinates are copied over from Homo sapiens.
type: Protein
entity reference: UniProt:P0C016
data source: Provenance1
name: RPS27A(1-76)
name: P0C016
name: ubiquitin (RPS27A)
xref: UnificationXref8767
feature: FragmentFeature1358
cellular location: GO:0010008
comment: Reactome DB_ID: 3663453
display name: RPS27A

(d)AMP
type: SmallMolecule
data source: Provenance1
member physical entity: SmallMolecule116
member physical entity: SmallMolecule54
xref: UnificationXref4186
xref: UnificationXref4187
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 500088

UnificationXref6819
type: UnificationXref
id: REACT_163474
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_163474.2

UnificationXref6818
type: UnificationXref
id: 3665394
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665394

UnificationXref6817
type: UnificationXref
id: REACT_162503
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_162503.2

UnificationXref6815
type: UnificationXref
id: 3664684
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664684

UnificationXref6816
type: UnificationXref
id: 3664686
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664686

UnificationXref6813
type: UnificationXref
id: Q9UUA6
db: UniProt

UnificationXref6814
type: UnificationXref
id: 3664683
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664683

UnificationXref6811
type: UnificationXref
id: 3664690
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664690

UnificationXref6812
type: UnificationXref
id: REACT_162925
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_162925.2

UnificationXref6810
type: UnificationXref
id: 3664688
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664688

Purine-6-ol
type: SmallMolecule
entity reference: CHEBI:17368
data source: Provenance1
name: hypoxanthine
xref: UnificationXref4225
xref: UnificationXref4226
cellular location: GO:0005829
comment: Reactome DB_ID: 113599
display name: Hyp

inosine, deoxyinosine
type: SmallMolecule
data source: Provenance1
member physical entity: inosine
member physical entity: 2'-deoxyinosine
xref: UnificationXref4234
xref: UnificationXref4233
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 500172

guanosine
type: SmallMolecule
entity reference: CHEBI:16750
data source: Provenance1
xref: UnificationXref4212
xref: UnificationXref4213
cellular location: GO:0005829
comment: Reactome DB_ID: 83926
display name: Gua-Rib

deoxyguanosine
type: SmallMolecule
entity reference: CHEBI:17172
data source: Provenance1
name: 2'-deoxyguanosine
xref: UnificationXref4215
xref: UnificationXref4216
cellular location: GO:0005829
comment: Reactome DB_ID: 109328
display name: dG

guanine
type: SmallMolecule
entity reference: guanine
data source: Provenance1
name: 2-amino-6-hydroxypurine
xref: UnificationXref4209
xref: UnificationXref4210
cellular location: GO:0005829
comment: Reactome DB_ID: 83956
display name: Gua

guanosine, deoxyguanosine
type: SmallMolecule
data source: Provenance1
member physical entity: guanosine
member physical entity: deoxyguanosine
xref: UnificationXref4218
xref: UnificationXref4217
cellular location: GO:0005829
comment: Reactome DB_ID: 500245
comment: Converted from EntitySet in Reactome
display name: G, dG

D-ribose 1-phosphate
type: SmallMolecule
entity reference: CHEBI:35425
data source: Provenance1
xref: UnificationXref4202
xref: UnificationXref4201
cellular location: GO:0005829
comment: Reactome DB_ID: 112016
display name: R1P

2-deoxy-D-ribose 1-phosphate
type: SmallMolecule
entity reference: 2-Deoxy-D-ribose 1-phosphate
data source: Provenance1
xref: UnificationXref4204
xref: UnificationXref4205
cellular location: GO:0005829
comment: Reactome DB_ID: 112032
display name: dRibP

ATP6V0 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry410
component stoichiometry: Stoichiometry411
component stoichiometry: Stoichiometry408
component stoichiometry: Stoichiometry406
component stoichiometry: Stoichiometry407
component: PhysicalEntity76
component: ATP6V0C hexamer (name copied from entity in Homo sapiens)
component: ATP6V0D
component: Note: the coordinates are copied over from Homo sapiens.
component: ATP6V0A
xref: UnificationXref1165
cellular location: GO:0010008
comment: Reactome DB_ID: 3659681

a-ketoisocaproate, a-keto b-methylvalerate, a-ketoisovalerate
type: SmallMolecule
data source: Provenance1
member physical entity: 3-methyl-2-oxobutanoate
member physical entity: alpha-keto-beta-methylvalerate
member physical entity: alpha-ketoisocaproate
xref: UnificationXref4876
xref: UnificationXref4877
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 508187

ATP6V0C hexamer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry409
component: ATP6V0C
xref: UnificationXref1163
cellular location: GO:0010008
comment: Reactome DB_ID: 3659673

2-Amino-3-methylbutyric acid
type: SmallMolecule
entity reference: CHEBI:16414
data source: Provenance1
name: L-Valine
xref: UnificationXref4864
xref: UnificationXref4863
cellular location: GO:0005829
comment: Reactome DB_ID: 29702
display name: L-Val

PIP3:PDK1 complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry404
component stoichiometry: Stoichiometry405
component: Homologues of PDPK1
component: SmallMolecule35
xref: UnificationXref1131
cellular location: GO:0005886
comment: Reactome DB_ID: 3660160

alpha-keto-beta-methylvalerate
type: SmallMolecule
entity reference: 3-Methyl-2-oxopentanoate
data source: Provenance1
name: 3-methyl-2-oxopentanoate
xref: UnificationXref4872
xref: UnificationXref4871
cellular location: GO:0005829
comment: Reactome DB_ID: 70721
display name: KMVA

G-protein beta:gamma signalling
type: Pathway
data source: Provenance1
pathway component: REACT 80512.9
evidence: Evidence264
xref: UnificationXref1420
xref: UnificationXref1421
pathway order: PathwayStep261
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

PLCG1 events in ERBB2 signaling
type: Pathway
data source: Provenance1
pathway component: REACT 80694.9
evidence: Evidence249
xref: UnificationXref1290
xref: UnificationXref1289
pathway order: PathwayStep173
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

V-ATPase (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry412
component stoichiometry: Stoichiometry424
component: ATP6V0 (name copied from entity in Homo sapiens)
component: ATP6V1 (name copied from entity in Homo sapiens)
xref: UnificationXref1194
cellular location: GO:0010008
comment: Reactome DB_ID: 3659726

alpha-ketoisocaproate
type: SmallMolecule
entity reference: CHEBI:17865
data source: Provenance1
name: 4-methyl-2-oxopentanoate
xref: UnificationXref4869
xref: UnificationXref4868
cellular location: GO:0005829
comment: Reactome DB_ID: 70701
display name: KIC

ATP6V1A trimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry420
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1187
cellular location: GO:0005829
comment: Reactome DB_ID: 3659686

UnificationXref4652
type: UnificationXref
id: 3661746
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661746

Leucine, Isoleucine, Valine
type: SmallMolecule
data source: Provenance1
member physical entity: L-Isoleucine
member physical entity: L-Leucine
member physical entity: 2-Amino-3-methylbutyric acid
xref: UnificationXref4866
xref: UnificationXref4865
cellular location: GO:0005829
comment: Reactome DB_ID: 508182
comment: Converted from EntitySet in Reactome
display name: Leu, Ile, Val

ATP6V1G dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry422
component: ATP6V1G
xref: UnificationXref1192
cellular location: GO:0005829
comment: Reactome DB_ID: 3659720

UnificationXref4651
type: UnificationXref
id: REACT_11368
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11368.2

ATP6V1 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry423
component stoichiometry: Stoichiometry419
component stoichiometry: Stoichiometry414
component stoichiometry: Stoichiometry413
component stoichiometry: Stoichiometry417
component stoichiometry: Stoichiometry416
component stoichiometry: Stoichiometry421
component stoichiometry: Stoichiometry418
component: ATP6V1A trimer (name copied from entity in Homo sapiens)
component: Note: the coordinates are copied over from Homo sapiens.
component: ATP6V1G dimer (name copied from entity in Homo sapiens)
component: ATP6V1C
component: ATP6V1B trimer (name copied from entity in Homo sapiens)
component: ATP6V1E
xref: UnificationXref1193
cellular location: GO:0005829
comment: Reactome DB_ID: 3659725

UnificationXref4650
type: UnificationXref
id: 200493
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=200493

L-Isoleucine
type: SmallMolecule
entity reference: CHEBI:17191
data source: Provenance1
name: 2-Amino-3-methylvaleric acid
xref: UnificationXref4860
xref: UnificationXref4861
cellular location: GO:0005829
comment: Reactome DB_ID: 30102
display name: L-Ile

ATP6V1B trimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry415
component: ATP6V1B
xref: UnificationXref1176
cellular location: GO:0005829
comment: Reactome DB_ID: 3659693

L-Leucine
type: SmallMolecule
entity reference: CHEBI:15603
data source: Provenance1
name: (2S)-alpha-2-Amino-4-methylvaleric acid
name: (2S)-alpha-Leucine
name: 2-amino-4-methylvaleric acid
xref: UnificationXref4857
xref: UnificationXref4858
cellular location: GO:0005829
comment: Reactome DB_ID: 29588
display name: L-Leu

UnificationXref4656
type: UnificationXref
id: REACT_11294
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11294.1

UnificationXref4655
type: UnificationXref
id: 197220
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=197220

UnificationXref4654
type: UnificationXref
id: REACT_96395
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_96395.9

UnificationXref4653
type: UnificationXref
id: 3661748
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661748

TSC1:p-S1387-TSC2 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry402
component stoichiometry: Stoichiometry403
component: Q09778
component: phospho-p-S1387-TSC2
xref: UnificationXref1117
cellular location: GO:0005829
comment: Reactome DB_ID: 3662440

UnificationXref4659
type: UnificationXref
id: 3661614
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661614

UnificationXref4658
type: UnificationXref
id: REACT_11409
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11409.2

UnificationXref4657
type: UnificationXref
id: 197256
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=197256

Activated mTORC1 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry395
component stoichiometry: Stoichiometry396
component stoichiometry: Stoichiometry397
component stoichiometry: Stoichiometry394
component: Rheb:GTP (name copied from entity in Homo sapiens)
component: O74184
component: Homologues of MTOR
component: P87141
xref: UnificationXref1080
cellular location: GO:0005829
comment: Reactome DB_ID: 3660767

Rheb:GTP (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry393
component stoichiometry: Stoichiometry392
component: Note: the coordinates are copied over from Homo sapiens.
component: SmallMolecule17
xref: UnificationXref1068
cellular location: GO:0005829
comment: Reactome DB_ID: 3660748

L-Asparagine
type: SmallMolecule
entity reference: CHEBI:17196
data source: Provenance1
name: 2-Aminosuccinamic acid
xref: UnificationXref4812
xref: UnificationXref4811
cellular location: GO:0005829
comment: Reactome DB_ID: 29642
display name: L-Asn

2-oxoglutaramic acid
type: SmallMolecule
entity reference: CHEBI:30882
data source: Provenance1
xref: UnificationXref4825
xref: UnificationXref4824
cellular location: GO:0005829
comment: Reactome DB_ID: 893598
display name: 2OGA

3-phosphonooxypyruvic acid
type: SmallMolecule
entity reference: CHEBI:30933
data source: Provenance1
xref: UnificationXref4832
xref: UnificationXref4833
cellular location: GO:0005829
comment: Reactome DB_ID: 977329

O-phospho-L-serine
type: SmallMolecule
entity reference: CHEBI:15811
data source: Provenance1
xref: UnificationXref4840
xref: UnificationXref4841
cellular location: GO:0005829
comment: Reactome DB_ID: 936706

phospho-ERK-1 dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry380
component: phospho-p-T202,Y204-MAPK3
xref: UnificationXref1000
cellular location: GO:0005829
comment: Reactome DB_ID: 3660171

propionyl coenzyme A
type: SmallMolecule
entity reference: CHEBI:15539
data source: Provenance1
xref: UnificationXref4911
xref: UnificationXref4912
cellular location: GO:0005759
comment: Reactome DB_ID: 70843
display name: propionyl-CoA

phosphorylated residue
type: SequenceModificationVocabulary
xref: UnificationXref436

phospho-ERK-1 dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry381
component: phospho-p-T202,Y204-MAPK3
xref: UnificationXref1004
cellular location: GO:0005654
comment: Reactome DB_ID: 3660179

alpha-methylacetoacetyl-CoA
type: SmallMolecule
entity reference: CHEBI:15476
data source: Provenance1
xref: UnificationXref4908
xref: UnificationXref4909
cellular location: GO:0005759
comment: Reactome DB_ID: 70836
display name: 2-methylacetoacetyl-CoA

phospho-ERK-2 dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry383
component: phospho-p-T185,Y187-MAPK1
xref: UnificationXref1010
cellular location: GO:0005829
comment: Reactome DB_ID: 3660176

3-methyl-2-oxobutanoate
type: SmallMolecule
entity reference: CHEBI:16530
data source: Provenance1
name: alpha-ketoisovalerate
xref: UnificationXref4897
xref: UnificationXref4898
cellular location: GO:0005759
comment: Reactome DB_ID: 113584
display name: KIV

phospho-ERK-2 dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry384
component: phospho-p-T185,Y187-MAPK1
xref: UnificationXref1014
cellular location: GO:0005654
comment: Reactome DB_ID: 3660182

alpha-keto-beta-methylvalerate
type: SmallMolecule
entity reference: 3-Methyl-2-oxopentanoate
data source: Provenance1
name: 3-methyl-2-oxopentanoate
xref: UnificationXref4896
xref: UnificationXref4895
cellular location: GO:0005759
comment: Reactome DB_ID: 113576
display name: KMVA

PDPK1:PIP3 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry386
component stoichiometry: Stoichiometry385
component: Homologues of PDPK1
component: SmallMolecule19
xref: UnificationXref1035
cellular location: GO:0005886
comment: Reactome DB_ID: 3664759

UnificationXref4661
type: UnificationXref
id: REACT_11509
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11509.2

alpha-ketoisocaproate
type: SmallMolecule
entity reference: CHEBI:17865
data source: Provenance1
name: 4-methyl-2-oxopentanoate
xref: UnificationXref4894
xref: UnificationXref4893
cellular location: GO:0005759
comment: Reactome DB_ID: 113598
display name: KIC

PDPK1:PIP2 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry387
component stoichiometry: Stoichiometry388
component: Homologues of PDPK1
component: SmallMolecule20
xref: UnificationXref1038
cellular location: GO:0005886
comment: Reactome DB_ID: 3664751

UnificationXref4660
type: UnificationXref
id: 200503
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=200503

a-ketoisocaproate, a-keto b-methylvalerate, a-ketoisovalerate
type: SmallMolecule
data source: Provenance1
member physical entity: 3-methyl-2-oxobutanoate
member physical entity: alpha-keto-beta-methylvalerate
member physical entity: alpha-ketoisocaproate
xref: UnificationXref4900
xref: UnificationXref4899
cellular location: GO:0005759
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 508181

p-ERK dimer
type: Complex
data source: Provenance1
member physical entity: phospho-ERK-1 dimer (name copied from entity in Homo sapiens)
member physical entity: phospho-ERK-2 dimer (name copied from entity in Homo sapiens)
xref: UnificationXref1056
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3663821

UnificationXref4663
type: UnificationXref
id: 3661617
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661617

2-Amino-3-methylbutyric acid
type: SmallMolecule
entity reference: CHEBI:16414
data source: Provenance1
name: L-Valine
xref: UnificationXref4889
xref: UnificationXref4890
cellular location: GO:0005759
comment: Reactome DB_ID: 113540
display name: L-Val

Rheb:GDP (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry391
component stoichiometry: Stoichiometry390
component: Note: the coordinates are copied over from Homo sapiens.
component: SmallMolecule18
xref: UnificationXref1067
cellular location: GO:0005829
comment: Reactome DB_ID: 3660747

UnificationXref4662
type: UnificationXref
id: 3661615
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661615

L-Isoleucine
type: SmallMolecule
entity reference: CHEBI:17191
data source: Provenance1
name: 2-Amino-3-methylvaleric acid
xref: UnificationXref4888
xref: UnificationXref4887
cellular location: GO:0005759
comment: Reactome DB_ID: 113537
display name: L-Ile

UnificationXref4665
type: UnificationXref
id: 3661741
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661741

http://identifiers.org/pubmed/12853463
type: PublicationXref
id: 12853463
author: Nagai, K
author: Menichelli, E
author: Kuglstatter, A
author: Isel, C
author: Oubridge, C
author: Jovine, L
db: Pubmed
title: Structure, function and evolution of the signal recognition particle
source: EMBO J 22:3479-85
year: 2003

UnificationXref4664
type: UnificationXref
id: REACT_114560
db: Reactome
id version: 8
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_114560.8

UnificationXref4667
type: UnificationXref
id: 3661744
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661744

UnificationXref4666
type: UnificationXref
id: 3661742
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661742

UnificationXref4669
type: UnificationXref
id: O74940
db: UniProt

UnificationXref4668
type: UnificationXref
id: REACT_80724
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_80724.9

http://identifiers.org/pubmed/12686127
type: PublicationXref
id: 12686127
author: Hillary, RA
author: Pegg, AE
db: Pubmed
title: Decarboxylases involved in polyamine biosynthesis and their inactivation by nitric oxide
source: Biochim Biophys Acta 1647:161-6
year: 2003

Succinic semialdehyde
type: SmallMoleculeReference
name: Succinate semialdehyde
name: ChEBI:16265 Succinate semialdehyde
xref: UnificationXref4012

UDP-N-acetyl-D-glucosamine
type: SmallMoleculeReference
name: UDP-N-acetyl-D-glucosamine [ChEBI:16264]
xref: UnificationXref6445

PKA tetramer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry374
component stoichiometry: Stoichiometry375
component: Note: the coordinates are copied over from Homo sapiens.
component: PKA regulatory subunit
xref: UnificationXref979
cellular location: GO:0005829
comment: Reactome DB_ID: 3660360

Kinesin-8 dimer
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry370
component: Kinesin-8 monomers
xref: UnificationXref946
xref: UnificationXref945
cellular location: GO:0005829
comment: Reactome DB_ID: 984632

cAMP:PKA regulatory subunit (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry376
component stoichiometry: Stoichiometry377
component: SmallMolecule33
component: PKA regulatory subunit
xref: UnificationXref980
cellular location: GO:0005829
comment: Reactome DB_ID: 3660361

L-Leucine
type: SmallMolecule
entity reference: CHEBI:15603
data source: Provenance1
name: (2S)-alpha-2-Amino-4-methylvaleric acid
name: (2S)-alpha-Leucine
name: 2-amino-4-methylvaleric acid
xref: UnificationXref4886
xref: UnificationXref4885
cellular location: GO:0005759
comment: Reactome DB_ID: 113580
display name: L-Leu

3-methyl-2-oxobutanoate
type: SmallMolecule
entity reference: CHEBI:16530
data source: Provenance1
name: alpha-ketoisovalerate
xref: UnificationXref4875
xref: UnificationXref4874
cellular location: GO:0005829
comment: Reactome DB_ID: 70846
display name: KIV

Leucine, Isoleucine, Valine
type: SmallMolecule
data source: Provenance1
member physical entity: 2-Amino-3-methylbutyric acid
member physical entity: L-Isoleucine
member physical entity: L-Leucine
xref: UnificationXref4892
xref: UnificationXref4891
cellular location: GO:0005759
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 508190
display name: Leu, Ile, Val

Lsm1-7 Complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry476
component stoichiometry: Stoichiometry477
component stoichiometry: Stoichiometry483
component stoichiometry: Stoichiometry479
component stoichiometry: Stoichiometry481
component stoichiometry: Stoichiometry480
component stoichiometry: Stoichiometry478
component stoichiometry: Stoichiometry482
component: Note: the coordinates are copied over from Homo sapiens.
component: PhysicalEntity90
xref: UnificationXref1617
cellular location: GO:0005829
comment: Reactome DB_ID: 3662749

UnificationXref4674
type: UnificationXref
id: 3665392
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665392

UnificationXref4673
type: UnificationXref
id: REACT_98272
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_98272.9

Exosome Complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry467
component stoichiometry: Stoichiometry466
component stoichiometry: Stoichiometry465
component stoichiometry: Stoichiometry468
component stoichiometry: Stoichiometry475
component: Exosome Ring Hexamer (name copied from entity in Homo sapiens)
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1588
cellular location: GO:0005829
comment: Reactome DB_ID: 3662800

Deamino-NAD+
type: SmallMolecule
entity reference: Deamido-NAD+
data source: Provenance1
xref: UnificationXref4658
xref: UnificationXref4657
cellular location: GO:0005829
comment: Reactome DB_ID: 197256
display name: DA-NAD+

UnificationXref4672
type: UnificationXref
id: 3661624
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661624

Exosome Ring Hexamer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry473
component stoichiometry: Stoichiometry474
component stoichiometry: Stoichiometry469
component stoichiometry: Stoichiometry470
component stoichiometry: Stoichiometry471
component stoichiometry: Stoichiometry472
component: Q10205
component: Note: the coordinates are copied over from Homo sapiens.
component: Exosome complex exonuclease RRP45
component: PhysicalEntity88
component: PhysicalEntity87
xref: UnificationXref1587
cellular location: GO:0005829
comment: Reactome DB_ID: 3662783

UnificationXref4671
type: UnificationXref
id: 3661622
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661622

SPO11 Dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry462
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1545
cellular location: GO:0005654
comment: Reactome DB_ID: 3663419

UnificationXref4670
type: UnificationXref
id: 3661621
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661621

THF-polyglutamate
type: SmallMolecule
entity reference: THF-polyglutamate
data source: Provenance1
xref: UnificationXref4678
xref: UnificationXref4677
cellular location: GO:0005829
comment: Reactome DB_ID: 197969
display name: THFPG

SPO11 Covalently Attached to Double-strand Break (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry463
component stoichiometry: Stoichiometry464
component: PhysicalEntity20
component: SPO11 Dimer (name copied from entity in Homo sapiens)
xref: UnificationXref1546
cellular location: GO:0005654
comment: Reactome DB_ID: 3663420

Mg++
type: SmallMolecule
entity reference: Mg++
data source: Provenance1
name: Magnesium
xref: UnificationXref4660
xref: UnificationXref4661
cellular location: GO:0000139
comment: Reactome DB_ID: 200503
display name: Mg2+

PPA1 dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry459
component: Homologues of PPA1
xref: UnificationXref1517
cellular location: GO:0005829
comment: Reactome DB_ID: 3658528

5-methyltetrahydrofolate polyglutamate
type: SmallMolecule
entity reference: CHEBI:63907
data source: Provenance1
xref: UnificationXref4688
xref: UnificationXref4687
cellular location: GO:0005829
comment: Reactome DB_ID: 174404
display name: MTHFPG

PPA2 dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry461
component: Homologues of PPA2
xref: UnificationXref1533
cellular location: GO:0005759
comment: Reactome DB_ID: 3663101

5-methyltetrahydrofolate
type: SmallMolecule
entity reference: CHEBI:15641
data source: Provenance1
xref: UnificationXref4684
xref: UnificationXref4685
cellular location: GO:0005829
comment: Reactome DB_ID: 200665
display name: MTHF

VPS35:VPS29:VPS26 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry451
component stoichiometry: Stoichiometry450
component stoichiometry: Stoichiometry449
component: Note: the coordinates are copied over from Homo sapiens.
component: O74552
xref: UnificationXref1454
cellular location: GO:0005829
comment: Reactome DB_ID: 3665024

WLS:retromer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry457
component stoichiometry: Stoichiometry456
component stoichiometry: Stoichiometry455
component: PhysicalEntity83
component: VPS35:VPS29:VPS26 (name copied from entity in Homo sapiens)
component: SDP3
xref: UnificationXref1461
cellular location: GO:0000139
comment: Reactome DB_ID: 3665032

WLS:retromer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry452
component stoichiometry: Stoichiometry453
component stoichiometry: Stoichiometry454
component: PhysicalEntity82
component: VPS35:VPS29:VPS26 (name copied from entity in Homo sapiens)
component: SDP3
xref: UnificationXref1458
cellular location: early endosome membrane
comment: Reactome DB_ID: 3665030

UnificationXref4679
type: UnificationXref
id: O74742
db: UniProt

UnificationXref4678
type: UnificationXref
id: REACT_11817
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11817.2

UnificationXref4677
type: UnificationXref
id: 197969
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=197969

UnificationXref4676
type: UnificationXref
id: CHEBI:28624
db: ChEBI

UnificationXref4675
type: UnificationXref
id: REACT_29368
db: Reactome
id version: 10
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_29368.10

Cobalamin
type: SmallMolecule
entity reference: cobalamin(III)
data source: Provenance1
xref: UnificationXref4611
xref: UnificationXref4612
cellular location: GO:0005576
comment: Reactome DB_ID: 3000125
display name: Cbl

Coenzyme R
type: SmallMolecule
entity reference: CHEBI:15956
data source: Provenance1
name: D-Biotin
name: Biotin
name: Vitamin H
xref: UnificationXref4620
xref: UnificationXref4619
cellular location: GO:0005829
comment: Reactome DB_ID: 199207
display name: Btn

Nicotinate D-ribonucleotide
type: SmallMolecule
entity reference: CHEBI:15763
data source: Provenance1
xref: UnificationXref4644
xref: UnificationXref4643
cellular location: GO:0005654
comment: Reactome DB_ID: 200492

Deamino-NAD+
type: SmallMolecule
entity reference: Deamido-NAD+
data source: Provenance1
xref: UnificationXref4647
xref: UnificationXref4646
cellular location: GO:0005654
comment: Reactome DB_ID: 200499
display name: DA-NAD+

Zn(II)
type: SmallMolecule
entity reference: CHEBI:29105
data source: Provenance1
name: Zn++
name: Zinc ion
xref: UnificationXref4651
xref: UnificationXref4650
cellular location: GO:0005654
comment: Reactome DB_ID: 200493
display name: Zn2+

Nicotinate D-ribonucleotide
type: SmallMolecule
entity reference: CHEBI:15763
data source: Provenance1
xref: UnificationXref4656
xref: UnificationXref4655
cellular location: GO:0005829
comment: Reactome DB_ID: 197220

RhoGTPase:GDP (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry441
component stoichiometry: Stoichiometry440
component: PhysicalEntity80
component: SmallMolecule18
xref: UnificationXref1399
cellular location: GO:0005829
comment: Reactome DB_ID: 3661462

UnificationXref4683
type: UnificationXref
id: CHEBI:15641
db: ChEBI

L-alpha-Alanine
type: SmallMolecule
entity reference: CHEBI:16977
data source: Provenance1
name: L-Alanine
name: L-2-Aminopropionic acid
xref: UnificationXref4766
xref: UnificationXref4767
cellular location: GO:0005759
comment: Reactome DB_ID: 379697
display name: L-Ala

RhoA,B,C:GDP (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry443
component stoichiometry: Stoichiometry444
component: SmallMolecule41
component: PhysicalEntity81
xref: UnificationXref1412
cellular location: GO:0005886
comment: Reactome DB_ID: 3662577

UnificationXref4682
type: UnificationXref
id: REACT_82018
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_82018.9

L-alpha-Alanine
type: SmallMolecule
entity reference: CHEBI:16977
data source: Provenance1
name: L-Alanine
name: L-2-Aminopropionic acid
xref: UnificationXref4746
xref: UnificationXref4747
cellular location: GO:0005829
comment: Reactome DB_ID: 29432
display name: L-Ala

RhoA/B/C:GTP (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry446
component stoichiometry: Stoichiometry445
component: SmallMolecule42
component: PhysicalEntity81
xref: UnificationXref1413
cellular location: GO:0005886
comment: Reactome DB_ID: 3662578

UnificationXref4685
type: UnificationXref
id: REACT_11451
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11451.2

Protein Kinase C, alpha type: DAG (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry448
component stoichiometry: Stoichiometry447
component: Homologues of PRKCA
component: SmallMolecule21
xref: UnificationXref1434
cellular location: GO:0005886
comment: Reactome DB_ID: 3662551

UnificationXref4684
type: UnificationXref
id: 200665
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=200665

PIP3:RhoA (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry433
component stoichiometry: Stoichiometry434
component: SmallMolecule35
component: Homologues of RHOA
xref: UnificationXref1268
cellular location: GO:0005886
comment: Reactome DB_ID: 3661860

2-Pyrrolidinecarboxylic acid
type: SmallMolecule
entity reference: CHEBI:17203
data source: Provenance1
name: L-Proline
xref: UnificationXref4804
xref: UnificationXref4803
cellular location: GO:0005759
comment: Reactome DB_ID: 379717
display name: L-Pro

H2O2
type: SmallMoleculeReference
name: Hydrogen peroxide
name: H2O2 [ChEBI:16240]
xref: UnificationXref4262

RhoGTPase:GDP (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry436
component stoichiometry: Stoichiometry435
component: SmallMolecule41
component: PhysicalEntity77
xref: UnificationXref1308
cellular location: GO:0005886
comment: Reactome DB_ID: 3661438

1-Pyrroline-5-carboxylic acid
type: SmallMolecule
entity reference: CHEBI:17388
data source: Provenance1
name: (S)-1-Pyrroline-5-carboxylate
xref: UnificationXref4801
xref: UnificationXref4800
cellular location: GO:0005759
comment: Reactome DB_ID: 113590
display name: L-1-Pyrroline-5-carboxylate

RhoGTPase:GTP (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry437
component stoichiometry: Stoichiometry438
component: SmallMolecule42
component: PhysicalEntity77
xref: UnificationXref1309
cellular location: GO:0005886
comment: Reactome DB_ID: 3661465

UnificationXref4681
type: UnificationXref
id: 3661630
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661630

L-Glutamate gamma-semialdehyde
type: SmallMolecule
entity reference: CHEBI:17232
data source: Provenance1
name: L-Glutamate 5-semialdehyde
xref: UnificationXref4782
xref: UnificationXref4783
cellular location: GO:0005759
comment: Reactome DB_ID: 31339
display name: L-Glu5S

http://identifiers.org/pubmed/7917292
type: PublicationXref
id: 7917292
author: Furness, J
author: Doherty, P
author: Walsh, FS
author: Williams, EJ
db: Pubmed
title: Activation of the FGF receptor underlies neurite outgrowth stimulated by L1, N-CAM, and N-cadherin
source: Neuron 13:583-94
year: 1994

Inactivated RhoGTPase:GDP:GDI complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry439
component stoichiometry: Stoichiometry442
component: RhoGTPase:GDP (name copied from entity in Homo sapiens)
component: GDI proteins
xref: UnificationXref1400
cellular location: GO:0005829
comment: Reactome DB_ID: 3661463

UnificationXref4680
type: UnificationXref
id: 3661628
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661628

(S)-2,5-Diaminopentanoate
type: SmallMolecule
entity reference: CHEBI:15729
data source: Provenance1
name: (S)-2,5-Diaminopentanoic acid
name: (S)-2,5-diaminovaleric acid
name: L-Ornithine
xref: UnificationXref4780
xref: UnificationXref4779
cellular location: GO:0005759
comment: Reactome DB_ID: 113585
display name: L-Orn

4-Trimethylammoniobutanoate
type: SmallMoleculeReference
name: 4-Trimethylammoniobutanoate [ChEBI:16244]
xref: UnificationXref5081

RhoA (Mg cofactor):GDP (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry427
component stoichiometry: Stoichiometry429
component stoichiometry: Stoichiometry428
component: SmallMolecule41
component: Homologues of RHOA
component: SmallMolecule40
xref: UnificationXref1235
cellular location: GO:0005886
comment: Reactome DB_ID: 3661372

RhoA (Mg cofactor):GTP (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry430
component stoichiometry: Stoichiometry431
component stoichiometry: Stoichiometry432
component: Homologues of RHOA
component: SmallMolecule40
component: SmallMolecule42
xref: UnificationXref1238
cellular location: GO:0005886
comment: Reactome DB_ID: 3661373

UnificationXref4687
type: UnificationXref
id: 174404
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=174404

http://identifiers.org/pubmed/16319170
type: PublicationXref
id: 16319170
author: Kiss, T
author: Jady, BE
author: Bertrand, E
author: Richard, P
db: Pubmed
title: Cell cycle-dependent recruitment of telomerase RNA and Cajal bodies to human telomeres
source: Mol Biol Cell 17:944-54
year: 2006

UnificationXref4686
type: UnificationXref
id: CHEBI:63907
db: ChEBI

UnificationXref4689
type: UnificationXref
id: 3661789
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661789

UnificationXref4688
type: UnificationXref
id: REACT_7545
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_7545.3

10-formyltetrahydrofolate polyglutamate
type: SmallMolecule
entity reference: CHEBI:28010
data source: Provenance1
name: 10-Formyl-THF polyglutamate
xref: UnificationXref4706
xref: UnificationXref4705
cellular location: GO:0005829
comment: Reactome DB_ID: 111353
display name: 10-FTHFPG

5,10-methenylTHF polyglutamate
type: SmallMolecule
entity reference: CHEBI:65049
data source: Provenance1
name: 5,10-methenyltetrahydrofolate polyglutamate
xref: UnificationXref4716
xref: UnificationXref4717
cellular location: GO:0005829
comment: Reactome DB_ID: 200640
display name: 5,10-MTHFPG

5,6,7,8-tetrahydrofolate
type: SmallMolecule
entity reference: CHEBI:15635
data source: Provenance1
name: Tetrahydrofolate
name: tetrahydrofolic acid
xref: UnificationXref4692
xref: UnificationXref4691
cellular location: GO:0005759
comment: Reactome DB_ID: 200671
display name: THF

THF-polyglutamate
type: SmallMolecule
entity reference: THF-polyglutamate
data source: Provenance1
xref: UnificationXref4699
xref: UnificationXref4700
cellular location: GO:0005759
comment: Reactome DB_ID: 200679
display name: THFPG

Active N-SMase:Mg2+ (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry426
component stoichiometry: Stoichiometry425
component: O74369
component: SmallMolecule40
xref: UnificationXref1224
cellular location: GO:0005886
comment: Reactome DB_ID: 3661356

5,10-methyleneTHF polyglutamate
type: SmallMolecule
entity reference: CHEBI:60473
data source: Provenance1
name: 5,10-methylenetetrahydrofolate polyglutamate
xref: UnificationXref4721
xref: UnificationXref4722
cellular location: GO:0005829
comment: Reactome DB_ID: 200739
display name: 5,10-MetTHFPG

Ubiquitinated AUF1 Tetramer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry495
component: Ubiquitinated AUF1 (isoform p37 or p40)
xref: UnificationXref1650
cellular location: GO:0005829
comment: Reactome DB_ID: 3663156

UnificationXref4611
type: UnificationXref
id: 3000125
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3000125

UnificationXref4612
type: UnificationXref
id: REACT_165600
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_165600.1

UnificationXref4610
type: UnificationXref
id: REACT_164390
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_164390.1

SMG1:UPF1:EJC:Translated mRNP (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry547
component stoichiometry: Stoichiometry662
component stoichiometry: Stoichiometry551
component: Note: the coordinates are copied over from Homo sapiens.
component: Translated mRNA Complex with Premature Termination Codon Preceding Exon Junction (name copied from entity in Homo sapiens)
component: SMG1:SMG8:SMG9 Complex (name copied from entity in Homo sapiens)
xref: UnificationXref2074
cellular location: GO:0005829
comment: Reactome DB_ID: 3663529

UnificationXref4615
type: UnificationXref
id: 3665628
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665628

TTP:mRNA Complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry546
component stoichiometry: Stoichiometry544
component stoichiometry: Stoichiometry545
component: Note: the coordinates are copied over from Homo sapiens.
component: PhysicalEntity101
xref: UnificationXref1747
cellular location: GO:0005829
comment: Reactome DB_ID: 3663135

UnificationXref4616
type: UnificationXref
id: REACT_166159
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_166159.1

BRF1:mRNA Complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry543
component stoichiometry: Stoichiometry542
component: PhysicalEntity100
component: ZFP36L1
xref: UnificationXref1737
cellular location: GO:0005829
comment: Reactome DB_ID: 3663160

UnificationXref4613
type: UnificationXref
id: 3665010
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665010

26S proteasome (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry506
component stoichiometry: Stoichiometry533
component stoichiometry: Stoichiometry510
component stoichiometry: Stoichiometry502
component stoichiometry: Stoichiometry508
component stoichiometry: Stoichiometry503
component stoichiometry: Stoichiometry501
component stoichiometry: Stoichiometry522
component stoichiometry: Stoichiometry505
component stoichiometry: Stoichiometry514
component stoichiometry: Stoichiometry527
component stoichiometry: Stoichiometry521
component stoichiometry: Stoichiometry526
component stoichiometry: Stoichiometry530
component stoichiometry: Stoichiometry509
component stoichiometry: Stoichiometry512
component stoichiometry: Stoichiometry515
component stoichiometry: Stoichiometry516
component stoichiometry: Stoichiometry535
component stoichiometry: Stoichiometry534
component stoichiometry: Stoichiometry517
component stoichiometry: Stoichiometry537
component stoichiometry: Stoichiometry507
component stoichiometry: Stoichiometry539
component stoichiometry: Stoichiometry525
component stoichiometry: Stoichiometry531
component stoichiometry: Stoichiometry498
component stoichiometry: Stoichiometry528
component stoichiometry: Stoichiometry513
component stoichiometry: Stoichiometry538
component stoichiometry: Stoichiometry511
component stoichiometry: Stoichiometry540
component stoichiometry: Stoichiometry541
component stoichiometry: Stoichiometry518
component stoichiometry: Stoichiometry504
component stoichiometry: Stoichiometry524
component stoichiometry: Stoichiometry523
component stoichiometry: Stoichiometry499
component stoichiometry: Stoichiometry536
component stoichiometry: Stoichiometry519
component stoichiometry: Stoichiometry532
component stoichiometry: Stoichiometry529
component stoichiometry: Stoichiometry500
component stoichiometry: Stoichiometry520
component: Q9UQY2
component: Proteasome chain 6
component: PhysicalEntity96
component: Note: the coordinates are copied over from Homo sapiens.
component: O94517
component: PhysicalEntity99
component: Proteasome component C13
component: PhysicalEntity97
component: PhysicalEntity94
component: PhysicalEntity93
component: Multicatalytic endopeptidase complex subunit C9
component: O94579
component: PhysicalEntity98
component: 26S proteasome subunit p112
component: Q10311
component: PSA7L_HUMAN
component: O42897
component: PhysicalEntity95
component: Tumor necrosis factor type 1 receptor associated protein 2

UnificationXref4614
type: UnificationXref
id: REACT_168678
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_168678.1

Core Exon Junction Complex (Core EJC) (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry560
component stoichiometry: Stoichiometry559
component stoichiometry: Stoichiometry558
component: PhysicalEntity105
component: Note: the coordinates are copied over from Homo sapiens.
component: Magoh-Y14 complex (name copied from entity in Homo sapiens)
xref: UnificationXref1777
cellular location: GO:0005829
comment: Reactome DB_ID: 3663499

Exon Junction:UPF2:UPF3 Complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry555
component stoichiometry: Stoichiometry562
component stoichiometry: Stoichiometry561
component stoichiometry: Stoichiometry554
component: UPF3
component: Q1MTR2
component: Core Exon Junction Complex (Core EJC) (name copied from entity in Homo sapiens)
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1782
cellular location: GO:0005829
comment: Reactome DB_ID: 3663506

Ascorbate
type: SmallMolecule
entity reference: CHEBI:29073
data source: Provenance1
xref: UnificationXref4518
xref: UnificationXref4519
cellular location: GO:0005829
comment: Reactome DB_ID: 198816
display name: VitC

Translated mRNA Complex with Premature Termination Codon Preceding Exon Junction (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry654
component stoichiometry: Stoichiometry566
component stoichiometry: Stoichiometry661
component stoichiometry: Stoichiometry563
component stoichiometry: Stoichiometry552
component stoichiometry: Stoichiometry553
component: SmallMolecule59
component: mRNA Complex with a Premature Termination Codon Preceding an Exon Junction (name copied from entity in Homo sapiens)
component: 80S ribosome (name copied from entity in Homo sapiens)
component: GDP bound eRF3 (name copied from entity in Homo sapiens)
component: Note: the coordinates are copied over from Homo sapiens.
component: Exon Junction:UPF2:UPF3 Complex (name copied from entity in Homo sapiens)
xref: UnificationXref2073
cellular location: GO:0005829
comment: Reactome DB_ID: 3663507

ferriheme
type: SmallMolecule
entity reference: CHEBI:36144
data source: Provenance1
xref: UnificationXref4522
xref: UnificationXref4521
cellular location: GO:0005741
comment: Reactome DB_ID: 198853
display name: FeHM

http://identifiers.org/pubmed/11788603
type: PublicationXref
id: 11788603
author: Zhou, T
author: Tomchick, DR
author: Zhang, H
author: Marquez, VE
author: Osterman, AL
author: Binns, DD
author: Grishin, NV
author: Kurnasov, OV
db: Pubmed
title: Structure of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase. Basis for the dual substrate specificity and activation of the oncolytic agent tiazofurin.
source: J Biol Chem 277:13148-54
year: 2002

SMG1:SMG8:SMG9 Complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry550
component stoichiometry: Stoichiometry549
component stoichiometry: Stoichiometry548
component: PhysicalEntity102
component: PhysicalEntity104
component: PhysicalEntity103
xref: UnificationXref1759
cellular location: GO:0005829
comment: Reactome DB_ID: 3663528

Riboflavin
type: SmallMolecule
entity reference: CHEBI:17015
data source: Provenance1
xref: UnificationXref4529
xref: UnificationXref4530
cellular location: GO:0005829
comment: Reactome DB_ID: 196931
display name: RIB

Magoh-Y14 complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry557
component stoichiometry: Stoichiometry556
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1773
cellular location: GO:0005829
comment: Reactome DB_ID: 3659900

phys-ent-participant34100
type: SmallMolecule
entity reference: CHEBI:16960
data source: Provenance1
xref: UnificationXref4499
xref: UnificationXref4498
cellular location: GO:0005829
comment: Reactome DB_ID: 1131972
display name: ADP-D-ribose

xanthosine 5'-triphosphate
type: SmallMolecule
entity reference: CHEBI:10049
data source: Provenance1
xref: UnificationXref4493
xref: UnificationXref4492
cellular location: GO:0005829
comment: Reactome DB_ID: 2509848
display name: XTP

monodehydroascorbate
type: SmallMolecule
entity reference: CHEBI:16504
data source: Provenance1
name: semidehydroascorbate
name: MDASC
xref: UnificationXref4515
xref: UnificationXref4516
cellular location: GO:0005829
comment: Reactome DB_ID: 198803
display name: SHAS

ferroheme
type: SmallMolecule
entity reference: CHEBI:17627
data source: Provenance1
xref: UnificationXref4512
xref: UnificationXref4511
cellular location: GO:0005741
comment: Reactome DB_ID: 198842
display name: heme

inosine 5'-triphosphate
type: SmallMolecule
entity reference: CHEBI:16039
data source: Provenance1
xref: UnificationXref4474
xref: UnificationXref4475
cellular location: GO:0005829
comment: Reactome DB_ID: 2509836
display name: ITP

gamma-L-Glutamyl-L-cysteinyl-glycine
type: SmallMolecule
entity reference: CHEBI:16856
data source: Provenance1
name: 5-L-Glutamyl-L-cysteinylglycine
name: N-(N-gamma-L-Glutamyl-L-cysteinyl)glycine
name: Reduced glutathione
name: Glutathione
xref: UnificationXref4464
xref: UnificationXref4465
cellular location: GO:0005829
comment: Reactome DB_ID: 29450
display name: GSH

deoxyinosinic acid
type: SmallMolecule
entity reference: 2'-Deoxyinosine 5'-phosphate [ChEBI:28806]
data source: Provenance1
name: 2'-deoxyinosine 5'-monophosphate
xref: UnificationXref4486
xref: UnificationXref4487
cellular location: GO:0005829
comment: Reactome DB_ID: 109330
display name: dIMP

2'-deoxyinosine 5'-triphosphate
type: SmallMolecule
entity reference: dITP
data source: Provenance1
xref: UnificationXref4484
xref: UnificationXref4483
cellular location: GO:0005829
comment: Reactome DB_ID: 2509835
display name: dITP

UnificationXref4619
type: UnificationXref
id: 199207
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=199207

UnificationXref4618
type: UnificationXref
id: 3664972
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664972

UnificationXref4617
type: UnificationXref
id: 3664971
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664971

UnificationXref4620
type: UnificationXref
id: REACT_11360
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11360.3

UniProt:P22774
type: ProteinReference
xref: UnificationXref8449
organism: BioSource1

UnificationXref4621
type: UnificationXref
id: 3664974
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664974

UnificationXref4622
type: UnificationXref
id: 3664975
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664975

UnificationXref4623
type: UnificationXref
id: O14353
db: UniProt

Decapped mRNA:LSM1-7 Complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry487
component stoichiometry: Stoichiometry486
component: Lsm1-7 Complex (name copied from entity in Homo sapiens)
component: PhysicalEntity91
xref: UnificationXref1623
cellular location: GO:0005829
comment: Reactome DB_ID: 3662750

UnificationXref4624
type: UnificationXref
id: 3664979
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664979

Deadenylated mRNA:Lsm1-7 Complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry485
component stoichiometry: Stoichiometry484
component: PhysicalEntity85
component: Lsm1-7 Complex (name copied from entity in Homo sapiens)
xref: UnificationXref1618
cellular location: GO:0005829
comment: Reactome DB_ID: 3662757

UnificationXref4625
type: UnificationXref
id: 3664981
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664981

AUF1 p37 Dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry488
component: HNRNPD-4
xref: UnificationXref1636
cellular location: GO:0005829
comment: Reactome DB_ID: 3663141

UnificationXref4626
type: UnificationXref
id: REACT_168964
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_168964.1

AUF1 Dimer (isoform p37 or p40)
type: Complex
data source: Provenance1
member physical entity: Phosphorylated AUF1 p40 Dimer (name copied from entity in Homo sapiens)
member physical entity: AUF1 p37 Dimer (name copied from entity in Homo sapiens)
xref: UnificationXref1639
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3663146

UnificationXref4627
type: UnificationXref
id: 3665007
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665007

AUF1 Tetramer: Destabilized mRNA Complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry494
component stoichiometry: Stoichiometry493
component: AUF1 Tetramer (isoform p37 or p40)
component: PhysicalEntity92
xref: UnificationXref1643
cellular location: GO:0005829
comment: Reactome DB_ID: 3663150

Hydrogen peroxide
type: SmallMolecule
entity reference: H2O2
data source: Provenance1
xref: UnificationXref4598
xref: UnificationXref4597
cellular location: GO:0005829
comment: Reactome DB_ID: 29408
display name: H2O2

Phosphorylated AUF1 p40 Dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry489
component: phospho-p-S83,S87-HNRNPD-3
xref: UnificationXref1638
cellular location: GO:0005829
comment: Reactome DB_ID: 3663145

Cobalamin
type: SmallMolecule
entity reference: cobalamin(III)
data source: Provenance1
xref: UnificationXref4609
xref: UnificationXref4610
cellular location: GO:0005829
comment: Reactome DB_ID: 3000241
display name: Cbl

AUF1 p37 Tetramer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry491
component: HNRNPD-4
xref: UnificationXref1640
cellular location: GO:0005829
comment: Reactome DB_ID: 3663147

Pyridoxine
type: SmallMolecule
entity reference: CHEBI:16709
data source: Provenance1
xref: UnificationXref4591
xref: UnificationXref4590
cellular location: GO:0005829
comment: Reactome DB_ID: 965053
display name: PDX

AUF1 Tetramer (isoform p37 or p40)
type: Complex
data source: Provenance1
member physical entity: Phosphorylated AUF1 p40 Tetramer (name copied from entity in Homo sapiens)
member physical entity: AUF1 p37 Tetramer (name copied from entity in Homo sapiens)
xref: UnificationXref1642
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3663149

Pyridoxine phosphate
type: SmallMolecule
entity reference: Pyridoxine phosphate [ChEBI:8672]
data source: Provenance1
xref: UnificationXref4594
xref: UnificationXref4593
cellular location: GO:0005829
comment: Reactome DB_ID: 964952
display name: PDXP

Ubiquitinated AUF1 Tetramer: Destabilized mRNA Complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry496
component stoichiometry: Stoichiometry497
component: Ubiquitinated AUF1 Tetramer (name copied from entity in Homo sapiens)
component: PhysicalEntity92
xref: UnificationXref1651
cellular location: GO:0005829
comment: Reactome DB_ID: 3663157

Phosphorylated AUF1 p40 Tetramer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry492
component: phospho-p-S83,S87-HNRNPD-3
xref: UnificationXref1641
cellular location: GO:0005829
comment: Reactome DB_ID: 3663148

Pyridoxamine phosphate
type: SmallMolecule
entity reference: Pyridoxamine phosphate [ChEBI:8670]
data source: Provenance1
xref: UnificationXref4585
xref: UnificationXref4586
cellular location: GO:0005829
comment: Reactome DB_ID: 965146
display name: PXAP

Pyridoxamine
type: SmallMolecule
entity reference: CHEBI:16410
data source: Provenance1
xref: UnificationXref4582
xref: UnificationXref4583
cellular location: GO:0005829
comment: Reactome DB_ID: 964945
display name: PXA

Pyridoxal
type: SmallMolecule
entity reference: CHEBI:17310
data source: Provenance1
xref: UnificationXref4571
xref: UnificationXref4572
cellular location: GO:0005829
comment: Reactome DB_ID: 965131
display name: PXL

http://identifiers.org/pubmed/8946909
type: PublicationXref
id: 8946909
author: Reinberg, D
author: Lagrange, T
author: Orphanides, G
db: Pubmed
title: The general transcription factors of RNA polymerase II.
source: Genes Dev 10:2657-83
year: 1997

Phosphopantothenoylcysteine
type: SmallMolecule
entity reference: CHEBI:15769
data source: Provenance1
xref: UnificationXref4556
xref: UnificationXref4555
cellular location: GO:0005829
comment: Reactome DB_ID: 196834
display name: PPC

Phospho-pantothenate
type: SmallMolecule
entity reference: CHEBI:15905
data source: Provenance1
xref: UnificationXref4553
xref: UnificationXref4552
cellular location: GO:0005829
comment: Reactome DB_ID: 196786
display name: PPanK

L-2-amino-3-mercaptopropionic acid
type: SmallMolecule
entity reference: CHEBI:17561
data source: Provenance1
name: L-cysteine
xref: UnificationXref4550
xref: UnificationXref4549
cellular location: GO:0005829
comment: Reactome DB_ID: 111707
display name: Cys

Riboflavin-5-phosphate
type: SmallMolecule
entity reference: CHEBI:17621
data source: Provenance1
name: Flavin mononucleotide
xref: UnificationXref4531
xref: UnificationXref4532
cellular location: GO:0005829
comment: Reactome DB_ID: 73524
display name: FMN

UnificationXref4629
type: UnificationXref
id: 3665034
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665034

UnificationXref4628
type: UnificationXref
id: 3665008
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665008

phosphofructokinase, P4 complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry693
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2236
cellular location: GO:0005829
comment: Reactome DB_ID: 3658088

UnificationXref4637
type: UnificationXref
id: 3664989
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664989

phosphofructokinase, L4 complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry692
component: PFK-B
xref: UnificationXref2234
cellular location: GO:0005829
comment: Reactome DB_ID: 3658086

UnificationXref4638
type: UnificationXref
id: 3664990
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664990

phosphofructokinase tetramer
type: Complex
data source: Provenance1
member physical entity: phosphofructokinase, P3L complex (name copied from entity in Homo sapiens)
member physical entity: phosphofructokinase, P4 complex (name copied from entity in Homo sapiens)
member physical entity: phosphofructokinase, PL3 complex (name copied from entity in Homo sapiens)
member physical entity: phosphofructokinase, P2L2 complex (name copied from entity in Homo sapiens)
member physical entity: phosphofructokinase, L4 complex (name copied from entity in Homo sapiens)
xref: UnificationXref2240
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 3658092

UnificationXref4635
type: UnificationXref
id: 3664987
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664987

glucose 6-phosphate isomerase dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry691
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2226
cellular location: GO:0005829
comment: Reactome DB_ID: 3658104

UnificationXref4636
type: UnificationXref
id: 3664988
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664988

CPSF:capped intronless pre-mRNA:CBC complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry687
component stoichiometry: Stoichiometry686
component: CPSF (name copied from entity in Homo sapiens)
component: capped intronless pre-mRNA:CBC complex (name copied from entity in Homo sapiens)
xref: UnificationXref2108
cellular location: GO:0005654
comment: Reactome DB_ID: 3660079

UnificationXref4633
type: UnificationXref
id: 3664984
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664984

CPSF (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry684
component stoichiometry: Stoichiometry682
component stoichiometry: Stoichiometry683
component stoichiometry: Stoichiometry685
component: Note: the coordinates are copied over from Homo sapiens.
component: PhysicalEntity123
component: O13794
xref: UnificationXref2107
cellular location: GO:0005654
comment: Reactome DB_ID: 3658622

UnificationXref4634
type: UnificationXref
id: 3664985
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664985

capped intronless pre-mRNA:CBC complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry680
component stoichiometry: Stoichiometry679
component stoichiometry: Stoichiometry681
component: PhysicalEntity122
component: Protein66
component: Protein65
xref: UnificationXref2098
cellular location: GO:0005654
comment: Reactome DB_ID: 3660078

UnificationXref4631
type: UnificationXref
id: 3664982
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664982

UnificationXref4632
type: UnificationXref
id: 3664983
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3664983

http://identifiers.org/pubmed/12118249
type: PublicationXref
id: 12118249
author: Kato, RM
author: Guo, B
author: Leitges, M
author: Kawakami, T
author: Humphries, LA
author: Patrone, L
author: Wall, R
author: Sommer, K
author: Kang, S
author: Kawakami, Y
author: Teitell, M
author: Su, TT
author: Chae, K
author: Rawlings, DJ
db: Pubmed
title: PKC-beta controls I kappa B kinase lipid raft recruitment and activation in response to BCR signaling
source: Nat Immunol 3:780-6
year: 2002

ChEBI:16290 5alpha-cholesta-7,24-dien-3beta-ol
type: SmallMoleculeReference
name: 5alpha-cholesta-7,24-dien-3beta-ol
xref: UnificationXref3083

UnificationXref4630
type: UnificationXref
id: REACT_165706
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_165706.1

phosphofructokinase, PL3 complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry699
component stoichiometry: Stoichiometry698
component: PFK-B
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2239
cellular location: GO:0005829
comment: Reactome DB_ID: 3658091

phosphofructokinase, P2L2 complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry696
component stoichiometry: Stoichiometry697
component: PFK-B
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2238
cellular location: GO:0005829
comment: Reactome DB_ID: 3658090

phosphofructokinase, P3L complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry695
component stoichiometry: Stoichiometry694
component: PFK-B
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2237
cellular location: GO:0005829
comment: Reactome DB_ID: 3658089

ADP, dADP, CDP, dCDP
type: SmallMolecule
data source: Provenance1
member physical entity: 2'-deoxyadenosine 5'-diphosphate
member physical entity: Cytidine diphosphate
member physical entity: 2'-Deoxycytidine diphosphate
member physical entity: SmallMolecule31
xref: UnificationXref4411
xref: UnificationXref4410
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 500060
display name: (d)ADP, (d)CDP

http://identifiers.org/pubmed/12853446
type: PublicationXref
id: 12853446
author: McCarthy, CC
author: Stringer, DK
author: Koeppel, MA
author: Jakobi, R
db: Pubmed
title: Caspase-activated PAK-2 is regulated by subcellular targeting and proteasomal degradation
source: J Biol Chem 278:38675-85
year: 2003

http://identifiers.org/pubmed/18195086
type: PublicationXref
id: 18195086
author: Ashmore, J
db: Pubmed
title: Cochlear outer hair cell motility
source: Physiol Rev 88:173-210
year: 2008

UnificationXref4639
type: UnificationXref
id: REACT_167884
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_167884.1

http://identifiers.org/pubmed/7228857
type: PublicationXref
id: 7228857
author: Gaylor, JL
author: Grinstead, GF
author: Fukushima, H
db: Pubmed
title: Total enzymic synthesis of cholesterol from lanosterol. Cytochrome b5-dependence of 4-methyl sterol oxidase.
source: J Biol Chem 256:4822-6
year: 1981

60S ribosomal complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry619
component stoichiometry: Stoichiometry622
component stoichiometry: Stoichiometry628
component stoichiometry: Stoichiometry650
component stoichiometry: Stoichiometry614
component stoichiometry: Stoichiometry615
component stoichiometry: Stoichiometry633
component stoichiometry: Stoichiometry647
component stoichiometry: Stoichiometry616
component stoichiometry: Stoichiometry606
component stoichiometry: Stoichiometry630
component stoichiometry: Stoichiometry636
component stoichiometry: Stoichiometry645
component stoichiometry: Stoichiometry632
component stoichiometry: Stoichiometry627
component stoichiometry: Stoichiometry646
component stoichiometry: Stoichiometry607
component stoichiometry: Stoichiometry649
component stoichiometry: Stoichiometry609
component stoichiometry: Stoichiometry644
component stoichiometry: Stoichiometry617
component stoichiometry: Stoichiometry638
component stoichiometry: Stoichiometry629
component stoichiometry: Stoichiometry642
component stoichiometry: Stoichiometry651
component stoichiometry: Stoichiometry621
component stoichiometry: Stoichiometry620
component stoichiometry: Stoichiometry612
component stoichiometry: Stoichiometry608
component stoichiometry: Stoichiometry639
component stoichiometry: Stoichiometry618
component stoichiometry: Stoichiometry635
component stoichiometry: Stoichiometry637
component stoichiometry: Stoichiometry631
component stoichiometry: Stoichiometry611
component stoichiometry: Stoichiometry602
component stoichiometry: Stoichiometry603
component stoichiometry: Stoichiometry613
component stoichiometry: Stoichiometry634
component stoichiometry: Stoichiometry648
component stoichiometry: Stoichiometry610
component stoichiometry: Stoichiometry625
component stoichiometry: Stoichiometry624
component stoichiometry: Stoichiometry626
component stoichiometry: Stoichiometry640
component stoichiometry: Stoichiometry601
component stoichiometry: Stoichiometry604
component stoichiometry: Stoichiometry652
component stoichiometry: Stoichiometry643
component stoichiometry: Stoichiometry623
component stoichiometry: Stoichiometry605
component stoichiometry: Stoichiometry641
component: PhysicalEntity116
component: Homologues of RPL3L(2-407)
component: Homologues of RPL18
component: Note: the coordinates are copied over from Homo sapiens.
component: Homologues of RPL10
component: PhysicalEntity111
component: Homologues of RPL13A
component: Homologues of RPL34
component: Homologues of RPL38
component: Homologues of RPLP2
component: Homologues of RPL21
component: Homologues of RPL7
component: Homologues of RPL4
component: Homologues of RPL27A
component: Homologues of RPL30(2-115)
component: Homologues of RPL9
component: Homologues of RPL19
component: PhysicalEntity114
component: Homologues of RPL15(2-204)
component: Homologues of RPL37A

UnificationXref4646
type: UnificationXref
id: 200499
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=200499

40S ribosomal complex (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry597
component stoichiometry: Stoichiometry598
component stoichiometry: Stoichiometry579
component stoichiometry: Stoichiometry586
component stoichiometry: Stoichiometry592
component stoichiometry: Stoichiometry587
component stoichiometry: Stoichiometry590
component stoichiometry: Stoichiometry585
component stoichiometry: Stoichiometry575
component stoichiometry: Stoichiometry583
component stoichiometry: Stoichiometry599
component stoichiometry: Stoichiometry568
component stoichiometry: Stoichiometry580
component stoichiometry: Stoichiometry574
component stoichiometry: Stoichiometry596
component stoichiometry: Stoichiometry573
component stoichiometry: Stoichiometry578
component stoichiometry: Stoichiometry570
component stoichiometry: Stoichiometry569
component stoichiometry: Stoichiometry572
component stoichiometry: Stoichiometry576
component stoichiometry: Stoichiometry581
component stoichiometry: Stoichiometry571
component stoichiometry: Stoichiometry591
component stoichiometry: Stoichiometry588
component stoichiometry: Stoichiometry595
component stoichiometry: Stoichiometry593
component stoichiometry: Stoichiometry589
component stoichiometry: Stoichiometry577
component stoichiometry: Stoichiometry584
component stoichiometry: Stoichiometry594
component stoichiometry: Stoichiometry567
component stoichiometry: Stoichiometry582
component: Homologues of RPS6
component: Homologues of RPS10
component: Homologues of RPS9
component: Note: the coordinates are copied over from Homo sapiens.
component: Homologues of RPSA
component: Homologues of RPS4X
component: Homologues of RPS24
component: Homologues of RPS26
component: Homologues of RPS17
component: PhysicalEntity106
component: Homologues of RPS3A
component: 40S small ribosomal protein 13
component: Homologues of RPS5(1-204)
component: Homologues of RPS25
component: PhysicalEntity107
component: MPS-1
component: Homologues of RPS27A(77-156)
component: Homologues of RPS12
component: PhysicalEntity108
component: Homologues of RPS8(2-208)
component: Homologues of RPS15
component: Homologues of RPS19
xref: UnificationXref1894
cellular location: GO:0005829
comment: Reactome DB_ID: 3658836

UnificationXref4647
type: UnificationXref
id: REACT_11729
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11729.2

Cap Binding Complex (CBC) (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry656
component stoichiometry: Stoichiometry655
component: Note: the coordinates are copied over from Homo sapiens.
component: NCBP 20 kDa subunit
xref: UnificationXref2067
cellular location: GO:0005829
comment: Reactome DB_ID: 3659903

UnificationXref4648
type: UnificationXref
id: Q9UT53
db: UniProt

mRNA Complex with a Premature Termination Codon Preceding an Exon Junction (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry659
component stoichiometry: Stoichiometry657
component stoichiometry: Stoichiometry660
component stoichiometry: Stoichiometry658
component: Cap Binding Complex (CBC) (name copied from entity in Homo sapiens)
component: PhysicalEntity120
component: PhysicalEntity118
component: PhysicalEntity119
xref: UnificationXref2072
cellular location: GO:0005829
comment: Reactome DB_ID: 3663493

UnificationXref4649
type: UnificationXref
id: 3661745
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661745

UnificationXref4642
type: UnificationXref
id: CHEBI:15763
db: ChEBI

UnificationXref4643
type: UnificationXref
id: 200492
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=200492

80S ribosome (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry600
component stoichiometry: Stoichiometry653
component: 60S ribosomal complex (name copied from entity in Homo sapiens)
component: 40S ribosomal complex (name copied from entity in Homo sapiens)
xref: UnificationXref2064
cellular location: GO:0005829
comment: Reactome DB_ID: 3659275

UnificationXref4644
type: UnificationXref
id: REACT_11276
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11276.1

GDP bound eRF3 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry564
component stoichiometry: Stoichiometry565
component: SmallMolecule18
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref1785
cellular location: GO:0005829
comment: Reactome DB_ID: 3660549

UnificationXref4645
type: UnificationXref
id: CHEBI:18304
db: ChEBI

UnificationXref4640
type: UnificationXref
id: 3665626
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665626

UnificationXref4641
type: UnificationXref
id: REACT_168707
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_168707.1

2'-deoxyadenosine 5'-triphosphate
type: SmallMoleculeReference
name: Deoxyadenosine 5'-triphosphate
name: dATP [ChEBI:16284]
name: dATP
name: Deoxyadenosine triphosphate
xref: UnificationXref2545

Translated mRNA Complex with Premature Termination Codon Not Preceding Exon Junction (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry668
component stoichiometry: Stoichiometry676
component stoichiometry: Stoichiometry675
component stoichiometry: Stoichiometry674
component stoichiometry: Stoichiometry669
component: SmallMolecule59
component: mRNA Complex with a Premature Termination Codon Not Preceding an Exon Junction (name copied from entity in Homo sapiens)
component: 80S ribosome (name copied from entity in Homo sapiens)
component: GDP bound eRF3 (name copied from entity in Homo sapiens)
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref2084
cellular location: GO:0005829
comment: Reactome DB_ID: 3663490

dTDP
type: SmallMolecule
entity reference: dTDP
data source: Provenance1
name: thymidine 5'-diphosphate
name: deoxythymidine 5'-diphosphate
xref: UnificationXref4441
xref: UnificationXref4440
cellular location: GO:0005829
comment: Reactome DB_ID: 110095
display name: TDP

Assembly of the ORC complex at the origin of replication
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction535
pathway component: BiochemicalReaction534
pathway component: BiochemicalReaction532
pathway component: BiochemicalReaction533
evidence: Evidence905
xref: UnificationXref5915
xref: UnificationXref5916
pathway order: PathwayStep887
pathway order: PathwayStep890
pathway order: PathwayStep888
pathway order: PathwayStep889
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

SMG1:Phosphorylated UPF1:EJC:Translated mRNP (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry667
component stoichiometry: Stoichiometry666
component stoichiometry: Stoichiometry665
component: Translated mRNA Complex with Premature Termination Codon Preceding Exon Junction (name copied from entity in Homo sapiens)
component: phospho-p-3S1089,S1107-UPF1
component: SMG1:SMG8:SMG9 Complex (name copied from entity in Homo sapiens)
xref: UnificationXref2076
cellular location: GO:0005829
comment: Reactome DB_ID: 3663530

glutathione disulfide
type: SmallMolecule
entity reference: CHEBI:17858
data source: Provenance1
name: oxidized glutathione
xref: UnificationXref4461
xref: UnificationXref4462
cellular location: GO:0005829
comment: Reactome DB_ID: 111745
display name: GSSG

UPF1:eRF3 Complex on Translated mRNA (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry678
component stoichiometry: Stoichiometry677
component: Note: the coordinates are copied over from Homo sapiens.
component: Translated mRNA Complex with Premature Termination Codon Not Preceding Exon Junction (name copied from entity in Homo sapiens)
xref: UnificationXref2085
cellular location: GO:0005829
comment: Reactome DB_ID: 3663491

mRNA Complex with a Premature Termination Codon Not Preceding an Exon Junction (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry672
component stoichiometry: Stoichiometry671
component stoichiometry: Stoichiometry670
component stoichiometry: Stoichiometry673
component: PhysicalEntity121
component: Cap Binding Complex (CBC) (name copied from entity in Homo sapiens)
component: PhysicalEntity118
component: PhysicalEntity119
xref: UnificationXref2083
cellular location: GO:0005829
comment: Reactome DB_ID: 3663489

http://identifiers.org/pubmed/2188967
type: PublicationXref
id: 2188967
author: Hackert, ML
author: Reed, LJ
db: Pubmed
title: Structure-function relationships in dihydrolipoamide acyltransferases.
source: J Biol Chem 265:8971-4
year: 1990

deoxyguanylic acid
type: SmallMolecule
entity reference: dGMP
data source: Provenance1
name: 2'-deoxyguanosine 5'-monophosphate
xref: UnificationXref4419
xref: UnificationXref4420
cellular location: GO:0005829
comment: Reactome DB_ID: 109327
display name: dGMP

(d)GMP
type: SmallMolecule
data source: Provenance1
member physical entity: deoxyguanylic acid
member physical entity: SmallMolecule57
xref: UnificationXref4421
xref: UnificationXref4422
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 500071

2'-Deoxycytidine diphosphate
type: SmallMolecule
entity reference: dCDP
data source: Provenance1
name: 2'-deoxycytidine 5'-diphosphate
xref: UnificationXref4408
xref: UnificationXref4409
cellular location: GO:0005829
comment: Reactome DB_ID: 110091
display name: dCDP

Cytidine diphosphate
type: SmallMolecule
entity reference: CHEBI:17239
data source: Provenance1
name: cytidine 5'-diphosphate
xref: UnificationXref4405
xref: UnificationXref4406
cellular location: GO:0005829
comment: Reactome DB_ID: 110094
display name: CDP

dUDP, TDP
type: SmallMolecule
data source: Provenance1
member physical entity: dTDP
member physical entity: 2'-deoxyuridine 5'-diphosphate
xref: UnificationXref4442
xref: UnificationXref4443
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 499999

dUMP, TMP
type: SmallMolecule
data source: Provenance1
member physical entity: 2'-Deoxyuridine 5'-phosphate
member physical entity: Deoxythymidylic acid
xref: UnificationXref4435
xref: UnificationXref4434
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 499997

2'-deoxyguanosine 5'-diphosphate
type: SmallMolecule
entity reference: 2'-Deoxyguanosine 5'-diphosphate
data source: Provenance1
xref: UnificationXref4424
xref: UnificationXref4425
cellular location: GO:0005829
comment: Reactome DB_ID: 110092
display name: dGDP

(d)GDP
type: SmallMolecule
data source: Provenance1
member physical entity: 2'-deoxyguanosine 5'-diphosphate
member physical entity: SmallMolecule18
xref: UnificationXref4427
xref: UnificationXref4426
cellular location: GO:0005829
comment: Converted from EntitySet in Reactome
comment: Reactome DB_ID: 500077

http://identifiers.org/pubmed/11001937
type: PublicationXref
id: 11001937
author: Francis, P
author: Berry, V
author: Wyatt, MK
author: Agre, P
author: Yasui, M
author: Bhattacharya, SS
author: Wistow, G
author: Moore, A
author: Chung, JJ
db: Pubmed
title: Functional impairment of lens aquaporin in two families with dominantly inherited cataracts
source: Hum Mol Genet 9:2329-34
year: 2000

2'-deoxyuridine 5'-diphosphate
type: SmallMolecule
entity reference: dUDP [ChEBI:28850]
data source: Provenance1
xref: UnificationXref4438
xref: UnificationXref4437
cellular location: GO:0005829
comment: Reactome DB_ID: 110093
display name: dUDP

http://identifiers.org/pubmed/15337521
type: PublicationXref
id: 15337521
author: Moens, U
author: Johannessen, M
author: Delghandi, MP
db: Pubmed
title: What turns CREB on?
source: Cell Signal 16:1211-27
year: 2004

Catalysis49
type: Catalysis
data source: Provenance1
controlled: RDH8 reduces atRAL to atROL
control type: ACTIVATION
xref: RelationshipXref103
xref: RelationshipXref104
controller: Homologues of RDH8

Catalysis47
type: Catalysis
data source: Provenance1
controlled: GAPs inactivate Rho GTPase:GTP by hydrolysis
control type: ACTIVATION
xref: RelationshipXref80
xref: RelationshipXref101
controller: PhysicalEntity79

Catalysis48
type: Catalysis
data source: Provenance1
controlled: GEFs activate RhoA,B,C
control type: ACTIVATION
xref: RelationshipXref100
xref: RelationshipXref90
controller: PhysicalEntity78

http://identifiers.org/pubmed/12207013
type: PublicationXref
id: 12207013
author: Ma, Sheng
author: Jang, Young-Joo
author: Terada, Yasuhiko
author: Erikson, Raymond L
db: Pubmed
title: Phosphorylation of threonine 210 and the role of serine 137 in the regulation of mammalian polo-like kinase
source: J. Biol. Chem. 277:44115-20
year: 2002

Evidence272
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/20398727
xref: http://identifiers.org/pubmed/16816139
comment: Gastrin, through the action of diacylglycerol produced from downstream G alpha (q) events, transactivates EGFR via a PKC-mediated pathway by activation of MMP3 (Matrix Metalloproteinase 3) which allows formation of mature HBEGF (heparin-binding epidermal growth factor) by cleaving pro-HBEGF. Mature HBEGF is then free to bind the EGFR, resulting in EGFR activation (Dufresne et al. 2006, Liebmann 2011).

Evidence273
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10413847
xref: http://identifiers.org/pubmed/7491953
xref: http://identifiers.org/pubmed/17698287
comment: Gastrin is a hormone whose main function is to stimulate secretion of hydrochloric acid by the gastric mucosa, which results in gastrin formation inhibition. This hormone also acts as a mitogenic factor for gastrointestinal epithelial cells. Gastrin has two biologically active peptide forms, G34 and G17.Gastrin gene expression is upregulated in both a number of pre-malignant conditions and in established cancer through a variety of mechanisms. Depending on the tissue where it is expressed and the level of expression, differential processing of the polypeptide product leads to the production of different biologically active peptides. In turn, acting through the classical gastrin cholecystokinin B receptor CCK-BR, its isoforms and alternative receptors, these peptides trigger signalling pathways which influence the expression of downstream genes that affect cell survival, angiogenesis and invasion (Wank 1995, de Weerth et al. 1999, Grabowska & Watson 2007)

Evidence270
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9422713
xref: http://identifiers.org/pubmed/9218123
xref: http://identifiers.org/pubmed/16612131
comment: Opioids are chemical substances similar to opiates, the active substances found in opium (morphine, codeine etc.). Opioid action is mediated by the receptors for endogenous opioids; peptides such as the enkephalins, the endorphins or the dynorphins. Opioids possess powerful analgesic and sedative effects, and are widely used as pain-killers. Their main side-effect is the rapid establishment of a strong addiction. Opioids receptors are G-protein coupled receptors (GPCR). There are four classes of receptors: mu (MOR), kappa (KOR) and delta (DOR), and the nociceptin receptor (NOP).

Evidence271
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11588141
comment: Diacylglycerol, produced by PLC beta-mediated PIP2 hydrolysis in G alpha (q) signalling, remains in the plasma membrane and binds Protein Kinase C alpha (PKC-alpha), causing PKC-alpha to translocate from the cytosol to the plasma membrane. PKC-alpha is thereby activated and phosphorylates target proteins.

http://identifiers.org/pubmed/12145188
type: PublicationXref
id: 12145188
author: Hardt, B
author: Völker, C
author: Van Coster, RN
author: Breuer, W
author: Bause, E
author: De Praeter, CM
author: Kalz-Füller, B
db: Pubmed
title: Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb)
source: Glycobiology 12:473-83
year: 2002

UniProt:P30290
type: ProteinReference
xref: UnificationXref7704
organism: BioSource1

Evidence269
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/14744247
xref: http://identifiers.org/pubmed/2908293
comment: Dopamine- and cAMP-regulated phosphoprotein, Mr 32 kDa (DARPP-32), was identified as a major target for dopamine and protein kinase A (PKA) in striatum. Recent advances now indicate that regulation DARPP-32 phosphorylation provides a mechanism for integrating information arriving at dopaminoceptive neurons, in multiple brain regions, via a variety of neurotransmitters, neuromodulators, neuropeptides, and steroid hormones. Activation of PKA or PKG stimulates DARPP-32 phosphorylation at Thr34, converting DARPP-32 into a potent inhibitor of protein phosphatase-1 (PP-1). DARPP-32 is also phosphorylated at Thr75 by Cdk5, converting DARPP-32 into an inhibitor of PKA. Thus, DARPP-32 has the unique property of being a dual-function protein, acting either as an inhibitor of PP-1 or of PKA.

Evidence268
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9422713
xref: http://identifiers.org/pubmed/9218123
comment: When dissociated Galpha-GTP and Gbeta-gamma can activate or inhibit different signalling cascades and effector proteins. The precise pathways depends on the identity of the alpha and beta/gamma subtypes.

Evidence267
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16183910
xref: http://identifiers.org/pubmed/9218123
xref: http://identifiers.org/pubmed/1335363
comment: The phospholipase C (PLC) family of enzymes is both diverse and complex. The isoforms beta, gamma and delta (each have subtypes) make up the members of this family. PLC hydrolyzes phosphatidylinositol bisphosphate (PIP2) into two second messengers, inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). IP3 mobilizes intracellular calcium stores while DAG activates protein kinase C isoforms which are involved in regulatory functions.

Evidence266
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18083096
xref: http://identifiers.org/pubmed/11162741
xref: http://identifiers.org/pubmed/16076488
xref: http://identifiers.org/pubmed/17697045
comment: Calcium, as the ion Ca2+, is essential in many biological processes. The majority of Ca2+ in many organisms is bound to phosphates which form skeletal structures and also buffer Ca2+ levels in extracellular fluids (typically 1 millimolar). Intracellular free Ca2+, by contrast, is 10,000 times lower than the outside of the cell (typically 10 micromolar). This concentration gradient is used to import Ca2+ into cells where it acts as a second messenger.

Evidence265
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18515421
xref: http://identifiers.org/pubmed/13679574
xref: http://identifiers.org/pubmed/18240029
xref: http://identifiers.org/pubmed/12040175
xref: http://identifiers.org/pubmed/19935667
xref: http://identifiers.org/pubmed/18488142
xref: http://identifiers.org/pubmed/15251227
comment: G protein-coupled receptors (GPCRs) are classically defined as the receptor, G-protein and downstream effectors, the alpha subunit of the G-protein being the primary signaling molecule. However, it has become clear that this greatly oversimplifies the complexities of GPCR signaling (see Gurevich & Gurevich, 2008). The beta:gamma G-protein dimer is also involved in downstream signaling (Smrcka, 2008), and some receptors form part of metastable complexes of receptor and accessory proteins such as the arrestins. GPCRs are involved in many diverse signaling events (Kristiansen 2004), using a variety of pathways that include modulation of adenylyl cyclase, phospholipase C, the mitogen activated protein kinases (MAPKs), extracellular signal regulated kinase (ERK) c-Jun-NH2-terminal kinase (JNK) and p38 MAPK.

Evidence264
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18834311
comment: The classical role of the G-protein beta/gamma dimer was believed to be the inactivation of the alpha subunit, Gbeta/gamma was viewed as a negative regulator of Galpha signalling. It is now known that Gbeta/gamma subunits can directly modulate many effectors, including some also regulated by G alpha.

http://identifiers.org/pubmed/10358005
type: PublicationXref
id: 10358005
author: Kobayashi, T
author: Katada, T
author: Imai, M
author: Hoshino, S
author: Uchida, N
db: Pubmed
title: The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3'-Poly(A) tail of mRNA. Direct association of erf3/GSPT with polyadenylate-binding protein.
source: J Biol Chem 274:16677-80
year: 1999

Evidence263
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17041586
xref: http://identifiers.org/pubmed/17916723
comment: PI3K gamma (PI3KG) is a heterodimer consisting of a p110 catalytic subunit associated with a regulatory p101 or p84 subunit. PI3KG is most highly expressed in neutrophils, where the p101 form predominates (approximately 95%). G beta:gamma recruits PI3KG to the plasma membrane, both activating PI3KG and providing access to its substrate PIP2, which is converted to PIP3.

Catalysis42
type: Catalysis
data source: Provenance1
controlled: TSC2 activates intrinsic GTPase activity of Rheb
control type: ACTIVATION
xref: RelationshipXref80
xref: RelationshipXref81
controller: TSC1:p-S1387-TSC2 (name copied from entity in Homo sapiens)

Catalysis41
type: Catalysis
data source: Provenance1
controlled: Phosphorylation and activation of eIF4B by activated S6K1
control type: ACTIVATION
xref: RelationshipXref16
xref: RelationshipXref79
controller: phospho-p-S371,T389-RPS6KB1

Catalysis40
type: Catalysis
data source: Provenance1
controlled: Phosphorylation of Ribosomal protein S6 by activated S6K1
control type: ACTIVATION
xref: RelationshipXref16
xref: RelationshipXref79
controller: phospho-p-S371,T389-RPS6KB1

Catalysis46
type: Catalysis
data source: Provenance1
controlled: GEFs activate Rho GTPase:GDP
control type: ACTIVATION
xref: RelationshipXref100
xref: RelationshipXref90
controller: PhysicalEntity78

Catalysis45
type: Catalysis
data source: Provenance1
controlled: RhoA is activated by nucleotide exchange and inhibits axonal growth
control type: ACTIVATION
xref: RelationshipXref91
xref: RelationshipXref90
controller: Homologues of ARHGEF1

Catalysis44
type: Catalysis
data source: Provenance1
controlled: Production of ceramide which can activate JNK and other targets
control type: ACTIVATION
xref: RelationshipXref88
xref: RelationshipXref89
controller: Active N-SMase:Mg2+ (name copied from entity in Homo sapiens)

Catalysis43
type: Catalysis
data source: Provenance1
controlled: Endosome acidification
control type: ACTIVATION
xref: RelationshipXref84
xref: RelationshipXref83
controller: V-ATPase (name copied from entity in Homo sapiens)

Catalysis58
type: Catalysis
data source: Provenance1
controlled: SMG1 Phosphorylates UPF1 (Enhanced by Exon Junction Complex)
control type: ACTIVATION
xref: RelationshipXref125
xref: RelationshipXref124
controller: SMG1:UPF1:EJC:Translated mRNP (name copied from entity in Homo sapiens)

Catalysis59
type: Catalysis
data source: Provenance1
controlled: Autophosphorylation of PAK-2p34 in the activation loop
control type: ACTIVATION
xref: RelationshipXref131
xref: RelationshipXref16
controller: Homologues of PAK2(213-524)

http://identifiers.org/pubmed/17242360
type: PublicationXref
id: 17242360
author: Jackowski, S
author: Zhang, YM
author: Rock, CO
author: Leonardi, R
db: Pubmed
title: Activation of human mitochondrial pantothenate kinase 2 by palmitoylcarnitine
source: Proc Natl Acad Sci U S A 104:1494-9
year: 2007

Evidence281
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/21042815
xref: http://identifiers.org/pubmed/20975071
xref: http://identifiers.org/pubmed/22649417
xref: http://identifiers.org/pubmed/20098959
xref: http://identifiers.org/pubmed/17598937
xref: http://identifiers.org/pubmed/18927274
comment: The phosphorylated type 1 insulin-like growth factor receptor phosphorylates IR1, IRS2, IRS4 and possibly other IRS/DOK family members (reviewed in Pavelic et al. 2007, Chitnis et al. 2008, Maki et al. 2010, Parrella et al. 2010, Siddle et al. 2012). The phosphorylated IRS proteins serve as scaffolds that bind the effector molecules PI3K and GRB2:SOS. PI3K then activates PKB (AKT) signaling while GRB2:SOS activates RAS-RAF-MAPK signaling.

Evidence282
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/21042815
xref: http://identifiers.org/pubmed/20975071
xref: http://identifiers.org/pubmed/22649417
xref: http://identifiers.org/pubmed/20098959
xref: http://identifiers.org/pubmed/17598937
xref: http://identifiers.org/pubmed/18927274
comment: After autophosphorylation the type 1 insulin-like growth factor receptor (IGF1R) binds and phosphorylates scaffold proteins, IRS1/2/4 and SHC1, which in turn bind effectors possessing enzymatic activity (recently reviewed in Pavelic et al. 2007, Chitnis et al. 2008, Maki et al. 2010, Parrella et al. 2010, and Siddle et al. 2012). IRS1/2/4 can bind both PI3K (via the p85 subunit of PI3K) and the GRB2:SOS complex. PI3K activates PKB (AKT, AKT1) signaling. GRB:SOS stimulates RAS to exchange GDP for GTP leading to activation of RAF and MAPK.

Evidence283
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/22044904
xref: http://identifiers.org/pubmed/21042815
xref: http://identifiers.org/pubmed/20975071
xref: http://identifiers.org/pubmed/22649417
xref: http://identifiers.org/pubmed/20098959
xref: http://identifiers.org/pubmed/17598937
xref: http://identifiers.org/pubmed/18927274
comment: Binding of IGF1 (IGF-I) or IGF2 (IGF-II) to the extracellular alpha peptides of the type 1 insulin-like growth factor receptor (IGF1R) triggers the activation of two major signaling pathways: the SOS-RAS-RAF-MAPK (ERK) pathway and the PI3K-PKB (AKT) pathway (recently reviewed in Pavelic et al. 2007, Chitnis et al. 2008, Maki et al. 2010, Parella et al. 2010, Annunziata et al. 2011, Siddle et al. 2012, Holzenberger 2012).

Evidence284
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10753906
comment: The reversible, NADP(H)-dependent reduction of all-trans-retinal (atRAL) to all-trans-retinol (atROL) occurs in both rod and cone photoreceptor cells where multiple retinol dehydrogenases (RHDs) are located. RHDs belong to the short-chain dehydrogenase/reductase (SDR) superfamily. RDH8 (located in photoreceptor outer segments) is partially responsible, together with other RDHs, for mediating this reaction. The activity for human RDH8 is inferred from a bovine experiment (Rattner et al. 2000).

Evidence280
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/20975071
xref: http://identifiers.org/pubmed/22649417
xref: http://identifiers.org/pubmed/20098959
xref: http://identifiers.org/pubmed/17598937
xref: http://identifiers.org/pubmed/18927274
comment: Phosphorylated IGF1R binds and phosphorylates SHC1 (reviewed in Pavelic et al. 2007, Chitnis et al. 2008, Maki et al. 2010, Parrella et al. 2010, Siddle et al. 2012). Phosphorylated SHC then binds GRB:SOS, which activates RAS-RAF-MAPK signaling.

Evidence279
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18710302
xref: http://identifiers.org/pubmed/19204114
xref: http://identifiers.org/pubmed/16099039
xref: http://identifiers.org/pubmed/23256519
xref: http://identifiers.org/pubmed/10858654
xref: http://identifiers.org/pubmed/17143292
xref: http://identifiers.org/pubmed/22952392
xref: http://identifiers.org/pubmed/12967557
xref: http://identifiers.org/pubmed/19365405
xref: http://identifiers.org/pubmed/19619488
xref: http://identifiers.org/pubmed/19530173
xref: http://identifiers.org/pubmed/17230199
xref: http://identifiers.org/pubmed/20576942
comment: WNT signaling pathways control a wide range of developmental and adult process in metozoans including cell proliferation, cell fate decisions, cell polarity and stem cell maintenance (reviewed in Saito-Diaz et al, 2013; MacDonald et al, 2009). The pathway is named for the WNT ligands, a large family of secreted cysteine-rich glycoproteins. At least 19 WNT members have been identified in humans and mice with distinct expression patterns during development (reviewed in Willert and Nusse, 2012). These ligands can activate at least three different downstream signaling cascades depending on which receptors they engage. In the so-called 'canonical' WNT signaling pathway, WNT ligands bind one of the 10 human Frizzled (FZD) receptors in conjunction with the LRP5/6 co-receptors to activate a transcriptional cascade that controls processes such as cell fate, proliferation and self-renenwal of stem cells. Engagement of the FZD-LRP receptor by WNT ligand results in the stabilization and translocation of cytosolic beta-catenin to the nucleus where it is a co-activator for LEF (lymphoid enhancer-binding factor)- and TCF (T cell factor) -dependent transcription. In the absence of WNT ligand, cytosolic beta-catenin is phosphorylated by a degradation complex consisting of glycogen synthase kinase 3 (GSK3), casein kinase 1 (CK1), Axin and Adenomatous polyposis coli (APC), and subsequently ubiquitinated and degraded by the 26S proteasome (reviewed in Saito-Diaz et al, 2013; Kimmelman and Xu, 2006). In addition to the beta-catenin-dependent transcriptional response, WNT signaling can also activate distinct non-transcriptional pathways that regulate cell migration and polarity. These beta-catenin-independent 'non-canonical' pathways signal through Frizzled receptors independently of LRP5/6, or occur through the tyrosine kinase receptors ROR and RYK (reviewed in Veeman et al, 2003; James et al, 2009). Non-canonical WNT pathways are best studied in Drosophila where the planar cell polarit…

Evidence278
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16678095
xref: http://identifiers.org/pubmed/21768372
xref: http://identifiers.org/pubmed/17108000
xref: http://identifiers.org/pubmed/22653731
xref: http://identifiers.org/pubmed/23256519
xref: http://identifiers.org/pubmed/23260141
xref: http://identifiers.org/pubmed/22983114
xref: http://identifiers.org/pubmed/19837038
xref: http://identifiers.org/pubmed/21725318
xref: http://identifiers.org/pubmed/22952392
xref: http://identifiers.org/pubmed/22796206
xref: http://identifiers.org/pubmed/16678096
xref: http://identifiers.org/pubmed/21554866
xref: http://identifiers.org/pubmed/17141155
comment: 19 WNT proteins have been identified in human cells. The WNTs are members of a conserved metazoan family of secreted morphogens that activate several signaling pathways in the responding cell: the canonical (beta-catenin) WNT signaling cascade and several non-canonical pathways, including the planar cell polarity (PCP), the regulation of intracellular calcium signaling and activation of JNK kinases. WNT proteins exist in a gradient outside the secreting cell and are able to act over both short and long ranges to promote proliferation, changes in cell migration and polarity and tissue homeostasis, among others (reviewed in Saito-Diaz et al, 2012; Willert and Nusse, 2012). The WNTs are ~40kDa proteins with 23 conserved cysteine residues in the N-terminal that may form intramolecular disulphide bonds. They also contain an N-terminal signal sequence and a number of N-linked glycosylation sites (Janda et al, 2012). In addition to being glycosylated, WNTs are also lipid-modified in the endoplasmic reticulum by a WNT-specific O-acyl-transferase, Porcupine (PORCN), contributing to their characteristic hydrophobicity. PORCN-dependent palmitoylation is required for the secretion of WNT as well as its signaling activity, as either depletion of PORCN or mutation of the conserved serine acylation site results in the intracellular accumulation of WNT ligand (Takada et al, 2006; Barrott et al, 2011; Biechele et al, 2011; reviewed in Willert and Nusse, 2012). Secretion of WNT requires a number of other dedicated factors including the sorting receptor Wntless (WLS) (also knownas Evi, Sprinter, and GPR177), which binds WNT and escorts it to the cell surface (Bänziger et al, 2006; Bartscherer et al, 2006; Goodman et al, 2006). A WNT-specific retromer containing SNX3 is subsequently required for the recycling of WLS back to the Golgi (reviewed in Herr et al, 2012; Johannes and Wunder, 2011). Once at the cell surface, WNT makes extensive contacts with components of the extracellular mat…

Evidence275
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8167409
xref: http://identifiers.org/pubmed/17397399
xref: http://identifiers.org/pubmed/17117926
xref: http://identifiers.org/pubmed/12717451
xref: http://identifiers.org/pubmed/22108505
comment: All WNT ligands are predicted to be highly glycosylated. By similarity with WNT ligands in mouse, human WNTs are believed to undergo N-linked glycosylation at multiple asparagine residues and this glycosylation is critical for their secretion (Smolich et al, 1993; Willert et al, 2003, Komekado et al, 2006; Kurayoshi et al, 2007). The mechanism of N-linked glycosylation is not shown here. For a more detailed description, please refer to pathway "Asparagine N-linked glycosylation".

Evidence274
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16902930
xref: http://identifiers.org/pubmed/18043707
xref: http://identifiers.org/pubmed/10202136
comment: G protein-coupled receptors (GPCRs; 7TM receptors; seven transmembrane domain receptors; heptahelical receptors; G protein-linked receptors [GPLR]) are the largest family of transmembrane receptors in humans, accounting for more than 1% of the protein-coding capacity of the human genome. All known GPCRs share a common architecture of seven membrane-spanning helices connected by intra- and extracellular loops. The extracellular loops contain two highly-conserved cysteine residues that form disulphide bonds to stabilize the structure of the receptor. They recognize diverse messengers such as light, odorants, small molecules, hormones and neurotransmitters. Most GPCRs act as guanine nucleotide exchange factors; activated by ligand binding, they promote GDP-GTP exchange on associated heterotrimeric guanine nucleotide-binding (G) proteins. There are two models for GPCR-G Protein interactions: 1) ligand-GPCR binding first, then binding to G Proteins; 2) "Pre-coupling" of GPCRs and G Proteins before ligand binding (review Oldham WM and Hamm HE, 2008). These in turn activate effector enzymes or ion channels. GPCRs are involved in a range of physiological roles which include the visual sense, smell, behavioural regulation, functions of the autonomic nervous system and regulation of the immune system and inflammation. GPCRs are divided into 6 classes based on sequence homology and functional similarity; the main mammalian families are classes A/1-C/3; Class A/1 (Rhodopsin-like) Class B/2 (Secretin receptor family) Class C/3 (Metabotropic glutamate/pheromones) Class D/4 (fungal mating pheromone receptors) Class E/5 (cAMP receptors) Class F/6 (Frizzled/Smoothened) Here, those Class A/1 (Rhodopsin-like) receptors that bind peptide ligands have been annotated. The binding events mediated by other classes of receptors, as well as the downstream events triggered by receptor-ligand interactions will be annotated in future releases of Reactome.

Evidence277
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/22952392
xref: http://identifiers.org/pubmed/21725318
comment: Retromer is believed to escort WLS from the early endosome back to the Golgi for subsequent rounds of WNT secretion (reviewed in Johannes and Wunder, 2011; Willert and Nusse, 2012 ).

Evidence276
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/22094269
xref: http://identifiers.org/pubmed/19566487
xref: http://identifiers.org/pubmed/11031247
xref: http://identifiers.org/pubmed/22094272
xref: http://identifiers.org/pubmed/20533886
xref: http://identifiers.org/pubmed/21886182
comment: This black box event represents the non-WNT-specific ER-to-Golgi trafficking step of protein secretion (reviewed in Dancourt and Barlowe, 2010; Lippincott Schwatz et al, 2000; for more details, please refer to the pathway "ER to Golgi transport"). Two recent screens in Drosophila have identified members of the p24 family as WNT-specific regulators of ER-to-Golgi transport, although the details have not been elucidated (Port et al, 2011; Buechling et al, 2011; reviewed in Strating and Martens, 2009). Depletion of the Drosophila p24 protein Opossum causes accumulation of WNT ligand in the ER, suggesting a role for Opm in ER-to-Golgi transport of WNTs. WNT-dependent reporter activity was reduced in HEK293 cells that were depleted for the human p24 homologue TMED5, supporting a conserved role for these proteins in WNT signaling (Buechling et al, 2011; reviewed in Palmer et al, 2012).

Catalysis51
type: Catalysis
data source: Provenance1
controlled: pyrophosphate + H2O => 2 orthophosphate [cytosolic]
control type: ACTIVATION
xref: RelationshipXref109
xref: RelationshipXref108
controller: PPA1 dimer (name copied from entity in Homo sapiens)

Catalysis50
type: Catalysis
data source: Provenance1
controlled: atRAL is reduced to atROL
control type: ACTIVATION
xref: RelationshipXref103
xref: RelationshipXref106
controller: Note: the coordinates are copied over from Homo sapiens.

Catalysis53
type: Catalysis
data source: Provenance1
controlled: Formation of Double-strand Break in DNA by SPO11
control type: ACTIVATION
xref: RelationshipXref113
xref: RelationshipXref112
controller: SPO11 Dimer (name copied from entity in Homo sapiens)

Catalysis52
type: Catalysis
data source: Provenance1
controlled: pyrophosphate + H2O => 2 orthophosphate [mitochondrial]
control type: ACTIVATION
xref: RelationshipXref108
xref: RelationshipXref110
controller: PPA2 dimer (name copied from entity in Homo sapiens)

Catalysis55
type: Catalysis
data source: Provenance1
controlled: Scavenging of the 7-methylguanosine Cap by DCPS
control type: ACTIVATION
xref: RelationshipXref116
xref: RelationshipXref117
controller: Note: the coordinates are copied over from Homo sapiens.

Catalysis54
type: Catalysis
data source: Provenance1
controlled: 3' to 5' Exoribonuclease Digestion of mRNA by the Exosome Complex
control type: ACTIVATION
xref: RelationshipXref114
xref: RelationshipXref115
controller: Exosome Complex (name copied from entity in Homo sapiens)

Catalysis57
type: Catalysis
data source: Provenance1
controlled: Destruction of AUF1 and mRNA
control type: ACTIVATION
xref: RelationshipXref122
xref: RelationshipXref123
controller: 26S proteasome (name copied from entity in Homo sapiens)

Catalysis56
type: Catalysis
data source: Provenance1
controlled: 5' to 3' Exoribonuclease Digestion of Decapped mRNA
control type: ACTIVATION
xref: RelationshipXref119
xref: RelationshipXref120
controller: XRN1_HUMAN

Catalysis29
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction63
control type: ACTIVATION
xref: RelationshipXref43
xref: RelationshipXref44
controller: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)

Catalysis27
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction61
control type: ACTIVATION
xref: RelationshipXref26
xref: RelationshipXref42
controller: TFIIH (name copied from entity in Homo sapiens)

Catalysis28
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction62
control type: ACTIVATION
xref: RelationshipXref43
xref: RelationshipXref44
controller: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)

Catalysis25
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction60
control type: ACTIVATION
xref: RelationshipXref26
xref: RelationshipXref42
controller: TFIIH (name copied from entity in Homo sapiens)

Catalysis26
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction61
control type: ACTIVATION
xref: RelationshipXref43
xref: RelationshipXref44
controller: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)

Evidence290
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/6022858
xref: http://identifiers.org/pubmed/4130389
xref: http://identifiers.org/pubmed/656444
comment: Cytosolic PPA1 (pyrophosphatase (inorganic) 1) catalyzes the hydrolysis of pyrophosphate to yield two molecules of orthophosphate. The enzyme, a homodimer, requires Mg++ for activity (Fisher et al. 1974; Pynes and Younathan 1967; Thuiller et al. 1978).

Evidence291
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16300924
comment: Mitochondrial PPA2 (pyrophosphatase (inorganic) 2) catalyzes the hydrolysis of pyrophosphate to yield two molecules of orthophosphate. The enzyme requires Mg++ for activity (Curbo et al. 2006). The enzyme is inferred to be a homodimer by analogy to its cytosolic isoform.

Evidence294
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16543383
xref: http://identifiers.org/pubmed/20364103
xref: http://identifiers.org/pubmed/20051984
comment: Meiotic recombination exchanges segments of duplex DNA between chromosomal homologs, generating genetic diversity (reviewed in Handel and Schimenti 2010, Inagaki et al. 2010, Cohen et al. 2006). There are two forms of recombination: non-crossover (NCO) and crossover (CO). In mammals, the former is required for correct pairing and synapsis of homologous chromosomes, while CO intermediates called chiasmata are required for correct segregation of bivalents. Meiotic recombination is initiated by double-strand breaks created by SPO11, which remains covalently attached to the 5' ends after cleavage. SPO11 is removed by cleavage of single DNA strands adjacent to the covalent linkage. The resulting 5' ends are further resected to produce protruding 3' ends. The single-stranded 3' ends are bound by RAD51 and DMC1, homologs of RecA that catalyze a search for homology between the bound single strand and duplex DNA of the chromosomal homolog. RAD51 and DMC1 then catalyze the invasion of the single strand into the homologous duplex and the formation of a D-loop heteroduplex. Approximately 90% of heteroduplexes are resolved without crossovers (NCO), probably by synthesis-dependent strand annealing. The invasive strand is extended along the homolog and ligated back to its original duplex, creating a double Holliday junction. The mismatch repair proteins MSH4, MSH5 participate in this process, possibly by stabilizing the duplexes. The mismatch repair proteins MLH1 and MLH3 are then recruited to the double Holliday structure and an unidentified resolvase (Mus81? Gen1?) cleaves the junctions to yield a crossover. Crossovers are not randomly distributed: The histone methyltransferase PRDM9 recruits the recombination machinery to genetically determined hotspots in the genome and each incipient crossover somehow inhibits formation of crossovers nearby, a phenomenon called crossover interference. Each chromosome bivalent, including the X-Y body in males, has at least one crossover and th…

Evidence295
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16543383
xref: http://identifiers.org/pubmed/20364103
xref: http://identifiers.org/pubmed/18948708
xref: http://identifiers.org/pubmed/20051984
comment: During meiosis the replicated chromosomes of a single diploid cell are segregated into 4 haploid daughter cells by two successive divisions, meiosis I and meiosis II. In meiosis I, the distinguishing event of meiosis, pairs (bivalents) of homologous chromosomes in the form of sister chromatids are paired, synapsed along their regions of homologous DNA (reviewed in Yang and Wang 2009), and then segregated, resulting in haploid daughters containing sister chromatids paired at their centromeres (reviewed in Cohen et al. 2006, Handel and Schimenti 2010). The sister chromatids are then separated and segregated during meiosis II. Recombination between chromosomal homologues but not between sister chromatids occurs during prophase of meiosis I (reviewed in Inagaki et al. 2010). Though hundreds of recombination events are initiated, most are resolved without crossovers and only tens proceed to become crossovers. In mammals recombination events are required between homologues for normal pairing, synapsis, and segregation.

Evidence292
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/6120771
comment: Many biosynthetic reactions are coupled to the cleavage of ATP to yield AMP and pyrophosphate. These reactions are typically freely reversible when carried out with purified substrates and enzymes in vitro. In vivo, however, the pyrophosphate is rapdily and essentially irreversibly hydrolyzed by a ubiquitous inorganic pyrophosphatase. This hydrolysis has the effect of pulling the first reaction strongly in the direction of biosynthesis, at the expense of two high-energy phosphate bonds. Studies of human cells have identified two forms of the enzyme, one localized to the cytosol and the other to the mitochondrial matrix (Raja et al. 1981).

UniProt:Q09914
type: ProteinReference
xref: UnificationXref736
organism: BioSource1

Evidence293
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: The gene encoding SPO11 shares sequence similarity to TopoVI, a type II topoisomerase. SPO11 dimers cleave both strands of DNA. Each subunit of the dimer remains covalently attached to the 5' end of one strand of DNA via a phosphodiester linkage to a conserved tyrosine residue of SPO11. In addition to SPO11, work from budding yeast has shown a total of 7 proteins essential for double strand break formation. The mammalian ortholog of Mei4 (S. cerevisiae) as well as a mammalian-specific gene called Mei1 are essential to formation of meiotic double strand breaks.

Evidence288
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/21111842
xref: http://identifiers.org/pubmed/22658984
xref: http://identifiers.org/pubmed/22074928
xref: http://identifiers.org/pubmed/11340090
xref: http://identifiers.org/pubmed/21350678
xref: http://identifiers.org/pubmed/15384919
xref: http://identifiers.org/pubmed/22074927
xref: http://identifiers.org/pubmed/16688755
xref: http://identifiers.org/pubmed/20188572
xref: http://identifiers.org/pubmed/16011460
xref: http://identifiers.org/pubmed/8382952
xref: http://identifiers.org/pubmed/20430952
comment: Visual phototransduction is the process by which photon absorption by visual pigment molecules in photoreceptor cells is converted to an electrical cellular response. The events in this process are photochemical, biochemical and electrophysiological and are highly conserved across many species. This process occurs in two types of photoreceptors in the retina, rods and cones. Each type consists of two parts, the outer segment which detects a photon signal and the inner segment which contains the necessary machinery for cell metabolism. Each type of cell functions differently. Rods are very light sensitive but their flash response is slow so they work best in twilight conditions but are not good at detecting objects moving quickly. Cones are less light-sensitive and have a fast flash response so they work best in daylight conditions and are better at detecting fast moving objects than rods. The visual pigment consists of a chromophore (11-cis-retinal, 11cRAL, A1) covalently attached to a GPCR opsin family member. The linkage is via a Schiff base forming retinylidene protein. Upon photon absorption, 11cRAL isomerises to all-trans retinal (atRAL), changing the conformation of opsin to an activated form which can activate the regulatory G protein transducin (Gt). The alpha subunit of Gt activates phosphodiesterase which hydrolyses cGMP to 5'-GMP. As high level of cGMP keep cGMP-gated sodium channels open, the lowering of cGMP levels closes these channels which causes hyperpolarization of the cell and subsequently, closure of voltage-gated calcium channels. As calcium levels drop, the level of the neurotransmitter glutamate also drops causing depolarization of the cell. This effectively relays the light signal to postsynaptic neurons as electrical signal (Burns & Pugh 2010, Korenbrot 2012, Pugh & Lamb 1993). 11cRAL cannot be synthesised in vertebrates. Vitamin A from many dietary sources is the precursor for 11cRAL. It is taken from food in the form of esters such as reti…

Evidence287
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/21111842
xref: http://identifiers.org/pubmed/22074928
xref: http://identifiers.org/pubmed/15384919
xref: http://identifiers.org/pubmed/22074927
comment: Rods and cones share the same mechanism for the phototransduction process but perform functionally different roles. Although cone photoreceptors make up around 5% of all photoreceptor cells and are outnumbered 20 to 1 by rod photoreceptors, they mediate daylight vision in the human eye whereas rods mediate twilight vision. Also, cones are around 100-times less light-sensitive than rods thereby depriving us of colour vision in dark conditions in which cones cannot function. Rod function saturates in even moderate amounts of light whereas cones can adjust to even very bright light conditions, a process called light adaptation. In bright conditions, rods can take up to one hour to regain their sensitivity whereas cones can recover in a few minutes, a process called dark adaptation and which allows us to retain visual perception in changing light conditions. Cone cells express three types of opsin which allow colour discrimination. Long Wavelength Sensitive Opsin (OPN1LW) detects red , Short Wavelength Sensitive Opsin (OPN1SW) detects blue, and Short Wavelength Sensitive Opsin (OPN1SW) detects green regions of the light spectrum. In the canonical retinoid (visual) cycle, the visual chromophore is regenerated in reactions involving the rod outer segments (ROS) and the retinal pigment epithelium (RPE). For cones, chromophore recycling is independent of the RPE and instead involves Muller cells in the retina which supply the chromophore selectively to cones. The molecular steps of the cone retinoid (visual) cycle are outlined in this section. The ability of cones to react to bright and differing light conditions means it has to regenerate the chromophore much quicker than rods. All-trans-retinol (atROL) released from cone outer segments is taken up by Muller cells where it is directly isomerized back to 11-cis-retinol (11cROL) then esterified by LRAT. When required, these 11-cis-retinyl esters can be hydrolysed by 11-cis-RE hydrolases back to 11cROL then oxidised in the co…

Evidence286
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9705317
comment: All-trans-retinal (atRAL) can diffuse across membranes to the cytosol and is reduced to all-trans-retinol (atROL) by the action of a short-chain dehydrogenase/reductase 3 using NADP+/NADPH as cofactor (Haeseleer et al. 1998).

Evidence285
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/21350678
xref: http://identifiers.org/pubmed/22074927
xref: http://identifiers.org/pubmed/16688755
xref: http://identifiers.org/pubmed/20188572
comment: The retinoid cycle (also referred to as the visual cycle) is the process by which the visual chromophore 11-cis-retinal (11cRAL) is released from light-activated opsins in the form all-trans-retinal and isomerized back to its 11-cis isomer ready for another photoisomerization reaction. This process involves oxidation, reduction and isomerization reactions and take place in the retinal pigment epithelium (RPE) and photoreceptor segments of the eye (von Lintig 2012, Blomhoff & Blomhoff 2006, von Lintig et al. 2010, D'Ambrosio et al. 2011). This section describes the retinoid cycle in rods during dark/twilight conditions.

Evidence289
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19648010
xref: http://identifiers.org/pubmed/18483217
xref: http://identifiers.org/pubmed/15520807
xref: http://identifiers.org/pubmed/19379690
xref: http://identifiers.org/pubmed/21781017
xref: http://identifiers.org/pubmed/21252999
xref: http://identifiers.org/pubmed/19935667
xref: http://identifiers.org/pubmed/19762341
xref: http://identifiers.org/pubmed/16260143
xref: http://identifiers.org/pubmed/18043707
xref: http://identifiers.org/pubmed/15863030
xref: http://identifiers.org/pubmed/19536106
xref: http://identifiers.org/pubmed/17604717
xref: http://identifiers.org/pubmed/17084981
xref: http://identifiers.org/pubmed/16939974
xref: http://identifiers.org/pubmed/11742412
xref: http://identifiers.org/pubmed/17496910
xref: http://identifiers.org/pubmed/19619488
xref: http://identifiers.org/pubmed/19458711
xref: http://identifiers.org/pubmed/15450248
comment: Signal transduction is a process in which extracellular signals elicit changes in cell state and activity. Transmembrane receptors sense changes in the cellular environment by binding ligands, such as hormones and growth factors, or reacting to other types of stimuli, such as light. Stimulation of transmembrane receptors leads to their conformational change which propagates the signal to the intracellular environment by activating downstream signaling cascades. Depending on the cellular context, this may impact cellular proliferation, differentiation, and survival. On the organism level, signal transduction regulates overall growth and behavior. Receptor tyrosine kinases (RTKs) transmit extracellular signals by phosphorylating their protein partners on conserved tyrosine residues. Some of the best studied RTKs are EGFR (reviewed in Avraham and Yarden, 2011), FGFR (reviewed in Eswarakumar et al, 2005), insulin receptor (reviewed in Saltiel and Kahn, 2001), NGF (reviewed in Reichardt, 2006), PDGF (reviewed in Andrae et al, 2008) and VEGF (reviewed in Xie et al, 2004). RTKs frequently activate downstream signaling through RAF/MAP kinases (reviewed in McKay and Morrison, 2007 and Wellbrock et al 2004), AKT (reviewed in Manning and Cantley, 2007) and PLC- gamma (reviewed in Patterson et al), which ultimately results in changes in gene expression and cellular metabolism. Receptor serine/threonine kinases of the TGF-beta family, such as TGF-beta receptors (reviewed in Kang et al. 2009) and BMP receptors (reviewed in Miyazono et al. 2009), transmit extracellular signals by phosphorylating regulatory SMAD proteins on conserved serine and threonine residues. This leads to formation of complexes of regulatory SMADs and SMAD4, which translocate to the nucleus where they act as transcription factors. WNT receptors transmit their signal through beta-catenin. In the absence of ligand, beta-catenin is constitutively degraded in a ubiquitin-dependent manner. WNT receptor stimulation…

Catalysis24
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction60
control type: ACTIVATION
xref: RelationshipXref43
xref: RelationshipXref44
controller: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)

Catalysis23
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction56
control type: ACTIVATION
xref: RelationshipXref26
xref: RelationshipXref42
controller: TFIIH (name copied from entity in Homo sapiens)

Catalysis22
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction49
control type: ACTIVATION
xref: RelationshipXref21
xref: RelationshipXref20
controller: Protein24

http://identifiers.org/pubmed/21102611
type: PublicationXref
id: 21102611
author: Gareau, Jaclyn R
author: Lima, Christopher D
db: Pubmed
title: The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition
source: Nat. Rev. Mol. Cell Biol. 11:861-71
year: 2010

Catalysis21
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction48
control type: ACTIVATION
xref: RelationshipXref37
xref: RelationshipXref36
controller: Transcription-coupled (TC) repair complex (name copied from entity in Homo sapiens)

Catalysis20
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction47
control type: ACTIVATION
xref: RelationshipXref37
xref: RelationshipXref36
controller: Transcription-coupled (TC) repair complex (name copied from entity in Homo sapiens)

UniProt:Q09900
type: ProteinReference
xref: UnificationXref1982
organism: BioSource1

http://identifiers.org/pubmed/19513348
type: PublicationXref
id: 19513348
author: Szczepanowska, J
db: Pubmed
title: Involvement of Rac/Cdc42/PAK pathway in cytoskeletal rearrangements
source: Acta Biochim Pol 56:225-34
year: 2009

Catalysis36
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction87
control type: ACTIVATION
xref: RelationshipXref62
xref: RelationshipXref63
controller: Activated conventional protein kinase C

Catalysis37
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction88
control type: ACTIVATION
xref: RelationshipXref62
xref: RelationshipXref63
controller: Activated conventional protein kinase C

Catalysis38
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction98
control type: ACTIVATION
xref: RelationshipXref69
xref: RelationshipXref68
controller: PhysicalEntity74

Catalysis39
type: Catalysis
data source: Provenance1
controlled: Activation of S6K1
control type: ACTIVATION
xref: RelationshipXref16
xref: RelationshipXref78
controller: Activated mTORC1 (name copied from entity in Homo sapiens)

UniProt:Q09907
type: ProteinReference
xref: UnificationXref44
organism: BioSource1

Evidence297
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19239894
xref: http://identifiers.org/pubmed/17245413
xref: http://identifiers.org/pubmed/15769464
xref: http://identifiers.org/pubmed/18441014
xref: http://identifiers.org/pubmed/11283721
xref: http://identifiers.org/pubmed/15273322
xref: http://identifiers.org/pubmed/16141059
xref: http://identifiers.org/pubmed/14749774
xref: http://identifiers.org/pubmed/15068804
xref: http://identifiers.org/pubmed/15475613
comment: The scavenging nuclease DCPS hydrolyzes the triphosphate bond between the 7-methylguanosine cap and the remaining oligoribonucleotide body of the mRNA. The products are 7-methylguanosine 5'-monophosphate and an oligoribonucleotide with a 5'-diphosphate.

Evidence296
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19239894
xref: http://identifiers.org/pubmed/19225159
xref: http://identifiers.org/pubmed/17545563
xref: http://identifiers.org/pubmed/17174896
xref: http://identifiers.org/pubmed/17245413
xref: http://identifiers.org/pubmed/19060886
xref: http://identifiers.org/pubmed/11283721
xref: http://identifiers.org/pubmed/16141059
xref: http://identifiers.org/pubmed/14749774
xref: http://identifiers.org/pubmed/15231747
xref: http://identifiers.org/pubmed/15475613
comment: The exosome complex hydrolyzes capped, deadenylated mRNA from 3' to 5' and yields ribonucleotides having 5'-monophosphates. In yeast the Ski2-Ski3-Ski8 complex assists degradation by the exosome complex, however little is known about the function of the homologous Ski complex in mammals. Although many exosomal components contain exonuclease signatures, only two components have been shown to degrade RNA. Rrp6/PMSCL-100 has been shown to be involved in the 3â-5â decay of nuclear mRNAs in yeast. Rrp6 may also function in the absence of the core exosomal components. The Rrp44/dDis3 component of the core exosome has been shown to possess both 3â-5â exonuclease activity along with endonuclease activity via its PIN domain.

Evidence299
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19239894
xref: http://identifiers.org/pubmed/16051491
xref: http://identifiers.org/pubmed/17245413
xref: http://identifiers.org/pubmed/15711010
xref: http://identifiers.org/pubmed/11283721
xref: http://identifiers.org/pubmed/19279404
xref: http://identifiers.org/pubmed/16141059
xref: http://identifiers.org/pubmed/14749774
xref: http://identifiers.org/pubmed/15231747
xref: http://identifiers.org/pubmed/15475613
comment: The Lsm1-7 complex forms a heptameric ring that binds the 3' oligoadenylated ends of mRNAs that have been deadenylated. The bound Lsm1-7 may prevent access of the exosome (a 3' to 5' exonuclease) to the 3' end and thereby direct the mRNA to the 5' to 3' exonuclease pathway. The yeast Lsm1-7 complex has a preference for oligoadenylated RNA compared to polyadenylated RNA, however other determinants of binding by Lsm1-7 are unknown.

Evidence298
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19239894
xref: http://identifiers.org/pubmed/17245413
xref: http://identifiers.org/pubmed/11283721
xref: http://identifiers.org/pubmed/16141059
xref: http://identifiers.org/pubmed/14749774
xref: http://identifiers.org/pubmed/15475613
comment: The degradation of mRNA from 3' to 5' occurs in two steps. First, the exosome exoribonuclease complex binds the 3' end of the oligoadenylated mRNA and hydrolyzes it from 3' to 5', yielding ribonucleotides having 5'-monophosphates, until a capped oligoribonucleotide remains. Second, the scavenging decapping enzyme DCPS hydrolyzes the 7-methylguanosine cap.

Catalysis33
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction80
control type: ACTIVATION
xref: RelationshipXref58
xref: RelationshipXref57
controller: phospho-p-Y172-VAV2

Catalysis32
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction73
control type: ACTIVATION
xref: RelationshipXref43
xref: RelationshipXref51
controller: RNA Polymerase I promoter escape complex (name copied from entity in Homo sapiens)

Catalysis35
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction85
control type: ACTIVATION
xref: RelationshipXref60
xref: RelationshipXref61
controller: Note: the coordinates are copied over from Homo sapiens.

Catalysis34
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction81
control type: ACTIVATION
xref: RelationshipXref57
xref: RelationshipXref59
controller: phospho-p-Y173-VAV3

Catalysis31
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction68
control type: ACTIVATION
xref: RelationshipXref48
xref: RelationshipXref47
controller: Protein70

Catalysis30
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction65
control type: ACTIVATION
xref: RelationshipXref46
xref: RelationshipXref16
controller: TFIIH (name copied from entity in Homo sapiens)

http://identifiers.org/pubmed/14556004
type: PublicationXref
id: 14556004
author: Sato, S
author: Takeda, K
author: Takeuchi, O
author: Hoshino, K
author: Kaisho, T
author: Uematsu, S
author: Hemmi, H
author: Yamamoto, M
db: Pubmed
title: TRAM is specifically involved in the Toll-like receptor 4-mediated
source: Nat Immunol 4:1144-50
year: 2003

UnificationXref1
type: UnificationXref
id: GO:0005654
db: GENE ONTOLOGY

http://identifiers.org/pubmed/15945070
type: PublicationXref
id: 15945070
author: Neupert, C
author: Clarke, JT
author: Frank, CG
author: Hennet, T
author: Weinstein, M
author: Poplawski, N
author: Schollen, E
author: Seargeant, L
author: Aebi, M
author: Matthijs, G
author: Griffiths, A
author: Grubenmann, CE
db: Pubmed
title: CDG-IL: an infant with a novel mutation in the ALG9 gene and additional phenotypic features
source: Am J Med Genet A 136:194-7
year: 2005

UnificationXref2
type: UnificationXref
id: 4896
db: NCBI Taxonomy

UnificationXref3
type: UnificationXref
id: Q10159
db: UniProt

UnificationXref4
type: UnificationXref
id: 3660269
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660269

UnificationXref5
type: UnificationXref
id: 110198
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110198

UnificationXref6
type: UnificationXref
id: REACT_4167
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4167.1

UnificationXref7
type: UnificationXref
id: 3660270
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660270

http://identifiers.org/pubmed/11111075
type: PublicationXref
id: 11111075
author: Houten, SM
author: Waterham, HR
db: Pubmed
title: Biochemical and genetic aspects of mevalonate kinase and its deficiency
source: Biochim Biophys Acta 1529:19-32
year: 2000

Catalysis85
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction175
control type: ACTIVATION
xref: RelationshipXref179
xref: RelationshipXref180
controller: Note: the coordinates are copied over from Homo sapiens.

UnificationXref4697
type: UnificationXref
id: 3661796
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661796

FAD [ChEBI:16238]
type: SmallMoleculeReference
name: FAD
name: Flavin adenine dinucleotide
xref: UnificationXref2841

Catalysis86
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction176
control type: ACTIVATION
xref: RelationshipXref182
xref: RelationshipXref181
controller: GALE dimer (name copied from entity in Homo sapiens)

UnificationXref4698
type: UnificationXref
id: REACT_88962
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_88962.9

guanine
type: SmallMoleculeReference
name: guanine [ChEBI:16235]
name: 2-amino-6-hydroxypurine
xref: UnificationXref4208

Catalysis83
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction173
control type: ACTIVATION
xref: RelationshipXref174
xref: RelationshipXref175
controller: 8xUGP2 (name copied from entity in Homo sapiens)

UnificationXref4699
type: UnificationXref
id: 200679
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=200679

Catalysis84
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction174
control type: ACTIVATION
xref: RelationshipXref172
xref: RelationshipXref173
controller: phosphoglucomutase

Catalysis89
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction179
control type: ACTIVATION
xref: RelationshipXref189
xref: RelationshipXref188
controller: PGD dimer (name copied from entity in Homo sapiens)

Catalysis87
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction177
control type: ACTIVATION
xref: RelationshipXref185
xref: RelationshipXref184
controller: G6PD dimer and tetramer

Catalysis88
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction178
control type: ACTIVATION
xref: RelationshipXref186
xref: RelationshipXref187
controller: Note: the coordinates are copied over from Homo sapiens.

UnificationXref9
type: UnificationXref
id: REACT_94584
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_94584.9

UnificationXref8
type: UnificationXref
id: 3660271
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3660271

UnificationXref4690
type: UnificationXref
id: REACT_85380
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_85380.9

UnificationXref4691
type: UnificationXref
id: 200671
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=200671

UnificationXref4692
type: UnificationXref
id: REACT_11639
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11639.2

Catalysis81
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction171
control type: ACTIVATION
xref: RelationshipXref145
xref: RelationshipXref146
controller: glucose 6-phosphate isomerase dimer (name copied from entity in Homo sapiens)

UnificationXref4693
type: UnificationXref
id: O13660
db: UniProt

Catalysis82
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction172
control type: ACTIVATION
xref: RelationshipXref172
xref: RelationshipXref173
controller: phosphoglucomutase

UnificationXref4694
type: UnificationXref
id: 3661786
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661786

UnificationXref4695
type: UnificationXref
id: 3661788
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661788

Catalysis80
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction170
control type: ACTIVATION
xref: RelationshipXref169
xref: RelationshipXref170
controller: fructose-1,6-bisphosphatase isoforms

UnificationXref4696
type: UnificationXref
id: REACT_89284
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_89284.9

Cross-presentation of soluble exogenous antigens (endosomes)
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction603
evidence: Evidence1031
xref: RelationshipXref870
xref: UnificationXref6652
xref: UnificationXref6653
pathway order: PathwayStep1012
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Catalysis94
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction184
control type: ACTIVATION
xref: RelationshipXref194
xref: RelationshipXref195
controller: Note: the coordinates are copied over from Homo sapiens.

Catalysis95
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction185
control type: ACTIVATION
xref: RelationshipXref194
xref: RelationshipXref195
controller: Note: the coordinates are copied over from Homo sapiens.

Catalysis96
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction186
control type: ACTIVATION
xref: RelationshipXref198
xref: RelationshipXref197
controller: phosphoribosyl pyrophosphate synthetase 1 holoenzyme (name copied from entity in Homo sapiens)

Catalysis97
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction187
control type: ACTIVATION
xref: RelationshipXref199
xref: RelationshipXref197
controller: phosphoribosyl pyrophosphate synthetase holoenzyme

Catalysis98
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction188
control type: ACTIVATION
xref: RelationshipXref203
xref: RelationshipXref202
controller: Homologues of SYNJ1

Catalysis99
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction189
control type: ACTIVATION
xref: RelationshipXref205
xref: RelationshipXref206
controller: IP6K1/2

Catalysis90
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction180
control type: ACTIVATION
xref: RelationshipXref190
xref: RelationshipXref191
controller: RPE dimer (name copied from entity in Homo sapiens)

Catalysis91
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction181
control type: ACTIVATION
xref: RelationshipXref190
xref: RelationshipXref191
controller: RPE dimer (name copied from entity in Homo sapiens)

Catalysis92
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction182
control type: ACTIVATION
xref: RelationshipXref193
xref: RelationshipXref192
controller: Note: the coordinates are copied over from Homo sapiens.

Catalysis93
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction183
control type: ACTIVATION
xref: RelationshipXref193
xref: RelationshipXref192
controller: Note: the coordinates are copied over from Homo sapiens.

http://identifiers.org/pubmed/10567352
type: PublicationXref
id: 10567352
author: Painter, GF
author: Cooke, FT
author: Holmes, AB
author: McEwen, RK
author: Ohya, Y
author: Shisheva, A
author: Michell, RH
author: Parker, PJ
author: Dove, SK
db: Pubmed
title: Complementation analysis in PtdInsP kinase-deficient yeast mutants demonstrates that Schizosaccharomyces pombe and murine Fab1p homologues are phosphatidylinositol 3-phosphate 5-kinases
source: J Biol Chem 274:33905-12
year: 1999

Catalysis69
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction159
control type: ACTIVATION
xref: RelationshipXref155
xref: RelationshipXref156
controller: enolase 1 dimer, (alpha) (name copied from entity in Homo sapiens)

Catalysis67
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction157
control type: ACTIVATION
xref: RelationshipXref151
xref: RelationshipXref152
controller: glyceraldehyde-3-phosphate dehydrogenase tetramer

Catalysis68
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction158
control type: ACTIVATION
xref: RelationshipXref153
xref: RelationshipXref154
controller: phosphoglycerate kinase 1 complex (name copied from entity in Homo sapiens)

Catalysis65
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction155
control type: ACTIVATION
xref: RelationshipXref148
xref: RelationshipXref147
controller: phosphofructokinase tetramer

Catalysis66
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction156
control type: ACTIVATION
xref: RelationshipXref149
xref: RelationshipXref150
controller: triosephosphate isomerase dimer (name copied from entity in Homo sapiens)

http://identifiers.org/pubmed/3053703
type: PublicationXref
id: 3053703
author: Meister, A
db: Pubmed
title: Glutathione metabolism and its selective modification
source: J Biol Chem 263:17205-8
year: 1988

Catalysis63
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction152
control type: ACTIVATION
xref: RelationshipXref140
xref: RelationshipXref141
controller: PhysicalEntity124

Catalysis64
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction154
control type: ACTIVATION
xref: RelationshipXref145
xref: RelationshipXref146
controller: glucose 6-phosphate isomerase dimer (name copied from entity in Homo sapiens)

http://identifiers.org/pubmed/3053705
type: PublicationXref
id: 3053705
author: Sample, C
author: Bell, GI
author: Sanke, T
author: Rubenstein, AH
author: Steiner, DF
db: Pubmed
title: An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing
source: J Biol Chem 263:17243-6
year: 1988

Catalysis61
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction150
control type: ACTIVATION
xref: RelationshipXref122
xref: RelationshipXref123
controller: 26S proteasome (name copied from entity in Homo sapiens)

dolichyl phosphate [ChEBI:16214]
type: SmallMoleculeReference
name: Dolichyl monophosphate
name: dolichyl phosphate
name: Dolichol phosphate
name: dolichol monophosphate
xref: UnificationXref8055

Catalysis62
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction151
control type: ACTIVATION
xref: RelationshipXref137
xref: RelationshipXref138
controller: Note: the coordinates are copied over from Homo sapiens.

Kinesin-5 homotetramer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry362
component: P24339
xref: UnificationXref921
cellular location: GO:0005829
comment: Reactome DB_ID: 3663676

Catalysis60
type: Catalysis
data source: Provenance1
controlled: Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197
control type: ACTIVATION
xref: RelationshipXref132
xref: RelationshipXref16
controller: Homologues of PAK2(1-524)

Rabenosyn-5:VPS-45 (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry358
component stoichiometry: Stoichiometry359
component stoichiometry: Stoichiometry360
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref916
cellular location: GO:0010008
comment: Reactome DB_ID: 3663713

CENP-E dimer (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry368
component: Q1MTQ1
xref: UnificationXref934
cellular location: GO:0005829
comment: Reactome DB_ID: 3663686

Centralspindlin (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry365
component stoichiometry: Stoichiometry366
component: Kinesin-6
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref929
cellular location: GO:0005829
comment: Reactome DB_ID: 3663680

Activated PKC beta (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry349
component stoichiometry: Stoichiometry348
component stoichiometry: Stoichiometry350
component stoichiometry: Stoichiometry351
component: SmallMolecule29
component: Homologues of PRKCB
component: SmallMolecule27
component: SmallMolecule21
xref: UnificationXref850
cellular location: GO:0005886
comment: Reactome DB_ID: 3660508

F-actin capping protein (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry356
component stoichiometry: Stoichiometry357
component: Note: the coordinates are copied over from Homo sapiens.
xref: UnificationXref906
cellular location: GO:0005829
comment: Reactome DB_ID: 3663366

Activated PKC gamma (name copied from entity in Homo sapiens)
type: Complex
data source: Provenance1
component stoichiometry: Stoichiometry353
component stoichiometry: Stoichiometry355
component stoichiometry: Stoichiometry354
component stoichiometry: Stoichiometry352
component: SmallMolecule29
component: SmallMolecule27
component: Homologues of PRKCG
component: SmallMolecule21
xref: UnificationXref851
cellular location: GO:0005886
comment: Reactome DB_ID: 3660509

http://identifiers.org/pubmed/12034743
type: PublicationXref
id: 12034743
author: Lees-Miller, S
author: Beamish, H
author: Chen, P
author: Lavin, MF
author: Purdie, D
author: Kondo, N
author: Kaneko, H
author: Gueven, N
author: Kedar, P
author: Peng, C
author: Fukao, T
author: Beresten, S
author: Ellis, N
db: Pubmed
title: Functional link between BLM defective in Bloom's syndrome and the ataxia-telangiectasia-mutated protein, ATM.
source: J Biol Chem 277:30515-23
year: 2002

Catalysis76
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction166
control type: ACTIVATION
xref: RelationshipXref155
xref: RelationshipXref156
controller: enolase 1 dimer, (alpha) (name copied from entity in Homo sapiens)

Catalysis77
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction167
control type: ACTIVATION
xref: RelationshipXref153
xref: RelationshipXref154
controller: phosphoglycerate kinase 1 complex (name copied from entity in Homo sapiens)

Catalysis78
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction168
control type: ACTIVATION
xref: RelationshipXref151
xref: RelationshipXref152
controller: glyceraldehyde-3-phosphate dehydrogenase tetramer

Catalysis79
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction169
control type: ACTIVATION
xref: RelationshipXref149
xref: RelationshipXref150
controller: triosephosphate isomerase dimer (name copied from entity in Homo sapiens)

Catalysis72
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction162
control type: ACTIVATION
xref: RelationshipXref163
xref: RelationshipXref162
controller: malate dehydrogenase 2 dimer (name copied from entity in Homo sapiens)

Catalysis73
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction163
control type: ACTIVATION
xref: RelationshipXref164
xref: RelationshipXref165
controller: GOT2 dimer (name copied from entity in Homo sapiens)

Catalysis74
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction164
control type: ACTIVATION
xref: RelationshipXref164
xref: RelationshipXref166
controller: GOT1 dimer (name copied from entity in Homo sapiens)

Catalysis75
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction165
control type: ACTIVATION
xref: RelationshipXref168
xref: RelationshipXref167
controller: Note: the coordinates are copied over from Homo sapiens.

http://identifiers.org/pubmed/18195019
type: PublicationXref
id: 18195019
author: Bonacci, TM
author: Li, S
author: Kowala, M
author: Konrad, RJ
author: Moller, DE
author: Bredt, DS
author: Cao, G
author: Zhao, Y
author: Bensch, WR
author: Chen, YQ
db: Pubmed
title: Identification and characterization of a major liver lysophosphatidylcholine acyltransferase
source: J Biol Chem 283:8258-65
year: 2008

Catalysis70
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction160
control type: ACTIVATION
xref: RelationshipXref157
xref: RelationshipXref158
controller: pyruvate kinase tetramer

Catalysis71
type: Catalysis
data source: Provenance1
controlled: BiochemicalReaction161
control type: ACTIVATION
xref: RelationshipXref160
xref: RelationshipXref161
controller: pyruvate carboxylase holoenzyme (name copied from entity in Homo sapiens)

http://identifiers.org/pubmed/8969170
type: PublicationXref
id: 8969170
author: Gorski, JL
author: Xu, Y
author: Santos, MF
author: Fischer, DJ
author: Pasteris, NG
author: Tigyi, G
author: Zheng, Y
db: Pubmed
title: The faciogenital dysplasia gene product FGD1 functions as a Cdc42Hs-specific guanine-nucleotide exchange factor
source: J Biol Chem 271:33169-72
year: 1996

Stoichiometry246
type: Stoichiometry
physical entity: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry245
type: Stoichiometry
physical entity: TFIIH (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry244
type: Stoichiometry
physical entity: SmallMolecule14
stoichiometric coefficient: 2.0

Stoichiometry243
type: Stoichiometry
physical entity: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry242
type: Stoichiometry
physical entity: TFIIH (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry241
type: Stoichiometry
physical entity: PhysicalEntity49
stoichiometric coefficient: 1.0

Stoichiometry240
type: Stoichiometry
physical entity: SmallMolecule10
stoichiometric coefficient: 2.0

UnificationXref6543
type: UnificationXref
id: 3663558
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663558

UnificationXref6544
type: UnificationXref
id: 3663559
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663559

UnificationXref6541
type: UnificationXref
id: O36028
db: UniProt

UnificationXref6542
type: UnificationXref
id: 3663557
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663557

Stoichiometry249
type: Stoichiometry
physical entity: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

UnificationXref6540
type: UnificationXref
id: 3663553
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663553

Stoichiometry247
type: Stoichiometry
physical entity: PhysicalEntity50
stoichiometric coefficient: 1.0

Stoichiometry248
type: Stoichiometry
physical entity: TFIIH (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

UnificationXref6549
type: UnificationXref
id: REACT_145040
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_145040.5

UnificationXref6547
type: UnificationXref
id: 3663562
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663562

UnificationXref6548
type: UnificationXref
id: 3663564
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663564

UnificationXref6545
type: UnificationXref
id: 3663560
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663560

UnificationXref6546
type: UnificationXref
id: 3663561
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663561

http://identifiers.org/pubmed/16906134
type: PublicationXref
id: 16906134
author: Lee, JW
author: Ackerman, SL
author: Beebe, K
author: Longo-Guess, CM
author: Davisson, MT
author: Jang, J
author: Schimmel, P
author: Cook, SA
author: Nangle, LA
author: Sundberg, JP
db: Pubmed
title: Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration
source: Nature 443:50-5
year: 2006

Stoichiometry233
type: Stoichiometry
physical entity: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry232
type: Stoichiometry
physical entity: TFIIH (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry235
type: Stoichiometry
physical entity: TFIIA (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry234
type: Stoichiometry
physical entity: TFIID (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry231
type: Stoichiometry
physical entity: PhysicalEntity47
stoichiometric coefficient: 1.0

Stoichiometry230
type: Stoichiometry
physical entity: TFIIE (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

UnificationXref6530
type: UnificationXref
id: GO:0009898
db: GENE ONTOLOGY

UnificationXref6531
type: UnificationXref
id: 939760
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=939760

UnificationXref6532
type: UnificationXref
id: REACT_26149
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_26149.2

UnificationXref6533
type: UnificationXref
id: 947592
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=947592

Stoichiometry236
type: Stoichiometry
physical entity: PhysicalEntity48
stoichiometric coefficient: 1.0

Stoichiometry237
type: Stoichiometry
physical entity: TFIIE (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry238
type: Stoichiometry
physical entity: TFIIH (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry239
type: Stoichiometry
physical entity: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

UnificationXref6538
type: UnificationXref
id: 3663549
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663549

UnificationXref6539
type: UnificationXref
id: Q09891
db: UniProt

UnificationXref6534
type: UnificationXref
id: REACT_25925
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_25925.2

UnificationXref6535
type: UnificationXref
id: 947588
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=947588

UnificationXref6536
type: UnificationXref
id: REACT_26709
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_26709.2

UnificationXref6537
type: UnificationXref
id: O94296
db: UniProt

Stoichiometry260
type: Stoichiometry
physical entity: Protein55
stoichiometric coefficient: 1.0

http://identifiers.org/pubmed/3053686
type: PublicationXref
id: 3053686
author: Rozen, R
author: MacKenzie, RE
author: Bell, AW
author: Hum, DW
db: Pubmed
title: Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase.
source: J Biol Chem 263:15946-50
year: 1988

Stoichiometry264
type: Stoichiometry
physical entity: TFIIF (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry263
type: Stoichiometry
physical entity: RNA Polymerase II holoenzyme complex (phosphorylated) (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry262
type: Stoichiometry
physical entity: Protein58
stoichiometric coefficient: 1.0

Stoichiometry261
type: Stoichiometry
physical entity: Protein57
stoichiometric coefficient: 1.0

Stoichiometry268
type: Stoichiometry
physical entity: PhysicalEntity52
stoichiometric coefficient: 1.0

Stoichiometry267
type: Stoichiometry
physical entity: PhysicalEntity51
stoichiometric coefficient: 1.0

Stoichiometry266
type: Stoichiometry
physical entity: TFIIH (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry265
type: Stoichiometry
physical entity: RNA polymerase II (phosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

http://identifiers.org/pubmed/19336658
type: PublicationXref
id: 19336658
author: Reue, K
author: Takeuchi, K
db: Pubmed
title: Biochemistry, physiology, and genetics of GPAT, AGPAT, and lipin enzymes in triglyceride synthesis
source: Am J Physiol Endocrinol Metab 296:E1195-209
year: 2009

Stoichiometry269
type: Stoichiometry
physical entity: RNA polymerase II (phosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

http://identifiers.org/pubmed/21310273
type: PublicationXref
id: 21310273
author: Müller, JS
author: Straub, V
author: Schoser, B
author: Abicht, A
author: Hübner, A
author: Krause, S
author: Rodolico, C
author: Mallebrera, CJ
author: Strom, TM
author: Vilchez, JJ
author: Nascimento, A
author: Herrmann, R
author: Colomer, J
author: Bozorgmehr, B
author: Lochmüller, H
author: von der Hagen, M
author: Oldfors, A
author: Guergueltcheva, V
author: Urtizberea, A
author: Voit, T
author: Sieb, JP
author: Nafissi, S
author: Najmabadi, H
author: Palace, J
author: Maxwell, S
author: Diepolder, I
author: Schlotter, B
author: Muelas, N
author: Kariminejad, A
author: Dusl, M
author: Beeson, D
author: Nilipour, Y
author: Lindbergh, C
author: Steinlein, OK
author: Bushby, K
author: Senderek, J
author: Laval, SH
author: Kirschner, J
author: Cossins, J
db: Pubmed
title: Hexosamine biosynthetic pathway mutations cause neuromuscular transmission defect
source: Am J Hum Genet 88:162-72
year: 2011

http://identifiers.org/pubmed/16125054
type: PublicationXref
id: 16125054
author: Moens, U
author: Johannessen, M
author: Delghandi, MP
db: Pubmed
title: The cAMP signalling pathway activates CREB through PKA, p38 and MSK1 in NIH 3T3 cells
source: Cell Signal 17:1343-51
year: 2005

UnificationXref6521
type: UnificationXref
id: 3663545
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663545

UnificationXref6522
type: UnificationXref
id: REACT_129491
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_129491.5

UnificationXref6520
type: UnificationXref
id: 3663543
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663543

UnificationXref6525
type: UnificationXref
id: REACT_25558
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_25558.2

UnificationXref6526
type: UnificationXref
id: 939747
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=939747

UnificationXref6523
type: UnificationXref
id: GO:0009897
db: GENE ONTOLOGY

UnificationXref6524
type: UnificationXref
id: 947595
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=947595

UnificationXref6529
type: UnificationXref
id: REACT_26259
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_26259.2

UnificationXref6527
type: UnificationXref
id: REACT_26138
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_26138.2

UnificationXref6528
type: UnificationXref
id: 947594
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=947594

http://identifiers.org/pubmed/12890864
type: PublicationXref
id: 12890864
author: Mochizuki, Y
author: Majerus, PW
db: Pubmed
title: Characterization of myotubularin-related protein 7 and its binding partner, myotubularin-related protein 9
source: Proc Natl Acad Sci U S A 100:9768-73
year: 2003

Stoichiometry251
type: Stoichiometry
physical entity: Protein47
stoichiometric coefficient: 1.0

Stoichiometry250
type: Stoichiometry
physical entity: PhysicalEntity51
stoichiometric coefficient: 1.0

Stoichiometry253
type: Stoichiometry
physical entity: Protein49
stoichiometric coefficient: 1.0

Stoichiometry252
type: Stoichiometry
physical entity: Protein48
stoichiometric coefficient: 1.0

Stoichiometry255
type: Stoichiometry
physical entity: Protein52
stoichiometric coefficient: 1.0

Stoichiometry254
type: Stoichiometry
physical entity: Protein50
stoichiometric coefficient: 1.0

Stoichiometry257
type: Stoichiometry
physical entity: Protein69
stoichiometric coefficient: 1.0

Stoichiometry256
type: Stoichiometry
physical entity: Protein53
stoichiometric coefficient: 1.0

Stoichiometry258
type: Stoichiometry
physical entity: Protein54
stoichiometric coefficient: 1.0

UnificationXref4299
type: UnificationXref
id: REACT_4914
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4914.1

Stoichiometry259
type: Stoichiometry
physical entity: Protein56
stoichiometric coefficient: 1.0

UnificationXref4297
type: UnificationXref
id: CHEBI:17025
db: ChEBI

UnificationXref4298
type: UnificationXref
id: 76630
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=76630

UnificationXref4295
type: UnificationXref
id: 3659317
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3659317

UnificationXref4296
type: UnificationXref
id: REACT_85283
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_85283.9

UnificationXref4293
type: UnificationXref
id: 111628
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111628

UnificationXref6510
type: UnificationXref
id: 3665525
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665525

UnificationXref4294
type: UnificationXref
id: REACT_3042
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3042.1

UnificationXref6511
type: UnificationXref
id: REACT_131473
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_131473.5

http://identifiers.org/pubmed/10409700
type: PublicationXref
id: 10409700
author: Ma, W
author: Kaiser, MW
author: Miller, C
author: Fors, L
author: Lyamicheva, N
author: Lyamichev, VI
author: Neri, B
db: Pubmed
title: A comparison of eubacterial and archaeal structure-specific 5'-exonucleases.
source: J Biol Chem 274:21387-94
year: 1999

UnificationXref6512
type: UnificationXref
id: 3665526
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665526

http://identifiers.org/pubmed/19720617
type: PublicationXref
id: 19720617
author: Deponte, M
author: Hell, K
db: Pubmed
title: Disulphide bond formation in the intermembrane space of mitochondria
source: J Biochem 146:599-608
year: 2009

UnificationXref6513
type: UnificationXref
id: REACT_126859
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_126859.5

UnificationXref6514
type: UnificationXref
id: 167012
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=167012

UnificationXref6515
type: UnificationXref
id: REACT_10868
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10868.2

UnificationXref6516
type: UnificationXref
id: O59868
db: UniProt

UnificationXref6517
type: UnificationXref
id: 3663540
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663540

UnificationXref6518
type: UnificationXref
id: 3663541
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663541

UnificationXref6519
type: UnificationXref
id: 3663542
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663542

Stoichiometry201
type: Stoichiometry
physical entity: pol II promoter:TFIID:TFIIA:TFIIB:Pol II:TFIIF complex (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

UnificationXref6590
type: UnificationXref
id: 3662482
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662482

Stoichiometry202
type: Stoichiometry
physical entity: TFIIE (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

UnificationXref6591
type: UnificationXref
id: 3662483
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662483

Stoichiometry200
type: Stoichiometry
physical entity: TFIIH (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

PKA activation
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction99
evidence: Evidence170
xref: UnificationXref983
xref: UnificationXref984
xref: RelationshipXref70
pathway order: PathwayStep167
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/9006323
type: PublicationXref
id: 9006323
author: Engström, U
author: Eriksson, L
author: Westermark, P
author: Eneström, S
author: Sletten, K
db: Pubmed
title: Prolactin-derived amyloid in the aging pituitary gland
source: Am J Pathol 150:67-73
year: 1997

UnificationXref6589
type: UnificationXref
id: REACT_149821
db: Reactome
id version: 4
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_149821.4

Evidence699
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/22123817
xref: http://identifiers.org/pubmed/20153287
xref: http://identifiers.org/pubmed/9630604
comment: Once biotinylated, three halocarboxylases (hCBXs) are localised to the mitochondrial matrix. The mechanism of transfer is still unclear. Pyruvate carboxylase (PC) is required for gluconeogenesis, lipogenesis, neurotransmitter synthesis and insulin secretion; Methylcrotonyl-CoA carboxylase (MCC) is required for amino acid metabolism; propionyl-CoA carboxylase (PCC) is required for odd-chain fatty acid oxidation (Ingaramo & Beckett 2012, Hiratsuka et al. 1998, Bailey et al. 2010).

UnificationXref6588
type: UnificationXref
id: 3665605
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665605

Stoichiometry209
type: Stoichiometry
physical entity: TFIIH (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Evidence698
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/22123817
xref: http://identifiers.org/pubmed/16134170
xref: http://identifiers.org/pubmed/20153287
xref: http://identifiers.org/pubmed/9630604
xref: http://identifiers.org/pubmed/18297087
comment: Biotin (Btn) acts as a coenzyme to 4 carboxylases which exist in their inactive apo forms. In the cytosol, these apo carboxylases are biotinylated to their active halo forms by the activity of biotin-protein ligase (HCLS) (Ingaramo & Beckett 2012, Hiratsuka et al. 1998, Bailey et al. 2010). Defects in HLCS causes holocarboxylase synthetase deficiency (HLCS deficiency aka biotin-responsive multiple carboxylase deficiency; MIM:253270). HLCS deficiency is an autosomal recessive disorder whereby deficient HLCS activity results in reduced activity of multiple carboxylases. Symptoms include metabolic acidosis, organic aciduria, lethargy, hypotonia, convulsions and dermatitis (Suzuki et al. 2005). Pyruvate carboxylase (PC) is homotetrameric, binds 1 Mn2+ and 1 Btn per PC subunit (Xiang & Tong 2008). The exact order in which this complex is constructed is unknown.

UnificationXref6587
type: UnificationXref
id: REACT_106901
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_106901.9

Stoichiometry208
type: Stoichiometry
physical entity: TFIIE (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Evidence697
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19832808
xref: http://identifiers.org/pubmed/21312325
xref: http://identifiers.org/pubmed/20185591
xref: http://identifiers.org/pubmed/10448521
comment: Vitamin B12 (cobalamin, Cbl) is a water-soluble vitamin with a key role in blood formation and normal functioning of the brain and nervous system. Cbl consists of a planar corrin ring coordinating with a cobalt atom through four nitrogen atoms. A 5,6-dimethylbenzamidizole base coordinates with the cobalt atom in the lower axial position while a number of different species can coordinate with the cobalt atom in the upper axial position. It is the cobalt-corrin ring complex that gives all Cbls a deep red colour. Only bacteria and archaea are able to synthesize Cbl thus humans need a dietary intake to prevent deficiency (Green 2010, Quadros 2010, Watkins & Rosenblatt 2011). A common semi-synthetic form of the vitamin, cyanocobalamin (CNCbl, where a cyanide group is in the upper axial position), is produced from bacterial hydroxocobalamin and used in many pharmaceuticals, supplements and as a food additive. In mammalian cells, Cbl or CNCbl is converted to two active coenzyme derivatives; methylcobalamin (MetCbl) and adenosylcobalamin (AdoCbl). MetCbl is required for activity of the cytoplasmic enzyme methionine synthase, which converts homocysteine to methionine. AdoCbl is required for activity of the mitochondrial enzyme methylmalonyl CoA mutase, which converts L-methylmalonyl-CoA to succinyl-CoA (Seetharam 1999). This pathway outlines the intake, transport and metabolism of Cbl and is assumed to be equally applicable to CNCbl.

UnificationXref6586
type: UnificationXref
id: 3665401
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665401

Stoichiometry207
type: Stoichiometry
physical entity: PhysicalEntity44
stoichiometric coefficient: 1.0

Evidence696
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/21511966
comment: Multidrug resistance-associated protein 1 (ABCC1, MRP1) can specifically mediate the ATP-dependant export of free cobalamin (Cbl aka vitamin B12) from small intestine cells to the portal vein (Shah et al. 2011).

UnificationXref6585
type: UnificationXref
id: REACT_95520
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_95520.9

Stoichiometry206
type: Stoichiometry
physical entity: Protein84
stoichiometric coefficient: 1.0

Evidence695
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10024608
comment: Animals cannot synthesize pyridoxal 5'-phosphate (PLP) which is a ligand in aminotransferases and other enzymes. PLP's accessible derivatives pyridoxine, pyridoxal, and pyridoxamine are traditionally called vitamins B6. They are taken up nutritionally from bacteria and plants, but also created from PLP in the body. The pathways used to recycle PLP from these three compounds can therefore be called vitamin B6 activation as well as PLP salvage. Because of the close similarity of the molecules, only two enzymes are needed for the task (McCormick & Chen, 1999).

UnificationXref6584
type: UnificationXref
id: 3665400
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665400

Stoichiometry205
type: Stoichiometry
physical entity: TFIIA (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Evidence694
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15182361
comment: Pyridoxine-5'-phosphate oxidase (PNPO) is able to oxidize pyridoxine phosphate (PDXP) to pyridoxal 5'-phosphate (PXLP) (Kang et al. 2004).

UnificationXref6583
type: UnificationXref
id: REACT_113600
db: Reactome
id version: 8
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_113600.8

Stoichiometry204
type: Stoichiometry
physical entity: TFIID (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Evidence693
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15182361
comment: Pyridoxine-5'-phosphate oxidase (PNPO) is able to oxidize pyridoxamine phosphate (PXAP) to pyridoxal 5'-phosphate (PXLP) (Kang et al. 2004).

UnificationXref6582
type: UnificationXref
id: 3661845
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661845

Stoichiometry203
type: Stoichiometry
physical entity: SmallMolecule10
stoichiometric coefficient: 2.0

Evidence692
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10987144
xref: http://identifiers.org/pubmed/15249053
comment: Pyridoxal kinase (PDXK) catalyzes the ATP-dependent phosphorylation of pyridoxine (PDX) to form pyridoxine phosphate (PDXP) (Lee et al. 2000, di Salvo et al. 2004).

UnificationXref6581
type: UnificationXref
id: 3661843
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661843

Evidence690
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10987144
xref: http://identifiers.org/pubmed/15249053
comment: Pyridoxal kinase (PDXK) catalyzes the ATP-dependent phosphorylation of pyridoxal (PXL) to form pyridoxal 5'-phosphate (PXLP) (Lee et al. 2000, di Salvo et al. 2004).

Evidence691
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10987144
xref: http://identifiers.org/pubmed/15249053
comment: Pyridoxal kinase (PDXK) catalyzes the ATP-dependent phosphorylation of pyridoxamine (PXA) to form pyridoxamine phosphate (PXAP) (Lee et al. 2000, di Salvo et al. 2004).

UnificationXref6580
type: UnificationXref
id: 3661842
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661842

UnificationXref6579
type: UnificationXref
id: 3661841
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661841

Evidence689
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/2981478
xref: http://identifiers.org/pubmed/12815048
comment: Panthothenate (vitamin B5) is the precursor of coenzyme A (Robishaw and Neely 1985) and is the prosthetic group of acyl carrier protein (ACP) (Joshi et al. 2003). Its name is derived from the Greek pantothen meaning "from everywhere" and small quantities of pantothenic acid are found in nearly every foodstuff.

UnificationXref6578
type: UnificationXref
id: 3661837
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661837

Evidence686
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12906824
xref: http://identifiers.org/pubmed/11923312
comment: The conjugation of cysteine (Cys) and 4'- phosphopantothenate (PPanK) to form 4-phosphopantothenoylcysteine (PPC) , coupled to the conversion of ATP to AMP and pyrophosphate, is catalyzed by cytosolic phosphopantothenate-cysteine ligase (PPCS aka Phosphopantothenoylcysteine synthase or PPC synthase). Mammalian PPCS prefers ATP to CTP, unlike the E. coli ortholog (Daughtery et al. 2002; Manoj et al. 2003).

UnificationXref6575
type: UnificationXref
id: 3661831
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661831

http://identifiers.org/pubmed/7649538
type: PublicationXref
id: 7649538
author: Sansaricq, C
author: Jakobs, C
author: Qureshi, IA
author: Snyderman, SE
author: Matsuda, I
author: Lambert, M
author: Smit, LM
author: Shapira, SK
author: Uchino, T
db: Pubmed
title: Molecular basis of phenotypic variation in patients with argininemia
source: Hum Genet 96:255-60
year: 1995

Evidence685
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/4915004
comment: Riboflavin (vitamin B2, E101) is an essential component for the cofactors FAD (flavin-adenine dinucleotide) and FMN (flavin mononucleotide). Together with NAD+ and NADP+, FAD and FMN are important hydrogen carriers and take part in more than 100 redox reactions involved in energy metabolism. Riboflavin is present in many vegetables and meat and during digestion, various flavoproteins from food are degraded and riboflavin is resorbed. The major degradation and excretion product in humans is riboflavin (Rivlin 1970).

UnificationXref6574
type: UnificationXref
id: 3661829
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661829

Evidence688
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/13032008
xref: http://identifiers.org/pubmed/11158296
xref: http://identifiers.org/pubmed/11923312
xref: http://identifiers.org/pubmed/2981478
xref: http://identifiers.org/pubmed/15893380
comment: Coenzyme A (CoA) is a ubiquitous cofactor that functions as an acyl group carrier in diverse processes including fatty acid metabolism and the TCA cycle (Lipmann 1953). It is synthesized from the vitamin pantothenate in a sequence of five reactions (Daugherty et al. 2002; Leonardi et al. 2005; Robishaw and Neely 1985). These reactions all occur in the cytosol or the mitochondrial intermembrane space (Leonardi et al. 2005). A recently described transport protein appears to mediate the uptake of Coenzyme A into the mitochondrial matrix (Prohl et al. 2001).

UnificationXref6577
type: UnificationXref
id: 3661833
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661833

Evidence687
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17242360
xref: http://identifiers.org/pubmed/11158296
comment: Graves disease carrier protein (SLC25A16), associated with the inner mitochondrial membrane, mediates the transport of cytosolic coenzyme A (CoA-SH) into the mitochondrial matrix. Evidence for this event is indirect. The protein has the sequence motifs expected for a transport protein, and yeast cells deficient in its homologue, Leu5p, fail to accumulate mitochondrial CoA-SH and can be rescued by expression of SLC25A16. At the same time, neither the yeast nor the human protein has been shown directly to function as a transporter (Prohl et al. 2001, Leonardi et al. 2007).

UnificationXref6576
type: UnificationXref
id: 3661832
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661832

Evidence682
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/12623014
comment: Phosphorylation of riboflavin (RIB) results in the formation of the first cofactor, flavin mononucleotide (FMN). This reaction is catalyzed by riboflavin kinase (RFK), a cytosolic enzyme existing as a monomer. It utilizes either zinc or magnesium ions in the reaction.

UnificationXref6571
type: UnificationXref
id: 3661849
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661849

Evidence681
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17222174
comment: Vitamin C (ascorbate) is an antioxidant and a cofactor in reactions catalyzed by Cu+-dependent monooxygenases and Fe++-dependent dioxygenases. Many mammals can synthesize ascorbate de novo; humans and other primates cannot due to an evolutionarily recent mutation in the gene catalyzing the last step of the biosynthetic pathway. Reactions annotated here mediate the uptake of ascorbate and its fully oxidized form, dehydroascorbate (DHA) by cells, and the reduction of DHA and monodehydroascorbate to regenerate ascorbate (Linster and Van Schaftingen 2007).

UnificationXref6570
type: UnificationXref
id: 3661848
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661848

Evidence684
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8001561
comment: Phosphatase action on flavin adenine dinucleotide (FAD) can reform flavin mononucleotide (FMN). The enzyme performing the reaction is nucleotide pyrophosphatase (ENPP1) and it exists as a homodimer on the plasma membrane.

UnificationXref6573
type: UnificationXref
id: REACT_167689
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_167689.1

Evidence683
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16643857
comment: FMN can be phosphorylated and adenylated to produce the second cofactor from riboflavin origins, flavin adenine dinucleotide (FAD). The enzyme responsible , FMN adenylyltransferase (FLAD1 aka FAD synthase), is cytosolic and transfers a phosphate and an adenyl group from ATP to form FAD.

UnificationXref6572
type: UnificationXref
id: 3661850
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661850

Stoichiometry220
type: Stoichiometry
physical entity: TFIID (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

http://identifiers.org/pubmed/16102047
type: PublicationXref
id: 16102047
author: Coughlin, SR
db: Pubmed
title: Protease-activated receptors in hemostasis, thrombosis and vascular biology
source: J Thromb Haemost 3:1800-14
year: 2005

Stoichiometry223
type: Stoichiometry
physical entity: TFIIE (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry224
type: Stoichiometry
physical entity: TFIIH (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Evidence680
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7668255
xref: http://identifiers.org/pubmed/17222174
comment: The reduction of cytosolic semidehydroascorbate (SDA) to ascorbate (vitC) is catalyzed by cytochrome B5 (CYB5A) associated with the mitochondrial outer membrane. In the course of the reaction, the heme iron of the cytochrome is oxidized (Linster & Van Schaftingen 2007, Shirabe et al. 1995).

Stoichiometry221
type: Stoichiometry
physical entity: TFIIA (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry222
type: Stoichiometry
physical entity: Protein84
stoichiometric coefficient: 1.0

UnificationXref6569
type: UnificationXref
id: 3661847
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661847

Evidence679
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/17266529
xref: http://identifiers.org/pubmed/20494131
xref: http://identifiers.org/pubmed/8283301
comment: Nucleotides and their derivatives are used for short-term energy storage (ATP, GTP), for intra- and extra-cellular signaling (cAMP; adenosine), as enzyme cofactors (NAD, FAD), and for the synthesis of DNA and RNA. Most dietary nucleotides are consumed by gut flora; the human body's own supply of these molecules is synthesized de novo. Additional metabolic pathways allow the interconversion of nucleotides, the salvage and reutilization of nucleotides released by degradation of DNA and RNA, and the catabolism of excess nucleotides (Rudolph 1994). These pathways are regulated to control the total size of the intracellular nucleotide pool, to balance the relative amounts of individual nucleotides, and to couple the synthesis of deoxyribonucleotides to the onset of DNA replication (S phase of the cell cycle). These pathways are also of major clinical interest as they are the means by which nucleotide analogues used as anti-viral and anti-tumor drugs are taken up by cells, activated, and catabolized (Weilin and Nordlund 2010). As well, differences in nuclotide metabolic pathways between humans and aplicomplexan parasites like Plasmodium have been exploited to design drugs to attack the latter (Hyde 2007). The movement of nucleotides and purine and pyrimidine bases across lipid bilayer membranes, mediated by SLC transporters, is annotated as part of the module "transmembrane transport of small molecules".

UnificationXref6568
type: UnificationXref
id: 3661846
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661846

Evidence678
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/20385596
xref: http://identifiers.org/pubmed/12948489
xref: http://identifiers.org/pubmed/12427752
xref: http://identifiers.org/pubmed/16378245
xref: http://identifiers.org/pubmed/22556419
xref: http://identifiers.org/pubmed/15581572
comment: Enzymes that belong to the NUDT (Nudix) superfamily catalyze the hydrolysis of phosphodiester bonds in molecules including nucleoside triphosphates and diphosphates and nucleotide sugars. Family members are defined by the presence of an amino acid sequence motif shared with the E. coli MutT gene product, and are involved in diverse physiological processes (Mildvan et al. 2005; McLennan 2006). The hydrolysis of nucleoside di and triphosphates whose purine bases have been oxidized or deaminated may protect the cell from the mutational damage that would occur if modified deoxyribonucleotides were incorporated into DNA and from the aberrant protein synthesis that would occur if modified ribonucleotides were incorporated into mRNA (Iyama et al. 2010; Takagi et al. 2012). The hydrolysis of ADP ribose may prevent the aberrant spontaneous ADP ribosylation of cellular proteins that could occur were this molecule to accumulate to high levels in the cell (Perraud et al. 2003; Shen et al. 2003).

UnificationXref6567
type: UnificationXref
id: REACT_110225
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_110225.9

Stoichiometry228
type: Stoichiometry
physical entity: TFIIA (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Evidence673
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref1113
xref: http://identifiers.org/pubmed/5940
xref: PublicationXref1111
xref: http://identifiers.org/pubmed/177353
xref: http://identifiers.org/pubmed/11008000
comment: An array of kinases catalyze the reversible phosphorylation of nucleotide monophosphates to form nucleotide diphosphates and triphosphates. Nucleoside monophosphate kinases catalyze the reversible phosphorylation of nucleoside and deoxynucleoside 5'-monophosphates to form the corresponding nucleoside 5'-diphosphates. Most appear to have restricted specificities for nucleoside monophosphates, and to use ATP preferentially (Van Rompay et al. 2000; Anderson 1973; Noda 1973). The total number of human enzymes that catalyze these reactions in vivo is not clear. In six cases, a well-defined biochemical activity has been associated with a purified protein, and these are annotated here. However, additional nucleoside monophosphate kinase-like human proteins have been identified in molecular cloning studies whose enzymatic activities are unknown, and several distinctive nucleoside monophosphate kinase activities detected in cell extracts, e.g., a GTP-requiring adenylate kinase activity (Wilson et al. 1976) and one or more guanylate kinase activities (Jamil et al. 1975) have not been unambiguously associated with specific human proteins. The nucleoside monophosphates against which each of the six well-characterized enzymes is active is shown in the table (Van Rompay et al. 2000). All six efficiently use ATP as a phosphate donor, but have some activity with other nucleoside triphosphates as well in vitro. The high concentrations of ATP relative to other nucleoside triphosphates in vivo makes it the likely major phosphate donor in these reactions under most conditions. All of these phosphorylation reactions are freely reversible in vitro when carried out with purified enzymes and substrates, having equilibrium constants near 1. In vivo, high ratios of ATP to ADP are likely to favor the forward direction of these reactions, i.e., the conversion of (d)NMP and ATP to (d)NDP and ADP. At the same time, the reversibility of the reactions and the overlapping substrate specificities of…

UnificationXref6562
type: UnificationXref
id: REACT_12881
db: Reactome
id version: 1
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_12881.1

Stoichiometry227
type: Stoichiometry
physical entity: TFIID (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Evidence672
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/947404
comment: Cytosolic glutathione reductase catalyzes the reaction of glutathione (oxidized) and NADPH + H+ to form two molecules of glutathione (reduced) and NADP+ (Loos et al. 1976).

UnificationXref6561
type: UnificationXref
id: 202247
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=202247

Stoichiometry226
type: Stoichiometry
physical entity: PhysicalEntity46
stoichiometric coefficient: 1.0

Evidence671
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16179339
xref: http://identifiers.org/pubmed/10899599
comment: Cytosolic CTP synthase 2 (CTPS) catalyzes the reaction of UTP, glutamine, ATP and water to form CTP, glutamate, ADP, and orthophosphate (Han et al. 2005; van Kuilenberg et al. 2000). Unpublished X-ray crystallographic data suggest that the enzyme is a tetramer (PDB 3IHL). Both CTPS2 and a second human gene product, CPTS, have CTP synthase activity in various test systems; their relative contributions to CTP metabolism in the body is not clear.

UnificationXref6560
type: UnificationXref
id: CHEBI:16152
db: ChEBI

Stoichiometry225
type: Stoichiometry
physical entity: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Evidence670
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16820675
xref: http://identifiers.org/pubmed/16179339
comment: Cytosolic CTP synthase 1 (CTPS) catalyzes the reaction of UTP, glutamine, ATP and water to form CTP, glutamate, ADP, and orthophosphate (Han et al. 2005). The active form of the enzyme is a tetramer (Kursala et al. 2006). Both CTPS and a second human gene product, CPTS2, have CTP synthase activity in various test systems; their relative contributions to CTP metabolism in the body is not clear.

Evidence677
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/21389046
xref: http://identifiers.org/pubmed/18462755
xref: http://identifiers.org/pubmed/17052728
comment: Cytosolic NUDT5 dimer (ADP-ribose pyrophosphatase) catalyzes the hydrolysis of ADP-ribose to form AMP and D-ribose 5-phosphate. Each NUDT5 subunit is associated with three magnesium ions (Zha et al. 2006, 2008). NUDT5 also catalyzes the hydrolysis of 8-oxo-dGTP but with a strongly alkaline pH optimum (Ito et al. 2011) so the physiological relevance of this reaction is unclear and it is not annotated here.

UnificationXref6566
type: UnificationXref
id: 3661827
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661827

Evidence676
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/20081199
xref: http://identifiers.org/pubmed/11278832
comment: Cytosolic ITPA dimer catalyzes the reaction of XTP and water to form XMP and PPi (pyrophosphate). Mg++ is required for enzymatic activity. The hydrolysis of XTP is thought to prevent its incorporation into mRNA, which would lead to aberrant protein synthesis (Lin et al. 2001; Abolhassani et al. 2010).

UnificationXref6565
type: UnificationXref
id: 3661826
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3661826

Evidence675
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/20081199
xref: http://identifiers.org/pubmed/11278832
comment: Cytosolic ITPA dimer catalyzes the reaction of dITP and water to form dIMP and PPi (pyrophosphate). Mg++ is required for enzymatic activity. The hydrolysis of dITP is thought to prevent its incorporation into DNA, which would be mutagenic (Lin et al. 2001; Abolhassani et al. 2010).

UnificationXref6564
type: UnificationXref
id: REACT_12804
db: Reactome
id version: 2
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_12804.2

Stoichiometry229
type: Stoichiometry
physical entity: Protein84
stoichiometric coefficient: 1.0

Evidence674
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/20081199
xref: http://identifiers.org/pubmed/11278832
comment: Cytosolic ITPA dimer catalyzes the reaction of ITP and water to form IMP and PPi (pyrophosphate). Mg++ is required for enzymatic activity. The hydrolysis of ITP is thought to prevent its incorporation into mRNA, which would lead to aberrant protein synthesis (Lin et al. 2001; Abolhassani et al. 2010).

UnificationXref6563
type: UnificationXref
id: 202277
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=202277

Stoichiometry210
type: Stoichiometry
physical entity: SmallMolecule10
stoichiometric coefficient: 1.0

Stoichiometry211
type: Stoichiometry
physical entity: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry212
type: Stoichiometry
physical entity: RNA Polymearse II:NTP:TFIIF complex (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

UniProt:Q12126
type: ProteinReference
xref: UnificationXref313
organism: BioSource1

Stoichiometry213
type: Stoichiometry
physical entity: TFIID (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Evidence668
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18469
comment: Cytosolic deoxythymidylate kinase (DTYMK) catalyzes the reversible reaction of either dUMP or TMP with ATP to form dUDP or TDP. The active form of the enzyme is a homodimer (Lee and Cheng 1977).

UnificationXref6557
type: UnificationXref
id: REACT_86576
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_86576.9

Evidence667
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8663313
xref: http://identifiers.org/pubmed/177353
xref: http://identifiers.org/pubmed/211390
xref: http://identifiers.org/pubmed/6248551
comment: Cytosolic guanylate kinase 1 (GUK1) catalyzes the reversible reactions of GDP and dGDP with ADP to form GMP and dGMP respectively and ATP. While native gel electrophoretic studies of whole cell extracts suggested the existence of multiple human enzymes with guanylate kinase activity (Jamil et al. 1975), only one has been purified and biochemically characterized (Agarwal et al. 1978; Brady et al. 1996). The enzyme is of clinical importance as it is a target of antitumor drugs and antiviral drugs such as acyclovir (Miller and Miller 1980).

UnificationXref6556
type: UnificationXref
id: 3665080
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665080

UnificationXref6559
type: UnificationXref
id: REACT_157731
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_157731.3

Evidence669
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18469
comment: Cytosolic deoxythymidylate kinase (DTYMK) catalyzes the reversible reaction of either dUDP or TDP with ADP to form dUMP or TMP. The active form of the enzyme is a homodimer (Lee and Cheng 1977).

UnificationXref6558
type: UnificationXref
id: 3665483
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665483

Stoichiometry215
type: Stoichiometry
physical entity: Protein84
stoichiometric coefficient: 1.0

Evidence660
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/211388
xref: http://identifiers.org/pubmed/2542324
comment: Cytosolic adenylate kinase 1 (AK1) catalyzes the reversible reactions of AMP and dAMP with ATP to form ADP and dADP respectively, plus ADP (Tsuboi 1978; Matsuura et al. 1989).

Stoichiometry214
type: Stoichiometry
physical entity: TFIIA (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

http://identifiers.org/pubmed/16102042
type: PublicationXref
id: 16102042
author: Pearce, AC
author: Auger, JM
author: McCarty, OJ
author: Watson, SP
db: Pubmed
title: GPVI and integrin alphaIIb beta3 signaling in platelets
source: J Thromb Haemost 3:1752-62
year: 2005

Stoichiometry217
type: Stoichiometry
physical entity: TFIIH (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Evidence662
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/5484814
xref: http://identifiers.org/pubmed/6182143
comment: Mitochondrial adenylate kinase 2 (AK2) catalyzes the reaction of AMP and ATP to form two molecules of ADP (Hamade et al. 1982). Localization of AK2 specifically to the mitochondrial intermembrane space is inferred from studies of the homologous rat enzyme (Criss 1970).

UnificationXref6551
type: UnificationXref
id: REACT_96301
db: Reactome
id version: 9
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_96301.9

Stoichiometry216
type: Stoichiometry
physical entity: TFIIE (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Evidence661
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/211388
xref: http://identifiers.org/pubmed/2542324
comment: Cytosolic adenylate kinase 1 (AK1) catalyzes the reversible reactions of ADP and dADP with ADP to form AMP and dAMP respectively, plus ATP (Tsuboi 1978; Matsuura et al. 1989).

UnificationXref6550
type: UnificationXref
id: 3663580
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663580

Stoichiometry219
type: Stoichiometry
physical entity: RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Evidence664
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10215863
comment: Cytosolic adenylate kinase 5 [AK5] catalyzes the reactions of (d)AMP and (d)CMP with ATP to form (d)ADP and (d)CDP, respectively, and ADP. In the body AK5 expression was observed only in brain of nine tissues tested by Northern blotting (Van Rompay et al. 1999). AK5 is inferred to occur as a dimer from unpublished crystallographic data obtained for the catalytically active carboxyterminal third of the protein (PDB 2BWJ).

UnificationXref6553
type: UnificationXref
id: REACT_126743
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_126743.5

http://identifiers.org/pubmed/11252894
type: PublicationXref
id: 11252894
author: Kirchhausen, T
db: Pubmed
title: Three ways to make a vesicle
source: Nat Rev Mol Cell Biol 1:187-98
year: 2000

Stoichiometry218
type: Stoichiometry
physical entity: PhysicalEntity45
stoichiometric coefficient: 1.0

Evidence663
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/5484814
xref: http://identifiers.org/pubmed/6182143
comment: Mitochondrial adenylate kinase 2 (AK2) catalyzes the reaction of two molecules of ADP to form AMP and ATP (Hamade et al. 1982). Localization of AK2 specifically to the mitochondrial intermembrane space is inferred from studies of the homologous rat enzyme (Criss 1970).

UnificationXref6552
type: UnificationXref
id: 3665530
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665530

Evidence666
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8663313
xref: http://identifiers.org/pubmed/177353
xref: http://identifiers.org/pubmed/211390
xref: http://identifiers.org/pubmed/6248551
comment: Cytosolic guanylate kinase 1 (GUK1) catalyzes the reversible reactions of GMP and dGMP with ATP to form GDP and dGDP respectively and ADP. While native gel electrophoretic studies of whole cell extracts suggested the existence of multiple human enzymes with guanylate kinase activity (Jamil et al. 1975), only one has been purified and biochemically characterized (Agarwal et al. 1978; Brady et al. 1996). The enzyme is of clinical importance as it is a target of antitumor drugs and antiviral drugs such as acyclovir (Miller and Miller 1980).

UnificationXref6555
type: UnificationXref
id: REACT_131765
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_131765.5

Evidence665
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10215863
comment: Cytosolic adenylate kinase 5 [AK5] catalyzes the reactions of (d)ADP and (d)CDP with ADP to form (d)AMP and (d)CMP, respectively, and ATP. In the body AK5 expression was observed only in brain of nine tissues tested by Northern blotting (Van Rompay et al. 1999). AK5 is inferred to occur as a dimer from unpublished crystallographic data obtained for the catalytically active carboxyterminal third of the protein (PDB 2BWJ).

UnificationXref6554
type: UnificationXref
id: 3665531
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665531

Formation of Double-strand Break in DNA by SPO11
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence293
EC number: 3.1.21
xref: UnificationXref1547
xref: UnificationXref1548
left: SPO11 Dimer (name copied from entity in Homo sapiens)
left: PhysicalEntity84
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SPO11 Covalently Attached to Double-strand Break (name copied from entity in Homo sapiens)

Evidence652
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9042911
xref: http://identifiers.org/pubmed/8631878
xref: http://identifiers.org/pubmed/18184586
xref: http://identifiers.org/pubmed/6893554
comment: The decarboxylation of orotidine 5'-monophosphate (OMP) to form uridine 5'-monophosphate (UMP) is catalyzed by the orotidine 5'-phosphate decarboxylase activity of the bifunctional "uridine monophosphate synthetase (orotate phosphoribosyl transferase and orotidine 5'-decarboxylase)" protein. While purified human protein has not been characterized in detail, the close similarity of the human gene to that encoding the well-studied hamster protein, and the demonstration that mutations in the human gene are associated with failure to convert orotate to UMP in vivo, provide convincing evidence that the human uridine monophosphate synthetase protein indeed catalyzes these two reactions (McClard et al. 1980; Suchi et al. 1997). The active form of the human protein is a dimer (Yablonski et al. 1996; Wittmann et al. 2008).

3' to 5' Exoribonuclease Digestion of mRNA by the Exosome Complex
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence296
xref: UnificationXref1590
xref: UnificationXref1589
left: SmallMolecule22
left: PhysicalEntity85
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule56
right: SmallMolecule55
right: SmallMolecule54
right: PhysicalEntity86
right: SmallMolecule57

Evidence653
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8448179
xref: http://identifiers.org/pubmed/7685356
comment: Cytosolic deoxycytidylate deaminase (DCTD) catalyzes the hydrolysis of dCMP (2'-deoxyuridine 5'-monophosphate) to yield dUMP (2'-deoxyuridine 5'-monophosphate) and ammonia. The active enzyme is a homohexamer (Maley et al. 1993; Weiner et al. 1993; unpublished crystallography data - PDB 2W4L).

pyrophosphate + H2O => 2 orthophosphate [cytosolic]
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence290
EC number: 3.6.1.1
xref: UnificationXref1518
xref: UnificationXref1519
participant stoichiometry: Stoichiometry458
left: SmallMolecule22
left: SmallMolecule48
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule34

Evidence654
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8631816
xref: http://identifiers.org/pubmed/8805593
comment: Deoxyuridine triphosphatase (DUT) catalyzes the hydrolysis of dUTP to form dUMP and pyrophosphate. Two isoforms of DUT are expressed, generated by alternative splicing. The major one, annotated here, is localized to the nucleoplasm (Ladner et al. 1996). The enzyme is a homotrimer (Mol et al. 1996). In the cell, this reaction depletes the supply of dUTP, preventing its incorporation into DNA, while generating dUMP, the immediate precursor of thymidine nucleotides.

pyrophosphate + H2O => 2 orthophosphate [mitochondrial]
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence291
EC number: 3.6.1.1
xref: UnificationXref1534
xref: UnificationXref1535
participant stoichiometry: Stoichiometry460
left: SmallMolecule50
left: SmallMolecule51
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule52

Evidence655
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/2656695
xref: http://identifiers.org/pubmed/11278511
comment: Cytosolic thymidylate synthase catalyzes the reaction of dUMP and N5,N10-methylene tetrahydrofolate to form TMP and dihydrofolate (Davisson et al. 1989). The enzyme is a homodimer (Phan et al. 2001).

PublicationXref1038
type: PublicationXref
author: Metzler, DE
title: Biochemistry - The Chemical Reactions of Living Cells 2nd Edn.
source: 2:1018-84
year: 2003

atRAL is reduced to atROL
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence286
EC number: 1.1.1.300
xref: UnificationXref1503
xref: UnificationXref1502
left: SmallMolecule44
left: SmallMolecule26
left: SmallMolecule43
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule47
right: SmallMolecule46

PublicationXref1037
type: PublicationXref
author: Michal, G
title: Biochemical Pathways - An Atlas of Biochemistry and Molecular Biology
source: 193-200
year: 1999

PublicationXref1036
type: PublicationXref
author: Cox, MM
author: Nelson, DL
title: Lehninger - Principles of Biochemistry 4th Edn.
source: 690-750
year: 2005

Evidence650
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/13115431
xref: http://identifiers.org/pubmed/6105839
xref: http://identifiers.org/pubmed/10889450
xref: http://identifiers.org/pubmed/165196
xref: http://identifiers.org/pubmed/9693067
comment: Dihydroorotate dehydrogenase catalyzes the oxidation of dihydroorotate to orotate (orotic acid). The enzyme is located in the inner mitochondrial membrane oriented so that cytosolic dihydroorotate molecules have access to it, and orotate is released into the cytosol. The reducing equivalents generated by the reaction are transferred by ubiquinone (Coenzyme Q) to the electron transport chain within the inner mitochondrial membrane. There is no evidence for the involvement of NAD+ as an acceptor of reducing equivalents in this reaction in mammalian cells (Jones 1980). In contrast, the reaction catalyzed by the enzyme isolated from the anaerobic bacterium Clostridium oroticum requires NAD+ as a cofactor but also proceeds strongly in the direction of dihydroorotate synthesis consistent with the greater electronegativity of NAD+ (Lieberman and Kornberg 1953). Early studies of purified rat liver enzyme by Forman and Kennedy suggested the presence of flavin mononucleotide and iron-sulfur complexes as cofactors. More recent work by Bader, Beuneu, and their colleagues with recombinant human protein expressed in insect cells has confirmed the presence of flavin mononucleotide, at a stoichiometry of one molecule per molecule of apoenzyme but suggests that iron-sulfur complexes, if indeed they are involved in the oxidation and electron transport process, are not an integral part of the dihydroorotate dehydrogenase holoenzyme.

Evidence651
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9042911
xref: http://identifiers.org/pubmed/8631878
xref: http://identifiers.org/pubmed/18184586
xref: http://identifiers.org/pubmed/6893554
comment: The synthesis of orotidine 5'-monophosphate (OMP) from orotate and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) is catalyzed by the orotate phosphoribosyltransferase activity of the bifunctional "uridine monophosphate synthetase (orotate phosphoribosyl transferase and orotidine 5'-decarboxylase)" protein. The reaction itself is freely reversible, but is pulled in the forward direction in vivo by the irreversible hydrolysis of pyrophosphate. While purified human protein has not been characterized in detail, the close similarity of the human gene to that encoding the well-studied hamster protein, and the demonstration that mutations in the human gene are associated with failure to convert orotate to UMP in vivo, provide convincing evidence that the human uridine monophosphate synthetase protein indeed catalyzes these two reactions (McClard et al. 1980; Suchi et al. 1997). The active form of the human protein is a dimer (Yablonski et al. 1996; Wittmann et al. 2008).

Destruction of AUF1 and mRNA
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence304
xref: UnificationXref1729
xref: UnificationXref1730
left: Ubiquitinated AUF1 Tetramer: Destabilized mRNA Complex (name copied from entity in Homo sapiens)
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.

5' to 3' Exoribonuclease Digestion of Decapped mRNA
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence300
xref: UnificationXref1627
xref: UnificationXref1626
left: SmallMolecule22
left: Decapped mRNA:LSM1-7 Complex (name copied from entity in Homo sapiens)
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule56
right: SmallMolecule55
right: Lsm1-7 Complex (name copied from entity in Homo sapiens)
right: SmallMolecule54
right: SmallMolecule57

Evidence656
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref1092
xref: http://identifiers.org/pubmed/6105839
comment: The pyrimidine orotate (orotic acid) is synthesized in a sequence of four reactions, deriving its atoms from glutamine, bicarbonate, and aspartate. A single multifunctional cytosolic enzyme catalyzes the first three of these reactions, while the last one is catalyzed by an enzyme associated with the inner mitochondrial membrane. In two further reactions, catalyzed by a bifunctional cytosolic enzyme, orotate reacts with 1-phosphoribosyl 5-pyrophosphate (PRPP) to yield orotidine 5'-monophosphate, which is decarboxylated to yield uridine 5'-monophosphate (UMP). While several individual reactions in this pathway are reversible, other irreversible reactions drive the pathway in the direction of UMP biosynthesis in the normal cell. All reactions are thus annotated here only in the forward direction. This pathway has been most extensively analyzed at the genetic and biochemical level in hamster cell lines. All three enzymes have also been purified from human sources, however, and the key features of these reactions have been confirmed from studies of this human material (Jones 1980; Webster et al. 2001). All other pyrimidines are synthesized from UMP. The reactions annotaed here, catalyzed by dCMP deaminase and dUTP diphosphatase yield dUMP, which in turn is converted to TMP by thymidylate synthase.

AUF1(hnRNP D0) Dimers Bind AU-rich Element in 3' UTR of Transcripts
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence303
xref: UnificationXref1645
xref: UnificationXref1644
participant stoichiometry: Stoichiometry490
left: AUF1 Dimer (isoform p37 or p40)
left: PhysicalEntity92
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: AUF1 Tetramer: Destabilized mRNA Complex (name copied from entity in Homo sapiens)

Evidence657
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/15689149
xref: http://identifiers.org/pubmed/7923172
comment: Cytosolic cytidine deaminase catalyzes the hydrolysis of cytidine or dexoycytidine to form uridine or deoxyuridine and ammonia (Laliberte and Momparler 1994). The active form of the enzyme is a tetramer (Chung et al. 2005).

Scavenging of the 7-methylguanosine Cap by DCPS
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence297
xref: UnificationXref1599
xref: UnificationXref1598
left: SmallMolecule22
left: PhysicalEntity86
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule58
right: PhysicalEntity89

Evidence658
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref1092
comment: In pyrimidine salvage reactions, nucleosides and free bases generated by DNA and RNA breakdown are converted back to nucleotide monophosphates, allowing them to re-enter the pathways of pyrimidine biosynthesis (interconversion).

Binding of Lsm1-7 Complex to Deadenylated mRNA
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence299
xref: UnificationXref1619
xref: UnificationXref1620
left: PhysicalEntity85
left: Lsm1-7 Complex (name copied from entity in Homo sapiens)
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Deadenylated mRNA:Lsm1-7 Complex (name copied from entity in Homo sapiens)

Evidence659
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16098809
comment: The events of human pyrimidine metabolism are conveniently, if somewhat arbitrarily, grouped into four pathways: de novo synthesis of the pyrimidine ring and its conversion to uridine 5'-monophosphate (UMP), the biosynthesis of other pyrimidine ribo- and deoxyribonucleotides, pyrimidine salvage reactions, and pyrimidine catabolism (Loffler et al. 2005). De novo synthesis of the pyrimidine ring and its conversion to UMP. The pyrimidine base orotate is synthesized from glutamine, bicarbonate, and aspartate. Orotate reacts with 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) and is then decarboxylated to form the pyrimidine nucleotide UMP. Pyrimidine biosynthesis [interconversion]. Pyrimidine ribo- and deoxyribonucleotide di- and triphosphates are synthesized, both from UMP and from pyrimidine ribonucleotide monophosphates generated in salvage reactions. Pyrimidine salvage reactions. Pyrimidine nucleosides and free bases generated by DNA and RNA breakdown are converted to nucleotide monophosphates. Pyrimidine catabolism. The pyrimidine bases thymine and uracil are degraded to beta-aminoisobutyrate and beta-alanine, respectively, which are excreted from the body.

PublicationXref1033
type: PublicationXref
author: Nicholls, DG
author: Ferguson, SJ
title: Bioenergetics 3
source: 89-134
year: 2002

PublicationXref1034
type: PublicationXref
author: Murray, RK
title: Harper's Biochemistry 25th Edn.
source: 137-48

http://identifiers.org/pubmed/16243729
type: PublicationXref
id: 16243729
author: Chen, C
author: Yu, L
author: Ye, GM
author: Guo, JH
author: Huang, S
author: Wan, B
author: Han, DD
db: Pubmed
title: Cloning and characterization a novel human 1-acyl-sn-glycerol-3-phosphate acyltransferase gene AGPAT7
source: DNA Seq 16:386-90
year: 2005

SMG1 Phosphorylates UPF1 (Enhanced by Exon Junction Complex)
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence311
EC number: 2.7.11
xref: UnificationXref2077
xref: UnificationXref2078
participant stoichiometry: Stoichiometry663
participant stoichiometry: Stoichiometry664
left: SMG1:UPF1:EJC:Translated mRNP (name copied from entity in Homo sapiens)
left: SmallMolecule30
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SMG1:Phosphorylated UPF1:EJC:Translated mRNP (name copied from entity in Homo sapiens)
right: SmallMolecule31

Evidence643
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/19470646
xref: http://identifiers.org/pubmed/10075721
comment: Cytosolic guanine deaminase (GDA) catalyzes the reaction of guanine and water to form xanthine and ammonia (Yuan et al. 1999). The active enzyme is a homodimer (Murphy et al. 2009).

Formation of UPF1:eRF3 Complex on mRNA with a Premature Termination Codon and No Exon Junction Complex
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence313
xref: UnificationXref2086
xref: UnificationXref2087
left: Note: the coordinates are copied over from Homo sapiens.
left: Translated mRNA Complex with Premature Termination Codon Not Preceding Exon Junction (name copied from entity in Homo sapiens)
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: UPF1:eRF3 Complex on Translated mRNA (name copied from entity in Homo sapiens)

Evidence644
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/10656833
xref: http://identifiers.org/pubmed/1999334
comment: Hydrogen peroxide is generated in the course of peroxisomal fatty acid oxidation and purine catabolism, and is rapidly converted to water and molecular oxygen by the enzyme catalase. This enzyme is widely distributed in the body, but is especially abundant in liver, kidney, and red blood cells.

Recognition of AAUAAA sequence by CPSF
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence318
xref: UnificationXref2110
xref: UnificationXref2109
left: CPSF (name copied from entity in Homo sapiens)
left: capped intronless pre-mRNA:CBC complex (name copied from entity in Homo sapiens)
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: CPSF:capped intronless pre-mRNA:CBC complex (name copied from entity in Homo sapiens)

Evidence641
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3029074
xref: http://identifiers.org/pubmed/2104852
xref: http://identifiers.org/pubmed/6771276
comment: Cytosolic nucleoside phosphorylase (NP) trimer catalyzes the reversible reaction of guanosine or deoxyguanosine with orthophosphate to form guanine and ribose 1-phosphate or deoxyribose 1-phosphate (Ealick et al. 1990; Wiginton et al. 1980). While NP is active with either nuckeotide in vitro, levels of deoxyguanosine are normally low in vivo, limiting the extent of this reaction. NP deficiency in vivo is associated with defects in purine nucleotide salvage and leads to immunodeficiency (Williams et al. 1987).

Release of Cytochrome c from mitochondria
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence323
xref: UnificationXref2124
xref: UnificationXref2123
left: Note: the coordinates are copied over from Homo sapiens.
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Note: the coordinates are copied over from Homo sapiens.

Evidence642
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3029074
xref: http://identifiers.org/pubmed/2104852
xref: http://identifiers.org/pubmed/6771276
comment: Cytosolic nucleoside phosphorylase (NP) trimer catalyzes the reversible reaction of inosine or deoxyinosine with orthophosphate to form hypoxanthine and ribose 1-phosphate or deoxyribose 1-phosphate (Ealick et al. 1990; Wiginton et al. 1980). While NP is active with either nuckeotide in vitro, levels of deoxyinosine are normally low in vivo, limiting the extent of this reaction. NP deficiency in vivo is associated with defects in purine nucleotide salvage and leads to immunodeficiency (Williams et al. 1987).

http://identifiers.org/pubmed/12676795
type: PublicationXref
id: 12676795
author: Reichardt, LF
author: Huang, EJ
db: Pubmed
title: Trk receptors: roles in neuronal signal transduction
source: Annu Rev Biochem 72:609-42
year: 2003

Evidence640
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/4620886
comment: Nucleosides and free bases generated by DNA and RNA breakdown are converted back to nucleotide monophosphates, allowing them to re-enter the pathway of purine biosynthesis. Nucleosides and free bases generated by DNA breakdown are converted back to nucleotide monophosphates, allowing them to re-enter the pathway of purine biosynthesis. Nucleosides and free bases generated by RNA breakdown are converted back to nucleotide monophosphates, allowing them to re-enter the pathways of purine biosynthesis. Under normal conditions, DNA turnover is limited and deoxyribonucleotide salvage operates at a correspondingly low level (Watts 1974).

Butyrate Response Factor1 (BRF1) Binds AU-rich Element in 3' UTR of mRNA
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence306
xref: UnificationXref1739
xref: UnificationXref1738
left: PhysicalEntity100
left: ZFP36L1
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: BRF1:mRNA Complex (name copied from entity in Homo sapiens)

http://identifiers.org/pubmed/12676794
type: PublicationXref
id: 12676794
author: Shilatifard, A
author: Conaway, JW
author: Conaway, RC
db: Pubmed
title: The RNA polymerase II elongation complex.
source: Annu Rev Biochem 72:693-715
year: 2003

Tristetraproline (TTP) Binds AU-rich Elements in 3' UTR of Target mRNAs
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence308
xref: UnificationXref1748
xref: UnificationXref1749
left: Note: the coordinates are copied over from Homo sapiens.
left: PhysicalEntity101
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: TTP:mRNA Complex (name copied from entity in Homo sapiens)

Evidence649
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8619816
comment: The synthesis of dihydroorotate from N-carbamoyl L-aspartate is catalyzed by the dihydroorotase activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein. This activity has not been directly demonstrated in experimental studies of the purified human protein, but has been inferred from the behavior of the purified hamster protein and the high degree of sequence similarity between the cloned hamster and human genes (Iwahana et al. 1996). Also on the basis of this similarity, the active human protein is annotated as a hexamer (Lee et al. 1985).

Autophosphorylation of PAK-2p34 in the activation loop
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence326
xref: UnificationXref2138
xref: UnificationXref2137
left: Homologues of PAK2(213-524)
left: SmallMolecule30
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Homologues of p-T402-PAK2(213-524)
right: SmallMolecule31

Evidence647
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8619816
xref: http://identifiers.org/pubmed/4684686
comment: The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985).

Proteolytic PAK-2p34 fragment translocates to the nucleus
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence327
xref: UnificationXref2143
xref: UnificationXref2142
left: Homologues of p-T402-PAK2(213-524)
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Homologues of p-T402-PAK2(1-524)

Evidence648
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8619816
xref: http://identifiers.org/pubmed/4684686
xref: http://identifiers.org/pubmed/2995985
comment: The synthesis of N-carbamoyl L-aspartate from carbamoyl phosphate and L-aspartate is catalyzed by the aspartate carbamoyltansferase activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985).

Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence328
xref: UnificationXref2151
xref: UnificationXref2150
participant stoichiometry: Stoichiometry688
participant stoichiometry: Stoichiometry689
left: Homologues of PAK2(1-524)
left: SmallMolecule30
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Homologues of p-5S-PAK2(1-524)
right: SmallMolecule31

Evidence645
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/4620886
comment: The purine bases guanine and hypoxanthine (derived from adenine by events in the purine salvage pathways) are converted to xanthine and then to uric acid, which is excreted from the body (Watts 1974). The end-point of this pathway in humans and hominoid primates is unusual. Most other mammals metabolize uric acid further to yield more soluble end products, and much speculation has centered on possible roles for high uric acid levels in normal human physiology.

Mitochondrial recruitment of Drp1
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence330
xref: UnificationXref2158
xref: UnificationXref2159
left: Note: the coordinates are copied over from Homo sapiens.
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Note: the coordinates are copied over from Homo sapiens.

Evidence646
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/4620886
comment: The events of human purine metabolism are conveniently, if somewhat arbitrarily, grouped into four pathways: de novo synthesis of inosine 5'-monophosphate (IMP), the biosynthesis of other purine ribo- and deoxyribonucleotides, purine salvage reactions, and purine catabolism (Watts 1974). De novo synthesis of inosine 5'-monophosphate (IMP). The purine ribonucleotide IMP is assembled on 5-phospho-alpha-D-ribose 1-diphosphate (PRPP). Purine biosynthesis [interconversion]. Purine ribo- and deoxyribonucleotide di- and triphosphates are synthesized, both from IMP and from guanosine and adenosine ribo- and deoxyribonucleotide monophosphates generated in salvage reactions. Purine salvage reactions. Purine nucleosides and free bases generated by DNA and RNA breakdown are converted to nucleotide monophosphates. Purine catabolism. The purine bases guanine and hypoxanthine are degraded to uric acid, which is excreted from the body.

Phosphorylation of Ribosomal protein S6 by activated S6K1
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence203
xref: UnificationXref1098
xref: UnificationXref1099
participant stoichiometry: Stoichiometry401
participant stoichiometry: Stoichiometry400
left: Homologues of RPS6
left: SmallMolecule30
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Homologues of p-5S-RPS6
right: SmallMolecule31

Evidence630
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/7903306
comment: Two human isoenzymes, IMP dehydrogenase 1 and 2 (IMPDH1,2) catalyze the irreversible dehydrogenation of inosine 5'-monophosphate (IMP) to form xanthosine 5'-monophosphate (XMP). The active forms of both isoenzymes are homotetramers, and they are nearly identical in their catalytic efficiencies and their susceptibility to inhibition by XMP (Carr et al. 1993; Colby et al. 1999; Hager et al. 1995). Both enzymes occur as homotetramers (Colby et al. 1999 - IMPDH2; unpubliched data in PDB 1JCN IMPDH1). A variety of experiments suggest that IMPDH1 and 2 have distinct functions in vivo. While IMPDH1 is expressed at constant levels, IMPDH2 is expressed at elevated levels in tumor cells and in mitotic normal cells. In humans, heterozygosity for mutant forms of IMPDH1 is associated with a form of retinitis pigmentosa (Bowne et al. 2002). In laboratory mice, mutations that disrupt the homologue of IMPDH1 have no obvious effect at the level of the whole organism, while ones that disrupt IMPDH2 are lethal (Gu et al. 2003). This reaction is the rate limiting step in the synthesis of guanosine 5'-monophosphate (GMP) from IMP, and GMP competitively inhibits the well-characterized bacterial IMP dehydrogenase enzyme. Evidence for an inhibitory effect of GMP on the human isoenzymes has not been reported. Rather, they appear to be inhibited by XMP; in addition, transcription of one or both IMP dehydrogenase mRNAs may be inhibited by high cellular GMP concentrations (Glesne et al. 1991).

Phosphorylation and activation of eIF4B by activated S6K1
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence204
xref: UnificationXref1104
xref: UnificationXref1103
left: SmallMolecule30
left: Note: the coordinates are copied over from Homo sapiens.
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule31
right: phospho-p-S422-EIF4B

Evidence631
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8089153
xref: http://identifiers.org/pubmed/7706277
comment: Cytosolic GMP synthase (GMPS) catalyzes the reaction of xanthosine 5'-monophosphate (XMP), ATP, glutamine and water to form guanosine 5'-monophosphate (GMP), AMP, glutamate and pyrophosphate. GMPS is a monomer (Hirst et al. 1994; Nakamura and Lou 1995).

Evidence632
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1592113
xref: http://identifiers.org/pubmed/15786719
comment: Two isoforms of adenylosuccinate synthetase, ADSS and ADSSL1, catalyze the reaction of IMP, aspartate, and GTP to form adenylosuccinate, GDP, and orthophosphate (Powell et al. 1992; Sun et al. 2005). ADSS is a homotetramer (unpublished crystallographic data - PDB 2V40) and ADSSL1 is inferred to be a tetramer likewise.

Activation of S6K1
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence202
xref: UnificationXref1087
xref: UnificationXref1086
participant stoichiometry: Stoichiometry398
participant stoichiometry: Stoichiometry399
left: Note: the coordinates are copied over from Homo sapiens.
left: SmallMolecule30
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule31
right: phospho-p-S371,T389-RPS6KB1

Evidence633
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8366112
xref: http://identifiers.org/pubmed/10958654
comment: The irreversible conversion of adenylosuccinate to adenosine 5'-monophosphate and fumarate is catalyzed by adenylosuccinate lyase. The active form of this enzyme is a cytosolic tetramer (Stone et al. 1993). The enzyme also catalyzes the conversion of 5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide (SAICAR) to 5'-phosphoribosyl-5-aminoimidazole-4-carboxamide (AICAR) and fumarate. Humans lacking the enzyme accumulate dephosphorylated forms of both substrates, indicating that the enzyme mediates both reactions in vivo as well (Race et al. 2000).

Endosome acidification
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence220
xref: UnificationXref1195
xref: UnificationXref1196
left: SmallMolecule26
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule36

Evidence634
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/1574589
comment: The purine ribonucleotide inosine 5'-monophosphate (IMP) is assembled on 5-phospho-alpha-D-ribose 1-diphosphate (PRPP), with atoms derived from aspartate, glutamine, glycine, N10-formyl-tetrahydrofolate, and carbon dioxide. Although several of the individual reactions in this sequence are reversible, as indicated by the double-headed arrows in the diagram, other irreversible steps drive the pathway in the direction of IMP synthesis in the normal cell. All of these reactions are thus annotated here only in the direction of IMP synthesis. Guanosine 5'-monophosphate (GMP) and adenosine 5'-monophosphate (AMP) are synthesized from IMP.

Active JNK moves to the nucleus and phosphorylates different transcription factors
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence223
xref: UnificationXref1205
xref: UnificationXref1204
left: phospho-p-T,Y-MAPK8
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: phospho-p-T,Y-MAPK8

Evidence635
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9843365
xref: http://identifiers.org/pubmed/6281270
xref: http://identifiers.org/pubmed/227870
xref: http://identifiers.org/pubmed/2999129
comment: Cytosolic adenosine linase (ADK) catalyzes the reactions of adenosine and deoxyadenosine with ATP to yield the corresponding nucleotide monophosphates and ADP (Andres and Fox 1979). The enzyme is substantially more active on adenosine than deoxyadenosine in vitro (Hurley at al. 1985) though studies of cultured cells suggest that both reactions may be physiologically relevant (Hershfield et al. 1982). The enzyme is a monomer complexed with magnesium (Mathews et al. 1998).

TSC2 activates intrinsic GTPase activity of Rheb
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence208
xref: UnificationXref1118
xref: UnificationXref1119
left: Rheb:GTP (name copied from entity in Homo sapiens)
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule34
right: Rheb:GDP (name copied from entity in Homo sapiens)

Evidence636
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/9857047
xref: http://identifiers.org/pubmed/1429593
comment: Cytosolic AMP deaminase (AMPD) catalyzes the hydrolysis of AMP to yield IMP and ammonia. Three isoforms of AMPD, E, L, and M, have been identified that differ in their expression patterns in the body. All occur as tetramers and all have qualitatively the same catalytic activity, however (Bausch-Jurken et al. 1992; Mahnke-Zizelman et al. 1998).

PDK1 attachment to plasma membrane
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence213
xref: UnificationXref1132
xref: UnificationXref1133
left: Homologues of PDPK1
left: SmallMolecule35
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: PIP3:PDK1 complex (name copied from entity in Homo sapiens)

Evidence637
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3029074
xref: http://identifiers.org/pubmed/2104852
xref: http://identifiers.org/pubmed/6771276
comment: Cytosolic nucleoside phosphorylase (NP) trimer catalyzes the reversible reaction of guanine with ribose 1-phosphate or deoxyribose 1-phosphate to form guanosine or deoxyguanosine and orthophosphate (Ealick et al. 1990; Wiginton et al. 1980). While NP is active with either ribose 1-phosphate or deoxyribose 1-phosphate in vitro, levels of deoxyribose 1-phosphate are normally low in vivo, limiting the extent of this reaction. NP deficiency in vivo is associated with defects in purine nucleotide salvage and leads to immunodeficiency (Williams et al. 1987).

PIP3 binds to RhoA and activates it
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence239
xref: UnificationXref1269
xref: UnificationXref1270
left: Homologues of RHOA
left: SmallMolecule19
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: PIP3:RhoA (name copied from entity in Homo sapiens)

Evidence638
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3029074
xref: http://identifiers.org/pubmed/2104852
xref: http://identifiers.org/pubmed/6771276
comment: Cytosolic nucleoside phosphorylase (NP) trimer catalyzes the reversible reaction of hypoxanthine with ribose 1-phosphate or deoxyribose 1-phosphate to form inosine or deoxyinosine and orthophosphate (Ealick et al. 1990; Wiginton et al. 1980). While NP is active with either ribose 1-phosphate or deoxyribose 1-phosphate in vitro, levels of deoxyribose 1-phosphate are normally low in vivo, limiting the extent of this reaction. NP deficiency in vivo is associated with defects in purine nucleotide salvage and leads to immunodeficiency (Williams et al. 1987).

Evidence639
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/457664
comment: Cytosolic APRT dimer catalyzes the reaction of adenine and 5-phospho-alpha-D-ribose 1-diphosphate to form AMP and pyrophosphate (Holden et al. 1979).

Production of ceramide which can activate JNK and other targets
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence226
EC number: 3.1.4.12
xref: UnificationXref1226
xref: UnificationXref1225
left: SmallMolecule22
left: SmallMolecule37
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule39
right: SmallMolecule38

RhoA is activated by nucleotide exchange and inhibits axonal growth
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence228
xref: UnificationXref1247
xref: UnificationXref1246
left: RhoA (Mg cofactor):GDP (name copied from entity in Homo sapiens)
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: RhoA (Mg cofactor):GTP (name copied from entity in Homo sapiens)

Choline
type: SmallMoleculeReference
name: ChEBI:15354 Choline
xref: UnificationXref3171

Citric acid cycle (TCA cycle)
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction325
pathway component: BiochemicalReaction330
pathway component: BiochemicalReaction327
pathway component: BiochemicalReaction326
pathway component: BiochemicalReaction329
pathway component: BiochemicalReaction332
pathway component: BiochemicalReaction324
pathway component: BiochemicalReaction323
pathway component: BiochemicalReaction162
pathway component: BiochemicalReaction331
pathway component: BiochemicalReaction328
evidence: Evidence608
xref: UnificationXref3995
xref: RelationshipXref453
xref: UnificationXref3996
pathway order: PathwayStep589
pathway order: PathwayStep597
pathway order: PathwayStep592
pathway order: PathwayStep598
pathway order: PathwayStep591
pathway order: PathwayStep596
pathway order: PathwayStep595
pathway order: PathwayStep590
pathway order: PathwayStep344
pathway order: PathwayStep594
pathway order: PathwayStep593
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/6788766
type: PublicationXref
id: 6788766
author: Sagawa, N
author: Johnston, JM
author: Okazaki, T
author: Bleasdale, JE
author: MacDonald, PC
author: Okita, JR
db: Pubmed
title: Diacylglycerol metabolism and arachidonic acid release in human fetal membranes and decidua vera
source: J Biol Chem 256:7316-21
year: 1981

Cell Cycle
type: Pathway
data source: Provenance1
pathway component: REACT 99737.9
pathway component: REACT 128243.5
pathway component: REACT 79085.9
evidence: Evidence1271
xref: UnificationXref7905
xref: UnificationXref7906
pathway order: PathwayStep1250
pathway order: PathwayStep1178
pathway order: PathwayStep1223
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

http://identifiers.org/pubmed/7118399
type: PublicationXref
id: 7118399
author: Lee, HH
author: Lo, KY
author: Pai, SH
author: Pan, F
db: Pubmed
title: Purification and subunit structure studies of human placental threonyl-tRNA synthetase
source: Int J Pept Protein Res 19:300-9
year: 1982

Choline phosphate [ChEBI:3667]
type: SmallMoleculeReference
name: Choline phosphate
name: O-Phosphocholine
name: Phosphorylcholine
name: Phosphocholine
xref: UnificationXref1216

GEFs activate Rho GTPase:GDP
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence254
xref: UnificationXref1350
xref: UnificationXref1349
left: RhoGTPase:GDP (name copied from entity in Homo sapiens)
left: SmallMolecule17
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: RhoGTPase:GTP (name copied from entity in Homo sapiens)
right: SmallMolecule18

Evidence621
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/4348202
xref: http://identifiers.org/pubmed/4726295
comment: PRPP stimulates the dissociation of phosphoribosyl pyrophosphate amidotransferase tetramers to form dimers (Holmes et al. 1973a,b).

GAPs inactivate Rho GTPase:GTP by hydrolysis
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence255
xref: UnificationXref1386
xref: UnificationXref1387
left: RhoGTPase:GTP (name copied from entity in Homo sapiens)
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule34
right: RhoGTPase:GDP (name copied from entity in Homo sapiens)

Evidence622
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18388293
xref: http://identifiers.org/pubmed/4348202
xref: http://identifiers.org/pubmed/762062
xref: http://identifiers.org/pubmed/8380692
xref: http://identifiers.org/pubmed/4726295
comment: Cytosolic PPAT (phosphoribosyl pyrophosphate amidotransferase) catalyzes the reaction of 5-phospho-alpha-D-ribose 1-diphosphate (PRPP), water, and L-glutamine to form 5-phosphoribosylamine, L-glutamate, and pyrophosphate. This event is the committed step in de novo purine synthesis. The reaction itself is reversible, but it is pulled strongly in the direction of 5'-phosphoribosylamine synthesis by the irreversible hydrolysis of the pyrophosphate that is also formed in the reaction. Fluoresence microscopy studies of cultured human cells have shown that PPAT is cytosolic and suggest that it may co-localize with other enzymes of de novo IMP biosynthesis under some metabolic conditions (An et al. 2008). The PPAT enzyme is inferred to be an iron-sulfur protein, like its well-characterized B. subtilis homologue, because incubation of purified enzyme with molecular oxygen or chelating agents inactivates it, and activity can be restored by incubation with ferrous iron and inorganic sulfide. The stoichiometry of the iron-sulfur moiety and its role in enzyme activity remain unknown (Itakura and Holmes 1979). The fully active form of the enzyme is a dimer, which can associate further to form a tetramer with sharply reduced activity (Holmes et al. 1973b; Iwahana et al. 1993). Interaction of the enzyme with inosine 5'-monophosphate (IMP), guanosine 5'-monophosphate (GMP), and adenosine 5'-monophosphate (AMP), end products of de novo purine biosynthesis, favors tetramer formation, while interaction with 5-phospho-alpha-D-ribose 1-diphosphate (PRPP), a required substrate, favors formation of the active dimer. Kinetic studies suggest that the enzyme's binding site for GMP and IMP is separate from its AMP binding site (Holmes et al. 1973a).

GDIs block activation of Rho GTPase:GDP
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence256
xref: UnificationXref1402
xref: UnificationXref1401
left: RhoGTPase:GDP (name copied from entity in Homo sapiens)
left: GDI proteins
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Inactivated RhoGTPase:GDP:GDI complex (name copied from entity in Homo sapiens)

Dissociation of Rho GTP:GDP from GDI complex
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence257
xref: UnificationXref1403
xref: UnificationXref1404
left: Inactivated RhoGTPase:GDP:GDI complex (name copied from entity in Homo sapiens)
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: RhoGTPase:GDP (name copied from entity in Homo sapiens)
right: GDI proteins

Evidence620
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/4348202
xref: http://identifiers.org/pubmed/4726295
comment: Cytosolic AMP, GMP, and IMP stimulate the association of phosphoribosyl pyrophosphate amidotransferase (PPAT) dimers to form tetramers (Holmes et al. 1973a,b).

GEFs activate RhoA,B,C
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence261
xref: UnificationXref1415
xref: UnificationXref1414
left: RhoA,B,C:GDP (name copied from entity in Homo sapiens)
left: SmallMolecule17
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule18
right: RhoA/B/C:GTP (name copied from entity in Homo sapiens)

Evidence625
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8110788
xref: http://identifiers.org/pubmed/18388293
comment: The irreversible transfer of an amino group from L-glutamine to 5'-phosphoribosylformylglycinamide (FGAR), forming 5'-phosphoribosylformylglycinamidine (FGAM) and glutamate, accompanied by the conversion of ATP to ADP and orthophosphate, is catalyzed by phosphoribosylformylglycinamidine synthetase. The human enzyme has been purified and characterized biochemically (Barnes et al. 1994). Fluoresence microscopy studies of cultured human cells have shown that the enzyme is cytosolic and suggest that it may co-localize with other enzymes of de novo IMP biosynthesis under some metabolic conditions (An et al. 2008).

Activation of Protein kinase C, alpha type by Diacylglycerol
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence271
xref: UnificationXref1436
xref: UnificationXref1435
left: Homologues of PRKCA
left: SmallMolecule21
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Protein Kinase C, alpha type: DAG (name copied from entity in Homo sapiens)

Evidence626
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18388293
xref: http://identifiers.org/pubmed/2147474
xref: http://identifiers.org/pubmed/11381136
comment: The irreversible synthesis of cytosolic 5'-phosphoribosyl-5-aminoimidazole (AIR) from 5'-phosphoribosylformylglycinamidine (FGAM), accompanied by the conversion of ATP to ADP and orthophosphate, is catalyzed by the phosphoribosylaminoimidazole synthetase domain of the trifunctional protein, "phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase" (GART) (Aimi et al. 1990). The active form of the protein is cytosolic and may co-localize with other enzymes of de novo IMP biosynthesis under some metabolic conditions (Gooljarsingh et al. 2001; An et al. 2008).

http://identifiers.org/pubmed/16747180
type: PublicationXref
id: 16747180
author: Eggleston, LV
author: Krebs, HA
db: Pubmed
title: The oxidation of pyruvate in pigeon breast muscle
source: Biochem J 34:442-459
year: 1940

N-linked glycosylation of WNTs
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence275
xref: UnificationXref1443
xref: UnificationXref1444
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.

Evidence623
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18388293
xref: http://identifiers.org/pubmed/2147474
xref: http://identifiers.org/pubmed/11381136
comment: The synthesis of cytosolic 5-phosphoribosylglycinamide from 5-phosphoribosylamine and glycine, accompanied by the conversion of ATP to ADP and orthophosphate, is catalyzed by the phosphoribosylglycinamide synthetase domain of the trifunctional protein, "phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase" (GART) (Aimi et al. 1990). The active form of the protein is cytosolic (Gooljarsingh et al. 2001; An et al. 2008).

WNT ligands traffic to the Golgi
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence276
xref: UnificationXref1445
xref: UnificationXref1446
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.

Evidence624
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18388293
xref: http://identifiers.org/pubmed/2147474
xref: http://identifiers.org/pubmed/11381136
xref: http://identifiers.org/pubmed/12450384
comment: The irreversible transfer of a formyl group to cytosolic 5-phosphoribosylglycinamide (GAR) to form 5'-phosphoribosylformylglycinamide (FGAR) is catalyzed by the phosphoribosylglycinamide formyltransferase domain of the trifunctional protein, "phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase" (GART) (Aimi et al. 1990; Zhang et al. 2002). Fluoresence microscopy studies of cultured human cells have shown that GART is cytosolic and suggest that it may co-localize with other enzymes of de novo IMP biosynthesis under some metabolic conditions (Gooljarsingh et al. 2001; An et al. 2008).

Retromer recycles WLS to the Golgi
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence277
xref: UnificationXref1463
xref: UnificationXref1462
left: WLS:retromer (name copied from entity in Homo sapiens)
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: WLS:retromer (name copied from entity in Homo sapiens)

Evidence629
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11096114
xref: http://identifiers.org/pubmed/18388293
xref: http://identifiers.org/pubmed/8567683
comment: The reversible synthesis of inosine 5'-monophosphate from 5'-phosphoribosyl-5-formaminoimidazole-4-carboxamide (FAICAR) is catalyzed by the IMP cyclohydrolase activity of the bifunctional 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase enzyme. This cytosolic protein occurs primarily as a dimer (Rayl et al. 1996; Vergis et al. 2001) and may further associate with other enzymes of de novo IMP biosynthesis under some metabolic conditions (An et al. 2008).

http://identifiers.org/pubmed/15021249
type: PublicationXref
id: 15021249
author: de Koning, TJ
author: Klomp, LW
db: Pubmed
title: Serine-deficiency syndromes
source: Curr Opin Neurol 17:197-204
year: 2004

RDH8 reduces atRAL to atROL
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence284
EC number: 1.1.1.300
xref: UnificationXref1495
xref: UnificationXref1494
left: SmallMolecule44
left: SmallMolecule26
left: SmallMolecule43
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: SmallMolecule45
right: SmallMolecule46

Evidence627
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/18388293
xref: http://identifiers.org/pubmed/8366112
xref: http://identifiers.org/pubmed/10958654
comment: The reversible conversion of 5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide (SAICAR) to 5'-phosphoribosyl-5-aminoimidazole-4-carboxamide (AICAR) and fumarate is catalyzed by adenylosuccinate lyase. The active form of this enzyme is a cytosolic tetramer (Stone et al. 1993), and fluoresence microscopy of cultured human cells suggests that it may associate with other enzymes of de novo IMP biosynthesis under some metabolic conditions (An et al. 2008). The enzyme also catalyzes the conversion of adenylosuccinate to adenosine 5'-monophosphate and fumarate. Humans lacking the enzyme accumulate dephosphorylated forms of both substrates, indicating that the enzyme mediates both reactions in vivo as well (Race et al. 2000).

Evidence628
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/11096114
xref: http://identifiers.org/pubmed/18388293
xref: http://identifiers.org/pubmed/8567683
comment: The irreversible transfer of a formyl group to 5'-phosphoribosyl-5-aminoimidazole-4-carboxamide (AICAR), to yield 5'-phosphoribosyl-5-formaminoimidazole-4-carboxamide (FAICAR), is catalyzed by the phosphoribosylaminoimidazolecarboxamide formyltransferase activity of the bifunctional 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase enzyme. This cytosolic protein occurs primarily as a dimer (Rayl et al. 1996; Vergis et al. 2001) and may further associate with other enzymes of de novo IMP biosynthesis under some metabolic conditions (An et al. 2008).

Evidence617
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: PublicationXref1036
xref: PublicationXref1033
xref: PublicationXref1034
xref: http://identifiers.org/pubmed/10647174
xref: PublicationXref1038
xref: http://identifiers.org/pubmed/2862839
xref: PublicationXref1037
comment: Mitochondria are often described as the "powerhouse" of a cell as it is here that energy is largely released from the oxidation of food. Reducing equivalents generated from beta-oxidation of fatty acids and from the Krebs cycle enter the electron transport chain (also called the respiratory chain). During a series of redox reactions, electrons travel down the chain releasing their energy in controlled steps. These reactions drive the active transport of H+ ions from the mitochondrial matrix , through the inner membrane to the intermembrane space. The respiratory chain consists of five main types of carrier; flavins, iron-sulfur centres, quinones, cytochromes (heme proteins) and copper. The two main reducing equivalents entering the respiratory chain are NADH and FADH2. NADH is linked through the NADH-specific dehydrogenase whereas FADH2 is reoxidised within succinate dehydrogenase and a ubiquinone reductase of the fatty acid oxidation pathway. Oxygen is the final acceptor of electrons and with H+ ions, is converted to form water, the end product of aerobic cellular respiration. A proton electrochemical gradient (often called protonmotive force) is established across the inner membrane, with positive charge in the intermembrane space relative to the matrix. Protons driven by the proton-motive force, can enter ATP synthase thus returning to the mitochondrial matrix. ATP synthases use this exergonic flow to form ATP in the matrix, a process called chemiosmotic coupling. A by-product of this process is heat generation. An antiport, ATP-ADP translocase, preferentially exports ATP from the matrix thereby maintaining a high ADP:ATP ratio in the matrix. The tight coupling of electron flow to ATP synthesis means oxygen consumption is dependent on ADP availability (termed respiratory control). High ADP (low ATP) increases electron flow thereby increasing oxygen consumption and low ADP (high ATP) decreases electron flow and thereby decreases oxygen consumption. There are many …

UnificationXref6506
type: UnificationXref
id: 3665305
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665305

Evidence616
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: ETF-ubiquinone oxidoreductase (ETF-QO), catalyzes the re-oxidation of reduced ETF, with ubiquinone as the electron acceptor.

UnificationXref6505
type: UnificationXref
id: REACT_158240
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_158240.3

Evidence619
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: The metabolism of pyruvate provides one source of acetyl-CoA which enters the citric acid (TCA, tricarboxylic acid) cycle to generate energy and the reducing equivalent NADH. These reducing equivalents are re-oxidized back to NAD+ in the electron transport chain (ETC), coupling this process with the export of protons across the inner mitochondrial membrane. The chemiosmotic gradient created is used to drive ATP synthesis.

UnificationXref6508
type: UnificationXref
id: 3663484
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3663484

http://identifiers.org/pubmed/16141327
type: PublicationXref
id: 16141327
author: Centeno, F
author: Mora, A
author: Christianson, DW
author: Ochoa, AC
author: Rodriguez, PC
author: Sabio, G
author: Di Costanzo, L
db: Pubmed
title: Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response
source: Proc Natl Acad Sci U S A 102:13058-63
year: 2005

Evidence618
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Oxidation of fatty acids and pyruvate in the mitochondrial matrix yield large amounts of NADH. The respiratory electron transport chain couples the re-oxidation of this NADH to NAD+ to the export of protons from the mitochonrial matrix, generating a chemiosmotic gradient across the inner mitochondrial membrane. This gradient is used to drive the synthesis of ATP; it can also be bypassed by uncoupling proteins to generate heat, a reaction in brown fat that may be important in regulation of body temperature in newborn children.

UnificationXref6507
type: UnificationXref
id: REACT_128053
db: Reactome
id version: 5
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_128053.5

Evidence613
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Pyruvate metabolism and the citric acid (TCA) cycle together link the processes of energy metabolism in a human cell with one another and with key biosynthetic reactions. Pyruvate, derived from the reversible oxidation of lactate or transamination of alanine, can be converted to acetyl CoA. Other sources of acetyl CoA include breakdown of free fatty acids and ketone bodies in the fasting state. Acetyl CoA can enter the citric acid cycle, a major source of reducing equivalents used to synthesize ATP, or enter biosynthetic pathways. In addition to its role in energy generation, the citric acid cycle is a source of carbon skeletons for amino acid metabolism and other biosynthetic processes. One such process included here is the interconversion of 2-hydroxyglutarate, probably derived from porphyrin and amino acid metabolism, and 2-oxoglutarate (alpha-ketoglutarate), a citric acid cycle intermediate.

UnificationXref6502
type: UnificationXref
id: 3662809
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662809

Evidence612
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16601864
xref: http://identifiers.org/pubmed/18772396
xref: http://identifiers.org/pubmed/19935646
comment: The two stereoisomers of 2-hydroxyglutarate are normally converted to 2-oxoglutarate in the mitochondrial matrix, and can then be metabolized by the citric acid cycle. The physiological sources of 2-hydroxyglutarate have not been established although plausible hypotheses are that it is generated by lysine breakdown or as a byproduct of delta-aminolevulinate metabolism. The stereoisomers are oxidized to 2-oxoglutarate in FAD-dependent reactions catalyzed by the enzymes D2HGDH (specific for R(-)-2-hydroxyglutarate) and L2HGDH (specific for S(-)-2-hydroxyglutarate). An inherited deficiency in either enzyme is associated with accumulation of 2-hydroxyglutarate and variable neurological symptoms. R(-)-2-hydroxyglutarate also reacts reversibly with succinate semialdehyde to form 4-hydroxybutyrate and 2-oxoglutarate, catalyzed by ADHFE1. No deficiencies of this enzyme have been found in patients with elevated 2-hydroxyglutarate levels (Struys 2006).

UnificationXref6501
type: UnificationXref
id: REACT_155477
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_155477.3

Evidence615
type: Evidence
evidence code: EvidenceCodeVocabulary1
comment: Electron transfer flavoprotein, ETF, a 63kDa heterodimer composed of alpha and beta subunit, binds one FAD and one AMP per dimer. ETF resides on the matrix face of the mitochondrial inner membrane. Reducing equivalents from the beta-oxidation of fatty acyl CoAs are transferred to ETF, reducing the ETF-bound FAD to FADH2.

UnificationXref6504
type: UnificationXref
id: 3665480
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3665480

Evidence614
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8682198
comment: This event is deduced on the basis of bovine experimental data. Complex II (succinate dehydrogenase) transfers electrons from the TCA cycle to ubiquinone. The 6th step in the TCA cycle is where succinate is dehydrogenated to fumarate with subsequent reduction of FAD to FADH2. FADH2 provides the electrons for the transport chain. Succinate dehydrogenase belongs to subclass 1 of the SQR family (succinate:quinone reductase) (classified by Hagerhall, C and Hederstedt, L [1996]). It consists of 4 subunits (referred to as A, B, C and D), all nuclear-encoded and is located on the matrix side of the inner mitochondrial membrane. Subunits A and B are hydrophilic whereas subunits C and D are integral proteins of the inner membrane. SQRs usually contain 3 Fe-S clusters bound by the B subunit. Succinate dehydrogenase contains one [2Fe-2S] cluster, one [4Fe-4S] cluster and one [3Fe-4S] cluster. Additionally, the A subunit has a covalently-bound FAD group. Reduced complex II has this FAD converted to FADH2. The electrons from complex II are transferred to ubiquinone (also called Q, Coenzyme Q or CoQ), a small mobile carrier of electrons located within the inner membrane. Ubiquinone is reduced to ubiquinol during this process.

UnificationXref6503
type: UnificationXref
id: REACT_160064
db: Reactome
id version: 3
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_160064.3

Evidence611
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3182820
xref: http://identifiers.org/pubmed/16435184
comment: ADHFE1 catalyzes the reversible reaction of 2-oxoglutarate and 4-hydroxybutyrate to form (R)-2-hydroxyglutarate and succinate semialdehyde (Struys et al. 2005). The localization of human ADHFE1 to the mitochondrial matrix is inferred from the location determined experimentally for its rat homolog (Kaufman et al. 1988).

UnificationXref6500
type: UnificationXref
id: 3662813
db: Reactome Database ID Release 45
comment: Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3662813

Evidence610
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/3182820
xref: http://identifiers.org/pubmed/16435184
comment: ADHFE1 catalyzes the reversible reaction of (R)-2-hydroxyglutarate and succinate semialdehyde to form 2-oxoglutarate and 4-hydroxybutyrate (Struys et al. 2005). The localization of human ADHFE1 to the mitochondrial matrix is inferred from the location determined experimentally for its rat homolog (Kaufman et al. 1988).

Stoichiometry287
type: Stoichiometry
physical entity: Protein91
stoichiometric coefficient: 1.0

Stoichiometry288
type: Stoichiometry
physical entity: RNA Polymerase I Holoenzyme (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry289
type: Stoichiometry
physical entity: Protein92
stoichiometric coefficient: 1.0

Stoichiometry283
type: Stoichiometry
physical entity: Protein88
stoichiometric coefficient: 1.0

Stoichiometry284
type: Stoichiometry
physical entity: Protein50
stoichiometric coefficient: 1.0

Stoichiometry285
type: Stoichiometry
physical entity: Protein89
stoichiometric coefficient: 1.0

Stoichiometry286
type: Stoichiometry
physical entity: Protein90
stoichiometric coefficient: 1.0

http://identifiers.org/pubmed/10024882
type: PublicationXref
id: 10024882
author: Tirode, F
author: Coin, F
author: Egly, JM
author: Busso, D
db: Pubmed
title: Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7
source: Mol Cell 3:87-95
year: 1999

Stoichiometry280
type: Stoichiometry
physical entity: RNA polymerase II (phosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry281
type: Stoichiometry
physical entity: RNA Polymerase II (phosphorylated):TFIIF:capped pre-mRNA (name copied from entity in Homo sapiens)
stoichiometric coefficient: 1.0

Stoichiometry282
type: Stoichiometry
physical entity: Protein48
stoichiometric coefficient: 1.0

UnificationXref6509
type: UnificationXref
id: REACT_114392
db: Reactome
id version: 8
comment: Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_114392.8

PLC beta mediated events
type: Pathway
data source: Provenance1
pathway component: REACT 143719.5
evidence: Evidence267
xref: UnificationXref1427
xref: UnificationXref1426
pathway order: PathwayStep264
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

Synthesis of Prostaglandins (PG) and Thromboxanes (TX)
type: Pathway
data source: Provenance1
pathway component: BiochemicalReaction296
evidence: Evidence547
xref: UnificationXref3561
xref: UnificationXref3560
xref: RelationshipXref377
pathway order: PathwayStep538
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
organism: BioSource1

p-ERK dimerizes
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence196
xref: UnificationXref1058
xref: UnificationXref1057
participant stoichiometry: Stoichiometry389
left: Phospho-ERK
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: p-ERK dimer

Evidence608
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/6773467
xref: http://identifiers.org/pubmed/16746585
xref: http://identifiers.org/pubmed/16747180
comment: In the citric acid or tricarboxylic acid (TCA) cycle, the acetyl group of acetyl CoA (derived primarily from oxidative decarboxylation of pyruvate, beta-oxidation of long-chain fatty acids, and catabolism of ketone bodies and several amino acids) can be completely oxidized to CO2 in reactions that also yield one high-energy phosphate bond (as GTP or ATP) and four reducing equivalents (three NADH + H+, and one FADH2). The NADH and FADH2 are then oxidized by the electron transport chain to yield nine more high-energy phosphate bonds (as ATP). All reactions of the citric acid cycle take place in the mitochondrion. Eight canonical reactions mediate the synthesis of citrate from acetyl-CoA and oxaloacetate and the metabolism of citrate to re-form oxaloacetate. Six additional reactions are included here. Three reversible reactions, the interconversions of citrate and isocitrate, of fumarate and malate, and of malate and oxaloacetate are annotated in both their canonical (forward) and reverse directions. The synthesis of succinate from succinyl-CoA can be coupled to the phosphorylation of either GDP (the canonical reaction) or ADP; both reactions are annotated. Two mitochondrial isocitrate dehydrogenase isozymes catalyze the oxidative decarboxylation of isocitrate to form alpha-ketoglutarate (2-oxoglutarate): IDH3 catalyzes the canonical reaction coupled to the reduction of NAD+, while IDH2 catalyzes the same reaction coupled to reduction of NADP+, a reaction whose normal physiological function is unclear. Both reactions are annotated. Finally, a reaction is annotated in which reducing equivalents are transferred from NADPH to NAD+ coupled to proton import across the inner mitochondrial membrane. The cyclical nature of the reactions responsible for the oxidation of acetate was first suggested by Hans Krebs, from biochemical studies of pigeon breast muscle (Krebs et al. 1938; Krebs and Eggleston 1940). Many of the molecular details of individual reactions were worked out by…

PDPK1 binds PIP2
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence188
xref: UnificationXref1040
xref: UnificationXref1039
left: Homologues of PDPK1
left: SmallMolecule20
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: PDPK1:PIP2 (name copied from entity in Homo sapiens)

Evidence607
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/16740313
comment: Mitochondrial malate dehydrogenase catalyzes the reversible reaction of malate and NAD+ to form oxaloacetate and NADH + H+ (Luo et al. 2006). This reaction is highly endergonic but is pulled in the direction annotated here when the TCA cycle is operating. Unpublished crystallographic data indicate that the protein is a dimer (PDB 3E04).

Formation of active mTORC1 complex
type: BiochemicalReaction
data source: Provenance1
evidence: Evidence201
xref: UnificationXref1082
xref: UnificationXref1081
left: Rheb:GTP (name copied from entity in Homo sapiens)
left: O74184
left: Homologues of MTOR
left: P87141
comment: This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
right: Activated mTORC1 (name copied from entity in Homo sapiens)

Evidence606
type: Evidence
evidence code: EvidenceCodeVocabulary1
xref: http://identifiers.org/pubmed/8200987
comment: Mitochondrial fumarate hydratase catalyzes the reversible reaction of malate to form fumarate and water (Bourgeron et al. 1994). Unpublished crystallographic data indicate that the protein is a tetramer (PDB 3E04).