UniProtKB - P00355 (G3P_PIG)
Glyceraldehyde-3-phosphate dehydrogenase
GAPDH
Functioni
Catalytic activityi
- D-glyceraldehyde 3-phosphate + NAD+ + phosphate = (2R)-3-phospho-glyceroyl phosphate + H+ + NADHPROSITE-ProRule annotationEC:1.2.1.12PROSITE-ProRule annotation
Activity regulationi
: glycolysis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.Proteins known to be involved in the 5 steps of the subpathway in this organism are:
- Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (GAPDHS), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
- Phosphoglycerate kinase (PGK1), Phosphoglycerate kinase, Phosphoglycerate kinase 2 (PGK2), Phosphoglycerate kinase (PGK2), Phosphoglycerate kinase (PGK2), Phosphoglycerate kinase, Phosphoglycerate kinase (PGK1), Phosphoglycerate kinase 1 (PGK1), Phosphoglycerate kinase (PGK2), Phosphoglycerate kinase (PGK1), Phosphoglycerate kinase (PGK1), Phosphoglycerate kinase (PGK1), Phosphoglycerate kinase (PGK2), Phosphoglycerate kinase, Phosphoglycerate kinase (PGK1)
- no protein annotated in this organism
- 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase (ENO4), Beta-enolase (ENO3), 2-phospho-D-glycerate hydro-lyase (ENO3), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase (ENO3), 2-phospho-D-glycerate hydro-lyase (ENO1), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase (ENO3), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase (ENO2), 2-phospho-D-glycerate hydro-lyase (ENO3), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase (ENO2), 2-phospho-D-glycerate hydro-lyase (ENO4), 2-phospho-D-glycerate hydro-lyase (ENO3), 2-phospho-D-glycerate hydro-lyase (ENO3), 2-phospho-D-glycerate hydro-lyase (ENO3), 2-phospho-D-glycerate hydro-lyase (ENO1), 2-phospho-D-glycerate hydro-lyase (ENO1), 2-phospho-D-glycerate hydro-lyase (ENO1), 2-phospho-D-glycerate hydro-lyase (ENO2), 2-phospho-D-glycerate hydro-lyase (ENO4), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase (ENO4), 2-phospho-D-glycerate hydro-lyase (ENO4), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase (ENO4), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase
- Pyruvate kinase (PKLR), Pyruvate kinase (PKM), Multifunctional fusion protein (PKM), Multifunctional fusion protein (PKM), Multifunctional fusion protein (PKM), Pyruvate kinase, Multifunctional fusion protein (PKM), Pyruvate kinase (PKLR), Pyruvate kinase, Multifunctional fusion protein (PKM), Pyruvate kinase, Multifunctional fusion protein (PKM), Pyruvate kinase (PKLR), Multifunctional fusion protein (PKM), Pyruvate kinase (PKM), Pyruvate kinase (PKM), Pyruvate kinase (PKLR), Multifunctional fusion protein (PKM), Pyruvate kinase, Pyruvate kinase (PKM), Pyruvate kinase (PKM), Pyruvate kinase, Multifunctional fusion protein (PKM), Multifunctional fusion protein (PKM)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 33 | NADBy similarity | 1 | |
Binding sitei | 78 | NAD; via carbonyl oxygenBy similarity | 1 | |
Binding sitei | 120 | NADBy similarity | 1 | |
Active sitei | 150 | NucleophilePROSITE-ProRule annotation | 1 | |
Sitei | 177 | Activates thiol group during catalysisBy similarity | 1 | |
Binding sitei | 180 | Glyceraldehyde 3-phosphateBy similarity | 1 | |
Binding sitei | 232 | Glyceraldehyde 3-phosphateBy similarity | 1 | |
Binding sitei | 314 | NADBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 11 – 12 | NADBy similarity | 2 |
GO - Molecular functioni
- glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: UniProtKB
- microtubule binding Source: UniProtKB
- NAD binding Source: InterPro
- NADP binding Source: InterPro
- peptidyl-cysteine S-nitrosylase activity Source: UniProtKB
GO - Biological processi
- glucose metabolic process Source: InterPro
- glycolytic process Source: GO_Central
- microtubule cytoskeleton organization Source: UniProtKB
- neuron apoptotic process Source: UniProtKB
- peptidyl-cysteine S-trans-nitrosylation Source: UniProtKB
- protein stabilization Source: UniProtKB
- regulation of translation Source: UniProtKB-KW
Keywordsi
Molecular function | Oxidoreductase, Transferase |
Biological process | Apoptosis, Glycolysis, Translation regulation |
Ligand | NAD |
Enzyme and pathway databases
UniPathwayi | UPA00109;UER00184 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:GAPDH Synonyms:GAPD |
Organismi | Sus scrofa (Pig) |
Taxonomic identifieri | 9823 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Suina › Suidae › Sus |
Proteomesi |
|
Subcellular locationi
Cytosol
- cytosol By similarity
Cytoskeleton
- cytoskeleton By similarity
Nucleus
- Nucleus By similarity
Note: Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal.By similarity
Cytoskeleton
- microtubule cytoskeleton Source: UniProtKB
Cytosol
- cytosol Source: UniProtKB
Nucleus
- nucleus Source: UniProtKB
Other locations
- cytoplasm Source: UniProtKB
- GAIT complex Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, Cytoskeleton, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000145491 | 2 – 333 | Glyceraldehyde-3-phosphate dehydrogenaseAdd BLAST | 332 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 3 | N6,N6-dimethyllysineBy similarity | 1 | |
Modified residuei | 7 | Deamidated asparagineBy similarity | 1 | |
Modified residuei | 40 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 59 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 62 | Deamidated asparagineBy similarity | 1 | |
Modified residuei | 64 | N6,N6-dimethyllysineBy similarity | 1 | |
Modified residuei | 68 | Deamidated asparagineBy similarity | 1 | |
Modified residuei | 73 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 120 | PhosphoserineBy similarity | 1 | |
Modified residuei | 146 | PhosphoserineBy similarity | 1 | |
Modified residuei | 147 | Deamidated asparagineBy similarity | 1 | |
Modified residuei | 149 | PhosphoserineBy similarity | 1 | |
Modified residuei | 150 | ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited formBy similarity | 1 | |
Modified residuei | 150 | Cysteine persulfideBy similarity | 1 | |
Modified residuei | 150 | S-(2-succinyl)cysteineBy similarity | 1 | |
Modified residuei | 150 | S-nitrosocysteine; in reversibly inhibited formBy similarity | 1 | |
Modified residuei | 151 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 153 | Deamidated asparagineBy similarity | 1 | |
Modified residuei | 175 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 180 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 182 | PhosphothreonineBy similarity | 1 | |
Cross-linki | 184 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 192 | N6,N6-dimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 192 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 192 | N6-malonyllysine; alternateBy similarity | 1 | |
Modified residuei | 209 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 213 | N6,N6-dimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 213 | N6-malonyllysine; alternateBy similarity | 1 | |
Modified residuei | 217 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 223 | Deamidated asparagineBy similarity | 1 | |
Modified residuei | 225 | N6,N6-dimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 225 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 227 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 235 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 239 | PhosphoserineBy similarity | 1 | |
Modified residuei | 245 | S-(2-succinyl)cysteineBy similarity | 1 | |
Modified residuei | 245 | S-nitrosocysteineBy similarity | 1 | |
Modified residuei | 252 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 258 | N6,N6-dimethyllysineBy similarity | 1 | |
Modified residuei | 261 | N6,N6-dimethyllysineBy similarity | 1 | |
Modified residuei | 310 | PhosphoserineBy similarity | 1 | |
Modified residuei | 314 | Deamidated asparagineBy similarity | 1 | |
Modified residuei | 331 | PhosphoserineBy similarity | 1 | |
Modified residuei | 332 | N6,N6-dimethyllysineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, ADP-ribosylation, Isopeptide bond, Methylation, Phosphoprotein, S-nitrosylation, Ubl conjugationProteomic databases
PaxDbi | P00355 |
PeptideAtlasi | P00355 |
PRIDEi | P00355 |
Interactioni
Subunit structurei
Homotetramer.
Interacts with EIF1AD, USP25, PRKCI and WARS1.
Interacts with TPPP; the interaction is direct.
Interacts (when S-nitrosylated) with SIAH1; leading to nuclear translocation.
Interacts with RILPL1/GOSPEL, leading to prevent the interaction between GAPDH and SIAH1 and prevent nuclear translocation.
Interacts with CHP1; the interaction increases the binding of CHP1 with microtubules. Associates with microtubules.
Interacts with phosphorylated RPL13A (By similarity).
Component of the GAIT complex.
Interacts with FKBP6; leading to inhibit GAPDH catalytic activity (By similarity).
By similarityGO - Molecular functioni
- microtubule binding Source: UniProtKB
Protein-protein interaction databases
IntActi | P00355, 1 interactor |
STRINGi | 9823.ENSSSCP00000000740 |
Structurei
Secondary structure
3D structure databases
SMRi | P00355 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2 – 146 | Interaction with WARS1By similarityAdd BLAST | 145 | |
Regioni | 149 – 151 | Glyceraldehyde 3-phosphate bindingBy similarity | 3 | |
Regioni | 209 – 210 | Glyceraldehyde 3-phosphate bindingBy similarity | 2 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 243 – 248 | [IL]-x-C-x-x-[DE] motifBy similarity | 6 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0657, Eukaryota |
InParanoidi | P00355 |
OMAi | HETYKGE |
Family and domain databases
InterProi | View protein in InterPro IPR020831, GlycerAld/Erythrose_P_DH IPR020830, GlycerAld_3-P_DH_AS IPR020829, GlycerAld_3-P_DH_cat IPR020828, GlycerAld_3-P_DH_NAD(P)-bd IPR006424, Glyceraldehyde-3-P_DH_1 IPR036291, NAD(P)-bd_dom_sf |
PANTHERi | PTHR10836, PTHR10836, 1 hit |
Pfami | View protein in Pfam PF02800, Gp_dh_C, 1 hit PF00044, Gp_dh_N, 1 hit |
PIRSFi | PIRSF000149, GAP_DH, 1 hit |
PRINTSi | PR00078, G3PDHDRGNASE |
SMARTi | View protein in SMART SM00846, Gp_dh_N, 1 hit |
SUPFAMi | SSF51735, SSF51735, 1 hit |
TIGRFAMsi | TIGR01534, GAPDH-I, 1 hit |
PROSITEi | View protein in PROSITE PS00071, GAPDH, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MVKVGVNGFG RIGRLVTRAA FNSGKVDIVA INDPFIDLHY MVYMFQYDST
60 70 80 90 100
HGKFHGTVKA ENGKLVINGK AITIFQERDP ANIKWGDAGA TYVVESTGVF
110 120 130 140 150
TTMEKAGAHL KGGAKRVIIS APSADAPMFV MGVNHEKYDN SLKIVSNASC
160 170 180 190 200
TTNCLAPLAK VIHDHFGIVE GLMTTVHAIT ATQKTVDGPS GKLWRDGRGA
210 220 230 240 250
AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV VDLTCRLEKP
260 270 280 290 300
AKYDDIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSDTHS STFDAGAGIA
310 320 330
LNDHFVKLIS WYDNEFGYSN RVVDLMVHMA SKE
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 7 | N → D AA sequence (PubMed:4299800).Curated | 1 | |
Sequence conflicti | 62 | N → D AA sequence (PubMed:4299800).Curated | 1 | |
Sequence conflicti | 68 | N → D AA sequence (PubMed:4299800).Curated | 1 | |
Sequence conflicti | 70 – 71 | KA → NP in AAB94053 (Ref. 1) Curated | 2 | |
Sequence conflicti | 82 | N → K in AAB94053 (Ref. 1) Curated | 1 | |
Sequence conflicti | 90 – 91 | AT → TA AA sequence (PubMed:4299800).Curated | 2 | |
Sequence conflicti | 91 | T → E in AAB94053 (Ref. 1) Curated | 1 | |
Sequence conflicti | 133 | V → M in AAB94053 (Ref. 1) Curated | 1 | |
Sequence conflicti | 145 | V → I in AAB94053 (Ref. 1) Curated | 1 | |
Sequence conflicti | 165 | H → N in AAB94053 (Ref. 1) Curated | 1 | |
Sequence conflicti | 201 | A → L in AAB94053 (Ref. 1) Curated | 1 | |
Sequence conflicti | 223 | N → D AA sequence (PubMed:4299800).Curated | 1 | |
Sequence conflicti | 236 | P → A in AAB94053 (Ref. 1) Curated | 1 | |
Sequence conflicti | 277 | D → H in AAB94053 (Ref. 1) Curated | 1 | |
Sequence conflicti | 282 | C → S in AAB94053 (Ref. 1) Curated | 1 | |
Sequence conflicti | 286 – 287 | SD → DS AA sequence (PubMed:4299800).Curated | 2 | |
Sequence conflicti | 311 | W → S in AAB94053 (Ref. 1) Curated | 1 | |
Sequence conflicti | 321 | R → W in AAB40155 (PubMed:9241041).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF017079 mRNA Translation: AAB94053.1 Z84063 mRNA Translation: CAB06323.1 U48832 mRNA Translation: AAA91804.1 U82261 mRNA Translation: AAB40155.1 X94251 mRNA Translation: CAA63935.1 |
PIRi | B12055 |
RefSeqi | NP_001193288.1, NM_001206359.1 |
Genome annotation databases
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF017079 mRNA Translation: AAB94053.1 Z84063 mRNA Translation: CAB06323.1 U48832 mRNA Translation: AAA91804.1 U82261 mRNA Translation: AAB40155.1 X94251 mRNA Translation: CAA63935.1 |
PIRi | B12055 |
RefSeqi | NP_001193288.1, NM_001206359.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
5DDI | X-ray | 2.40 | P/R/S | 2-333 | [»] | |
5TSO | X-ray | 1.90 | P/R/S | 1-333 | [»] | |
SMRi | P00355 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P00355, 1 interactor |
STRINGi | 9823.ENSSSCP00000000740 |
Protein family/group databases
Allergomei | 12129, Sus s GAPDH |
Proteomic databases
PaxDbi | P00355 |
PeptideAtlasi | P00355 |
PRIDEi | P00355 |
Genome annotation databases
Organism-specific databases
CTDi | 2597 |
Phylogenomic databases
eggNOGi | KOG0657, Eukaryota |
InParanoidi | P00355 |
OMAi | HETYKGE |
Enzyme and pathway databases
UniPathwayi | UPA00109;UER00184 |
Gene expression databases
ExpressionAtlasi | P00355, baseline and differential |
Family and domain databases
InterProi | View protein in InterPro IPR020831, GlycerAld/Erythrose_P_DH IPR020830, GlycerAld_3-P_DH_AS IPR020829, GlycerAld_3-P_DH_cat IPR020828, GlycerAld_3-P_DH_NAD(P)-bd IPR006424, Glyceraldehyde-3-P_DH_1 IPR036291, NAD(P)-bd_dom_sf |
PANTHERi | PTHR10836, PTHR10836, 1 hit |
Pfami | View protein in Pfam PF02800, Gp_dh_C, 1 hit PF00044, Gp_dh_N, 1 hit |
PIRSFi | PIRSF000149, GAP_DH, 1 hit |
PRINTSi | PR00078, G3PDHDRGNASE |
SMARTi | View protein in SMART SM00846, Gp_dh_N, 1 hit |
SUPFAMi | SSF51735, SSF51735, 1 hit |
TIGRFAMsi | TIGR01534, GAPDH-I, 1 hit |
PROSITEi | View protein in PROSITE PS00071, GAPDH, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | G3P_PIG | |
Accessioni | P00355Primary (citable) accession number: P00355 Secondary accession number(s): O18816 Q29546 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | January 23, 2007 | |
Last modified: | December 2, 2020 | |
This is version 162 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families