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HMDB Protein ID HMDBP00695
Secondary Accession Numbers
  • 5968
  • HMDBP06429
Name Glyceraldehyde-3-phosphate dehydrogenase
  1. GAPDH
  2. Peptidyl-cysteine S-nitrosylase GAPDH
Gene Name GAPDH
Protein Type Unknown
Biological Properties
General Function Involved in glyceraldehyde-3-phosphate dehydrogenase activity
Specific Function Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.
  • Alzheimer's disease
  • Fanconi-bickel syndrome
  • Fructose-1,6-diphosphatase deficiency
  • Gluconeogenesis
  • Glycerol Phosphate Shuttle
  • Glycogen Storage Disease Type 1A (GSD1A) or Von Gierke Disease
  • Glycogenosis, Type IA. Von gierke disease
  • Glycogenosis, Type IB
  • Glycogenosis, Type IC
  • Glycogenosis, Type VII. Tarui disease
  • glycolysis
  • Glycolysis
  • Glycolysis / Gluconeogenesis
  • HIF-1 signaling pathway
  • Mitochondrial Electron Transport Chain
  • Phosphoenolpyruvate carboxykinase deficiency 1 (PEPCK1)
  • Triosephosphate isomerase
  • Warburg Effect
Glyceraldehyde 3-phosphate + Phosphate + NAD → Glyceric acid 1,3-biphosphate + NADH details
Glyceraldehyde 3-phosphate + Phosphate + NAD → Glyceric acid 1,3-biphosphate + NADH + Hydrogen Ion details
GO Classification
Biological Process
small molecule metabolic process
neuron apoptotic process
peptidyl-cysteine S-trans-nitrosylation
protein stabilization
negative regulation of translation
cellular response to interferon-gamma
microtubule cytoskeleton organization
Cellular Component
microtubule cytoskeleton
extracellular vesicular exosome
plasma membrane
perinuclear region of cytoplasm
lipid particle
ribonucleoprotein complex
nucleotide binding
catalytic activity
nad or nadh binding
glyceraldehyde-3-phosphate dehydrogenase activity
oxidoreductase activity
oxidoreductase activity, acting on the aldehyde or oxo group of donors
oxidoreductase activity, acting on the aldehyde or oxo group of donors, nad or nadp as acceptor
Molecular Function
NAD binding
NADP binding
glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
peptidyl-cysteine S-nitrosylase activity
microtubule binding
metabolic process
small molecule metabolic process
alcohol metabolic process
monosaccharide metabolic process
hexose metabolic process
glucose metabolic process
oxidation reduction
Cellular Location
  1. Cytoplasm
  2. Cytoplasm
  3. perinuclear region
  4. Membrane
Gene Properties
Chromosome Location 12
Locus 12p13
Gene Sequence
>1008 bp
Protein Properties
Number of Residues 335
Molecular Weight 31547.76
Theoretical pI 7.604
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Glyceraldehyde-3-phosphate dehydrogenase
GenBank ID Protein 21104392
UniProtKB/Swiss-Prot ID P04406
UniProtKB/Swiss-Prot Entry Name G3P_HUMAN
GenBank Gene ID AB062273
General References
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  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
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  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
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  11. Ye Z, Connor JR: cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs. Biochem Biophys Res Commun. 2000 Aug 18;275(1):223-7. [PubMed:10944468 ]
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