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GAPDH - glyceraldehyde-3-phosphate dehydrogenase

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Gene
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Literature

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Expression

Regulation

SNP

Entrez Gene Name: glyceraldehyde-3-phosphate dehydrogenase
Entrez GeneID: Human(2597), Mouse(100043349), Rat(500983)
Synonyms: G3PD, G3PDH, GAPD, GAPDH, Glyceraldehyde-3-phosphate Dehydrogenase, LOC100048438, LOC685186, LOC686275, LOC689689, MGC102544, MGC102546, MGC103190, MGC103191, MGC105239, MGC127711, MGC88685, NUCLEAR URACIL DNA GLYCOSYLASE, OTTMUSG00000014946, RGD1565368

Gene Summary

  • Human (2597): The product of this gene catalyzes an important energy-yielding step in carbohydrate metabolism, the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD). The enzyme exists as a tetramer of identical chains. Many pseudogenes similar to this locus are present in the human genome. [provided by RefSeq, Jan 2009]
Molecular Functions | Biological Process | Cellular Components | Protein Domains | Subcellular Locations | Pathways | Literature References | IPA Extras

Cell Regulation

Regulates:
  • GAPDH
  • STAT1
  • ENPP1
View all 50 in IPA
Regulated by:
  • GAPDH
  • D-glucose
  • cytarabine
View all 109 in IPA
Binds:
  • HTT
  • AR
  • KCNJ11
View all 111 in IPA
Role in cell:
  • apoptosis
  • phosphorylation in
  • gluconeogenesis in
View all 14 in IPA
Disease:
  • Alzheimer's disease
  • Huntington's disease
  • plaque psoriasis
View all 5 in IPA

Biological Process

apoptosis, carbohydrate metabolic process, gluconeogenesis, glucose metabolic process, glycolysis, multicellular organismal development, neuron apoptosis, oxidation-reduction process, peptidyl-cysteine S-trans-nitrosylation, protein stabilization, response to ammonium ion

Cellular Components

cytoplasm, cytosol, membrane, mitochondrion, nucleus, perinuclear region of cytoplasm, soluble fraction

Literature References

  • 16169070Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE. A human protein-protein interaction network: a resource for annotating the proteome.Cell 2005 Sep 23;122(6):957-68
  • 19605696Mookherjee N, Lippert DN, Hamill P, Falsafi R, Nijnik A, Kindrachuk J, Pistolic J, Gardy J, Miri P, Naseer M, Foster LJ, Hancock RE. Intracellular receptor for human host defense peptide LL-37 in monocytes.J Immunol 2009 Aug 15;183(4):2688-96
  • 19451232Lee MN, Ha SH, Kim J, Koh A, Lee CS, Kim JH, Jeon H, Kim DH, Suh PG, Ryu SH. Glycolytic flux signals to mTOR through glyceraldehyde-3-phosphate dehydrogenase-mediated regulation of Rheb.Mol Cell Biol 2009 Jul 01;29(14):3991-4001
View 1065 categorized literature findings and their references in IPA

Molecular Functions

binding, glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity, NAD binding, oxidoreductase activity, peptidyl-cysteine S-nitrosylase activity, protein binding, transferase activity

Pathways

Protein Domains

enzyme, erythrose-4-phosphate dehydrogenase, Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain, Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain, glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), glyceraldehyde-3-phosphate dehydrogenase, type I, protein binding, rossmann fold

Subcellular Locations

cell surface, cellular membrane, clathrin-coated vesicles, Cytoplasm, cytoplasmic fraction, cytosol, cytosolic fraction, detergent resistant lipid raft fraction, endosomes and endoplasmic reticulum fractions, exosomes, membrane fraction, membrane rafts, mitochondria, nuclear fraction, Nucleus, pH resistant lipid raft fraction, Plasma Membrane, polysomes, postsynaptic density (PSD) fractions, soluble fraction, vesicles

IPA Extras