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GAPDH - glyceraldehyde-3-phosphate dehydrogenase
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]
Molecular Functions | Biological Process | Cellular Components | Protein Domains | Subcellular Locations | Pathways | Literature References | IPA Extras
Cell Regulation
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
Cellular Components
cytoplasm, cytosol, membrane, mitochondrion, nucleus, perinuclear region of cytoplasm, soluble fraction
Literature References
- 16169070
Stelzl 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 - 19605696
Mookherjee 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 - 19451232
Lee 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
Molecular Functions
binding, catalytic activity, glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity, glyceraldehyde-3-phosphate dehydrogenase activity, NAD binding, oxidoreductase activity, peptidyl-cysteine S-nitrosylase activity, protein binding, transferase activity
Protein Domains
enzyme, erythrose-4-phosphate dehydrogenase, glyceraldehyde 3-phosphate dehydrogenase, Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain, glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), glyceraldehyde-3-phosphate dehydrogenase, type I, protein binding, rossmann fold, Rossmann-fold NAD(P)(+)-binding proteins
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
