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Showing Protein Glyceraldehyde-3-phosphate dehydrogenase (HMDBP13199)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 0 metabolites
Identification
HMDB Protein ID HMDBP13199
Secondary Accession Numbers None
Name Glyceraldehyde-3-phosphate dehydrogenase
Synonyms
  1. GAPDH
  2. 38 kDa BFA-dependent ADP-ribosylation substrate
  3. BARS-38
  4. Peptidyl-cysteine S-nitrosylase GAPDH
Gene Name GAPDH
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:17934141, PubMed:15951807, PubMed:20972425). 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 (PubMed:17934141). 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 (PubMed:15312048). 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 (By similarity). Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis (PubMed:10424669, PubMed:15951807, PubMed:20972425). Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (PubMed:15951807, PubMed:20972425).
Pathways
  • Alzheimer disease
  • Biosynthesis of amino acids
  • Carbon metabolism
  • Diabetic cardiomyopathy
  • glycolysis
  • Glycolysis / Gluconeogenesis
  • HIF-1 signaling pathway
  • Salmonella infection
Reactions Not Available
GO Classification
Biological Process
multicellular organismal development
cAMP-mediated signaling
female pregnancy
apoptotic process
neuron apoptotic process
peptidyl-cysteine S-trans-nitrosylation
protein stabilization
glycolysis
positive regulation of cytokine production
negative regulation of translation
negative regulation of endopeptidase activity
gluconeogenesis
antimicrobial humoral immune response mediated by antimicrobial peptide
killing of cells of other organism
killing by host of symbiont cells
negative regulation of vascular associated smooth muscle cell apoptotic process
response to ammonium ion
carbohydrate metabolic process
cellular response to interferon-gamma
microtubule cytoskeleton organization
defense response to fungus
Cellular Component
cytosol
microtubule cytoskeleton
cytoplasm
plasma membrane
nucleus
ribonucleoprotein complex
glutamatergic synapse
lipid particle
GAIT complex
postsynaptic density, intracellular component
Molecular Function
NAD binding
NADP binding
glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
peptidyl-cysteine S-nitrosylase activity
disordered domain specific binding
microtubule binding
enzyme binding
aspartic-type endopeptidase inhibitor activity
identical protein binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 333
Molecular Weight 35827.75
Theoretical pI 8.031
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P04797
UniProtKB/Swiss-Prot Entry Name G3P_RAT
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Tso JY, Sun XH, Kao TH, Reece KS, Wu R: Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic complexity and molecular evolution of the gene. Nucleic Acids Res. 1985 Apr 11;13(7):2485-502. [PubMed:2987855 ]
  3. Fort P, Marty L, Piechaczyk M, el Sabrouty S, Dani C, Jeanteur P, Blanchard JM: Various rat adult tissues express only one major mRNA species from the glyceraldehyde-3-phosphate-dehydrogenase multigenic family. Nucleic Acids Res. 1985 Mar 11;13(5):1431-42. doi: 10.1093/nar/13.5.1431. [PubMed:2987824 ]
  4. Tajima H, Tsuchiya K, Yamada M, Kondo K, Katsube N, Ishitani R: Over-expression of GAPDH induces apoptosis in COS-7 cells transfected with cloned GAPDH cDNAs. Neuroreport. 1999 Jul 13;10(10):2029-33. doi: 10.1097/00001756-199907130-00007. [PubMed:10424669 ]
  5. Leung TK, Hall C, Monfries C, Lim L: Trifluoperazine activates and releases latent ATP-generating enzymes associated with the synaptic plasma membrane. J Neurochem. 1987 Jul;49(1):232-8. doi: 10.1111/j.1471-4159.1987.tb03420.x. [PubMed:3585333 ]
  6. Piechaczyk M, Blanchard JM, Marty L, Dani C, Panabieres F, El Sabouty S, Fort P, Jeanteur P: Post-transcriptional regulation of glyceraldehyde-3-phosphate-dehydrogenase gene expression in rat tissues. Nucleic Acids Res. 1984 Sep 25;12(18):6951-63. doi: 10.1093/nar/12.18.6951. [PubMed:6548307 ]
  7. Maehara Y, Fujiyoshi T, Takahashi K, Yamamoto M, Endo H: 1.5 kb mRNA abundantly expressed in rat tumors encodes a 37 kilodalton protein in vitro. Biochem Biophys Res Commun. 1985 Sep 16;131(2):800-5. doi: 10.1016/0006-291x(85)91310-5. [PubMed:2413848 ]
  8. Molina y Vedia L, McDonald B, Reep B, Brune B, Di Silvio M, Billiar TR, Lapetina EG: Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase inhibits enzymatic activity and increases endogenous ADP-ribosylation. J Biol Chem. 1992 Dec 15;267(35):24929-32. [PubMed:1281150 ]
  9. Mohr S, Stamler JS, Brune B: Posttranslational modification of glyceraldehyde-3-phosphate dehydrogenase by S-nitrosylation and subsequent NADH attachment. J Biol Chem. 1996 Feb 23;271(8):4209-14. doi: 10.1074/jbc.271.8.4209. [PubMed:8626764 ]
  10. Andrade J, Pearce ST, Zhao H, Barroso M: Interactions among p22, glyceraldehyde-3-phosphate dehydrogenase and microtubules. Biochem J. 2004 Dec 1;384(Pt 2):327-36. doi: 10.1042/BJ20040622. [PubMed:15312048 ]
  11. Hara MR, Agrawal N, Kim SF, Cascio MB, Fujimuro M, Ozeki Y, Takahashi M, Cheah JH, Tankou SK, Hester LD, Ferris CD, Hayward SD, Snyder SH, Sawa A: S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding. Nat Cell Biol. 2005 Jul;7(7):665-74. doi: 10.1038/ncb1268. Epub 2005 Jun 12. [PubMed:15951807 ]
  12. Sen N, Hara MR, Ahmad AS, Cascio MB, Kamiya A, Ehmsen JT, Agrawal N, Hester L, Dore S, Snyder SH, Sawa A: GOSPEL: a neuroprotective protein that binds to GAPDH upon S-nitrosylation. Neuron. 2009 Jul 16;63(1):81-91. doi: 10.1016/j.neuron.2009.05.024. [PubMed:19607794 ]
  13. Kornberg MD, Sen N, Hara MR, Juluri KR, Nguyen JV, Snowman AM, Law L, Hester LD, Snyder SH: GAPDH mediates nitrosylation of nuclear proteins. Nat Cell Biol. 2010 Nov;12(11):1094-100. doi: 10.1038/ncb2114. Epub 2010 Oct 24. [PubMed:20972425 ]