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GAPDH  Gene / cDNA Clone

All GAPDH Reagents

HP100003 
MP200537 
RP300644 

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GAPDH Related Area

GAPDH Related Pathways

    GAPDH Summary & Protein Information

    GAPDH Background

    Gene Summary: 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. Two transcript variants encoding different isoforms have been found for this gene.
    General information above from NCBI
    Catalytic activity: D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. {ECO:0000255|PROSITE-ProRule:PRU10009, ECO:0000269|PubMed:3170585}.
    Subunit structure: Homotetramer. 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 (By similarity). Interacts with EIF1AD, USP25, PRKCI and WARS. Component of the GAIT complex. Interacts with FKBP6; leading to inhibit GAPDH catalytic activity. {ECO:0000250, ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:15479637, ECO:0000269|PubMed:15628863, ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16501887, ECO:0000269|PubMed:16510976, ECO:0000269|PubMed:19001379, ECO:0000269|PubMed:20644585}.
    Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:12829261}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12829261}. Membrane {ECO:0000269|PubMed:12829261}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal (By similarity). Postnuclear and Perinuclear regions. {ECO:0000250}.
    Post-translational: S-nitrosylation of Cys-152 leads to interaction with SIAH1, followed by translocation to the nucleus. {ECO:0000250}.; ISGylated. {ECO:0000305|PubMed:16815975}.; Sulfhydration at Cys-152 increases catalytic activity. {ECO:0000250}.
    Sequence similarity: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. {ECO:0000305}.
    General information above from UniProt

    Glyceraldehyde 3-phosphate dehydrogenase (GAPDH or G3PDH) is an enzyme of about 37kDa that is consisdered as a cellular enzyme involved in glycolysis. It catelyzes the sixth step of glycolysis. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a pleiotropic enzyme that is overexpressed in apoptosis and in several human chronic pathologies. Its role as a mediator for cell death has also been highlighted. A recent report suggests that GAPDH may be genetically associated with late-onset of Alzheimer's disease. Besides, deprenyl, which has originally been used as a monoamine oxidase inhibitor for Parkinson's disease, binds to GAPDH and displays neuroprotective actions.

    GAPDH Alternative Name

    G3PD,GAPD,HEL-S-162eP, [homo-sapiens]
    CDABP0047,G3PD,GAPD,MGC88685, [human]
    Gapd,MGC102544,MGC102546,MGC103191,MGC103190,MGC105239, [mouse]
    Gapd, [mus-musculus]

    GAPDH Related Studies

  • Hara MR, et al. (2006) Neuroprotection by pharmacologic blockade of the GAPDH death cascade. PNA. 103 (10): 3887-9.
  • Hara MR, et al. (2006) GAPDH as a sensor of NO stress.Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1762 (5): 502-9.
  • Tarze A, et al. (2007) GAPDH, a novel regulator of the pro-apoptotic mitochondrial membrane permeabilizationGAPDH and apoptosis. Oncogene. 26: 2606-20.
  • Yi MK, et al. (2000) Functional Significance of the Interaction of Hepatitis A Virus RNA with Glyceraldehyde 3-Phosphate Dehydrogenase (GAPDH): Opposing Effects of GAPDH and Polypyrimidine Tract Binding Protein on Internal Ribosome Entry Site Function. Journal of Virology. 74 (14) : 6459-68.
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