GAPDH Antibody – Rabbit Polyclonal

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. [provided by RefSeq, Feb 2012]

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. Ref.6 Ref.23 Ref.41

Catalytic activity: D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH. Ref.6

Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.

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. Ref.23 Ref.25 Ref.26 Ref.29 Ref.36 Ref.43 Ref.44

Subcellular location: Cytoplasm › cytosol. Nucleus

By similarity. Cytoplasm › perinuclear region. Membrane. Cytoplasm › cytoskeleton

By similarity. Note: Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal

By similarity. Postnuclear and Perinuclear regions. Ref.24

Post-translational modification: S-nitrosylation of Cys-152 leads to interaction with SIAH1, followed by translocation to the nucleus

By similarity.ISGylated

Probable. Ref.30Sulfhydration at Cys-152 increases catalytic activity

By similarity.

Sequence similarities: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.