| Function | Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. 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. 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. 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. 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. 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. |
| Protein Name | Glyceraldehyde-3-Phosphate DehydrogenaseGapdhPeptidyl-Cysteine S-Nitrosylase Gapdh |
| Database Links | Reactome: R-HSA-70171Reactome: R-HSA-70263 |
| Cellular Localisation | CytoplasmCytosolNucleusPerinuclear RegionMembraneCytoskeletonTranslocates To The Nucleus Following S-Nitrosylation And Interaction With Siah1Which Contains A Nuclear Localization SignalPostnuclear And Perinuclear Regions |
| Alternative Protein Names | Glyceraldehyde-3-Phosphate Dehydrogenase proteinGapdh proteinPeptidyl-Cysteine S-Nitrosylase Gapdh proteinGAPDH proteinGAPD proteinCDABP0047 proteinOK proteinSW-cl.12 protein |
Information sourced from Uniprot.org
