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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic

UniprotKB/SwissProt ID: P25858 (P25858)

Gene Name: GAPC1

Organism: Arabidopsis thaliana (Mouse-ear cress)

Function: 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. Essential for the maintenance of cellular ATP levels and carbohydrate metabolism. Required for full fertility (PubMed:18820081). Involved in response to oxidative stress by mediating plant responses to abscisic acid (ABA) and water deficits through the activation of PLDDELTA and production of phosphatidic acid (PA), a multifunctional stress signaling lipid in plants (PubMed:22589465). Associates with FBA6 to the outer mitochondrial membrane, in a redox-dependent manner, leading to binding and bundling of actin. Actin binding and bundling occurs under oxidizing conditions and is reversible under reducing conditions. May be part of a redox-dependent retrograde signal transduction network for adaptation upon oxidative stress (PubMed:23316205). Binds DNA in vitro. Together with DNA polymerase II subunit B3-1 (DPB3-1) and GAPC2, enhances heat tolerance and promotes the expression of heat-inducible genes (PubMed:32651385)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR020831 GlycerAld/Erythrose_P_DH
IPR020830 GlycerAld_3-P_DH_AS
IPR020829 GlycerAld_3-P_DH_cat
IPR020828 GlycerAld_3-P_DH_NAD(P)-bd
IPR006424 Glyceraldehyde-3-P_DH_1
IPR036291 NAD(P)-bd_dom_sf

The S-nitrosylation sites of P25858

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 156 SDLDIVSNAS C TTNCLAPLAK  CCCCCEEEEC C CCHHHHHHHH 
2 160 IVSNASCTTN C LAPLAKVIND  CCCCCEEEEC C CCHHHHHHHH