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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: Fructose-bisphosphate aldolase 6, cytosolic

UniprotKB/SwissProt ID: Q9SJQ9 (Q9SJQ9)

Gene Name: FBA6

Organism: Arabidopsis thaliana (Mouse-ear cress)

Function: Fructose-bisphosphate aldolase that plays a key role in glycolysis and gluconeogenesis (PubMed:21782461). Associates with GAPC1 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)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm, cytosol. Nucleus. Mitochondrion

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR029768 Aldolase_I_AS
IPR013785 Aldolase_TIM
IPR000741 FBA_I

The S-nitrosylation sites of Q9SJQ9

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 173 AYGLARYAVI C QENGLVPIVE  CCCHHHHHHH H HHHCCEEECC  21782461