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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: Chronophin

UniprotKB/SwissProt ID: Q96GD0 (Q96GD0)

Gene Name: PDXP

Organism: Homo sapiens (Human)

Function: Functions as a pyridoxal phosphate (PLP) phosphatase, which also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), with order of substrate preference PLP > PNP > PMP and therefore plays a role in vitamin B6 metabolism (PubMed:14522954, PubMed:8132548). Also functions as a protein serine phosphatase that specifically dephosphorylates 'Ser-3' in proteins of the actin-depolymerizing factor (ADF)/cofilin family like CFL1 and DSTN. Thereby, regulates cofilin-dependent actin cytoskeleton reorganization, being required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phosphothreonines in LIMK1. Does not dephosphorylate peptides containing phosphotyrosine (PubMed:15580268)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Cell projection, ruffle membrane. Cell projection, lamellipodium membrane. Cell membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR036412 HAD-like_sf
IPR006357 HAD-SF_hydro_IIA
IPR023214 HAD_sf
IPR006349 PGP_euk

The S-nitrosylation sites of Q96GD0

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 250 LETDILFGHR C GMTTVLTLTG    37478858
2 91 RAEQLFSSAL C AARLLRQRLP    37478858