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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: Phospholipid phosphatase 2

UniprotKB/SwissProt ID: O43688 (O43688)

Gene Name: PLPP2

Organism: Homo sapiens (Human)

Function: Magnesium-independent phospholipid phosphatase that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P (PubMed:16467304, PubMed:9607309, PubMed:9705349). Has no apparent extracellular phosphatase activity and therefore most probably acts intracellularly (PubMed:16467304). Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound (PubMed:9607309). Through dephosphorylation of these bioactive lipid mediators produces new bioactive compounds and may regulate signal transduction in different cellular processes (Probable). Indirectly regulates, for instance, cell cycle G1/S phase transition through its phospholipid phosphatase activity (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Membrane. Cell membrane. Early endosome membrane. Endoplasmic reticulum membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR036938 P_Acid_Pase_2/haloperoxi_sf
IPR000326 P_Acid_Pase_2/haloperoxidase
IPR043216 PA_PP_rel

The S-nitrosylation sites of O43688

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 38 VNAPYKRGFY C GDDSIRYPYR