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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: Myotubularin-related protein 9

UniprotKB/SwissProt ID: Q96QG7 (Q96QG7)

Gene Name: MTMR9

Organism: Homo sapiens (Human)

Function: Acts as an adapter for myotubularin-related phosphatases (PubMed:19038970, PubMed:22647598). Increases lipid phosphatase MTMR6 catalytic activity, specifically towards phosphatidylinositol 3,5-bisphosphate and MTMR6 binding affinity for phosphorylated phosphatidylinositols (PubMed:19038970, PubMed:22647598). Positively regulates lipid phosphatase MTMR7 catalytic activity (By similarity). Increases MTMR8 catalytic activity towards phosphatidylinositol 3-phosphate (PubMed:22647598). The formation of the MTMR6-MTMR9 complex, stabilizes both MTMR6 and MTMR9 protein levels (PubMed:19038970). Stabilizes MTMR8 protein levels (PubMed:22647598). Plays a role in the late stages of macropinocytosis possibly by regulating MTMR6-mediated dephosphorylation of phosphatidylinositol 3-phosphate in membrane ruffles (PubMed:24591580). Negatively regulates autophagy, in part via its association with MTMR8 (PubMed:22647598). Negatively regulates DNA damage-induced apoptosis, in part via its association with MTMR6 (PubMed:19038970, PubMed:22647598). Does not bind mono-, di- and tri-phosphorylated phosphatidylinositols, phosphatidic acid and phosphatidylserine (PubMed:19038970)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Cell projection, ruffle membrane. Cytoplasm, perinuclear region. Endoplasmic reticulum

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR030564 Myotubularin
IPR010569 Myotubularin-like_Pase_dom
IPR011993 PH-like_dom_sf
IPR029021 Prot-tyrosine_phosphatase-like

The S-nitrosylation sites of Q96QG7

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 386 FQQRCAQSAY C NTKQKWEAPV