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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: SH3 domain-binding protein 1

UniprotKB/SwissProt ID: P55194 (P55194)

Gene Name: Sh3bp1

Organism: Mus musculus (Mouse)

Function: GTPase activating protein (GAP) which specifically converts GTP-bound Rho-type GTPases including RAC1 and CDC42 in their inactive GDP-bound form (PubMed:7621827). By specifically inactivating RAC1 at the leading edge of migrating cells, it regulates the spatiotemporal organization of cell protrusions which is important for proper cell migration. Also negatively regulates CDC42 in the process of actin remodeling and the formation of epithelial cell junctions. Through its GAP activity toward RAC1 and/or CDC42 plays a specific role in phagocytosis of large particles. Specifically recruited by a PI3 kinase/PI3K-dependent mechanism to sites of large particles engagement, inactivates RAC1 and/or CDC42 allowing the reorganization of the underlying actin cytoskeleton required for engulfment. It also plays a role in angiogenesis and the process of repulsive guidance as part of a semaphorin-plexin signaling pathway. Following the binding of PLXND1 to extracellular SEMA3E it dissociates from PLXND1 and inactivates RAC1, inducing the intracellular reorganization of the actin cytoskeleton and the collapse of cells (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cell projection. Cell junction, tight junction. Cell junction, adherens junction. Cell projection, phagocytic cup. Nucleus. Cytoplasm, cytosol

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR027267 AH/BAR_dom_sf
IPR004148 BAR_dom
IPR047165 RHG17/44/SH3BP1-like
IPR008936 Rho_GTPase_activation_prot
IPR000198 RhoGAP_dom

The S-nitrosylation sites of P55194

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 102 SSMGKALEMT C AIQNQLARIL