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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: Breakpoint cluster region protein

UniprotKB/SwissProt ID: P11274 (P11274)

Gene Name: BCR

Organism: Homo sapiens (Human)

Function: Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein (GAP) domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulation of the active GTP-bound form (PubMed:17116687, PubMed:1903516, PubMed:7479768). The central Dbl homology (DH) domain functions as guanine nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound form (PubMed:23940119, PubMed:7479768). The amino terminus contains an intrinsic kinase activity (PubMed:1657398). Functions as an important negative regulator of neuronal RAC1 activity (By similarity). Regulates macrophage functions such as CSF1-directed motility and phagocytosis through the modulation of RAC1 activity (PubMed:17116687). Plays a major role as a RHOA GEF in keratinocytes being involved in focal adhesion formation and keratinocyte differentiation (PubMed:23940119)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Postsynaptic density. Cell projection, dendritic spine. Cell projection, axon. Synapse

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR037769 Abr/Bcr
IPR015123 Bcr-Abl_oncoprot_oligo
IPR036481 Bcr-Abl_oncoprot_oligo_sf
IPR000008 C2_dom
IPR035892 C2_domain_sf
IPR035899 DBL_dom_sf
IPR000219 DH_dom
IPR001331 GDS_CDC24_CS
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR008936 Rho_GTPase_activation_prot
IPR000198 RhoGAP_dom

The S-nitrosylation sites of P11274

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 240 PYRGRSSESS C GVDGDYEDAE