a protein with serine/threonine protein kinase activity and is a GTPase-activating protein (GAP) for RAC1 and CDC42. The amino-terminal region of Bcr contains an oligomerization domain, a serine/threonine kinase domain and a region that binds SH2 domains. The middle of the protein has a PH domain and a region of sequence similarity to the guanine nucleotide exchange factors for the Rho family of GTP binding proteins. The carboxy-terminal region promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them. A breakpoint cluster region protein that participates in a t(9;22)(q34;q11) chromosomal translocation that produces a BCR-ABL oncogene responsible for chronic myeloid leukemia (CML), acute myeloid leukemia (AML) and acute lymphoblastic leukemia (ALL). The function of wild type Bcr in cells remains unclear. PDGF receptor may use Bcr as a downstream signaling mediator. Tyr177 of human Bcr, phosphorylated in the Bcr-Abl fusion protein, provides a docking site for Gab2 and GRB2, and is important in the transforming activity of Bcr-Abl. Sequence variants of the Bcr protein may be associated with bipolar disorder. Two alternatively spliced isoforms of the human protein have been reported. Note: This description may include information from UniProtKB.
Protein type: Kinase, protein; Oncoprotein; GAPs, Rac/Rho; GEFs, Rac/Rho; Protein kinase, Ser/Thr (non-receptor); GAPs; Protein kinase, atypical; EC 220.127.116.11; ATYPICAL group; BCR family
Molecular Function: ATP binding; enzyme binding; GTPase activator activity; kinase activity; protein binding; protein serine/threonine kinase activity; protein-tyrosine kinase activity; Rho guanyl-nucleotide exchange factor activity
Biological Process: actin cytoskeleton organization and biogenesis; brain development; inner ear morphogenesis; negative regulation of cellular extravasation; negative regulation of inflammatory response; negative regulation of neutrophil degranulation; neuromuscular process controlling balance; peptidyl-tyrosine phosphorylation; platelet-derived growth factor receptor signaling pathway; positive regulation of GTPase activity; positive regulation of phagocytosis; protein amino acid autophosphorylation; protein amino acid phosphorylation; regulation of cell cycle; regulation of Rho protein signal transduction; regulation of small GTPase mediated signal transduction; regulation of vascular permeability; response to lipopolysaccharide; signal transduction
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.