Human Gene BCR (uc002zww.3) Description and Page Index
Description: Homo sapiens breakpoint cluster region (BCR), transcript variant 1, mRNA. RefSeq Summary (NM_004327): A reciprocal translocation between chromosomes 22 and 9 produces the Philadelphia chromosome, which is often found in patients with chronic myelogenous leukemia. The chromosome 22 breakpoint for this translocation is located within the BCR gene. The translocation produces a fusion protein which is encoded by sequence from both BCR and ABL, the gene at the chromosome 9 breakpoint. Although the BCR-ABL fusion protein has been extensively studied, the function of the normal BCR gene product is not clear. The protein has serine/threonine kinase activity and is a GTPase-activating protein for p21rac. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]. Transcript (Including UTRs) Position: hg19 chr22:23,522,552-23,660,224 Size: 137,673 Total Exon Count: 23 Strand: + Coding Region Position: hg19 chr22:23,523,148-23,657,709 Size: 134,562 Coding Exon Count: 23
ID:BCR_HUMAN DESCRIPTION: RecName: Full=Breakpoint cluster region protein; EC=188.8.131.52; AltName: Full=Renal carcinoma antigen NY-REN-26; FUNCTION: GTPase-activating protein for RAC1 and CDC42. Promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them. Displays serine/threonine kinase activity. CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. SUBUNIT: Homotetramer. Interacts with PDZK1. May interact with CCPG1 (By similarity). Interacts with FES/FPS, ABL1, PIK3R1 and GRB2. Interacts with HCK. INTERACTION: Q9H2K2:TNKS2; NbExp=3; IntAct=EBI-712838, EBI-4398527; DOMAIN: The region involved in binding to ABL1 SH2-domain is rich in serine residues and needs to be Ser/Thr phosphorylated prior to SH2 binding. This region is essential for the activation of the ABL1 tyrosine kinase and transforming potential of the chimeric BCR-ABL oncogene. DOMAIN: The DH domain is involved in interaction with CCPG1 (By similarity). PTM: Autophosphorylated. Phosphorylated by FES/FPS on tyrosine residues, leading to down-regulation of the BCR kinase activity. Phosphorylation at Tyr-177 by HCK is important for interaction with GRB2. DISEASE: Note=A chromosomal aberration involving BCR is a cause of chronic myeloid leukemia. Translocation t(9;22)(q34;q11) with ABL1. The translocation produces a BCR-ABL found also in acute myeloid leukemia (AML) and acute lymphoblastic leukemia (ALL). SIMILARITY: Contains 1 C2 domain. SIMILARITY: Contains 1 DH (DBL-homology) domain. SIMILARITY: Contains 1 PH domain. SIMILARITY: Contains 1 Rho-GAP domain. SEQUENCE CAUTION: Sequence=BAE06073.1; Type=Erroneous initiation; WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/BCR.html";
Genetic Association Studies of Complex Diseases and Disorders
Blood Vessels Ramachandran S Vasan et al. BMC medical genetics 2007, Genome-wide association of echocardiographic dimensions, brachial artery endothelial function and treadmill exercise responses in the Framingham Heart Study., BMC medical genetics.
In hypothesis-generating GWAS of echocardiography, ETT and BA vascular function in a moderate-sized community-based sample, we identified several SNPs that are candidates for replication attempts and we provide a web-based GWAS resource for the research community.
Body Height Daniel F Gudbjartsson et al. Nature genetics 2008, Many sequence variants affecting diversity of adult human height., Nature genetics.
depressive disorder, major; bipolar disorder Hashimoto, R. et al. 2005, The Breakpoint Cluster Region Gene on Chromosome 22q11 is Associated with Bipolar Disorder, Biological psychiatry. 2005 May;57(10):1097-102.
Our results suggest that genetic variations in the BCR gene could confer susceptibility to bipolar disorder and major depressive disorder.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P11274
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.