BRCA1-associated protein-1,' or BAP1 interacts with the RING finger domain of BRCA1. The N-terminal 240 amino acids of the predicted 729-amino acid human protein show homology to ubiquitin C-terminal hydrolases (UCHs), thiol proteases that catalyze proteolytic processing of ubiquitin. In addition, BAP1 contains an acidic region, a highly charged C-terminal region, and 2 putative nuclear localization signals. BAP1 and BRCA1 associate in vivo and have overlapping subnuclear localization patterns. BAP1 enhances BRCA1-mediated inhibition of breast cancer cell growth. Northern blot analysis indicates that BAP1 is expressed as a 4-kb mRNA in all human tissues tested, with A 4.8-kb transcript expressed exclusively in testis. Northern blot analysis and in situ hybridization reveal that BAP1 and BRCA1 are coexpressed during murine breast development and remodeling. The BAP1 gene has been mapped to 3p21.3, a region of loss of heterozygosity for breast cancer as well as frequently deleted in lung carcinomas. Intragenic homozygous rearrangements and deletions of BAP1 appear in lung carcinoma cell lines. It has been postulated that BAP1 is a tumor suppressor gene that functions in the BRCA1 growth control pathway.
BRCA1 associated protein-1 (ubiquitin carboxy-terminal hydrolase); BRCA1-associated protein 1; Cerebral protein 6; cerebral protein-13; Ubiquitin C-terminal hydrolase X4; Ubiquitin carboxyl-terminal hydrolase BAP1; UCH-X4