BAP1 binds BRCA1:BARD1

Stable Identifier
Reaction [binding]
Homo sapiens
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BRCA1-associated protein 1 (BAP1) is a ubiquitin COOH-terminal hydrolase that was initially identified as a protein that binds the RING finger domain of the breast and ovarian tumor suppressor BRCA1. The extreme C-terminal segment of BAP1, which is 38% identical to the C-terminus of UCHL5 (UCH37), is necessary for binding to BRCA1 (Jensen et al. 1998). The N-terminal portion of BAP1 binds BARD1 (Nishikawa et al. 2009). BARD1:BRCA1 constitutes a RING heterodimer E3 ligase. BAP1 binding with BARD1 interferes with BARD1-BRCA association. BAP1 can also deubiquitinate the polyubiquitin chains mediated by BRCA1:BARD1 (Nishikawa et al. 2009).

BAP1 is a tumour suppressor that is believed to mediate its effects through chromatin modulation, transcriptional regulation, and possibly via the ubiquitin-proteasome system and the DNA damage response pathway (Murali et al. 2013).
Literature References
PubMed ID Title Journal Year
9528852 BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression

Marquis, ST, Maul, GG, Borodovsky, A, Minna, J, Chodosh, LA, Rauscher, FJ, Barlev, N, Proctor, M, Schultz, DC, Sekido, Y, Ishov, AM, Vissing, H, Tommerup, N, Berger, SL, Jensen, DE, Ha, SI, Wilkinson, KD, Gardner, HP, Prendergast, GC

Oncogene 1998
Orthologous Events
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