Description
Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains.
Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the brca1-bard1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the rnf8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating numa1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor ifnar1; deubiquitination increases ifnar1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in ifnar1 deubiquitination.
Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains, leaving the last ubiquitin chain attached to its substrates. Catalytic subunit of the BRISC complex; does not have activity by itself, but needs to be associated into a heterotetramer with ABRAXAS2 for minimal in vitro activity (PubMed:26344097). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (By similarity). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating spindle assembly factors (By similarity).
Subunit
Component of the BRCA1-A complex, at least composed of brca1, bard1, uimc1/rap80, abraxas1, brcc3/brcc36, babam2 and babam1/nba1. In the BRCA1-A complex, interacts directly with ABRAXAS1 and babam2. Component of the BRISC complex, at least composed of ABRAXAS2, brcc3/brcc36, babam2 and babam1/nba1. Within the complex, interacts directly with abraxas2. Both the BRCA1-A complex and the BRISC complex bind polyubiquitin (By similarity).
Component of the BRISC complex, at least composed of ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Within the complex, interacts directly with ABRAXAS2. The heterodimer with ABRAXAS2 assembles into a heterotetramer. The BRISC complex binds polyubiquitin.
Component of the BRCA1-A complex, at least composed of brca1, bard1, uimc1/rap80, abraxas1, brcc3/brcc36, babam2 and babam1/nba1. In the BRCA1-A complex, interacts directly with abraxas1 and babam2. Component of the BRISC complex, at least composed of abraxas2, brcc3/brcc36, babam2 and babam1/nba1. Within the complex, interacts directly with abraxas2. Both the BRCA1-A complex and the BRISC complex bind polyubiquitin (By similarity).
Subcellular location
Nucleus
Localizes at sites of DNA damage at double-strand breaks (DSBs). Interaction with abraxas2 retains brcc3 in the cytoplasm. With evidence from 2 publications.
Cytoplasm
Localizes at sites of DNA damage at double-strand breaks (DSBs). Interaction with abraxas2 retains brcc3 in the cytoplasm. With evidence from 2 publications.
Cytoskeleton
Localizes at sites of DNA damage at double-strand breaks (DSBs). Interaction with abraxas2 retains brcc3 in the cytoplasm. With evidence from 2 publications.
Spindle pole
Localizes at sites of DNA damage at double-strand breaks (DSBs). Interaction with abraxas2 retains brcc3 in the cytoplasm. With evidence from 2 publications.