Anti-BRCC36 antibody

Target data

Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains (PubMed : 19214193, PubMed : 20656690, PubMed : 24075985, PubMed : 26344097). Does not have activity toward 'Lys-48'-linked polyubiquitin chains (PubMed : 19214193, PubMed : 20656690, PubMed : 24075985, PubMed : 26344097). 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) (PubMed : 14636569, PubMed : 16707425, PubMed : 17525341, PubMed : 19202061, PubMed : 19261746, PubMed : 19261748, PubMed : 19261749). 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) (PubMed : 20656690). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates (PubMed : 20656690, PubMed : 24075985, PubMed : 26195665, PubMed : 26344097). 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 (PubMed : 19214193). The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1 (PubMed : 26195665). 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 (PubMed : 24075985, PubMed : 26344097). Acts as a regulator of the NLRP3 inflammasome by mediating deubiquitination of NLRP3, leading to NLRP3 inflammasome assembly (By similarity). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed : 24075985). Deubiquitinates HDAC1 and PWWP2B leading to their stabilization (By similarity).