Lys-63-specific deubiquitinase BRCC36 (EC 3.4.19.-) (BRCA1-A complex subunit BRCC36) (BRCA1/BRCA2-containing complex subunit 3) (BRCA1/BRCA2-containing complex subunit 36) (BRISC complex subunit BRCC36)
1_MAVQV 6_ VQAVQ 11_ AVHLE 16_ SDAFL 21_ VCLNH 26_ ALSTE 31_ KEEVM 36_ GLCIG 41_ ELNDD 46_ TRSDS 51_ KFAYT 56_ GTEMR 61_ TVAEK 66_ VDAVR 71_ IVHIH 76_ SVIIL 81_ RRSDK 86_ RKDRV 91_ EISPE 96_ QLSAA 101_ STEAE 106_ RLAEL 111_ TGRPM 116_ RVVGW 121_ YHSHP 126_ HITVW 131_ PSHVD 136_ VRTQA 141_ MYQMM 146_ DQGFV 151_ GLIFS 156_ CFIED 161_ KNTKT 166_ GRVLY 171_ TCFQS 176_ IQAQK 181_ SSESL 186_ HGPRD 191_ FWSSS 196_ QHISI 201_ EGQKE 206_ EERYE 211_ RIEIP 216_ IHIVP 221_ HVTIG 226_ KVCLE 231_ SAVEL 236_ PKILC 241_ QEEQD 246_ AYRRI 251_ HSLTH 256_ LDSVT 261_ KIHNG 266_ SVFTK 271_ NLCSQ 276_ MSAVS 281_ GPLLQ 286_ WLEDR 291_ LEQNQ 296_ QHLQE 301_ LQQEK 306_ EELMQ 311_ELSSL
1: 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)