ID A0A2J8RM60_PONAB Unreviewed; 292 AA. AC A0A2J8RM60; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 02-DEC-2020, entry version 12. DE RecName: Full=Lys-63-specific deubiquitinase {ECO:0000256|RuleBase:RU367116}; DE EC=3.4.19.- {ECO:0000256|RuleBase:RU367116}; GN ORFNames=CR201_G0049981 {ECO:0000313|EMBL:PNJ09616.1}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pongo. OX NCBI_TaxID=9601 {ECO:0000313|EMBL:PNJ09616.1, ECO:0000313|Proteomes:UP000236516}; RN [1] {ECO:0000313|EMBL:PNJ09616.1, ECO:0000313|Proteomes:UP000236516} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Susie {ECO:0000313|EMBL:PNJ09616.1}; RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M., RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J., RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M., RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B., RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.; RT "High-resolution comparative analysis of great ape genomes."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Metalloprotease that specifically cleaves 'Lys-63'-linked CC polyubiquitin chains. Component of the BRCA1-A complex, a complex that CC specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and CC H2AX at DNA lesions sites, leading to target the brca1-bard1 CC heterodimer to sites of DNA damage at double-strand breaks (DSBs). CC Catalytic subunit of the BRISC complex, a multiprotein complex that CC specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. CC Mediates the specific 'Lys-63'-specific deubiquitination associated CC with the COP9 signalosome complex (CSN), via the interaction of the CC BRISC complex with the CSN complex. The BRISC complex is required for CC normal mitotic spindle assembly and microtubule attachment to CC kinetochores via its role in deubiquitinating NUMA1. CC {ECO:0000256|RuleBase:RU367116}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU367116}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU367116}; CC -!- SUBUNIT: Component of the BRCA1-A complex. Component of the BRISC CC complex. Both the BRCA1-A complex and the BRISC complex bind CC polyubiquitin. {ECO:0000256|RuleBase:RU367116}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367116}. CC Cytoplasm {ECO:0000256|RuleBase:RU367116}. Cytoplasm, cytoskeleton, CC spindle pole {ECO:0000256|RuleBase:RU367116}. CC -!- SIMILARITY: Belongs to the peptidase M67A family. BRCC36 subfamily. CC {ECO:0000256|ARBA:ARBA00008021, ECO:0000256|RuleBase:RU367116}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PNJ09616.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NDHI03003672; PNJ09616.1; -; Genomic_DNA. DR RefSeq; XP_009233711.1; XM_009235436.1. DR SMR; A0A2J8RM60; -. DR GeneID; 100172840; -. DR CTD; 79184; -. DR OrthoDB; 968461at2759; -. DR Proteomes; UP000236516; Unassembled WGS sequence. DR GO; GO:0070531; C:BRCA1-A complex; IEA:InterPro. DR GO; GO:0070552; C:BRISC complex; IEA:InterPro. DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro. DR GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0070536; P:protein K63-linked deubiquitination; IEA:InterPro. DR CDD; cd08068; MPN_BRCC36; 1. DR InterPro; IPR040749; BRCC36_C. DR InterPro; IPR000555; JAMM/MPN+_dom. DR InterPro; IPR037518; MPN. DR InterPro; IPR033860; MPN_BRCC36. DR Pfam; PF18110; BRCC36_C; 1. DR Pfam; PF01398; JAB; 1. DR SMART; SM00232; JAB_MPN; 1. DR PROSITE; PS50249; MPN; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000256|RuleBase:RU367116}; KW Cell division {ECO:0000256|RuleBase:RU367116}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|RuleBase:RU367116}; KW Cytoskeleton {ECO:0000256|RuleBase:RU367116}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367116}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU367116}; KW Metalloprotease {ECO:0000256|RuleBase:RU367116}; KW Mitosis {ECO:0000256|RuleBase:RU367116}; KW Nucleus {ECO:0000256|RuleBase:RU367116}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU367116}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786, KW ECO:0000256|RuleBase:RU367116}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367116}. FT DOMAIN 12..180 FT /note="MPN" FT /evidence="ECO:0000259|PROSITE:PS50249" FT COILED 260..292 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 292 AA; 33237 MW; 70302DC19999753C CRC64; MAVQVVQAVQ AVHLESDAFL VCLNHALSTE KEEVMGLCIG ELNDDTSRSD SKFAYTGTEM RTVAEKVDAV RIVHIHSVII LRRSDKRKDR VEISPEQLSA ASTEAERLAE LTGRPMRVVG WYHSHPHITV WPSHVDVRTQ AMYQMMDQGF VGLIFSCFIE DKNTKTGRVL YTCFQSIQAQ KSSEYERIEI PIHIVPHVTI GKVCLESAVE LPKILCQEEQ DAYRRIHSLT HLDSVTKIHN GSVFTKNLCS QMSAVSGPLL QWLEDRLEQN QQHLQELQQE KEELMQELSS LE //