BRISC and BRCA1-A complex member 2 (BRCA1-A complex subunit BRE) (BRCA1/BRCA2-containing complex subunit 45) (Brain and reproductive organ-expressed protein)
1_MSPEV 6_ ALNRI 11_ SPMLS 16_ PFISS 21_ VVRNG 26_ KVGLD 31_ ATNCL 36_ RITDL 41_ KSGCT 46_ SLTPG 51_ PNCDR 56_ FKLHI 61_ PYAGE 66_ TLKWD 71_ IIFNA 76_ QYPEL 81_ PPDFI 86_ FGEDA 91_ EFLPD 96_ PSALQ 101_ NLASW 106_ NPSNP 111_ ECLLL 116_ VVKEL 121_ VQQYH 126_ QFQCS 131_ RLRES 136_ SRLMF 141_ EYQTL 146_ LEEPQ 151_ YGENM 156_ EIYAG 161_ KKNNW 166_ TGEFS 171_ ARFLL 176_ KLPVD 181_ FSNIP 186_ TYLLK 191_ DVNED 196_ PGEDV 201_ ALLSV 206_ SFEDT 211_ EATQV 216_ YPKLY 221_ LSPRI 226_ EHALG 231_ GSSAL 236_ HIPAF 241_ PGGGC 246_ LIDYV 251_ PQVCH 256_ LLTNK 261_ VQYVI 266_ QGYHK 271_ RREYI 276_ AAFLS 281_ HFGTG 286_ VVEYD 291_ AEGFT 296_ KLTLL 301_ LMWKD 306_ FCFLV 311_ HIDLP 316_ LFFPR 321_ DQPTL 326_ TFQSV 331_ YHFTN 336_ SGQLY 341_ SQAQK 346_ NYPYS 351_ PRWDG 356_ NEMAK 361_ RAKAY 366_ FKTFV 371_ PQFQE 376_AAFAN
1: 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). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX (PubMed:17525341, PubMed:19261746, PubMed:19261748, PubMed:19261749). In the BRCA1-A complex, it acts as an adapter that bridges the interaction between BABAM1/NBA1 and the rest of the complex, thereby being required for the complex integrity and modulating the E3 ubiquitin ligase activity of the BRCA1-BARD1 heterodimer (PubMed:19261748, PubMed:21282113). Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates (PubMed:19214193, PubMed:24075985, PubMed:25283148, PubMed:26195665). Within the BRISC complex, acts as an adapter that bridges the interaction between BABAM1/NBA1 and the rest of the complex, thereby being required for the complex integrity (PubMed:21282113). The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1 (PubMed:26195665). The BRISC complex 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). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985). May play a role in homeostasis or cellular differentiation in cells of neural, epithelial and germline origins. May also act as a death receptor-associated anti-apoptotic protein, which inhibits the mitochondrial apoptotic pathway. May regulate TNF-alpha signaling through its interactions with TNFRSF1A; however these effects may be indirect (PubMed:15465831)