BRCC3
entrez
79184
canonical
uniprot
P46736
canonical
ensembl
ENSG00000185515
resolver
ensp
ENSP00000328641
resolver
ensp
ENSP00000344103
resolver
ensp
ENSP00000358474
resolver
genesymbol
BRCC3
resolver
genesymbol_syn
BRCC36
resolver
genesymbol_syn
C6.1A
resolver
genesymbol_syn
CXorf53
resolver
hgnc
HGNC:24185
resolver
uniprot
A6QRF8
resolver
uniprot
A6QRF9
resolver
uniprot
A8MUX5
resolver
uniprot
A8MWH0
resolver
uniprot
A9Z1Y0
resolver
uniprot
A9Z1Y5
resolver
uniprot
B1B062
resolver
uniprot
B4DQN7
resolver
uniprot
Q16107
resolver
uniprot
Q53YX5
resolver
uniprot
Q9BTZ6
resolver
uniprot_entry
BRCC3_HUMAN
resolver
uniprot_sec
A6QRF8
resolver
uniprot_sec
A6QRF9
resolver
uniprot_sec
A8MUX5
resolver
uniprot_sec
A8MWH0
resolver
uniprot_sec
A9Z1Y0
resolver
uniprot_sec
A9Z1Y5
resolver
uniprot_sec
B1B062
resolver
uniprot_sec
B4DQN7
resolver
uniprot_sec
Q16107
resolver
uniprot_sec
Q53YX5
resolver
uniprot_sec
Q9BTZ6
resolver
amino_acid_sequence
MAVQVVQAVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDTRSDSKFAYTGTEMRTVAEKVDAVRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSIQAQKSSESLHGPRDFWSSSQHISIEGQKEEERYERIEIPIHIVPHVTIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHLQELQQEKEELMQELSSLE
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving BRCC3 is a cause of pro-lymphocytic T-cell leukemia (T-PLL). Translocation t(X;14)(q28;q11) with TCRA. {ECO:0000269|PubMed:8247530}.
uniprot
proteins
ec_number
3.4.19.-
uniprot
proteins
function
FUNCTION: 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). {ECO:0000250|UniProtKB:P46737, ECO:0000269|PubMed:14636569, ECO:0000269|PubMed:16707425, ECO:0000269|PubMed:17525341, ECO:0000269|PubMed:19202061, ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749, ECO:0000269|PubMed:20656690, ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:26195665, ECO:0000269|PubMed:26344097}.
uniprot
proteins
mass_dalton
36072
uniprot
proteins
mutagenesis
MUTAGEN 23; /note="L->R: Abolishes localization to sites of DNA damage and interaction with ABRAXAS2; UIMC1; SHMT2; BARAM2 and BABAM1; when associated with R-27."; /evidence="ECO:0000269|PubMed:26344097"; MUTAGEN 27; /note="L->R: Abolishes localization to sites of DNA damage and interaction with ABRAXAS2; UIMC1; SHMT2; BABAM2 and BABAM1; when associated with R-23."; /evidence="ECO:0000269|PubMed:26344097"; MUTAGEN 122..124; /note="HSH->QSQ: Abolishes metalloprotease activity and function in DNA repair."; /evidence="ECO:0000269|PubMed:17525341, ECO:0000269|PubMed:19202061, ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:26195665"; MUTAGEN 122; /note="H->Q: Loss of deubiquitinase activity."; /evidence="ECO:0000269|PubMed:19214193"; MUTAGEN 278; /note="A->R: Abolishes interaction with UIMC1 and SHMT2."; /evidence="ECO:0000269|PubMed:26344097
uniprot
proteins
protein_family
BRCC36 subfamily
uniprot
proteins
protein_family
Peptidase M67A family
uniprot
proteins
pubmed
1303175
uniprot
proteins
pubmed
14636569
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16707425
uniprot
proteins
pubmed
17525341
uniprot
proteins
pubmed
18077395
uniprot
proteins
pubmed
19202061
uniprot
proteins
pubmed
19214193
uniprot
proteins
pubmed
19261746
uniprot
proteins
pubmed
19261748
uniprot
proteins
pubmed
19261749
uniprot
proteins
pubmed
20656690
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24075985
uniprot
proteins
pubmed
25283148
uniprot
proteins
pubmed
26195665
uniprot
proteins
pubmed
26344097
uniprot
proteins
pubmed
8247530
uniprot
proteins
sequence_length
316
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18077395, ECO:0000269|PubMed:19202061, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749, ECO:0000269|PubMed:20656690, ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:26344097}. Cytoplasm {ECO:0000269|PubMed:20656690, ECO:0000269|PubMed:24075985}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000305|PubMed:26195665}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs) (PubMed:20656690, PubMed:26344097). Interaction with ABRAXAS2 retains BRCC3 in the cytoplasm (PubMed:20656690). {ECO:0000269|PubMed:20656690, ECO:0000269|PubMed:26344097}.
uniprot
proteins