Reviewed, UniProtKB/Swiss-Prot B0KWU8 (BRCC3_CALJA)

Names and origin

Protein names

Recommended name:
    Lys-63-specific deubiquitinase BRCC36
    EC=3.1.2.15
Alternative name(s):
    BRCA1-A complex subunit BRCC36
    BRISC complex subunit BRCC36
    BRCA1/BRCA2-containing complex subunit 3
    BRCA1/BRCA2-containing complex subunit 36

Gene names

Name:	BRCC3
Synonyms:	BRCC36

Organism

Callithrix jacchus (Common marmoset)

Taxonomic identifier

9483 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Platyrrhini › Cebidae › Callitrichinae › Callithrix

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. 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). 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). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. 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 By similarity.
Catalytic activity	Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol.
Subunit structure	Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1/RAP80, FAM175A/Abraxas, BRCC3/BRCC36, BRE/BRCC45 and MERIT40/NBA1. In the BRCA1-A complex, interacts directly with FAM175A/Abraxas and BRE/BRCC45. Component of the BRISC complex, at least composed of the FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 and MERIT40/NBA1. The BRISC complex interacts with the CSN complex. Component of the BRCA1/BRCA2 containing complex (BRCC), which also contains BRCA1, BRCA2, BARD1, BRE and RAD51. BRCC is a ubiquitin E3 ligase complex that enhances cellular survival following DNA damage. Interacts with BRCA1. Binds polyubiquitin By similarity.
Subcellular location	Nucleus By similarity. Note: Localizes at sites of DNA damage at double-strand breaks (DSBs) By similarity.
Sequence similarities	Belongs to the peptidase M67A family. BRCC36 subfamily. Contains 1 MPN (JAB/Mov34) domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Nucleus
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator Hydrolase Metalloprotease Protease
PTM	Acetylation
Gene Ontology (GO)
Biological process	G2/M transition DNA damage checkpoint Inferred from sequence or structural similarity. Source: UniProtKB double-strand break repair Inferred from sequence or structural similarity. Source: UniProtKB histone H2A K63-linked deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of DNA repair Inferred from sequence or structural similarity. Source: UniProtKB response to ionizing radiation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	BRCA1-A complex Inferred from sequence or structural similarity. Source: UniProtKB BRISC complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	metallopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB polyubiquitin binding Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin thiolesterase activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-specific protease activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 316	315	Lys-63-specific deubiquitinase BRCC36		PRO_0000373945
Regions
	Motif	122 – 135	14	JAMM motif
Sites
	Metal binding	122	1	Zinc; catalytic By similarity
	Metal binding	124	1	Zinc; catalytic By similarity
	Metal binding	135	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0KWU8-1 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 58C2421C1A2F6E21	FASTA	316	36,100
	10 20 30 40 50 60 MAVQVVQAVQ AVHLESDAFL VCLNHALSTE KEEVMGLCIG ELNDDTRSDS KFAYTGTEMR 70 80 90 100 110 120 TVAEKVDAVR IVHIHSVIIL RRSDKRKDRV EISPEQLSAA STEAERLAEL TGRPMRVVGW 130 140 150 160 170 180 YHSHPHITVW PSHVDVRTQA MYQMMDQGFV GLIFSCFIED KNTKTGRVLY TCFQSIQAQK 190 200 210 220 230 240 SSESLHGPRD FWSSSKHISI EGQKEEERYE RIEIPIHIVP HVTIGKVCLE SAVELPKILC 250 260 270 280 290 300 QEEQDAYRRI HSLTHLDSVT KIHNGSVFTK NLCSQMSAVS GPLLQWLEDR LEQNQQHLRE 310 LQQEKEELMQ ELSSLE

References

[1]

"NISC comparative sequencing initiative." Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A., Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J., Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N. , Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P., Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A., Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O., Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S., Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L., Vogt J.L., Wetherby K.D., Young A., Green E.D. Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	DP000587 Genomic DNA. Translation: ABZ10507.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M67.004.
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

BRCC3_CALJA

Accession

Primary (citable) accession number: B0KWU8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	May 5, 2009
Last modified:	June 16, 2009
This is version 9 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)