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P46737 (BRCC3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lys-63-specific deubiquitinase BRCC36

EC=3.4.19.-
Alternative name(s):
BRCA1-A complex subunit BRCC36
BRCA1/BRCA2-containing complex subunit 3
BRCA1/BRCA2-containing complex subunit 36
BRISC complex subunit BRCC36
Gene names
Name:Brcc3
Synonyms:Brcc36, C6.1a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length291 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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.

Subunit structure

Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1/RAP80, FAM175A/Abraxas, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/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 BABAM1/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 processDNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
Hydrolase
Metalloprotease
Protease
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2 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

positive regulation of DNA repair

Inferred from sequence or structural similarity. Source: UniProtKB

protein K63-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

response to X-ray

Inferred from electronic annotation. Source: Ensembl

response to ionizing radiation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentBRCA1-A complex

Inferred from sequence or structural similarity. Source: UniProtKB

BRISC complex

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear ubiquitin ligase complex

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionenzyme regulator activity

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

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

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P46737-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P46737-2)

The sequence of this isoform differs from the canonical sequence as follows:
     183-227: EYERIEIPIHIVPHITIGKVCLESAVELPKILCQEEQDAYRRIHS → D

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 291290Lys-63-specific deubiquitinase BRCC36
PRO_0000213968

Regions

Domain7 – 148142MPN
Motif122 – 13514JAMM motif

Sites

Metal binding1221Zinc; catalytic By similarity
Metal binding1241Zinc; catalytic By similarity
Metal binding1351Zinc; catalytic By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Natural variations

Alternative sequence183 – 22745EYERI…RRIHS → D in isoform 2.
VSP_037260

Experimental info

Sequence conflict1081A → S in BAE29117. Ref.2
Sequence conflict2011K → E in BAE29117. Ref.2
Sequence conflict2801K → R in BAB27894. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 82D18B79D8EC5F72

FASTA29133,340
        10         20         30         40         50         60 
MAVQVVQAVQ AVHLESDAFL VCLNHALSTE KEEVMGLCIG ELNDDIRSDS KFTYTGTEMR 

        70         80         90        100        110        120 
TVQEKMDTIR IVHIHSVIIL RRSDKRKDRV EISPEQLSAA STEAERLAEL TGRPMRVVGW 

       130        140        150        160        170        180 
YHSHPHITVW PSHVDVRTQA MYQMMDQGFV GLIFSCFIED KNTKTGRVLY TCFQSIQAQK 

       190        200        210        220        230        240 
SSEYERIEIP IHIVPHITIG KVCLESAVEL PKILCQEEQD AYRRIHSLTH LDSVTKIHNG 

       250        260        270        280        290 
SVFTKNLCSQ MSAVSGPLLQ WLEDRLEQNQ QHLQELQQEK EELMEELSSL E 

« Hide

Isoform 2 [UniParc].

Checksum: 6FEF9E1B6BC8DA73
Show »

FASTA24728,203

References

« Hide 'large scale' references
[1]"The chromosomal translocation t(X;14)(q28;q11) in T-cell pro-lymphocytic leukaemia breaks within one gene and activates another."
Fisch P., Forster A., Sherrington P.D., Dyer M.J.S., Rabbitts T.H.
Oncogene 8:3271-3276(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Embryo.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Bone marrow and Embryo.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Brain and Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S68022 mRNA. Translation: AAB29006.2.
AK011876 mRNA. Translation: BAB27894.1.
AK149844 mRNA. Translation: BAE29117.1.
AL671860 Genomic DNA. Translation: CAM46071.1.
AL671860 Genomic DNA. Translation: CAP19082.1.
BC021313 mRNA. Translation: AAH21313.1.
BC048179 mRNA. Translation: AAH48179.1.
RefSeqNP_001159929.1. NM_001166457.1.
NP_001159931.1. NM_001166459.1.
NP_666068.1. NM_145956.4.
UniGeneMm.226957.

3D structure databases

ProteinModelPortalP46737.
SMRP46737. Positions 5-223.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid229180. 1 interaction.
IntActP46737. 2 interactions.
MINTMINT-4089567.

Protein family/group databases

MEROPSM67.004.

PTM databases

PhosphoSiteP46737.

Proteomic databases

PaxDbP46737.
PRIDEP46737.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033544; ENSMUSP00000033544; ENSMUSG00000031201. [P46737-1]
ENSMUST00000114074; ENSMUSP00000109708; ENSMUSG00000031201. [P46737-1]
ENSMUST00000118428; ENSMUSP00000114057; ENSMUSG00000031201. [P46737-2]
GeneID210766.
KEGGmmu:210766.
UCSCuc009tpy.2. mouse. [P46737-1]

Organism-specific databases

CTD79184.
MGIMGI:2389572. Brcc3.

Phylogenomic databases

eggNOGNOG322509.
GeneTreeENSGT00390000000360.
HOGENOMHOG000007866.
HOVERGENHBG002142.
InParanoidQ3UDZ4.
KOK11864.
OMAIPIHVVP.
OrthoDBEOG7KM5TH.
PhylomeDBP46737.
TreeFamTF328524.

Gene expression databases

ArrayExpressP46737.
BgeeP46737.
CleanExMM_BRCC3.
GenevestigatorP46737.

Family and domain databases

InterProIPR000555. JAMM/MPN+_dom.
[Graphical view]
PfamPF01398. JAB. 1 hit.
[Graphical view]
SMARTSM00232. JAB_MPN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio373053.
PROP46737.
SOURCESearch...

Entry information

Entry nameBRCC3_MOUSE
AccessionPrimary (citable) accession number: P46737
Secondary accession number(s): A3KGA9 expand/collapse secondary AC list , A8Y5K0, Q3UDZ4, Q9D025
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot