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P46737

- BRCC3_MOUSE

UniProt

P46737 - BRCC3_MOUSE

Protein

Lys-63-specific deubiquitinase BRCC36

Gene

Brcc3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi122 – 1221Zinc; catalyticBy similarity
    Metal bindingi124 – 1241Zinc; catalyticBy similarity
    Metal bindingi135 – 1351Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. enzyme regulator activity Source: Ensembl
    2. metal ion binding Source: UniProtKB-KW
    3. metallopeptidase activity Source: UniProtKB
    4. polyubiquitin binding Source: UniProtKB
    5. protein binding Source: MGI
    6. ubiquitin-specific protease activity Source: UniProtKB
    7. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. double-strand break repair Source: UniProtKB
    2. G2 DNA damage checkpoint Source: UniProtKB
    3. histone H2A K63-linked deubiquitination Source: UniProtKB
    4. positive regulation of DNA repair Source: UniProtKB
    5. protein K63-linked deubiquitination Source: UniProtKB
    6. response to ionizing radiation Source: UniProtKB
    7. response to X-ray Source: Ensembl

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    DNA damage, DNA repair, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM67.004.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Brcc3
    Synonyms:Brcc36, C6.1a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:2389572. Brcc3.

    Subcellular locationi

    Nucleus By similarity
    Note: Localizes at sites of DNA damage at double-strand breaks (DSBs).By similarity

    GO - Cellular componenti

    1. BRCA1-A complex Source: UniProtKB
    2. BRISC complex Source: UniProtKB
    3. nuclear ubiquitin ligase complex Source: Ensembl
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 291290Lys-63-specific deubiquitinase BRCC36PRO_0000213968Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP46737.
    PaxDbiP46737.
    PRIDEiP46737.

    PTM databases

    PhosphoSiteiP46737.

    Expressioni

    Gene expression databases

    ArrayExpressiP46737.
    BgeeiP46737.
    CleanExiMM_BRCC3.
    GenevestigatoriP46737.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    BioGridi229180. 1 interaction.
    IntActiP46737. 2 interactions.
    MINTiMINT-4089567.

    Structurei

    3D structure databases

    ProteinModelPortaliP46737.
    SMRiP46737. Positions 9-215.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 148142MPNAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi122 – 13514JAMM motifAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M67A family. BRCC36 subfamily.Curated
    Contains 1 MPN (JAB/Mov34) domain.Curated

    Phylogenomic databases

    eggNOGiNOG322509.
    GeneTreeiENSGT00390000000360.
    HOGENOMiHOG000007866.
    HOVERGENiHBG002142.
    InParanoidiQ3UDZ4.
    KOiK11864.
    OMAiDAFLVCM.
    OrthoDBiEOG7KM5TH.
    PhylomeDBiP46737.
    TreeFamiTF328524.

    Family and domain databases

    InterProiIPR000555. JAMM/MPN+_dom.
    [Graphical view]
    PfamiPF01398. JAB. 1 hit.
    [Graphical view]
    SMARTiSM00232. JAB_MPN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P46737-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAVQVVQAVQ AVHLESDAFL VCLNHALSTE KEEVMGLCIG ELNDDIRSDS    50
    KFTYTGTEMR TVQEKMDTIR IVHIHSVIIL RRSDKRKDRV EISPEQLSAA 100
    STEAERLAEL TGRPMRVVGW YHSHPHITVW PSHVDVRTQA MYQMMDQGFV 150
    GLIFSCFIED KNTKTGRVLY TCFQSIQAQK SSEYERIEIP IHIVPHITIG 200
    KVCLESAVEL PKILCQEEQD AYRRIHSLTH LDSVTKIHNG SVFTKNLCSQ 250
    MSAVSGPLLQ WLEDRLEQNQ QHLQELQQEK EELMEELSSL E 291
    Length:291
    Mass (Da):33,340
    Last modified:November 1, 1995 - v1
    Checksum:i82D18B79D8EC5F72
    GO
    Isoform 2 (identifier: P46737-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:247
    Mass (Da):28,203
    Checksum:i6FEF9E1B6BC8DA73
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti108 – 1081A → S in BAE29117. (PubMed:16141072)Curated
    Sequence conflicti201 – 2011K → E in BAE29117. (PubMed:16141072)Curated
    Sequence conflicti280 – 2801K → R in BAB27894. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei183 – 22745EYERI…RRIHS → D in isoform 2. CuratedVSP_037260Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS41031.1. [P46737-1]
    RefSeqiNP_001159929.1. NM_001166457.1. [P46737-1]
    NP_001159931.1. NM_001166459.1. [P46737-1]
    NP_666068.1. NM_145956.4. [P46737-1]
    UniGeneiMm.226957.

    Genome annotation databases

    EnsembliENSMUST00000033544; ENSMUSP00000033544; ENSMUSG00000031201. [P46737-1]
    ENSMUST00000114074; ENSMUSP00000109708; ENSMUSG00000031201. [P46737-1]
    ENSMUST00000118428; ENSMUSP00000114057; ENSMUSG00000031201. [P46737-2]
    GeneIDi210766.
    KEGGimmu:210766.
    UCSCiuc009tpy.2. mouse. [P46737-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS41031.1. [P46737-1 ]
    RefSeqi NP_001159929.1. NM_001166457.1. [P46737-1 ]
    NP_001159931.1. NM_001166459.1. [P46737-1 ]
    NP_666068.1. NM_145956.4. [P46737-1 ]
    UniGenei Mm.226957.

    3D structure databases

    ProteinModelPortali P46737.
    SMRi P46737. Positions 9-215.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 229180. 1 interaction.
    IntActi P46737. 2 interactions.
    MINTi MINT-4089567.

    Protein family/group databases

    MEROPSi M67.004.

    PTM databases

    PhosphoSitei P46737.

    Proteomic databases

    MaxQBi P46737.
    PaxDbi P46737.
    PRIDEi P46737.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033544 ; ENSMUSP00000033544 ; ENSMUSG00000031201 . [P46737-1 ]
    ENSMUST00000114074 ; ENSMUSP00000109708 ; ENSMUSG00000031201 . [P46737-1 ]
    ENSMUST00000118428 ; ENSMUSP00000114057 ; ENSMUSG00000031201 . [P46737-2 ]
    GeneIDi 210766.
    KEGGi mmu:210766.
    UCSCi uc009tpy.2. mouse. [P46737-1 ]

    Organism-specific databases

    CTDi 79184.
    MGIi MGI:2389572. Brcc3.

    Phylogenomic databases

    eggNOGi NOG322509.
    GeneTreei ENSGT00390000000360.
    HOGENOMi HOG000007866.
    HOVERGENi HBG002142.
    InParanoidi Q3UDZ4.
    KOi K11864.
    OMAi DAFLVCM.
    OrthoDBi EOG7KM5TH.
    PhylomeDBi P46737.
    TreeFami TF328524.

    Miscellaneous databases

    NextBioi 373053.
    PROi P46737.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46737.
    Bgeei P46737.
    CleanExi MM_BRCC3.
    Genevestigatori P46737.

    Family and domain databases

    InterProi IPR000555. JAMM/MPN+_dom.
    [Graphical view ]
    Pfami PF01398. JAB. 1 hit.
    [Graphical view ]
    SMARTi SM00232. JAB_MPN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    Entry informationi

    Entry nameiBRCC3_MOUSE
    AccessioniPrimary (citable) accession number: P46737
    Secondary accession number(s): A3KGA9
    , A8Y5K0, Q3UDZ4, Q9D025
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3