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P46736

- BRCC3_HUMAN

UniProt

P46736 - BRCC3_HUMAN

Protein

Lys-63-specific deubiquitinase BRCC36

Gene

BRCC3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (10 May 2002)
      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.8 Publications

    Sites

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

    GO - Molecular functioni

    1. enzyme regulator activity Source: MGI
    2. metal ion binding Source: UniProtKB-KW
    3. metallopeptidase activity Source: UniProtKB
    4. polyubiquitin binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    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. regulation of catalytic activity Source: GOC
    7. response to ionizing radiation Source: UniProtKB
    8. response to X-ray Source: MGI

    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, CXorf53
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:24185. BRCC3.

    Subcellular locationi

    Nucleus 4 Publications
    Note: Localizes at sites of DNA damage at double-strand breaks (DSBs).

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving BRCC3 is a cause of pro-lymphocytic T-cell leukemia (T-PLL). Translocation t(X;14)(q28;q11) with TCRA.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi122 – 1243HSH → QSQ: Abolishes metalloprotease activity and function in DNA repair. 1 Publication
    Mutagenesisi122 – 1221H → Q: Loss of deubiquitinase activity. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    Orphaneti280679. Moyamoya disease - short stature - facial dysmorphism - hypergonadotropic hypogonadism.
    PharmGKBiPA134922847.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 316315Lys-63-specific deubiquitinase BRCC36PRO_0000213967Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP46736.
    PaxDbiP46736.
    PRIDEiP46736.

    PTM databases

    PhosphoSiteiP46736.

    Expressioni

    Tissue specificityi

    Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Aberrantly expressed in the vast majority of breast tumors.1 Publication

    Gene expression databases

    ArrayExpressiP46736.
    BgeeiP46736.
    CleanExiHS_BRCC3.
    GenevestigatoriP46736.

    Organism-specific databases

    HPAiHPA048737.

    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.7 Publications

    Protein-protein interaction databases

    BioGridi122599. 46 interactions.
    DIPiDIP-48719N.
    IntActiP46736. 21 interactions.
    MINTiMINT-1475401.

    Structurei

    3D structure databases

    ProteinModelPortaliP46736.
    SMRiP46736. Positions 10-176.
    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.
    HOVERGENiHBG002142.
    KOiK11864.
    PhylomeDBiP46736.
    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 (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: P46736-1) [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 ELNDDTRSDS    50
    KFAYTGTEMR TVAEKVDAVR IVHIHSVIIL RRSDKRKDRV EISPEQLSAA 100
    STEAERLAEL TGRPMRVVGW YHSHPHITVW PSHVDVRTQA MYQMMDQGFV 150
    GLIFSCFIED KNTKTGRVLY TCFQSIQAQK SSESLHGPRD FWSSSQHISI 200
    EGQKEEERYE RIEIPIHIVP HVTIGKVCLE SAVELPKILC QEEQDAYRRI 250
    HSLTHLDSVT KIHNGSVFTK NLCSQMSAVS GPLLQWLEDR LEQNQQHLQE 300
    LQQEKEELMQ ELSSLE 316
    Length:316
    Mass (Da):36,072
    Last modified:May 10, 2002 - v2
    Checksum:i5720358C1A2F7421
    GO
    Isoform 1 (identifier: P46736-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         184-208: Missing.

    Show »
    Length:291
    Mass (Da):33,150
    Checksum:i56F03D91E313E1D9
    GO
    Isoform 3 (identifier: P46736-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         46-46: T → TS
         184-208: Missing.

    Show »
    Length:292
    Mass (Da):33,237
    Checksum:i70302DC19999753C
    GO
    Isoform 4 (identifier: P46736-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-114: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:202
    Mass (Da):23,458
    Checksum:iD6F04C7365A7336D
    GO
    Isoform 5 (identifier: P46736-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         183-252: ESLHGPRDFWSSSQHISIEGQKEEERYERIEIPIHIVPHVTIGKVCLESAVELPKILCQEEQDAYRRIHS → D

    Note: No experimental confirmation available.

    Show »
    Length:247
    Mass (Da):28,027
    Checksum:i817A177F34ED1ED8
    GO

    Sequence cautioni

    The sequence AAB29005.2 differs from that shown. Reason: Erroneous initiation.
    The sequence CAO03573.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti225 – 2251G → W in AAB29005. (PubMed:8247530)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti74 – 741I → V.
    Corresponds to variant rs28997578 [ dbSNP | Ensembl ].
    VAR_050097

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 114114Missing in isoform 4. 1 PublicationVSP_037257Add
    BLAST
    Alternative sequencei46 – 461T → TS in isoform 3. 1 PublicationVSP_037258
    Alternative sequencei183 – 25270ESLHG…RRIHS → D in isoform 5. CuratedVSP_037259Add
    BLAST
    Alternative sequencei184 – 20825Missing in isoform 1 and isoform 3. 2 PublicationsVSP_003261Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64643 mRNA. Translation: CAA45917.1.
    S68015 mRNA. Translation: AAB29005.2. Different initiation.
    AY438030 mRNA. Translation: AAR30498.1.
    AK298886 mRNA. Translation: BAG60999.1.
    AK299194 mRNA. Translation: BAG61237.1.
    AK313544 mRNA. Translation: BAG36320.1.
    BX293995, BX470111 Genomic DNA. Translation: CAH70537.1.
    BX293995, BX470111 Genomic DNA. Translation: CAH70538.1.
    BX470111, BX293995 Genomic DNA. Translation: CAI41654.1.
    BX470111, BX293995 Genomic DNA. Translation: CAI41655.1.
    BX470111 Genomic DNA. Translation: CAO03573.1. Sequence problems.
    BX470111 Genomic DNA. Translation: CAO03574.1.
    BX470111, BX293995 Genomic DNA. Translation: CAO03575.1.
    BX470111, BX293995 Genomic DNA. Translation: CAO03576.1.
    BX293995, BX470111 Genomic DNA. Translation: CAO03601.1.
    BX293995, BX470111 Genomic DNA. Translation: CAO03602.1.
    BC002999 mRNA. Translation: AAH02999.1.
    BC006540 mRNA. Translation: AAH06540.1.
    CCDSiCCDS56610.1. [P46736-3]
    CCDS56611.1. [P46736-1]
    CCDS56612.1. [P46736-2]
    PIRiI38167.
    RefSeqiNP_001018065.1. NM_001018055.2. [P46736-2]
    NP_001229569.1. NM_001242640.1. [P46736-3]
    NP_077308.1. NM_024332.3. [P46736-1]
    XP_005274806.1. XM_005274749.1. [P46736-5]
    XP_005274807.1. XM_005274750.1. [P46736-4]
    UniGeneiHs.558537.

    Genome annotation databases

    EnsembliENST00000330045; ENSP00000328641; ENSG00000185515. [P46736-2]
    ENST00000340647; ENSP00000344103; ENSG00000185515. [P46736-3]
    ENST00000369459; ENSP00000358471; ENSG00000185515. [P46736-5]
    ENST00000369462; ENSP00000358474; ENSG00000185515. [P46736-1]
    GeneIDi79184.
    KEGGihsa:79184.
    UCSCiuc004fna.3. human. [P46736-1]
    uc004fnb.3. human. [P46736-2]
    uc011mzy.2. human. [P46736-3]

    Polymorphism databases

    DMDMi20532383.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64643 mRNA. Translation: CAA45917.1 .
    S68015 mRNA. Translation: AAB29005.2 . Different initiation.
    AY438030 mRNA. Translation: AAR30498.1 .
    AK298886 mRNA. Translation: BAG60999.1 .
    AK299194 mRNA. Translation: BAG61237.1 .
    AK313544 mRNA. Translation: BAG36320.1 .
    BX293995 , BX470111 Genomic DNA. Translation: CAH70537.1 .
    BX293995 , BX470111 Genomic DNA. Translation: CAH70538.1 .
    BX470111 , BX293995 Genomic DNA. Translation: CAI41654.1 .
    BX470111 , BX293995 Genomic DNA. Translation: CAI41655.1 .
    BX470111 Genomic DNA. Translation: CAO03573.1 . Sequence problems.
    BX470111 Genomic DNA. Translation: CAO03574.1 .
    BX470111 , BX293995 Genomic DNA. Translation: CAO03575.1 .
    BX470111 , BX293995 Genomic DNA. Translation: CAO03576.1 .
    BX293995 , BX470111 Genomic DNA. Translation: CAO03601.1 .
    BX293995 , BX470111 Genomic DNA. Translation: CAO03602.1 .
    BC002999 mRNA. Translation: AAH02999.1 .
    BC006540 mRNA. Translation: AAH06540.1 .
    CCDSi CCDS56610.1. [P46736-3 ]
    CCDS56611.1. [P46736-1 ]
    CCDS56612.1. [P46736-2 ]
    PIRi I38167.
    RefSeqi NP_001018065.1. NM_001018055.2. [P46736-2 ]
    NP_001229569.1. NM_001242640.1. [P46736-3 ]
    NP_077308.1. NM_024332.3. [P46736-1 ]
    XP_005274806.1. XM_005274749.1. [P46736-5 ]
    XP_005274807.1. XM_005274750.1. [P46736-4 ]
    UniGenei Hs.558537.

    3D structure databases

    ProteinModelPortali P46736.
    SMRi P46736. Positions 10-176.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122599. 46 interactions.
    DIPi DIP-48719N.
    IntActi P46736. 21 interactions.
    MINTi MINT-1475401.

    Protein family/group databases

    MEROPSi M67.004.

    PTM databases

    PhosphoSitei P46736.

    Polymorphism databases

    DMDMi 20532383.

    Proteomic databases

    MaxQBi P46736.
    PaxDbi P46736.
    PRIDEi P46736.

    Protocols and materials databases

    DNASUi 79184.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330045 ; ENSP00000328641 ; ENSG00000185515 . [P46736-2 ]
    ENST00000340647 ; ENSP00000344103 ; ENSG00000185515 . [P46736-3 ]
    ENST00000369459 ; ENSP00000358471 ; ENSG00000185515 . [P46736-5 ]
    ENST00000369462 ; ENSP00000358474 ; ENSG00000185515 . [P46736-1 ]
    GeneIDi 79184.
    KEGGi hsa:79184.
    UCSCi uc004fna.3. human. [P46736-1 ]
    uc004fnb.3. human. [P46736-2 ]
    uc011mzy.2. human. [P46736-3 ]

    Organism-specific databases

    CTDi 79184.
    GeneCardsi GC0XP154299.
    HGNCi HGNC:24185. BRCC3.
    HPAi HPA048737.
    MIMi 300617. gene.
    neXtProti NX_P46736.
    Orphaneti 280679. Moyamoya disease - short stature - facial dysmorphism - hypergonadotropic hypogonadism.
    PharmGKBi PA134922847.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG322509.
    HOVERGENi HBG002142.
    KOi K11864.
    PhylomeDBi P46736.
    TreeFami TF328524.

    Miscellaneous databases

    GeneWikii BRCC3.
    GenomeRNAii 79184.
    NextBioi 68176.
    PROi P46736.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46736.
    Bgeei P46736.
    CleanExi HS_BRCC3.
    Genevestigatori P46736.

    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. "Isolation and sequence of two genes associated with a CpG island 5' of the factor VIII gene."
      Kenwrick S., Levinson B., Taylor S., Shapiro A., Gitschier J.
      Hum. Mol. Genet. 1:179-186(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "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 2), CHROMOSOMAL TRANSLOCATION.
    3. "Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair."
      Dong Y., Hakimi M.-A., Chen X., Kumaraswamy E., Cooch N.S., Godwin A.K., Shiekhattar R.
      Mol. Cell 12:1087-1099(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, IDENTIFICATION IN BRCC COMPLEX, INTERACTION WITH BRCA1.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
      Tissue: Brain and Teratocarcinoma.
    5. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 2).
      Tissue: Lung.
    7. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-31; 90-106 AND 227-237, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    8. "BRCC36 is essential for ionizing radiation-induced BRCA1 phosphorylation and nuclear foci formation."
      Chen X., Arciero C.A., Wang C., Broccoli D., Godwin A.K.
      Cancer Res. 66:5039-5046(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    9. "Ubc13/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage."
      Wang B., Elledge S.J.
      Proc. Natl. Acad. Sci. U.S.A. 104:20759-20763(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH FAM175A.
    10. "RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites."
      Sobhian B., Shao G., Lilli D.R., Culhane A.C., Moreau L.A., Xia B., Livingston D.M., Greenberg R.A.
      Science 316:1198-1202(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, MUTAGENESIS OF 122-HIS--HIS-124.
    11. "NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control."
      Wang B., Hurov K., Hofmann K., Elledge S.J.
      Genes Dev. 23:729-739(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION, UBIQUITIN-BINDING, INTERACTION WITH FAM175A.
    12. "MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA double-strand breaks."
      Shao G., Patterson-Fortin J., Messick T.E., Feng D., Shanbhag N., Wang Y., Greenberg R.A.
      Genes Dev. 23:740-754(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BRCA1-A COMPLEX, MUTAGENESIS OF 122-HIS--HIS-124.
    13. "MERIT40 facilitates BRCA1 localization and DNA damage repair."
      Feng L., Huang J., Chen J.
      Genes Dev. 23:719-728(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH BRE AND FAM175A.
    14. "K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1."
      Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M., Cohen R.E.
      EMBO J. 28:621-631(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE BRISC COMPLEX, INTERACTION WITH THE CSN COMPLEX, MUTAGENESIS OF HIS-122.
    15. "The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks."
      Shao G., Lilli D.R., Patterson-Fortin J., Coleman K.A., Morrissey D.E., Greenberg R.A.
      Proc. Natl. Acad. Sci. U.S.A. 106:3166-3171(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 122-HIS--HIS-124.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiBRCC3_HUMAN
    AccessioniPrimary (citable) accession number: P46736
    Secondary accession number(s): A6QRF8
    , A6QRF9, A8MUX5, A8MWH0, A9Z1Y0, A9Z1Y5, B1B062, B4DQN7, Q16107, Q53YX5, Q9BTZ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: May 10, 2002
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3