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P48754

- BRCA1_MOUSE

UniProt

P48754 - BRCA1_MOUSE

Protein

Breast cancer type 1 susceptibility protein homolog

Gene

Brca1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 3 (03 Oct 2012)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The E3 ubiquitin-protein ligase activity is required for its tumor suppressor function. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for normal cell cycle progression from G2 to mitosis. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8 By similarity. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation.By similarity1 Publication

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri24 – 6542RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. damaged DNA binding Source: MGI
    2. ligase activity Source: UniProtKB-KW
    3. RNA binding Source: MGI
    4. transcription regulatory region DNA binding Source: BHF-UCL
    5. ubiquitin-protein transferase activity Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: MGI
    2. centrosome cycle Source: MGI
    3. centrosome duplication Source: UniProtKB
    4. chordate embryonic development Source: MGI
    5. DNA recombination Source: UniProtKB-KW
    6. DNA repair Source: UniProtKB-KW
    7. DNA replication Source: MGI
    8. dosage compensation by inactivation of X chromosome Source: MGI
    9. fatty acid biosynthetic process Source: UniProtKB-KW
    10. intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
    11. negative regulation of fatty acid biosynthetic process Source: UniProtKB
    12. negative regulation of histone acetylation Source: BHF-UCL
    13. negative regulation of histone H3-K4 methylation Source: BHF-UCL
    14. negative regulation of histone H3-K9 methylation Source: BHF-UCL
    15. positive regulation of histone acetylation Source: BHF-UCL
    16. positive regulation of histone H3-K4 methylation Source: BHF-UCL
    17. positive regulation of histone H3-K9 acetylation Source: BHF-UCL
    18. positive regulation of histone H3-K9 methylation Source: BHF-UCL
    19. positive regulation of histone H4-K16 acetylation Source: BHF-UCL
    20. positive regulation of histone H4-K20 methylation Source: BHF-UCL
    21. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    22. protein autoubiquitination Source: UniProtKB
    23. protein K6-linked ubiquitination Source: UniProtKB
    24. regulation of DNA methylation Source: BHF-UCL
    25. regulation of gene expression by genetic imprinting Source: BHF-UCL

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Cell cycle, DNA damage, DNA recombination, DNA repair, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198626. Meiotic synapsis.
    REACT_198629. Meiotic recombination.
    REACT_27235. Meiotic Recombination.
    REACT_75800. Meiotic Synapsis.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Breast cancer type 1 susceptibility protein homolog (EC:6.3.2.-)
    Gene namesi
    Name:Brca1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:104537. Brca1.

    Subcellular locationi

    Nucleus By similarity. Chromosome 2 Publications
    Note: Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex.By similarity

    GO - Cellular componenti

    1. BRCA1-BARD1 complex Source: UniProtKB
    2. centrosome Source: UniProtKB
    3. chromosome Source: UniProtKB
    4. condensed chromosome Source: MGI
    5. condensed nuclear chromosome Source: MGI
    6. cytoplasm Source: MGI
    7. nucleoplasm Source: Reactome
    8. ribonucleoprotein complex Source: MGI

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18121812Breast cancer type 1 susceptibility protein homologPRO_0000055832Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei114 – 1141PhosphoserineBy similarity
    Modified residuei305 – 3051PhosphoserineBy similarity
    Modified residuei392 – 3921PhosphoserineBy similarity
    Modified residuei686 – 6861PhosphoserineBy similarity
    Modified residuei831 – 8311Phosphoserine1 Publication
    Modified residuei971 – 9711Phosphoserine; by CHEK2By similarity
    Modified residuei1174 – 11741PhosphoserineBy similarity
    Modified residuei1180 – 11801PhosphoserineBy similarity
    Modified residuei1241 – 12411PhosphoserineBy similarity
    Modified residuei1297 – 12971PhosphoserineBy similarity
    Modified residuei1303 – 13031PhosphoserineBy similarity
    Modified residuei1343 – 13431PhosphoserineBy similarity
    Modified residuei1350 – 13501PhosphothreonineBy similarity
    Modified residuei1413 – 14131PhosphoserineBy similarity
    Modified residuei1481 – 14811PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated in response to IR, UV, and various stimuli that cause checkpoint activation, probably by ATM or ATR. Phosphorylation at Ser-971 by CHEK2 regulates mitotic spindle assembly By similarity.By similarity
    Autoubiquitinated, undergoes 'Lys-6'-linked polyubiquitination. 'Lys-6'-linked polyubiquitination does not promote degradation By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP48754.

    PTM databases

    PhosphoSiteiP48754.

    Expressioni

    Tissue specificityi

    In the embryo, expressed in otic vesicles at day 9.5. At day 10.5, this expression decreases and high levels are found in the neuroectoderm. At days 11-12.5, high levels in differentiating keratinocytes and whisker pad primordia. At days 14-17, expression also observed in kidney epithelial cells. In the adult, highest levels found in spleen, thymus, lymph nodes, epithelial organs, and alveolar and ductal epithelial cells of the mammary gland. Very low levels in brain, kidney, and skin. No expression in heart, liver or lung.

    Developmental stagei

    In the mammary gland, expression increases dramatically during pregnancy. Levels fall during lactation and increase again during post-lactational regression of the mammary gland.

    Gene expression databases

    ArrayExpressiP48754.
    CleanExiMM_BRCA1.
    GenevestigatoriP48754.

    Interactioni

    Subunit structurei

    Heterodimer with BARD1. Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the MRE11-RAD50-NBN protein (MRN) complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1, BRCC3, BRE and BABAM1. Interacts (via the BRCT domains) with FAM175A. Component of the BRCA1-RBBP8 complex. Interacts (via the BRCT domains) with RBBP8 ('Ser-327' phosphorylated form); the interaction ubiquitinates RBBP8, regulates CHEK1 activation, and involves RBBP8 in BRCA1-dependent G2/M checkpoint control on DNA damage. Associates with RNA polymerase II holoenzyme. Interacts with SMC1A, COBRA1, DCLRE1C, CLSPN. CHEK1, CHEK2, BAP1, BRCC3, AURKA, UBXN1 and KIAA0101/PAF15. Interacts (via BRCT domains) with BRIP1 (phosphorylated form). Interacts with FANCD2 (ubiquitinated form). Interacts with H2AFX (phosphorylated on 'Ser-140'). Interacts (via the BRCT domains) with ACACA (phosphorylated form); the interaction prevents dephosphorylation of ACACA. Part of a BRCA complex containing BRCA1, BRCA2 and PALB2. Interacts directly with PALB2; the interaction is essential for its function in HRR. Interacts directly with BRCA2; the interaction occurs only in the presence of PALB2 which serves as the bridging protein. Interacts (via the BRCT domains) with LMO4; the interaction represses the transcriptional activity of BRCA1.1 Publication

    Protein-protein interaction databases

    BioGridi198383. 21 interactions.
    DIPiDIP-41981N.
    IntActiP48754. 2 interactions.
    STRINGi10090.ENSMUSP00000102847.

    Structurei

    3D structure databases

    ProteinModelPortaliP48754.
    SMRiP48754. Positions 1-103, 1588-1798.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1585 – 167995BRCT 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1698 – 1797100BRCT 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1353 – 138028Interaction with PALB2By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1562 – 15676Poly-Ala

    Domaini

    The BRCT domains recognize and bind phosphorylated pSXXF motif on proteins. The interaction with the phosphorylated pSXXF motif of FAM175A/Abraxas, recruits BRCA1 at DNA damage sites By similarity.By similarity
    The RING-type zinc finger domain interacts with BAP1.By similarity

    Sequence similaritiesi

    Contains 2 BRCT domains.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri24 – 6542RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG274496.
    GeneTreeiENSGT00440000034289.
    HOGENOMiHOG000230969.
    HOVERGENiHBG050730.
    InParanoidiP48754.
    KOiK10605.
    OMAiKGPSQCP.
    OrthoDBiEOG79CXXK.
    TreeFamiTF105060.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    3.40.50.10190. 2 hits.
    InterProiIPR011364. BRCA1.
    IPR025994. BRCA1_serine_dom.
    IPR001357. BRCT_dom.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PANTHERiPTHR13763. PTHR13763. 1 hit.
    PfamiPF00533. BRCT. 2 hits.
    PF12820. BRCT_assoc. 1 hit.
    PF00097. zf-C3HC4. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001734. BRCA1. 1 hit.
    PRINTSiPR00493. BRSTCANCERI.
    SMARTiSM00292. BRCT. 2 hits.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF52113. SSF52113. 2 hits.
    PROSITEiPS50172. BRCT. 2 hits.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P48754-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDLSAVQIQE VQNVLHAMQK ILECPICLEL IKEPVSTKCD HIFCKFCMLK     50
    LLNQKKGPSQ CPLCKNEITK RSLQGSTRFS QLAEELLRIM AAFELDTGMQ 100
    LTNGFSFSKK RNNSCERLNE EASIIQSVGY RNRVRRLPQV EPGNATLKDS 150
    LGVQLSNLGI VRSVKKNRQT QPRKKSVYIE LDSDSSEETV TKPGDCSVRD 200
    QELLQTAPQE AGDEGKLHSA EEAACEFSEG IRNIEHHQCS DDLNPTENHA 250
    TERHPEKCQS ISISNVCVEP CGTDAHASSL QPETSSLLLI EDRMNAEKAE 300
    FCNKSKQPGI AVSQQSRWAA SKGTCNDRQV PSTGEKVGPN ADSLSDREKW 350
    THPQSLCPEN SGATTDVPWI TLNSSVQKVN EWFSRTGEML TSDSASARRH 400
    ESNAEAAVVL EVSNEVDGGF SSSRKTDLVT PDPHHTLMCK SGRDFSKPVE 450
    DNISDKIFGK SYQRKGSRPH LNHVTEIIGT FITEPQITQE QPFTNKLKRK 500
    RSTSLQPEDF IKKADSAGVQ RTPDNINQGT DLMEPNEQAV STTSNCQENK 550
    IAGSNLQKEK SAHPTESLRK EPASTAGAKS ISNSVSDLEV ELNVHSSKAP 600
    KKNRLRRKSS IRCALPLEPI SRNPSPPTCA ELQIDSCGSS EETKKNHSNQ 650
    QPAGHLREPQ LIEDTEPAAD AKKNEPNEHI RKRRASDAFP EEKLMNKAGL 700
    LTSCSSPRKS QGPVNPSPQR TGTEQLETRQ MSDSAKELGD RVLGGEPSGK 750
    TTDRSEESTS VSLVSDTDYD TQNSVSVLDA HTVRYARTGS AQCMTQFVAS 800
    ENPKELVHGS NNAGSGTEGL KPPLRHALNL SQEKVEMEDS ELDTQYLQNT 850
    FQVSKRQSFA LFSKPRSPQK DCAHSVPSKE LSPKVTAKGK QKERQGQEEF 900
    EISHVQAVAA TVGLPVPCQE GKLAADTMCD RGCRLCPSSH YRSGENGLSA 950
    TGKSGISQNS HFKQSVSPIR SSIKTDNRKP LTEGRFERHT SSTEMAVGNE 1000
    NILQSTVHTV SLNNRGNACQ EAGSGSIHEV CSTGDSFPGQ LGRNRGPKVN 1050
    TVPPLDSMQP GVCQQSVPVS DKYLEIKKQE GEAVCADFSP CLFSDHLEQS 1100
    MSGKVFQVCS ETPDDLLDDV EIQGHTSFGE GDIMERSAVF NGSILRRESS 1150
    RSPSPVTHAS KSQSLHRASR KLESSEESDS TEDEDLPCFQ HLLSRISNTP 1200
    ELTRCSSAVT QRMPEKAEGT QAPWKGSSSD CNNEVIMIEA SQEHQFSEDP 1250
    RCSGSMFSSQ HSAAQGSTAN ANSQDSNFIP PSKQRSHQCG NEEAFLSDKE 1300
    LISDNEEMAT CLEEDNDQEE DSIIPDSEAS GYESETNLSE DCSQSDILTT 1350
    QQRATMKYNL IKLQQEMAHL EAVLEQRGNQ PSGHSPSLLA DPCALEDLPD 1400
    LEPNMSGAAI LTSKNINENP VSQNLKSACD DKFQLQHLEG PTSGDDESGM 1450
    GRPSPFKSPL AGSRGSAHGC SRHLQKRNSP SQEELLQPAG SEASSEPHNS 1500
    TGQSCLPRRE LEGTPYLGSG ISLFSSRDPE SESPKEPAHI GTTPASTSAL 1550
    KIPQGQVAFR SAAAAGADKA VVGIVSKIKP ELTSSEERAD RDISMVVSGL 1600
    TPKEVMTVQK FAEKYRLTLT DAITEETTHV IIKTDAEFVC ERTLKYFLGI 1650
    AGGKWIVSYS WVVRSIQERR LLNVHEFEVK GDVVTGRNHQ GPRRSRESRE 1700
    KLFKGLQVYC CEPFTNMPKD ELERMLQLCG ASVVKELPSL THDTGAHLVV 1750
    IVQPSAWTED SNCPDIGQLC KARLVMWDWV LDSLSSYRCR DLDAYLVQNI 1800
    TCDSSEPQDS ND 1812
    Length:1,812
    Mass (Da):198,795
    Last modified:October 3, 2012 - v3
    Checksum:i2B47FB55B149FD71
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti93 – 931F → L in AAA96393. (PubMed:8575748)Curated
    Sequence conflicti305 – 3051S → T in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti319 – 3191A → P in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti377 – 3771Q → E in AAA96393. (PubMed:8575748)Curated
    Sequence conflicti550 – 5501K → Q in AAA96393. (PubMed:8575748)Curated
    Sequence conflicti652 – 6521P → A in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti765 – 7651S → P in AAA96393. (PubMed:8575748)Curated
    Sequence conflicti765 – 7651S → P in AAC52323. (PubMed:7590247)Curated
    Sequence conflicti917 – 9171P → L in AAA96393. (PubMed:8575748)Curated
    Sequence conflicti933 – 9331C → S in AAA96393. (PubMed:8575748)Curated
    Sequence conflicti933 – 9331C → S in AAA99742. (PubMed:8566965)Curated
    Sequence conflicti1091 – 10911C → R in AAB17114. (PubMed:8634697)Curated
    Sequence conflicti1122 – 11221I → K in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti1206 – 12061S → R in AAA96393. (PubMed:8575748)Curated
    Sequence conflicti1212 – 12132RM → GI in AAA96393. (PubMed:8575748)Curated
    Sequence conflicti1255 – 12551S → R in AAA96393. (PubMed:8575748)Curated
    Sequence conflicti1261 – 12611H → N in AAA96393. (PubMed:8575748)Curated
    Sequence conflicti1264 – 12641A → V in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti1269 – 12691A → P in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti1283 – 12831K → T in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti1337 – 13371N → T in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti1349 – 13491T → P in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti1352 – 13532QR → EG in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti1381 – 13811P → S in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti1390 – 13901A → G in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti1400 – 14001D → V in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti1503 – 15031Q → E in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti1549 – 15491A → V in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti1680 – 16801K → T in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti1712 – 17121E → D in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti1721 – 17211E → D in AAB17113. (PubMed:8634698)Curated
    Sequence conflicti1791 – 17911D → G in AAB17114. (PubMed:8634697)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U31625 mRNA. Translation: AAB17114.1.
    U35641 mRNA. Translation: AAB17113.1.
    U32446 mRNA. Translation: AAA96393.1.
    U36475 mRNA. Translation: AAC52323.1.
    AL590996 Genomic DNA. Translation: CAM21026.1.
    U33835 Genomic DNA. Translation: AAA99742.1.
    CCDSiCCDS25474.1.
    PIRiI49350.
    RefSeqiNP_033894.3. NM_009764.3.
    UniGeneiMm.244975.

    Genome annotation databases

    EnsembliENSMUST00000017290; ENSMUSP00000017290; ENSMUSG00000017146.
    GeneIDi12189.
    KEGGimmu:12189.
    UCSCiuc007lpd.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U31625 mRNA. Translation: AAB17114.1 .
    U35641 mRNA. Translation: AAB17113.1 .
    U32446 mRNA. Translation: AAA96393.1 .
    U36475 mRNA. Translation: AAC52323.1 .
    AL590996 Genomic DNA. Translation: CAM21026.1 .
    U33835 Genomic DNA. Translation: AAA99742.1 .
    CCDSi CCDS25474.1.
    PIRi I49350.
    RefSeqi NP_033894.3. NM_009764.3.
    UniGenei Mm.244975.

    3D structure databases

    ProteinModelPortali P48754.
    SMRi P48754. Positions 1-103, 1588-1798.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198383. 21 interactions.
    DIPi DIP-41981N.
    IntActi P48754. 2 interactions.
    STRINGi 10090.ENSMUSP00000102847.

    PTM databases

    PhosphoSitei P48754.

    Proteomic databases

    PRIDEi P48754.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000017290 ; ENSMUSP00000017290 ; ENSMUSG00000017146 .
    GeneIDi 12189.
    KEGGi mmu:12189.
    UCSCi uc007lpd.2. mouse.

    Organism-specific databases

    CTDi 672.
    MGIi MGI:104537. Brca1.

    Phylogenomic databases

    eggNOGi NOG274496.
    GeneTreei ENSGT00440000034289.
    HOGENOMi HOG000230969.
    HOVERGENi HBG050730.
    InParanoidi P48754.
    KOi K10605.
    OMAi KGPSQCP.
    OrthoDBi EOG79CXXK.
    TreeFami TF105060.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_198626. Meiotic synapsis.
    REACT_198629. Meiotic recombination.
    REACT_27235. Meiotic Recombination.
    REACT_75800. Meiotic Synapsis.

    Miscellaneous databases

    NextBioi 280581.
    PROi P48754.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48754.
    CleanExi MM_BRCA1.
    Genevestigatori P48754.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    3.40.50.10190. 2 hits.
    InterProi IPR011364. BRCA1.
    IPR025994. BRCA1_serine_dom.
    IPR001357. BRCT_dom.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    PANTHERi PTHR13763. PTHR13763. 1 hit.
    Pfami PF00533. BRCT. 2 hits.
    PF12820. BRCT_assoc. 1 hit.
    PF00097. zf-C3HC4. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001734. BRCA1. 1 hit.
    PRINTSi PR00493. BRSTCANCERI.
    SMARTi SM00292. BRCT. 2 hits.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52113. SSF52113. 2 hits.
    PROSITEi PS50172. BRCT. 2 hits.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mouse Brca1: localization sequence analysis and identification of evolutionarily conserved domains."
      Abel K.J., Xy J., Yin G.Y., Lyons R.H., Meisler M.H., Weber B.L.
      Hum. Mol. Genet. 4:2265-2273(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Embryo.
    2. "Murine Brca1: sequence and significance for human missense mutations."
      Sharan S.K., Wims M., Bradley A.
      Hum. Mol. Genet. 4:2275-2278(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
    3. "Isolation of the mouse homologue of BRCA1 and genetic mapping to mouse chromosome 11."
      Bennett L.M., Haugen-Strano A., Cochran C., Brownlee H.A., Fiedorek F.T. Jr., Wiseman R.W.
      Genomics 29:576-581(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 129/SvJ.
    4. "Expression of Brca1 is associated with terminal differentiation of ectodermally and mesodermally derived tissues in mice."
      Lane T.F., Deng C., Elson A., Lyu M.S., Kozak C.A., Leder P.
      Genes Dev. 9:2712-2722(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 129/SvJ.
      Tissue: Embryo.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    6. "The developmental pattern of Brca1 expression implies a role in differentiation of the breast and other tissues."
      Marquis S.T., Rajan J.V., Wynshaw-Boris A., Xu J., Yin G.Y., Abel K.J., Weber B.L., Chodosh L.A.
      Nat. Genet. 11:17-26(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 727-1111.
      Strain: C57BL/6.
      Tissue: Embryo.
    7. "The murine homolog of the human breast and ovarian cancer susceptibility gene Brca1 maps to mouse chromosome 11D."
      Schroeck E., Badger P., Larson D., Erdos M., Wynshaw-Boris A., Ried T., Brody L.
      Hum. Genet. 97:256-259(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 789-1250.
      Strain: 129/SvJ.
    8. "BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains."
      Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S., Lenoir G.M., Venezia N.D.
      Oncogene 21:6729-6739(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ACACA, FUNCTION.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    10. "HORMAD2 is essential for synapsis surveillance during meiotic prophase via the recruitment of ATR activity."
      Kogo H., Tsutsumi M., Inagaki H., Ohye T., Kiyonari H., Kurahashi H.
      Genes Cells 17:897-912(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. "Meiotic DNA double-strand breaks and chromosome asynapsis in mice are monitored by distinct HORMAD2-independent and -dependent mechanisms."
      Wojtasz L., Cloutier J.M., Baumann M., Daniel K., Varga J., Fu J., Anastassiadis K., Stewart A.F., Remenyi A., Turner J.M., Toth A.
      Genes Dev. 26:958-973(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiBRCA1_MOUSE
    AccessioniPrimary (citable) accession number: P48754
    Secondary accession number(s): A2A4Q4, Q60957, Q60983
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 140 of the entry and version 3 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3