Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P48754 (BRCA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Breast cancer type 1 susceptibility protein homolog

EC=6.3.2.-
Gene names
Name:Brca1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1812 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.8

Subcellular location

Nucleus By similarity. Chromosome. 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. Ref.10 Ref.11

Tissue specificity

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 stage

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

Domain

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.

The RING-type zinc finger domain interacts with BAP1 By similarity.

Post-translational modification

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.

Autoubiquitinated, undergoes 'Lys-6'-linked polyubiquitination. 'Lys-6'-linked polyubiquitination does not promote degradation By similarity.

Sequence similarities

Contains 2 BRCT domains.

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processCell cycle
DNA damage
DNA recombination
DNA repair
Fatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Ubl conjugation pathway
   Cellular componentChromosome
Nucleus
   DiseaseTumor suppressor
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

DNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

DNA replication

Inferred from mutant phenotype PubMed 15254237. Source: MGI

cellular response to DNA damage stimulus

Inferred from mutant phenotype PubMed 23271346. Source: MGI

centrosome cycle

Inferred from genetic interaction PubMed 15123655. Source: MGI

centrosome duplication

Traceable author statement PubMed 10855792. Source: UniProtKB

chordate embryonic development

Inferred from mutant phenotype PubMed 9171368. Source: MGI

dosage compensation by inactivation of X chromosome

Inferred from direct assay PubMed 12419249. Source: MGI

fatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from sequence orthology PubMed 14654789. Source: MGI

negative regulation of fatty acid biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of histone H3-K4 methylation

Inferred from mutant phenotype PubMed 20820192. Source: BHF-UCL

negative regulation of histone H3-K9 methylation

Inferred from mutant phenotype PubMed 20820192. Source: BHF-UCL

negative regulation of histone acetylation

Inferred from mutant phenotype PubMed 20820192. Source: BHF-UCL

positive regulation of histone H3-K4 methylation

Inferred from mutant phenotype PubMed 20820192. Source: BHF-UCL

positive regulation of histone H3-K9 acetylation

Inferred from mutant phenotype PubMed 20820192. Source: BHF-UCL

positive regulation of histone H3-K9 methylation

Inferred from mutant phenotype PubMed 20820192. Source: BHF-UCL

positive regulation of histone H4-K16 acetylation

Inferred from mutant phenotype PubMed 20820192. Source: BHF-UCL

positive regulation of histone H4-K20 methylation

Inferred from mutant phenotype PubMed 20820192. Source: BHF-UCL

positive regulation of histone acetylation

Inferred from mutant phenotype PubMed 20820192. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20820192. Source: BHF-UCL

protein K6-linked ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein autoubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of DNA methylation

Inferred from mutant phenotype PubMed 20820192. Source: BHF-UCL

regulation of gene expression by genetic imprinting

Inferred from mutant phenotype PubMed 20820192. Source: BHF-UCL

   Cellular_componentBRCA1-BARD1 complex

Inferred from sequence or structural similarity. Source: UniProtKB

centrosome

Traceable author statement PubMed 10855792. Source: UniProtKB

chromosome

Inferred from direct assay Ref.11Ref.10. Source: UniProtKB

condensed chromosome

Inferred from direct assay PubMed 12913077. Source: MGI

condensed nuclear chromosome

Inferred from direct assay PubMed 20551173. Source: MGI

cytoplasm

Inferred from direct assay PubMed 11172592. Source: MGI

nucleoplasm

Traceable author statement. Source: Reactome

ribonucleoprotein complex

Inferred from sequence orthology PubMed 18809582. Source: MGI

   Molecular_functionRNA binding

Inferred from sequence orthology PubMed 12419249. Source: MGI

damaged DNA binding

Inferred from direct assay PubMed 11934988. Source: MGI

transcription regulatory region DNA binding

Inferred from direct assay PubMed 20820192. Source: BHF-UCL

ubiquitin-protein ligase activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18121812Breast cancer type 1 susceptibility protein homolog
PRO_0000055832

Regions

Domain1585 – 167995BRCT 1
Domain1698 – 1797100BRCT 2
Zinc finger24 – 6542RING-type
Region1353 – 138028Interaction with PALB2 By similarity
Compositional bias1562 – 15676Poly-Ala

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue1141Phosphoserine By similarity
Modified residue3051Phosphoserine By similarity
Modified residue3921Phosphoserine By similarity
Modified residue6861Phosphoserine By similarity
Modified residue8311Phosphoserine Ref.9
Modified residue9711Phosphoserine; by CHEK2 By similarity
Modified residue11741Phosphoserine By similarity
Modified residue11801Phosphoserine By similarity
Modified residue12411Phosphoserine By similarity
Modified residue12971Phosphoserine By similarity
Modified residue13031Phosphoserine By similarity
Modified residue13431Phosphoserine By similarity
Modified residue13501Phosphothreonine By similarity
Modified residue14131Phosphoserine By similarity
Modified residue14811Phosphoserine By similarity

Experimental info

Sequence conflict931F → L in AAA96393. Ref.3
Sequence conflict3051S → T in AAB17113. Ref.2
Sequence conflict3191A → P in AAB17113. Ref.2
Sequence conflict3771Q → E in AAA96393. Ref.3
Sequence conflict5501K → Q in AAA96393. Ref.3
Sequence conflict6521P → A in AAB17113. Ref.2
Sequence conflict7651S → P in AAA96393. Ref.3
Sequence conflict7651S → P in AAC52323. Ref.4
Sequence conflict9171P → L in AAA96393. Ref.3
Sequence conflict9331C → S in AAA96393. Ref.3
Sequence conflict9331C → S in AAA99742. Ref.7
Sequence conflict10911C → R in AAB17114. Ref.1
Sequence conflict11221I → K in AAB17113. Ref.2
Sequence conflict12061S → R in AAA96393. Ref.3
Sequence conflict1212 – 12132RM → GI in AAA96393. Ref.3
Sequence conflict12551S → R in AAA96393. Ref.3
Sequence conflict12611H → N in AAA96393. Ref.3
Sequence conflict12641A → V in AAB17113. Ref.2
Sequence conflict12691A → P in AAB17113. Ref.2
Sequence conflict12831K → T in AAB17113. Ref.2
Sequence conflict13371N → T in AAB17113. Ref.2
Sequence conflict13491T → P in AAB17113. Ref.2
Sequence conflict1352 – 13532QR → EG in AAB17113. Ref.2
Sequence conflict13811P → S in AAB17113. Ref.2
Sequence conflict13901A → G in AAB17113. Ref.2
Sequence conflict14001D → V in AAB17113. Ref.2
Sequence conflict15031Q → E in AAB17113. Ref.2
Sequence conflict15491A → V in AAB17113. Ref.2
Sequence conflict16801K → T in AAB17113. Ref.2
Sequence conflict17121E → D in AAB17113. Ref.2
Sequence conflict17211E → D in AAB17113. Ref.2
Sequence conflict17911D → G in AAB17114. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P48754 [UniParc].

Last modified October 3, 2012. Version 3.
Checksum: 2B47FB55B149FD71

FASTA1,812198,795
        10         20         30         40         50         60 
MDLSAVQIQE VQNVLHAMQK ILECPICLEL IKEPVSTKCD HIFCKFCMLK LLNQKKGPSQ 

        70         80         90        100        110        120 
CPLCKNEITK RSLQGSTRFS QLAEELLRIM AAFELDTGMQ LTNGFSFSKK RNNSCERLNE 

       130        140        150        160        170        180 
EASIIQSVGY RNRVRRLPQV EPGNATLKDS LGVQLSNLGI VRSVKKNRQT QPRKKSVYIE 

       190        200        210        220        230        240 
LDSDSSEETV TKPGDCSVRD QELLQTAPQE AGDEGKLHSA EEAACEFSEG IRNIEHHQCS 

       250        260        270        280        290        300 
DDLNPTENHA TERHPEKCQS ISISNVCVEP CGTDAHASSL QPETSSLLLI EDRMNAEKAE 

       310        320        330        340        350        360 
FCNKSKQPGI AVSQQSRWAA SKGTCNDRQV PSTGEKVGPN ADSLSDREKW THPQSLCPEN 

       370        380        390        400        410        420 
SGATTDVPWI TLNSSVQKVN EWFSRTGEML TSDSASARRH ESNAEAAVVL EVSNEVDGGF 

       430        440        450        460        470        480 
SSSRKTDLVT PDPHHTLMCK SGRDFSKPVE DNISDKIFGK SYQRKGSRPH LNHVTEIIGT 

       490        500        510        520        530        540 
FITEPQITQE QPFTNKLKRK RSTSLQPEDF IKKADSAGVQ RTPDNINQGT DLMEPNEQAV 

       550        560        570        580        590        600 
STTSNCQENK IAGSNLQKEK SAHPTESLRK EPASTAGAKS ISNSVSDLEV ELNVHSSKAP 

       610        620        630        640        650        660 
KKNRLRRKSS IRCALPLEPI SRNPSPPTCA ELQIDSCGSS EETKKNHSNQ QPAGHLREPQ 

       670        680        690        700        710        720 
LIEDTEPAAD AKKNEPNEHI RKRRASDAFP EEKLMNKAGL LTSCSSPRKS QGPVNPSPQR 

       730        740        750        760        770        780 
TGTEQLETRQ MSDSAKELGD RVLGGEPSGK TTDRSEESTS VSLVSDTDYD TQNSVSVLDA 

       790        800        810        820        830        840 
HTVRYARTGS AQCMTQFVAS ENPKELVHGS NNAGSGTEGL KPPLRHALNL SQEKVEMEDS 

       850        860        870        880        890        900 
ELDTQYLQNT FQVSKRQSFA LFSKPRSPQK DCAHSVPSKE LSPKVTAKGK QKERQGQEEF 

       910        920        930        940        950        960 
EISHVQAVAA TVGLPVPCQE GKLAADTMCD RGCRLCPSSH YRSGENGLSA TGKSGISQNS 

       970        980        990       1000       1010       1020 
HFKQSVSPIR SSIKTDNRKP LTEGRFERHT SSTEMAVGNE NILQSTVHTV SLNNRGNACQ 

      1030       1040       1050       1060       1070       1080 
EAGSGSIHEV CSTGDSFPGQ LGRNRGPKVN TVPPLDSMQP GVCQQSVPVS DKYLEIKKQE 

      1090       1100       1110       1120       1130       1140 
GEAVCADFSP CLFSDHLEQS MSGKVFQVCS ETPDDLLDDV EIQGHTSFGE GDIMERSAVF 

      1150       1160       1170       1180       1190       1200 
NGSILRRESS RSPSPVTHAS KSQSLHRASR KLESSEESDS TEDEDLPCFQ HLLSRISNTP 

      1210       1220       1230       1240       1250       1260 
ELTRCSSAVT QRMPEKAEGT QAPWKGSSSD CNNEVIMIEA SQEHQFSEDP RCSGSMFSSQ 

      1270       1280       1290       1300       1310       1320 
HSAAQGSTAN ANSQDSNFIP PSKQRSHQCG NEEAFLSDKE LISDNEEMAT CLEEDNDQEE 

      1330       1340       1350       1360       1370       1380 
DSIIPDSEAS GYESETNLSE DCSQSDILTT QQRATMKYNL IKLQQEMAHL EAVLEQRGNQ 

      1390       1400       1410       1420       1430       1440 
PSGHSPSLLA DPCALEDLPD LEPNMSGAAI LTSKNINENP VSQNLKSACD DKFQLQHLEG 

      1450       1460       1470       1480       1490       1500 
PTSGDDESGM GRPSPFKSPL AGSRGSAHGC SRHLQKRNSP SQEELLQPAG SEASSEPHNS 

      1510       1520       1530       1540       1550       1560 
TGQSCLPRRE LEGTPYLGSG ISLFSSRDPE SESPKEPAHI GTTPASTSAL KIPQGQVAFR 

      1570       1580       1590       1600       1610       1620 
SAAAAGADKA VVGIVSKIKP ELTSSEERAD RDISMVVSGL TPKEVMTVQK FAEKYRLTLT 

      1630       1640       1650       1660       1670       1680 
DAITEETTHV IIKTDAEFVC ERTLKYFLGI AGGKWIVSYS WVVRSIQERR LLNVHEFEVK 

      1690       1700       1710       1720       1730       1740 
GDVVTGRNHQ GPRRSRESRE KLFKGLQVYC CEPFTNMPKD ELERMLQLCG ASVVKELPSL 

      1750       1760       1770       1780       1790       1800 
THDTGAHLVV IVQPSAWTED SNCPDIGQLC KARLVMWDWV LDSLSSYRCR DLDAYLVQNI 

      1810 
TCDSSEPQDS ND 

« Hide

References

« Hide 'large scale' references
[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]"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].
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI49350.
RefSeqNP_033894.3. NM_009764.3.
UniGeneMm.244975.

3D structure databases

ProteinModelPortalP48754.
SMRP48754. Positions 1-103, 1588-1798.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198383. 20 interactions.
DIPDIP-41981N.
IntActP48754. 2 interactions.
STRING10090.ENSMUSP00000102847.

PTM databases

PhosphoSiteP48754.

Proteomic databases

PRIDEP48754.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000017290; ENSMUSP00000017290; ENSMUSG00000017146.
GeneID12189.
KEGGmmu:12189.
UCSCuc007lpd.2. mouse.

Organism-specific databases

CTD672.
MGIMGI:104537. Brca1.

Phylogenomic databases

eggNOGNOG274496.
GeneTreeENSGT00440000034289.
HOGENOMHOG000230969.
HOVERGENHBG050730.
InParanoidP48754.
KOK10605.
OMAKGPSQCP.
OrthoDBEOG79CXXK.
TreeFamTF105060.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.
REACT_198624. Meiosis.
REACT_27235. Meiotic Recombination.
REACT_75800. Meiotic Synapsis.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressP48754.
CleanExMM_BRCA1.
GenevestigatorP48754.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
3.40.50.10190. 2 hits.
InterProIPR011364. 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]
PANTHERPTHR13763. PTHR13763. 1 hit.
PfamPF00533. BRCT. 2 hits.
PF12820. BRCT_assoc. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
PIRSFPIRSF001734. BRCA1. 1 hit.
PRINTSPR00493. BRSTCANCERI.
SMARTSM00292. BRCT. 2 hits.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF52113. SSF52113. 2 hits.
PROSITEPS50172. BRCT. 2 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio280581.
PROP48754.
SOURCESearch...

Entry information

Entry nameBRCA1_MOUSE
AccessionPrimary (citable) accession number: P48754
Secondary accession number(s): A2A4Q4, Q60957, Q60983
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 3, 2012
Last modified: April 16, 2014
This is version 136 of the entry and version 3 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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