Breast cancer type 1 susceptibility protein homolog

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P48754 (BRCA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 128. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Breast cancer type 1 susceptibility protein homolog
EC=6.3.2.-

Gene names

Name:

Brca1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1812 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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 and COBRA1. Interacts (via BRCT domains) with BRIP1 (phosphorylated form). Interacts with FANCD2 (ubiquitinated form). Interacts with BAP1. Interacts with DCLRE1C and CLSPN. Interacts with H2AFX (phosphorylated on 'Ser-140'). Interacts with CHEK1 and CHEK2. Interacts with BRCC3. Interacts with AURKA. Interacts with UBXN1. Part of a trimeric 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. Interacts with KIAA0101/PAF15 By similarity. Interacts (via the BRCT domains) with ACACA (phosphorylated form); the interaction prevents dephosphorylation of ACACA. 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 process	Cell cycle DNA damage DNA recombination DNA repair Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Ubl conjugation pathway
Cellular component	Chromosome Nucleus
Disease	Tumor suppressor
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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 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 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_component	BRCA1-BARD1 complex Inferred from sequence or structural similarity. Source: UniProtKB centrosome Traceable author statement PubMed 10855792. Source: UniProtKB 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_function	RNA 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1812

1812

Breast cancer type 1 susceptibility protein homolog

PRO_0000055832

Regions

Domain

1585 – 1679

BRCT 1

Domain

1698 – 1797

100

BRCT 2

Zinc finger

24 – 65

RING-type

Region

1353 – 1380

Interaction with PALB2 By similarity

Compositional bias

1562 – 1567

Poly-Ala

Amino acid modifications

Modified residue

114

Phosphoserine By similarity

Modified residue

305

Phosphoserine By similarity

Modified residue

392

Phosphoserine By similarity

Modified residue

686

Phosphoserine By similarity

Modified residue

831

Phosphoserine Ref.9

Modified residue

957

Phosphoserine Ref.9

Modified residue

971

Phosphoserine; by CHEK2 By similarity

Modified residue

1174

Phosphoserine By similarity

Modified residue

1180

Phosphoserine By similarity

Modified residue

1241

Phosphoserine By similarity

Modified residue

1297

Phosphoserine By similarity

Modified residue

1343

Phosphoserine By similarity

Modified residue

1350

Phosphothreonine By similarity

Modified residue

1413

Phosphoserine By similarity

Modified residue

1481

Phosphoserine By similarity

Experimental info

Sequence conflict

F → L in AAA96393. Ref.3

Sequence conflict

305

S → T in AAB17113. Ref.2

Sequence conflict

319

A → P in AAB17113. Ref.2

Sequence conflict

377

Q → E in AAA96393. Ref.3

Sequence conflict

550

K → Q in AAA96393. Ref.3

Sequence conflict

652

P → A in AAB17113. Ref.2

Sequence conflict

765

S → P in AAA96393. Ref.3

Sequence conflict

765

S → P in AAC52323. Ref.4

Sequence conflict

917

P → L in AAA96393. Ref.3

Sequence conflict

933

C → S in AAA96393. Ref.3

Sequence conflict

933

C → S in AAA99742. Ref.7

Sequence conflict

1091

C → R in AAB17114. Ref.1

Sequence conflict

1122

I → K in AAB17113. Ref.2

Sequence conflict

1206

S → R in AAA96393. Ref.3

Sequence conflict

1212 – 1213

RM → GI in AAA96393. Ref.3

Sequence conflict

1255

S → R in AAA96393. Ref.3

Sequence conflict

1261

H → N in AAA96393. Ref.3

Sequence conflict

1264

A → V in AAB17113. Ref.2

Sequence conflict

1269

A → P in AAB17113. Ref.2

Sequence conflict

1283

K → T in AAB17113. Ref.2

Sequence conflict

1337

N → T in AAB17113. Ref.2

Sequence conflict

1349

T → P in AAB17113. Ref.2

Sequence conflict

1352 – 1353

QR → EG in AAB17113. Ref.2

Sequence conflict

1381

P → S in AAB17113. Ref.2

Sequence conflict

1390

A → G in AAB17113. Ref.2

Sequence conflict

1400

D → V in AAB17113. Ref.2

Sequence conflict

1503

Q → E in AAB17113. Ref.2

Sequence conflict

1549

A → V in AAB17113. Ref.2

Sequence conflict

1680

K → T in AAB17113. Ref.2

Sequence conflict

1712

E → D in AAB17113. Ref.2

Sequence conflict

1721

E → D in AAB17113. Ref.2

Sequence conflict

1791

D → G in AAB17114. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P48754 [UniParc].

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

FASTA

1,812

198,795

        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' referencesShow '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. 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 AND SER-957, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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.
IPI	IPI00331711. IPI00421063.
PIR	I49350.
RefSeq	NP_033894.3. NM_009764.3.
UniGene	Mm.244975.
3D structure databases
ProteinModelPortal	P48754.
SMR	P48754. Positions 1-103, 1588-1798.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-41981N.
STRING	10090.ENSMUSP00000102847.
PTM databases
PhosphoSite	P48754.
Proteomic databases
PRIDE	P48754.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000017290; ENSMUSP00000017290; ENSMUSG00000017146.
GeneID	12189.
KEGG	mmu:12189.
UCSC	uc007lpd.2. mouse.
Organism-specific databases
CTD	672.
MGI	MGI:104537. Brca1.
Phylogenomic databases
eggNOG	NOG274496.
GeneTree	ENSGT00440000034289.
HOGENOM	HOG000230969.
HOVERGEN	HBG050730.
InParanoid	P48754.
KO	K10605.
OMA	CMLKLLN.
OrthoDB	EOG42RD7C.
Enzyme and pathway databases
Reactome	REACT_118161. Cell Cycle. REACT_120463. Meiosis. REACT_27235. Meiotic Recombination (mouse). REACT_75800. Meiotic Synapsis (mouse).
UniPathway	UPA00143.
Gene expression databases
CleanEx	MM_BRCA1.
Genevestigator	P48754.
GermOnline	ENSMUSG00000017146. Mus musculus.
Family and domain databases
Gene3D	3.30.40.10. 1 hit. 3.40.50.10190. 2 hits.
InterPro	IPR011364. BRCA1. IPR025994. BRCA1_serine_dom. IPR001357. BRCT_dom. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. [Graphical view]
PANTHER	PTHR13763. PTHR13763. 1 hit.
Pfam	PF00533. BRCT. 2 hits. PF12820. BRCT_assoc. 1 hit. [Graphical view]
PIRSF	PIRSF001734. BRCA1. 1 hit.
PRINTS	PR00493. BRSTCANCERI.
SMART	SM00292. BRCT. 2 hits. SM00184. RING. 1 hit. [Graphical view]
SUPFAM	SSF52113. BRCT. 2 hits.
PROSITE	PS50172. BRCT. 2 hits. PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	280581.
SOURCE	Search...

Entry information

Entry name

BRCA1_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 128 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents