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Protein

Breast cancer type 1 susceptibility protein homolog

Gene

Brca1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Acts as a transcriptional activator (By similarity). Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation.By similarity1 Publication

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri24 – 65RING-typePROSITE-ProRule annotationAdd BLAST42

GO - Molecular functioni

GO - Biological processi

  • cellular response to DNA damage stimulus Source: MGI
  • cellular response to indole-3-methanol Source: MGI
  • cellular response to tumor necrosis factor Source: MGI
  • centrosome cycle Source: MGI
  • centrosome duplication Source: UniProtKB
  • chordate embryonic development Source: MGI
  • chromosome breakage Source: MGI
  • chromosome segregation Source: MGI
  • DNA replication Source: MGI
  • dosage compensation by inactivation of X chromosome Source: MGI
  • double-strand break repair Source: CACAO
  • double-strand break repair via homologous recombination Source: MGI
  • fatty acid biosynthetic process Source: UniProtKB-KW
  • G2 DNA damage checkpoint Source: Ensembl
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
  • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
  • negative regulation of fatty acid biosynthetic process Source: UniProtKB
  • negative regulation of histone acetylation Source: BHF-UCL
  • negative regulation of histone H3-K4 methylation Source: BHF-UCL
  • negative regulation of histone H3-K9 methylation Source: BHF-UCL
  • negative regulation of intracellular estrogen receptor signaling pathway Source: MGI
  • negative regulation of reactive oxygen species metabolic process Source: MGI
  • negative regulation of transcription, DNA-templated Source: MGI
  • positive regulation of angiogenesis Source: MGI
  • positive regulation of cell cycle arrest Source: MGI
  • positive regulation of DNA repair Source: MGI
  • positive regulation of gene expression Source: MGI
  • positive regulation of histone acetylation Source: BHF-UCL
  • positive regulation of histone H3-K4 methylation Source: BHF-UCL
  • positive regulation of histone H3-K9 acetylation Source: BHF-UCL
  • positive regulation of histone H3-K9 methylation Source: BHF-UCL
  • positive regulation of histone H4-K16 acetylation Source: BHF-UCL
  • positive regulation of histone H4-K20 methylation Source: BHF-UCL
  • positive regulation of protein ubiquitination Source: MGI
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of vascular endothelial growth factor production Source: MGI
  • postreplication repair Source: MGI
  • protein autoubiquitination Source: UniProtKB
  • protein K6-linked ubiquitination Source: UniProtKB
  • protein ubiquitination Source: MGI
  • regulation of cell proliferation Source: GO_Central
  • regulation of DNA methylation Source: BHF-UCL
  • regulation of gene expression by genetic imprinting Source: BHF-UCL
  • response to estrogen Source: MGI
  • response to ionizing radiation Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Transferase

Keywords - Biological processi

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

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-5685938. HDR through Single Strand Annealing (SSA).
R-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5689901. Metalloprotease DUBs.
R-MMU-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-MMU-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-MMU-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-MMU-5693571. Nonhomologous End-Joining (NHEJ).
R-MMU-5693579. Homologous DNA Pairing and Strand Exchange.
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-69473. G2/M DNA damage checkpoint.
R-MMU-912446. Meiotic recombination.
R-MMU-912497. Meiotic Recombination.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Breast cancer type 1 susceptibility protein homolog (EC:2.3.2.27By similarity)
Alternative name(s):
RING-type E3 ubiquitin transferase BRCA1Curated
Gene namesi
Name:Brca1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:104537. Brca1.

Subcellular locationi

GO - Cellular componenti

  • BRCA1-A complex Source: MGI
  • BRCA1-BARD1 complex Source: UniProtKB
  • centrosome Source: UniProtKB
  • chromosome Source: UniProtKB
  • condensed chromosome Source: MGI
  • condensed nuclear chromosome Source: MGI
  • cytoplasm Source: MGI
  • intracellular ribonucleoprotein complex Source: MGI
  • lateral element Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
  • plasma membrane Source: MGI
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000558321 – 1812Breast cancer type 1 susceptibility protein homologAdd BLAST1812

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei114PhosphoserineBy similarity1
Modified residuei305PhosphoserineBy similarity1
Cross-linki336Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei392PhosphoserineBy similarity1
Cross-linki440Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki456Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei686PhosphoserineBy similarity1
Modified residuei706PhosphoserineCombined sources1
Modified residuei717PhosphoserineCombined sources1
Modified residuei831PhosphoserineCombined sources1
Modified residuei971Phosphoserine; by CHEK2By similarity1
Modified residuei992PhosphoserineBy similarity1
Modified residuei1152PhosphoserineBy similarity1
Modified residuei1154PhosphoserineBy similarity1
Modified residuei1174PhosphoserineBy similarity1
Modified residuei1180PhosphoserineBy similarity1
Modified residuei1241PhosphoserineBy similarity1
Modified residuei1297PhosphoserineBy similarity1
Modified residuei1303PhosphoserineBy similarity1
Modified residuei1343PhosphoserineBy similarity1
Modified residuei1350PhosphothreonineBy similarity1
Modified residuei1413PhosphoserineBy similarity1
Modified residuei1481PhosphoserineBy similarity1
Modified residuei1495PhosphoserineBy similarity1

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP48754.
MaxQBiP48754.
PaxDbiP48754.
PeptideAtlasiP48754.
PRIDEiP48754.

PTM databases

iPTMnetiP48754.
PhosphoSitePlusiP48754.

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

BgeeiENSMUSG00000017146.
CleanExiMM_BRCA1.
ExpressionAtlasiP48754. baseline and differential.
GenevisibleiP48754. MM.

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 BRCA1, BARD1, UIMC1/RAP80, FAM175A/Abraxas, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1. Interacts (via the BRCT domains) with FAM175A (phosphorylated form); this is important for recruitment to sites of DNA damage. Can form a heterotetramer with two molecules of FAM175A (phosphorylated form). 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. Interacts (via the BRCT domains) with CCAR2 (via N-terminus); the interaction represses the transcriptional activator activity of BRCA1 (By similarity). Interacts with EXD2 (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198383. 41 interactors.
DIPiDIP-41981N.
IntActiP48754. 15 interactors.
STRINGi10090.ENSMUSP00000017290.

Structurei

3D structure databases

ProteinModelPortaliP48754.
SMRiP48754.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1585 – 1679BRCT 1PROSITE-ProRule annotationAdd BLAST95
Domaini1698 – 1797BRCT 2PROSITE-ProRule annotationAdd BLAST100

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1353 – 1380Interaction with PALB2By similarityAdd BLAST28

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1562 – 1567Poly-Ala6

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
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)DescriptionActionsGraphical viewLength
Zinc fingeri24 – 65RING-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITQ6. Eukaryota.
ENOG4111WR7. LUCA.
GeneTreeiENSGT00440000034289.
HOGENOMiHOG000230969.
HOVERGENiHBG050730.
InParanoidiP48754.
KOiK10605.
OMAiFQHLLFG.
OrthoDBiEOG091G0670.
TreeFamiTF105060.

Family and domain databases

CDDicd00027. BRCT. 2 hits.
Gene3Di3.30.40.10. 1 hit.
3.40.50.10190. 2 hits.
InterProiIPR011364. BRCA1.
IPR031099. BRCA1-associated.
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.
PTHR13763:SF0. PTHR13763:SF0. 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

        10         20         30         40         50
MDLSAVQIQE VQNVLHAMQK ILECPICLEL IKEPVSTKCD HIFCKFCMLK
60 70 80 90 100
LLNQKKGPSQ CPLCKNEITK RSLQGSTRFS QLAEELLRIM AAFELDTGMQ
110 120 130 140 150
LTNGFSFSKK RNNSCERLNE EASIIQSVGY RNRVRRLPQV EPGNATLKDS
160 170 180 190 200
LGVQLSNLGI VRSVKKNRQT QPRKKSVYIE LDSDSSEETV TKPGDCSVRD
210 220 230 240 250
QELLQTAPQE AGDEGKLHSA EEAACEFSEG IRNIEHHQCS DDLNPTENHA
260 270 280 290 300
TERHPEKCQS ISISNVCVEP CGTDAHASSL QPETSSLLLI EDRMNAEKAE
310 320 330 340 350
FCNKSKQPGI AVSQQSRWAA SKGTCNDRQV PSTGEKVGPN ADSLSDREKW
360 370 380 390 400
THPQSLCPEN SGATTDVPWI TLNSSVQKVN EWFSRTGEML TSDSASARRH
410 420 430 440 450
ESNAEAAVVL EVSNEVDGGF SSSRKTDLVT PDPHHTLMCK SGRDFSKPVE
460 470 480 490 500
DNISDKIFGK SYQRKGSRPH LNHVTEIIGT FITEPQITQE QPFTNKLKRK
510 520 530 540 550
RSTSLQPEDF IKKADSAGVQ RTPDNINQGT DLMEPNEQAV STTSNCQENK
560 570 580 590 600
IAGSNLQKEK SAHPTESLRK EPASTAGAKS ISNSVSDLEV ELNVHSSKAP
610 620 630 640 650
KKNRLRRKSS IRCALPLEPI SRNPSPPTCA ELQIDSCGSS EETKKNHSNQ
660 670 680 690 700
QPAGHLREPQ LIEDTEPAAD AKKNEPNEHI RKRRASDAFP EEKLMNKAGL
710 720 730 740 750
LTSCSSPRKS QGPVNPSPQR TGTEQLETRQ MSDSAKELGD RVLGGEPSGK
760 770 780 790 800
TTDRSEESTS VSLVSDTDYD TQNSVSVLDA HTVRYARTGS AQCMTQFVAS
810 820 830 840 850
ENPKELVHGS NNAGSGTEGL KPPLRHALNL SQEKVEMEDS ELDTQYLQNT
860 870 880 890 900
FQVSKRQSFA LFSKPRSPQK DCAHSVPSKE LSPKVTAKGK QKERQGQEEF
910 920 930 940 950
EISHVQAVAA TVGLPVPCQE GKLAADTMCD RGCRLCPSSH YRSGENGLSA
960 970 980 990 1000
TGKSGISQNS HFKQSVSPIR SSIKTDNRKP LTEGRFERHT SSTEMAVGNE
1010 1020 1030 1040 1050
NILQSTVHTV SLNNRGNACQ EAGSGSIHEV CSTGDSFPGQ LGRNRGPKVN
1060 1070 1080 1090 1100
TVPPLDSMQP GVCQQSVPVS DKYLEIKKQE GEAVCADFSP CLFSDHLEQS
1110 1120 1130 1140 1150
MSGKVFQVCS ETPDDLLDDV EIQGHTSFGE GDIMERSAVF NGSILRRESS
1160 1170 1180 1190 1200
RSPSPVTHAS KSQSLHRASR KLESSEESDS TEDEDLPCFQ HLLSRISNTP
1210 1220 1230 1240 1250
ELTRCSSAVT QRMPEKAEGT QAPWKGSSSD CNNEVIMIEA SQEHQFSEDP
1260 1270 1280 1290 1300
RCSGSMFSSQ HSAAQGSTAN ANSQDSNFIP PSKQRSHQCG NEEAFLSDKE
1310 1320 1330 1340 1350
LISDNEEMAT CLEEDNDQEE DSIIPDSEAS GYESETNLSE DCSQSDILTT
1360 1370 1380 1390 1400
QQRATMKYNL IKLQQEMAHL EAVLEQRGNQ PSGHSPSLLA DPCALEDLPD
1410 1420 1430 1440 1450
LEPNMSGAAI LTSKNINENP VSQNLKSACD DKFQLQHLEG PTSGDDESGM
1460 1470 1480 1490 1500
GRPSPFKSPL AGSRGSAHGC SRHLQKRNSP SQEELLQPAG SEASSEPHNS
1510 1520 1530 1540 1550
TGQSCLPRRE LEGTPYLGSG ISLFSSRDPE SESPKEPAHI GTTPASTSAL
1560 1570 1580 1590 1600
KIPQGQVAFR SAAAAGADKA VVGIVSKIKP ELTSSEERAD RDISMVVSGL
1610 1620 1630 1640 1650
TPKEVMTVQK FAEKYRLTLT DAITEETTHV IIKTDAEFVC ERTLKYFLGI
1660 1670 1680 1690 1700
AGGKWIVSYS WVVRSIQERR LLNVHEFEVK GDVVTGRNHQ GPRRSRESRE
1710 1720 1730 1740 1750
KLFKGLQVYC CEPFTNMPKD ELERMLQLCG ASVVKELPSL THDTGAHLVV
1760 1770 1780 1790 1800
IVQPSAWTED SNCPDIGQLC KARLVMWDWV LDSLSSYRCR DLDAYLVQNI
1810
TCDSSEPQDS ND
Length:1,812
Mass (Da):198,795
Last modified:October 3, 2012 - v3
Checksum:i2B47FB55B149FD71
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti93F → L in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti305S → T in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti319A → P in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti377Q → E in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti550K → Q in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti652P → A in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti765S → P in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti765S → P in AAC52323 (PubMed:7590247).Curated1
Sequence conflicti917P → L in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti933C → S in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti933C → S in AAA99742 (PubMed:8566965).Curated1
Sequence conflicti1091C → R in AAB17114 (PubMed:8634697).Curated1
Sequence conflicti1122I → K in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1206S → R in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti1212 – 1213RM → GI in AAA96393 (PubMed:8575748).Curated2
Sequence conflicti1255S → R in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti1261H → N in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti1264A → V in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1269A → P in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1283K → T in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1337N → T in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1349T → P in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1352 – 1353QR → EG in AAB17113 (PubMed:8634698).Curated2
Sequence conflicti1381P → S in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1390A → G in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1400D → V in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1503Q → E in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1549A → V in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1680K → T in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1712E → D in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1721E → D in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1791D → G in AAB17114 (PubMed:8634697).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP48754.
SMRiP48754.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198383. 41 interactors.
DIPiDIP-41981N.
IntActiP48754. 15 interactors.
STRINGi10090.ENSMUSP00000017290.

PTM databases

iPTMnetiP48754.
PhosphoSitePlusiP48754.

Proteomic databases

EPDiP48754.
MaxQBiP48754.
PaxDbiP48754.
PeptideAtlasiP48754.
PRIDEiP48754.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi672.
MGIiMGI:104537. Brca1.

Phylogenomic databases

eggNOGiENOG410ITQ6. Eukaryota.
ENOG4111WR7. LUCA.
GeneTreeiENSGT00440000034289.
HOGENOMiHOG000230969.
HOVERGENiHBG050730.
InParanoidiP48754.
KOiK10605.
OMAiFQHLLFG.
OrthoDBiEOG091G0670.
TreeFamiTF105060.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-5685938. HDR through Single Strand Annealing (SSA).
R-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5689901. Metalloprotease DUBs.
R-MMU-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-MMU-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-MMU-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-MMU-5693571. Nonhomologous End-Joining (NHEJ).
R-MMU-5693579. Homologous DNA Pairing and Strand Exchange.
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-69473. G2/M DNA damage checkpoint.
R-MMU-912446. Meiotic recombination.
R-MMU-912497. Meiotic Recombination.

Miscellaneous databases

PROiP48754.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000017146.
CleanExiMM_BRCA1.
ExpressionAtlasiP48754. baseline and differential.
GenevisibleiP48754. MM.

Family and domain databases

CDDicd00027. BRCT. 2 hits.
Gene3Di3.30.40.10. 1 hit.
3.40.50.10190. 2 hits.
InterProiIPR011364. BRCA1.
IPR031099. BRCA1-associated.
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.
PTHR13763:SF0. PTHR13763:SF0. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 165 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.