UniProtKB - P48754 (BRCA1_MOUSE)
Breast cancer type 1 susceptibility protein homolog
Brca1
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 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 appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Required for FANCD2 targeting to sites of DNA damage. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. 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 similarityCatalytic 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 EC:2.3.2.27
: protein ubiquitination Pathwayi
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 24 – 65 | RING-typePROSITE-ProRule annotationAdd BLAST | 42 |
GO - Molecular functioni
- chromatin binding Source: MGI
- damaged DNA binding Source: MGI
- enzyme binding Source: MGI
- RNA binding Source: MGI
- RNA polymerase binding Source: UniProtKB
- transcription cis-regulatory region binding Source: BHF-UCL
- transcription coactivator activity Source: UniProtKB
- ubiquitin protein ligase binding Source: MGI
- ubiquitin-protein transferase activity Source: UniProtKB
- zinc ion binding Source: InterPro
GO - Biological processi
- cellular response to DNA damage stimulus Source: MGI
- cellular response to indole-3-methanol Source: MGI
- cellular response to ionizing radiation Source: Ensembl
- cellular response to tumor necrosis factor Source: MGI
- centrosome cycle Source: MGI
- centrosome duplication Source: UniProtKB
- chordate embryonic development Source: MGI
- chromosome segregation 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
- intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
- mitotic G2/M transition checkpoint Source: MGI
- mitotic G2 DNA damage checkpoint signaling 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 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 import into nucleus Source: MGI
- positive regulation of protein ubiquitination Source: MGI
- positive regulation of transcription, DNA-templated Source: UniProtKB
- positive regulation of transcription by RNA polymerase II 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 cycle Source: MGI
- regulation of DNA methylation Source: BHF-UCL
- regulation of gene expression by genetic imprinting Source: BHF-UCL
- regulation of transcription by RNA polymerase II Source: UniProtKB
- response to estrogen Source: MGI
- response to ionizing radiation Source: MGI
Keywordsi
Molecular function | Activator, DNA-binding, Transferase |
Biological process | Cell cycle, DNA damage, DNA recombination, DNA repair, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transcription, Transcription regulation, Ubl conjugation pathway |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
Reactomei | R-MMU-3108214, SUMOylation of DNA damage response and repair proteins |
UniPathwayi | UPA00143 |
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 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:104537, Brca1 |
VEuPathDBi | HostDB:ENSMUSG00000017146 |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm By similarity
Nucleus
- Nucleus By similarity
Other locations
- 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. Translocated to the cytoplasm during UV-induced apoptosis.By similarity
Cytoskeleton
- centrosome Source: UniProtKB
Mitochondrion
- mitochondrial matrix Source: MGI
Nucleus
- BRCA1-A complex Source: MGI
- BRCA1-B complex Source: Ensembl
- BRCA1-BARD1 complex Source: UniProtKB
- BRCA1-C complex Source: Ensembl
- condensed nuclear chromosome Source: MGI
- lateral element Source: MGI
- nuclear body Source: MGI
- nucleoplasm Source: MGI
- nucleus Source: MGI
Plasma Membrane
- plasma membrane Source: MGI
Other locations
- chromosome Source: UniProtKB
- condensed chromosome Source: MGI
- cytoplasm Source: MGI
- DNA repair complex Source: Ensembl
- protein-containing complex Source: MGI
- ribonucleoprotein complex Source: MGI
Keywords - Cellular componenti
Chromosome, Cytoplasm, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000055832 | 1 – 1812 | Breast cancer type 1 susceptibility protein homologAdd BLAST | 1812 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionineBy similarity | 1 | |
Cross-linki | 109 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 114 | PhosphoserineBy similarity | 1 | |
Cross-linki | 298 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 336 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 392 | PhosphoserineBy similarity | 1 | |
Cross-linki | 440 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 456 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 512 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 686 | PhosphoserineBy similarity | 1 | |
Modified residuei | 706 | PhosphoserineCombined sources | 1 | |
Modified residuei | 717 | PhosphoserineCombined sources | 1 | |
Modified residuei | 831 | PhosphoserineCombined sources | 1 | |
Modified residuei | 971 | Phosphoserine; by CHEK2By similarity | 1 | |
Modified residuei | 992 | PhosphoserineBy similarity | 1 | |
Cross-linki | 1048 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 1152 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1154 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1174 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1180 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1241 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1297 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1303 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1343 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1350 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 1413 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1481 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1495 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | P48754 |
jPOSTi | P48754 |
MaxQBi | P48754 |
PaxDbi | P48754 |
PeptideAtlasi | P48754 |
PRIDEi | P48754 |
ProteomicsDBi | 273840 |
PTM databases
iPTMneti | P48754 |
PhosphoSitePlusi | P48754 |
Expressioni
Tissue specificityi
Developmental stagei
Gene expression databases
Bgeei | ENSMUSG00000017146, Expressed in secondary oocyte and 268 other tissues |
ExpressionAtlasi | P48754, baseline and differential |
Genevisiblei | P48754, 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, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1.
Interacts (via the BRCT domains) with ABRAXAS1 (phosphorylated form); this is important for recruitment to sites of DNA damage. Can form a heterotetramer with two molecules of ABRAXAS1 (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, NELFB, DCLRE1C, CLSPN. CHEK1, CHEK2, BAP1, BRCC3, UBXN1 and PCLAF.
Interacts (via BRCT domains) with BRIP1 (phosphorylated form).
Interacts with FANCD2 (ubiquitinated form).
Interacts with H2AX (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).
Interacts (via C-terminus) with DHX9; this interaction is direct and links BRCA1 to the RNA polymerase II holoenzyme (By similarity).
By similarity1 PublicationGO - Molecular functioni
- enzyme binding Source: MGI
- RNA polymerase binding Source: UniProtKB
- ubiquitin protein ligase binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 198383, 46 interactors |
ComplexPortali | CPX-4701, BRCA1-BARD1 complex CPX-972, BRCC ubiquitin ligase complex |
DIPi | DIP-41981N |
IntActi | P48754, 21 interactors |
MINTi | P48754 |
STRINGi | 10090.ENSMUSP00000017290 |
Miscellaneous databases
RNActi | P48754, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1585 – 1679 | BRCT 1PROSITE-ProRule annotationAdd BLAST | 95 | |
Domaini | 1698 – 1797 | BRCT 2PROSITE-ProRule annotationAdd BLAST | 100 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 165 – 198 | DisorderedSequence analysisAdd BLAST | 34 | |
Regioni | 321 – 362 | DisorderedSequence analysisAdd BLAST | 42 | |
Regioni | 492 – 581 | DisorderedSequence analysisAdd BLAST | 90 | |
Regioni | 640 – 767 | DisorderedSequence analysisAdd BLAST | 128 | |
Regioni | 864 – 899 | DisorderedSequence analysisAdd BLAST | 36 | |
Regioni | 947 – 995 | DisorderedSequence analysisAdd BLAST | 49 | |
Regioni | 1030 – 1056 | DisorderedSequence analysisAdd BLAST | 27 | |
Regioni | 1147 – 1185 | DisorderedSequence analysisAdd BLAST | 39 | |
Regioni | 1205 – 1230 | DisorderedSequence analysisAdd BLAST | 26 | |
Regioni | 1244 – 1289 | DisorderedSequence analysisAdd BLAST | 46 | |
Regioni | 1313 – 1343 | DisorderedSequence analysisAdd BLAST | 31 | |
Regioni | 1353 – 1380 | Interaction with PALB2By similarityAdd BLAST | 28 | |
Regioni | 1437 – 1547 | DisorderedSequence analysisAdd BLAST | 111 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 173 – 195 | Basic and acidic residuesSequence analysisAdd BLAST | 23 | |
Compositional biasi | 321 – 339 | Polar residuesSequence analysisAdd BLAST | 19 | |
Compositional biasi | 494 – 508 | Basic and acidic residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 520 – 561 | Polar residuesSequence analysisAdd BLAST | 42 | |
Compositional biasi | 640 – 655 | Polar residuesSequence analysisAdd BLAST | 16 | |
Compositional biasi | 659 – 691 | Basic and acidic residuesSequence analysisAdd BLAST | 33 | |
Compositional biasi | 699 – 729 | Polar residuesSequence analysisAdd BLAST | 31 | |
Compositional biasi | 885 – 899 | Basic and acidic residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 947 – 975 | Polar residuesSequence analysisAdd BLAST | 29 | |
Compositional biasi | 976 – 990 | Basic and acidic residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 1147 – 1163 | Polar residuesSequence analysisAdd BLAST | 17 | |
Compositional biasi | 1247 – 1289 | Polar residuesSequence analysisAdd BLAST | 43 | |
Compositional biasi | 1329 – 1343 | Polar residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 1472 – 1507 | Polar residuesSequence analysisAdd BLAST | 36 |
Domaini
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 24 – 65 | RING-typePROSITE-ProRule annotationAdd BLAST | 42 |
Keywords - Domaini
Repeat, Zinc-fingerPhylogenomic databases
eggNOGi | KOG4362, Eukaryota |
GeneTreei | ENSGT00440000034289 |
HOGENOMi | CLU_002290_0_0_1 |
InParanoidi | P48754 |
OMAi | NKQKPPC |
OrthoDBi | 496760at2759 |
PhylomeDBi | P48754 |
TreeFami | TF105060 |
Family and domain databases
Gene3Di | 3.30.40.10, 1 hit 3.40.50.10190, 2 hits |
InterProi | View protein in InterPro IPR011364, BRCA1 IPR031099, BRCA1-associated IPR025994, BRCA1_serine_dom IPR001357, BRCT_dom IPR036420, BRCT_dom_sf IPR018957, Znf_C3HC4_RING-type IPR001841, Znf_RING IPR013083, Znf_RING/FYVE/PHD IPR017907, Znf_RING_CS |
PANTHERi | PTHR13763, PTHR13763, 1 hit |
Pfami | View protein in Pfam PF00533, BRCT, 2 hits PF12820, BRCT_assoc, 1 hit PF00097, zf-C3HC4, 1 hit |
PIRSFi | PIRSF001734, BRCA1, 1 hit |
PRINTSi | PR00493, BRSTCANCERI |
SMARTi | View protein in SMART SM00292, BRCT, 2 hits SM00184, RING, 1 hit |
SUPFAMi | SSF52113, SSF52113, 2 hits |
PROSITEi | View protein in PROSITE PS50172, BRCT, 2 hits PS00518, ZF_RING_1, 1 hit PS50089, ZF_RING_2, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All
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
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A087WPK5 | A0A087WPK5_MOUSE | Breast cancer type 1 susceptibility... | Brca1 | 75 | Annotation score: | ||
A0A087WPE1 | A0A087WPE1_MOUSE | Breast cancer type 1 susceptibility... | Brca1 | 177 | Annotation score: | ||
A0A087WP26 | A0A087WP26_MOUSE | Breast cancer type 1 susceptibility... | Brca1 | 79 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 93 | F → L in AAA96393 (PubMed:8575748).Curated | 1 | |
Sequence conflicti | 305 | S → T in AAB17113 (PubMed:8634698).Curated | 1 | |
Sequence conflicti | 319 | A → P in AAB17113 (PubMed:8634698).Curated | 1 | |
Sequence conflicti | 377 | Q → E in AAA96393 (PubMed:8575748).Curated | 1 | |
Sequence conflicti | 550 | K → Q in AAA96393 (PubMed:8575748).Curated | 1 | |
Sequence conflicti | 652 | P → A in AAB17113 (PubMed:8634698).Curated | 1 | |
Sequence conflicti | 765 | S → P in AAA96393 (PubMed:8575748).Curated | 1 | |
Sequence conflicti | 765 | S → P in AAC52323 (PubMed:7590247).Curated | 1 | |
Sequence conflicti | 917 | P → L in AAA96393 (PubMed:8575748).Curated | 1 | |
Sequence conflicti | 933 | C → S in AAA96393 (PubMed:8575748).Curated | 1 | |
Sequence conflicti | 933 | C → S in AAA99742 (PubMed:8566965).Curated | 1 | |
Sequence conflicti | 1091 | C → R in AAB17114 (PubMed:8634697).Curated | 1 | |
Sequence conflicti | 1122 | I → K in AAB17113 (PubMed:8634698).Curated | 1 | |
Sequence conflicti | 1206 | S → R in AAA96393 (PubMed:8575748).Curated | 1 | |
Sequence conflicti | 1212 – 1213 | RM → GI in AAA96393 (PubMed:8575748).Curated | 2 | |
Sequence conflicti | 1255 | S → R in AAA96393 (PubMed:8575748).Curated | 1 | |
Sequence conflicti | 1261 | H → N in AAA96393 (PubMed:8575748).Curated | 1 | |
Sequence conflicti | 1264 | A → V in AAB17113 (PubMed:8634698).Curated | 1 | |
Sequence conflicti | 1269 | A → P in AAB17113 (PubMed:8634698).Curated | 1 | |
Sequence conflicti | 1283 | K → T in AAB17113 (PubMed:8634698).Curated | 1 | |
Sequence conflicti | 1337 | N → T in AAB17113 (PubMed:8634698).Curated | 1 | |
Sequence conflicti | 1349 | T → P in AAB17113 (PubMed:8634698).Curated | 1 | |
Sequence conflicti | 1352 – 1353 | QR → EG in AAB17113 (PubMed:8634698).Curated | 2 | |
Sequence conflicti | 1381 | P → S in AAB17113 (PubMed:8634698).Curated | 1 | |
Sequence conflicti | 1390 | A → G in AAB17113 (PubMed:8634698).Curated | 1 | |
Sequence conflicti | 1400 | D → V in AAB17113 (PubMed:8634698).Curated | 1 | |
Sequence conflicti | 1503 | Q → E in AAB17113 (PubMed:8634698).Curated | 1 | |
Sequence conflicti | 1549 | A → V in AAB17113 (PubMed:8634698).Curated | 1 | |
Sequence conflicti | 1680 | K → T in AAB17113 (PubMed:8634698).Curated | 1 | |
Sequence conflicti | 1712 | E → D in AAB17113 (PubMed:8634698).Curated | 1 | |
Sequence conflicti | 1721 | E → D in AAB17113 (PubMed:8634698).Curated | 1 | |
Sequence conflicti | 1791 | D → G in AAB17114 (PubMed:8634697).Curated | 1 |
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 No translation available. U33835 Genomic DNA Translation: AAA99742.1 |
CCDSi | CCDS25474.1 |
PIRi | I49350 |
RefSeqi | NP_033894.3, NM_009764.3 |
Genome annotation databases
Ensembli | ENSMUST00000017290; ENSMUSP00000017290; ENSMUSG00000017146 |
GeneIDi | 12189 |
KEGGi | mmu:12189 |
UCSCi | uc007lpd.2, mouse |
Similar proteinsi
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 No translation available. U33835 Genomic DNA Translation: AAA99742.1 |
CCDSi | CCDS25474.1 |
PIRi | I49350 |
RefSeqi | NP_033894.3, NM_009764.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
7K3S | NMR | - | A | 1337-1388 | [»] | |
SMRi | P48754 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 198383, 46 interactors |
ComplexPortali | CPX-4701, BRCA1-BARD1 complex CPX-972, BRCC ubiquitin ligase complex |
DIPi | DIP-41981N |
IntActi | P48754, 21 interactors |
MINTi | P48754 |
STRINGi | 10090.ENSMUSP00000017290 |
PTM databases
iPTMneti | P48754 |
PhosphoSitePlusi | P48754 |
Proteomic databases
EPDi | P48754 |
jPOSTi | P48754 |
MaxQBi | P48754 |
PaxDbi | P48754 |
PeptideAtlasi | P48754 |
PRIDEi | P48754 |
ProteomicsDBi | 273840 |
Protocols and materials databases
Antibodypediai | 4527, 2257 antibodies from 44 providers |
DNASUi | 12189 |
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 |
VEuPathDBi | HostDB:ENSMUSG00000017146 |
Phylogenomic databases
eggNOGi | KOG4362, Eukaryota |
GeneTreei | ENSGT00440000034289 |
HOGENOMi | CLU_002290_0_0_1 |
InParanoidi | P48754 |
OMAi | NKQKPPC |
OrthoDBi | 496760at2759 |
PhylomeDBi | P48754 |
TreeFami | TF105060 |
Enzyme and pathway databases
UniPathwayi | UPA00143 |
Reactomei | R-MMU-3108214, SUMOylation of DNA damage response and repair proteins |
Miscellaneous databases
BioGRID-ORCSi | 12189, 23 hits in 104 CRISPR screens |
ChiTaRSi | Brca1, mouse |
PROi | PR:P48754 |
RNActi | P48754, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000017146, Expressed in secondary oocyte and 268 other tissues |
ExpressionAtlasi | P48754, baseline and differential |
Genevisiblei | P48754, MM |
Family and domain databases
Gene3Di | 3.30.40.10, 1 hit 3.40.50.10190, 2 hits |
InterProi | View protein in InterPro IPR011364, BRCA1 IPR031099, BRCA1-associated IPR025994, BRCA1_serine_dom IPR001357, BRCT_dom IPR036420, BRCT_dom_sf IPR018957, Znf_C3HC4_RING-type IPR001841, Znf_RING IPR013083, Znf_RING/FYVE/PHD IPR017907, Znf_RING_CS |
PANTHERi | PTHR13763, PTHR13763, 1 hit |
Pfami | View protein in Pfam PF00533, BRCT, 2 hits PF12820, BRCT_assoc, 1 hit PF00097, zf-C3HC4, 1 hit |
PIRSFi | PIRSF001734, BRCA1, 1 hit |
PRINTSi | PR00493, BRSTCANCERI |
SMARTi | View protein in SMART SM00292, BRCT, 2 hits SM00184, RING, 1 hit |
SUPFAMi | SSF52113, SSF52113, 2 hits |
PROSITEi | View protein in PROSITE PS50172, BRCT, 2 hits PS00518, ZF_RING_1, 1 hit PS50089, ZF_RING_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | BRCA1_MOUSE | |
Accessioni | P48754Primary (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: | February 23, 2022 | |
This is version 203 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references