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UniProtKB - P48754 (BRCA1_MOUSE)

Protein

Breast cancer type 1 susceptibility protein homolog

Gene

Brca1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 + N6-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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionActivator, DNA-binding, Transferase
Biological processCell cycle, DNA damage, DNA recombination, DNA repair, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transcription, Transcription regulation, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-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-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
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:104537 Brca1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
Cross-linki109Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei114PhosphoserineBy similarity1
Cross-linki298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
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
Cross-linki512Glycyl 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
Cross-linki1048Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
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 Expressed in 243 organ(s), highest expression level in zygote
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, 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, COBRA1, DCLRE1C, CLSPN. CHEK1, CHEK2, BAP1, BRCC3, AURKA, UBXN1 and PCLAF. 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). Interacts (via C-terminus) with DHX9; this interaction is direct and links BRCA1 to the RNA polymerase II holoenzyme (By similarity).By similarity1 Publication

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi198383, 43 interactors
ComplexPortaliCPX-972 BRCC ubiquitin ligase complex
DIPiDIP-41981N
IntActiP48754, 16 interactors
MINTiP48754
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 ABRAXAS1, recruits BRCA1 at DNA damage sites.By similarity
The RING-type zinc finger domain interacts with BAP1.By similarity

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
OMAiCNDRQTP
OrthoDBiEOG091G0670
TreeFamiTF105060

Family and domain databases

CDDicd00027 BRCT, 2 hits
Gene3Di3.30.40.10, 1 hit
3.40.50.10190, 2 hits
InterProiView 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
PANTHERiPTHR13763 PTHR13763, 1 hit
PTHR13763:SF0 PTHR13763:SF0, 1 hit
PfamiView protein in Pfam
PF00533 BRCT, 2 hits
PF12820 BRCT_assoc, 1 hit
PF00097 zf-C3HC4, 1 hit
PIRSFiPIRSF001734 BRCA1, 1 hit
PRINTSiPR00493 BRSTCANCERI
SMARTiView protein in SMART
SM00292 BRCT, 2 hits
SM00184 RING, 1 hit
SUPFAMiSSF52113 SSF52113, 2 hits
PROSITEiView protein in PROSITE
PS50172 BRCT, 2 hits
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WPK5A0A087WPK5_MOUSE
Breast cancer type 1 susceptibility...
Brca1
75Annotation score:
A0A087WP26A0A087WP26_MOUSE
Breast cancer type 1 susceptibility...
Brca1
79Annotation score:
A0A087WPE1A0A087WPE1_MOUSE
Breast cancer type 1 susceptibility...
Brca1
177Annotation score:

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

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 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, 43 interactors
ComplexPortaliCPX-972 BRCC ubiquitin ligase complex
DIPiDIP-41981N
IntActiP48754, 16 interactors
MINTiP48754
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
OMAiCNDRQTP
OrthoDBiEOG091G0670
TreeFamiTF105060

Enzyme and pathway databases

UniPathwayi
UPA00143

ReactomeiR-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-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

Miscellaneous databases

PROiPR:P48754
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000017146 Expressed in 243 organ(s), highest expression level in zygote
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
InterProiView 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
PANTHERiPTHR13763 PTHR13763, 1 hit
PTHR13763:SF0 PTHR13763:SF0, 1 hit
PfamiView protein in Pfam
PF00533 BRCT, 2 hits
PF12820 BRCT_assoc, 1 hit
PF00097 zf-C3HC4, 1 hit
PIRSFiPIRSF001734 BRCA1, 1 hit
PRINTSiPR00493 BRSTCANCERI
SMARTiView protein in SMART
SM00292 BRCT, 2 hits
SM00184 RING, 1 hit
SUPFAMiSSF52113 SSF52113, 2 hits
PROSITEiView protein in PROSITE
PS50172 BRCT, 2 hits
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiBRCA1_MOUSE
AccessioniPrimary (citable) accession number: P48754
Secondary accession number(s): A2A4Q4, Q60957, Q60983
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 3, 2012
Last modified: November 7, 2018
This is version 184 of the entry and version 3 of the sequence. See 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
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