BRCA1_MOUSE
ID BRCA1_MOUSE Reviewed; 1812 AA.
AC P48754; A2A4Q4; Q60957; Q60983;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Breast cancer type 1 susceptibility protein homolog;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:P38398};
DE AltName: Full=RING-type E3 ubiquitin transferase BRCA1 {ECO:0000305};
GN Name=Brca1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=8634697; DOI=10.1093/hmg/4.12.2265;
RA Abel K.J., Xy J., Yin G.Y., Lyons R.H., Meisler M.H., Weber B.L.;
RT "Mouse Brca1: localization sequence analysis and identification of
RT evolutionarily conserved domains.";
RL Hum. Mol. Genet. 4:2265-2273(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=8634698; DOI=10.1093/hmg/4.12.2275;
RA Sharan S.K., Wims M., Bradley A.;
RT "Murine Brca1: sequence and significance for human missense mutations.";
RL Hum. Mol. Genet. 4:2275-2278(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/SvJ;
RX PubMed=8575748; DOI=10.1006/geno.1995.9963;
RA Bennett L.M., Haugen-Strano A., Cochran C., Brownlee H.A.,
RA Fiedorek F.T. Jr., Wiseman R.W.;
RT "Isolation of the mouse homologue of BRCA1 and genetic mapping to mouse
RT chromosome 11.";
RL Genomics 29:576-581(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/SvJ; TISSUE=Embryo;
RX PubMed=7590247; DOI=10.1101/gad.9.21.2712;
RA Lane T.F., Deng C., Elson A., Lyu M.S., Kozak C.A., Leder P.;
RT "Expression of Brca1 is associated with terminal differentiation of
RT ectodermally and mesodermally derived tissues in mice.";
RL Genes Dev. 9:2712-2722(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 727-1111.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=7550308; DOI=10.1038/ng0995-17;
RA Marquis S.T., Rajan J.V., Wynshaw-Boris A., Xu J., Yin G.Y., Abel K.J.,
RA Weber B.L., Chodosh L.A.;
RT "The developmental pattern of Brca1 expression implies a role in
RT differentiation of the breast and other tissues.";
RL Nat. Genet. 11:17-26(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 789-1250.
RC STRAIN=129/SvJ;
RX PubMed=8566965; DOI=10.1007/bf02265277;
RA Schroeck E., Badger P., Larson D., Erdos M., Wynshaw-Boris A., Ried T.,
RA Brody L.;
RT "The murine homolog of the human breast and ovarian cancer susceptibility
RT gene Brca1 maps to mouse chromosome 11D.";
RL Hum. Genet. 97:256-259(1996).
RN [8]
RP INTERACTION WITH ACACA.
RX PubMed=12360400; DOI=10.1038/sj.onc.1205915;
RA Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S., Lenoir G.M.,
RA Venezia N.D.;
RT "BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT
RT domains.";
RL Oncogene 21:6729-6739(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706 AND SER-717, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=23039116; DOI=10.1111/gtc.12005;
RA Kogo H., Tsutsumi M., Inagaki H., Ohye T., Kiyonari H., Kurahashi H.;
RT "HORMAD2 is essential for synapsis surveillance during meiotic prophase via
RT the recruitment of ATR activity.";
RL Genes Cells 17:897-912(2012).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=22549958; DOI=10.1101/gad.187559.112;
RA Wojtasz L., Cloutier J.M., Baumann M., Daniel K., Varga J., Fu J.,
RA Anastassiadis K., Stewart A.F., Remenyi A., Turner J.M., Toth A.;
RT "Meiotic DNA double-strand breaks and chromosome asynapsis in mice are
RT monitored by distinct HORMAD2-independent and -dependent mechanisms.";
RL Genes Dev. 26:958-973(2012).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that specifically mediates the
CC formation of 'Lys-6'-linked polyubiquitin chains and plays a central
CC role in DNA repair by facilitating cellular responses to DNA damage. It
CC is unclear whether it also mediates the formation of other types of
CC polyubiquitin chains. The BRCA1-BARD1 heterodimer coordinates a diverse
CC range of cellular pathways such as DNA damage repair, ubiquitination
CC and transcriptional regulation to maintain genomic stability. Regulates
CC centrosomal microtubule nucleation. Required for appropriate cell cycle
CC arrests after ionizing irradiation in both the S-phase and the G2 phase
CC of the cell cycle. Required for FANCD2 targeting to sites of DNA
CC damage. Inhibits lipid synthesis by binding to inactive phosphorylated
CC ACACA and preventing its dephosphorylation. Contributes to homologous
CC recombination repair (HRR) via its direct interaction with PALB2, fine-
CC tunes recombinational repair partly through its modulatory role in the
CC PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks.
CC Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation
CC and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-
CC mediated ubiquitination of RBBP8. Acts as a transcriptional activator.
CC {ECO:0000250|UniProtKB:P38398}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:P38398};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Heterodimer with BARD1. Part of the BRCA1-associated genome
CC surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1,
CC ATM, BLM, PMS2 and the MRE11-RAD50-NBN protein (MRN) complex. This
CC association could be a dynamic process changing throughout the cell
CC cycle and within subnuclear domains. Component of the BRCA1-A complex,
CC at least composed of BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36,
CC BABAM2 and BABAM1/NBA1. Interacts (via the BRCT domains) with ABRAXAS1
CC (phosphorylated form); this is important for recruitment to sites of
CC DNA damage. Can form a heterotetramer with two molecules of ABRAXAS1
CC (phosphorylated form). Component of the BRCA1-RBBP8 complex. Interacts
CC (via the BRCT domains) with RBBP8 ('Ser-327' phosphorylated form); the
CC interaction ubiquitinates RBBP8, regulates CHEK1 activation, and
CC involves RBBP8 in BRCA1-dependent G2/M checkpoint control on DNA
CC damage. Associates with RNA polymerase II holoenzyme. Interacts with
CC SMC1A, NELFB, DCLRE1C, CLSPN. CHEK1, CHEK2, BAP1, BRCC3, UBXN1 and
CC PCLAF. Interacts (via BRCT domains) with BRIP1 (phosphorylated form).
CC Interacts with FANCD2 (ubiquitinated form). Interacts with H2AX
CC (phosphorylated on 'Ser-140'). Interacts (via the BRCT domains) with
CC ACACA (phosphorylated form); the interaction prevents dephosphorylation
CC of ACACA. Part of a BRCA complex containing BRCA1, BRCA2 and PALB2.
CC Interacts directly with PALB2; the interaction is essential for its
CC function in HRR. Interacts directly with BRCA2; the interaction occurs
CC only in the presence of PALB2 which serves as the bridging protein.
CC Interacts (via the BRCT domains) with LMO4; the interaction represses
CC the transcriptional activity of BRCA1. Interacts (via the BRCT domains)
CC with CCAR2 (via N-terminus); the interaction represses the
CC transcriptional activator activity of BRCA1 (By similarity). Interacts
CC with EXD2 (By similarity). Interacts (via C-terminus) with DHX9; this
CC interaction is direct and links BRCA1 to the RNA polymerase II
CC holoenzyme (By similarity). {ECO:0000250|UniProtKB:P38398,
CC ECO:0000269|PubMed:12360400}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P38398}.
CC Chromosome {ECO:0000269|PubMed:22549958, ECO:0000269|PubMed:23039116}.
CC Cytoplasm {ECO:0000250|UniProtKB:P38398}. Note=Localizes at sites of
CC DNA damage at double-strand breaks (DSBs); recruitment to DNA damage
CC sites is mediated by the BRCA1-A complex. Translocated to the cytoplasm
CC during UV-induced apoptosis. {ECO:0000250|UniProtKB:P38398}.
CC -!- TISSUE SPECIFICITY: In the embryo, expressed in otic vesicles at day
CC 9.5. At day 10.5, this expression decreases and high levels are found
CC in the neuroectoderm. At days 11-12.5, high levels in differentiating
CC keratinocytes and whisker pad primordia. At days 14-17, expression also
CC observed in kidney epithelial cells. In the adult, highest levels found
CC in spleen, thymus, lymph nodes, epithelial organs, and alveolar and
CC ductal epithelial cells of the mammary gland. Very low levels in brain,
CC kidney, and skin. No expression in heart, liver or lung.
CC -!- DEVELOPMENTAL STAGE: In the mammary gland, expression increases
CC dramatically during pregnancy. Levels fall during lactation and
CC increase again during post-lactational regression of the mammary gland.
CC -!- DOMAIN: The BRCT domains recognize and bind phosphorylated pSXXF motif
CC on proteins. The interaction with the phosphorylated pSXXF motif of
CC ABRAXAS1, recruits BRCA1 at DNA damage sites.
CC {ECO:0000250|UniProtKB:P38398}.
CC -!- DOMAIN: The RING-type zinc finger domain interacts with BAP1.
CC {ECO:0000250|UniProtKB:P38398}.
CC -!- PTM: Phosphorylated in response to IR, UV, and various stimuli that
CC cause checkpoint activation, probably by ATM or ATR. Phosphorylation at
CC Ser-971 by CHEK2 regulates mitotic spindle assembly. Phosphorylation by
CC AURKA regulates centrosomal microtubule nucleation.
CC {ECO:0000250|UniProtKB:P38398}.
CC -!- PTM: Autoubiquitinated, undergoes 'Lys-6'-linked polyubiquitination.
CC 'Lys-6'-linked polyubiquitination does not promote degradation.
CC {ECO:0000250|UniProtKB:P38398}.
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DR EMBL; U31625; AAB17114.1; -; mRNA.
DR EMBL; U35641; AAB17113.1; -; mRNA.
DR EMBL; U32446; AAA96393.1; -; mRNA.
DR EMBL; U36475; AAC52323.1; -; mRNA.
DR EMBL; AL590996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U33835; AAA99742.1; -; Genomic_DNA.
DR CCDS; CCDS25474.1; -.
DR PIR; I49350; I49350.
DR RefSeq; NP_033894.3; NM_009764.3.
DR PDB; 7K3S; NMR; -; A=1337-1388.
DR PDBsum; 7K3S; -.
DR AlphaFoldDB; P48754; -.
DR SMR; P48754; -.
DR BioGRID; 198383; 46.
DR ComplexPortal; CPX-4701; BRCA1-BARD1 complex.
DR ComplexPortal; CPX-972; BRCC ubiquitin ligase complex.
DR DIP; DIP-41981N; -.
DR IntAct; P48754; 21.
DR MINT; P48754; -.
DR STRING; 10090.ENSMUSP00000017290; -.
DR iPTMnet; P48754; -.
DR PhosphoSitePlus; P48754; -.
DR EPD; P48754; -.
DR jPOST; P48754; -.
DR MaxQB; P48754; -.
DR PaxDb; P48754; -.
DR PeptideAtlas; P48754; -.
DR PRIDE; P48754; -.
DR ProteomicsDB; 273840; -.
DR Antibodypedia; 4527; 2285 antibodies from 45 providers.
DR DNASU; 12189; -.
DR Ensembl; ENSMUST00000017290; ENSMUSP00000017290; ENSMUSG00000017146.
DR GeneID; 12189; -.
DR KEGG; mmu:12189; -.
DR UCSC; uc007lpd.2; mouse.
DR CTD; 672; -.
DR MGI; MGI:104537; Brca1.
DR VEuPathDB; HostDB:ENSMUSG00000017146; -.
DR eggNOG; KOG4362; Eukaryota.
DR GeneTree; ENSGT00440000034289; -.
DR HOGENOM; CLU_002290_0_0_1; -.
DR InParanoid; P48754; -.
DR OMA; DMTTEHL; -.
DR OrthoDB; 496760at2759; -.
DR PhylomeDB; P48754; -.
DR TreeFam; TF105060; -.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 12189; 25 hits in 116 CRISPR screens.
DR ChiTaRS; Brca1; mouse.
DR PRO; PR:P48754; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P48754; protein.
DR Bgee; ENSMUSG00000017146; Expressed in secondary oocyte and 229 other tissues.
DR ExpressionAtlas; P48754; baseline and differential.
DR Genevisible; P48754; MM.
DR GO; GO:0070531; C:BRCA1-A complex; ISO:MGI.
DR GO; GO:0070532; C:BRCA1-B complex; ISO:MGI.
DR GO; GO:0031436; C:BRCA1-BARD1 complex; ISS:UniProtKB.
DR GO; GO:0070533; C:BRCA1-C complex; ISO:MGI.
DR GO; GO:0005813; C:centrosome; TAS:UniProtKB.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:1990391; C:DNA repair complex; ISO:MGI.
DR GO; GO:0000800; C:lateral element; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0000152; C:nuclear ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0003684; F:damaged DNA binding; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0071681; P:cellular response to indole-3-methanol; ISO:MGI.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
DR GO; GO:0007098; P:centrosome cycle; IGI:MGI.
DR GO; GO:0051298; P:centrosome duplication; TAS:UniProtKB.
DR GO; GO:0043009; P:chordate embryonic development; IMP:MGI.
DR GO; GO:0007059; P:chromosome segregation; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; IC:ComplexPortal.
DR GO; GO:0110025; P:DNA strand resection involved in replication fork processing; IC:ComplexPortal.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IDA:MGI.
DR GO; GO:0006302; P:double-strand break repair; IMP:CACAO.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070537; P:histone H2A K63-linked deubiquitination; IC:ComplexPortal.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IC:ComplexPortal.
DR GO; GO:0035825; P:homologous recombination; IC:ComplexPortal.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISO:MGI.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; IMP:MGI.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0035067; P:negative regulation of histone acetylation; IMP:BHF-UCL.
DR GO; GO:0051572; P:negative regulation of histone H3-K4 methylation; IMP:BHF-UCL.
DR GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IMP:BHF-UCL.
DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; ISO:MGI.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0045787; P:positive regulation of cell cycle; IC:ComplexPortal.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IMP:BHF-UCL.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:BHF-UCL.
DR GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; IMP:BHF-UCL.
DR GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; IMP:BHF-UCL.
DR GO; GO:2000620; P:positive regulation of histone H4-K16 acetylation; IMP:BHF-UCL.
DR GO; GO:0070512; P:positive regulation of histone H4-K20 methylation; IMP:BHF-UCL.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:MGI.
DR GO; GO:0006301; P:postreplication repair; ISO:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0085020; P:protein K6-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IC:ComplexPortal.
DR GO; GO:0044030; P:regulation of DNA methylation; IMP:BHF-UCL.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IMP:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; ISO:MGI.
DR GO; GO:0010212; P:response to ionizing radiation; ISO:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.10190; -; 2.
DR InterPro; IPR011364; BRCA1.
DR InterPro; IPR031099; BRCA1-associated.
DR InterPro; IPR025994; BRCA1_serine_dom.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13763; PTHR13763; 1.
DR Pfam; PF00533; BRCT; 2.
DR Pfam; PF12820; BRCT_assoc; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PIRSF; PIRSF001734; BRCA1; 1.
DR PRINTS; PR00493; BRSTCANCERI.
DR SMART; SM00292; BRCT; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52113; SSF52113; 2.
DR PROSITE; PS50172; BRCT; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Cell cycle; Chromosome; Cytoplasm;
KW DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Fatty acid biosynthesis; Fatty acid metabolism; Isopeptide bond;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase; Tumor suppressor; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1812
FT /note="Breast cancer type 1 susceptibility protein homolog"
FT /id="PRO_0000055832"
FT DOMAIN 1585..1679
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 1698..1797
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT ZN_FING 24..65
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 165..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1244..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1353..1380
FT /note="Interaction with PALB2"
FT /evidence="ECO:0000250"
FT REGION 1437..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1472..1507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 971
FT /note="Phosphoserine; by CHEK2"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 992
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1350
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 336
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 440
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 456
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 512
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 1048
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CONFLICT 93
FT /note="F -> L (in Ref. 3; AAA96393)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="S -> T (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="A -> P (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="Q -> E (in Ref. 3; AAA96393)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="K -> Q (in Ref. 3; AAA96393)"
FT /evidence="ECO:0000305"
FT CONFLICT 652
FT /note="P -> A (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 765
FT /note="S -> P (in Ref. 3; AAA96393 and 4; AAC52323)"
FT /evidence="ECO:0000305"
FT CONFLICT 917
FT /note="P -> L (in Ref. 3; AAA96393)"
FT /evidence="ECO:0000305"
FT CONFLICT 933
FT /note="C -> S (in Ref. 3; AAA96393 and 7; AAA99742)"
FT /evidence="ECO:0000305"
FT CONFLICT 1091
FT /note="C -> R (in Ref. 1; AAB17114)"
FT /evidence="ECO:0000305"
FT CONFLICT 1122
FT /note="I -> K (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 1206
FT /note="S -> R (in Ref. 3; AAA96393)"
FT /evidence="ECO:0000305"
FT CONFLICT 1212..1213
FT /note="RM -> GI (in Ref. 3; AAA96393)"
FT /evidence="ECO:0000305"
FT CONFLICT 1255
FT /note="S -> R (in Ref. 3; AAA96393)"
FT /evidence="ECO:0000305"
FT CONFLICT 1261
FT /note="H -> N (in Ref. 3; AAA96393)"
FT /evidence="ECO:0000305"
FT CONFLICT 1264
FT /note="A -> V (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 1269
FT /note="A -> P (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 1283
FT /note="K -> T (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 1337
FT /note="N -> T (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 1349
FT /note="T -> P (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 1352..1353
FT /note="QR -> EG (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 1381
FT /note="P -> S (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 1390
FT /note="A -> G (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 1400
FT /note="D -> V (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 1503
FT /note="Q -> E (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 1549
FT /note="A -> V (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 1680
FT /note="K -> T (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 1712
FT /note="E -> D (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 1721
FT /note="E -> D (in Ref. 2; AAB17113)"
FT /evidence="ECO:0000305"
FT CONFLICT 1791
FT /note="D -> G (in Ref. 1; AAB17114)"
FT /evidence="ECO:0000305"
FT STRAND 1346..1348
FT /evidence="ECO:0007829|PDB:7K3S"
FT HELIX 1350..1377
FT /evidence="ECO:0007829|PDB:7K3S"
FT TURN 1378..1382
FT /evidence="ECO:0007829|PDB:7K3S"
SQ SEQUENCE 1812 AA; 198795 MW; 2B47FB55B149FD71 CRC64;
MDLSAVQIQE VQNVLHAMQK ILECPICLEL IKEPVSTKCD HIFCKFCMLK LLNQKKGPSQ
CPLCKNEITK RSLQGSTRFS QLAEELLRIM AAFELDTGMQ LTNGFSFSKK RNNSCERLNE
EASIIQSVGY RNRVRRLPQV EPGNATLKDS LGVQLSNLGI VRSVKKNRQT QPRKKSVYIE
LDSDSSEETV TKPGDCSVRD QELLQTAPQE AGDEGKLHSA EEAACEFSEG IRNIEHHQCS
DDLNPTENHA TERHPEKCQS ISISNVCVEP CGTDAHASSL QPETSSLLLI EDRMNAEKAE
FCNKSKQPGI AVSQQSRWAA SKGTCNDRQV PSTGEKVGPN ADSLSDREKW THPQSLCPEN
SGATTDVPWI TLNSSVQKVN EWFSRTGEML TSDSASARRH ESNAEAAVVL EVSNEVDGGF
SSSRKTDLVT PDPHHTLMCK SGRDFSKPVE DNISDKIFGK SYQRKGSRPH LNHVTEIIGT
FITEPQITQE QPFTNKLKRK RSTSLQPEDF IKKADSAGVQ RTPDNINQGT DLMEPNEQAV
STTSNCQENK IAGSNLQKEK SAHPTESLRK EPASTAGAKS ISNSVSDLEV ELNVHSSKAP
KKNRLRRKSS IRCALPLEPI SRNPSPPTCA ELQIDSCGSS EETKKNHSNQ QPAGHLREPQ
LIEDTEPAAD AKKNEPNEHI RKRRASDAFP EEKLMNKAGL LTSCSSPRKS QGPVNPSPQR
TGTEQLETRQ MSDSAKELGD RVLGGEPSGK TTDRSEESTS VSLVSDTDYD TQNSVSVLDA
HTVRYARTGS AQCMTQFVAS ENPKELVHGS NNAGSGTEGL KPPLRHALNL SQEKVEMEDS
ELDTQYLQNT FQVSKRQSFA LFSKPRSPQK DCAHSVPSKE LSPKVTAKGK QKERQGQEEF
EISHVQAVAA TVGLPVPCQE GKLAADTMCD RGCRLCPSSH YRSGENGLSA TGKSGISQNS
HFKQSVSPIR SSIKTDNRKP LTEGRFERHT SSTEMAVGNE NILQSTVHTV SLNNRGNACQ
EAGSGSIHEV CSTGDSFPGQ LGRNRGPKVN TVPPLDSMQP GVCQQSVPVS DKYLEIKKQE
GEAVCADFSP CLFSDHLEQS MSGKVFQVCS ETPDDLLDDV EIQGHTSFGE GDIMERSAVF
NGSILRRESS RSPSPVTHAS KSQSLHRASR KLESSEESDS TEDEDLPCFQ HLLSRISNTP
ELTRCSSAVT QRMPEKAEGT QAPWKGSSSD CNNEVIMIEA SQEHQFSEDP RCSGSMFSSQ
HSAAQGSTAN ANSQDSNFIP PSKQRSHQCG NEEAFLSDKE LISDNEEMAT CLEEDNDQEE
DSIIPDSEAS GYESETNLSE DCSQSDILTT QQRATMKYNL IKLQQEMAHL EAVLEQRGNQ
PSGHSPSLLA DPCALEDLPD LEPNMSGAAI LTSKNINENP VSQNLKSACD DKFQLQHLEG
PTSGDDESGM GRPSPFKSPL AGSRGSAHGC SRHLQKRNSP SQEELLQPAG SEASSEPHNS
TGQSCLPRRE LEGTPYLGSG ISLFSSRDPE SESPKEPAHI GTTPASTSAL KIPQGQVAFR
SAAAAGADKA VVGIVSKIKP ELTSSEERAD RDISMVVSGL TPKEVMTVQK FAEKYRLTLT
DAITEETTHV IIKTDAEFVC ERTLKYFLGI AGGKWIVSYS WVVRSIQERR LLNVHEFEVK
GDVVTGRNHQ GPRRSRESRE KLFKGLQVYC CEPFTNMPKD ELERMLQLCG ASVVKELPSL
THDTGAHLVV IVQPSAWTED SNCPDIGQLC KARLVMWDWV LDSLSSYRCR DLDAYLVQNI
TCDSSEPQDS ND
