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P48754

- BRCA1_MOUSE

UniProt

P48754 - BRCA1_MOUSE

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Protein

Breast cancer type 1 susceptibility protein homolog

Gene
Brca1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 By similarity. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation.1 Publication

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri24 – 6542RING-typeAdd
BLAST

GO - Molecular functioni

  1. damaged DNA binding Source: MGI
  2. ligase activity Source: UniProtKB-KW
  3. RNA binding Source: MGI
  4. transcription regulatory region DNA binding Source: BHF-UCL
  5. ubiquitin-protein transferase activity Source: UniProtKB
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: MGI
  2. centrosome cycle Source: MGI
  3. centrosome duplication Source: UniProtKB
  4. chordate embryonic development Source: MGI
  5. DNA recombination Source: UniProtKB-KW
  6. DNA repair Source: UniProtKB-KW
  7. DNA replication Source: MGI
  8. dosage compensation by inactivation of X chromosome Source: MGI
  9. fatty acid biosynthetic process Source: UniProtKB-KW
  10. intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
  11. negative regulation of fatty acid biosynthetic process Source: UniProtKB
  12. negative regulation of histone acetylation Source: BHF-UCL
  13. negative regulation of histone H3-K4 methylation Source: BHF-UCL
  14. negative regulation of histone H3-K9 methylation Source: BHF-UCL
  15. positive regulation of histone acetylation Source: BHF-UCL
  16. positive regulation of histone H3-K4 methylation Source: BHF-UCL
  17. positive regulation of histone H3-K9 acetylation Source: BHF-UCL
  18. positive regulation of histone H3-K9 methylation Source: BHF-UCL
  19. positive regulation of histone H4-K16 acetylation Source: BHF-UCL
  20. positive regulation of histone H4-K20 methylation Source: BHF-UCL
  21. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  22. protein autoubiquitination Source: UniProtKB
  23. protein K6-linked ubiquitination Source: UniProtKB
  24. regulation of DNA methylation Source: BHF-UCL
  25. regulation of gene expression by genetic imprinting Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

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

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_198626. Meiotic synapsis.
REACT_198629. Meiotic recombination.
REACT_27235. Meiotic Recombination.
REACT_75800. Meiotic Synapsis.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Breast cancer type 1 susceptibility protein homolog (EC:6.3.2.-)
Gene namesi
Name:Brca1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:104537. Brca1.

Subcellular locationi

Nucleus By similarity. Chromosome
Note: Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex By similarity.2 Publications

GO - Cellular componenti

  1. BRCA1-BARD1 complex Source: UniProtKB
  2. centrosome Source: UniProtKB
  3. chromosome Source: UniProtKB
  4. condensed chromosome Source: MGI
  5. condensed nuclear chromosome Source: MGI
  6. cytoplasm Source: MGI
  7. nucleoplasm Source: Reactome
  8. ribonucleoprotein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18121812Breast cancer type 1 susceptibility protein homologPRO_0000055832Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei114 – 1141Phosphoserine By similarity
Modified residuei305 – 3051Phosphoserine By similarity
Modified residuei392 – 3921Phosphoserine By similarity
Modified residuei686 – 6861Phosphoserine By similarity
Modified residuei831 – 8311Phosphoserine1 Publication
Modified residuei971 – 9711Phosphoserine; by CHEK2 By similarity
Modified residuei1174 – 11741Phosphoserine By similarity
Modified residuei1180 – 11801Phosphoserine By similarity
Modified residuei1241 – 12411Phosphoserine By similarity
Modified residuei1297 – 12971Phosphoserine By similarity
Modified residuei1303 – 13031Phosphoserine By similarity
Modified residuei1343 – 13431Phosphoserine By similarity
Modified residuei1350 – 13501Phosphothreonine By similarity
Modified residuei1413 – 14131Phosphoserine By similarity
Modified residuei1481 – 14811Phosphoserine By similarity

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, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP48754.

PTM databases

PhosphoSiteiP48754.

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

ArrayExpressiP48754.
CleanExiMM_BRCA1.
GenevestigatoriP48754.

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 the BRCA1, BARD1, UIMC1, BRCC3, BRE and BABAM1. Interacts (via the BRCT domains) with FAM175A. 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 BRCA1.1 Publication

Protein-protein interaction databases

BioGridi198383. 20 interactions.
DIPiDIP-41981N.
IntActiP48754. 2 interactions.
STRINGi10090.ENSMUSP00000102847.

Structurei

3D structure databases

ProteinModelPortaliP48754.
SMRiP48754. Positions 1-103, 1588-1798.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1585 – 167995BRCT 1Add
BLAST
Domaini1698 – 1797100BRCT 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1353 – 138028Interaction with PALB2 By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1562 – 15676Poly-Ala

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.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri24 – 6542RING-typeAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG274496.
GeneTreeiENSGT00440000034289.
HOGENOMiHOG000230969.
HOVERGENiHBG050730.
InParanoidiP48754.
KOiK10605.
OMAiKGPSQCP.
OrthoDBiEOG79CXXK.
TreeFamiTF105060.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.40.50.10190. 2 hits.
InterProiIPR011364. BRCA1.
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.
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

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MDLSAVQIQE VQNVLHAMQK ILECPICLEL IKEPVSTKCD HIFCKFCMLK     50
LLNQKKGPSQ CPLCKNEITK RSLQGSTRFS QLAEELLRIM AAFELDTGMQ 100
LTNGFSFSKK RNNSCERLNE EASIIQSVGY RNRVRRLPQV EPGNATLKDS 150
LGVQLSNLGI VRSVKKNRQT QPRKKSVYIE LDSDSSEETV TKPGDCSVRD 200
QELLQTAPQE AGDEGKLHSA EEAACEFSEG IRNIEHHQCS DDLNPTENHA 250
TERHPEKCQS ISISNVCVEP CGTDAHASSL QPETSSLLLI EDRMNAEKAE 300
FCNKSKQPGI AVSQQSRWAA SKGTCNDRQV PSTGEKVGPN ADSLSDREKW 350
THPQSLCPEN SGATTDVPWI TLNSSVQKVN EWFSRTGEML TSDSASARRH 400
ESNAEAAVVL EVSNEVDGGF SSSRKTDLVT PDPHHTLMCK SGRDFSKPVE 450
DNISDKIFGK SYQRKGSRPH LNHVTEIIGT FITEPQITQE QPFTNKLKRK 500
RSTSLQPEDF IKKADSAGVQ RTPDNINQGT DLMEPNEQAV STTSNCQENK 550
IAGSNLQKEK SAHPTESLRK EPASTAGAKS ISNSVSDLEV ELNVHSSKAP 600
KKNRLRRKSS IRCALPLEPI SRNPSPPTCA ELQIDSCGSS EETKKNHSNQ 650
QPAGHLREPQ LIEDTEPAAD AKKNEPNEHI RKRRASDAFP EEKLMNKAGL 700
LTSCSSPRKS QGPVNPSPQR TGTEQLETRQ MSDSAKELGD RVLGGEPSGK 750
TTDRSEESTS VSLVSDTDYD TQNSVSVLDA HTVRYARTGS AQCMTQFVAS 800
ENPKELVHGS NNAGSGTEGL KPPLRHALNL SQEKVEMEDS ELDTQYLQNT 850
FQVSKRQSFA LFSKPRSPQK DCAHSVPSKE LSPKVTAKGK QKERQGQEEF 900
EISHVQAVAA TVGLPVPCQE GKLAADTMCD RGCRLCPSSH YRSGENGLSA 950
TGKSGISQNS HFKQSVSPIR SSIKTDNRKP LTEGRFERHT SSTEMAVGNE 1000
NILQSTVHTV SLNNRGNACQ EAGSGSIHEV CSTGDSFPGQ LGRNRGPKVN 1050
TVPPLDSMQP GVCQQSVPVS DKYLEIKKQE GEAVCADFSP CLFSDHLEQS 1100
MSGKVFQVCS ETPDDLLDDV EIQGHTSFGE GDIMERSAVF NGSILRRESS 1150
RSPSPVTHAS KSQSLHRASR KLESSEESDS TEDEDLPCFQ HLLSRISNTP 1200
ELTRCSSAVT QRMPEKAEGT QAPWKGSSSD CNNEVIMIEA SQEHQFSEDP 1250
RCSGSMFSSQ HSAAQGSTAN ANSQDSNFIP PSKQRSHQCG NEEAFLSDKE 1300
LISDNEEMAT CLEEDNDQEE DSIIPDSEAS GYESETNLSE DCSQSDILTT 1350
QQRATMKYNL IKLQQEMAHL EAVLEQRGNQ PSGHSPSLLA DPCALEDLPD 1400
LEPNMSGAAI LTSKNINENP VSQNLKSACD DKFQLQHLEG PTSGDDESGM 1450
GRPSPFKSPL AGSRGSAHGC SRHLQKRNSP SQEELLQPAG SEASSEPHNS 1500
TGQSCLPRRE LEGTPYLGSG ISLFSSRDPE SESPKEPAHI GTTPASTSAL 1550
KIPQGQVAFR SAAAAGADKA VVGIVSKIKP ELTSSEERAD RDISMVVSGL 1600
TPKEVMTVQK FAEKYRLTLT DAITEETTHV IIKTDAEFVC ERTLKYFLGI 1650
AGGKWIVSYS WVVRSIQERR LLNVHEFEVK GDVVTGRNHQ GPRRSRESRE 1700
KLFKGLQVYC CEPFTNMPKD ELERMLQLCG ASVVKELPSL THDTGAHLVV 1750
IVQPSAWTED SNCPDIGQLC KARLVMWDWV LDSLSSYRCR DLDAYLVQNI 1800
TCDSSEPQDS ND 1812
Length:1,812
Mass (Da):198,795
Last modified:October 3, 2012 - v3
Checksum:i2B47FB55B149FD71
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 931F → L in AAA96393. 1 Publication
Sequence conflicti305 – 3051S → T in AAB17113. 1 Publication
Sequence conflicti319 – 3191A → P in AAB17113. 1 Publication
Sequence conflicti377 – 3771Q → E in AAA96393. 1 Publication
Sequence conflicti550 – 5501K → Q in AAA96393. 1 Publication
Sequence conflicti652 – 6521P → A in AAB17113. 1 Publication
Sequence conflicti765 – 7651S → P in AAA96393. 1 Publication
Sequence conflicti765 – 7651S → P in AAC52323. 1 Publication
Sequence conflicti917 – 9171P → L in AAA96393. 1 Publication
Sequence conflicti933 – 9331C → S in AAA96393. 1 Publication
Sequence conflicti933 – 9331C → S in AAA99742. 1 Publication
Sequence conflicti1091 – 10911C → R in AAB17114. 1 Publication
Sequence conflicti1122 – 11221I → K in AAB17113. 1 Publication
Sequence conflicti1206 – 12061S → R in AAA96393. 1 Publication
Sequence conflicti1212 – 12132RM → GI in AAA96393. 1 Publication
Sequence conflicti1255 – 12551S → R in AAA96393. 1 Publication
Sequence conflicti1261 – 12611H → N in AAA96393. 1 Publication
Sequence conflicti1264 – 12641A → V in AAB17113. 1 Publication
Sequence conflicti1269 – 12691A → P in AAB17113. 1 Publication
Sequence conflicti1283 – 12831K → T in AAB17113. 1 Publication
Sequence conflicti1337 – 13371N → T in AAB17113. 1 Publication
Sequence conflicti1349 – 13491T → P in AAB17113. 1 Publication
Sequence conflicti1352 – 13532QR → EG in AAB17113. 1 Publication
Sequence conflicti1381 – 13811P → S in AAB17113. 1 Publication
Sequence conflicti1390 – 13901A → G in AAB17113. 1 Publication
Sequence conflicti1400 – 14001D → V in AAB17113. 1 Publication
Sequence conflicti1503 – 15031Q → E in AAB17113. 1 Publication
Sequence conflicti1549 – 15491A → V in AAB17113. 1 Publication
Sequence conflicti1680 – 16801K → T in AAB17113. 1 Publication
Sequence conflicti1712 – 17121E → D in AAB17113. 1 Publication
Sequence conflicti1721 – 17211E → D in AAB17113. 1 Publication
Sequence conflicti1791 – 17911D → G in AAB17114. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS25474.1.
PIRi I49350.
RefSeqi NP_033894.3. NM_009764.3.
UniGenei Mm.244975.

3D structure databases

ProteinModelPortali P48754.
SMRi P48754. Positions 1-103, 1588-1798.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198383. 20 interactions.
DIPi DIP-41981N.
IntActi P48754. 2 interactions.
STRINGi 10090.ENSMUSP00000102847.

PTM databases

PhosphoSitei P48754.

Proteomic databases

PRIDEi P48754.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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.

Phylogenomic databases

eggNOGi NOG274496.
GeneTreei ENSGT00440000034289.
HOGENOMi HOG000230969.
HOVERGENi HBG050730.
InParanoidi P48754.
KOi K10605.
OMAi KGPSQCP.
OrthoDBi EOG79CXXK.
TreeFami TF105060.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_198626. Meiotic synapsis.
REACT_198629. Meiotic recombination.
REACT_27235. Meiotic Recombination.
REACT_75800. Meiotic Synapsis.

Miscellaneous databases

NextBioi 280581.
PROi P48754.
SOURCEi Search...

Gene expression databases

ArrayExpressi P48754.
CleanExi MM_BRCA1.
Genevestigatori P48754.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
3.40.50.10190. 2 hits.
InterProi IPR011364. BRCA1.
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 ]
PANTHERi PTHR13763. PTHR13763. 1 hit.
Pfami PF00533. BRCT. 2 hits.
PF12820. BRCT_assoc. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view ]
PIRSFi PIRSF001734. BRCA1. 1 hit.
PRINTSi PR00493. BRSTCANCERI.
SMARTi SM00292. BRCT. 2 hits.
SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF52113. SSF52113. 2 hits.
PROSITEi PS50172. BRCT. 2 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse Brca1: localization sequence analysis and identification of evolutionarily conserved domains."
    Abel K.J., Xy J., Yin G.Y., Lyons R.H., Meisler M.H., Weber B.L.
    Hum. Mol. Genet. 4:2265-2273(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
    Tissue: Embryo.
  2. "Murine Brca1: sequence and significance for human missense mutations."
    Sharan S.K., Wims M., Bradley A.
    Hum. Mol. Genet. 4:2275-2278(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
  3. "Isolation of the mouse homologue of BRCA1 and genetic mapping to mouse chromosome 11."
    Bennett L.M., Haugen-Strano A., Cochran C., Brownlee H.A., Fiedorek F.T. Jr., Wiseman R.W.
    Genomics 29:576-581(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129/SvJ.
  4. "Expression of Brca1 is associated with terminal differentiation of ectodermally and mesodermally derived tissues in mice."
    Lane T.F., Deng C., Elson A., Lyu M.S., Kozak C.A., Leder P.
    Genes Dev. 9:2712-2722(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129/SvJ.
    Tissue: Embryo.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "The developmental pattern of Brca1 expression implies a role in differentiation of the breast and other tissues."
    Marquis S.T., Rajan J.V., Wynshaw-Boris A., Xu J., Yin G.Y., Abel K.J., Weber B.L., Chodosh L.A.
    Nat. Genet. 11:17-26(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 727-1111.
    Strain: C57BL/6.
    Tissue: Embryo.
  7. "The murine homolog of the human breast and ovarian cancer susceptibility gene Brca1 maps to mouse chromosome 11D."
    Schroeck E., Badger P., Larson D., Erdos M., Wynshaw-Boris A., Ried T., Brody L.
    Hum. Genet. 97:256-259(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 789-1250.
    Strain: 129/SvJ.
  8. "BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains."
    Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S., Lenoir G.M., Venezia N.D.
    Oncogene 21:6729-6739(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACACA, FUNCTION.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. "HORMAD2 is essential for synapsis surveillance during meiotic prophase via the recruitment of ATR activity."
    Kogo H., Tsutsumi M., Inagaki H., Ohye T., Kiyonari H., Kurahashi H.
    Genes Cells 17:897-912(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Meiotic DNA double-strand breaks and chromosome asynapsis in mice are monitored by distinct HORMAD2-independent and -dependent mechanisms."
    Wojtasz L., Cloutier J.M., Baumann M., Daniel K., Varga J., Fu J., Anastassiadis K., Stewart A.F., Remenyi A., Turner J.M., Toth A.
    Genes Dev. 26:958-973(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

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: September 3, 2014
This is version 139 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

External Data

Dasty 3

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