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Breast cancer type 1 susceptibility protein homolog (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BRCA1)

 BRCA1_MOUSE             Reviewed;        1812 AA.
P48754; A2A4Q4; Q60957; Q60983;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 3.
25-APR-2018, entry version 179.
RecName: Full=Breast cancer type 1 susceptibility protein homolog;
EC=2.3.2.27 {ECO:0000250|UniProtKB:P38398};
AltName: Full=RING-type E3 ubiquitin transferase BRCA1 {ECO:0000305};
Name=Brca1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=8634697; DOI=10.1093/hmg/4.12.2265;
Abel K.J., Xy J., Yin G.Y., Lyons R.H., Meisler M.H., Weber B.L.;
"Mouse Brca1: localization sequence analysis and identification of
evolutionarily conserved domains.";
Hum. Mol. Genet. 4:2265-2273(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
PubMed=8634698; DOI=10.1093/hmg/4.12.2275;
Sharan S.K., Wims M., Bradley A.;
"Murine Brca1: sequence and significance for human missense
mutations.";
Hum. Mol. Genet. 4:2275-2278(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=129/SvJ;
PubMed=8575748; DOI=10.1006/geno.1995.9963;
Bennett L.M., Haugen-Strano A., Cochran C., Brownlee H.A.,
Fiedorek F.T. Jr., Wiseman R.W.;
"Isolation of the mouse homologue of BRCA1 and genetic mapping to
mouse chromosome 11.";
Genomics 29:576-581(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=129/SvJ; TISSUE=Embryo;
PubMed=7590247; DOI=10.1101/gad.9.21.2712;
Lane T.F., Deng C., Elson A., Lyu M.S., Kozak C.A., Leder P.;
"Expression of Brca1 is associated with terminal differentiation of
ectodermally and mesodermally derived tissues in mice.";
Genes Dev. 9:2712-2722(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 727-1111.
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=7550308; DOI=10.1038/ng0995-17;
Marquis S.T., Rajan J.V., Wynshaw-Boris A., Xu J., Yin G.Y.,
Abel K.J., Weber B.L., Chodosh L.A.;
"The developmental pattern of Brca1 expression implies a role in
differentiation of the breast and other tissues.";
Nat. Genet. 11:17-26(1995).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 789-1250.
STRAIN=129/SvJ;
PubMed=8566965; DOI=10.1007/BF02265277;
Schroeck E., Badger P., Larson D., Erdos M., Wynshaw-Boris A.,
Ried T., Brody L.;
"The murine homolog of the human breast and ovarian cancer
susceptibility gene Brca1 maps to mouse chromosome 11D.";
Hum. Genet. 97:256-259(1996).
[8]
INTERACTION WITH ACACA, AND FUNCTION.
PubMed=12360400; DOI=10.1038/sj.onc.1205915;
Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S.,
Lenoir G.M., Venezia N.D.;
"BRCA1 interacts with acetyl-CoA carboxylase through its tandem of
BRCT domains.";
Oncogene 21:6729-6739(2002).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706 AND SER-717, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
SUBCELLULAR LOCATION.
PubMed=23039116; DOI=10.1111/gtc.12005;
Kogo H., Tsutsumi M., Inagaki H., Ohye T., Kiyonari H., Kurahashi H.;
"HORMAD2 is essential for synapsis surveillance during meiotic
prophase via the recruitment of ATR activity.";
Genes Cells 17:897-912(2012).
[12]
SUBCELLULAR LOCATION.
PubMed=22549958; DOI=10.1101/gad.187559.112;
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.;
"Meiotic DNA double-strand breaks and chromosome asynapsis in mice are
monitored by distinct HORMAD2-independent and -dependent mechanisms.";
Genes Dev. 26:958-973(2012).
-!- FUNCTION: 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.
{ECO:0000250|UniProtKB:P38398, ECO:0000269|PubMed:12360400}.
-!- CATALYTIC ACTIVITY: 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. {ECO:0000250|UniProtKB:P38398}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: 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).
{ECO:0000250|UniProtKB:P38398, ECO:0000269|PubMed:12360400}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P38398}.
Chromosome {ECO:0000269|PubMed:22549958,
ECO:0000269|PubMed:23039116}. Cytoplasm
{ECO:0000250|UniProtKB:P38398}. 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.
{ECO:0000250|UniProtKB:P38398}.
-!- TISSUE SPECIFICITY: 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 STAGE: In the mammary gland, expression increases
dramatically during pregnancy. Levels fall during lactation and
increase again during post-lactational regression of the mammary
gland.
-!- DOMAIN: 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.
{ECO:0000250|UniProtKB:P38398}.
-!- DOMAIN: The RING-type zinc finger domain interacts with BAP1.
{ECO:0000250|UniProtKB:P38398}.
-!- PTM: 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. {ECO:0000250|UniProtKB:P38398}.
-!- PTM: Autoubiquitinated, undergoes 'Lys-6'-linked
polyubiquitination. 'Lys-6'-linked polyubiquitination does not
promote degradation. {ECO:0000250|UniProtKB:P38398}.
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EMBL; U31625; AAB17114.1; -; mRNA.
EMBL; U35641; AAB17113.1; -; mRNA.
EMBL; U32446; AAA96393.1; -; mRNA.
EMBL; U36475; AAC52323.1; -; mRNA.
EMBL; AL590996; CAM21026.1; -; Genomic_DNA.
EMBL; U33835; AAA99742.1; -; Genomic_DNA.
CCDS; CCDS25474.1; -.
PIR; I49350; I49350.
RefSeq; NP_033894.3; NM_009764.3.
UniGene; Mm.244975; -.
ProteinModelPortal; P48754; -.
SMR; P48754; -.
BioGrid; 198383; 43.
DIP; DIP-41981N; -.
IntAct; P48754; 16.
MINT; P48754; -.
STRING; 10090.ENSMUSP00000017290; -.
iPTMnet; P48754; -.
PhosphoSitePlus; P48754; -.
EPD; P48754; -.
MaxQB; P48754; -.
PaxDb; P48754; -.
PeptideAtlas; P48754; -.
PRIDE; P48754; -.
Ensembl; ENSMUST00000017290; ENSMUSP00000017290; ENSMUSG00000017146.
GeneID; 12189; -.
KEGG; mmu:12189; -.
UCSC; uc007lpd.2; mouse.
CTD; 672; -.
MGI; MGI:104537; Brca1.
eggNOG; ENOG410ITQ6; Eukaryota.
eggNOG; ENOG4111WR7; LUCA.
GeneTree; ENSGT00440000034289; -.
HOGENOM; HOG000230969; -.
HOVERGEN; HBG050730; -.
InParanoid; P48754; -.
KO; K10605; -.
OMA; FQHLLFG; -.
OrthoDB; EOG091G0670; -.
TreeFam; TF105060; -.
Reactome; R-MMU-1221633; Meiotic Synapsis.
Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-MMU-5689901; Metalloprotease DUBs.
Reactome; R-MMU-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
Reactome; R-MMU-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
Reactome; R-MMU-912497; Meiotic Recombination.
UniPathway; UPA00143; -.
PRO; PR:P48754; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000017146; -.
CleanEx; MM_BRCA1; -.
ExpressionAtlas; P48754; baseline and differential.
Genevisible; P48754; MM.
GO; GO:0070531; C:BRCA1-A complex; ISO:MGI.
GO; GO:0031436; C:BRCA1-BARD1 complex; ISS:UniProtKB.
GO; GO:0005813; C:centrosome; TAS:UniProtKB.
GO; GO:0005694; C:chromosome; IDA:UniProtKB.
GO; GO:0000793; C:condensed chromosome; IDA:MGI.
GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISO:MGI.
GO; GO:0000800; C:lateral element; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0003684; F:damaged DNA binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; ISS:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
GO; GO:0071681; P:cellular response to indole-3-methanol; ISO:MGI.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
GO; GO:0007098; P:centrosome cycle; IGI:MGI.
GO; GO:0051298; P:centrosome duplication; TAS:UniProtKB.
GO; GO:0043009; P:chordate embryonic development; IMP:MGI.
GO; GO:0007059; P:chromosome segregation; ISO:MGI.
GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IDA:MGI.
GO; GO:0006302; P:double-strand break repair; IMP:CACAO.
GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI.
GO; GO:0044818; P:mitotic G2/M transition checkpoint; IMP:MGI.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISS:UniProtKB.
GO; GO:0035067; P:negative regulation of histone acetylation; IMP:BHF-UCL.
GO; GO:0051572; P:negative regulation of histone H3-K4 methylation; IMP:BHF-UCL.
GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IMP:BHF-UCL.
GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; ISO:MGI.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
GO; GO:0071158; P:positive regulation of cell cycle arrest; ISO:MGI.
GO; GO:0045739; P:positive regulation of DNA repair; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0035066; P:positive regulation of histone acetylation; IMP:BHF-UCL.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:BHF-UCL.
GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; IMP:BHF-UCL.
GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; IMP:BHF-UCL.
GO; GO:2000620; P:positive regulation of histone H4-K16 acetylation; IMP:BHF-UCL.
GO; GO:0070512; P:positive regulation of histone H4-K20 methylation; IMP:BHF-UCL.
GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:MGI.
GO; GO:0006301; P:postreplication repair; ISO:MGI.
GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
GO; GO:0085020; P:protein K6-linked ubiquitination; ISS:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0044030; P:regulation of DNA methylation; IMP:BHF-UCL.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IMP:BHF-UCL.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0043627; P:response to estrogen; ISO:MGI.
GO; GO:0010212; P:response to ionizing radiation; ISO:MGI.
GO; GO:0072425; P:signal transduction involved in G2 DNA damage checkpoint; ISO:MGI.
CDD; cd00027; BRCT; 2.
Gene3D; 3.30.40.10; -; 1.
Gene3D; 3.40.50.10190; -; 2.
InterPro; IPR011364; BRCA1.
InterPro; IPR031099; BRCA1-associated.
InterPro; IPR025994; BRCA1_serine_dom.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR036420; BRCT_dom_sf.
InterPro; IPR018957; Znf_C3HC4_RING-type.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
PANTHER; PTHR13763; PTHR13763; 1.
PANTHER; PTHR13763:SF0; PTHR13763:SF0; 1.
Pfam; PF00533; BRCT; 2.
Pfam; PF12820; BRCT_assoc; 1.
Pfam; PF00097; zf-C3HC4; 1.
PIRSF; PIRSF001734; BRCA1; 1.
PRINTS; PR00493; BRSTCANCERI.
SMART; SM00292; BRCT; 2.
SMART; SM00184; RING; 1.
SUPFAM; SSF52113; SSF52113; 2.
PROSITE; PS50172; BRCT; 2.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Acetylation; Activator; Cell cycle; Chromosome; Complete proteome;
Cytoplasm; DNA damage; DNA recombination; DNA repair; DNA-binding;
Fatty acid biosynthesis; Fatty acid metabolism; Isopeptide bond;
Lipid biosynthesis; Lipid metabolism; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation; Transferase; Tumor suppressor;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 1812 Breast cancer type 1 susceptibility
protein homolog.
/FTId=PRO_0000055832.
DOMAIN 1585 1679 BRCT 1. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 1698 1797 BRCT 2. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
ZN_FING 24 65 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 1353 1380 Interaction with PALB2. {ECO:0000250}.
COMPBIAS 1562 1567 Poly-Ala.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 305 305 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 392 392 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 686 686 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 706 706 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 717 717 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 831 831 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 971 971 Phosphoserine; by CHEK2.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 992 992 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1152 1152 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1154 1154 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1174 1174 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1180 1180 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1241 1241 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1297 1297 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1303 1303 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1343 1343 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1350 1350 Phosphothreonine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1413 1413 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1481 1481 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1495 1495 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 109 109 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 298 298 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 336 336 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 440 440 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 456 456 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 512 512 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 1048 1048 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CONFLICT 93 93 F -> L (in Ref. 3; AAA96393).
{ECO:0000305}.
CONFLICT 305 305 S -> T (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 319 319 A -> P (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 377 377 Q -> E (in Ref. 3; AAA96393).
{ECO:0000305}.
CONFLICT 550 550 K -> Q (in Ref. 3; AAA96393).
{ECO:0000305}.
CONFLICT 652 652 P -> A (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 765 765 S -> P (in Ref. 3; AAA96393 and 4;
AAC52323). {ECO:0000305}.
CONFLICT 917 917 P -> L (in Ref. 3; AAA96393).
{ECO:0000305}.
CONFLICT 933 933 C -> S (in Ref. 3; AAA96393 and 7;
AAA99742). {ECO:0000305}.
CONFLICT 1091 1091 C -> R (in Ref. 1; AAB17114).
{ECO:0000305}.
CONFLICT 1122 1122 I -> K (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 1206 1206 S -> R (in Ref. 3; AAA96393).
{ECO:0000305}.
CONFLICT 1212 1213 RM -> GI (in Ref. 3; AAA96393).
{ECO:0000305}.
CONFLICT 1255 1255 S -> R (in Ref. 3; AAA96393).
{ECO:0000305}.
CONFLICT 1261 1261 H -> N (in Ref. 3; AAA96393).
{ECO:0000305}.
CONFLICT 1264 1264 A -> V (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 1269 1269 A -> P (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 1283 1283 K -> T (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 1337 1337 N -> T (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 1349 1349 T -> P (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 1352 1353 QR -> EG (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 1381 1381 P -> S (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 1390 1390 A -> G (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 1400 1400 D -> V (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 1503 1503 Q -> E (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 1549 1549 A -> V (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 1680 1680 K -> T (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 1712 1712 E -> D (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 1721 1721 E -> D (in Ref. 2; AAB17113).
{ECO:0000305}.
CONFLICT 1791 1791 D -> G (in Ref. 1; AAB17114).
{ECO:0000305}.
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


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