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BRCA1-associated RING domain protein 1 (BARD-1) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BARD1)

 BARD1_HUMAN             Reviewed;         777 AA.
Q99728; F6MDH7; F6MDH8; F6MDH9; O43574; Q53SS5;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
25-OCT-2017, entry version 191.
RecName: Full=BRCA1-associated RING domain protein 1;
Short=BARD-1;
EC=2.3.2.27 {ECO:0000269|PubMed:12890688, ECO:0000269|PubMed:20351172};
AltName: Full=RING-type E3 ubiquitin transferase BARD1 {ECO:0000305};
Name=BARD1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
TISSUE=B-cell;
PubMed=8944023; DOI=10.1038/ng1296-430;
Wu L.C., Wang Z.W., Tsan J.T., Spillman M.A., Phung A., Xu X.L.,
Yang M.-C.W., Hwang L.-Y., Bowcock A.M., Baer R.;
"Identification of a RING protein that can interact in vivo with the
BRCA1 gene product.";
Nat. Genet. 14:430-440(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-24; GLU-153;
SER-378; MET-507; SER-557; HIS-564; CYS-658; LEU-695 AND ASN-761.
PubMed=9425226; DOI=10.1093/hmg/7.2.195;
Thai T.H., Du F., Tsan J.T., Jin Y., Phung A., Spillman M.A.,
Massa H.F., Muller C.Y., Ashfaq R., Mathis J.M., Miller D.S.,
Trask B.J., Baer R., Bowcock A.M.;
"Mutations in the BRCA1-associated RING domain (BARD1) gene in primary
breast, ovarian and uterine cancers.";
Hum. Mol. Genet. 7:195-202(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA), AND
ALTERNATIVE SPLICING.
PubMed=18089818; DOI=10.1158/0008-5472.CAN-07-2370;
Li L., Ryser S., Dizin E., Pils D., Krainer M., Jefford C.E.,
Bertoni F., Zeillinger R., Irminger-Finger I.;
"Oncogenic BARD1 isoforms expressed in gynecological cancers.";
Cancer Res. 67:11876-11885(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
DOMAINS.
PubMed=10026184; DOI=10.1074/jbc.274.9.5659;
Meza J.E., Brzovic P.S., King M.-C., Klevit R.E.;
"Mapping the functional domains of BRCA1. Interaction of the ring
finger domains of BRCA1 and BARD1.";
J. Biol. Chem. 274:5659-5665(1999).
[7]
POSSIBLE FUNCTION.
PubMed=10477523; DOI=10.1126/science.285.5433.1576;
Kleiman F.E., Manley J.L.;
"Functional interaction of BRCA1-associated BARD1 with polyadenylation
factor CstF-50.";
Science 285:1576-1579(1999).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH BRCA1.
PubMed=12890688; DOI=10.1074/jbc.C300249200;
Wu-Baer F., Lagrazon K., Yuan W., Baer R.;
"The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an
unconventional linkage involving lysine residue K6 of ubiquitin.";
J. Biol. Chem. 278:34743-34746(2003).
[9]
FUNCTION, AND INTERACTION WITH BRCA1.
PubMed=14976165; DOI=10.1093/hmg/ddh095;
Morris J.R., Solomon E.;
"BRCA1:BARD1 induces the formation of conjugated ubiquitin structures,
dependent on K6 of ubiquitin, in cells during DNA replication and
repair.";
Hum. Mol. Genet. 13:807-817(2004).
[10]
IDENTIFICATION IN THE BRCA1-A COMPLEX.
PubMed=17643122; DOI=10.1038/nsmb1277;
Kim H., Huang J., Chen J.;
"CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA
damage response.";
Nat. Struct. Mol. Biol. 14:710-715(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391 AND THR-394, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
IDENTIFICATION IN THE BRCA1-A COMPLEX.
PubMed=19261749; DOI=10.1101/gad.1770309;
Wang B., Hurov K., Hofmann K., Elledge S.J.;
"NBA1, a new player in the Brca1 A complex, is required for DNA damage
resistance and checkpoint control.";
Genes Dev. 23:729-739(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH BRCA1.
PubMed=20351172; DOI=10.1128/MCB.01056-09;
Wu-Baer F., Ludwig T., Baer R.;
"The UBXN1 protein associates with autoubiquitinated forms of the
BRCA1 tumor suppressor and inhibits its enzymatic function.";
Mol. Cell. Biol. 30:2787-2798(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND THR-299, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-170, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-160; LYS-170; LYS-423 AND
LYS-548, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[19]
STRUCTURE BY NMR OF 26-140 IN COMPLEX WITH BRCA1 AND ZINC IONS, AND
SUBUNIT.
PubMed=11573085; DOI=10.1038/nsb1001-833;
Brzovic P.S., Rajagopal P., Hoyt D.W., King M.C., Klevit R.E.;
"Structure of a BRCA1-BARD1 heterodimeric RING-RING complex.";
Nat. Struct. Biol. 8:833-837(2001).
[20]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 568-777.
PubMed=17550235; DOI=10.1021/bi700323t;
Birrane G., Varma A.K., Soni A., Ladias J.A.;
"Crystal structure of the BARD1 BRCT domains.";
Biochemistry 46:7706-7712(2007).
[21]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 569-777, INTERACTION WITH
CSTF1, DOMAIN STRUCTURE, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18842000; DOI=10.1021/bi801115g;
Edwards R.A., Lee M.S., Tsutakawa S.E., Williams R.S., Nazeer I.,
Kleiman F.E., Tainer J.A., Glover J.N.;
"The BARD1 C-terminal domain structure and interactions with
polyadenylation factor CstF-50.";
Biochemistry 47:11446-11456(2008).
[22]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 425-555, IDENTIFICATION BY
MASS SPECTROMETRY, DOMAINS ANK REPEATS, AND DOMAIN STRUCTURE.
PubMed=18480049; DOI=10.1074/jbc.M802333200;
Fox D. III, Le Trong I., Rajagopal P., Brzovic P.S., Stenkamp R.E.,
Klevit R.E.;
"Crystal structure of the BARD1 ankyrin repeat domain and its
functional consequences.";
J. Biol. Chem. 283:21179-21186(2008).
-!- FUNCTION: E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer
specifically mediates the formation of 'Lys-6'-linked
polyubiquitin chains and coordinates a diverse range of cellular
pathways such as DNA damage repair, ubiquitination and
transcriptional regulation to maintain genomic stability. Plays a
central role in the control of the cell cycle in response to DNA
damage. Acts by mediating ubiquitin E3 ligase activity that is
required for its tumor suppressor function. Also forms a
heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and
RNAP II stability by inhibiting pre-mRNA 3' cleavage.
{ECO:0000269|PubMed:12890688, ECO:0000269|PubMed:14976165,
ECO:0000269|PubMed:20351172}.
-!- 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:0000269|PubMed:12890688,
ECO:0000269|PubMed:20351172}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Homo- and heterodimer. Heterodimer (RING-type zinc
finger) with BRCA1. Heterodimer (via ANK repeats and BRCT domains)
with CSTF1/CSTF-50. Component of the BRCA1-A complex, at least
composed of the BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36,
BABAM2 and BABAM1/NBA1. Interacts with UBXN1.
{ECO:0000269|PubMed:11573085, ECO:0000269|PubMed:12890688,
ECO:0000269|PubMed:14976165, ECO:0000269|PubMed:17643122,
ECO:0000269|PubMed:18842000, ECO:0000269|PubMed:19261749,
ECO:0000269|PubMed:20351172}.
-!- INTERACTION:
P38398:BRCA1; NbExp=14; IntAct=EBI-473181, EBI-349905;
Q9P2H0:CEP126; NbExp=2; IntAct=EBI-473181, EBI-473176;
Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-473181, EBI-739624;
Q12873:CHD3; NbExp=2; IntAct=EBI-473181, EBI-523590;
Q05048:CSTF1; NbExp=4; IntAct=EBI-473181, EBI-1789619;
P33240:CSTF2; NbExp=8; IntAct=EBI-473181, EBI-711360;
O00471:EXOC5; NbExp=3; IntAct=EBI-473181, EBI-949824;
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-473181, EBI-10175124;
Q9Y2X7:GIT1; NbExp=2; IntAct=EBI-473181, EBI-466061;
Q08379:GOLGA2; NbExp=5; IntAct=EBI-473181, EBI-618309;
O95251:KAT7; NbExp=2; IntAct=EBI-473181, EBI-473199;
Q6A162:KRT40; NbExp=3; IntAct=EBI-473181, EBI-10171697;
O95751:LDOC1; NbExp=5; IntAct=EBI-473181, EBI-740738;
Q5JR59-3:MTUS2; NbExp=4; IntAct=EBI-473181, EBI-11522433;
O95453:PARN; NbExp=4; IntAct=EBI-473181, EBI-372832;
O14776:TCERG1; NbExp=2; IntAct=EBI-473181, EBI-473271;
-!- SUBCELLULAR LOCATION: Nucleus. Note=During S phase of the cell
cycle, colocalizes with BRCA1 into discrete subnuclear foci. Can
translocate to the cytoplasm. Localizes at sites of DNA damage at
double-strand breaks (DSBs); recruitment to DNA damage sites is
mediated by the BRCA1-A complex.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=FL;
IsoId=Q99728-1; Sequence=Displayed;
Name=alpha;
IsoId=Q99728-2; Sequence=VSP_055876;
Name=beta;
IsoId=Q99728-3; Sequence=VSP_055874, VSP_055875;
Name=gamma;
IsoId=Q99728-4; Sequence=VSP_055877, VSP_055878;
-!- PTM: Processed during apoptosis. The homodimer is more susceptible
to proteolytic cleavage than the BARD1/BRCA1 heterodimer.
-!- CAUTION: It is uncertain whether Met-1 or Met-26 is the initiator.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BARD1ID756ch2q35.html";
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EMBL; U76638; AAB38316.1; -; mRNA.
EMBL; AF038042; AAB99978.1; -; Genomic_DNA.
EMBL; AF038034; AAB99978.1; JOINED; Genomic_DNA.
EMBL; AF038035; AAB99978.1; JOINED; Genomic_DNA.
EMBL; AF038036; AAB99978.1; JOINED; Genomic_DNA.
EMBL; AF038037; AAB99978.1; JOINED; Genomic_DNA.
EMBL; AF038038; AAB99978.1; JOINED; Genomic_DNA.
EMBL; AF038039; AAB99978.1; JOINED; Genomic_DNA.
EMBL; AF038040; AAB99978.1; JOINED; Genomic_DNA.
EMBL; AF038041; AAB99978.1; JOINED; Genomic_DNA.
EMBL; JF790280; AEF57471.1; -; mRNA.
EMBL; JF790281; AEF57472.1; -; mRNA.
EMBL; JF790282; AEF57473.1; -; mRNA.
EMBL; AC016708; AAX93130.1; -; Genomic_DNA.
EMBL; BC126426; AAI26427.1; -; mRNA.
CCDS; CCDS2397.1; -. [Q99728-1]
CCDS; CCDS74646.1; -. [Q99728-2]
RefSeq; NP_000456.2; NM_000465.3. [Q99728-1]
RefSeq; NP_001269472.1; NM_001282543.1. [Q99728-2]
UniGene; Hs.591642; -.
UniGene; Hs.597413; -.
PDB; 1JM7; NMR; -; B=26-140.
PDB; 2NTE; X-ray; 1.90 A; A/B=568-777.
PDB; 2R1Z; X-ray; 2.10 A; A/B=569-777.
PDB; 3C5R; X-ray; 2.00 A; A/B=425-555.
PDB; 3FA2; X-ray; 2.20 A; A/B=566-777.
PDBsum; 1JM7; -.
PDBsum; 2NTE; -.
PDBsum; 2R1Z; -.
PDBsum; 3C5R; -.
PDBsum; 3FA2; -.
ProteinModelPortal; Q99728; -.
SMR; Q99728; -.
BioGrid; 107056; 270.
CORUM; Q99728; -.
DIP; DIP-5972N; -.
IntAct; Q99728; 44.
MINT; MINT-207047; -.
STRING; 9606.ENSP00000260947; -.
BindingDB; Q99728; -.
iPTMnet; Q99728; -.
PhosphoSitePlus; Q99728; -.
BioMuta; BARD1; -.
DMDM; 116241265; -.
EPD; Q99728; -.
MaxQB; Q99728; -.
PaxDb; Q99728; -.
PeptideAtlas; Q99728; -.
PRIDE; Q99728; -.
Ensembl; ENST00000260947; ENSP00000260947; ENSG00000138376. [Q99728-1]
Ensembl; ENST00000617164; ENSP00000480470; ENSG00000138376. [Q99728-2]
Ensembl; ENST00000620057; ENSP00000481988; ENSG00000138376. [Q99728-4]
GeneID; 580; -.
KEGG; hsa:580; -.
UCSC; uc002veu.4; human. [Q99728-1]
CTD; 580; -.
DisGeNET; 580; -.
EuPathDB; HostDB:ENSG00000138376.10; -.
GeneCards; BARD1; -.
H-InvDB; HIX0030010; -.
HGNC; HGNC:952; BARD1.
HPA; CAB034106; -.
HPA; HPA035354; -.
HPA; HPA044864; -.
MalaCards; BARD1; -.
MIM; 601593; gene.
neXtProt; NX_Q99728; -.
OpenTargets; ENSG00000138376; -.
Orphanet; 145; Hereditary breast and ovarian cancer syndrome.
PharmGKB; PA25256; -.
eggNOG; KOG0504; Eukaryota.
eggNOG; KOG4362; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00760000119090; -.
HOGENOM; HOG000237306; -.
HOVERGEN; HBG050662; -.
InParanoid; Q99728; -.
KO; K10683; -.
OMA; KNSIKMW; -.
OrthoDB; EOG091G0JNZ; -.
PhylomeDB; Q99728; -.
TreeFam; TF326440; -.
Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689901; Metalloprotease DUBs.
Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
SignaLink; Q99728; -.
SIGNOR; Q99728; -.
UniPathway; UPA00143; -.
ChiTaRS; BARD1; human.
EvolutionaryTrace; Q99728; -.
GeneWiki; BARD1; -.
GenomeRNAi; 580; -.
PRO; PR:Q99728; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000138376; -.
CleanEx; HS_BARD1; -.
ExpressionAtlas; Q99728; baseline and differential.
Genevisible; Q99728; HS.
GO; GO:0070531; C:BRCA1-A complex; IDA:UniProtKB.
GO; GO:0031436; C:BRCA1-BARD1 complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000151; C:ubiquitin ligase complex; NAS:UniProtKB.
GO; GO:0019900; F:kinase binding; NAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; NAS:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; NAS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; NAS:UniProtKB.
GO; GO:0000729; P:DNA double-strand break processing; TAS:Reactome.
GO; GO:0006260; P:DNA replication; TAS:Reactome.
GO; GO:0000731; P:DNA synthesis involved in DNA repair; TAS:Reactome.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0031441; P:negative regulation of mRNA 3'-end processing; NAS:UniProtKB.
GO; GO:0046826; P:negative regulation of protein export from nucleus; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0045732; P:positive regulation of protein catabolic process; NAS:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0085020; P:protein K6-linked ubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; NAS:UniProtKB.
GO; GO:0042325; P:regulation of phosphorylation; IMP:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0000732; P:strand displacement; TAS:Reactome.
GO; GO:0001894; P:tissue homeostasis; TAS:UniProtKB.
CDD; cd00204; ANK; 1.
CDD; cd00027; BRCT; 2.
Gene3D; 1.25.40.20; -; 2.
Gene3D; 3.30.40.10; -; 1.
Gene3D; 3.40.50.10190; -; 2.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR033097; BARD1.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR036420; BRCT_dom_sf.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
PANTHER; PTHR24171:SF8; PTHR24171:SF8; 1.
Pfam; PF12796; Ank_2; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 3.
SMART; SM00292; BRCT; 2.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF52113; SSF52113; 2.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 3.
PROSITE; PS50172; BRCT; 2.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ANK repeat; Complete proteome;
DNA damage; DNA repair; Isopeptide bond; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 777 BRCA1-associated RING domain protein 1.
/FTId=PRO_0000055819.
REPEAT 427 459 ANK 1.
REPEAT 460 492 ANK 2.
REPEAT 493 525 ANK 3.
REPEAT 526 546 ANK 4; degenerate.
DOMAIN 560 653 BRCT 1. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 667 777 BRCT 2. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
ZN_FING 50 87 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 26 119 Interaction with BRCA1.
REGION 554 558 Flexible linker.
COMPBIAS 400 403 Poly-Ser.
COMPBIAS 542 545 Poly-Leu.
MOD_RES 186 186 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 299 299 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 391 391 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 394 394 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
CROSSLNK 160 160 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 170 170 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 423 423 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 548 548 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 24 MPDNRQPRNRQPRIRSGNEPRSAP -> MVAVPGPTVAPRS
TAWRSCCAARV (in isoform beta).
{ECO:0000303|PubMed:18089818}.
/FTId=VSP_055874.
VAR_SEQ 25 121 Missing (in isoform beta).
{ECO:0000303|PubMed:18089818}.
/FTId=VSP_055875.
VAR_SEQ 54 72 Missing (in isoform alpha).
{ECO:0000303|PubMed:18089818}.
/FTId=VSP_055876.
VAR_SEQ 122 127 DLKEDK -> GRHTFC (in isoform gamma).
{ECO:0000303|PubMed:18089818}.
/FTId=VSP_055877.
VAR_SEQ 128 777 Missing (in isoform gamma).
{ECO:0000303|PubMed:18089818}.
/FTId=VSP_055878.
VARIANT 24 24 P -> S (common polymorphism in
Caucasians; less frequent in Africans;
dbSNP:rs1048108).
{ECO:0000269|PubMed:9425226}.
/FTId=VAR_010354.
VARIANT 153 153 K -> E (in dbSNP:rs753377280).
{ECO:0000269|PubMed:9425226}.
/FTId=VAR_010355.
VARIANT 186 186 S -> G (in dbSNP:rs16852741).
/FTId=VAR_038371.
VARIANT 241 241 S -> C (in dbSNP:rs3738885).
/FTId=VAR_020109.
VARIANT 378 378 R -> S (in dbSNP:rs2229571).
{ECO:0000269|PubMed:9425226}.
/FTId=VAR_024611.
VARIANT 507 507 V -> M (in dbSNP:rs2070094).
{ECO:0000269|PubMed:9425226}.
/FTId=VAR_010356.
VARIANT 557 557 C -> S (rare polymorphism in Caucasians;
dbSNP:rs28997576).
{ECO:0000269|PubMed:9425226}.
/FTId=VAR_010357.
VARIANT 564 564 Q -> H (in an ovarian clear cell
adenocarcinoma).
{ECO:0000269|PubMed:9425226}.
/FTId=VAR_010358.
VARIANT 645 645 C -> R (in dbSNP:rs34744268).
/FTId=VAR_038372.
VARIANT 658 658 R -> C (rare polymorphism in Caucasians;
absent in Africans; dbSNP:rs3738888).
{ECO:0000269|PubMed:9425226}.
/FTId=VAR_010359.
VARIANT 695 695 V -> L (in a breast cancer sample;
somatic mutation; dbSNP:rs111367604).
{ECO:0000269|PubMed:9425226}.
/FTId=VAR_010360.
VARIANT 728 728 S -> F (in dbSNP:rs13389423).
/FTId=VAR_028309.
VARIANT 761 761 S -> N (in an uterine cancer sample;
somatic mutation; dbSNP:rs142155101).
{ECO:0000269|PubMed:9425226}.
/FTId=VAR_010361.
CONFLICT 85 85 V -> A (in Ref. 3; AEF57473).
{ECO:0000305}.
CONFLICT 406 406 R -> Q (in Ref. 1; AAB38316 and 3;
AEF57471/AEF57472). {ECO:0000305}.
HELIX 35 46 {ECO:0000244|PDB:1JM7}.
STRAND 51 53 {ECO:0000244|PDB:1JM7}.
STRAND 65 67 {ECO:0000244|PDB:1JM7}.
TURN 72 74 {ECO:0000244|PDB:1JM7}.
HELIX 75 78 {ECO:0000244|PDB:1JM7}.
TURN 79 81 {ECO:0000244|PDB:1JM7}.
STRAND 84 86 {ECO:0000244|PDB:1JM7}.
HELIX 99 116 {ECO:0000244|PDB:1JM7}.
HELIX 431 438 {ECO:0000244|PDB:3C5R}.
HELIX 441 449 {ECO:0000244|PDB:3C5R}.
HELIX 464 470 {ECO:0000244|PDB:3C5R}.
HELIX 474 482 {ECO:0000244|PDB:3C5R}.
HELIX 492 494 {ECO:0000244|PDB:3C5R}.
HELIX 497 503 {ECO:0000244|PDB:3C5R}.
HELIX 507 515 {ECO:0000244|PDB:3C5R}.
HELIX 530 533 {ECO:0000244|PDB:3C5R}.
HELIX 537 543 {ECO:0000244|PDB:3C5R}.
STRAND 571 576 {ECO:0000244|PDB:2NTE}.
HELIX 579 591 {ECO:0000244|PDB:2NTE}.
STRAND 595 599 {ECO:0000244|PDB:2NTE}.
STRAND 606 613 {ECO:0000244|PDB:2NTE}.
HELIX 618 625 {ECO:0000244|PDB:2NTE}.
STRAND 629 632 {ECO:0000244|PDB:2NTE}.
HELIX 634 642 {ECO:0000244|PDB:2NTE}.
HELIX 648 650 {ECO:0000244|PDB:2NTE}.
HELIX 656 665 {ECO:0000244|PDB:2NTE}.
TURN 671 674 {ECO:0000244|PDB:2NTE}.
STRAND 676 679 {ECO:0000244|PDB:2NTE}.
STRAND 684 686 {ECO:0000244|PDB:2NTE}.
HELIX 688 697 {ECO:0000244|PDB:2NTE}.
STRAND 701 705 {ECO:0000244|PDB:2NTE}.
HELIX 709 711 {ECO:0000244|PDB:2NTE}.
HELIX 713 715 {ECO:0000244|PDB:2NTE}.
HELIX 729 731 {ECO:0000244|PDB:2NTE}.
STRAND 735 739 {ECO:0000244|PDB:2NTE}.
STRAND 750 752 {ECO:0000244|PDB:2NTE}.
STRAND 755 759 {ECO:0000244|PDB:2NTE}.
HELIX 760 769 {ECO:0000244|PDB:2NTE}.
SEQUENCE 777 AA; 86648 MW; 95E2D904046B5646 CRC64;
MPDNRQPRNR QPRIRSGNEP RSAPAMEPDG RGAWAHSRAA LDRLEKLLRC SRCTNILREP
VCLGGCEHIF CSNCVSDCIG TGCPVCYTPA WIQDLKINRQ LDSMIQLCSK LRNLLHDNEL
SDLKEDKPRK SLFNDAGNKK NSIKMWFSPR SKKVRYVVSK ASVQTQPAIK KDASAQQDSY
EFVSPSPPAD VSERAKKASA RSGKKQKKKT LAEINQKWNL EAEKEDGEFD SKEESKQKLV
SFCSQPSVIS SPQINGEIDL LASGSLTESE CFGSLTEVSL PLAEQIESPD TKSRNEVVTP
EKVCKNYLTS KKSLPLENNG KRGHHNRLSS PISKRCRTSI LSTSGDFVKQ TVPSENIPLP
ECSSPPSCKR KVGGTSGRKN SNMSDEFISL SPGTPPSTLS SSSYRRVMSS PSAMKLLPNM
AVKRNHRGET LLHIASIKGD IPSVEYLLQN GSDPNVKDHA GWTPLHEACN HGHLKVVELL
LQHKALVNTT GYQNDSPLHD AAKNGHVDIV KLLLSYGASR NAVNIFGLRP VDYTDDESMK
SLLLLPEKNE SSSASHCSVM NTGQRRDGPL VLIGSGLSSE QQKMLSELAV ILKAKKYTEF
DSTVTHVVVP GDAVQSTLKC MLGILNGCWI LKFEWVKACL RRKVCEQEEK YEIPEGPRRS
RLNREQLLPK LFDGCYFYLW GTFKHHPKDN LIKLVTAGGG QILSRKPKPD SDVTQTINTV
AYHARPDSDQ RFCTQYIIYE DLCNYHPERV RQGKVWKAPS SWFIDCVMSF ELLPLDS


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