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Breast cancer type 1 susceptibility protein (EC 2.3.2.27) (RING finger protein 53) (RING-type E3 ubiquitin transferase BRCA1)

 BRCA1_HUMAN             Reviewed;        1863 AA.
P38398; E9PFZ0; O15129; Q1RMC1; Q3LRJ0; Q3LRJ6; Q6IN79; Q7KYU9;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 2.
30-AUG-2017, entry version 228.
RecName: Full=Breast cancer type 1 susceptibility protein;
EC=2.3.2.27 {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:12887909, ECO:0000269|PubMed:12890688, ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:20351172};
AltName: Full=RING finger protein 53;
AltName: Full=RING-type E3 ubiquitin transferase BRCA1 {ECO:0000305};
Name=BRCA1; Synonyms=RNF53;
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 VARIANT BC ARG-1775.
PubMed=7545954; DOI=10.1126/science.7545954;
Miki Y., Swensen J., Shattuck-Eidens D., Futreal P.A., Harshman K.,
Tavtigian S., Liu Q., Cochran C., Bennett L.M., Ding W., Bell R.,
Rosenthal J., Hussey C., Tran T., McClure M., Frye C., Hattier T.,
Phelps R., Haugen-Strano A., Katcher H., Yakumo K., Gholami Z.,
Shaffer D., Stone S., Bayer S., Wray C., Bogden R., Dayananth P.,
Ward J., Tonin P., Narod S., Bristow P.K., Norris F.H., Helvering L.,
Morrison P., Rosteck P., Lai M., Barrett J.C., Lewis C., Neuhausen S.,
Cannon-Albright L., Godlgar D., Wiseman R., Kamb A., Skolnick M.H.;
"A strong candidate for the breast and ovarian cancer susceptibility
gene BRCA1.";
Science 266:66-71(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8938427; DOI=10.1101/gr.6.11.1029;
Smith T.M., Lee M.K., Szabo C.I., Jerome N., McEuen M., Taylor M.,
Hood L., King M.-C.;
"Complete genomic sequence and analysis of 117 kb of human DNA
containing the gene BRCA1.";
Genome Res. 6:1029-1049(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION (ISOFORM
2), VARIANTS ARG-239 AND GLY-1613, AND TISSUE SPECIFICITY (ISOFORMS 1
AND 3).
TISSUE=Mammary gland;
PubMed=9010228; DOI=10.1038/sj.onc.1200924;
Wilson C.A., Payton M.N., Elliott G.S., Buaas F.W., Cajulis E.E.,
Grosshans D., Ramos L., Reese D.M., Slamon D.J., Calzone F.J.;
"Differential subcellular localization, expression and biological
toxicity of BRCA1 and the splice variant BRCA1-delta11b.";
Oncogene 14:1-16(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Testis;
Holt J.T., Robinson-Benion C.;
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-356.
Raymond C.K., Paddock M., Subramanian S., Deodato C., Zhou Y.,
Haugen E., Kaul R., Olson M.V.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-275; ARG-356;
ASN-693; LEU-871; GLY-1038; ASN-1040; GLY-1140; ARG-1183; GLY-1613 AND
ALA-1620.
NIEHS SNPs program;
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 7), AND
VARIANTS LEU-871; GLY-1038; ARG-1183; GLY-1613 AND ILE-1652.
TISSUE=PNS;
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).
[9]
PROTEIN SEQUENCE OF 6-18 (ISOFORM 1), PROTEIN SEQUENCE OF 18-26
(ISOFORM 4), AND ALTERNATIVE INITIATION (ISOFORM 4).
PubMed=10851077; DOI=10.1038/sj.onc.1203599;
Liu J., Prolla G., Rostagno A., Chiarle R., Feiner H., Inghirami G.;
"Initiation of translation from a downstream in-frame AUG codon on
BRCA1 can generate the novel isoform protein DeltaBRCA1(17aa).";
Oncogene 19:2767-2773(2000).
[10]
ALTERNATIVE SPLICING (ISOFORM 5), AND SUBCELLULAR LOCATION (ISOFORM
5).
PubMed=8972225; DOI=10.1128/MCB.17.1.444;
Thakur S., Zhang H.B., Peng Y., Le H., Carroll B., Ward T., Yao J.,
Farid L.M., Couch F.J., Wilson R.B., Weber B.L.;
"Localization of BRCA1 and a splice variant identifies the nuclear
localization signal.";
Mol. Cell. Biol. 17:444-452(1997).
[11]
INTERACTION WITH BAP1, SUBCELLULAR LOCATION, VARIANTS GLY-61 AND
GLY-64, AND MUTAGENESIS OF ARG-71.
PubMed=9528852; DOI=10.1038/sj.onc.1201861;
Jensen D.E., Proctor M., Marquis S.T., Gardner H.P., Ha S.I.,
Chodosh L.A., Ishov A.M., Tommerup N., Vissing H., Sekido Y.,
Minna J., Borodovsky A., Schultz D.C., Wilkinson K.D., Maul G.G.,
Barlev N., Berger S., Prendergast G.C., Rauscher F.J. III;
"BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING
finger and enhances BRCA1-mediated cell growth suppression.";
Oncogene 16:1097-1112(1998).
[12]
INTERACTION WITH RBBP8.
PubMed=9811458; DOI=10.1038/sj.onc.1202150;
Wong A.K., Ormonde P.A., Pero R., Chen Y., Lian L., Salada G.,
Berry S., Lawrence Q., Dayananth P., Ha P., Tavtigian S.V., Teng D.H.,
Bartel P.L.;
"Characterization of a carboxy-terminal BRCA1 interacting protein.";
Oncogene 17:2279-2285(1998).
[13]
FUNCTION AS AN E2-DEPENDENT UBIQUITIN-PROTEIN LIGASE, AND CATALYTIC
ACTIVITY.
PubMed=10500182; DOI=10.1073/pnas.96.20.11364;
Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S.,
Weissman A.M.;
"RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent
ubiquitination.";
Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999).
[14]
IDENTIFICATION IN THE BASC COMPLEX.
PubMed=10783165;
Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.;
"BASC, a super complex of BRCA1-associated proteins involved in the
recognition and repair of aberrant DNA structures.";
Genes Dev. 14:927-939(2000).
[15]
PHOSPHORYLATION AT SER-1143; SER-1280; SER-1387; THR-1394; SER-1423
AND SER-1457, MUTAGENESIS OF SER-1143; SER-1239; SER-1280; SER-1298;
SER-1330; SER-1387; THR-1394; SER-1423; SER-1457; SER-1466; SER-1524
AND SER-1755, AND CHARACTERIZATION OF VARIANT BC ALA-1720.
PubMed=11114888; DOI=10.1101/gad.851000;
Tibbetts R.S., Cortez D., Brumbaugh K.M., Scully R., Livingston D.,
Elledge S.J., Abraham R.T.;
"Functional interactions between BRCA1 and the checkpoint kinase ATR
during genotoxic stress.";
Genes Dev. 14:2989-3002(2000).
[16]
FUNCTION IN DNA DAMAGE RESPONSE, PHOSPHORYLATION AT SER-988 BY CHEK2,
AND INTERACTION WITH CHEK2.
PubMed=10724175; DOI=10.1038/35004614;
Lee J.S., Collins K.M., Brown A.L., Lee C.H., Chung J.H.;
"hCds1-mediated phosphorylation of BRCA1 regulates the DNA damage
response.";
Nature 404:201-204(2000).
[17]
INTERACTION WITH BRIP1, CHARACTERIZATION OF VARIANT OVARIAN CANCER
ARG-1749, AND CHARACTERIZATION OF VARIANT BC ARG-1775.
PubMed=11301010; DOI=10.1016/S0092-8674(01)00304-X;
Cantor S.B., Bell D.W., Ganesan S., Kass E.M., Drapkin R.,
Grossman S., Wahrer D.C.R., Sgroi D.C., Lane W.S., Haber D.A.,
Livingston D.M.;
"BACH1, a novel helicase-like protein, interacts directly with BRCA1
and contributes to its DNA repair function.";
Cell 105:149-160(2001).
[18]
INTERACTION WITH NELFB.
PubMed=11739404; DOI=10.1083/jcb.200108049;
Ye Q., Hu Y.-F., Zhong H., Nye A.C., Belmont A.S., Li R.;
"BRCA1-induced large-scale chromatin unfolding and allele-specific
effects of cancer-predisposing mutations.";
J. Cell Biol. 155:911-921(2001).
[19]
INTERACTION WITH FANCD2.
PubMed=11239454; DOI=10.1016/S1097-2765(01)00173-3;
Garcia-Higuera I., Taniguchi T., Ganesan S., Meyn M.S., Timmers C.,
Hejna J., Grompe M., D'Andrea A.D.;
"Interaction of the Fanconi anemia proteins and BRCA1 in a common
pathway.";
Mol. Cell 7:249-262(2001).
[20]
PHOSPHORYLATION BY ATM, AND MUTAGENESIS OF SER-1387; SER-1423 AND
SER-1524.
PubMed=12183412;
Xu B., O'Donnell A.H., Kim S.-T., Kastan M.B.;
"Phosphorylation of serine 1387 in BRCA1 is specifically required for
the Atm-mediated S-phase checkpoint after ionizing irradiation.";
Cancer Res. 62:4588-4591(2002).
[21]
INTERACTION WITH H2AFX.
PubMed=12419185; DOI=10.1016/S0960-9822(02)01259-9;
Kobayashi J., Tauchi H., Sakamoto S., Nakamura A., Morishima K.,
Matsuura S., Kobayashi T., Tamai K., Tanimoto K., Komatsu K.;
"NBS1 localizes to gamma-H2AX foci through interaction with the
FHA/BRCT domain.";
Curr. Biol. 12:1846-1851(2002).
[22]
INTERACTION WITH SMC1A.
PubMed=11877377; DOI=10.1101/gad.970702;
Yazdi P.T., Wang Y., Zhao S., Patel N., Lee E.Y.-H.P., Qin J.;
"SMC1 is a downstream effector in the ATM/NBS1 branch of the human S-
phase checkpoint.";
Genes Dev. 16:571-582(2002).
[23]
INTERACTION WITH LMO4.
PubMed=11751867; DOI=10.1074/jbc.M110603200;
Sum E.Y., Peng B., Yu X., Chen J., Byrne J., Lindeman G.J.,
Visvader J.E.;
"The LIM domain protein LMO4 interacts with the cofactor CtIP and the
tumor suppressor BRCA1 and inhibits BRCA1 activity.";
J. Biol. Chem. 277:7849-7856(2002).
[24]
FUNCTION, AND INTERACTION WITH CHEK1.
PubMed=11836499; DOI=10.1038/ng837;
Yarden R.I., Pardo-Reoyo S., Sgagias M., Cowan K.H., Brody L.C.;
"BRCA1 regulates the G2/M checkpoint by activating Chk1 kinase upon
DNA damage.";
Nat. Genet. 30:285-289(2002).
[25]
INTERACTION WITH ACACA.
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).
[26]
FUNCTION, UBIQUITINATION, CATALYTIC ACTIVITY, AND INTERACTION WITH
BARD1.
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).
[27]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=12887909; DOI=10.1016/S1097-2765(03)00281-8;
Vandenberg C.J., Gergely F., Ong C.Y., Pace P., Mallery D.L., Hiom K.,
Patel K.J.;
"BRCA1-independent ubiquitination of FANCD2.";
Mol. Cell 12:247-254(2003).
[28]
INTERACTION WITH BRCC3.
PubMed=14636569; DOI=10.1016/S1097-2765(03)00424-6;
Dong Y., Hakimi M.-A., Chen X., Kumaraswamy E., Cooch N.S.,
Godwin A.K., Shiekhattar R.;
"Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2,
by a signalosome-like subunit and its role in DNA repair.";
Mol. Cell 12:1087-1099(2003).
[29]
FUNCTION, AND INTERACTION WITH BARD1.
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).
[30]
INTERACTION WITH AURKA, FUNCTION, MUTAGENESIS OF SER-308, AND
PHOSPHORYLATION AT SER-308.
PubMed=14990569; DOI=10.1074/jbc.M311780200;
Ouchi M., Fujiuchi N., Sasai K., Katayama H., Minamishima Y.A.,
Ongusaha P.P., Deng C., Sen S., Lee S.W., Ouchi T.;
"BRCA1 phosphorylation by Aurora-A in the regulation of G2 to M
transition.";
J. Biol. Chem. 279:19643-19648(2004).
[31]
INTERACTION WITH DCLRE1C.
PubMed=15456891; DOI=10.1128/MCB.24.20.9207-9220.2004;
Zhang X., Succi J., Feng Z., Prithivirajsingh S., Story M.D.,
Legerski R.J.;
"Artemis is a phosphorylation target of ATM and ATR and is involved in
the G2/M DNA damage checkpoint response.";
Mol. Cell. Biol. 24:9207-9220(2004).
[32]
INTERACTION WITH CLSPN.
PubMed=15096610; DOI=10.1073/pnas.0401847101;
Lin S.-Y., Li K., Stewart G.S., Elledge S.J.;
"Human claspin works with BRCA1 to both positively and negatively
regulate cell proliferation.";
Proc. Natl. Acad. Sci. U.S.A. 101:6484-6489(2004).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1336, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[34]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH RBBP8, AND MUTAGENESIS
OF ILE-26.
PubMed=16818604; DOI=10.1101/gad.1431006;
Yu X., Fu S., Lai M., Baer R., Chen J.;
"BRCA1 ubiquitinates its phosphorylation-dependent binding partner
CtIP.";
Genes Dev. 20:1721-1726(2006).
[35]
FUNCTION, AND INTERACTION WITH ACACA.
PubMed=16326698; DOI=10.1074/jbc.M504652200;
Moreau K., Dizin E., Ray H., Luquain C., Lefai E., Foufelle F.,
Billaud M., Lenoir G.M., Venezia N.D.;
"BRCA1 affects lipid synthesis through its interaction with acetyl-CoA
carboxylase.";
J. Biol. Chem. 281:3172-3181(2006).
[36]
INTERACTION WITH ACACA.
PubMed=16698035; DOI=10.1016/j.jmb.2006.04.010;
Ray H., Moreau K., Dizin E., Callebaut I., Venezia N.D.;
"ACCA phosphopeptide recognition by the BRCT repeats of BRCA1.";
J. Mol. Biol. 359:973-982(2006).
[37]
FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION BY AURKA, AND ENZYME
REGULATION.
PubMed=18056443; DOI=10.1158/0008-5472.CAN-07-2578;
Sankaran S., Crone D.E., Palazzo R.E., Parvin J.D.;
"Aurora-A kinase regulates breast cancer associated gene 1 inhibition
of centrosome-dependent microtubule nucleation.";
Cancer Res. 67:11186-11194(2007).
[38]
INTERACTION WITH ABRAXAS1.
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).
[39]
INTERACTION WITH ABRAXAS1.
PubMed=17643121; DOI=10.1038/nsmb1279;
Liu Z., Wu J., Yu X.;
"CCDC98 targets BRCA1 to DNA damage sites.";
Nat. Struct. Mol. Biol. 14:716-720(2007).
[40]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
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).
[41]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ABRAXAS1.
PubMed=17525340; DOI=10.1126/science.1139476;
Wang B., Matsuoka S., Ballif B.A., Zhang D., Smogorzewska A., Giyi S.,
Elledge S.J.;
"Abraxas and RAP80 form a BRCA1 protein complex required for the DNA
damage response.";
Science 316:1194-1198(2007).
[42]
INVOLVEMENT IN PNCA4.
PubMed=18762988; DOI=10.1007/s00439-008-0554-0;
Al-Sukhni W., Rothenmund H., Borgida A.E., Zogopoulos G., O'Shea A.M.,
Pollett A., Gallinger S.;
"Germline BRCA1 mutations predispose to pancreatic adenocarcinoma.";
Hum. Genet. 124:271-278(2008).
[43]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395; SER-398; SER-753;
SER-1211; SER-1217 AND SER-1218, 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).
[44]
FUNCTION, AND IDENTIFICATION IN THE BRCA1-A COMPLEX.
PubMed=19261748; DOI=10.1101/gad.1770609;
Feng L., Huang J., Chen J.;
"MERIT40 facilitates BRCA1 localization and DNA damage repair.";
Genes Dev. 23:719-728(2009).
[45]
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).
[46]
IDENTIFICATION IN THE BRCA1-A COMPLEX.
PubMed=19261746; DOI=10.1101/gad.1739609;
Shao G., Patterson-Fortin J., Messick T.E., Feng D., Shanbhag N.,
Wang Y., Greenberg R.A.;
"MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA
double-strand breaks.";
Genes Dev. 23:740-754(2009).
[47]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH PALB2,
IDENTIFICATION IN A BRCA COMPLEX WITH BRCA1 AND PALB2, AND
CHARACTERIZATION OF VARIANT OVARIAN CANCER 1411-THR.
PubMed=19369211; DOI=10.1073/pnas.0811159106;
Sy S.M., Huen M.S., Chen J.;
"PALB2 is an integral component of the BRCA complex required for
homologous recombination repair.";
Proc. Natl. Acad. Sci. U.S.A. 106:7155-7160(2009).
[48]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395 AND SER-398, AND
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).
[49]
FUNCTION, INTERACTION WITH CCAR2, AND SUBCELLULAR LOCATION.
PubMed=20160719; DOI=10.1038/sj.bjc.6605577;
Hiraike H., Wada-Hiraike O., Nakagawa S., Koyama S., Miyamoto Y.,
Sone K., Tanikawa M., Tsuruga T., Nagasaka K., Matsumoto Y., Oda K.,
Shoji K., Fukuhara H., Saji S., Nakagawa K., Kato S., Yano T.,
Taketani Y.;
"Identification of DBC1 as a transcriptional repressor for BRCA1.";
Br. J. Cancer 102:1061-1067(2010).
[50]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BARD1 AND UBXN1,
UBIQUITINATION, AND MUTAGENESIS OF ILE-26.
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).
[51]
FUNCTION IN CHROMOSOMAL STABILITY, AND PHOSPHORYLATION AT SER-988 BY
CHEK2.
PubMed=20364141; DOI=10.1038/ncb2051;
Stolz A., Ertych N., Kienitz A., Vogel C., Schneider V., Fritz B.,
Jacob R., Dittmar G., Weichert W., Petersen I., Bastians H.;
"The CHK2-BRCA1 tumour suppressor pathway ensures chromosomal
stability in human somatic cells.";
Nat. Cell Biol. 12:492-499(2010).
[52]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-423; SER-694;
SER-1328; SER-1336 AND SER-1342, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[53]
PHOSPHORYLATION AT SER-1524, AND SUBCELLULAR LOCATION.
PubMed=21144835; DOI=10.1016/j.bbrc.2010.12.005;
Kang Y., Cheong H.M., Lee J.H., Song P.I., Lee K.H., Kim S.Y.,
Jun J.Y., You H.J.;
"Protein phosphatase 5 is necessary for ATR-mediated DNA repair.";
Biochem. Biophys. Res. Commun. 404:476-481(2011).
[54]
INTERACTION WITH PCLAF.
PubMed=21673012; DOI=10.1158/1541-7786.MCR-10-0503;
Kais Z., Barsky S.H., Mathsyaraja H., Zha A., Ransburgh D.J., He G.,
Pilarski R.T., Shapiro C.L., Huang K., Parvin J.D.;
"KIAA0101 interacts with BRCA1 and regulates centrosome number.";
Mol. Cancer Res. 9:1091-1099(2011).
[55]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-1218; SER-1336
AND SER-1342, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[56]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[57]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-434; SER-551;
SER-694; SER-708; SER-1009; SER-1189; SER-1191 AND SER-1542, 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).
[58]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-339; LYS-459; LYS-583;
LYS-654; LYS-734 AND LYS-739, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[59]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-339; LYS-443 AND LYS-583,
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).
[60]
INTERACTION WITH EXD2.
PubMed=26807646; DOI=10.1038/ncb3303;
Broderick R., Nieminuszczy J., Baddock H.T., Deshpande R.A.,
Gileadi O., Paull T.T., McHugh P.J., Niedzwiedz W.;
"EXD2 promotes homologous recombination by facilitating DNA end
resection.";
Nat. Cell Biol. 18:271-280(2016).
[61]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109; LYS-301; LYS-339;
LYS-443; LYS-459; LYS-519; LYS-583; LYS-918; LYS-987 AND LYS-1079, 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).
[62]
STRUCTURE BY NMR OF 1-110 IN COMPLEX WITH ZINC IONS AND BARD1, 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).
[63]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1646-1859, PARTIAL PROTEIN
SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11573086; DOI=10.1038/nsb1001-838;
Williams R.S., Green R., Glover J.N.;
"Crystal structure of the BRCT repeat region from the breast cancer-
associated protein BRCA1.";
Nat. Struct. Biol. 8:838-842(2001).
[64]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1646-1859 OF VARIANT BC
ARG-1775, CHARACTERIZATION OF VARIANT BC ARG-1775, AND CIRCULAR
DICHROISM.
PubMed=12427738; DOI=10.1074/jbc.M210019200;
Williams R.S., Glover J.N.;
"Structural consequences of a cancer-causing BRCA1-BRCT missense
mutation.";
J. Biol. Chem. 278:2630-2635(2003).
[65]
STRUCTURE BY NMR OF 1755-1863.
PubMed=15609993; DOI=10.1021/bi049550q;
Gaiser O.J., Ball L.J., Schmieder P., Leitner D., Strauss H., Wahl M.,
Kuhne R., Oschkinat H., Heinemann U.;
"Solution structure, backbone dynamics, and association behavior of
the C-terminal BRCT domain from the breast cancer-associated protein
BRCA1.";
Biochemistry 43:15983-15995(2004).
[66]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1649-1859 IN COMPLEX WITH
WITH PHOSPHORYLATED BRIP1 PEPTIDE, MUTAGENESIS OF SER-1655; LYS-1702
AND GLY-1738, CHARACTERIZATION OF VARIANT OVARIAN CANCER ARG-1749,
CHARACTERIZATION OF VARIANT BC ARG-1775, SUBCELLULAR LOCATION, AND
INTERACTION WITH PHOSPHORYLATED BRIP1.
PubMed=15133502; DOI=10.1038/nsmb775;
Clapperton J.A., Manke I.A., Lowery D.M., Ho T., Haire L.F.,
Yaffe M.B., Smerdon S.J.;
"Structure and mechanism of BRCA1 BRCT domain recognition of
phosphorylated BACH1 with implications for cancer.";
Nat. Struct. Mol. Biol. 11:512-518(2004).
[67]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1646-1859 IN COMPLEX WITH
PHOSPHORYLATED RBBP8 PEPTIDE, AND SUBUNIT.
PubMed=16101277; DOI=10.1021/bi0509651;
Varma A.K., Brown R.S., Birrane G., Ladias J.A.;
"Structural basis for cell cycle checkpoint control by the BRCA1-CtIP
complex.";
Biochemistry 44:10941-10946(2005).
[68]
X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS) OF 1646-1859 IN COMPLEX WITH
PHOSPHORYLATED ACACA PEPTIDE, AND SUBUNIT.
PubMed=18452305; DOI=10.1021/bi800314m;
Shen Y., Tong L.;
"Structural evidence for direct interactions between the BRCT domains
of human BRCA1 and a phospho-peptide from human ACC1.";
Biochemistry 47:5767-5773(2008).
[69]
X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 1649-1859 OF VARIANT BC
LYS-1775, VARIANT BC LYS-1775, AND CHARACTERIZATION OF VARIANT BC
LYS-1775.
PubMed=18285836; DOI=10.1038/ejhg.2008.13;
Tischkowitz M., Hamel N., Carvalho M.A., Birrane G., Soni A.,
van Beers E.H., Joosse S.A., Wong N., Novak D., Quenneville L.A.,
Grist S.A., Nederlof P.M., Goldgar D.E., Tavtigian S.V.,
Monteiro A.N., Ladias J.A., Foulkes W.D.;
"Pathogenicity of the BRCA1 missense variant M1775K is determined by
the disruption of the BRCT phosphopeptide-binding pocket: a multi-
modal approach.";
Eur. J. Hum. Genet. 16:820-832(2008).
[70]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1646-1859 IN COMPLEX WITH
PHOSPHORYLATED PEPTIDES, AND DOMAIN.
PubMed=20159462; DOI=10.1016/j.str.2009.12.008;
Campbell S.J., Edwards R.A., Glover J.N.;
"Comparison of the structures and peptide binding specificities of the
BRCT domains of MDC1 and BRCA1.";
Structure 18:167-176(2010).
[71]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1646-1859 IN COMPLEX WITH
PHOSPHORYLATED BRIP1 PEPTIDE, INTERACTION WITH BRIP1, MUTAGENESIS OF
GLY-1656; THR-1700; ARG-1835 AND GLU-1836, AND CHARACTERIZATION OF
VARIANTS BC GLN-1699 AND TRP-1699.
PubMed=21473589; DOI=10.1021/bi2003795;
Coquelle N., Green R., Glover J.N.;
"Impact of BRCA1 BRCT domain missense substitutions on phosphopeptide
recognition.";
Biochemistry 50:4579-4589(2011).
[72]
X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 1649-1859 IN COMPLEX WITH
ABRAXAS1, AND INTERACTION WITH ABRAXAS1.
PubMed=24316840; DOI=10.1107/S1744309113030649;
Badgujar D.C., Sawant U., Vikrant X., Yadav L., Hosur M.V.,
Varma A.K.;
"Preliminary crystallographic studies of BRCA1 BRCT-ABRAXAS complex.";
Acta Crystallogr. F 69:1401-1404(2013).
[73]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1646-1859 IN COMPLEX WITH
ABRAXAS1, INTERACTION WITH ABRAXAS1, SUBUNIT, SUBCELLULAR LOCATION,
AND MUTAGENESIS OF PHE-1662; MET-1663; TYR-1666; ARG-1670 AND
LYS-1671.
PubMed=26778126; DOI=10.1016/j.molcel.2015.12.017;
Wu Q., Paul A., Su D., Mehmood S., Foo T.K., Ochi T., Bunting E.L.,
Xia B., Robinson C.V., Wang B., Blundell T.L.;
"Structure of BRCA1-BRCT/Abraxas complex reveals phosphorylation-
dependent BRCT dimerization at DNA damage sites.";
Mol. Cell 61:434-448(2016).
[74]
REVIEW ON VARIANTS.
PubMed=8807330; DOI=10.1002/humu.1380080102;
Couch F.J., Weber B.L.;
"Mutations and polymorphisms in the familial early-onset breast cancer
(BRCA1) gene.";
Hum. Mutat. 8:8-18(1996).
[75]
VARIANT BC ARG-1775, AND VARIANTS LEU-1637 AND GLU-1708.
PubMed=7939630; DOI=10.1126/science.7939630;
Futreal P.A., Liu Q., Shattuck-Eidens D., Cochran C., Harshman K.,
Tavtigian S., Bennett L.M., Haugen-Strano A., Swensen J., Miki Y.,
Eddington K., McClure M., Frye C., Weaver-Felhaus J., Ding W.,
Gholami Z., Soederkvist P., Terry L., Jhanwar S., Berchuk A.,
Iglehart J.D., Marks J., Ballinger D.G., Barrett J.C., Skolnick M.H.,
Kamb A., Wiseman R.;
"BRCA1 mutations in primary breast and ovarian carcinomas.";
Science 266:120-122(1994).
[76]
VARIANT BC GLY-64, AND VARIANTS ALA-772; ASN-1040 AND GLY-1443.
PubMed=7894491; DOI=10.1038/ng1294-387;
Castilla L.H., Couch F.J., Erdos M.R., Hoskins K.F., Calzone K.,
Garber J.E., Boyd J., Lubin M.B., Deshano M.L., Brody L.C.,
Collins F.S., Weber B.L.;
"Mutations in the BRCA1 gene in families with early-onset breast and
ovarian cancer.";
Nat. Genet. 8:387-391(1994).
[77]
VARIANT BC GLY-61, AND VARIANTS ARG-356; GLY-1038; ASN-1040; ARG-1183
AND GLY-1613.
PubMed=7894493; DOI=10.1038/ng1294-399;
Friedman L.S., Ostermeyer E.A., Szabo C.I., Dowd P., Lynch E.D.,
Rowell S.E., King M.-C.;
"Confirmation of BRCA1 by analysis of germline mutations linked to
breast and ovarian cancer in ten families.";
Nat. Genet. 8:399-404(1994).
[78]
VARIANT BC GLY-61.
PubMed=8554067;
Serova O., Montagna M., Torchard D., Narod S.A., Tonin P., Sylla B.,
Lynch H.T., Feunteun J., Lenoir G.M.;
"A high incidence of BRCA1 mutations in 20 breast-ovarian cancer
families.";
Am. J. Hum. Genet. 58:42-51(1996).
[79]
VARIANT BROVCA1 TRP-841.
PubMed=8968716;
DOI=10.1002/(SICI)1098-2272(1996)13:6<595::AID-GEPI5>3.3.CO;2-0;
Barker D.F., Almeida E.F.A., Casey G., Fain P.R., Liao S.-Y.,
Masunaka I., Noble B., Kurosaki T., Anton-Culver H.;
"BRCA1 R841W: a strong candidate for a common mutation with moderate
phenotype.";
Genet. Epidemiol. 13:595-604(1996).
[80]
VARIANTS BC AND BROVCA1.
PubMed=8776600; DOI=10.1093/hmg/5.6.835;
Durocher F., Shattuck-Eidens D., McClure M., Labrie F., Skolnick M.H.,
Goldgar D.E., Simard J.;
"Comparison of BRCA1 polymorphisms, rare sequence variants and/or
missense mutations in unaffected and breast/ovarian cancer
populations.";
Hum. Mol. Genet. 5:835-842(1996).
[81]
VARIANTS BC MET-271 AND SER-1150.
PubMed=8723683;
DOI=10.1002/(SICI)1098-1004(1996)7:4<334::AID-HUMU7>3.3.CO;2-K;
Katagiri T., Emi M., Ito I., Kobayashi K., Yoshimoto M., Iwase T.,
Kasumi F., Miki Y., Skolnick M.H., Nakamura Y.;
"Mutations in the BRCA1 gene in Japanese breast cancer patients.";
Hum. Mutat. 7:334-339(1996).
[82]
VARIANT BC GLY-61, AND VARIANTS ARG-239; TRP-841 AND ILE-1512.
PubMed=9760198; DOI=10.1007/s004390050799;
Dong J., Chang-Claude J., Wu Y., Schumacher V., Debatin I., Tonin P.,
Royer-Pokora B.;
"A high proportion of mutations in the BRCA1 gene in German
breast/ovarian cancer families with clustering of mutations in the 3'
third of the gene.";
Hum. Genet. 103:154-161(1998).
[83]
VARIANT BC GLY-64, AND VARIANTS ALA-772; GLU-820; ASN-1040; GLY-1443;
ILE-1512; LEU-1637 AND ILE-1652.
PubMed=9482581;
DOI=10.1002/(SICI)1098-1004(1998)11:2<166::AID-HUMU10>3.0.CO;2-X;
Andersen T.I., Eiken H.G., Couch F., Kaada G., Skrede M., Johnsen H.,
Aloysius T.A., Tveit K.M., Tranebjaerg L., Doerum A., Moeller P.,
Weber B.L., Boerresen-Dale A.-L.;
"Constant denaturant gel electrophoresis (CDGE) in BRCA1 mutation
screening.";
Hum. Mutat. 11:166-174(1998).
[84]
VARIANTS BC SER-22; LEU-461; ASP-465; VAL-552; SER-892; ASP-960;
ILE-1025 AND ALA-1047.
PubMed=9609997; DOI=10.1007/s100380050035;
Katagiri T., Kasumi F., Yoshimoto M., Nomizu T., Asaishi K., Abe R.,
Tsuchiya A., Sugano M., Takai S., Yoneda M., Fukutomi T., Nanba K.,
Makita M., Okazaki H., Hirata K., Okazaki M., Furutsuma Y.,
Morishita Y., Iino Y., Karino T., Ayabe H., Hara S., Kajiwara T.,
Houga S., Shimizu T., Toda M., Yamazaki Y., Uchida T., Kunitomo K.,
Sonoo H., Kurebayashi J., Shimotsuma K., Nakamura Y., Miki Y.;
"High proportion of missense mutations of the BRCA1 and BRCA2 genes in
Japanese breast cancer families.";
J. Hum. Genet. 43:42-48(1998).
[85]
VARIANT OVARIAN CANCER ARG-1749.
PubMed=10486320; DOI=10.1086/302583;
Gayther S.A., Russell P., Harrington P., Antoniou A.C., Easton D.F.,
Ponder B.A.J.;
"The contribution of germline BRCA1 and BRCA2 mutations to familial
ovarian cancer: no evidence for other ovarian cancer-susceptibility
genes.";
Am. J. Hum. Genet. 65:1021-1029(1999).
[86]
VARIANT BC SER-346, AND VARIANTS LEU-871; GLY-1038; ARG-1183 AND
GLY-1613.
PubMed=10323242; DOI=10.1007/s004390050936;
Li S.S.-L., Tseng H.-M., Yang T.-P., Liu C.-H., Teng S.-J.,
Huang H.-W., Chen L.-M., Kao H.-W., Chen J.H., Tseng J.-N., Chen A.,
Hou M.-F., Huang T.-J., Chang H.-T., Mok K.-T., Tsai J.-H.;
"Molecular characterization of germline mutations in the BRCA1 and
BRCA2 genes from breast cancer families in Taiwan.";
Hum. Genet. 104:201-204(1999).
[87]
VARIANTS OVARIAN CANCER, AND VARIANTS.
PubMed=10196379; DOI=10.1093/hmg/8.5.889;
Janezic S.A., Ziogas A., Krumroy L.M., Krasner M., Plummer S.J.,
Cohen P., Gildea M., Barker D., Haile R., Casey G., Anton-Culver H.;
"Germline BRCA1 alterations in a population-based series of ovarian
cancer cases.";
Hum. Mol. Genet. 8:889-897(1999).
[88]
VARIANTS GLY-1347; ILE-1512 AND ILE-1652.
PubMed=12215251; DOI=10.1089/10906570260199375;
Deffenbaugh A.M., Frank T.S., Hoffman M., Cannon-Albright L.,
Neuhausen S.L.;
"Characterization of common BRCA1 and BRCA2 variants.";
Genet. Test. 6:119-121(2002).
[89]
VARIANTS ILE-656; LEU-871 AND GLY-1613.
PubMed=12442274; DOI=10.1002/humu.9083;
Zhi X., Szabo C., Chopin S., Suter N., Wang Q.-S., Ostrander E.A.,
Sinilnikova O.M., Lenoir G.M., Goldgar D., Shi Y.-R.;
"BRCA1 and BRCA2 sequence variants in Chinese breast cancer
families.";
Hum. Mutat. 20:474-474(2002).
[90]
VARIANT BC TYR-749.
PubMed=12442275; DOI=10.1002/humu.9084;
Ruiz-Flores P., Sinilnikova O.M., Badzioch M.,
Calderon-Garciduenas A.L., Chopin S., Fabrice O.,
Gonzalez-Guerrero J.F., Szabo C., Lenoir G., Goldgar D.E.,
Barrera-Saldana H.A.;
"BRCA1 and BRCA2 mutation analysis of early-onset and familial breast
cancer cases in Mexico.";
Hum. Mutat. 20:474-475(2002).
[91]
VARIANTS BC GLY-61; LYS-71; GLN-866; TYR-888; ILE-1139; GLY-1210 AND
PRO-1297, AND VARIANTS BROVCA1 TYR-835 AND PRO-1786.
PubMed=12938098; DOI=10.1002/humu.9174;
Meyer P., Voigtlaender T., Bartram C.R., Klaes R.;
"Twenty-three novel BRCA1 and BRCA2 sequence alterations in breast
and/or ovarian cancer families in Southern Germany.";
Hum. Mutat. 22:259-259(2003).
[92]
VARIANTS ASN-693; ASN-1040; ALA-1060 AND MET-1665.
PubMed=15026808; DOI=10.1038/sj.bjc.6601656;
Claes K., Poppe B., Coene I., De Paepe A., Messiaen L.;
"BRCA1 and BRCA2 germline mutation spectrum and frequencies in Belgian
breast/ovarian cancer families.";
Br. J. Cancer 90:1244-1251(2004).
[93]
VARIANTS OVARIAN CANCER GLY-61; THR-1411; ARG-1697 AND TRP-1699.
PubMed=14746861; DOI=10.1016/j.ejca.2003.09.016;
Malander S., Ridderheim M., Masbaeck A., Loman N., Kristoffersson U.,
Olsson H., Nilbert M., Borg A.;
"One in 10 ovarian cancer patients carry germ line BRCA1 or BRCA2
mutations: results of a prospective study in Southern Sweden.";
Eur. J. Cancer 40:422-428(2004).
[94]
VARIANTS BC/BROVCA1 LYS-10; LYS-23; ILE-1187; HIS-1200 AND TYR-1217,
VARIANTS BC ILE-1204 AND ASN-1207, VARIANTS BROVCA1 LEU-1226 AND
GLY-1243, AND VARIANT ARG-1183.
PubMed=14722926; DOI=10.1002/humu.9213;
Valarmathi M.T., Sawhney M., Deo S.S.V., Shukla N.K., Das S.N.;
"Novel germline mutations in the BRCA1 and BRCA2 genes in Indian
breast and breast-ovarian cancer families.";
Hum. Mutat. 23:205-205(2004).
[95]
VARIANTS HIS-856; LEU-871; GLY-1038; ARG-1183; THR-1628; GLN-1690 AND
GLY-1713.
PubMed=15365993; DOI=10.1002/humu.9275;
Seo J.H., Cho D.-Y., Ahn S.-H., Yoon K.-S., Kang C.-S., Cho H.M.,
Lee H.S., Choe J.J., Choi C.W., Kim B.S., Shin S.W., Kim Y.H.,
Kim J.S., Son G.-S., Lee J.-B., Koo B.H.;
"BRCA1 and BRCA2 germline mutations in Korean patients with sporadic
breast cancer.";
Hum. Mutat. 24:350-350(2004).
[96]
VARIANTS [LARGE SCALE ANALYSIS] PHE-30; PHE-758 AND CYS-778.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[97]
VARIANTS THR-18; MET-1495; GLY-1623; ILE-1685; ALA-1685; ARG-1689;
TRP-1699; GLU-1706; GLU-1708; ARG-1715; ARG-1738; PRO-1764; SER-1766
AND VAL-1788.
PubMed=17924331; DOI=10.1086/521032;
Easton D.F., Deffenbaugh A.M., Pruss D., Frye C., Wenstrup R.J.,
Allen-Brady K., Tavtigian S.V., Monteiro A.N.A., Iversen E.S.,
Couch F.J., Goldgar D.E.;
"A systematic genetic assessment of 1,433 sequence variants of unknown
clinical significance in the BRCA1 and BRCA2 breast cancer-
predisposition genes.";
Am. J. Hum. Genet. 81:873-883(2007).
[98]
CHARACTERIZATION OF VARIANTS GLY-1623 AND ILE-1685.
PubMed=20513136; DOI=10.1002/humu.21267;
Walker L.C., Whiley P.J., Couch F.J., Farrugia D.J., Healey S.,
Eccles D.M., Lin F., Butler S.A., Goff S.A., Thompson B.A.,
Lakhani S.R., Da Silva L.M., Tavtigian S.V., Goldgar D.E., Brown M.A.,
Spurdle A.B.;
"Detection of splicing aberrations caused by BRCA1 and BRCA2 sequence
variants encoding missense substitutions: implications for prediction
of pathogenicity.";
Hum. Mutat. 31:E1484-E1505(2010).
[99]
CHARACTERIZATION OF VARIANTS BC PHE-4; THR-18; GLN-45; GLY-61; GLY-64;
TYR-67; LYS-132; HIS-142; PHE-147; PRO-165; TRP-170; TYR-186; ILE-191;
MET-231; VAL-245; VAL-246; LEU-271; PHE-668; ASN-695; LEU-798;
TYR-810; LYS-826; GLN-841; HIS-856; ASN-1101; ASN-1140; GLY-1140;
LYS-1214; LYS-1236; SER-1267; VAL-1282; SER-1297 DEL; ARG-1301;
LYS-1346; ILE-1378; VAL-1400; PRO-1407; THR-1411; GLY-1443; GLY-1448;
CYS-1486; MET-1534; PRO-1589; THR-1628; PRO-1651; PHE-1651; PHE-1655;
ARG-1686; GLN-1686; VAL-1688 DEL; ILE-1691; TRP-1699; GLN-1699;
GLU-1706; ALA-1706; GLU-1708; CYS-1718; ALA-1720; LYS-1735; ALA-1736;
GLY-1739; VAL-1739; GLN-1746; THR-1753; PRO-1764; SER-1767; VAL-1770;
CYS-1782; THR-1789; ASP-1794; ASP-1804; ARG-1812; ARG-1837 AND
LEU-1862, AND VARIANTS CYS-105; CYS-866; ALA-1060; LYS-1250 AND
ILE-1652.
PubMed=23867111; DOI=10.1158/2159-8290.CD-13-0094;
Bouwman P., van der Gulden H., van der Heijden I., Drost R.,
Klijn C.N., Prasetyanti P., Pieterse M., Wientjens E., Seibler J.,
Hogervorst F.B., Jonkers J.;
"A high-throughput functional complementation assay for classification
of BRCA1 missense variants.";
Cancer Discov. 3:1142-1155(2013).
-!- 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. Inhibits lipid synthesis by
binding to inactive phosphorylated ACACA and preventing its
dephosphorylation. 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 (PubMed:20160719).
{ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:10724175,
ECO:0000269|PubMed:11836499, ECO:0000269|PubMed:12887909,
ECO:0000269|PubMed:12890688, ECO:0000269|PubMed:14976165,
ECO:0000269|PubMed:14990569, ECO:0000269|PubMed:16326698,
ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:17525340,
ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:19261748,
ECO:0000269|PubMed:19369211, ECO:0000269|PubMed:20160719,
ECO:0000269|PubMed:20351172, ECO:0000269|PubMed:20364141}.
-!- 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:10500182,
ECO:0000269|PubMed:12887909, ECO:0000269|PubMed:12890688,
ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:18056443,
ECO:0000269|PubMed:20351172}.
-!- ENZYME REGULATION: The E3 ubiquitin-protein ligase activity is
inhibited by phosphorylation by AURKA. Activity is increased by
phosphatase treatment. {ECO:0000269|PubMed:18056443}.
-!- 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. Interacts with
EXD2 (PubMed:26807646). {ECO:0000269|PubMed:10724175,
ECO:0000269|PubMed:10783165, ECO:0000269|PubMed:11239454,
ECO:0000269|PubMed:11301010, ECO:0000269|PubMed:11573085,
ECO:0000269|PubMed:11739404, ECO:0000269|PubMed:11751867,
ECO:0000269|PubMed:11836499, ECO:0000269|PubMed:11877377,
ECO:0000269|PubMed:12360400, ECO:0000269|PubMed:12419185,
ECO:0000269|PubMed:12890688, ECO:0000269|PubMed:14636569,
ECO:0000269|PubMed:14976165, ECO:0000269|PubMed:14990569,
ECO:0000269|PubMed:15096610, ECO:0000269|PubMed:15133502,
ECO:0000269|PubMed:15456891, ECO:0000269|PubMed:16101277,
ECO:0000269|PubMed:16326698, ECO:0000269|PubMed:16698035,
ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:17525340,
ECO:0000269|PubMed:17643121, ECO:0000269|PubMed:17643122,
ECO:0000269|PubMed:18452305, ECO:0000269|PubMed:19261746,
ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749,
ECO:0000269|PubMed:19369211, ECO:0000269|PubMed:20159462,
ECO:0000269|PubMed:20160719, ECO:0000269|PubMed:20351172,
ECO:0000269|PubMed:21473589, ECO:0000269|PubMed:21673012,
ECO:0000269|PubMed:24316840, ECO:0000269|PubMed:26778126,
ECO:0000269|PubMed:26807646, ECO:0000269|PubMed:9528852,
ECO:0000269|PubMed:9811458}.
-!- INTERACTION:
Q13085:ACACA; NbExp=2; IntAct=EBI-349905, EBI-717681;
Q92560:BAP1; NbExp=3; IntAct=EBI-349905, EBI-1791447;
Q99728:BARD1; NbExp=9; IntAct=EBI-349905, EBI-473181;
P10415:BCL2; NbExp=6; IntAct=EBI-349905, EBI-77694;
Q7Z569:BRAP; NbExp=3; IntAct=EBI-349905, EBI-349900;
Q6PJG6:BRAT1; NbExp=6; IntAct=EBI-349905, EBI-10826195;
Q9BX63:BRIP1; NbExp=12; IntAct=EBI-349905, EBI-3509650;
P24385:CCND1; NbExp=3; IntAct=EBI-349905, EBI-375001;
P24864:CCNE1; NbExp=2; IntAct=EBI-349905, EBI-519526;
O14757:CHEK1; NbExp=3; IntAct=EBI-349905, EBI-974488;
P03372:ESR1; NbExp=12; IntAct=EBI-349905, EBI-78473;
Q61188:Ezh2 (xeno); NbExp=5; IntAct=EBI-349905, EBI-904311;
Q6UWZ7:FAM175A; NbExp=10; IntAct=EBI-349905, EBI-1263451;
Q14192:FHL2; NbExp=6; IntAct=EBI-349905, EBI-701903;
P78347:GTF2I; NbExp=5; IntAct=EBI-349905, EBI-359622;
P16104:H2AFX; NbExp=4; IntAct=EBI-349905, EBI-494830;
P10809:HSPD1; NbExp=2; IntAct=EBI-349905, EBI-352528;
Q16666:IFI16; NbExp=9; IntAct=EBI-349905, EBI-2867186;
P52292:KPNA2; NbExp=3; IntAct=EBI-349905, EBI-349938;
Q8WX92:NELFB; NbExp=5; IntAct=EBI-349905, EBI-347721;
P62136:PPP1CA; NbExp=2; IntAct=EBI-349905, EBI-357253;
P62140:PPP1CB; NbExp=3; IntAct=EBI-349905, EBI-352350;
P36873:PPP1CC; NbExp=2; IntAct=EBI-349905, EBI-356283;
Q99708:RBBP8; NbExp=9; IntAct=EBI-349905, EBI-745715;
Q9Y4A5:TRRAP; NbExp=8; IntAct=EBI-349905, EBI-399128;
Q96RL1:UIMC1; NbExp=9; IntAct=EBI-349905, EBI-725300;
Q6NZY4:ZCCHC8; NbExp=2; IntAct=EBI-349905, EBI-1263058;
Q9GZX5:ZNF350; NbExp=3; IntAct=EBI-349905, EBI-396421;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15133502,
ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:20160719,
ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:26778126,
ECO:0000269|PubMed:9528852}. Chromosome
{ECO:0000250|UniProtKB:P48754}. Cytoplasm
{ECO:0000269|PubMed:20160719}. Note=Localizes at sites of DNA
damage at double-strand breaks (DSBs); recruitment to DNA damage
sites is mediated by ABRAXAS1 and the BRCA1-A complex
(PubMed:26778126). Translocated to the cytoplasm during UV-induced
apoptosis (PubMed:20160719). {ECO:0000269|PubMed:20160719,
ECO:0000269|PubMed:26778126}.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm
{ECO:0000269|PubMed:8972225}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=8;
Name=1;
IsoId=P38398-1; Sequence=Displayed;
Name=2;
IsoId=P38398-2; Sequence=VSP_047891;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=3; Synonyms=Delta11b;
IsoId=P38398-3; Sequence=VSP_035399, VSP_043797;
Name=4; Synonyms=DeltaBRCA1(17aa);
IsoId=P38398-4; Sequence=VSP_035396;
Note=Produced by alternative initiation at Met-18 of isoform 1.;
Name=5; Synonyms=Delta11, Delta772-3095;
IsoId=P38398-5; Sequence=VSP_035398;
Name=6;
IsoId=P38398-6; Sequence=VSP_035399, VSP_043797, VSP_043798;
Note=No experimental confirmation available.;
Name=7;
IsoId=P38398-7; Sequence=VSP_055404;
Note=No experimental confirmation available. Ref.8 (AAI15038)
sequence is in conflict in position: 1461:N->D. {ECO:0000305};
Name=8;
IsoId=P38398-8; Sequence=VSP_057569;
Note=No experimental confirmation available. The N-terminus is
confirmed by several cDNAs. {ECO:0000305};
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 3 are widely expressed.
Isoform 3 is reduced or absent in several breast and ovarian
cancer cell lines.
-!- 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:0000269|PubMed:20159462}.
-!- DOMAIN: The RING-type zinc finger domain interacts with BAP1.
{ECO:0000269|PubMed:20159462}.
-!- PTM: Phosphorylation at Ser-308 by AURKA is required for normal
cell cycle progression from G2 to mitosis. Phosphorylated in
response to IR, UV, and various stimuli that cause checkpoint
activation, probably by ATM or ATR. Phosphorylation at Ser-988 by
CHEK2 regulates mitotic spindle assembly.
{ECO:0000269|PubMed:10724175, ECO:0000269|PubMed:11114888,
ECO:0000269|PubMed:12183412, ECO:0000269|PubMed:14990569,
ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:20364141,
ECO:0000269|PubMed:21144835}.
-!- PTM: Autoubiquitinated, undergoes 'Lys-6'-linked
polyubiquitination. 'Lys-6'-linked polyubiquitination does not
promote degradation. {ECO:0000269|PubMed:12890688,
ECO:0000269|PubMed:20351172}.
-!- POLYMORPHISM: There is evidence that the presence of the rare form
of Gln-356-Arg and Leu-871-Pro polymorphisms may be associated
with an increased risk for developing ovarian cancer.
-!- DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy
originating from breast epithelial tissue. Breast neoplasms can be
distinguished by their histologic pattern. Invasive ductal
carcinoma is by far the most common type. Breast cancer is
etiologically and genetically heterogeneous. Important genetic
factors have been indicated by familial occurrence and bilateral
involvement. Mutations at more than one locus can be involved in
different families or even in the same case.
{ECO:0000269|PubMed:10323242, ECO:0000269|PubMed:11114888,
ECO:0000269|PubMed:11301010, ECO:0000269|PubMed:12427738,
ECO:0000269|PubMed:12442275, ECO:0000269|PubMed:12938098,
ECO:0000269|PubMed:14722926, ECO:0000269|PubMed:15133502,
ECO:0000269|PubMed:18285836, ECO:0000269|PubMed:21473589,
ECO:0000269|PubMed:23867111, ECO:0000269|PubMed:7545954,
ECO:0000269|PubMed:7894491, ECO:0000269|PubMed:7894493,
ECO:0000269|PubMed:7939630, ECO:0000269|PubMed:8554067,
ECO:0000269|PubMed:8723683, ECO:0000269|PubMed:8776600,
ECO:0000269|PubMed:9482581, ECO:0000269|PubMed:9609997,
ECO:0000269|PubMed:9760198}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry. Mutations in BRCA1 are thought to be responsible for 45% of
inherited breast cancer. Moreover, BRCA1 carriers have a 4-fold
increased risk of colon cancer, whereas male carriers face a 3-
fold increased risk of prostate cancer. Cells lacking BRCA1 show
defects in DNA repair by homologous recombination.
-!- DISEASE: Breast-ovarian cancer, familial, 1 (BROVCA1)
[MIM:604370]: A condition associated with familial predisposition
to cancer of the breast and ovaries. Characteristic features in
affected families are an early age of onset of breast cancer
(often before age 50), increased chance of bilateral cancers
(cancer that develop in both breasts, or both ovaries,
independently), frequent occurrence of breast cancer among men,
increased incidence of tumors of other specific organs, such as
the prostate. {ECO:0000269|PubMed:12938098,
ECO:0000269|PubMed:14722926, ECO:0000269|PubMed:8968716}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry. Mutations in BRCA1
are thought to be responsible for more than 80% of inherited
breast-ovarian cancer.
-!- DISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer
defines malignancies originating from ovarian tissue. Although
many histologic types of ovarian tumors have been described,
epithelial ovarian carcinoma is the most common form. Ovarian
cancers are often asymptomatic and the recognized signs and
symptoms, even of late-stage disease, are vague. Consequently,
most patients are diagnosed with advanced disease.
{ECO:0000269|PubMed:10196379, ECO:0000269|PubMed:10486320,
ECO:0000269|PubMed:14746861}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Pancreatic cancer 4 (PNCA4) [MIM:614320]: A malignant
neoplasm of the pancreas. Tumors can arise from both the exocrine
and endocrine portions of the pancreas, but 95% of them develop
from the exocrine portion, including the ductal epithelium, acinar
cells, connective tissue, and lymphatic tissue.
{ECO:0000269|PubMed:18762988}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SEQUENCE CAUTION:
Sequence=AAB61673.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
Sequence=AAI15038.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAI15038.1; Type=Erroneous termination; Positions=526; Note=Translated as Gln.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BRCA1ID163ch17q21.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/brca1/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=BRCA1";
-!- WEB RESOURCE: Name=Wikipedia; Note=BRCA1 entry;
URL="https://en.wikipedia.org/wiki/BRCA1";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U14680; AAA73985.1; -; mRNA.
EMBL; L78833; AAC37594.1; -; Genomic_DNA.
EMBL; U64805; AAC00049.1; -; mRNA.
EMBL; AF005068; AAB61673.1; ALT_SEQ; mRNA.
EMBL; DQ190450; ABA29208.1; -; Genomic_DNA.
EMBL; DQ190451; ABA29211.1; -; Genomic_DNA.
EMBL; DQ190452; ABA29214.1; -; Genomic_DNA.
EMBL; DQ190453; ABA29217.1; -; Genomic_DNA.
EMBL; DQ190454; ABA29220.1; -; Genomic_DNA.
EMBL; DQ190455; ABA29223.1; -; Genomic_DNA.
EMBL; DQ190456; ABA29226.1; -; Genomic_DNA.
EMBL; AY273801; AAP12647.1; -; Genomic_DNA.
EMBL; AC060780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC135721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC072418; AAH72418.1; -; mRNA.
EMBL; BC115037; AAI15038.1; ALT_SEQ; mRNA.
CCDS; CCDS11453.1; -. [P38398-1]
CCDS; CCDS11454.2; -. [P38398-3]
CCDS; CCDS11455.2; -. [P38398-6]
CCDS; CCDS11456.2; -. [P38398-7]
CCDS; CCDS11459.2; -. [P38398-8]
PIR; A58881; A58881.
RefSeq; NP_009225.1; NM_007294.3. [P38398-1]
RefSeq; NP_009228.2; NM_007297.3. [P38398-8]
RefSeq; NP_009229.2; NM_007298.3. [P38398-3]
RefSeq; NP_009230.2; NM_007299.3. [P38398-6]
RefSeq; NP_009231.2; NM_007300.3. [P38398-7]
UniGene; Hs.194143; -.
PDB; 1JM7; NMR; -; A=1-110.
PDB; 1JNX; X-ray; 2.50 A; X=1646-1859.
PDB; 1N5O; X-ray; 2.80 A; X=1646-1859.
PDB; 1OQA; NMR; -; A=1755-1863.
PDB; 1T15; X-ray; 1.85 A; A=1646-1859.
PDB; 1T29; X-ray; 2.30 A; A=1646-1859.
PDB; 1T2U; X-ray; 2.80 A; A=1646-1859.
PDB; 1T2V; X-ray; 3.30 A; A/B/C/D/E=1646-1859.
PDB; 1Y98; X-ray; 2.50 A; A=1646-1859.
PDB; 2ING; X-ray; 3.60 A; X=1649-1859.
PDB; 3COJ; X-ray; 3.21 A; A/B/C/D/E/F/G/X=1646-1859.
PDB; 3K0H; X-ray; 2.70 A; A=1646-1859.
PDB; 3K0K; X-ray; 2.70 A; A=1646-1859.
PDB; 3K15; X-ray; 2.80 A; A=1646-1859.
PDB; 3K16; X-ray; 3.00 A; A=1646-1859.
PDB; 3PXA; X-ray; 2.55 A; A=1646-1859.
PDB; 3PXB; X-ray; 2.50 A; A=1646-1859.
PDB; 3PXC; X-ray; 2.80 A; X=1646-1859.
PDB; 3PXD; X-ray; 2.80 A; A=1646-1859.
PDB; 3PXE; X-ray; 2.85 A; A/B/C/D=1646-1859.
PDB; 4IFI; X-ray; 2.20 A; A=1646-1859.
PDB; 4IGK; X-ray; 1.75 A; A/B=1646-1859.
PDB; 4JLU; X-ray; 3.50 A; A=1649-1859.
PDB; 4OFB; X-ray; 3.05 A; A=1646-1859.
PDB; 4U4A; X-ray; 3.51 A; A/B/C=1646-1859.
PDB; 4Y18; X-ray; 3.50 A; A/B/C/D/E/F/G/H=1646-1859.
PDB; 4Y2G; X-ray; 2.50 A; A=1646-1859.
PDBsum; 1JM7; -.
PDBsum; 1JNX; -.
PDBsum; 1N5O; -.
PDBsum; 1OQA; -.
PDBsum; 1T15; -.
PDBsum; 1T29; -.
PDBsum; 1T2U; -.
PDBsum; 1T2V; -.
PDBsum; 1Y98; -.
PDBsum; 2ING; -.
PDBsum; 3COJ; -.
PDBsum; 3K0H; -.
PDBsum; 3K0K; -.
PDBsum; 3K15; -.
PDBsum; 3K16; -.
PDBsum; 3PXA; -.
PDBsum; 3PXB; -.
PDBsum; 3PXC; -.
PDBsum; 3PXD; -.
PDBsum; 3PXE; -.
PDBsum; 4IFI; -.
PDBsum; 4IGK; -.
PDBsum; 4JLU; -.
PDBsum; 4OFB; -.
PDBsum; 4U4A; -.
PDBsum; 4Y18; -.
PDBsum; 4Y2G; -.
DisProt; DP00238; -.
ProteinModelPortal; P38398; -.
SMR; P38398; -.
BioGrid; 107140; 580.
DIP; DIP-5971N; -.
IntAct; P38398; 76.
MINT; MINT-90433; -.
STRING; 9606.ENSP00000418960; -.
BindingDB; P38398; -.
ChEMBL; CHEMBL5990; -.
iPTMnet; P38398; -.
PhosphoSitePlus; P38398; -.
BioMuta; BRCA1; -.
DMDM; 728984; -.
PaxDb; P38398; -.
PeptideAtlas; P38398; -.
PRIDE; P38398; -.
DNASU; 672; -.
Ensembl; ENST00000352993; ENSP00000312236; ENSG00000012048. [P38398-5]
Ensembl; ENST00000357654; ENSP00000350283; ENSG00000012048. [P38398-1]
Ensembl; ENST00000461221; ENSP00000418548; ENSG00000012048. [P38398-2]
Ensembl; ENST00000461798; ENSP00000417988; ENSG00000012048. [P38398-2]
Ensembl; ENST00000468300; ENSP00000417148; ENSG00000012048. [P38398-6]
Ensembl; ENST00000471181; ENSP00000418960; ENSG00000012048. [P38398-7]
Ensembl; ENST00000491747; ENSP00000420705; ENSG00000012048. [P38398-3]
Ensembl; ENST00000493795; ENSP00000418775; ENSG00000012048. [P38398-8]
GeneID; 672; -.
KEGG; hsa:672; -.
UCSC; uc002icq.4; human. [P38398-1]
UCSC; uc010cyx.4; human.
CTD; 672; -.
DisGeNET; 672; -.
GeneCards; BRCA1; -.
GeneReviews; BRCA1; -.
HGNC; HGNC:1100; BRCA1.
HPA; CAB001946; -.
HPA; HPA034966; -.
MalaCards; BRCA1; -.
MIM; 113705; gene.
MIM; 114480; phenotype.
MIM; 167000; phenotype.
MIM; 604370; phenotype.
MIM; 614320; phenotype.
neXtProt; NX_P38398; -.
OpenTargets; ENSG00000012048; -.
Orphanet; 1333; Familial pancreatic carcinoma.
Orphanet; 1331; Familial prostate cancer.
Orphanet; 145; Hereditary breast and ovarian cancer syndrome.
Orphanet; 227535; Hereditary breast cancer.
Orphanet; 213524; Hereditary site-specific ovarian cancer syndrome.
Orphanet; 168829; Primary peritoneal carcinoma.
PharmGKB; PA25411; -.
eggNOG; ENOG410ITQ4; Eukaryota.
eggNOG; ENOG4112BIH; LUCA.
GeneTree; ENSGT00440000034289; -.
HOGENOM; HOG000230969; -.
HOVERGEN; HBG050730; -.
InParanoid; P38398; -.
KO; K10605; -.
OMA; FQHLLFG; -.
OrthoDB; EOG091G0670; -.
PhylomeDB; P38398; -.
BRENDA; 6.3.2.19; 2681.
Reactome; R-HSA-1221632; Meiotic synapsis.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
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-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
Reactome; R-HSA-912446; Meiotic recombination.
SignaLink; P38398; -.
SIGNOR; P38398; -.
UniPathway; UPA00143; -.
ChiTaRS; BRCA1; human.
EvolutionaryTrace; P38398; -.
GeneWiki; BRCA1; -.
GenomeRNAi; 672; -.
PMAP-CutDB; P38398; -.
PRO; PR:P38398; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000012048; -.
CleanEx; HS_BRCA1; -.
ExpressionAtlas; P38398; baseline and differential.
Genevisible; P38398; HS.
GO; GO:0070531; C:BRCA1-A complex; IDA:UniProtKB.
GO; GO:0031436; C:BRCA1-BARD1 complex; IDA:UniProtKB.
GO; GO:0005694; C:chromosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0008274; C:gamma-tubulin ring complex; NAS:UniProtKB.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:MGI.
GO; GO:0000800; C:lateral element; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0000151; C:ubiquitin ligase complex; NAS:UniProtKB.
GO; GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:MGI.
GO; GO:0003713; F:transcription coactivator activity; NAS:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0015631; F:tubulin binding; NAS:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; TAS:ProtInc.
GO; GO:0071681; P:cellular response to indole-3-methanol; IDA:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:BHF-UCL.
GO; GO:0007098; P:centrosome cycle; IEA:Ensembl.
GO; GO:0043009; P:chordate embryonic development; IBA:GO_Central.
GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; TAS: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:0009048; P:dosage compensation by inactivation of X chromosome; IBA:GO_Central.
GO; GO:0006302; P:double-strand break repair; IDA:CACAO.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:HGNC.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0031572; P:G2 DNA damage checkpoint; IMP:UniProtKB.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:MGI.
GO; GO:0044818; P:mitotic G2/M transition checkpoint; IEA:Ensembl.
GO; GO:0046600; P:negative regulation of centriole replication; NAS:UniProtKB.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:BHF-UCL.
GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IMP:UniProtKB.
GO; GO:0035067; P:negative regulation of histone acetylation; IBA:GO_Central.
GO; GO:0051572; P:negative regulation of histone H3-K4 methylation; IEA:Ensembl.
GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IDA:BHF-UCL.
GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; IMP:CACAO.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IDA:BHF-UCL.
GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
GO; GO:0035066; P:positive regulation of histone acetylation; IDA:BHF-UCL.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IDA:BHF-UCL.
GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; IDA:BHF-UCL.
GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; IEA:Ensembl.
GO; GO:2000620; P:positive regulation of histone H4-K16 acetylation; IDA:BHF-UCL.
GO; GO:0070512; P:positive regulation of histone H4-K20 methylation; IDA:BHF-UCL.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:BHF-UCL.
GO; GO:0006301; P:postreplication repair; IDA:HGNC.
GO; GO:0051865; P:protein autoubiquitination; IDA: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; IDA:HGNC.
GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; TAS:UniProtKB.
GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IEA:Ensembl.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0006359; P:regulation of transcription from RNA polymerase III promoter; TAS:UniProtKB.
GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
GO; GO:0000732; P:strand displacement; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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; 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:SF3; PTHR13763:SF3; 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;
3D-structure; Acetylation; Activator; Alternative initiation;
Alternative splicing; Cell cycle; Chromosome; Complete proteome;
Cytoplasm; Direct protein sequencing; Disease mutation; DNA damage;
DNA recombination; DNA repair; DNA-binding; Fatty acid biosynthesis;
Fatty acid metabolism; Isopeptide bond; Lipid biosynthesis;
Lipid metabolism; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Transcription;
Transcription regulation; Transferase; Tumor suppressor;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 1863 Breast cancer type 1 susceptibility
protein.
/FTId=PRO_0000055830.
DOMAIN 1642 1736 BRCT 1. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 1756 1855 BRCT 2. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
ZN_FING 24 65 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 1397 1424 Interaction with PALB2.
{ECO:0000269|PubMed:19369211}.
COMPBIAS 651 654 Poly-Lys.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 308 308 Phosphoserine; by AURKA.
{ECO:0000269|PubMed:14990569}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 398 398 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 423 423 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 551 551 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 694 694 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 708 708 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 725 725 Phosphoserine.
{ECO:0000250|UniProtKB:P48754}.
MOD_RES 753 753 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 840 840 Phosphoserine.
{ECO:0000250|UniProtKB:P48754}.
MOD_RES 988 988 Phosphoserine; by CHEK2.
{ECO:0000269|PubMed:10724175,
ECO:0000269|PubMed:20364141}.
MOD_RES 1009 1009 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1143 1143 Phosphoserine; by ATR; in vitro.
{ECO:0000269|PubMed:11114888}.
MOD_RES 1189 1189 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1191 1191 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1211 1211 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1217 1217 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1218 1218 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 1280 1280 Phosphoserine; by ATR; in vitro.
{ECO:0000269|PubMed:11114888}.
MOD_RES 1328 1328 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1336 1336 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1342 1342 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1387 1387 Phosphoserine; by ATM and ATR.
{ECO:0000269|PubMed:11114888}.
MOD_RES 1394 1394 Phosphothreonine; by ATR; in vitro.
{ECO:0000269|PubMed:11114888}.
MOD_RES 1423 1423 Phosphoserine; by ATM and ATR.
{ECO:0000269|PubMed:11114888}.
MOD_RES 1457 1457 Phosphoserine; by ATR; in vitro.
{ECO:0000269|PubMed:11114888}.
MOD_RES 1524 1524 Phosphoserine; by ATM.
{ECO:0000269|PubMed:21144835}.
MOD_RES 1542 1542 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 109 109 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 301 301 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 339 339 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 443 443 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 459 459 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 519 519 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 583 583 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 654 654 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 734 734 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 739 739 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 918 918 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 987 987 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1079 1079 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 47 Missing (in isoform 8).
/FTId=VSP_057569.
VAR_SEQ 1 17 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_035396.
VAR_SEQ 64 1863 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_047891.
VAR_SEQ 224 1365 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_035398.
VAR_SEQ 264 1366 Missing (in isoform 3 and isoform 6).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9010228}.
/FTId=VSP_035399.
VAR_SEQ 1453 1453 Missing (in isoform 3 and isoform 6).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9010228}.
/FTId=VSP_043797.
VAR_SEQ 1453 1453 A -> DSHIHGQRNNSMFSKRPREHIS (in isoform
7). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_055404.
VAR_SEQ 1778 1863 DQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTED
NGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTYLIPQIP
HSHY -> GCPPNCGCAARCLDRGQWLPCNWADV (in
isoform 6).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043798.
VARIANT 4 4 S -> F (in BC; unknown pathological
significance; dbSNP:rs786203152).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070458.
VARIANT 10 10 E -> K (in BC and BROVCA1).
{ECO:0000269|PubMed:14722926}.
/FTId=VAR_020679.
VARIANT 11 11 V -> A (found in breast-ovarian cancer
patients; unknown pathological
significance; dbSNP:rs80357017).
/FTId=VAR_007754.
VARIANT 18 18 M -> T (in BC; unknown pathological
significance; dbSNP:rs80356929).
{ECO:0000269|PubMed:17924331,
ECO:0000269|PubMed:23867111}.
/FTId=VAR_063899.
VARIANT 21 21 I -> V (found in breast-ovarian cancer
patients; unknown pathological
significance; dbSNP:rs80357406).
/FTId=VAR_007755.
VARIANT 22 22 L -> S (in BC; dbSNP:rs80357438).
{ECO:0000269|PubMed:9609997}.
/FTId=VAR_007756.
VARIANT 23 23 E -> K (in BC and BROVCA1).
{ECO:0000269|PubMed:14722926}.
/FTId=VAR_020680.
VARIANT 30 30 L -> F (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035947.
VARIANT 45 45 K -> Q (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs769650474).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070459.
VARIANT 61 61 C -> G (in BC and ovarian cancer; no
interaction with BAP1; dbSNP:rs28897672).
{ECO:0000269|PubMed:12938098,
ECO:0000269|PubMed:14746861,
ECO:0000269|PubMed:23867111,
ECO:0000269|PubMed:7894493,
ECO:0000269|PubMed:8554067,
ECO:0000269|PubMed:9528852,
ECO:0000269|PubMed:9760198}.
/FTId=VAR_007757.
VARIANT 64 64 C -> G (in BC; no interaction with BAP1;
dbSNP:rs80357064).
{ECO:0000269|PubMed:23867111,
ECO:0000269|PubMed:7894491,
ECO:0000269|PubMed:9482581,
ECO:0000269|PubMed:9528852}.
/FTId=VAR_007758.
VARIANT 64 64 C -> Y (in dbSNP:rs55851803).
/FTId=VAR_007759.
VARIANT 67 67 D -> Y (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs80357102).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070460.
VARIANT 71 71 R -> K (in BC; unknown pathological
significance; dbSNP:rs80356913).
{ECO:0000269|PubMed:12938098}.
/FTId=VAR_020681.
VARIANT 105 105 Y -> C (in dbSNP:rs28897673).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070461.
VARIANT 132 132 N -> K (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs80357413).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070462.
VARIANT 142 142 P -> H (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs55971303).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070463.
VARIANT 147 147 L -> F (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs748876625).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070464.
VARIANT 153 153 S -> R (in dbSNP:rs28897674).
/FTId=VAR_052077.
VARIANT 165 165 L -> P (in BC; unknown pathological
significance; functionally neutral in
vitro). {ECO:0000269|PubMed:23867111}.
/FTId=VAR_070465.
VARIANT 170 170 R -> W (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs80357325).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070466.
VARIANT 186 186 S -> Y (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs55688530).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070467.
VARIANT 191 191 V -> I (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs80357090).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070468.
VARIANT 227 227 E -> K (in ovarian cancer; unknown
pathological significance).
/FTId=VAR_008759.
VARIANT 231 231 T -> M (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs80357001).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070469.
VARIANT 239 239 H -> R (in dbSNP:rs80357396).
{ECO:0000269|PubMed:9010228,
ECO:0000269|PubMed:9760198}.
/FTId=VAR_007760.
VARIANT 245 245 D -> V (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs80356865).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070470.
VARIANT 246 246 L -> V (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs28897675).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070471.
VARIANT 271 271 V -> L (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs80357244).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070472.
VARIANT 271 271 V -> M (in BC; dbSNP:rs80357244).
{ECO:0000269|PubMed:8723683}.
/FTId=VAR_007761.
VARIANT 275 275 G -> S (in dbSNP:rs8176153).
{ECO:0000269|Ref.6}.
/FTId=VAR_019944.
VARIANT 346 346 P -> S (in BC; unknown pathological
significance; dbSNP:rs80357015).
{ECO:0000269|PubMed:10323242}.
/FTId=VAR_008760.
VARIANT 356 356 Q -> R (common polymorphism;
dbSNP:rs1799950).
{ECO:0000269|PubMed:7894493,
ECO:0000269|Ref.5, ECO:0000269|Ref.6}.
/FTId=VAR_007762.
VARIANT 369 369 Missing (in BC).
/FTId=VAR_007763.
VARIANT 379 379 I -> M (in dbSNP:rs56128296).
/FTId=VAR_007764.
VARIANT 461 461 F -> L (in BC; dbSNP:rs56046357).
{ECO:0000269|PubMed:9609997}.
/FTId=VAR_007765.
VARIANT 465 465 Y -> D (in BC; dbSNP:rs397508869).
{ECO:0000269|PubMed:9609997}.
/FTId=VAR_007766.
VARIANT 507 507 R -> I (found in breast-ovarian cancer
patients; unknown pathological
significance; dbSNP:rs80357224).
/FTId=VAR_007767.
VARIANT 552 552 G -> V (in BC; dbSNP:rs397508893).
{ECO:0000269|PubMed:9609997}.
/FTId=VAR_007768.
VARIANT 656 656 N -> I. {ECO:0000269|PubMed:12442274}.
/FTId=VAR_020682.
VARIANT 668 668 L -> F (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs80357250).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070473.
VARIANT 693 693 D -> N (rare polymorphism;
dbSNP:rs4986850).
{ECO:0000269|PubMed:15026808,
ECO:0000269|Ref.6}.
/FTId=VAR_007769.
VARIANT 695 695 D -> N (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs28897681).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070474.
VARIANT 723 723 N -> D (in dbSNP:rs4986845).
/FTId=VAR_020110.
VARIANT 749 749 D -> Y (in BC; dbSNP:rs80357114).
{ECO:0000269|PubMed:12442275}.
/FTId=VAR_020683.
VARIANT 758 758 L -> F (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035948.
VARIANT 772 772 V -> A (rare polymorphism;
dbSNP:rs80357467).
{ECO:0000269|PubMed:7894491,
ECO:0000269|PubMed:9482581}.
/FTId=VAR_007770.
VARIANT 778 778 G -> C (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035949.
VARIANT 798 798 P -> L (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs876660005).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070475.
VARIANT 810 810 N -> Y (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs28897682).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070476.
VARIANT 820 820 K -> E (rare polymorphism;
dbSNP:rs56082113).
{ECO:0000269|PubMed:9482581}.
/FTId=VAR_007771.
VARIANT 826 826 T -> K (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs28897683).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_007772.
VARIANT 835 835 H -> Y (in BROVCA1; unknown pathological
significance; dbSNP:rs751656678).
{ECO:0000269|PubMed:12938098}.
/FTId=VAR_020684.
VARIANT 841 841 R -> Q (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs80357337).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070477.
VARIANT 841 841 R -> W (in BROVCA1; unknown pathological
significance; dbSNP:rs1800709).
{ECO:0000269|PubMed:8968716,
ECO:0000269|PubMed:9760198}.
/FTId=VAR_007773.
VARIANT 856 856 Y -> H (in a patient with sporadic breast
cancer; unknown pathological
significance; dbSNP:rs80356892).
{ECO:0000269|PubMed:15365993,
ECO:0000269|PubMed:23867111}.
/FTId=VAR_020685.
VARIANT 866 866 R -> C (in dbSNP:rs41286300).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070478.
VARIANT 866 866 R -> Q (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:12938098}.
/FTId=VAR_020686.
VARIANT 871 871 P -> L (common polymorphism;
dbSNP:rs799917).
{ECO:0000269|PubMed:10323242,
ECO:0000269|PubMed:12442274,
ECO:0000269|PubMed:15365993,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.6}.
/FTId=VAR_007774.
VARIANT 888 888 H -> Y (in BC; unknown pathological
significance; dbSNP:rs80357480).
{ECO:0000269|PubMed:12938098}.
/FTId=VAR_020687.
VARIANT 892 892 L -> S (in BC; dbSNP:rs397508994).
{ECO:0000269|PubMed:9609997}.
/FTId=VAR_007775.
VARIANT 925 925 I -> L (in dbSNP:rs4986847).
/FTId=VAR_021913.
VARIANT 960 960 G -> D (in BC; dbSNP:rs397509022).
{ECO:0000269|PubMed:9609997}.
/FTId=VAR_007776.
VARIANT 989 989 F -> S (in dbSNP:rs4986848).
/FTId=VAR_020111.
VARIANT 1008 1008 M -> I (common polymorphism;
dbSNP:rs1800704).
/FTId=VAR_007777.
VARIANT 1025 1025 T -> I (in BC; dbSNP:rs397509034).
{ECO:0000269|PubMed:9609997}.
/FTId=VAR_007778.
VARIANT 1038 1038 E -> G (common polymorphism;
dbSNP:rs16941).
{ECO:0000269|PubMed:10323242,
ECO:0000269|PubMed:15365993,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7894493,
ECO:0000269|Ref.6}.
/FTId=VAR_007779.
VARIANT 1040 1040 S -> N (rare polymorphism;
dbSNP:rs4986852).
{ECO:0000269|PubMed:15026808,
ECO:0000269|PubMed:7894491,
ECO:0000269|PubMed:7894493,
ECO:0000269|PubMed:9482581,
ECO:0000269|Ref.6}.
/FTId=VAR_007780.
VARIANT 1047 1047 V -> A (in BC; dbSNP:rs397509037).
{ECO:0000269|PubMed:9609997}.
/FTId=VAR_007781.
VARIANT 1060 1060 E -> A (in dbSNP:rs80357184).
{ECO:0000269|PubMed:15026808,
ECO:0000269|PubMed:23867111}.
/FTId=VAR_020688.
VARIANT 1101 1101 S -> N (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs41293447).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070479.
VARIANT 1139 1139 S -> I (in BC; unknown pathological
significance; dbSNP:rs80357228).
{ECO:0000269|PubMed:12938098}.
/FTId=VAR_020689.
VARIANT 1140 1140 S -> G (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs2227945).
{ECO:0000269|PubMed:23867111,
ECO:0000269|Ref.6}.
/FTId=VAR_019945.
VARIANT 1140 1140 S -> N (in BC; unknown pathological
significance; functionally neutral in
vitro). {ECO:0000269|PubMed:23867111}.
/FTId=VAR_070480.
VARIANT 1150 1150 P -> S (in BC; dbSNP:rs80357272).
{ECO:0000269|PubMed:8723683}.
/FTId=VAR_007782.
VARIANT 1183 1183 K -> R (common polymorphism;
dbSNP:rs16942).
{ECO:0000269|PubMed:10323242,
ECO:0000269|PubMed:14722926,
ECO:0000269|PubMed:15365993,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7894493,
ECO:0000269|Ref.6}.
/FTId=VAR_007783.
VARIANT 1187 1187 S -> I (in BC and BROVCA1).
{ECO:0000269|PubMed:14722926}.
/FTId=VAR_020690.
VARIANT 1200 1200 Q -> H (in BC and BROVCA1;
dbSNP:rs56214134).
{ECO:0000269|PubMed:14722926}.
/FTId=VAR_020691.
VARIANT 1204 1204 R -> I (in BC).
{ECO:0000269|PubMed:14722926}.
/FTId=VAR_020692.
VARIANT 1207 1207 K -> N (in BC).
{ECO:0000269|PubMed:14722926}.
/FTId=VAR_020693.
VARIANT 1210 1210 E -> G (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:12938098}.
/FTId=VAR_020694.
VARIANT 1214 1214 E -> K (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs80356923).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070481.
VARIANT 1217 1217 S -> Y (in BC and BROVCA1).
{ECO:0000269|PubMed:14722926}.
/FTId=VAR_020695.
VARIANT 1219 1219 E -> D (found in breast-ovarian cancer
patients; unknown pathological
significance; dbSNP:rs80356876).
/FTId=VAR_007784.
VARIANT 1226 1226 F -> L (in BROVCA1).
{ECO:0000269|PubMed:14722926}.
/FTId=VAR_020696.
VARIANT 1236 1236 N -> K (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs28897687).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_052078.
VARIANT 1243 1243 R -> G (in BROVCA1).
{ECO:0000269|PubMed:14722926}.
/FTId=VAR_020697.
VARIANT 1250 1250 E -> K (in dbSNP:rs28897686).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_052079.
VARIANT 1267 1267 L -> S (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs587782190).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070482.
VARIANT 1282 1282 E -> V (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs80357217).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070483.
VARIANT 1297 1297 S -> P (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:12938098}.
/FTId=VAR_020698.
VARIANT 1297 1297 Missing (in BC; unknown pathological
significance; functionally neutral in
vitro). {ECO:0000269|PubMed:23867111}.
/FTId=VAR_070484.
VARIANT 1301 1301 S -> R (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs273900719).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070485.
VARIANT 1346 1346 E -> K (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs80357407).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070486.
VARIANT 1347 1347 R -> G (in dbSNP:rs28897689).
{ECO:0000269|PubMed:12215251}.
/FTId=VAR_007785.
VARIANT 1378 1378 V -> I (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs28897690).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070487.
VARIANT 1400 1400 M -> V (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs80357306).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070488.
VARIANT 1406 1406 K -> N (polymorphism; dbSNP:rs1800707).
/FTId=VAR_008761.
VARIANT 1407 1407 L -> P (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs80357492).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070489.
VARIANT 1411 1411 M -> T (in BC and ovarian cancer; unknown
pathological significance; decreased
interaction with PALB2;
dbSNP:rs273900729).
{ECO:0000269|PubMed:14746861,
ECO:0000269|PubMed:19369211,
ECO:0000269|PubMed:23867111}.
/FTId=VAR_020699.
VARIANT 1431 1431 S -> P.
/FTId=VAR_007786.
VARIANT 1443 1443 R -> G (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs41293455).
{ECO:0000269|PubMed:23867111,
ECO:0000269|PubMed:7894491,
ECO:0000269|PubMed:9482581}.
/FTId=VAR_007787.
VARIANT 1443 1443 R -> Q (in dbSNP:rs4986849).
/FTId=VAR_020112.
VARIANT 1448 1448 S -> G (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs80357486).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070490.
VARIANT 1486 1486 S -> C (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs397507232).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070491.
VARIANT 1495 1495 R -> M (in BC; unknown pathological
significance; dbSNP:rs80357389).
{ECO:0000269|PubMed:17924331}.
/FTId=VAR_063900.
VARIANT 1512 1512 S -> I (in dbSNP:rs1800744).
{ECO:0000269|PubMed:12215251,
ECO:0000269|PubMed:9482581,
ECO:0000269|PubMed:9760198}.
/FTId=VAR_007788.
VARIANT 1534 1534 V -> M (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs55815649).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070492.
VARIANT 1561 1561 T -> I (found in breast cancer; unknown
pathological significance;
dbSNP:rs56158747).
/FTId=VAR_007789.
VARIANT 1589 1589 R -> P (in BC; unknown pathological
significance; functionally neutral in
vitro). {ECO:0000269|PubMed:23867111}.
/FTId=VAR_070493.
VARIANT 1606 1606 K -> E (found in breast cancer; unknown
pathological significance;
dbSNP:rs80356943).
/FTId=VAR_007790.
VARIANT 1613 1613 S -> G (common polymorphism;
dbSNP:rs1799966).
{ECO:0000269|PubMed:10323242,
ECO:0000269|PubMed:12442274,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7894493,
ECO:0000269|PubMed:9010228,
ECO:0000269|Ref.6}.
/FTId=VAR_007791.
VARIANT 1620 1620 T -> A (in dbSNP:rs8176219).
{ECO:0000269|Ref.6}.
/FTId=VAR_019946.
VARIANT 1623 1623 A -> G (could be associated with cancer
susceptibility; major splicing aberration
identified with this mutant;
dbSNP:rs80356862).
{ECO:0000269|PubMed:17924331,
ECO:0000269|PubMed:20513136}.
/FTId=VAR_063901.
VARIANT 1628 1628 M -> T (in some patients with sporadic
breast cancer; unknown pathological
significance; dbSNP:rs4986854).
{ECO:0000269|PubMed:15365993,
ECO:0000269|PubMed:23867111}.
/FTId=VAR_007793.
VARIANT 1628 1628 M -> V (found in breast and ovarian
cancer patients; unknown pathological
significance; dbSNP:rs80357465).
/FTId=VAR_007792.
VARIANT 1637 1637 P -> L (rare polymorphism;
dbSNP:rs80357048).
{ECO:0000269|PubMed:7939630,
ECO:0000269|PubMed:9482581}.
/FTId=VAR_007794.
VARIANT 1641 1641 A -> P (in ovarian cancer; unknown
pathological significance;
dbSNP:rs1800726).
/FTId=VAR_008762.
VARIANT 1651 1651 S -> F (in BC; unknown pathological
significance; dbSNP:rs80356938).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070494.
VARIANT 1651 1651 S -> P (in BC; unknown pathological
significance; dbSNP:rs879254042).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070495.
VARIANT 1652 1652 M -> I (rare polymorphism;
dbSNP:rs1799967).
{ECO:0000269|PubMed:12215251,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:23867111,
ECO:0000269|PubMed:9482581}.
/FTId=VAR_007795.
VARIANT 1655 1655 S -> F (in BC; unknown pathological
significance; functionally impaired in
vitro; dbSNP:rs80357390).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070496.
VARIANT 1662 1662 F -> C (in dbSNP:rs28897695).
/FTId=VAR_052080.
VARIANT 1665 1665 V -> M (in dbSNP:rs80357169).
{ECO:0000269|PubMed:15026808}.
/FTId=VAR_020700.
VARIANT 1685 1685 T -> A (in BC; unknown pathological
significance; dbSNP:rs80356890).
{ECO:0000269|PubMed:17924331}.
/FTId=VAR_063902.
VARIANT 1685 1685 T -> I (could be associated with cancer
susceptibility; multifactorial likelihood
analysis provides evidence for
pathogenicity; dbSNP:rs80357043).
{ECO:0000269|PubMed:17924331,
ECO:0000269|PubMed:20513136}.
/FTId=VAR_063903.
VARIANT 1686 1686 H -> Q (in BC; unknown pathological
significance; functionally impaired in
vitro; dbSNP:rs397509218).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070497.
VARIANT 1686 1686 H -> R (in BC; unknown pathological
significance; functionally impaired in
vitro; dbSNP:rs730882166).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070498.
VARIANT 1688 1688 Missing (in BC; unknown pathological
significance; functionally impaired in
vitro). {ECO:0000269|PubMed:23867111}.
/FTId=VAR_070499.
VARIANT 1689 1689 M -> R (in BC; unknown pathological
significance; dbSNP:rs80357061).
{ECO:0000269|PubMed:17924331}.
/FTId=VAR_063904.
VARIANT 1690 1690 K -> Q (in some patients with sporadic
breast cancer; unknown pathological
significance; dbSNP:rs397507239).
{ECO:0000269|PubMed:15365993}.
/FTId=VAR_020701.
VARIANT 1691 1691 T -> I (in BC; unknown pathological
significance; functionally impaired in
vitro; dbSNP:rs80357034).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070500.
VARIANT 1692 1692 D -> N (in ovarian cancer; unknown
pathological significance;
dbSNP:rs80187739).
/FTId=VAR_008763.
VARIANT 1697 1697 C -> R (in ovarian cancer;
dbSNP:rs80356993).
{ECO:0000269|PubMed:14746861}.
/FTId=VAR_020702.
VARIANT 1699 1699 R -> Q (in BC; unknown pathological
significance; strongly reduces affinity
for a BRIP1 phosphopeptide; functionally
impaired in vitro; dbSNP:rs41293459).
{ECO:0000269|PubMed:21473589,
ECO:0000269|PubMed:23867111}.
/FTId=VAR_070501.
VARIANT 1699 1699 R -> W (in BC and ovarian cancer; impairs
protein stability; functionally impaired
in vitro; dbSNP:rs55770810).
{ECO:0000269|PubMed:14746861,
ECO:0000269|PubMed:17924331,
ECO:0000269|PubMed:21473589,
ECO:0000269|PubMed:23867111}.
/FTId=VAR_075666.
VARIANT 1706 1706 G -> A (in BC; unknown pathological
significance; dbSNP:rs80356860).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070502.
VARIANT 1706 1706 G -> E (in BC; unknown pathological
significance; dbSNP:rs80356860).
{ECO:0000269|PubMed:17924331,
ECO:0000269|PubMed:23867111}.
/FTId=VAR_063905.
VARIANT 1708 1708 A -> E (in BC; abolishes ACACA binding;
dbSNP:rs28897696).
{ECO:0000269|PubMed:17924331,
ECO:0000269|PubMed:23867111,
ECO:0000269|PubMed:7939630}.
/FTId=VAR_007796.
VARIANT 1713 1713 V -> G. {ECO:0000269|PubMed:15365993}.
/FTId=VAR_007797.
VARIANT 1715 1715 S -> R (in BC; unknown pathological
significance; dbSNP:rs80357094).
{ECO:0000269|PubMed:17924331}.
/FTId=VAR_063906.
VARIANT 1718 1718 W -> C (in BC; unknown pathological
significance; functionally impaired in
vitro; dbSNP:rs80357239).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070503.
VARIANT 1720 1720 T -> A (in BC; unknown pathological
significance; functionally neutral in
vitro; no effect on in vitro
phosphorylation by ATR;
dbSNP:rs56195342).
{ECO:0000269|PubMed:11114888,
ECO:0000269|PubMed:23867111}.
/FTId=VAR_070504.
VARIANT 1735 1735 E -> K (in BC; unknown pathological
significance; dbSNP:rs397509238).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070505.
VARIANT 1736 1736 V -> A (in BC; unknown pathological
significance; dbSNP:rs45553935).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070506.
VARIANT 1738 1738 G -> R (in BC; unknown pathological
significance; dbSNP:rs80356937).
{ECO:0000269|PubMed:17924331}.
/FTId=VAR_063907.
VARIANT 1739 1739 D -> G (in BC; unknown pathological
significance; functionally impaired in
vitro; dbSNP:rs80357227).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070507.
VARIANT 1739 1739 D -> V (in BC; unknown pathological
significance; functionally impaired in
vitro; dbSNP:rs80357227).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070508.
VARIANT 1746 1746 H -> Q (in BC; unknown pathological
significance; dbSNP:rs786202389).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070509.
VARIANT 1749 1749 P -> R (in ovarian cancer; unknown
pathological significance; abolishes
ACACA binding and strongly reduces BRIP1
binding; dbSNP:rs80357462).
{ECO:0000269|PubMed:10486320,
ECO:0000269|PubMed:11301010,
ECO:0000269|PubMed:15133502}.
/FTId=VAR_007798.
VARIANT 1753 1753 R -> T (in BC; unknown pathological
significance; dbSNP:rs397509246).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070510.
VARIANT 1764 1764 L -> P (in BC; unknown pathological
significance; functionally impaired in
vitro; dbSNP:rs80357281).
{ECO:0000269|PubMed:17924331,
ECO:0000269|PubMed:23867111}.
/FTId=VAR_063908.
VARIANT 1766 1766 I -> S (in BC; unknown pathological
significance; dbSNP:rs80357463).
{ECO:0000269|PubMed:17924331}.
/FTId=VAR_063909.
VARIANT 1767 1767 C -> S (in BC; unknown pathological
significance; functionally neutral in
vitro). {ECO:0000269|PubMed:23867111}.
/FTId=VAR_070511.
VARIANT 1770 1770 G -> V (in BC; unknown pathological
significance; functionally impaired in
vitro). {ECO:0000269|PubMed:23867111}.
/FTId=VAR_070512.
VARIANT 1775 1775 M -> K (in BC; strongly reduced
transcription transactivation; abolishes
interaction with BRIP1 and RBBP8;
dbSNP:rs41293463).
{ECO:0000269|PubMed:18285836}.
/FTId=VAR_063212.
VARIANT 1775 1775 M -> R (in BC; alters protein stability
and abolishes ACACA and BRIP1 binding;
dbSNP:rs41293463).
{ECO:0000269|PubMed:11301010,
ECO:0000269|PubMed:12427738,
ECO:0000269|PubMed:15133502,
ECO:0000269|PubMed:7545954,
ECO:0000269|PubMed:7939630}.
/FTId=VAR_007799.
VARIANT 1776 1776 P -> S (in ovarian cancer; unknown
pathological significance;
dbSNP:rs1800757).
/FTId=VAR_008764.
VARIANT 1782 1782 W -> C (in BC; unknown pathological
significance; functionally neutral in
vitro). {ECO:0000269|PubMed:23867111}.
/FTId=VAR_070513.
VARIANT 1786 1786 L -> P (in BROVCA1; unknown pathological
significance; dbSNP:rs398122697).
{ECO:0000269|PubMed:12938098}.
/FTId=VAR_020704.
VARIANT 1788 1788 G -> V (in BC; unknown pathological
significance; dbSNP:rs80357069).
{ECO:0000269|PubMed:17924331}.
/FTId=VAR_063910.
VARIANT 1789 1789 A -> T (in BC; unknown pathological
significance; functionally impaired in
vitro; dbSNP:rs80357078).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070514.
VARIANT 1794 1794 E -> D (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs397509275).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070515.
VARIANT 1804 1804 V -> D (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs80356920).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070516.
VARIANT 1812 1812 P -> R (in BC; unknown pathological
significance; functionally neutral in
vitro). {ECO:0000269|PubMed:23867111}.
/FTId=VAR_070517.
VARIANT 1812 1812 P -> S (in ovarian cancer; unknown
pathological significance;
dbSNP:rs1800751).
/FTId=VAR_008765.
VARIANT 1837 1837 W -> R (in BC; unknown pathological
significance; functionally impaired in
vitro; dbSNP:rs80356959).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070518.
VARIANT 1862 1862 H -> L (in BC; unknown pathological
significance; functionally neutral in
vitro; dbSNP:rs80357183).
{ECO:0000269|PubMed:23867111}.
/FTId=VAR_070519.
MUTAGEN 26 26 I->A: Disrupts the interaction with E2
enzymes, thereby abolishing the E3
ubiquitin-protein ligase activity.
{ECO:0000269|PubMed:16818604,
ECO:0000269|PubMed:20351172}.
MUTAGEN 26 26 I->E: No ubiquitination of RBBP8. No
restoration RBBP8-mediated focus
formation or G2/M checkpoint control upon
DNA damage. {ECO:0000269|PubMed:16818604,
ECO:0000269|PubMed:20351172}.
MUTAGEN 71 71 R->G: No effect on interaction with BAP1.
{ECO:0000269|PubMed:9528852}.
MUTAGEN 308 308 S->N: Abolishes phosphorylation by AURKA
and interferes with cell cycle
progression from G2 to mitosis.
{ECO:0000269|PubMed:14990569}.
MUTAGEN 1143 1143 S->A: Reduces in vitro phosphorylation by
ATR. {ECO:0000269|PubMed:11114888}.
MUTAGEN 1239 1239 S->A: No effect on in vitro
phosphorylation by ATR.
{ECO:0000269|PubMed:11114888}.
MUTAGEN 1280 1280 S->A: Reduces in vitro phosphorylation by
ATR. {ECO:0000269|PubMed:11114888}.
MUTAGEN 1298 1298 S->A: No effect on in vitro
phosphorylation by ATR.
{ECO:0000269|PubMed:11114888}.
MUTAGEN 1330 1330 S->A: No effect on in vitro
phosphorylation by ATR.
{ECO:0000269|PubMed:11114888}.
MUTAGEN 1387 1387 S->A: Loss of IR-induced S-phase
checkpoint. Reduces in vitro
phosphorylation by ATR.
{ECO:0000269|PubMed:11114888,
ECO:0000269|PubMed:12183412}.
MUTAGEN 1394 1394 T->A: Reduces in vitro phosphorylation by
ATR. {ECO:0000269|PubMed:11114888}.
MUTAGEN 1423 1423 S->A: Inhibition of the infrared-induced
G2 arrest. Reduces phosphorylation by
ATR. {ECO:0000269|PubMed:11114888,
ECO:0000269|PubMed:12183412}.
MUTAGEN 1457 1457 S->A: Reduces in vitro phosphorylation by
ATR. {ECO:0000269|PubMed:11114888}.
MUTAGEN 1466 1466 S->A: No effect on in vitro
phosphorylation by ATR.
{ECO:0000269|PubMed:11114888}.
MUTAGEN 1524 1524 S->A: No change in infrared S-phase
delay; when associated with A-1387. No
effect on in vitro phosphorylation by
ATR. {ECO:0000269|PubMed:11114888,
ECO:0000269|PubMed:12183412}.
MUTAGEN 1655 1655 S->A: Abolishes interaction with BRIP1.
{ECO:0000269|PubMed:15133502}.
MUTAGEN 1656 1656 G->D: No effect on affinity for a BRIP1
phosphopeptide.
{ECO:0000269|PubMed:21473589}.
MUTAGEN 1662 1662 F->S: Does not abolish ABRAXAS1 binding,
but abolishes formation of a
heterotetramer with ABRAXAS1.
{ECO:0000269|PubMed:26778126}.
MUTAGEN 1663 1663 M->K: Does not abolish ABRAXAS1 binding,
but abolishes formation of a
heterotetramer with ABRAXAS1.
{ECO:0000269|PubMed:26778126}.
MUTAGEN 1666 1666 Y->A: Does not abolish ABRAXAS1 binding,
but impairs formation of a heterotetramer
with ABRAXAS1.
{ECO:0000269|PubMed:26778126}.
MUTAGEN 1670 1670 R->E: Impairs formation of a
heterotetramer with ABRAXAS1.
{ECO:0000269|PubMed:26778126}.
MUTAGEN 1671 1671 K->E: Impairs formation of a
heterotetramer with ABRAXAS1.
{ECO:0000269|PubMed:26778126}.
MUTAGEN 1700 1700 T->A: Strongly reduces affinity for a
BRIP1 phosphopeptide.
{ECO:0000269|PubMed:21473589}.
MUTAGEN 1702 1702 K->M: Abolishes interaction with BRIP1.
{ECO:0000269|PubMed:15133502}.
MUTAGEN 1738 1738 G->E: Abolishes interaction with BRIP1.
{ECO:0000269|PubMed:15133502}.
MUTAGEN 1755 1755 S->A: No effect on in vitro
phosphorylation by ATR.
{ECO:0000269|PubMed:11114888}.
MUTAGEN 1835 1835 R->P: Mildly reduces affinity for a BRIP1
phosphopeptide.
{ECO:0000269|PubMed:21473589}.
MUTAGEN 1836 1836 E->K: Slightly reduces affinity for a
BRIP1 phosphopeptide.
{ECO:0000269|PubMed:21473589}.
CONFLICT 89 89 I -> T (in Ref. 4; AAB61673).
{ECO:0000305}.
CONFLICT 148 148 Missing (in Ref. 4; AAB61673).
{ECO:0000305}.
CONFLICT 253 253 A -> V (in Ref. 3; AAC00049).
{ECO:0000305}.
CONFLICT 713 713 S -> P (in Ref. 8; AAI15038).
{ECO:0000305}.
CONFLICT 1077 1077 G -> R (in Ref. 4; AAB61673).
{ECO:0000305}.
CONFLICT 1426 1426 S -> P (in Ref. 3; AAC00049).
{ECO:0000305}.
CONFLICT 1527 1527 E -> G (in Ref. 8; AAI15038).
{ECO:0000305}.
HELIX 3 5 {ECO:0000244|PDB:1JM7}.
HELIX 8 21 {ECO:0000244|PDB:1JM7}.
STRAND 25 27 {ECO:0000244|PDB:1JM7}.
HELIX 46 53 {ECO:0000244|PDB:1JM7}.
STRAND 54 58 {ECO:0000244|PDB:1JM7}.
TURN 62 64 {ECO:0000244|PDB:1JM7}.
TURN 70 72 {ECO:0000244|PDB:1JM7}.
STRAND 78 80 {ECO:0000244|PDB:1JM7}.
HELIX 81 96 {ECO:0000244|PDB:1JM7}.
STRAND 1651 1656 {ECO:0000244|PDB:4IGK}.
HELIX 1659 1671 {ECO:0000244|PDB:4IGK}.
STRAND 1675 1679 {ECO:0000244|PDB:1T29}.
STRAND 1686 1689 {ECO:0000244|PDB:4IGK}.
STRAND 1695 1697 {ECO:0000244|PDB:4IGK}.
HELIX 1701 1708 {ECO:0000244|PDB:4IGK}.
STRAND 1712 1715 {ECO:0000244|PDB:4IGK}.
HELIX 1717 1725 {ECO:0000244|PDB:4IGK}.
HELIX 1731 1734 {ECO:0000244|PDB:4IGK}.
TURN 1740 1742 {ECO:0000244|PDB:4IGK}.
STRAND 1743 1745 {ECO:0000244|PDB:1T29}.
HELIX 1748 1754 {ECO:0000244|PDB:4IGK}.
TURN 1755 1757 {ECO:0000244|PDB:1T29}.
TURN 1760 1763 {ECO:0000244|PDB:4IGK}.
STRAND 1765 1768 {ECO:0000244|PDB:4IGK}.
STRAND 1770 1772 {ECO:0000244|PDB:1T2V}.
STRAND 1773 1775 {ECO:0000244|PDB:4IGK}.
HELIX 1777 1786 {ECO:0000244|PDB:4IGK}.
STRAND 1790 1794 {ECO:0000244|PDB:4IGK}.
HELIX 1795 1797 {ECO:0000244|PDB:4IGK}.
STRAND 1801 1803 {ECO:0000244|PDB:4IGK}.
STRAND 1806 1810 {ECO:0000244|PDB:4IGK}.
HELIX 1812 1814 {ECO:0000244|PDB:4IGK}.
STRAND 1817 1819 {ECO:0000244|PDB:1OQA}.
HELIX 1820 1822 {ECO:0000244|PDB:4IGK}.
HELIX 1824 1827 {ECO:0000244|PDB:4IGK}.
STRAND 1828 1830 {ECO:0000244|PDB:3PXE}.
STRAND 1832 1834 {ECO:0000244|PDB:4IGK}.
HELIX 1835 1844 {ECO:0000244|PDB:4IGK}.
HELIX 1851 1853 {ECO:0000244|PDB:4IGK}.
SEQUENCE 1863 AA; 207721 MW; 89C6D83FF56312AF CRC64;
MDLSALRVEE VQNVINAMQK ILECPICLEL IKEPVSTKCD HIFCKFCMLK LLNQKKGPSQ
CPLCKNDITK RSLQESTRFS QLVEELLKII CAFQLDTGLE YANSYNFAKK ENNSPEHLKD
EVSIIQSMGY RNRAKRLLQS EPENPSLQET SLSVQLSNLG TVRTLRTKQR IQPQKTSVYI
ELGSDSSEDT VNKATYCSVG DQELLQITPQ GTRDEISLDS AKKAACEFSE TDVTNTEHHQ
PSNNDLNTTE KRAAERHPEK YQGSSVSNLH VEPCGTNTHA SSLQHENSSL LLTKDRMNVE
KAEFCNKSKQ PGLARSQHNR WAGSKETCND RRTPSTEKKV DLNADPLCER KEWNKQKLPC
SENPRDTEDV PWITLNSSIQ KVNEWFSRSD ELLGSDDSHD GESESNAKVA DVLDVLNEVD
EYSGSSEKID LLASDPHEAL ICKSERVHSK SVESNIEDKI FGKTYRKKAS LPNLSHVTEN
LIIGAFVTEP QIIQERPLTN KLKRKRRPTS GLHPEDFIKK ADLAVQKTPE MINQGTNQTE
QNGQVMNITN SGHENKTKGD SIQNEKNPNP IESLEKESAF KTKAEPISSS ISNMELELNI
HNSKAPKKNR LRRKSSTRHI HALELVVSRN LSPPNCTELQ IDSCSSSEEI KKKKYNQMPV
RHSRNLQLME GKEPATGAKK SNKPNEQTSK RHDSDTFPEL KLTNAPGSFT KCSNTSELKE
FVNPSLPREE KEEKLETVKV SNNAEDPKDL MLSGERVLQT ERSVESSSIS LVPGTDYGTQ
ESISLLEVST LGKAKTEPNK CVSQCAAFEN PKGLIHGCSK DNRNDTEGFK YPLGHEVNHS
RETSIEMEES ELDAQYLQNT FKVSKRQSFA PFSNPGNAEE ECATFSAHSG SLKKQSPKVT
FECEQKEENQ GKNESNIKPV QTVNITAGFP VVGQKDKPVD NAKCSIKGGS RFCLSSQFRG
NETGLITPNK HGLLQNPYRI PPLFPIKSFV KTKCKKNLLE ENFEEHSMSP EREMGNENIP
STVSTISRNN IRENVFKEAS SSNINEVGSS TNEVGSSINE IGSSDENIQA ELGRNRGPKL
NAMLRLGVLQ PEVYKQSLPG SNCKHPEIKK QEYEEVVQTV NTDFSPYLIS DNLEQPMGSS
HASQVCSETP DDLLDDGEIK EDTSFAENDI KESSAVFSKS VQKGELSRSP SPFTHTHLAQ
GYRRGAKKLE SSEENLSSED EELPCFQHLL FGKVNNIPSQ STRHSTVATE CLSKNTEENL
LSLKNSLNDC SNQVILAKAS QEHHLSEETK CSASLFSSQC SELEDLTANT NTQDPFLIGS
SKQMRHQSES QGVGLSDKEL VSDDEERGTG LEENNQEEQS MDSNLGEAAS GCESETSVSE
DCSGLSSQSD ILTTQQRDTM QHNLIKLQQE MAELEAVLEQ HGSQPSNSYP SIISDSSALE
DLRNPEQSTS EKAVLTSQKS SEYPISQNPE GLSADKFEVS ADSSTSKNKE PGVERSSPSK
CPSLDDRWYM HSCSGSLQNR NYPSQEELIK VVDVEEQQLE ESGPHDLTET SYLPRQDLEG
TPYLESGISL FSDDPESDPS EDRAPESARV GNIPSSTSAL KVPQLKVAES AQSPAAAHTT
DTAGYNAMEE SVSREKPELT ASTERVNKRM SMVVSGLTPE EFMLVYKFAR KHHITLTNLI
TEETTHVVMK TDAEFVCERT LKYFLGIAGG KWVVSYFWVT QSIKERKMLN EHDFEVRGDV
VNGRNHQGPK RARESQDRKI FRGLEICCYG PFTNMPTDQL EWMVQLCGAS VVKELSSFTL
GTGVHPIVVV QPDAWTEDNG FHAIGQMCEA PVVTREWVLD SVALYQCQEL DTYLIPQIPH
SHY


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