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Database: UniProt
Entry: P38398
LinkDB: P38398
Original site: P38398 
ID   BRCA1_HUMAN             Reviewed;        1863 AA.
AC   P38398; E9PFZ0; O15129; Q1RMC1; Q3LRJ0; Q3LRJ6; Q6IN79; Q7KYU9;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   17-JUN-2020, entry version 256.
DE   RecName: Full=Breast cancer type 1 susceptibility protein;
DE            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};
DE   AltName: Full=RING finger protein 53;
DE   AltName: Full=RING-type E3 ubiquitin transferase BRCA1 {ECO:0000305};
GN   Name=BRCA1; Synonyms=RNF53;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT BC ARG-1775.
RX   PubMed=7545954; DOI=10.1126/science.7545954;
RA   Miki Y., Swensen J., Shattuck-Eidens D., Futreal P.A., Harshman K.,
RA   Tavtigian S., Liu Q., Cochran C., Bennett L.M., Ding W., Bell R.,
RA   Rosenthal J., Hussey C., Tran T., McClure M., Frye C., Hattier T.,
RA   Phelps R., Haugen-Strano A., Katcher H., Yakumo K., Gholami Z., Shaffer D.,
RA   Stone S., Bayer S., Wray C., Bogden R., Dayananth P., Ward J., Tonin P.,
RA   Narod S., Bristow P.K., Norris F.H., Helvering L., Morrison P., Rosteck P.,
RA   Lai M., Barrett J.C., Lewis C., Neuhausen S., Cannon-Albright L.,
RA   Godlgar D., Wiseman R., Kamb A., Skolnick M.H.;
RT   "A strong candidate for the breast and ovarian cancer susceptibility gene
RT   BRCA1.";
RL   Science 266:66-71(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8938427; DOI=10.1101/gr.6.11.1029;
RA   Smith T.M., Lee M.K., Szabo C.I., Jerome N., McEuen M., Taylor M., Hood L.,
RA   King M.-C.;
RT   "Complete genomic sequence and analysis of 117 kb of human DNA containing
RT   the gene BRCA1.";
RL   Genome Res. 6:1029-1049(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION (ISOFORM 2),
RP   VARIANTS ARG-239 AND GLY-1613, AND TISSUE SPECIFICITY (ISOFORMS 1 AND 3).
RC   TISSUE=Mammary gland;
RX   PubMed=9010228; DOI=10.1038/sj.onc.1200924;
RA   Wilson C.A., Payton M.N., Elliott G.S., Buaas F.W., Cajulis E.E.,
RA   Grosshans D., Ramos L., Reese D.M., Slamon D.J., Calzone F.J.;
RT   "Differential subcellular localization, expression and biological toxicity
RT   of BRCA1 and the splice variant BRCA1-delta11b.";
RL   Oncogene 14:1-16(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RA   Holt J.T., Robinson-Benion C.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-356.
RA   Raymond C.K., Paddock M., Subramanian S., Deodato C., Zhou Y., Haugen E.,
RA   Kaul R., Olson M.V.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-275; ARG-356; ASN-693;
RP   LEU-871; GLY-1038; ASN-1040; GLY-1140; ARG-1183; GLY-1613 AND ALA-1620.
RG   NIEHS SNPs program;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 7), AND VARIANTS
RP   LEU-871; GLY-1038; ARG-1183; GLY-1613 AND ILE-1652.
RC   TISSUE=PNS;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   PROTEIN SEQUENCE OF 6-18 (ISOFORM 1), PROTEIN SEQUENCE OF 18-26 (ISOFORM
RP   4), AND ALTERNATIVE INITIATION (ISOFORM 4).
RX   PubMed=10851077; DOI=10.1038/sj.onc.1203599;
RA   Liu J., Prolla G., Rostagno A., Chiarle R., Feiner H., Inghirami G.;
RT   "Initiation of translation from a downstream in-frame AUG codon on BRCA1
RT   can generate the novel isoform protein DeltaBRCA1(17aa).";
RL   Oncogene 19:2767-2773(2000).
RN   [10]
RP   ALTERNATIVE SPLICING (ISOFORM 5), AND SUBCELLULAR LOCATION (ISOFORM 5).
RX   PubMed=8972225; DOI=10.1128/mcb.17.1.444;
RA   Thakur S., Zhang H.B., Peng Y., Le H., Carroll B., Ward T., Yao J.,
RA   Farid L.M., Couch F.J., Wilson R.B., Weber B.L.;
RT   "Localization of BRCA1 and a splice variant identifies the nuclear
RT   localization signal.";
RL   Mol. Cell. Biol. 17:444-452(1997).
RN   [11]
RP   INTERACTION WITH DHX9.
RX   PubMed=9662397; DOI=10.1038/930;
RA   Anderson S.F., Schlegel B.P., Nakajima T., Wolpin E.S., Parvin J.D.;
RT   "BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via
RT   RNA helicase A.";
RL   Nat. Genet. 19:254-256(1998).
RN   [12]
RP   INTERACTION WITH BAP1, SUBCELLULAR LOCATION, VARIANTS GLY-61 AND GLY-64,
RP   AND MUTAGENESIS OF ARG-71.
RX   PubMed=9528852; DOI=10.1038/sj.onc.1201861;
RA   Jensen D.E., Proctor M., Marquis S.T., Gardner H.P., Ha S.I., Chodosh L.A.,
RA   Ishov A.M., Tommerup N., Vissing H., Sekido Y., Minna J., Borodovsky A.,
RA   Schultz D.C., Wilkinson K.D., Maul G.G., Barlev N., Berger S.,
RA   Prendergast G.C., Rauscher F.J. III;
RT   "BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and
RT   enhances BRCA1-mediated cell growth suppression.";
RL   Oncogene 16:1097-1112(1998).
RN   [13]
RP   INTERACTION WITH RBBP8.
RX   PubMed=9811458; DOI=10.1038/sj.onc.1202150;
RA   Wong A.K., Ormonde P.A., Pero R., Chen Y., Lian L., Salada G., Berry S.,
RA   Lawrence Q., Dayananth P., Ha P., Tavtigian S.V., Teng D.H., Bartel P.L.;
RT   "Characterization of a carboxy-terminal BRCA1 interacting protein.";
RL   Oncogene 17:2279-2285(1998).
RN   [14]
RP   FUNCTION AS AN E2-DEPENDENT UBIQUITIN-PROTEIN LIGASE, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=10500182; DOI=10.1073/pnas.96.20.11364;
RA   Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S., Weissman A.M.;
RT   "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent
RT   ubiquitination.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999).
RN   [15]
RP   IDENTIFICATION IN THE BASC COMPLEX.
RX   PubMed=10783165;
RA   Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.;
RT   "BASC, a super complex of BRCA1-associated proteins involved in the
RT   recognition and repair of aberrant DNA structures.";
RL   Genes Dev. 14:927-939(2000).
RN   [16]
RP   PHOSPHORYLATION AT SER-1143; SER-1280; SER-1387; THR-1394; SER-1423 AND
RP   SER-1457, MUTAGENESIS OF SER-1143; SER-1239; SER-1280; SER-1298; SER-1330;
RP   SER-1387; THR-1394; SER-1423; SER-1457; SER-1466; SER-1524 AND SER-1755,
RP   AND CHARACTERIZATION OF VARIANT BC ALA-1720.
RX   PubMed=11114888; DOI=10.1101/gad.851000;
RA   Tibbetts R.S., Cortez D., Brumbaugh K.M., Scully R., Livingston D.,
RA   Elledge S.J., Abraham R.T.;
RT   "Functional interactions between BRCA1 and the checkpoint kinase ATR during
RT   genotoxic stress.";
RL   Genes Dev. 14:2989-3002(2000).
RN   [17]
RP   FUNCTION IN DNA DAMAGE RESPONSE, PHOSPHORYLATION AT SER-988 BY CHEK2, AND
RP   INTERACTION WITH CHEK2.
RX   PubMed=10724175; DOI=10.1038/35004614;
RA   Lee J.S., Collins K.M., Brown A.L., Lee C.H., Chung J.H.;
RT   "hCds1-mediated phosphorylation of BRCA1 regulates the DNA damage
RT   response.";
RL   Nature 404:201-204(2000).
RN   [18]
RP   INTERACTION WITH BRIP1, CHARACTERIZATION OF VARIANT OVARIAN CANCER
RP   ARG-1749, AND CHARACTERIZATION OF VARIANT BC ARG-1775.
RX   PubMed=11301010; DOI=10.1016/s0092-8674(01)00304-x;
RA   Cantor S.B., Bell D.W., Ganesan S., Kass E.M., Drapkin R., Grossman S.,
RA   Wahrer D.C.R., Sgroi D.C., Lane W.S., Haber D.A., Livingston D.M.;
RT   "BACH1, a novel helicase-like protein, interacts directly with BRCA1 and
RT   contributes to its DNA repair function.";
RL   Cell 105:149-160(2001).
RN   [19]
RP   INTERACTION WITH NELFB.
RX   PubMed=11739404; DOI=10.1083/jcb.200108049;
RA   Ye Q., Hu Y.-F., Zhong H., Nye A.C., Belmont A.S., Li R.;
RT   "BRCA1-induced large-scale chromatin unfolding and allele-specific effects
RT   of cancer-predisposing mutations.";
RL   J. Cell Biol. 155:911-921(2001).
RN   [20]
RP   INTERACTION WITH FANCD2.
RX   PubMed=11239454; DOI=10.1016/s1097-2765(01)00173-3;
RA   Garcia-Higuera I., Taniguchi T., Ganesan S., Meyn M.S., Timmers C.,
RA   Hejna J., Grompe M., D'Andrea A.D.;
RT   "Interaction of the Fanconi anemia proteins and BRCA1 in a common
RT   pathway.";
RL   Mol. Cell 7:249-262(2001).
RN   [21]
RP   PHOSPHORYLATION BY ATM, AND MUTAGENESIS OF SER-1387; SER-1423 AND SER-1524.
RX   PubMed=12183412;
RA   Xu B., O'Donnell A.H., Kim S.-T., Kastan M.B.;
RT   "Phosphorylation of serine 1387 in BRCA1 is specifically required for the
RT   Atm-mediated S-phase checkpoint after ionizing irradiation.";
RL   Cancer Res. 62:4588-4591(2002).
RN   [22]
RP   INTERACTION WITH H2AX.
RX   PubMed=12419185; DOI=10.1016/s0960-9822(02)01259-9;
RA   Kobayashi J., Tauchi H., Sakamoto S., Nakamura A., Morishima K.,
RA   Matsuura S., Kobayashi T., Tamai K., Tanimoto K., Komatsu K.;
RT   "NBS1 localizes to gamma-H2AX foci through interaction with the FHA/BRCT
RT   domain.";
RL   Curr. Biol. 12:1846-1851(2002).
RN   [23]
RP   INTERACTION WITH SMC1A.
RX   PubMed=11877377; DOI=10.1101/gad.970702;
RA   Yazdi P.T., Wang Y., Zhao S., Patel N., Lee E.Y.-H.P., Qin J.;
RT   "SMC1 is a downstream effector in the ATM/NBS1 branch of the human S-phase
RT   checkpoint.";
RL   Genes Dev. 16:571-582(2002).
RN   [24]
RP   INTERACTION WITH LMO4.
RX   PubMed=11751867; DOI=10.1074/jbc.m110603200;
RA   Sum E.Y., Peng B., Yu X., Chen J., Byrne J., Lindeman G.J., Visvader J.E.;
RT   "The LIM domain protein LMO4 interacts with the cofactor CtIP and the tumor
RT   suppressor BRCA1 and inhibits BRCA1 activity.";
RL   J. Biol. Chem. 277:7849-7856(2002).
RN   [25]
RP   FUNCTION, AND INTERACTION WITH CHEK1.
RX   PubMed=11836499; DOI=10.1038/ng837;
RA   Yarden R.I., Pardo-Reoyo S., Sgagias M., Cowan K.H., Brody L.C.;
RT   "BRCA1 regulates the G2/M checkpoint by activating Chk1 kinase upon DNA
RT   damage.";
RL   Nat. Genet. 30:285-289(2002).
RN   [26]
RP   INTERACTION WITH ACACA.
RX   PubMed=12360400; DOI=10.1038/sj.onc.1205915;
RA   Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S., Lenoir G.M.,
RA   Venezia N.D.;
RT   "BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT
RT   domains.";
RL   Oncogene 21:6729-6739(2002).
RN   [27]
RP   FUNCTION, UBIQUITINATION, CATALYTIC ACTIVITY, AND INTERACTION WITH BARD1.
RX   PubMed=12890688; DOI=10.1074/jbc.c300249200;
RA   Wu-Baer F., Lagrazon K., Yuan W., Baer R.;
RT   "The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an
RT   unconventional linkage involving lysine residue K6 of ubiquitin.";
RL   J. Biol. Chem. 278:34743-34746(2003).
RN   [28]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=12887909; DOI=10.1016/s1097-2765(03)00281-8;
RA   Vandenberg C.J., Gergely F., Ong C.Y., Pace P., Mallery D.L., Hiom K.,
RA   Patel K.J.;
RT   "BRCA1-independent ubiquitination of FANCD2.";
RL   Mol. Cell 12:247-254(2003).
RN   [29]
RP   INTERACTION WITH BRCC3.
RX   PubMed=14636569; DOI=10.1016/s1097-2765(03)00424-6;
RA   Dong Y., Hakimi M.-A., Chen X., Kumaraswamy E., Cooch N.S., Godwin A.K.,
RA   Shiekhattar R.;
RT   "Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a
RT   signalosome-like subunit and its role in DNA repair.";
RL   Mol. Cell 12:1087-1099(2003).
RN   [30]
RP   FUNCTION, AND INTERACTION WITH BARD1.
RX   PubMed=14976165; DOI=10.1093/hmg/ddh095;
RA   Morris J.R., Solomon E.;
RT   "BRCA1:BARD1 induces the formation of conjugated ubiquitin structures,
RT   dependent on K6 of ubiquitin, in cells during DNA replication and repair.";
RL   Hum. Mol. Genet. 13:807-817(2004).
RN   [31]
RP   INTERACTION WITH AURKA, FUNCTION, MUTAGENESIS OF SER-308, AND
RP   PHOSPHORYLATION AT SER-308.
RX   PubMed=14990569; DOI=10.1074/jbc.m311780200;
RA   Ouchi M., Fujiuchi N., Sasai K., Katayama H., Minamishima Y.A.,
RA   Ongusaha P.P., Deng C., Sen S., Lee S.W., Ouchi T.;
RT   "BRCA1 phosphorylation by Aurora-A in the regulation of G2 to M
RT   transition.";
RL   J. Biol. Chem. 279:19643-19648(2004).
RN   [32]
RP   INTERACTION WITH DCLRE1C.
RX   PubMed=15456891; DOI=10.1128/mcb.24.20.9207-9220.2004;
RA   Zhang X., Succi J., Feng Z., Prithivirajsingh S., Story M.D.,
RA   Legerski R.J.;
RT   "Artemis is a phosphorylation target of ATM and ATR and is involved in the
RT   G2/M DNA damage checkpoint response.";
RL   Mol. Cell. Biol. 24:9207-9220(2004).
RN   [33]
RP   INTERACTION WITH CLSPN.
RX   PubMed=15096610; DOI=10.1073/pnas.0401847101;
RA   Lin S.-Y., Li K., Stewart G.S., Elledge S.J.;
RT   "Human claspin works with BRCA1 to both positively and negatively regulate
RT   cell proliferation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:6484-6489(2004).
RN   [34]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1336, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [35]
RP   FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH RBBP8, AND MUTAGENESIS OF
RP   ILE-26.
RX   PubMed=16818604; DOI=10.1101/gad.1431006;
RA   Yu X., Fu S., Lai M., Baer R., Chen J.;
RT   "BRCA1 ubiquitinates its phosphorylation-dependent binding partner CtIP.";
RL   Genes Dev. 20:1721-1726(2006).
RN   [36]
RP   FUNCTION, AND INTERACTION WITH ACACA.
RX   PubMed=16326698; DOI=10.1074/jbc.m504652200;
RA   Moreau K., Dizin E., Ray H., Luquain C., Lefai E., Foufelle F., Billaud M.,
RA   Lenoir G.M., Venezia N.D.;
RT   "BRCA1 affects lipid synthesis through its interaction with acetyl-CoA
RT   carboxylase.";
RL   J. Biol. Chem. 281:3172-3181(2006).
RN   [37]
RP   INTERACTION WITH ACACA.
RX   PubMed=16698035; DOI=10.1016/j.jmb.2006.04.010;
RA   Ray H., Moreau K., Dizin E., Callebaut I., Venezia N.D.;
RT   "ACCA phosphopeptide recognition by the BRCT repeats of BRCA1.";
RL   J. Mol. Biol. 359:973-982(2006).
RN   [38]
RP   FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION BY AURKA, AND ACTIVITY
RP   REGULATION.
RX   PubMed=18056443; DOI=10.1158/0008-5472.can-07-2578;
RA   Sankaran S., Crone D.E., Palazzo R.E., Parvin J.D.;
RT   "Aurora-A kinase regulates breast cancer associated gene 1 inhibition of
RT   centrosome-dependent microtubule nucleation.";
RL   Cancer Res. 67:11186-11194(2007).
RN   [39]
RP   INTERACTION WITH ABRAXAS1.
RX   PubMed=17643122; DOI=10.1038/nsmb1277;
RA   Kim H., Huang J., Chen J.;
RT   "CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA damage
RT   response.";
RL   Nat. Struct. Mol. Biol. 14:710-715(2007).
RN   [40]
RP   INTERACTION WITH ABRAXAS1.
RX   PubMed=17643121; DOI=10.1038/nsmb1279;
RA   Liu Z., Wu J., Yu X.;
RT   "CCDC98 targets BRCA1 to DNA damage sites.";
RL   Nat. Struct. Mol. Biol. 14:716-720(2007).
RN   [41]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [42]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ABRAXAS1.
RX   PubMed=17525340; DOI=10.1126/science.1139476;
RA   Wang B., Matsuoka S., Ballif B.A., Zhang D., Smogorzewska A., Giyi S.,
RA   Elledge S.J.;
RT   "Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage
RT   response.";
RL   Science 316:1194-1198(2007).
RN   [43]
RP   INVOLVEMENT IN PNCA4.
RX   PubMed=18762988; DOI=10.1007/s00439-008-0554-0;
RA   Al-Sukhni W., Rothenmund H., Borgida A.E., Zogopoulos G., O'Shea A.M.,
RA   Pollett A., Gallinger S.;
RT   "Germline BRCA1 mutations predispose to pancreatic adenocarcinoma.";
RL   Hum. Genet. 124:271-278(2008).
RN   [44]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395; SER-398; SER-753;
RP   SER-1211; SER-1217 AND SER-1218, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [45]
RP   FUNCTION, AND IDENTIFICATION IN THE BRCA1-A COMPLEX.
RX   PubMed=19261748; DOI=10.1101/gad.1770609;
RA   Feng L., Huang J., Chen J.;
RT   "MERIT40 facilitates BRCA1 localization and DNA damage repair.";
RL   Genes Dev. 23:719-728(2009).
RN   [46]
RP   IDENTIFICATION IN THE BRCA1-A COMPLEX.
RX   PubMed=19261749; DOI=10.1101/gad.1770309;
RA   Wang B., Hurov K., Hofmann K., Elledge S.J.;
RT   "NBA1, a new player in the Brca1 A complex, is required for DNA damage
RT   resistance and checkpoint control.";
RL   Genes Dev. 23:729-739(2009).
RN   [47]
RP   IDENTIFICATION IN THE BRCA1-A COMPLEX.
RX   PubMed=19261746; DOI=10.1101/gad.1739609;
RA   Shao G., Patterson-Fortin J., Messick T.E., Feng D., Shanbhag N., Wang Y.,
RA   Greenberg R.A.;
RT   "MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA
RT   double-strand breaks.";
RL   Genes Dev. 23:740-754(2009).
RN   [48]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH PALB2,
RP   IDENTIFICATION IN A BRCA COMPLEX WITH BRCA1 AND PALB2, AND CHARACTERIZATION
RP   OF VARIANT OVARIAN CANCER 1411-THR.
RX   PubMed=19369211; DOI=10.1073/pnas.0811159106;
RA   Sy S.M., Huen M.S., Chen J.;
RT   "PALB2 is an integral component of the BRCA complex required for homologous
RT   recombination repair.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:7155-7160(2009).
RN   [49]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395 AND SER-398, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [50]
RP   FUNCTION, INTERACTION WITH CCAR2, AND SUBCELLULAR LOCATION.
RX   PubMed=20160719; DOI=10.1038/sj.bjc.6605577;
RA   Hiraike H., Wada-Hiraike O., Nakagawa S., Koyama S., Miyamoto Y., Sone K.,
RA   Tanikawa M., Tsuruga T., Nagasaka K., Matsumoto Y., Oda K., Shoji K.,
RA   Fukuhara H., Saji S., Nakagawa K., Kato S., Yano T., Taketani Y.;
RT   "Identification of DBC1 as a transcriptional repressor for BRCA1.";
RL   Br. J. Cancer 102:1061-1067(2010).
RN   [51]
RP   FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BARD1 AND UBXN1,
RP   UBIQUITINATION, AND MUTAGENESIS OF ILE-26.
RX   PubMed=20351172; DOI=10.1128/mcb.01056-09;
RA   Wu-Baer F., Ludwig T., Baer R.;
RT   "The UBXN1 protein associates with autoubiquitinated forms of the BRCA1
RT   tumor suppressor and inhibits its enzymatic function.";
RL   Mol. Cell. Biol. 30:2787-2798(2010).
RN   [52]
RP   FUNCTION IN CHROMOSOMAL STABILITY, AND PHOSPHORYLATION AT SER-988 BY CHEK2.
RX   PubMed=20364141; DOI=10.1038/ncb2051;
RA   Stolz A., Ertych N., Kienitz A., Vogel C., Schneider V., Fritz B.,
RA   Jacob R., Dittmar G., Weichert W., Petersen I., Bastians H.;
RT   "The CHK2-BRCA1 tumour suppressor pathway ensures chromosomal stability in
RT   human somatic cells.";
RL   Nat. Cell Biol. 12:492-499(2010).
RN   [53]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-423; SER-694;
RP   SER-1328; SER-1336 AND SER-1342, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [54]
RP   PHOSPHORYLATION AT SER-1524, AND SUBCELLULAR LOCATION.
RX   PubMed=21144835; DOI=10.1016/j.bbrc.2010.12.005;
RA   Kang Y., Cheong H.M., Lee J.H., Song P.I., Lee K.H., Kim S.Y., Jun J.Y.,
RA   You H.J.;
RT   "Protein phosphatase 5 is necessary for ATR-mediated DNA repair.";
RL   Biochem. Biophys. Res. Commun. 404:476-481(2011).
RN   [55]
RP   INTERACTION WITH PCLAF.
RX   PubMed=21673012; DOI=10.1158/1541-7786.mcr-10-0503;
RA   Kais Z., Barsky S.H., Mathsyaraja H., Zha A., Ransburgh D.J., He G.,
RA   Pilarski R.T., Shapiro C.L., Huang K., Parvin J.D.;
RT   "KIAA0101 interacts with BRCA1 and regulates centrosome number.";
RL   Mol. Cancer Res. 9:1091-1099(2011).
RN   [56]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-1218; SER-1336 AND
RP   SER-1342, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [57]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [58]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-434; SER-551;
RP   SER-694; SER-708; SER-1009; SER-1189; SER-1191 AND SER-1542, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [59]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-339; LYS-459; LYS-583; LYS-654;
RP   LYS-734 AND LYS-739, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [60]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-339; LYS-443 AND LYS-583, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [61]
RP   INTERACTION WITH EXD2.
RX   PubMed=26807646; DOI=10.1038/ncb3303;
RA   Broderick R., Nieminuszczy J., Baddock H.T., Deshpande R.A., Gileadi O.,
RA   Paull T.T., McHugh P.J., Niedzwiedz W.;
RT   "EXD2 promotes homologous recombination by facilitating DNA end
RT   resection.";
RL   Nat. Cell Biol. 18:271-280(2016).
RN   [62]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109; LYS-301; LYS-339; LYS-443;
RP   LYS-459; LYS-519; LYS-583; LYS-918; LYS-987 AND LYS-1079, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [63]
RP   INTERACTION WITH PALB2.
RX   PubMed=28319063; DOI=10.1038/onc.2017.46;
RA   Foo T.K., Tischkowitz M., Simhadri S., Boshari T., Zayed N., Burke K.A.,
RA   Berman S.H., Blecua P., Riaz N., Huo Y., Ding Y.C., Neuhausen S.L.,
RA   Weigelt B., Reis-Filho J.S., Foulkes W.D., Xia B.;
RT   "Compromised BRCA1-PALB2 interaction is associated with breast cancer
RT   risk.";
RL   Oncogene 36:4161-4170(2017).
RN   [64]
RP   STRUCTURE BY NMR OF 1-110 IN COMPLEX WITH ZINC IONS AND BARD1, AND SUBUNIT.
RX   PubMed=11573085; DOI=10.1038/nsb1001-833;
RA   Brzovic P.S., Rajagopal P., Hoyt D.W., King M.C., Klevit R.E.;
RT   "Structure of a BRCA1-BARD1 heterodimeric RING-RING complex.";
RL   Nat. Struct. Biol. 8:833-837(2001).
RN   [65]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1646-1859, PARTIAL PROTEIN
RP   SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11573086; DOI=10.1038/nsb1001-838;
RA   Williams R.S., Green R., Glover J.N.;
RT   "Crystal structure of the BRCT repeat region from the breast cancer-
RT   associated protein BRCA1.";
RL   Nat. Struct. Biol. 8:838-842(2001).
RN   [66]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1646-1859 OF VARIANT BC ARG-1775,
RP   CHARACTERIZATION OF VARIANT BC ARG-1775, AND CIRCULAR DICHROISM.
RX   PubMed=12427738; DOI=10.1074/jbc.m210019200;
RA   Williams R.S., Glover J.N.;
RT   "Structural consequences of a cancer-causing BRCA1-BRCT missense
RT   mutation.";
RL   J. Biol. Chem. 278:2630-2635(2003).
RN   [67]
RP   STRUCTURE BY NMR OF 1755-1863.
RX   PubMed=15609993; DOI=10.1021/bi049550q;
RA   Gaiser O.J., Ball L.J., Schmieder P., Leitner D., Strauss H., Wahl M.,
RA   Kuhne R., Oschkinat H., Heinemann U.;
RT   "Solution structure, backbone dynamics, and association behavior of the C-
RT   terminal BRCT domain from the breast cancer-associated protein BRCA1.";
RL   Biochemistry 43:15983-15995(2004).
RN   [68]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1649-1859 IN COMPLEX WITH
RP   PHOSPHORYLATED BRIP1 PEPTIDE, MUTAGENESIS OF SER-1655; LYS-1702 AND
RP   GLY-1738, CHARACTERIZATION OF VARIANT OVARIAN CANCER ARG-1749,
RP   CHARACTERIZATION OF VARIANT BC ARG-1775, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH PHOSPHORYLATED BRIP1.
RX   PubMed=15133502; DOI=10.1038/nsmb775;
RA   Clapperton J.A., Manke I.A., Lowery D.M., Ho T., Haire L.F., Yaffe M.B.,
RA   Smerdon S.J.;
RT   "Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated
RT   BACH1 with implications for cancer.";
RL   Nat. Struct. Mol. Biol. 11:512-518(2004).
RN   [69]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1646-1859 IN COMPLEX WITH
RP   PHOSPHORYLATED RBBP8 PEPTIDE, AND SUBUNIT.
RX   PubMed=16101277; DOI=10.1021/bi0509651;
RA   Varma A.K., Brown R.S., Birrane G., Ladias J.A.;
RT   "Structural basis for cell cycle checkpoint control by the BRCA1-CtIP
RT   complex.";
RL   Biochemistry 44:10941-10946(2005).
RN   [70]
RP   X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS) OF 1646-1859 IN COMPLEX WITH
RP   PHOSPHORYLATED ACACA PEPTIDE, AND SUBUNIT.
RX   PubMed=18452305; DOI=10.1021/bi800314m;
RA   Shen Y., Tong L.;
RT   "Structural evidence for direct interactions between the BRCT domains of
RT   human BRCA1 and a phospho-peptide from human ACC1.";
RL   Biochemistry 47:5767-5773(2008).
RN   [71]
RP   X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 1649-1859 OF VARIANT BC LYS-1775,
RP   VARIANT BC LYS-1775, AND CHARACTERIZATION OF VARIANT BC LYS-1775.
RX   PubMed=18285836; DOI=10.1038/ejhg.2008.13;
RA   Tischkowitz M., Hamel N., Carvalho M.A., Birrane G., Soni A.,
RA   van Beers E.H., Joosse S.A., Wong N., Novak D., Quenneville L.A.,
RA   Grist S.A., Nederlof P.M., Goldgar D.E., Tavtigian S.V., Monteiro A.N.,
RA   Ladias J.A., Foulkes W.D.;
RT   "Pathogenicity of the BRCA1 missense variant M1775K is determined by the
RT   disruption of the BRCT phosphopeptide-binding pocket: a multi-modal
RT   approach.";
RL   Eur. J. Hum. Genet. 16:820-832(2008).
RN   [72]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1646-1859 IN COMPLEX WITH
RP   PHOSPHORYLATED PEPTIDES, AND DOMAIN.
RX   PubMed=20159462; DOI=10.1016/j.str.2009.12.008;
RA   Campbell S.J., Edwards R.A., Glover J.N.;
RT   "Comparison of the structures and peptide binding specificities of the BRCT
RT   domains of MDC1 and BRCA1.";
RL   Structure 18:167-176(2010).
RN   [73]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1646-1859 IN COMPLEX WITH
RP   PHOSPHORYLATED BRIP1 PEPTIDE, INTERACTION WITH BRIP1, MUTAGENESIS OF
RP   GLY-1656; THR-1700; ARG-1835 AND GLU-1836, AND CHARACTERIZATION OF VARIANTS
RP   BC GLN-1699 AND TRP-1699.
RX   PubMed=21473589; DOI=10.1021/bi2003795;
RA   Coquelle N., Green R., Glover J.N.;
RT   "Impact of BRCA1 BRCT domain missense substitutions on phosphopeptide
RT   recognition.";
RL   Biochemistry 50:4579-4589(2011).
RN   [74]
RP   X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 1649-1859 IN COMPLEX WITH
RP   ABRAXAS1, AND INTERACTION WITH ABRAXAS1.
RX   PubMed=24316840; DOI=10.1107/s1744309113030649;
RA   Badgujar D.C., Sawant U., Vikrant X., Yadav L., Hosur M.V., Varma A.K.;
RT   "Preliminary crystallographic studies of BRCA1 BRCT-ABRAXAS complex.";
RL   Acta Crystallogr. F 69:1401-1404(2013).
RN   [75]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1646-1859 IN COMPLEX WITH
RP   ABRAXAS1, INTERACTION WITH ABRAXAS1, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF PHE-1662; MET-1663; TYR-1666; ARG-1670 AND LYS-1671.
RX   PubMed=26778126; DOI=10.1016/j.molcel.2015.12.017;
RA   Wu Q., Paul A., Su D., Mehmood S., Foo T.K., Ochi T., Bunting E.L., Xia B.,
RA   Robinson C.V., Wang B., Blundell T.L.;
RT   "Structure of BRCA1-BRCT/Abraxas complex reveals phosphorylation-dependent
RT   BRCT dimerization at DNA damage sites.";
RL   Mol. Cell 61:434-448(2016).
RN   [76]
RP   REVIEW ON VARIANTS.
RX   PubMed=8807330; DOI=10.1002/humu.1380080102;
RA   Couch F.J., Weber B.L.;
RT   "Mutations and polymorphisms in the familial early-onset breast cancer
RT   (BRCA1) gene.";
RL   Hum. Mutat. 8:8-18(1996).
RN   [77]
RP   VARIANT BC ARG-1775, AND VARIANTS LEU-1637 AND GLU-1708.
RX   PubMed=7939630; DOI=10.1126/science.7939630;
RA   Futreal P.A., Liu Q., Shattuck-Eidens D., Cochran C., Harshman K.,
RA   Tavtigian S., Bennett L.M., Haugen-Strano A., Swensen J., Miki Y.,
RA   Eddington K., McClure M., Frye C., Weaver-Felhaus J., Ding W., Gholami Z.,
RA   Soederkvist P., Terry L., Jhanwar S., Berchuk A., Iglehart J.D., Marks J.,
RA   Ballinger D.G., Barrett J.C., Skolnick M.H., Kamb A., Wiseman R.;
RT   "BRCA1 mutations in primary breast and ovarian carcinomas.";
RL   Science 266:120-122(1994).
RN   [78]
RP   VARIANT BC GLY-64, AND VARIANTS ALA-772; ASN-1040 AND GLY-1443.
RX   PubMed=7894491; DOI=10.1038/ng1294-387;
RA   Castilla L.H., Couch F.J., Erdos M.R., Hoskins K.F., Calzone K.,
RA   Garber J.E., Boyd J., Lubin M.B., Deshano M.L., Brody L.C., Collins F.S.,
RA   Weber B.L.;
RT   "Mutations in the BRCA1 gene in families with early-onset breast and
RT   ovarian cancer.";
RL   Nat. Genet. 8:387-391(1994).
RN   [79]
RP   VARIANT BC GLY-61, AND VARIANTS ARG-356; GLY-1038; ASN-1040; ARG-1183 AND
RP   GLY-1613.
RX   PubMed=7894493; DOI=10.1038/ng1294-399;
RA   Friedman L.S., Ostermeyer E.A., Szabo C.I., Dowd P., Lynch E.D.,
RA   Rowell S.E., King M.-C.;
RT   "Confirmation of BRCA1 by analysis of germline mutations linked to breast
RT   and ovarian cancer in ten families.";
RL   Nat. Genet. 8:399-404(1994).
RN   [80]
RP   VARIANT BC GLY-61.
RX   PubMed=8554067;
RA   Serova O., Montagna M., Torchard D., Narod S.A., Tonin P., Sylla B.,
RA   Lynch H.T., Feunteun J., Lenoir G.M.;
RT   "A high incidence of BRCA1 mutations in 20 breast-ovarian cancer
RT   families.";
RL   Am. J. Hum. Genet. 58:42-51(1996).
RN   [81]
RP   VARIANT BROVCA1 TRP-841.
RX   PubMed=8968716;
RX   DOI=10.1002/(sici)1098-2272(1996)13:6<595::aid-gepi5>3.0.co;2-#;
RA   Barker D.F., Almeida E.F.A., Casey G., Fain P.R., Liao S.-Y., Masunaka I.,
RA   Noble B., Kurosaki T., Anton-Culver H.;
RT   "BRCA1 R841W: a strong candidate for a common mutation with moderate
RT   phenotype.";
RL   Genet. Epidemiol. 13:595-604(1996).
RN   [82]
RP   VARIANTS BC AND BROVCA1.
RX   PubMed=8776600; DOI=10.1093/hmg/5.6.835;
RA   Durocher F., Shattuck-Eidens D., McClure M., Labrie F., Skolnick M.H.,
RA   Goldgar D.E., Simard J.;
RT   "Comparison of BRCA1 polymorphisms, rare sequence variants and/or missense
RT   mutations in unaffected and breast/ovarian cancer populations.";
RL   Hum. Mol. Genet. 5:835-842(1996).
RN   [83]
RP   VARIANTS BC MET-271 AND SER-1150.
RX   PubMed=8723683;
RX   DOI=10.1002/(sici)1098-1004(1996)7:4<334::aid-humu7>3.0.co;2-8;
RA   Katagiri T., Emi M., Ito I., Kobayashi K., Yoshimoto M., Iwase T.,
RA   Kasumi F., Miki Y., Skolnick M.H., Nakamura Y.;
RT   "Mutations in the BRCA1 gene in Japanese breast cancer patients.";
RL   Hum. Mutat. 7:334-339(1996).
RN   [84]
RP   VARIANT BC GLY-61, AND VARIANTS ARG-239; TRP-841 AND ILE-1512.
RX   PubMed=9760198; DOI=10.1007/s004390050799;
RA   Dong J., Chang-Claude J., Wu Y., Schumacher V., Debatin I., Tonin P.,
RA   Royer-Pokora B.;
RT   "A high proportion of mutations in the BRCA1 gene in German breast/ovarian
RT   cancer families with clustering of mutations in the 3' third of the gene.";
RL   Hum. Genet. 103:154-161(1998).
RN   [85]
RP   VARIANT BC GLY-64, AND VARIANTS ALA-772; GLU-820; ASN-1040; GLY-1443;
RP   ILE-1512; LEU-1637 AND ILE-1652.
RX   PubMed=9482581;
RX   DOI=10.1002/(sici)1098-1004(1998)11:2<166::aid-humu10>3.0.co;2-x;
RA   Andersen T.I., Eiken H.G., Couch F., Kaada G., Skrede M., Johnsen H.,
RA   Aloysius T.A., Tveit K.M., Tranebjaerg L., Doerum A., Moeller P.,
RA   Weber B.L., Boerresen-Dale A.-L.;
RT   "Constant denaturant gel electrophoresis (CDGE) in BRCA1 mutation
RT   screening.";
RL   Hum. Mutat. 11:166-174(1998).
RN   [86]
RP   VARIANTS BC SER-22; LEU-461; ASP-465; VAL-552; SER-892; ASP-960; ILE-1025
RP   AND ALA-1047.
RX   PubMed=9609997; DOI=10.1007/s100380050035;
RA   Katagiri T., Kasumi F., Yoshimoto M., Nomizu T., Asaishi K., Abe R.,
RA   Tsuchiya A., Sugano M., Takai S., Yoneda M., Fukutomi T., Nanba K.,
RA   Makita M., Okazaki H., Hirata K., Okazaki M., Furutsuma Y., Morishita Y.,
RA   Iino Y., Karino T., Ayabe H., Hara S., Kajiwara T., Houga S., Shimizu T.,
RA   Toda M., Yamazaki Y., Uchida T., Kunitomo K., Sonoo H., Kurebayashi J.,
RA   Shimotsuma K., Nakamura Y., Miki Y.;
RT   "High proportion of missense mutations of the BRCA1 and BRCA2 genes in
RT   Japanese breast cancer families.";
RL   J. Hum. Genet. 43:42-48(1998).
RN   [87]
RP   VARIANT OVARIAN CANCER ARG-1749.
RX   PubMed=10486320; DOI=10.1086/302583;
RA   Gayther S.A., Russell P., Harrington P., Antoniou A.C., Easton D.F.,
RA   Ponder B.A.J.;
RT   "The contribution of germline BRCA1 and BRCA2 mutations to familial ovarian
RT   cancer: no evidence for other ovarian cancer-susceptibility genes.";
RL   Am. J. Hum. Genet. 65:1021-1029(1999).
RN   [88]
RP   VARIANT BC SER-346, AND VARIANTS LEU-871; GLY-1038; ARG-1183 AND GLY-1613.
RX   PubMed=10323242; DOI=10.1007/s004390050936;
RA   Li S.S.-L., Tseng H.-M., Yang T.-P., Liu C.-H., Teng S.-J., Huang H.-W.,
RA   Chen L.-M., Kao H.-W., Chen J.H., Tseng J.-N., Chen A., Hou M.-F.,
RA   Huang T.-J., Chang H.-T., Mok K.-T., Tsai J.-H.;
RT   "Molecular characterization of germline mutations in the BRCA1 and BRCA2
RT   genes from breast cancer families in Taiwan.";
RL   Hum. Genet. 104:201-204(1999).
RN   [89]
RP   VARIANTS OVARIAN CANCER, AND VARIANTS.
RX   PubMed=10196379; DOI=10.1093/hmg/8.5.889;
RA   Janezic S.A., Ziogas A., Krumroy L.M., Krasner M., Plummer S.J., Cohen P.,
RA   Gildea M., Barker D., Haile R., Casey G., Anton-Culver H.;
RT   "Germline BRCA1 alterations in a population-based series of ovarian cancer
RT   cases.";
RL   Hum. Mol. Genet. 8:889-897(1999).
RN   [90]
RP   VARIANTS GLY-1347; ILE-1512 AND ILE-1652.
RX   PubMed=12215251; DOI=10.1089/10906570260199375;
RA   Deffenbaugh A.M., Frank T.S., Hoffman M., Cannon-Albright L.,
RA   Neuhausen S.L.;
RT   "Characterization of common BRCA1 and BRCA2 variants.";
RL   Genet. Test. 6:119-121(2002).
RN   [91]
RP   VARIANTS ILE-656; LEU-871 AND GLY-1613.
RX   PubMed=12442274; DOI=10.1002/humu.9083;
RA   Zhi X., Szabo C., Chopin S., Suter N., Wang Q.-S., Ostrander E.A.,
RA   Sinilnikova O.M., Lenoir G.M., Goldgar D., Shi Y.-R.;
RT   "BRCA1 and BRCA2 sequence variants in Chinese breast cancer families.";
RL   Hum. Mutat. 20:474-474(2002).
RN   [92]
RP   VARIANT BC TYR-749.
RX   PubMed=12442275; DOI=10.1002/humu.9084;
RA   Ruiz-Flores P., Sinilnikova O.M., Badzioch M., Calderon-Garciduenas A.L.,
RA   Chopin S., Fabrice O., Gonzalez-Guerrero J.F., Szabo C., Lenoir G.,
RA   Goldgar D.E., Barrera-Saldana H.A.;
RT   "BRCA1 and BRCA2 mutation analysis of early-onset and familial breast
RT   cancer cases in Mexico.";
RL   Hum. Mutat. 20:474-475(2002).
RN   [93]
RP   VARIANTS BC GLY-61; LYS-71; GLN-866; TYR-888; ILE-1139; GLY-1210 AND
RP   PRO-1297, AND VARIANTS BROVCA1 TYR-835 AND PRO-1786.
RX   PubMed=12938098; DOI=10.1002/humu.9174;
RA   Meyer P., Voigtlaender T., Bartram C.R., Klaes R.;
RT   "Twenty-three novel BRCA1 and BRCA2 sequence alterations in breast and/or
RT   ovarian cancer families in Southern Germany.";
RL   Hum. Mutat. 22:259-259(2003).
RN   [94]
RP   VARIANTS ASN-693; ASN-1040; ALA-1060 AND MET-1665.
RX   PubMed=15026808; DOI=10.1038/sj.bjc.6601656;
RA   Claes K., Poppe B., Coene I., De Paepe A., Messiaen L.;
RT   "BRCA1 and BRCA2 germline mutation spectrum and frequencies in Belgian
RT   breast/ovarian cancer families.";
RL   Br. J. Cancer 90:1244-1251(2004).
RN   [95]
RP   VARIANTS OVARIAN CANCER GLY-61; THR-1411; ARG-1697 AND TRP-1699.
RX   PubMed=14746861; DOI=10.1016/j.ejca.2003.09.016;
RA   Malander S., Ridderheim M., Masbaeck A., Loman N., Kristoffersson U.,
RA   Olsson H., Nilbert M., Borg A.;
RT   "One in 10 ovarian cancer patients carry germ line BRCA1 or BRCA2
RT   mutations: results of a prospective study in Southern Sweden.";
RL   Eur. J. Cancer 40:422-428(2004).
RN   [96]
RP   VARIANTS BC/BROVCA1 LYS-10; LYS-23; ILE-1187; HIS-1200 AND TYR-1217,
RP   VARIANTS BC ILE-1204 AND ASN-1207, VARIANTS BROVCA1 LEU-1226 AND GLY-1243,
RP   AND VARIANT ARG-1183.
RX   PubMed=14722926; DOI=10.1002/humu.9213;
RA   Valarmathi M.T., Sawhney M., Deo S.S.V., Shukla N.K., Das S.N.;
RT   "Novel germline mutations in the BRCA1 and BRCA2 genes in Indian breast and
RT   breast-ovarian cancer families.";
RL   Hum. Mutat. 23:205-205(2004).
RN   [97]
RP   VARIANTS HIS-856; LEU-871; GLY-1038; ARG-1183; THR-1628; GLN-1690 AND
RP   GLY-1713.
RX   PubMed=15365993; DOI=10.1002/humu.9275;
RA   Seo J.H., Cho D.-Y., Ahn S.-H., Yoon K.-S., Kang C.-S., Cho H.M., Lee H.S.,
RA   Choe J.J., Choi C.W., Kim B.S., Shin S.W., Kim Y.H., Kim J.S., Son G.-S.,
RA   Lee J.-B., Koo B.H.;
RT   "BRCA1 and BRCA2 germline mutations in Korean patients with sporadic breast
RT   cancer.";
RL   Hum. Mutat. 24:350-350(2004).
RN   [98]
RP   VARIANTS [LARGE SCALE ANALYSIS] PHE-30; PHE-758 AND CYS-778.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [99]
RP   VARIANTS THR-18; MET-1495; GLY-1623; ILE-1685; ALA-1685; ARG-1689;
RP   TRP-1699; GLU-1706; GLU-1708; ARG-1715; ARG-1738; PRO-1764; SER-1766 AND
RP   VAL-1788.
RX   PubMed=17924331; DOI=10.1086/521032;
RA   Easton D.F., Deffenbaugh A.M., Pruss D., Frye C., Wenstrup R.J.,
RA   Allen-Brady K., Tavtigian S.V., Monteiro A.N.A., Iversen E.S., Couch F.J.,
RA   Goldgar D.E.;
RT   "A systematic genetic assessment of 1,433 sequence variants of unknown
RT   clinical significance in the BRCA1 and BRCA2 breast cancer-predisposition
RT   genes.";
RL   Am. J. Hum. Genet. 81:873-883(2007).
RN   [100]
RP   CHARACTERIZATION OF VARIANTS GLY-1623 AND ILE-1685.
RX   PubMed=20513136; DOI=10.1002/humu.21267;
RA   Walker L.C., Whiley P.J., Couch F.J., Farrugia D.J., Healey S.,
RA   Eccles D.M., Lin F., Butler S.A., Goff S.A., Thompson B.A., Lakhani S.R.,
RA   Da Silva L.M., Tavtigian S.V., Goldgar D.E., Brown M.A., Spurdle A.B.;
RT   "Detection of splicing aberrations caused by BRCA1 and BRCA2 sequence
RT   variants encoding missense substitutions: implications for prediction of
RT   pathogenicity.";
RL   Hum. Mutat. 31:E1484-E1505(2010).
RN   [101]
RP   VARIANT FANCS ALA-1736, CHARACTERIZATION OF VARIANT FANCS ALA-1736,
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH UIMC1.
RX   PubMed=23269703; DOI=10.1158/2159-8290.cd-12-0421;
RA   Domchek S.M., Tang J., Stopfer J., Lilli D.R., Hamel N., Tischkowitz M.,
RA   Monteiro A.N., Messick T.E., Powers J., Yonker A., Couch F.J.,
RA   Goldgar D.E., Davidson H.R., Nathanson K.L., Foulkes W.D., Greenberg R.A.;
RT   "Biallelic deleterious BRCA1 mutations in a woman with early-onset ovarian
RT   cancer.";
RL   Cancer Discov. 3:399-405(2013).
RN   [102]
RP   CHARACTERIZATION OF VARIANTS BC PHE-4; THR-18; GLN-45; GLY-61; GLY-64;
RP   TYR-67; LYS-132; HIS-142; PHE-147; PRO-165; TRP-170; TYR-186; ILE-191;
RP   MET-231; VAL-245; VAL-246; LEU-271; PHE-668; ASN-695; LEU-798; TYR-810;
RP   LYS-826; GLN-841; HIS-856; ASN-1101; ASN-1140; GLY-1140; LYS-1214;
RP   LYS-1236; SER-1267; VAL-1282; SER-1297 DEL; ARG-1301; LYS-1346; ILE-1378;
RP   VAL-1400; PRO-1407; THR-1411; GLY-1443; GLY-1448; CYS-1486; MET-1534;
RP   PRO-1589; THR-1628; PRO-1651; PHE-1651; PHE-1655; ARG-1686; GLN-1686;
RP   VAL-1688 DEL; ILE-1691; TRP-1699; GLN-1699; GLU-1706; ALA-1706; GLU-1708;
RP   CYS-1718; ALA-1720; LYS-1735; ALA-1736; GLY-1739; VAL-1739; GLN-1746;
RP   THR-1753; PRO-1764; SER-1767; VAL-1770; CYS-1782; THR-1789; ASP-1794;
RP   ASP-1804; ARG-1812; ARG-1837 AND LEU-1862, AND VARIANTS CYS-105; CYS-866;
RP   ALA-1060; LYS-1250 AND ILE-1652.
RX   PubMed=23867111; DOI=10.1158/2159-8290.cd-13-0094;
RA   Bouwman P., van der Gulden H., van der Heijden I., Drost R., Klijn C.N.,
RA   Prasetyanti P., Pieterse M., Wientjens E., Seibler J., Hogervorst F.B.,
RA   Jonkers J.;
RT   "A high-throughput functional complementation assay for classification of
RT   BRCA1 missense variants.";
RL   Cancer Discov. 3:1142-1155(2013).
RN   [103]
RP   VARIANT FANCS TRP-1699, AND SUBCELLULAR LOCATION.
RX   PubMed=25472942; DOI=10.1158/2159-8290.cd-14-1156;
RG   University of Washington Centre for Mendelian Genomics;
RG   FORGE Canada Consortium;
RA   Sawyer S.L., Tian L., Kaehkoenen M., Schwartzentruber J., Kircher M.,
RA   Majewski J., Dyment D.A., Innes A.M., Boycott K.M., Moreau L.A.,
RA   Moilanen J.S., Greenberg R.A.;
RT   "Biallelic mutations in BRCA1 cause a new Fanconi anemia subtype.";
RL   Cancer Discov. 5:135-142(2015).
RN   [104]
RP   VARIANT BC PRO-1780, VARIANT BROVCA1 PRO-1780, AND VARIANT OC PRO-1780.
RX   PubMed=28364669; DOI=10.1016/j.breast.2017.03.006;
RA   Ryu J.M., Kang G., Nam S.J., Kim S.W., Yu J., Lee S.K., Bae S.Y., Park S.,
RA   Paik H.J., Kim J.W., Park S.S., Lee J.E., Kim S.W.;
RT   "Suggestion of BRCA1 c.5339T>C (p.L1780P) variant confer from 'unknown
RT   significance' to 'Likely pathogenic' based on clinical evidence in Korea.";
RL   Breast 33:109-116(2017).
RN   [105]
RP   VARIANT FANCS 903-CYS--TYR-1863 DEL.
RX   PubMed=29133208; DOI=10.1016/j.ejmg.2017.11.003;
RA   Freire B.L., Homma T.K., Funari M.F.A., Lerario A.M., Leal A.M.,
RA   Velloso E.D.R.P., Malaquias A.C., Jorge A.A.L.;
RT   "Homozygous loss of function BRCA1 variant causing a Fanconi-anemia-like
RT   phenotype, a clinical report and review of previous patients.";
RL   Eur. J. Med. Genet. 61:130-133(2018).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that specifically mediates the
CC       formation of 'Lys-6'-linked polyubiquitin chains and plays a central
CC       role in DNA repair by facilitating cellular responses to DNA damage. It
CC       is unclear whether it also mediates the formation of other types of
CC       polyubiquitin chains. The E3 ubiquitin-protein ligase activity is
CC       required for its tumor suppressor function. The BRCA1-BARD1 heterodimer
CC       coordinates a diverse range of cellular pathways such as DNA damage
CC       repair, ubiquitination and transcriptional regulation to maintain
CC       genomic stability. Regulates centrosomal microtubule nucleation.
CC       Required for normal cell cycle progression from G2 to mitosis. Required
CC       for appropriate cell cycle arrests after ionizing irradiation in both
CC       the S-phase and the G2 phase of the cell cycle. Involved in
CC       transcriptional regulation of P21 in response to DNA damage. Required
CC       for FANCD2 targeting to sites of DNA damage. May function as a
CC       transcriptional regulator. Inhibits lipid synthesis by binding to
CC       inactive phosphorylated ACACA and preventing its dephosphorylation.
CC       Contributes to homologous recombination repair (HRR) via its direct
CC       interaction with PALB2, fine-tunes recombinational repair partly
CC       through its modulatory role in the PALB2-dependent loading of BRCA2-
CC       RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8
CC       complex which regulates CHEK1 activation and controls cell cycle G2/M
CC       checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8.
CC       Acts as a transcriptional activator (PubMed:20160719).
CC       {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:10724175,
CC       ECO:0000269|PubMed:11836499, ECO:0000269|PubMed:12887909,
CC       ECO:0000269|PubMed:12890688, ECO:0000269|PubMed:14976165,
CC       ECO:0000269|PubMed:14990569, ECO:0000269|PubMed:16326698,
CC       ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:17525340,
CC       ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:19261748,
CC       ECO:0000269|PubMed:19369211, ECO:0000269|PubMed:20160719,
CC       ECO:0000269|PubMed:20351172, ECO:0000269|PubMed:20364141}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000269|PubMed:10500182,
CC         ECO:0000269|PubMed:12887909, ECO:0000269|PubMed:12890688,
CC         ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:18056443,
CC         ECO:0000269|PubMed:20351172};
CC   -!- ACTIVITY REGULATION: The E3 ubiquitin-protein ligase activity is
CC       inhibited by phosphorylation by AURKA. Activity is increased by
CC       phosphatase treatment. {ECO:0000269|PubMed:18056443}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Heterodimer with BARD1 (PubMed:11573085, PubMed:12890688,
CC       PubMed:14976165). Part of the BRCA1-associated genome surveillance
CC       complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2
CC       and the MRE11-RAD50-NBN protein (MRN) complex (PubMed:10783165). This
CC       association could be a dynamic process changing throughout the cell
CC       cycle and within subnuclear domains (PubMed:10783165). Component of the
CC       BRCA1-A complex, at least composed of BRCA1, BARD1, UIMC1/RAP80,
CC       ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1 (PubMed:19261746,
CC       PubMed:19261748, PubMed:19261749, PubMed:20351172). Interacts (via the
CC       BRCT domains) with ABRAXAS1 (phosphorylated form); this is important
CC       for recruitment to sites of DNA damage (PubMed:17525340,
CC       PubMed:17643121, PubMed:17643122, PubMed:24316840, PubMed:26778126,
CC       PubMed:23269703). Can form a heterotetramer with two molecules of
CC       ABRAXAS1 (phosphorylated form) (PubMed:26778126). Component of the
CC       BRCA1-RBBP8 complex (PubMed:16101277). Interacts (via the BRCT domains)
CC       with RBBP8 ('Ser-327' phosphorylated form); the interaction
CC       ubiquitinates RBBP8, regulates CHEK1 activation, and involves RBBP8 in
CC       BRCA1-dependent G2/M checkpoint control on DNA damage (PubMed:16818604,
CC       PubMed:9811458). Associates with RNA polymerase II holoenzyme
CC       (PubMed:9662397). Interacts with SMC1A, NELFB, DCLRE1C, CLSPN
CC       (PubMed:11877377, PubMed:15096610, PubMed:15456891, PubMed:11739404).
CC       Interacts with CHEK1, CHEK2, BAP1, BRCC3, AURKA, UBXN1 and PCLAF
CC       (PubMed:10724175, PubMed:11836499, PubMed:14636569, PubMed:14990569,
CC       PubMed:20351172, PubMed:21673012). Interacts (via BRCT domains) with
CC       BRIP1 (phosphorylated form) (PubMed:11301010, PubMed:15133502,
CC       PubMed:21473589). Interacts with FANCD2 (ubiquitinated form)
CC       (PubMed:11239454). Interacts with H2AX (phosphorylated on 'Ser-140')
CC       (PubMed:12419185). Interacts (via the BRCT domains) with ACACA
CC       (phosphorylated form); the interaction prevents dephosphorylation of
CC       ACACA (PubMed:12360400, PubMed:16326698, PubMed:16698035,
CC       PubMed:18452305). Part of a BRCA complex containing BRCA1, BRCA2 and
CC       PALB2 (PubMed:19369211). Interacts directly with PALB2; the interaction
CC       is essential for its function in HRR (PubMed:19369211,
CC       PubMed:28319063). Interacts directly with BRCA2; the interaction occurs
CC       only in the presence of PALB2 which serves as the bridging protein
CC       (PubMed:19369211). Interacts (via the BRCT domains) with LMO4; the
CC       interaction represses the transcriptional activity of BRCA1
CC       (PubMed:11751867). Interacts (via the BRCT domains) with CCAR2 (via N-
CC       terminus); the interaction represses the transcriptional activator
CC       activity of BRCA1 (PubMed:20160719). Interacts with EXD2
CC       (PubMed:26807646). Interacts (via C-terminus) with DHX9; this
CC       interaction is direct and links BRCA1 to the RNA polymerase II
CC       holoenzyme (PubMed:9662397). {ECO:0000269|PubMed:10724175,
CC       ECO:0000269|PubMed:10783165, ECO:0000269|PubMed:11239454,
CC       ECO:0000269|PubMed:11301010, ECO:0000269|PubMed:11573085,
CC       ECO:0000269|PubMed:11739404, ECO:0000269|PubMed:11751867,
CC       ECO:0000269|PubMed:11836499, ECO:0000269|PubMed:11877377,
CC       ECO:0000269|PubMed:12360400, ECO:0000269|PubMed:12419185,
CC       ECO:0000269|PubMed:12890688, ECO:0000269|PubMed:14636569,
CC       ECO:0000269|PubMed:14976165, ECO:0000269|PubMed:14990569,
CC       ECO:0000269|PubMed:15096610, ECO:0000269|PubMed:15133502,
CC       ECO:0000269|PubMed:15456891, ECO:0000269|PubMed:16101277,
CC       ECO:0000269|PubMed:16326698, ECO:0000269|PubMed:16698035,
CC       ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:17525340,
CC       ECO:0000269|PubMed:17643121, ECO:0000269|PubMed:17643122,
CC       ECO:0000269|PubMed:18452305, ECO:0000269|PubMed:19261746,
CC       ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749,
CC       ECO:0000269|PubMed:19369211, ECO:0000269|PubMed:20159462,
CC       ECO:0000269|PubMed:20160719, ECO:0000269|PubMed:20351172,
CC       ECO:0000269|PubMed:21473589, ECO:0000269|PubMed:21673012,
CC       ECO:0000269|PubMed:23269703, ECO:0000269|PubMed:24316840,
CC       ECO:0000269|PubMed:26778126, ECO:0000269|PubMed:26807646,
CC       ECO:0000269|PubMed:28319063, ECO:0000269|PubMed:9528852,
CC       ECO:0000269|PubMed:9662397, ECO:0000269|PubMed:9811458}.
CC   -!- INTERACTION:
CC       P38398; Q6UWZ7: ABRAXAS1; NbExp=15; IntAct=EBI-349905, EBI-1263451;
CC       P38398; Q13085: ACACA; NbExp=2; IntAct=EBI-349905, EBI-717681;
CC       P38398; Q92560: BAP1; NbExp=3; IntAct=EBI-349905, EBI-1791447;
CC       P38398; Q99728: BARD1; NbExp=15; IntAct=EBI-349905, EBI-473181;
CC       P38398; P10415: BCL2; NbExp=6; IntAct=EBI-349905, EBI-77694;
CC       P38398; Q7Z569: BRAP; NbExp=3; IntAct=EBI-349905, EBI-349900;
CC       P38398; Q6PJG6: BRAT1; NbExp=6; IntAct=EBI-349905, EBI-10826195;
CC       P38398; P38398: BRCA1; NbExp=2; IntAct=EBI-349905, EBI-349905;
CC       P38398; Q9BX63: BRIP1; NbExp=24; IntAct=EBI-349905, EBI-3509650;
CC       P38398; P24385: CCND1; NbExp=3; IntAct=EBI-349905, EBI-375001;
CC       P38398; P24864: CCNE1; NbExp=2; IntAct=EBI-349905, EBI-519526;
CC       P38398; O14757: CHEK1; NbExp=3; IntAct=EBI-349905, EBI-974488;
CC       P38398; P03372: ESR1; NbExp=14; IntAct=EBI-349905, EBI-78473;
CC       P38398; Q92731: ESR2; NbExp=4; IntAct=EBI-349905, EBI-78505;
CC       P38398; Q14192: FHL2; NbExp=6; IntAct=EBI-349905, EBI-701903;
CC       P38398; P78347: GTF2I; NbExp=5; IntAct=EBI-349905, EBI-359622;
CC       P38398; P16104: H2AX; NbExp=4; IntAct=EBI-349905, EBI-494830;
CC       P38398; O75330: HMMR; NbExp=4; IntAct=EBI-349905, EBI-2556203;
CC       P38398; P10809: HSPD1; NbExp=2; IntAct=EBI-349905, EBI-352528;
CC       P38398; Q16666: IFI16; NbExp=9; IntAct=EBI-349905, EBI-2867186;
CC       P38398; P52292: KPNA2; NbExp=3; IntAct=EBI-349905, EBI-349938;
CC       P38398; Q14676: MDC1; NbExp=4; IntAct=EBI-349905, EBI-495644;
CC       P38398; Q8WX92: NELFB; NbExp=5; IntAct=EBI-349905, EBI-347721;
CC       P38398; Q86YC2: PALB2; NbExp=27; IntAct=EBI-349905, EBI-1222653;
CC       P38398; P62136: PPP1CA; NbExp=2; IntAct=EBI-349905, EBI-357253;
CC       P38398; P62140: PPP1CB; NbExp=3; IntAct=EBI-349905, EBI-352350;
CC       P38398; P36873: PPP1CC; NbExp=2; IntAct=EBI-349905, EBI-356283;
CC       P38398; Q99708: RBBP8; NbExp=12; IntAct=EBI-349905, EBI-745715;
CC       P38398; P63165: SUMO1; NbExp=3; IntAct=EBI-349905, EBI-80140;
CC       P38398; P61956: SUMO2; NbExp=2; IntAct=EBI-349905, EBI-473220;
CC       P38398; P11388: TOP2A; NbExp=3; IntAct=EBI-349905, EBI-539628;
CC       P38398; Q12888: TP53BP1; NbExp=5; IntAct=EBI-349905, EBI-396540;
CC       P38398; Q96RL1: UIMC1; NbExp=10; IntAct=EBI-349905, EBI-725300;
CC       P38398; Q96RL1-1: UIMC1; NbExp=2; IntAct=EBI-349905, EBI-9640371;
CC       P38398; Q6NZY4: ZCCHC8; NbExp=2; IntAct=EBI-349905, EBI-1263058;
CC       P38398; Q9GZX5: ZNF350; NbExp=3; IntAct=EBI-349905, EBI-396421;
CC       P38398; Q61188: Ezh2; Xeno; NbExp=5; IntAct=EBI-349905, EBI-904311;
CC       P38398-1; Q99728: BARD1; NbExp=3; IntAct=EBI-21498346, EBI-473181;
CC       P38398-1; Q13526: PIN1; NbExp=4; IntAct=EBI-21498346, EBI-714158;
CC       P38398-5; Q92560: BAP1; NbExp=2; IntAct=EBI-2015072, EBI-1791447;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15133502,
CC       ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:20160719,
CC       ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:26778126,
CC       ECO:0000269|PubMed:9528852}. Chromosome {ECO:0000269|PubMed:23269703,
CC       ECO:0000269|PubMed:25472942, ECO:0000269|PubMed:26778126}. Cytoplasm
CC       {ECO:0000269|PubMed:20160719}. Note=Localizes at sites of DNA damage at
CC       double-strand breaks (DSBs); recruitment to DNA damage sites is
CC       mediated by ABRAXAS1 and the BRCA1-A complex (PubMed:26778126).
CC       Translocated to the cytoplasm during UV-induced apoptosis
CC       (PubMed:20160719). {ECO:0000269|PubMed:20160719,
CC       ECO:0000269|PubMed:26778126}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.
CC   -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm
CC       {ECO:0000269|PubMed:8972225}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=8;
CC       Name=1;
CC         IsoId=P38398-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P38398-2; Sequence=VSP_047891;
CC       Name=3; Synonyms=Delta11b;
CC         IsoId=P38398-3; Sequence=VSP_035399, VSP_043797;
CC       Name=4; Synonyms=DeltaBRCA1(17aa);
CC         IsoId=P38398-4; Sequence=VSP_035396;
CC       Name=5; Synonyms=Delta11, Delta772-3095;
CC         IsoId=P38398-5; Sequence=VSP_035398;
CC       Name=6;
CC         IsoId=P38398-6; Sequence=VSP_035399, VSP_043797, VSP_043798;
CC       Name=7;
CC         IsoId=P38398-7; Sequence=VSP_055404;
CC       Name=8;
CC         IsoId=P38398-8; Sequence=VSP_057569;
CC   -!- TISSUE SPECIFICITY: Isoform 1 and isoform 3 are widely expressed.
CC       Isoform 3 is reduced or absent in several breast and ovarian cancer
CC       cell lines.
CC   -!- DOMAIN: The BRCT domains recognize and bind phosphorylated pSXXF motif
CC       on proteins. The interaction with the phosphorylated pSXXF motif of
CC       ABRAXAS1, recruits BRCA1 at DNA damage sites.
CC       {ECO:0000269|PubMed:20159462}.
CC   -!- DOMAIN: The RING-type zinc finger domain interacts with BAP1.
CC       {ECO:0000269|PubMed:20159462}.
CC   -!- PTM: Phosphorylation at Ser-308 by AURKA is required for normal cell
CC       cycle progression from G2 to mitosis. Phosphorylated in response to IR,
CC       UV, and various stimuli that cause checkpoint activation, probably by
CC       ATM or ATR. Phosphorylation at Ser-988 by CHEK2 regulates mitotic
CC       spindle assembly. {ECO:0000269|PubMed:10724175,
CC       ECO:0000269|PubMed:11114888, ECO:0000269|PubMed:12183412,
CC       ECO:0000269|PubMed:14990569, ECO:0000269|PubMed:18056443,
CC       ECO:0000269|PubMed:20364141, ECO:0000269|PubMed:21144835}.
CC   -!- PTM: Autoubiquitinated, undergoes 'Lys-6'-linked polyubiquitination.
CC       'Lys-6'-linked polyubiquitination does not promote degradation.
CC       {ECO:0000269|PubMed:12890688, ECO:0000269|PubMed:20351172}.
CC   -!- POLYMORPHISM: There is evidence that the presence of the rare form of
CC       Gln-356-Arg and Leu-871-Pro polymorphisms may be associated with an
CC       increased risk for developing ovarian cancer.
CC   -!- DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy
CC       originating from breast epithelial tissue. Breast neoplasms can be
CC       distinguished by their histologic pattern. Invasive ductal carcinoma is
CC       by far the most common type. Breast cancer is etiologically and
CC       genetically heterogeneous. Important genetic factors have been
CC       indicated by familial occurrence and bilateral involvement. Mutations
CC       at more than one locus can be involved in different families or even in
CC       the same case. {ECO:0000269|PubMed:10323242,
CC       ECO:0000269|PubMed:11114888, ECO:0000269|PubMed:11301010,
CC       ECO:0000269|PubMed:12427738, ECO:0000269|PubMed:12442275,
CC       ECO:0000269|PubMed:12938098, ECO:0000269|PubMed:14722926,
CC       ECO:0000269|PubMed:15133502, ECO:0000269|PubMed:18285836,
CC       ECO:0000269|PubMed:21473589, ECO:0000269|PubMed:23867111,
CC       ECO:0000269|PubMed:28364669, ECO:0000269|PubMed:7545954,
CC       ECO:0000269|PubMed:7894491, ECO:0000269|PubMed:7894493,
CC       ECO:0000269|PubMed:7939630, ECO:0000269|PubMed:8554067,
CC       ECO:0000269|PubMed:8723683, ECO:0000269|PubMed:8776600,
CC       ECO:0000269|PubMed:9482581, ECO:0000269|PubMed:9609997,
CC       ECO:0000269|PubMed:9760198}. Note=Disease susceptibility is associated
CC       with variations affecting the gene represented in this entry. Mutations
CC       in BRCA1 are thought to be responsible for 45% of inherited breast
CC       cancer. Moreover, BRCA1 carriers have a 4-fold increased risk of colon
CC       cancer, whereas male carriers face a 3-fold increased risk of prostate
CC       cancer. Cells lacking BRCA1 show defects in DNA repair by homologous
CC       recombination.
CC   -!- DISEASE: Breast-ovarian cancer, familial, 1 (BROVCA1) [MIM:604370]: A
CC       condition associated with familial predisposition to cancer of the
CC       breast and ovaries. Characteristic features in affected families are an
CC       early age of onset of breast cancer (often before age 50), increased
CC       chance of bilateral cancers (cancer that develop in both breasts, or
CC       both ovaries, independently), frequent occurrence of breast cancer
CC       among men, increased incidence of tumors of other specific organs, such
CC       as the prostate. {ECO:0000269|PubMed:12938098,
CC       ECO:0000269|PubMed:14722926, ECO:0000269|PubMed:28364669,
CC       ECO:0000269|PubMed:8968716}. Note=Disease susceptibility is associated
CC       with variations affecting the gene represented in this entry. Mutations
CC       in BRCA1 are thought to be responsible for more than 80% of inherited
CC       breast-ovarian cancer.
CC   -!- DISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer
CC       defines malignancies originating from ovarian tissue. Although many
CC       histologic types of ovarian tumors have been described, epithelial
CC       ovarian carcinoma is the most common form. Ovarian cancers are often
CC       asymptomatic and the recognized signs and symptoms, even of late-stage
CC       disease, are vague. Consequently, most patients are diagnosed with
CC       advanced disease. {ECO:0000269|PubMed:10196379,
CC       ECO:0000269|PubMed:10486320, ECO:0000269|PubMed:14746861,
CC       ECO:0000269|PubMed:28364669}. Note=Disease susceptibility is associated
CC       with variations affecting the gene represented in this entry.
CC   -!- DISEASE: Pancreatic cancer 4 (PNCA4) [MIM:614320]: A malignant neoplasm
CC       of the pancreas. Tumors can arise from both the exocrine and endocrine
CC       portions of the pancreas, but 95% of them develop from the exocrine
CC       portion, including the ductal epithelium, acinar cells, connective
CC       tissue, and lymphatic tissue. {ECO:0000269|PubMed:18762988}.
CC       Note=Disease susceptibility is associated with variations affecting the
CC       gene represented in this entry.
CC   -!- DISEASE: Fanconi anemia, complementation group S (FANCS) [MIM:617883]:
CC       A form of Fanconi anemia, a disorder affecting all bone marrow elements
CC       and resulting in anemia, leukopenia and thrombopenia. It is associated
CC       with cardiac, renal and limb malformations, dermal pigmentary changes,
CC       and a predisposition to the development of malignancies. At the
CC       cellular level it is associated with hypersensitivity to DNA-damaging
CC       agents, chromosomal instability (increased chromosome breakage) and
CC       defective DNA repair. {ECO:0000269|PubMed:23269703,
CC       ECO:0000269|PubMed:25472942, ECO:0000269|PubMed:29133208}. Note=Disease
CC       susceptibility is associated with variations affecting the gene
CC       represented in this entry.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative initiation at Met-
CC       18 of isoform 1. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 8]: The N-terminus is confirmed by several
CC       cDNAs. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB61673.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC       Sequence=AAI15038.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI15038.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/BRCA1ID163ch17q21.html";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/brca1/";
CC   -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC       polymorphism database;
CC       URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=BRCA1";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=BRCA1 entry;
CC       URL="https://en.wikipedia.org/wiki/BRCA1";
DR   EMBL; U14680; AAA73985.1; -; mRNA.
DR   EMBL; L78833; AAC37594.1; -; Genomic_DNA.
DR   EMBL; U64805; AAC00049.1; -; mRNA.
DR   EMBL; AF005068; AAB61673.1; ALT_SEQ; mRNA.
DR   EMBL; DQ190450; ABA29208.1; -; Genomic_DNA.
DR   EMBL; DQ190451; ABA29211.1; -; Genomic_DNA.
DR   EMBL; DQ190452; ABA29214.1; -; Genomic_DNA.
DR   EMBL; DQ190453; ABA29217.1; -; Genomic_DNA.
DR   EMBL; DQ190454; ABA29220.1; -; Genomic_DNA.
DR   EMBL; DQ190455; ABA29223.1; -; Genomic_DNA.
DR   EMBL; DQ190456; ABA29226.1; -; Genomic_DNA.
DR   EMBL; AY273801; AAP12647.1; -; Genomic_DNA.
DR   EMBL; AC060780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC135721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC072418; AAH72418.1; -; mRNA.
DR   EMBL; BC115037; AAI15038.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS11453.1; -. [P38398-1]
DR   CCDS; CCDS11454.2; -. [P38398-3]
DR   CCDS; CCDS11455.2; -. [P38398-6]
DR   CCDS; CCDS11456.2; -. [P38398-7]
DR   CCDS; CCDS11459.2; -. [P38398-8]
DR   PIR; A58881; A58881.
DR   RefSeq; NP_009225.1; NM_007294.3. [P38398-1]
DR   RefSeq; NP_009228.2; NM_007297.3. [P38398-8]
DR   RefSeq; NP_009229.2; NM_007298.3. [P38398-3]
DR   RefSeq; NP_009230.2; NM_007299.3. [P38398-6]
DR   RefSeq; NP_009231.2; NM_007300.3. [P38398-7]
DR   PDB; 1JM7; NMR; -; A=1-110.
DR   PDB; 1JNX; X-ray; 2.50 A; X=1646-1859.
DR   PDB; 1N5O; X-ray; 2.80 A; X=1646-1859.
DR   PDB; 1OQA; NMR; -; A=1755-1863.
DR   PDB; 1T15; X-ray; 1.85 A; A=1646-1859.
DR   PDB; 1T29; X-ray; 2.30 A; A=1646-1859.
DR   PDB; 1T2U; X-ray; 2.80 A; A=1646-1859.
DR   PDB; 1T2V; X-ray; 3.30 A; A/B/C/D/E=1646-1859.
DR   PDB; 1Y98; X-ray; 2.50 A; A=1646-1859.
DR   PDB; 2ING; X-ray; 3.60 A; X=1649-1859.
DR   PDB; 3COJ; X-ray; 3.21 A; A/B/C/D/E/F/G/X=1646-1859.
DR   PDB; 3K0H; X-ray; 2.70 A; A=1646-1859.
DR   PDB; 3K0K; X-ray; 2.70 A; A=1646-1859.
DR   PDB; 3K15; X-ray; 2.80 A; A=1646-1859.
DR   PDB; 3K16; X-ray; 3.00 A; A=1646-1859.
DR   PDB; 3PXA; X-ray; 2.55 A; A=1646-1859.
DR   PDB; 3PXB; X-ray; 2.50 A; A=1646-1859.
DR   PDB; 3PXC; X-ray; 2.80 A; X=1646-1859.
DR   PDB; 3PXD; X-ray; 2.80 A; A=1646-1859.
DR   PDB; 3PXE; X-ray; 2.85 A; A/B/C/D=1646-1859.
DR   PDB; 4IFI; X-ray; 2.20 A; A=1646-1859.
DR   PDB; 4IGK; X-ray; 1.75 A; A/B=1646-1859.
DR   PDB; 4JLU; X-ray; 3.50 A; A=1649-1859.
DR   PDB; 4OFB; X-ray; 3.05 A; A=1646-1859.
DR   PDB; 4U4A; X-ray; 3.51 A; A/B/C=1646-1859.
DR   PDB; 4Y18; X-ray; 3.50 A; A/B/C/D/E/F/G/H=1646-1859.
DR   PDB; 4Y2G; X-ray; 2.50 A; A=1646-1859.
DR   PDB; 6G2I; EM; 5.90 A; H/K/M/O/S/U/W/Y=1646-1859.
DR   PDBsum; 1JM7; -.
DR   PDBsum; 1JNX; -.
DR   PDBsum; 1N5O; -.
DR   PDBsum; 1OQA; -.
DR   PDBsum; 1T15; -.
DR   PDBsum; 1T29; -.
DR   PDBsum; 1T2U; -.
DR   PDBsum; 1T2V; -.
DR   PDBsum; 1Y98; -.
DR   PDBsum; 2ING; -.
DR   PDBsum; 3COJ; -.
DR   PDBsum; 3K0H; -.
DR   PDBsum; 3K0K; -.
DR   PDBsum; 3K15; -.
DR   PDBsum; 3K16; -.
DR   PDBsum; 3PXA; -.
DR   PDBsum; 3PXB; -.
DR   PDBsum; 3PXC; -.
DR   PDBsum; 3PXD; -.
DR   PDBsum; 3PXE; -.
DR   PDBsum; 4IFI; -.
DR   PDBsum; 4IGK; -.
DR   PDBsum; 4JLU; -.
DR   PDBsum; 4OFB; -.
DR   PDBsum; 4U4A; -.
DR   PDBsum; 4Y18; -.
DR   PDBsum; 4Y2G; -.
DR   PDBsum; 6G2I; -.
DR   SMR; P38398; -.
DR   BioGRID; 107140; 1128.
DR   ComplexPortal; CPX-715; BRCA1-BARD1 complex.
DR   ComplexPortal; CPX-955; BRCC ubiquitin ligase complex.
DR   CORUM; P38398; -.
DR   DIP; DIP-5971N; -.
DR   IntAct; P38398; 219.
DR   MINT; P38398; -.
DR   STRING; 9606.ENSP00000418960; -.
DR   BindingDB; P38398; -.
DR   ChEMBL; CHEMBL5990; -.
DR   GlyConnect; 2024; -.
DR   iPTMnet; P38398; -.
DR   PhosphoSitePlus; P38398; -.
DR   BioMuta; BRCA1; -.
DR   DMDM; 728984; -.
DR   CPTAC; CPTAC-2610; -.
DR   CPTAC; CPTAC-2611; -.
DR   CPTAC; CPTAC-3218; -.
DR   CPTAC; CPTAC-3219; -.
DR   CPTAC; CPTAC-916; -.
DR   EPD; P38398; -.
DR   jPOST; P38398; -.
DR   MassIVE; P38398; -.
DR   PaxDb; P38398; -.
DR   PeptideAtlas; P38398; -.
DR   PRIDE; P38398; -.
DR   ProteomicsDB; 20208; -.
DR   ProteomicsDB; 55287; -. [P38398-1]
DR   ProteomicsDB; 55288; -. [P38398-2]
DR   ProteomicsDB; 55289; -. [P38398-3]
DR   ProteomicsDB; 55290; -. [P38398-4]
DR   ProteomicsDB; 55291; -. [P38398-5]
DR   ProteomicsDB; 55292; -. [P38398-6]
DR   Antibodypedia; 4527; 2181 antibodies.
DR   DNASU; 672; -.
DR   Ensembl; ENST00000352993; ENSP00000312236; ENSG00000012048. [P38398-5]
DR   Ensembl; ENST00000357654; ENSP00000350283; ENSG00000012048. [P38398-1]
DR   Ensembl; ENST00000461221; ENSP00000418548; ENSG00000012048. [P38398-2]
DR   Ensembl; ENST00000461798; ENSP00000417988; ENSG00000012048. [P38398-2]
DR   Ensembl; ENST00000468300; ENSP00000417148; ENSG00000012048. [P38398-6]
DR   Ensembl; ENST00000471181; ENSP00000418960; ENSG00000012048. [P38398-7]
DR   Ensembl; ENST00000491747; ENSP00000420705; ENSG00000012048. [P38398-3]
DR   Ensembl; ENST00000493795; ENSP00000418775; ENSG00000012048. [P38398-8]
DR   GeneID; 672; -.
DR   KEGG; hsa:672; -.
DR   UCSC; uc002icq.4; human. [P38398-1]
DR   UCSC; uc010cyx.4; human.
DR   CTD; 672; -.
DR   DisGeNET; 672; -.
DR   EuPathDB; HostDB:ENSG00000012048.20; -.
DR   GeneCards; BRCA1; -.
DR   GeneReviews; BRCA1; -.
DR   HGNC; HGNC:1100; BRCA1.
DR   HPA; ENSG00000012048; Low tissue specificity.
DR   MalaCards; BRCA1; -.
DR   MIM; 113705; gene.
DR   MIM; 114480; phenotype.
DR   MIM; 167000; phenotype.
DR   MIM; 604370; phenotype.
DR   MIM; 614320; phenotype.
DR   MIM; 617883; phenotype.
DR   neXtProt; NX_P38398; -.
DR   OpenTargets; ENSG00000012048; -.
DR   Orphanet; 1333; Familial pancreatic carcinoma.
DR   Orphanet; 1331; Familial prostate cancer.
DR   Orphanet; 84; Fanconi anemia.
DR   Orphanet; 145; Hereditary breast and ovarian cancer syndrome.
DR   Orphanet; 227535; Hereditary breast cancer.
DR   Orphanet; 213524; Hereditary site-specific ovarian cancer syndrome.
DR   Orphanet; 168829; Primary peritoneal carcinoma.
DR   PharmGKB; PA25411; -.
DR   eggNOG; ENOG410ITQ4; Eukaryota.
DR   eggNOG; ENOG4112BIH; LUCA.
DR   GeneTree; ENSGT00440000034289; -.
DR   HOGENOM; CLU_002290_0_0_1; -.
DR   InParanoid; P38398; -.
DR   KO; K10605; -.
DR   OMA; DFEICCY; -.
DR   OrthoDB; 496760at2759; -.
DR   PhylomeDB; P38398; -.
DR   BRENDA; 6.3.2.19; 2681.
DR   Reactome; R-HSA-1221632; Meiotic synapsis.
DR   Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
DR   Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR   Reactome; R-HSA-5689901; Metalloprotease DUBs.
DR   Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
DR   Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR   Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
DR   Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
DR   Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR   Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR   Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR   Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR   Reactome; R-HSA-912446; Meiotic recombination.
DR   SignaLink; P38398; -.
DR   SIGNOR; P38398; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 672; 341 hits in 792 CRISPR screens.
DR   ChiTaRS; BRCA1; human.
DR   EvolutionaryTrace; P38398; -.
DR   GeneWiki; BRCA1; -.
DR   GenomeRNAi; 672; -.
DR   Pharos; P38398; Tchem.
DR   PRO; PR:P38398; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P38398; protein.
DR   Bgee; ENSG00000012048; Expressed in lung and 178 other tissues.
DR   ExpressionAtlas; P38398; baseline and differential.
DR   Genevisible; P38398; HS.
DR   GO; GO:0070531; C:BRCA1-A complex; IDA:UniProtKB.
DR   GO; GO:0031436; C:BRCA1-BARD1 complex; IDA:UniProtKB.
DR   GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0008274; C:gamma-tubulin ring complex; NAS:UniProtKB.
DR   GO; GO:0000800; C:lateral element; IDA:MGI.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR   GO; GO:0000151; C:ubiquitin ligase complex; NAS:UniProtKB.
DR   GO; GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0003723; F:RNA binding; IDA:MGI.
DR   GO; GO:0070063; F:RNA polymerase binding; IDA:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
DR   GO; GO:0015631; F:tubulin binding; NAS:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; TAS:ProtInc.
DR   GO; GO:0071681; P:cellular response to indole-3-methanol; IDA:UniProtKB.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:BHF-UCL.
DR   GO; GO:0007098; P:centrosome cycle; IEA:Ensembl.
DR   GO; GO:0043009; P:chordate embryonic development; IBA:GO_Central.
DR   GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR   GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; TAS:UniProtKB.
DR   GO; GO:0000729; P:DNA double-strand break processing; TAS:Reactome.
DR   GO; GO:0006260; P:DNA replication; TAS:Reactome.
DR   GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IBA:GO_Central.
DR   GO; GO:0006302; P:double-strand break repair; IDA:CACAO.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:HGNC-UCL.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:MGI.
DR   GO; GO:0044818; P:mitotic G2/M transition checkpoint; IEA:Ensembl.
DR   GO; GO:0046600; P:negative regulation of centriole replication; NAS:UniProtKB.
DR   GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:BHF-UCL.
DR   GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0070317; P:negative regulation of G0 to G1 transition; TAS:Reactome.
DR   GO; GO:0035067; P:negative regulation of histone acetylation; IBA:GO_Central.
DR   GO; GO:0051572; P:negative regulation of histone H3-K4 methylation; IEA:Ensembl.
DR   GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IDA:BHF-UCL.
DR   GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; IMP:CACAO.
DR   GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR   GO; GO:0071158; P:positive regulation of cell cycle arrest; IDA:BHF-UCL.
DR   GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR   GO; GO:0035066; P:positive regulation of histone acetylation; IDA:BHF-UCL.
DR   GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IDA:BHF-UCL.
DR   GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; IDA:BHF-UCL.
DR   GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; IEA:Ensembl.
DR   GO; GO:2000620; P:positive regulation of histone H4-K16 acetylation; IDA:BHF-UCL.
DR   GO; GO:0070512; P:positive regulation of histone H4-K20 methylation; IDA:BHF-UCL.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:BHF-UCL.
DR   GO; GO:0006301; P:postreplication repair; IDA:HGNC-UCL.
DR   GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR   GO; GO:0085020; P:protein K6-linked ubiquitination; IDA:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:HGNC-UCL.
DR   GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell population proliferation; TAS:UniProtKB.
DR   GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
DR   GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IEA:Ensembl.
DR   GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0006359; P:regulation of transcription by RNA polymerase III; TAS:UniProtKB.
DR   GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
DR   GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
DR   GO; GO:0072425; P:signal transduction involved in G2 DNA damage checkpoint; IMP:UniProtKB.
DR   DisProt; DP00238; -.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.50.10190; -; 2.
DR   IDEAL; IID00042; -.
DR   InterPro; IPR011364; BRCA1.
DR   InterPro; IPR031099; BRCA1-associated.
DR   InterPro; IPR025994; BRCA1_serine_dom.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR13763; PTHR13763; 1.
DR   PANTHER; PTHR13763:SF0; PTHR13763:SF0; 1.
DR   Pfam; PF00533; BRCT; 2.
DR   Pfam; PF12820; BRCT_assoc; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   PIRSF; PIRSF001734; BRCA1; 1.
DR   PRINTS; PR00493; BRSTCANCERI.
DR   SMART; SM00292; BRCT; 2.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52113; SSF52113; 2.
DR   PROSITE; PS50172; BRCT; 2.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Alternative initiation;
KW   Alternative splicing; Cell cycle; Chromosome; Cytoplasm;
KW   Direct protein sequencing; Disease mutation; DNA damage; DNA recombination;
KW   DNA repair; DNA-binding; Fanconi anemia; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Isopeptide bond; Lipid biosynthesis;
KW   Lipid metabolism; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Transferase; Tumor suppressor; Ubl conjugation; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..1863
FT                   /note="Breast cancer type 1 susceptibility protein"
FT                   /id="PRO_0000055830"
FT   DOMAIN          1642..1736
FT                   /note="BRCT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   DOMAIN          1756..1855
FT                   /note="BRCT 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   ZN_FING         24..65
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1397..1424
FT                   /note="Interaction with PALB2"
FT                   /evidence="ECO:0000269|PubMed:19369211"
FT   COMPBIAS        651..654
FT                   /note="Poly-Lys"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000244|PubMed:22814378"
FT   MOD_RES         114
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163"
FT   MOD_RES         308
FT                   /note="Phosphoserine; by AURKA"
FT                   /evidence="ECO:0000269|PubMed:14990569"
FT   MOD_RES         395
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332"
FT   MOD_RES         398
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332"
FT   MOD_RES         423
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         551
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         694
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         708
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         725
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48754"
FT   MOD_RES         753
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         840
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48754"
FT   MOD_RES         988
FT                   /note="Phosphoserine; by CHEK2"
FT                   /evidence="ECO:0000269|PubMed:10724175,
FT                   ECO:0000269|PubMed:20364141"
FT   MOD_RES         1009
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         1143
FT                   /note="Phosphoserine; by ATR; in vitro"
FT                   /evidence="ECO:0000269|PubMed:11114888"
FT   MOD_RES         1189
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         1191
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         1211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         1217
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         1218
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:21406692"
FT   MOD_RES         1280
FT                   /note="Phosphoserine; by ATR; in vitro"
FT                   /evidence="ECO:0000269|PubMed:11114888"
FT   MOD_RES         1328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         1336
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:17081983,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692"
FT   MOD_RES         1342
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:21406692"
FT   MOD_RES         1387
FT                   /note="Phosphoserine; by ATM and ATR"
FT                   /evidence="ECO:0000269|PubMed:11114888"
FT   MOD_RES         1394
FT                   /note="Phosphothreonine; by ATR; in vitro"
FT                   /evidence="ECO:0000269|PubMed:11114888"
FT   MOD_RES         1423
FT                   /note="Phosphoserine; by ATM and ATR"
FT                   /evidence="ECO:0000269|PubMed:11114888"
FT   MOD_RES         1457
FT                   /note="Phosphoserine; by ATR; in vitro"
FT                   /evidence="ECO:0000269|PubMed:11114888"
FT   MOD_RES         1524
FT                   /note="Phosphoserine; by ATM"
FT                   /evidence="ECO:0000269|PubMed:21144835"
FT   MOD_RES         1542
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   CROSSLNK        109
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   CROSSLNK        301
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   CROSSLNK        339
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:25218447,
FT                   ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:28112733"
FT   CROSSLNK        443
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:25755297,
FT                   ECO:0000244|PubMed:28112733"
FT   CROSSLNK        459
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:25218447,
FT                   ECO:0000244|PubMed:28112733"
FT   CROSSLNK        519
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   CROSSLNK        583
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:25218447,
FT                   ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:28112733"
FT   CROSSLNK        654
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:25218447"
FT   CROSSLNK        734
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:25218447"
FT   CROSSLNK        739
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:25218447"
FT   CROSSLNK        918
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   CROSSLNK        987
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   CROSSLNK        1079
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   VAR_SEQ         1..47
FT                   /note="Missing (in isoform 8)"
FT                   /id="VSP_057569"
FT   VAR_SEQ         1..17
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_035396"
FT   VAR_SEQ         64..1863
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_047891"
FT   VAR_SEQ         224..1365
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_035398"
FT   VAR_SEQ         264..1366
FT                   /note="Missing (in isoform 3 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9010228"
FT                   /id="VSP_035399"
FT   VAR_SEQ         1453
FT                   /note="Missing (in isoform 3 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9010228"
FT                   /id="VSP_043797"
FT   VAR_SEQ         1453
FT                   /note="A -> DSHIHGQRNNSMFSKRPREHIS (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055404"
FT   VAR_SEQ         1778..1863
FT                   /note="DQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTEDNGFHAIGQMCE
FT                   APVVTREWVLDSVALYQCQELDTYLIPQIPHSHY -> GCPPNCGCAARCLDRGQWLPC
FT                   NWADV (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043798"
FT   VARIANT         4
FT                   /note="S -> F (in BC; unknown pathological significance;
FT                   dbSNP:rs786203152)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070458"
FT   VARIANT         10
FT                   /note="E -> K (in BC and BROVCA1)"
FT                   /evidence="ECO:0000269|PubMed:14722926"
FT                   /id="VAR_020679"
FT   VARIANT         11
FT                   /note="V -> A (found in breast-ovarian cancer patients;
FT                   unknown pathological significance; dbSNP:rs80357017)"
FT                   /id="VAR_007754"
FT   VARIANT         18
FT                   /note="M -> T (in BC; unknown pathological significance;
FT                   dbSNP:rs80356929)"
FT                   /evidence="ECO:0000269|PubMed:17924331,
FT                   ECO:0000269|PubMed:23867111"
FT                   /id="VAR_063899"
FT   VARIANT         21
FT                   /note="I -> V (found in breast-ovarian cancer patients;
FT                   unknown pathological significance; dbSNP:rs80357406)"
FT                   /id="VAR_007755"
FT   VARIANT         22
FT                   /note="L -> S (in BC; dbSNP:rs80357438)"
FT                   /evidence="ECO:0000269|PubMed:9609997"
FT                   /id="VAR_007756"
FT   VARIANT         23
FT                   /note="E -> K (in BC and BROVCA1)"
FT                   /evidence="ECO:0000269|PubMed:14722926"
FT                   /id="VAR_020680"
FT   VARIANT         30
FT                   /note="L -> F (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035947"
FT   VARIANT         45
FT                   /note="K -> Q (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs769650474)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070459"
FT   VARIANT         61
FT                   /note="C -> G (in BC and ovarian cancer; no interaction
FT                   with BAP1; dbSNP:rs28897672)"
FT                   /evidence="ECO:0000269|PubMed:12938098,
FT                   ECO:0000269|PubMed:14746861, ECO:0000269|PubMed:23867111,
FT                   ECO:0000269|PubMed:7894493, ECO:0000269|PubMed:8554067,
FT                   ECO:0000269|PubMed:9528852, ECO:0000269|PubMed:9760198"
FT                   /id="VAR_007757"
FT   VARIANT         64
FT                   /note="C -> G (in BC; no interaction with BAP1;
FT                   dbSNP:rs80357064)"
FT                   /evidence="ECO:0000269|PubMed:23867111,
FT                   ECO:0000269|PubMed:7894491, ECO:0000269|PubMed:9482581,
FT                   ECO:0000269|PubMed:9528852"
FT                   /id="VAR_007758"
FT   VARIANT         64
FT                   /note="C -> Y (in dbSNP:rs55851803)"
FT                   /id="VAR_007759"
FT   VARIANT         67
FT                   /note="D -> Y (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs80357102)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070460"
FT   VARIANT         71
FT                   /note="R -> K (in BC; unknown pathological significance;
FT                   dbSNP:rs80356913)"
FT                   /evidence="ECO:0000269|PubMed:12938098"
FT                   /id="VAR_020681"
FT   VARIANT         105
FT                   /note="Y -> C (in dbSNP:rs28897673)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070461"
FT   VARIANT         132
FT                   /note="N -> K (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs80357413)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070462"
FT   VARIANT         142
FT                   /note="P -> H (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs55971303)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070463"
FT   VARIANT         147
FT                   /note="L -> F (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs748876625)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070464"
FT   VARIANT         153
FT                   /note="S -> R (in dbSNP:rs28897674)"
FT                   /id="VAR_052077"
FT   VARIANT         165
FT                   /note="L -> P (in BC; unknown pathological significance;
FT                   functionally neutral in vitro)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070465"
FT   VARIANT         170
FT                   /note="R -> W (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs80357325)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070466"
FT   VARIANT         186
FT                   /note="S -> Y (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs55688530)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070467"
FT   VARIANT         191
FT                   /note="V -> I (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs80357090)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070468"
FT   VARIANT         227
FT                   /note="E -> K (in ovarian cancer; unknown pathological
FT                   significance)"
FT                   /id="VAR_008759"
FT   VARIANT         231
FT                   /note="T -> M (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs80357001)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070469"
FT   VARIANT         239
FT                   /note="H -> R (in dbSNP:rs80357396)"
FT                   /evidence="ECO:0000269|PubMed:9010228,
FT                   ECO:0000269|PubMed:9760198"
FT                   /id="VAR_007760"
FT   VARIANT         245
FT                   /note="D -> V (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs80356865)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070470"
FT   VARIANT         246
FT                   /note="L -> V (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs28897675)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070471"
FT   VARIANT         271
FT                   /note="V -> L (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs80357244)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070472"
FT   VARIANT         271
FT                   /note="V -> M (in BC; dbSNP:rs80357244)"
FT                   /evidence="ECO:0000269|PubMed:8723683"
FT                   /id="VAR_007761"
FT   VARIANT         275
FT                   /note="G -> S (in dbSNP:rs8176153)"
FT                   /evidence="ECO:0000269|Ref.6"
FT                   /id="VAR_019944"
FT   VARIANT         346
FT                   /note="P -> S (in BC; unknown pathological significance;
FT                   dbSNP:rs80357015)"
FT                   /evidence="ECO:0000269|PubMed:10323242"
FT                   /id="VAR_008760"
FT   VARIANT         356
FT                   /note="Q -> R (in dbSNP:rs1799950)"
FT                   /evidence="ECO:0000269|PubMed:7894493, ECO:0000269|Ref.5,
FT                   ECO:0000269|Ref.6"
FT                   /id="VAR_007762"
FT   VARIANT         369
FT                   /note="Missing (in BC)"
FT                   /id="VAR_007763"
FT   VARIANT         379
FT                   /note="I -> M (in dbSNP:rs56128296)"
FT                   /id="VAR_007764"
FT   VARIANT         461
FT                   /note="F -> L (in BC; dbSNP:rs56046357)"
FT                   /evidence="ECO:0000269|PubMed:9609997"
FT                   /id="VAR_007765"
FT   VARIANT         465
FT                   /note="Y -> D (in BC; dbSNP:rs397508869)"
FT                   /evidence="ECO:0000269|PubMed:9609997"
FT                   /id="VAR_007766"
FT   VARIANT         507
FT                   /note="R -> I (found in breast-ovarian cancer patients;
FT                   unknown pathological significance; dbSNP:rs80357224)"
FT                   /id="VAR_007767"
FT   VARIANT         552
FT                   /note="G -> V (in BC; dbSNP:rs397508893)"
FT                   /evidence="ECO:0000269|PubMed:9609997"
FT                   /id="VAR_007768"
FT   VARIANT         656
FT                   /note="N -> I"
FT                   /evidence="ECO:0000269|PubMed:12442274"
FT                   /id="VAR_020682"
FT   VARIANT         668
FT                   /note="L -> F (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs80357250)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070473"
FT   VARIANT         693
FT                   /note="D -> N (in dbSNP:rs4986850)"
FT                   /evidence="ECO:0000269|PubMed:15026808, ECO:0000269|Ref.6"
FT                   /id="VAR_007769"
FT   VARIANT         695
FT                   /note="D -> N (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs28897681)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070474"
FT   VARIANT         723
FT                   /note="N -> D (in dbSNP:rs4986845)"
FT                   /id="VAR_020110"
FT   VARIANT         749
FT                   /note="D -> Y (in BC; dbSNP:rs80357114)"
FT                   /evidence="ECO:0000269|PubMed:12442275"
FT                   /id="VAR_020683"
FT   VARIANT         758
FT                   /note="L -> F (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035948"
FT   VARIANT         772
FT                   /note="V -> A (in dbSNP:rs80357467)"
FT                   /evidence="ECO:0000269|PubMed:7894491,
FT                   ECO:0000269|PubMed:9482581"
FT                   /id="VAR_007770"
FT   VARIANT         778
FT                   /note="G -> C (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035949"
FT   VARIANT         798
FT                   /note="P -> L (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs876660005)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070475"
FT   VARIANT         810
FT                   /note="N -> Y (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs28897682)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070476"
FT   VARIANT         820
FT                   /note="K -> E (in dbSNP:rs56082113)"
FT                   /evidence="ECO:0000269|PubMed:9482581"
FT                   /id="VAR_007771"
FT   VARIANT         826
FT                   /note="T -> K (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs28897683)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_007772"
FT   VARIANT         835
FT                   /note="H -> Y (in BROVCA1; unknown pathological
FT                   significance; dbSNP:rs751656678)"
FT                   /evidence="ECO:0000269|PubMed:12938098"
FT                   /id="VAR_020684"
FT   VARIANT         841
FT                   /note="R -> Q (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs80357337)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070477"
FT   VARIANT         841
FT                   /note="R -> W (in BROVCA1; unknown pathological
FT                   significance; dbSNP:rs1800709)"
FT                   /evidence="ECO:0000269|PubMed:8968716,
FT                   ECO:0000269|PubMed:9760198"
FT                   /id="VAR_007773"
FT   VARIANT         856
FT                   /note="Y -> H (in a patient with sporadic breast cancer;
FT                   unknown pathological significance; dbSNP:rs80356892)"
FT                   /evidence="ECO:0000269|PubMed:15365993,
FT                   ECO:0000269|PubMed:23867111"
FT                   /id="VAR_020685"
FT   VARIANT         866
FT                   /note="R -> C (in dbSNP:rs41286300)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070478"
FT   VARIANT         866
FT                   /note="R -> Q (in BC; unknown pathological significance)"
FT                   /evidence="ECO:0000269|PubMed:12938098"
FT                   /id="VAR_020686"
FT   VARIANT         871
FT                   /note="P -> L (in dbSNP:rs799917)"
FT                   /evidence="ECO:0000269|PubMed:10323242,
FT                   ECO:0000269|PubMed:12442274, ECO:0000269|PubMed:15365993,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|Ref.6"
FT                   /id="VAR_007774"
FT   VARIANT         888
FT                   /note="H -> Y (in BC; unknown pathological significance;
FT                   dbSNP:rs80357480)"
FT                   /evidence="ECO:0000269|PubMed:12938098"
FT                   /id="VAR_020687"
FT   VARIANT         892
FT                   /note="L -> S (in BC; dbSNP:rs397508994)"
FT                   /evidence="ECO:0000269|PubMed:9609997"
FT                   /id="VAR_007775"
FT   VARIANT         903..1863
FT                   /note="Missing (in FANCS)"
FT                   /evidence="ECO:0000269|PubMed:29133208"
FT                   /id="VAR_080693"
FT   VARIANT         925
FT                   /note="I -> L (in dbSNP:rs4986847)"
FT                   /id="VAR_021913"
FT   VARIANT         960
FT                   /note="G -> D (in BC; dbSNP:rs397509022)"
FT                   /evidence="ECO:0000269|PubMed:9609997"
FT                   /id="VAR_007776"
FT   VARIANT         989
FT                   /note="F -> S (in dbSNP:rs4986848)"
FT                   /id="VAR_020111"
FT   VARIANT         1008
FT                   /note="M -> I (in dbSNP:rs1800704)"
FT                   /id="VAR_007777"
FT   VARIANT         1025
FT                   /note="T -> I (in BC; dbSNP:rs397509034)"
FT                   /evidence="ECO:0000269|PubMed:9609997"
FT                   /id="VAR_007778"
FT   VARIANT         1038
FT                   /note="E -> G (in dbSNP:rs16941)"
FT                   /evidence="ECO:0000269|PubMed:10323242,
FT                   ECO:0000269|PubMed:15365993, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:7894493, ECO:0000269|Ref.6"
FT                   /id="VAR_007779"
FT   VARIANT         1040
FT                   /note="S -> N (in dbSNP:rs4986852)"
FT                   /evidence="ECO:0000269|PubMed:15026808,
FT                   ECO:0000269|PubMed:7894491, ECO:0000269|PubMed:7894493,
FT                   ECO:0000269|PubMed:9482581, ECO:0000269|Ref.6"
FT                   /id="VAR_007780"
FT   VARIANT         1047
FT                   /note="V -> A (in BC; dbSNP:rs397509037)"
FT                   /evidence="ECO:0000269|PubMed:9609997"
FT                   /id="VAR_007781"
FT   VARIANT         1060
FT                   /note="E -> A (in dbSNP:rs80357184)"
FT                   /evidence="ECO:0000269|PubMed:15026808,
FT                   ECO:0000269|PubMed:23867111"
FT                   /id="VAR_020688"
FT   VARIANT         1101
FT                   /note="S -> N (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs41293447)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070479"
FT   VARIANT         1139
FT                   /note="S -> I (in BC; unknown pathological significance;
FT                   dbSNP:rs80357228)"
FT                   /evidence="ECO:0000269|PubMed:12938098"
FT                   /id="VAR_020689"
FT   VARIANT         1140
FT                   /note="S -> G (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs2227945)"
FT                   /evidence="ECO:0000269|PubMed:23867111, ECO:0000269|Ref.6"
FT                   /id="VAR_019945"
FT   VARIANT         1140
FT                   /note="S -> N (in BC; unknown pathological significance;
FT                   functionally neutral in vitro)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070480"
FT   VARIANT         1150
FT                   /note="P -> S (in BC; dbSNP:rs80357272)"
FT                   /evidence="ECO:0000269|PubMed:8723683"
FT                   /id="VAR_007782"
FT   VARIANT         1183
FT                   /note="K -> R (in dbSNP:rs16942)"
FT                   /evidence="ECO:0000269|PubMed:10323242,
FT                   ECO:0000269|PubMed:14722926, ECO:0000269|PubMed:15365993,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7894493,
FT                   ECO:0000269|Ref.6"
FT                   /id="VAR_007783"
FT   VARIANT         1187
FT                   /note="S -> I (in BC and BROVCA1)"
FT                   /evidence="ECO:0000269|PubMed:14722926"
FT                   /id="VAR_020690"
FT   VARIANT         1200
FT                   /note="Q -> H (in BC and BROVCA1; dbSNP:rs56214134)"
FT                   /evidence="ECO:0000269|PubMed:14722926"
FT                   /id="VAR_020691"
FT   VARIANT         1204
FT                   /note="R -> I (in BC)"
FT                   /evidence="ECO:0000269|PubMed:14722926"
FT                   /id="VAR_020692"
FT   VARIANT         1207
FT                   /note="K -> N (in BC)"
FT                   /evidence="ECO:0000269|PubMed:14722926"
FT                   /id="VAR_020693"
FT   VARIANT         1210
FT                   /note="E -> G (in BC; unknown pathological significance;
FT                   dbSNP:rs1060502347)"
FT                   /evidence="ECO:0000269|PubMed:12938098"
FT                   /id="VAR_020694"
FT   VARIANT         1214
FT                   /note="E -> K (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs80356923)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070481"
FT   VARIANT         1217
FT                   /note="S -> Y (in BC and BROVCA1)"
FT                   /evidence="ECO:0000269|PubMed:14722926"
FT                   /id="VAR_020695"
FT   VARIANT         1219
FT                   /note="E -> D (found in breast-ovarian cancer patients;
FT                   unknown pathological significance; dbSNP:rs80356876)"
FT                   /id="VAR_007784"
FT   VARIANT         1226
FT                   /note="F -> L (in BROVCA1)"
FT                   /evidence="ECO:0000269|PubMed:14722926"
FT                   /id="VAR_020696"
FT   VARIANT         1236
FT                   /note="N -> K (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs28897687)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_052078"
FT   VARIANT         1243
FT                   /note="R -> G (in BROVCA1)"
FT                   /evidence="ECO:0000269|PubMed:14722926"
FT                   /id="VAR_020697"
FT   VARIANT         1250
FT                   /note="E -> K (in dbSNP:rs28897686)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_052079"
FT   VARIANT         1267
FT                   /note="L -> S (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs587782190)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070482"
FT   VARIANT         1282
FT                   /note="E -> V (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs80357217)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070483"
FT   VARIANT         1297
FT                   /note="S -> P (in BC; unknown pathological significance;
FT                   dbSNP:rs1450793674)"
FT                   /evidence="ECO:0000269|PubMed:12938098"
FT                   /id="VAR_020698"
FT   VARIANT         1297
FT                   /note="Missing (in BC; unknown pathological significance;
FT                   functionally neutral in vitro)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070484"
FT   VARIANT         1301
FT                   /note="S -> R (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs273900719)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070485"
FT   VARIANT         1346
FT                   /note="E -> K (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs80357407)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070486"
FT   VARIANT         1347
FT                   /note="R -> G (in dbSNP:rs28897689)"
FT                   /evidence="ECO:0000269|PubMed:12215251"
FT                   /id="VAR_007785"
FT   VARIANT         1378
FT                   /note="V -> I (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs28897690)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070487"
FT   VARIANT         1400
FT                   /note="M -> V (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs80357306)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070488"
FT   VARIANT         1406
FT                   /note="K -> N (in dbSNP:rs1800707)"
FT                   /id="VAR_008761"
FT   VARIANT         1407
FT                   /note="L -> P (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs80357492)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070489"
FT   VARIANT         1411
FT                   /note="M -> T (in BC and ovarian cancer; unknown
FT                   pathological significance; decreased interaction with
FT                   PALB2; dbSNP:rs273900729)"
FT                   /evidence="ECO:0000269|PubMed:14746861,
FT                   ECO:0000269|PubMed:19369211, ECO:0000269|PubMed:23867111"
FT                   /id="VAR_020699"
FT   VARIANT         1431
FT                   /note="S -> P"
FT                   /id="VAR_007786"
FT   VARIANT         1443
FT                   /note="R -> G (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs41293455)"
FT                   /evidence="ECO:0000269|PubMed:23867111,
FT                   ECO:0000269|PubMed:7894491, ECO:0000269|PubMed:9482581"
FT                   /id="VAR_007787"
FT   VARIANT         1443
FT                   /note="R -> Q (in dbSNP:rs4986849)"
FT                   /id="VAR_020112"
FT   VARIANT         1448
FT                   /note="S -> G (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs80357486)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070490"
FT   VARIANT         1486
FT                   /note="S -> C (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs397507232)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070491"
FT   VARIANT         1495
FT                   /note="R -> M (in BC; unknown pathological significance;
FT                   dbSNP:rs80357389)"
FT                   /evidence="ECO:0000269|PubMed:17924331"
FT                   /id="VAR_063900"
FT   VARIANT         1512
FT                   /note="S -> I (in dbSNP:rs1800744)"
FT                   /evidence="ECO:0000269|PubMed:12215251,
FT                   ECO:0000269|PubMed:9482581, ECO:0000269|PubMed:9760198"
FT                   /id="VAR_007788"
FT   VARIANT         1534
FT                   /note="V -> M (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs55815649)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070492"
FT   VARIANT         1561
FT                   /note="T -> I (found in breast cancer; unknown pathological
FT                   significance; dbSNP:rs56158747)"
FT                   /id="VAR_007789"
FT   VARIANT         1589
FT                   /note="R -> P (in BC; unknown pathological significance;
FT                   functionally neutral in vitro)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070493"
FT   VARIANT         1606
FT                   /note="K -> E (found in breast cancer; unknown pathological
FT                   significance; dbSNP:rs80356943)"
FT                   /id="VAR_007790"
FT   VARIANT         1613
FT                   /note="S -> G (in dbSNP:rs1799966)"
FT                   /evidence="ECO:0000269|PubMed:10323242,
FT                   ECO:0000269|PubMed:12442274, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:7894493, ECO:0000269|PubMed:9010228,
FT                   ECO:0000269|Ref.6"
FT                   /id="VAR_007791"
FT   VARIANT         1620
FT                   /note="T -> A (in dbSNP:rs8176219)"
FT                   /evidence="ECO:0000269|Ref.6"
FT                   /id="VAR_019946"
FT   VARIANT         1623
FT                   /note="A -> G (could be associated with cancer
FT                   susceptibility; major splicing aberration identified with
FT                   this mutant; dbSNP:rs80356862)"
FT                   /evidence="ECO:0000269|PubMed:17924331,
FT                   ECO:0000269|PubMed:20513136"
FT                   /id="VAR_063901"
FT   VARIANT         1628
FT                   /note="M -> T (in some patients with sporadic breast
FT                   cancer; unknown pathological significance;
FT                   dbSNP:rs4986854)"
FT                   /evidence="ECO:0000269|PubMed:15365993,
FT                   ECO:0000269|PubMed:23867111"
FT                   /id="VAR_007793"
FT   VARIANT         1628
FT                   /note="M -> V (found in breast and ovarian cancer patients;
FT                   unknown pathological significance; dbSNP:rs80357465)"
FT                   /id="VAR_007792"
FT   VARIANT         1637
FT                   /note="P -> L (in dbSNP:rs80357048)"
FT                   /evidence="ECO:0000269|PubMed:7939630,
FT                   ECO:0000269|PubMed:9482581"
FT                   /id="VAR_007794"
FT   VARIANT         1641
FT                   /note="A -> P (in ovarian cancer; unknown pathological
FT                   significance; dbSNP:rs1800726)"
FT                   /id="VAR_008762"
FT   VARIANT         1651
FT                   /note="S -> F (in BC; unknown pathological significance;
FT                   dbSNP:rs80356938)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070494"
FT   VARIANT         1651
FT                   /note="S -> P (in BC; unknown pathological significance;
FT                   dbSNP:rs879254042)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070495"
FT   VARIANT         1652
FT                   /note="M -> I (in dbSNP:rs1799967)"
FT                   /evidence="ECO:0000269|PubMed:12215251,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:23867111,
FT                   ECO:0000269|PubMed:9482581"
FT                   /id="VAR_007795"
FT   VARIANT         1655
FT                   /note="S -> F (in BC; unknown pathological significance;
FT                   functionally impaired in vitro; dbSNP:rs80357390)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070496"
FT   VARIANT         1662
FT                   /note="F -> C (in dbSNP:rs28897695)"
FT                   /id="VAR_052080"
FT   VARIANT         1665
FT                   /note="V -> M (in dbSNP:rs80357169)"
FT                   /evidence="ECO:0000269|PubMed:15026808"
FT                   /id="VAR_020700"
FT   VARIANT         1685
FT                   /note="T -> A (in BC; unknown pathological significance;
FT                   dbSNP:rs80356890)"
FT                   /evidence="ECO:0000269|PubMed:17924331"
FT                   /id="VAR_063902"
FT   VARIANT         1685
FT                   /note="T -> I (could be associated with cancer
FT                   susceptibility; multifactorial likelihood analysis provides
FT                   evidence for pathogenicity; dbSNP:rs80357043)"
FT                   /evidence="ECO:0000269|PubMed:17924331,
FT                   ECO:0000269|PubMed:20513136"
FT                   /id="VAR_063903"
FT   VARIANT         1686
FT                   /note="H -> Q (in BC; unknown pathological significance;
FT                   functionally impaired in vitro; dbSNP:rs397509218)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070497"
FT   VARIANT         1686
FT                   /note="H -> R (in BC; unknown pathological significance;
FT                   functionally impaired in vitro; dbSNP:rs730882166)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070498"
FT   VARIANT         1688
FT                   /note="Missing (in BC; unknown pathological significance;
FT                   functionally impaired in vitro)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070499"
FT   VARIANT         1689
FT                   /note="M -> R (in BC; unknown pathological significance;
FT                   dbSNP:rs80357061)"
FT                   /evidence="ECO:0000269|PubMed:17924331"
FT                   /id="VAR_063904"
FT   VARIANT         1690
FT                   /note="K -> Q (in some patients with sporadic breast
FT                   cancer; unknown pathological significance;
FT                   dbSNP:rs397507239)"
FT                   /evidence="ECO:0000269|PubMed:15365993"
FT                   /id="VAR_020701"
FT   VARIANT         1691
FT                   /note="T -> I (in BC; unknown pathological significance;
FT                   functionally impaired in vitro; dbSNP:rs80357034)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070500"
FT   VARIANT         1692
FT                   /note="D -> N (in ovarian cancer; unknown pathological
FT                   significance; dbSNP:rs80187739)"
FT                   /id="VAR_008763"
FT   VARIANT         1697
FT                   /note="C -> R (in ovarian cancer; dbSNP:rs80356993)"
FT                   /evidence="ECO:0000269|PubMed:14746861"
FT                   /id="VAR_020702"
FT   VARIANT         1699
FT                   /note="R -> Q (in BC; unknown pathological significance;
FT                   strongly reduces affinity for a BRIP1 phosphopeptide;
FT                   functionally impaired in vitro; dbSNP:rs41293459)"
FT                   /evidence="ECO:0000269|PubMed:21473589,
FT                   ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070501"
FT   VARIANT         1699
FT                   /note="R -> W (in BC, ovarian cancer and FANCS; impairs
FT                   protein stability; functionally impaired in vitro;
FT                   dbSNP:rs55770810)"
FT                   /evidence="ECO:0000269|PubMed:14746861,
FT                   ECO:0000269|PubMed:17924331, ECO:0000269|PubMed:21473589,
FT                   ECO:0000269|PubMed:23867111, ECO:0000269|PubMed:25472942"
FT                   /id="VAR_075666"
FT   VARIANT         1706
FT                   /note="G -> A (in BC; unknown pathological significance;
FT                   dbSNP:rs80356860)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070502"
FT   VARIANT         1706
FT                   /note="G -> E (in BC; unknown pathological significance;
FT                   dbSNP:rs80356860)"
FT                   /evidence="ECO:0000269|PubMed:17924331,
FT                   ECO:0000269|PubMed:23867111"
FT                   /id="VAR_063905"
FT   VARIANT         1708
FT                   /note="A -> E (in BC; abolishes ACACA binding;
FT                   dbSNP:rs28897696)"
FT                   /evidence="ECO:0000269|PubMed:17924331,
FT                   ECO:0000269|PubMed:23867111, ECO:0000269|PubMed:7939630"
FT                   /id="VAR_007796"
FT   VARIANT         1713
FT                   /note="V -> G"
FT                   /evidence="ECO:0000269|PubMed:15365993"
FT                   /id="VAR_007797"
FT   VARIANT         1715
FT                   /note="S -> R (in BC; unknown pathological significance;
FT                   dbSNP:rs80357094)"
FT                   /evidence="ECO:0000269|PubMed:17924331"
FT                   /id="VAR_063906"
FT   VARIANT         1718
FT                   /note="W -> C (in BC; unknown pathological significance;
FT                   functionally impaired in vitro; dbSNP:rs80357239)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070503"
FT   VARIANT         1720
FT                   /note="T -> A (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; no effect on in vitro
FT                   phosphorylation by ATR; dbSNP:rs56195342)"
FT                   /evidence="ECO:0000269|PubMed:11114888,
FT                   ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070504"
FT   VARIANT         1735
FT                   /note="E -> K (in BC; unknown pathological significance;
FT                   dbSNP:rs397509238)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070505"
FT   VARIANT         1736
FT                   /note="V -> A (in BC and FANCS; unknown pathological
FT                   significance; Decreased localization to DNA damage sites
FT                   and reduced interaction with UIMC1/RAP80;
FT                   dbSNP:rs45553935)"
FT                   /evidence="ECO:0000269|PubMed:23269703,
FT                   ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070506"
FT   VARIANT         1738
FT                   /note="G -> R (in BC; unknown pathological significance;
FT                   dbSNP:rs80356937)"
FT                   /evidence="ECO:0000269|PubMed:17924331"
FT                   /id="VAR_063907"
FT   VARIANT         1739
FT                   /note="D -> G (in BC; unknown pathological significance;
FT                   functionally impaired in vitro; dbSNP:rs80357227)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070507"
FT   VARIANT         1739
FT                   /note="D -> V (in BC; unknown pathological significance;
FT                   functionally impaired in vitro; dbSNP:rs80357227)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070508"
FT   VARIANT         1746
FT                   /note="H -> Q (in BC; unknown pathological significance;
FT                   dbSNP:rs786202389)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070509"
FT   VARIANT         1749
FT                   /note="P -> R (in ovarian cancer; unknown pathological
FT                   significance; abolishes ACACA binding and strongly reduces
FT                   BRIP1 binding; dbSNP:rs80357462)"
FT                   /evidence="ECO:0000269|PubMed:10486320,
FT                   ECO:0000269|PubMed:11301010, ECO:0000269|PubMed:15133502"
FT                   /id="VAR_007798"
FT   VARIANT         1753
FT                   /note="R -> T (in BC; unknown pathological significance;
FT                   dbSNP:rs397509246)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070510"
FT   VARIANT         1764
FT                   /note="L -> P (in BC; unknown pathological significance;
FT                   functionally impaired in vitro; dbSNP:rs80357281)"
FT                   /evidence="ECO:0000269|PubMed:17924331,
FT                   ECO:0000269|PubMed:23867111"
FT                   /id="VAR_063908"
FT   VARIANT         1766
FT                   /note="I -> S (in BC; unknown pathological significance;
FT                   dbSNP:rs80357463)"
FT                   /evidence="ECO:0000269|PubMed:17924331"
FT                   /id="VAR_063909"
FT   VARIANT         1767
FT                   /note="C -> S (in BC; unknown pathological significance;
FT                   functionally neutral in vitro)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070511"
FT   VARIANT         1770
FT                   /note="G -> V (in BC; unknown pathological significance;
FT                   functionally impaired in vitro; dbSNP:rs863224765)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070512"
FT   VARIANT         1775
FT                   /note="M -> K (in BC; strongly reduced transcription
FT                   transactivation; abolishes interaction with BRIP1 and
FT                   RBBP8; dbSNP:rs41293463)"
FT                   /evidence="ECO:0000269|PubMed:18285836"
FT                   /id="VAR_063212"
FT   VARIANT         1775
FT                   /note="M -> R (in BC; alters protein stability and
FT                   abolishes ACACA and BRIP1 binding; dbSNP:rs41293463)"
FT                   /evidence="ECO:0000269|PubMed:11301010,
FT                   ECO:0000269|PubMed:12427738, ECO:0000269|PubMed:15133502,
FT                   ECO:0000269|PubMed:7545954, ECO:0000269|PubMed:7939630"
FT                   /id="VAR_007799"
FT   VARIANT         1776
FT                   /note="P -> S (in ovarian cancer; unknown pathological
FT                   significance; dbSNP:rs1800757)"
FT                   /id="VAR_008764"
FT   VARIANT         1780
FT                   /note="L -> P (in BC, BROVCA1 and OC; unknown pathological
FT                   significance; dbSNP:rs80357474)"
FT                   /evidence="ECO:0000269|PubMed:28364669"
FT                   /id="VAR_079607"
FT   VARIANT         1782
FT                   /note="W -> C (in BC; unknown pathological significance;
FT                   functionally neutral in vitro)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070513"
FT   VARIANT         1786
FT                   /note="L -> P (in BROVCA1; unknown pathological
FT                   significance; dbSNP:rs398122697)"
FT                   /evidence="ECO:0000269|PubMed:12938098"
FT                   /id="VAR_020704"
FT   VARIANT         1788
FT                   /note="G -> V (in BC; unknown pathological significance;
FT                   dbSNP:rs80357069)"
FT                   /evidence="ECO:0000269|PubMed:17924331"
FT                   /id="VAR_063910"
FT   VARIANT         1789
FT                   /note="A -> T (in BC; unknown pathological significance;
FT                   functionally impaired in vitro; dbSNP:rs80357078)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070514"
FT   VARIANT         1794
FT                   /note="E -> D (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs397509275)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070515"
FT   VARIANT         1804
FT                   /note="V -> D (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs80356920)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070516"
FT   VARIANT         1812
FT                   /note="P -> R (in BC; unknown pathological significance;
FT                   functionally neutral in vitro)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070517"
FT   VARIANT         1812
FT                   /note="P -> S (in ovarian cancer; unknown pathological
FT                   significance; dbSNP:rs1800751)"
FT                   /id="VAR_008765"
FT   VARIANT         1837
FT                   /note="W -> R (in BC; unknown pathological significance;
FT                   functionally impaired in vitro; dbSNP:rs80356959)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070518"
FT   VARIANT         1862
FT                   /note="H -> L (in BC; unknown pathological significance;
FT                   functionally neutral in vitro; dbSNP:rs80357183)"
FT                   /evidence="ECO:0000269|PubMed:23867111"
FT                   /id="VAR_070519"
FT   MUTAGEN         26
FT                   /note="I->A: Disrupts the interaction with E2 enzymes,
FT                   thereby abolishing the E3 ubiquitin-protein ligase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:16818604,
FT                   ECO:0000269|PubMed:20351172"
FT   MUTAGEN         26
FT                   /note="I->E: No ubiquitination of RBBP8. No restoration
FT                   RBBP8-mediated focus formation or G2/M checkpoint control
FT                   upon DNA damage."
FT                   /evidence="ECO:0000269|PubMed:16818604,
FT                   ECO:0000269|PubMed:20351172"
FT   MUTAGEN         71
FT                   /note="R->G: No effect on interaction with BAP1."
FT                   /evidence="ECO:0000269|PubMed:9528852"
FT   MUTAGEN         308
FT                   /note="S->N: Abolishes phosphorylation by AURKA and
FT                   interferes with cell cycle progression from G2 to mitosis."
FT                   /evidence="ECO:0000269|PubMed:14990569"
FT   MUTAGEN         1143
FT                   /note="S->A: Reduces in vitro phosphorylation by ATR."
FT                   /evidence="ECO:0000269|PubMed:11114888"
FT   MUTAGEN         1239
FT                   /note="S->A: No effect on in vitro phosphorylation by ATR."
FT                   /evidence="ECO:0000269|PubMed:11114888"
FT   MUTAGEN         1280
FT                   /note="S->A: Reduces in vitro phosphorylation by ATR."
FT                   /evidence="ECO:0000269|PubMed:11114888"
FT   MUTAGEN         1298
FT                   /note="S->A: No effect on in vitro phosphorylation by ATR."
FT                   /evidence="ECO:0000269|PubMed:11114888"
FT   MUTAGEN         1330
FT                   /note="S->A: No effect on in vitro phosphorylation by ATR."
FT                   /evidence="ECO:0000269|PubMed:11114888"
FT   MUTAGEN         1387
FT                   /note="S->A: Loss of IR-induced S-phase checkpoint. Reduces
FT                   in vitro phosphorylation by ATR."
FT                   /evidence="ECO:0000269|PubMed:11114888,
FT                   ECO:0000269|PubMed:12183412"
FT   MUTAGEN         1394
FT                   /note="T->A: Reduces in vitro phosphorylation by ATR."
FT                   /evidence="ECO:0000269|PubMed:11114888"
FT   MUTAGEN         1423
FT                   /note="S->A: Inhibition of the infrared-induced G2 arrest.
FT                   Reduces phosphorylation by ATR."
FT                   /evidence="ECO:0000269|PubMed:11114888,
FT                   ECO:0000269|PubMed:12183412"
FT   MUTAGEN         1457
FT                   /note="S->A: Reduces in vitro phosphorylation by ATR."
FT                   /evidence="ECO:0000269|PubMed:11114888"
FT   MUTAGEN         1466
FT                   /note="S->A: No effect on in vitro phosphorylation by ATR."
FT                   /evidence="ECO:0000269|PubMed:11114888"
FT   MUTAGEN         1524
FT                   /note="S->A: No change in infrared S-phase delay; when
FT                   associated with A-1387. No effect on in vitro
FT                   phosphorylation by ATR."
FT                   /evidence="ECO:0000269|PubMed:11114888,
FT                   ECO:0000269|PubMed:12183412"
FT   MUTAGEN         1655
FT                   /note="S->A: Abolishes interaction with BRIP1."
FT                   /evidence="ECO:0000269|PubMed:15133502"
FT   MUTAGEN         1656
FT                   /note="G->D: No effect on affinity for a BRIP1
FT                   phosphopeptide."
FT                   /evidence="ECO:0000269|PubMed:21473589"
FT   MUTAGEN         1662
FT                   /note="F->S: Does not abolish ABRAXAS1 binding, but
FT                   abolishes formation of a heterotetramer with ABRAXAS1."
FT                   /evidence="ECO:0000269|PubMed:26778126"
FT   MUTAGEN         1663
FT                   /note="M->K: Does not abolish ABRAXAS1 binding, but
FT                   abolishes formation of a heterotetramer with ABRAXAS1."
FT                   /evidence="ECO:0000269|PubMed:26778126"
FT   MUTAGEN         1666
FT                   /note="Y->A: Does not abolish ABRAXAS1 binding, but impairs
FT                   formation of a heterotetramer with ABRAXAS1."
FT                   /evidence="ECO:0000269|PubMed:26778126"
FT   MUTAGEN         1670
FT                   /note="R->E: Impairs formation of a heterotetramer with
FT                   ABRAXAS1."
FT                   /evidence="ECO:0000269|PubMed:26778126"
FT   MUTAGEN         1671
FT                   /note="K->E: Impairs formation of a heterotetramer with
FT                   ABRAXAS1."
FT                   /evidence="ECO:0000269|PubMed:26778126"
FT   MUTAGEN         1700
FT                   /note="T->A: Strongly reduces affinity for a BRIP1
FT                   phosphopeptide."
FT                   /evidence="ECO:0000269|PubMed:21473589"
FT   MUTAGEN         1702
FT                   /note="K->M: Abolishes interaction with BRIP1."
FT                   /evidence="ECO:0000269|PubMed:15133502"
FT   MUTAGEN         1738
FT                   /note="G->E: Abolishes interaction with BRIP1."
FT                   /evidence="ECO:0000269|PubMed:15133502"
FT   MUTAGEN         1755
FT                   /note="S->A: No effect on in vitro phosphorylation by ATR."
FT                   /evidence="ECO:0000269|PubMed:11114888"
FT   MUTAGEN         1835
FT                   /note="R->P: Mildly reduces affinity for a BRIP1
FT                   phosphopeptide."
FT                   /evidence="ECO:0000269|PubMed:21473589"
FT   MUTAGEN         1836
FT                   /note="E->K: Slightly reduces affinity for a BRIP1
FT                   phosphopeptide."
FT                   /evidence="ECO:0000269|PubMed:21473589"
FT   CONFLICT        89
FT                   /note="I -> T (in Ref. 4; AAB61673)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="Missing (in Ref. 4; AAB61673)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        253
FT                   /note="A -> V (in Ref. 3; AAC00049)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        713
FT                   /note="S -> P (in Ref. 8; AAI15038)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1077
FT                   /note="G -> R (in Ref. 4; AAB61673)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1426
FT                   /note="S -> P (in Ref. 3; AAC00049)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1527
FT                   /note="E -> G (in Ref. 8; AAI15038)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..5
FT                   /evidence="ECO:0000244|PDB:1JM7"
FT   HELIX           8..21
FT                   /evidence="ECO:0000244|PDB:1JM7"
FT   STRAND          25..27
FT                   /evidence="ECO:0000244|PDB:1JM7"
FT   HELIX           46..53
FT                   /evidence="ECO:0000244|PDB:1JM7"
FT   STRAND          54..58
FT                   /evidence="ECO:0000244|PDB:1JM7"
FT   TURN            62..64
FT                   /evidence="ECO:0000244|PDB:1JM7"
FT   TURN            70..72
FT                   /evidence="ECO:0000244|PDB:1JM7"
FT   STRAND          78..80
FT                   /evidence="ECO:0000244|PDB:1JM7"
FT   HELIX           81..96
FT                   /evidence="ECO:0000244|PDB:1JM7"
FT   STRAND          1651..1656
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   HELIX           1659..1671
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   STRAND          1675..1679
FT                   /evidence="ECO:0000244|PDB:1T29"
FT   STRAND          1686..1689
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   STRAND          1695..1697
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   HELIX           1701..1708
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   STRAND          1712..1715
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   HELIX           1717..1725
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   HELIX           1731..1734
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   TURN            1740..1742
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   STRAND          1743..1745
FT                   /evidence="ECO:0000244|PDB:1T29"
FT   HELIX           1748..1754
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   TURN            1755..1757
FT                   /evidence="ECO:0000244|PDB:1T29"
FT   TURN            1760..1763
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   STRAND          1765..1768
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   STRAND          1770..1772
FT                   /evidence="ECO:0000244|PDB:1T2V"
FT   STRAND          1773..1775
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   HELIX           1777..1786
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   STRAND          1790..1794
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   HELIX           1795..1797
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   STRAND          1801..1803
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   STRAND          1806..1810
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   HELIX           1812..1814
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   STRAND          1817..1819
FT                   /evidence="ECO:0000244|PDB:1OQA"
FT   HELIX           1820..1822
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   HELIX           1824..1827
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   STRAND          1828..1830
FT                   /evidence="ECO:0000244|PDB:3PXE"
FT   STRAND          1832..1834
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   HELIX           1835..1844
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   HELIX           1851..1853
FT                   /evidence="ECO:0000244|PDB:4IGK"
FT   CONFLICT        P38398-7:1461
FT                   /note="N -> D (in Ref. 8; AAI15038)"
FT                   /evidence="ECO:0000305"
SQ   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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