[1]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-1775. DOI=10.1126/science.7545954; PubMed=7545954 [NCBI, ExPASy, EBI, Israel, Japan] Miki Y., Swensen J., Shattuck-Eidens D., Futreal P.A., Harshman K., Tavtigian S., Liu Q., Cochran C., Bennett L.M., Ding W., Bell R., Rosenthal J., Hussey C., Tran T., McClure M., Frye C., Hattier T., Phelps R., Haugen-Strano A., Katcher H., Yakumo K., Gholami Z., Shaffer D., Stone S., Bayer S., Wray C., Bogden R., Dayananth P., Ward J., Tonin P., Narod S., Bristow P.K., Norris F.H., Helvering L., Morrison P., Rosteck P., Lai M., Barrett J.C., Lewis C., Neuhausen S., Cannon-Albright L., Godlgar D., Wiseman R., Kamb A., Skolnick M.H.; "A strong candidate for the breast and ovarian cancer susceptibility gene BRCA1."; Science 266:66-71(1994).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=8938427 [NCBI, ExPASy, EBI, Israel, Japan] Smith T.M., Lee M.K., Szabo C.I., Jerome N., McEuen M., Taylor M., Hood L., King M.-C.; "Complete genomic sequence and analysis of 117 kb of human DNA containing the gene BRCA1."; Genome Res. 6:1029-1049(1996).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION (ISOFORM 2), VARIANTS ARG-239 AND GLY-1613, AND TISSUE SPECIFICITY (ISOFORMS 1 AND 3). TISSUE=Mammary gland; DOI=10.1038/sj.onc.1200924; PubMed=9010228 [NCBI, ExPASy, EBI, Israel, Japan] Wilson C.A., Payton M.N., Elliott G.S., Buaas F.W., Cajulis E.E., Grosshans D., Ramos L., Reese D.M., Slamon D.J., Calzone F.J.; "Differential subcellular localization, expression and biological toxicity of BRCA1 and the splice variant BRCA1-delta11b."; Oncogene 14:1-16(1997).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). TISSUE=Testis; Holt J.T., Robinson-Benion C.; Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-275; ARG-356; ASN-693; LEU-871; GLY-1038; ASN-1040; GLY-1140; ARG-1183; GLY-1613 AND ALA-1620. NIEHS SNPs program; Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[6]	PROTEIN SEQUENCE OF 6-18 (ISOFORM 1), PROTEIN SEQUENCE OF 18-26 (ISOFORM 4), AND ALTERNATIVE INITIATION (ISOFORM 4). DOI=10.1038/sj.onc.1203599; PubMed=10851077 [NCBI, ExPASy, EBI, Israel, Japan] Liu J., Prolla G., Rostagno A., Chiarle R., Feiner H., Inghirami G.; "Initiation of translation from a downstream in-frame AUG codon on BRCA1 can generate the novel isoform protein DeltaBRCA1(17aa)."; Oncogene 19:2767-2773(2000).
[7]	ALTERNATIVE SPLICING (ISOFORM 5), AND SUBCELLULAR LOCATION (ISOFORM 5). PubMed=8972225 [NCBI, ExPASy, EBI, Israel, Japan] Thakur S., Zhang H.B., Peng Y., Le H., Carroll B., Ward T., Yao J., Farid L.M., Couch F.J., Wilson R.B., Weber B.L.; "Localization of BRCA1 and a splice variant identifies the nuclear localization signal."; Mol. Cell. Biol. 17:444-452(1997).
[8]	INTERACTION WITH BAP1, SUBCELLULAR LOCATION, VARIANTS GLY-61 AND GLY-64, AND MUTAGENESIS OF ARG-71. DOI=10.1038/sj.onc.1201861; PubMed=9528852 [NCBI, ExPASy, EBI, Israel, Japan] Jensen D.E., Proctor M., Marquis S.T., Gardner H.P., Ha S.I., Chodosh L.A., Ishov A.M., Tommerup N., Vissing H., Sekido Y., Minna J., Borodovsky A., Schultz D.C., Wilkinson K.D., Maul G.G., Barlev N., Berger S., Prendergast G.C., Rauscher F.J. III; "BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression."; Oncogene 16:1097-1112(1998).
[9]	INTERACTION WITH RBBP8. DOI=10.1038/sj.onc.1202150; PubMed=9811458 [NCBI, ExPASy, EBI, Israel, Japan] Wong A.K., Ormonde P.A., Pero R., Chen Y., Lian L., Salada G., Berry S., Lawrence Q., Dayananth P., Ha P., Tavtigian S.V., Teng D.H., Bartel P.L.; "Characterization of a carboxy-terminal BRCA1 interacting protein."; Oncogene 17:2279-2285(1998).
[10]	FUNCTION AS A E2-DEPENDENT UBIQUITIN-PROTEIN LIGASE. DOI=10.1073/pnas.96.20.11364; PubMed=10500182 [NCBI, ExPASy, EBI, Israel, Japan] Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S., Weissman A.M.; "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination."; Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999).
[11]	IDENTIFICATION IN THE BASC COMPLEX. DOI=10.1101/gad.827000; PubMed=10783165 [NCBI, ExPASy, EBI, Israel, Japan] Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.; "BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures."; Genes Dev. 14:927-939(2000).
[12]	PHOSPHORYLATION AT SER-1143; SER-1280; SER-1387; THR-1394; SER-1423 AND SER-1457, AND MUTAGENESIS OF SER-1143; SER-1239; SER-1280; SER-1298; SER-1330; SER-1387; THR-1394; SER-1423; SER-1457; SER-1466; SER-1524; THR-1720 AND SER-1755. DOI=10.1101/gad.851000; PubMed=11114888 [NCBI, ExPASy, EBI, Israel, Japan] Tibbetts R.S., Cortez D., Brumbaugh K.M., Scully R., Livingston D., Elledge S.J., Abraham R.T.; "Functional interactions between BRCA1 and the checkpoint kinase ATR during genotoxic stress."; Genes Dev. 14:2989-3002(2000).
[13]	INTERACTION WITH BRIP1, CHARACTERIZATION OF VARIANT OVARIAN CANCER ARG-1749, AND CHARACTERIZATION OF VARIANT BC ARG-1775. DOI=10.1016/S0092-8674(01)00304-X; PubMed=11301010 [NCBI, ExPASy, EBI, Israel, Japan] Cantor S.B., Bell D.W., Ganesan S., Kass E.M., Drapkin R., Grossman S., Wahrer D.C.R., Sgroi D.C., Lane W.S., Haber D.A., Livingston D.M.; "BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function."; Cell 105:149-160(2001).
[14]	INTERACTION WITH NELFB. DOI=10.1083/jcb.200108049; PubMed=11739404 [NCBI, ExPASy, EBI, Israel, Japan] Ye Q., Hu Y.-F., Zhong H., Nye A.C., Belmont A.S., Li R.; "BRCA1-induced large-scale chromatin unfolding and allele-specific effects of cancer-predisposing mutations."; J. Cell Biol. 155:911-921(2001).
[15]	INTERACTION WITH FANCD2. DOI=10.1016/S1097-2765(01)00173-3; PubMed=11239454 [NCBI, ExPASy, EBI, Israel, Japan] Garcia-Higuera I., Taniguchi T., Ganesan S., Meyn M.S., Timmers C., Hejna J., Grompe M., D'Andrea A.D.; "Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway."; Mol. Cell 7:249-262(2001).
[16]	PHOSPHORYLATION BY ATM, AND MUTAGENESIS OF SER-1387; SER-1423 AND SER-1524. PubMed=12183412 [NCBI, ExPASy, EBI, Israel, Japan] Xu B., O'Donnell A.H., Kim S.-T., Kastan M.B.; "Phosphorylation of serine 1387 in BRCA1 is specifically required for the Atm-mediated S-phase checkpoint after ionizing irradiation."; Cancer Res. 62:4588-4591(2002).
[17]	INTERACTION WITH H2AFX. DOI=10.1016/S0960-9822(02)01259-9; PubMed=12419185 [NCBI, ExPASy, EBI, Israel, Japan] Kobayashi J., Tauchi H., Sakamoto S., Nakamura A., Morishima K., Matsuura S., Kobayashi T., Tamai K., Tanimoto K., Komatsu K.; "NBS1 localizes to gamma-H2AX foci through interaction with the FHA/BRCT domain."; Curr. Biol. 12:1846-1851(2002).
[18]	INTERACTION WITH SMC1A. DOI=10.1101/gad.970702; PubMed=11877377 [NCBI, ExPASy, EBI, Israel, Japan] Yazdi P.T., Wang Y., Zhao S., Patel N., Lee E.Y.-H.P., Qin J.; "SMC1 is a downstream effector in the ATM/NBS1 branch of the human S-phase checkpoint."; Genes Dev. 16:571-582(2002).
[19]	FUNCTION, AND INTERACTION WITH CHEK1. DOI=10.1038/ng837; PubMed=11836499 [NCBI, ExPASy, EBI, Israel, Japan] Yarden R.I., Pardo-Reoyo S., Sgagias M., Cowan K.H., Brody L.C.; "BRCA1 regulates the G2/M checkpoint by activating Chk1 kinase upon DNA damage."; Nat. Genet. 30:285-289(2002).
[20]	INTERACTION WITH ACACA. DOI=10.1038/sj.onc.1205915; PubMed=12360400 [NCBI, ExPASy, EBI, Israel, Japan] Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S., Lenoir G.M., Venezia N.D.; "BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains."; Oncogene 21:6729-6739(2002).
[21]	FUNCTION. DOI=10.1016/S1097-2765(03)00281-8; PubMed=12887909 [NCBI, ExPASy, EBI, Israel, Japan] Vandenberg C.J., Gergely F., Ong C.Y., Pace P., Mallery D.L., Hiom K., Patel K.J.; "BRCA1-independent ubiquitination of FANCD2."; Mol. Cell 12:247-254(2003).
[22]	INTERACTION WITH BRCC3. DOI=10.1016/S1097-2765(03)00424-6; PubMed=14636569 [NCBI, ExPASy, EBI, Israel, Japan] Dong Y., Hakimi M.-A., Chen X., Kumaraswamy E., Cooch N.S., Godwin A.K., Shiekhattar R.; "Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair."; Mol. Cell 12:1087-1099(2003).
[23]	INTERACTION WITH DCLRE1C. DOI=10.1128/MCB.24.20.9207-9220.2004; PubMed=15456891 [NCBI, ExPASy, EBI, Israel, Japan] Zhang X., Succi J., Feng Z., Prithivirajsingh S., Story M.D., Legerski R.J.; "Artemis is a phosphorylation target of ATM and ATR and is involved in the G2/M DNA damage checkpoint response."; Mol. Cell. Biol. 24:9207-9220(2004).
[24]	INTERACTION WITH CLSPN. DOI=10.1073/pnas.0401847101; PubMed=15096610 [NCBI, ExPASy, EBI, Israel, Japan] Lin S.-Y., Li K., Stewart G.S., Elledge S.J.; "Human claspin works with BRCA1 to both positively and negatively regulate cell proliferation."; Proc. Natl. Acad. Sci. U.S.A. 101:6484-6489(2004).
[25]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1211; SER-1212; SER-1217; SER-1218 AND SER-1336, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[26]	FUNCTION, AND INTERACTION WITH ACACA. DOI=10.1074/jbc.M504652200; PubMed=16326698 [NCBI, ExPASy, EBI, Israel, Japan] Moreau K., Dizin E., Ray H., Luquain C., Lefai E., Foufelle F., Billaud M., Lenoir G.M., Venezia N.D.; "BRCA1 affects lipid synthesis through its interaction with acetyl-CoA carboxylase."; J. Biol. Chem. 281:3172-3181(2006).
[27]	INTERACTION WITH ACACA. DOI=10.1016/j.jmb.2006.04.010; PubMed=16698035 [NCBI, ExPASy, EBI, Israel, Japan] Ray H., Moreau K., Dizin E., Callebaut I., Venezia N.D.; "ACCA phosphopeptide recognition by the BRCT repeats of BRCA1."; J. Mol. Biol. 359:973-982(2006).
[28]	REVIEW ON VARIANTS. DOI=10.1002/humu.1380080102; PubMed=8807330 [NCBI, ExPASy, EBI, Israel, Japan] Couch F.J., Weber B.L.; "Mutations and polymorphisms in the familial early-onset breast cancer (BRCA1) gene."; Hum. Mutat. 8:8-18(1996).
[29]	INTERACTION WITH FAM175A. DOI=10.1038/nsmb1277; PubMed=17643122 [NCBI, ExPASy, EBI, Israel, Japan] Kim H., Huang J., Chen J.; "CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA damage response."; Nat. Struct. Mol. Biol. 14:710-715(2007).
[30]	INTERACTION WITH FAM175A. DOI=10.1038/nsmb1279; PubMed=17643121 [NCBI, ExPASy, EBI, Israel, Japan] Liu Z., Wu J., Yu X.; "CCDC98 targets BRCA1 to DNA damage sites."; Nat. Struct. Mol. Biol. 14:716-720(2007).
[31]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1239; SER-1245; SER-1330; SER-1336; SER-1342; SER-1457; SER-1466; SER-1524; THR-1700 AND THR-1720, AND MASS SPECTROMETRY. DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan] Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."; Science 316:1160-1166(2007).
[32]	FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FAM175A. DOI=10.1126/science.1139476; PubMed=17525340 [NCBI, ExPASy, EBI, Israel, Japan] Wang B., Matsuoka S., Ballif B.A., Zhang D., Smogorzewska A., Giyi S., Elledge S.J.; "Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response."; Science 316:1194-1198(2007).
[33]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1542, AND MASS SPECTROMETRY. DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan] Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."; J. Proteome Res. 7:1346-1351(2008).
[34]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395; SER-398; SER-403; SER-753; SER-1211; SER-1217 AND SER-1218, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[35]	FUNCTION, AND IDENTIFICATION IN THE BRCA1-A COMPLEX. DOI=10.1101/gad.1770609; PubMed=19261748 [NCBI, ExPASy, EBI, Israel, Japan] Feng L., Huang J., Chen J.; "MERIT40 facilitates BRCA1 localization and DNA damage repair."; Genes Dev. 23:719-728(2009).
[36]	IDENTIFICATION IN THE BRCA1-A COMPLEX. DOI=10.1101/gad.1770309; PubMed=19261749 [NCBI, ExPASy, EBI, Israel, Japan] Wang B., Hurov K., Hofmann K., Elledge S.J.; "NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control."; Genes Dev. 23:729-739(2009).
[37]	IDENTIFICATION IN THE BRCA1-A COMPLEX. DOI=10.1101/gad.1739609; PubMed=19261746 [NCBI, ExPASy, EBI, Israel, Japan] Shao G., Patterson-Fortin J., Messick T.E., Feng D., Shanbhag N., Wang Y., Greenberg R.A.; "MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA double-strand breaks."; Genes Dev. 23:740-754(2009).
[38]	VARIANTS LEU-1637; GLU-1708 AND ARG-1775. DOI=10.1126/science.7939630; PubMed=7939630 [NCBI, ExPASy, EBI, Israel, Japan] Futreal P.A., Liu Q., Shattuck-Eidens D., Cochran C., Harshman K., Tavtigian S., Bennett L.M., Haugen-Strano A., Swensen J., Miki Y., Eddington K., McClure M., Frye C., Weaver-Felhaus J., Ding W., Gholami Z., Soederkvist P., Terry L., Jhanwar S., Berchuk A., Iglehart J.D., Marks J., Ballinger D.G., Barrett J.C., Skolnick M.H., Kamb A., Wiseman R.; "BRCA1 mutations in primary breast and ovarian carcinomas."; Science 266:120-122(1994).
[39]	VARIANT BC GLY-64, AND VARIANTS ALA-772; ASN-1040 AND GLY-1443. DOI=10.1038/ng1294-387; PubMed=7894491 [NCBI, ExPASy, EBI, Israel, Japan] Castilla L.H., Couch F.J., Erdos M.R., Hoskins K.F., Calzone K., Garber J.E., Boyd J., Lubin M.B., Deshano M.L., Brody L.C., Collins F.S., Weber B.L.; "Mutations in the BRCA1 gene in families with early-onset breast and ovarian cancer."; Nat. Genet. 8:387-391(1994).
[40]	VARIANT BC GLY-61, AND VARIANTS ARG-356; GLY-1038; ASN-1040; ARG-1183 AND GLY-1613. DOI=10.1038/ng1294-399; PubMed=7894493 [NCBI, ExPASy, EBI, Israel, Japan] Friedman L.S., Ostermeyer E.A., Szabo C.I., Dowd P., Lynch E.D., Rowell S.E., King M.-C.; "Confirmation of BRCA1 by analysis of germline mutations linked to breast and ovarian cancer in ten families."; Nat. Genet. 8:399-404(1994).
[41]	VARIANT BC GLY-61. PubMed=8554067 [NCBI, ExPASy, EBI, Israel, Japan] Serova O., Montagna M., Torchard D., Narod S.A., Tonin P., Sylla B., Lynch H.T., Feunteun J., Lenoir G.M.; "A high incidence of BRCA1 mutations in 20 breast-ovarian cancer families."; Am. J. Hum. Genet. 58:42-51(1996).
[42]	VARIANT BROVCA1 TRP-841. DOI=10.1002/(SICI)1098-2272(1996)13:6<595::AID-GEPI5>3.3.CO;2-0; PubMed=8968716 [NCBI, ExPASy, EBI, Israel, Japan] Barker D.F., Almeida E.F.A., Casey G., Fain P.R., Liao S.-Y., Masunaka I., Noble B., Kurosaki T., Anton-Culver H.; "BRCA1 R841W: a strong candidate for a common mutation with moderate phenotype."; Genet. Epidemiol. 13:595-604(1996).
[43]	VARIANTS BC AND BROVCA1. DOI=10.1093/hmg/5.6.835; PubMed=8776600 [NCBI, ExPASy, EBI, Israel, Japan] Durocher F., Shattuck-Eidens D., McClure M., Labrie F., Skolnick M.H., Goldgar D.E., Simard J.; "Comparison of BRCA1 polymorphisms, rare sequence variants and/or missense mutations in unaffected and breast/ovarian cancer populations."; Hum. Mol. Genet. 5:835-842(1996).
[44]	VARIANTS BC MET-271 AND SER-1150. DOI=10.1002/(SICI)1098-1004(1996)7:4<334::AID-HUMU7>3.3.CO;2-K; PubMed=8723683 [NCBI, ExPASy, EBI, Israel, Japan] Katagiri T., Emi M., Ito I., Kobayashi K., Yoshimoto M., Iwase T., Kasumi F., Miki Y., Skolnick M.H., Nakamura Y.; "Mutations in the BRCA1 gene in Japanese breast cancer patients."; Hum. Mutat. 7:334-339(1996).
[45]	VARIANT BC GLY-61, AND VARIANTS ARG-239; TRP-841 AND ILE-1512. DOI=10.1007/s004390050799; PubMed=9760198 [NCBI, ExPASy, EBI, Israel, Japan] Dong J., Chang-Claude J., Wu Y., Schumacher V., Debatin I., Tonin P., Royer-Pokora B.; "A high proportion of mutations in the BRCA1 gene in German breast/ovarian cancer families with clustering of mutations in the 3' third of the gene."; Hum. Genet. 103:154-161(1998).
[46]	VARIANT BC GLY-64, AND VARIANTS ALA-772; GLU-820; ASN-1040; GLY-1443; ILE-1512; LEU-1637 AND ILE-1652. DOI=10.1002/(SICI)1098-1004(1998)11:2<166::AID-HUMU10>3.3.CO;2-V; PubMed=9482581 [NCBI, ExPASy, EBI, Israel, Japan] Andersen T.I., Eiken H.G., Couch F., Kaada G., Skrede M., Johnsen H., Aloysius T.A., Tveit K.M., Tranebjaerg L., Doerum A., Moeller P., Weber B.L., Boerresen-Dale A.-L.; "Constant denaturant gel electrophoresis (CDGE) in BRCA1 mutation screening."; Hum. Mutat. 11:166-174(1998).
[47]	VARIANTS BC SER-22; LEU-461; ASP-465; VAL-552; SER-892; ASP-960; ILE-1025 AND ALA-1047. DOI=10.1007/s100380050035; PubMed=9609997 [NCBI, ExPASy, EBI, Israel, Japan] Katagiri T., Kasumi F., Yoshimoto M., Nomizu T., Asaishi K., Abe R., Tsuchiya A., Sugano M., Takai S., Yoneda M., Fukutomi T., Nanba K., Makita M., Okazaki H., Hirata K., Okazaki M., Furutsuma Y., Morishita Y., Iino Y., Karino T., Ayabe H., Hara S., Kajiwara T., Houga S., Shimizu T., Toda M., Yamazaki Y., Uchida T., Kunitomo K., Sonoo H., Kurebayashi J., Shimotsuma K., Nakamura Y., Miki Y.; "High proportion of missense mutations of the BRCA1 and BRCA2 genes in Japanese breast cancer families."; J. Hum. Genet. 43:42-48(1998).
[48]	VARIANT OVARIAN CANCER ARG-1749. DOI=10.1086/302583; PubMed=10486320 [NCBI, ExPASy, EBI, Israel, Japan] Gayther S.A., Russell P., Harrington P., Antoniou A.C., Easton D.F., Ponder B.A.J.; "The contribution of germline BRCA1 and BRCA2 mutations to familial ovarian cancer: no evidence for other ovarian cancer-susceptibility genes."; Am. J. Hum. Genet. 65:1021-1029(1999).
[49]	VARIANT BC SER-346, AND VARIANTS LEU-871; GLY-1038; ARG-1183 AND GLY-1613. DOI=10.1007/s004390050936; PubMed=10323242 [NCBI, ExPASy, EBI, Israel, Japan] Li S.S.-L., Tseng H.-M., Yang T.-P., Liu C.-H., Teng S.-J., Huang H.-W., Chen L.-M., Kao H.-W., Chen J.H., Tseng J.-N., Chen A., Hou M.-F., Huang T.-J., Chang H.-T., Mok K.-T., Tsai J.-H.; "Molecular characterization of germline mutations in the BRCA1 and BRCA2 genes from breast cancer families in Taiwan."; Hum. Genet. 104:201-204(1999).
[50]	VARIANTS OVARIAN CANCER, AND VARIANTS. DOI=10.1093/hmg/8.5.889; PubMed=10196379 [NCBI, ExPASy, EBI, Israel, Japan] Janezic S.A., Ziogas A., Krumroy L.M., Krasner M., Plummer S.J., Cohen P., Gildea M., Barker D., Haile R., Casey G., Anton-Culver H.; "Germline BRCA1 alterations in a population-based series of ovarian cancer cases."; Hum. Mol. Genet. 8:889-897(1999).
[51]	VARIANTS GLY-1347; ILE-1512 AND ILE-1652. DOI=10.1089/10906570260199375; PubMed=12215251 [NCBI, ExPASy, EBI, Israel, Japan] Deffenbaugh A.M., Frank T.S., Hoffman M., Cannon-Albright L., Neuhausen S.L.; "Characterization of common BRCA1 and BRCA2 variants."; Genet. Test. 6:119-121(2002).
[52]	VARIANTS ILE-656; LEU-871 AND GLY-1613. DOI=10.1002/humu.9083; PubMed=12442274 [NCBI, ExPASy, EBI, Israel, Japan] Zhi X., Szabo C., Chopin S., Suter N., Wang Q.-S., Ostrander E.A., Sinilnikova O.M., Lenoir G.M., Goldgar D., Shi Y.-R.; "BRCA1 and BRCA2 sequence variants in Chinese breast cancer families."; Hum. Mutat. 20:474-474(2002).
[53]	VARIANT BC TYR-749. DOI=10.1002/humu.9084; PubMed=12442275 [NCBI, ExPASy, EBI, Israel, Japan] Ruiz-Flores P., Sinilnikova O.M., Badzioch M., Calderon-Garciduenas A.L., Chopin S., Fabrice O., Gonzalez-Guerrero J.F., Szabo C., Lenoir G., Goldgar D.E., Barrera-Saldana H.A.; "BRCA1 and BRCA2 mutation analysis of early-onset and familial breast cancer cases in Mexico."; Hum. Mutat. 20:474-475(2002).
[54]	VARIANTS BC GLY-61; LYS-71; GLN-866; TYR-888; ILE-1139; GLY-1210 AND PRO-1297, AND VARIANTS BROVCA1 TYR-835 AND PRO-1786. DOI=10.1002/humu.9174; PubMed=12938098 [NCBI, ExPASy, EBI, Israel, Japan] Meyer P., Voigtlaender T., Bartram C.R., Klaes R.; "Twenty-three novel BRCA1 and BRCA2 sequence alterations in breast and/or ovarian cancer families in Southern Germany."; Hum. Mutat. 22:259-259(2003).
[55]	VARIANTS ASN-693; ASN-1040; ALA-1060 AND MET-1665. DOI=10.1038/sj.bjc.6601656; PubMed=15026808 [NCBI, ExPASy, EBI, Israel, Japan] Claes K., Poppe B., Coene I., De Paepe A., Messiaen L.; "BRCA1 and BRCA2 germline mutation spectrum and frequencies in Belgian breast/ovarian cancer families."; Br. J. Cancer 90:1244-1251(2004).
[56]	VARIANTS OVARIAN CANCER GLY-61; THR-1411; ARG-1697 AND TRP-1699. DOI=10.1016/j.ejca.2003.09.016; PubMed=14746861 [NCBI, ExPASy, EBI, Israel, Japan] Malander S., Ridderheim M., Masbaeck A., Loman N., Kristoffersson U., Olsson H., Nilbert M., Borg A.; "One in 10 ovarian cancer patients carry germ line BRCA1 or BRCA2 mutations: results of a prospective study in Southern Sweden."; Eur. J. Cancer 40:422-428(2004).
[57]	VARIANTS BC/BROVCA1 LYS-10; LYS-23; ILE-1187; HIS-1200 AND TYR-1217, VARIANTS BC ILE-1204 AND ASN-1207, VARIANTS BROVCA1 LEU-1226 AND GLY-1243, AND VARIANT ARG-1183. DOI=10.1002/humu.9213; PubMed=14722926 [NCBI, ExPASy, EBI, Israel, Japan] Valarmathi M.T., Sawhney M., Deo S.S.V., Shukla N.K., Das S.N.; "Novel germline mutations in the BRCA1 and BRCA2 genes in Indian breast and breast-ovarian cancer families."; Hum. Mutat. 23:205-205(2004).
[58]	VARIANTS HIS-856; LEU-871; GLY-1038; ARG-1183; THR-1628; GLN-1690 AND GLY-1713. DOI=10.1002/humu.9275; PubMed=15365993 [NCBI, ExPASy, EBI, Israel, Japan] Seo J.H., Cho D.-Y., Ahn S.-H., Yoon K.-S., Kang C.-S., Cho H.M., Lee H.S., Choe J.J., Choi C.W., Kim B.S., Shin S.W., Kim Y.H., Kim J.S., Son G.-S., Lee J.-B., Koo B.H.; "BRCA1 and BRCA2 germline mutations in Korean patients with sporadic breast cancer."; Hum. Mutat. 24:350-350(2004).
[59]	VARIANTS [LARGE SCALE ANALYSIS] PHE-30; PHE-758 AND CYS-778. DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan] Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.; "The consensus coding sequences of human breast and colorectal cancers."; Science 314:268-274(2006).

Comments

FUNCTION: The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Plays a central role in DNA repair by facilitating cellular response to DNA repair. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation.
PATHWAY: Protein modification; protein ubiquitination .
SUBUNIT: Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBN protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1/RAP80, FAM175A/Abraxas, BRCC3/BRCC36, BRE/BRCC45 and MERIT40/NBA1. Interacts (via BRCT domains) with FAM175A/Abraxas and RBBP8. Associates with RNA polymerase II holoenzyme. Interacts with SMC1A and COBRA1/NELFB. Interacts (via BRCT domains) with BRIP1. Interacts with FANCD2 (ubiquitinated). Interacts with BAP1. Interacts with DCLRE1C/Artemis and CLSPN. Interacts with H2AFX (phosphorylated on 'Ser-140'). Interacts with CHEK1/CHK1. Interacts with BRCC3. Interacts (via BRCT domains) with ACACA (phosphorylated); the interaction prevents dephosphorylation of ACACA.
INTERACTION:
Self; NbExp=1; IntAct=EBI-349905, EBI-349905;
Q13085:ACACA; NbExp=2; IntAct=EBI-349905, EBI-717681;
O14867:BACH1; NbExp=1; IntAct=EBI-349905, EBI-1263541;
Q92560:BAP1; NbExp=1; IntAct=EBI-349905, EBI-1791447;
Q92560:BAP1; NbExp=1; IntAct=EBI-2015072, EBI-1791447;
Q99PU7:Bap1 (xeno); NbExp=2; IntAct=EBI-349905, EBI-1791471;
Q99728:BARD1; NbExp=5; IntAct=EBI-349905, EBI-473181;
Q7Z569:BRAP; NbExp=1; IntAct=EBI-349905, EBI-349900;
P24385:CCND1; NbExp=2; IntAct=EBI-349905, EBI-375001;
P24864:CCNE1; NbExp=2; IntAct=EBI-349905, EBI-519526;
O14757:CHEK1; NbExp=1; IntAct=EBI-349905, EBI-974488;
Q8WX92:COBRA1; NbExp=3; IntAct=EBI-349905, EBI-347721;
P03372:ESR1; NbExp=4; IntAct=EBI-349905, EBI-78473;
Q6UWZ7:FAM175A; NbExp=4; IntAct=EBI-349905, EBI-1263451;
P16104:H2AFX; NbExp=1; IntAct=EBI-349905, EBI-494830;
P52292:KPNA2; NbExp=1; IntAct=EBI-349905, EBI-349938;
Q14676:MDC1; NbExp=1; IntAct=EBI-349905, EBI-495644;
P16333:NCK1; NbExp=1; IntAct=EBI-349905, EBI-389883;
Q9UBD5:ORC3L; NbExp=1; IntAct=EBI-349905, EBI-374916;
P27986:PIK3R1; NbExp=1; IntAct=EBI-349905, EBI-79464;
P62136:PPP1CA; NbExp=2; IntAct=EBI-349905, EBI-357253;
P62140:PPP1CB; NbExp=2; IntAct=EBI-349905, EBI-352350;
P36873:PPP1CC; NbExp=2; IntAct=EBI-349905, EBI-356283;
Q99708:RBBP8; NbExp=5; IntAct=EBI-349905, EBI-1263531;
Q14683:SMC1A; NbExp=1; IntAct=EBI-349905, EBI-80690;
Q12888:TP53BP1; NbExp=1; IntAct=EBI-349905, EBI-396540;
Q9Y4A5:TRRAP; NbExp=2; IntAct=EBI-349905, EBI-399128;
Q96RL1:UIMC1; NbExp=4; IntAct=EBI-349905, EBI-725300;
Q6NZY4:ZCCHC8; NbExp=2; IntAct=EBI-349905, EBI-1263058;
Q9GZX5:ZNF350; NbExp=2; IntAct=EBI-349905, EBI-396421;
SUBCELLULAR LOCATION: Nucleus. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex.
SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.
SUBCELLULAR LOCATION: Isoform 5: Cytoplasm.

ALTERNATIVE PRODUCTS: 5 named isoforms [FASTA] produced by alternative splicing and alternative initiation.

Name	1
Isoform ID	P38398-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	P38398-2
Features which should be applied to build the isoform sequence: VSP_035397.

Name	3
Synonyms	Delta11b
Isoform ID	P38398-3
Features which should be applied to build the isoform sequence: VSP_035399.

Name	4
Synonyms	DeltaBRCA1(17aa)
Isoform ID	P38398-4
Note: Produced by alternative initiation at Met-18 of isoform 1.
Features which should be applied to build the isoform sequence: VSP_035396.

Name	5
Synonyms	Delta11, Delta772-3095
Isoform ID	P38398-5
Features which should be applied to build the isoform sequence: VSP_035398.

TISSUE SPECIFICITY: Isoform 1 and isoform 3 are widely expressed. Isoform 3 is reduced or absent in several breast and ovarian cancer cell lines.
DOMAIN: The BRCT domains recognize and bind phosphorylated pSXXF motif on proteins. The interaction with the phosphorylated pSXXF motif of FAM175A/Abraxas, recruits BRCA1 at DNA damage sites.
DOMAIN: The RING-type zinc finger domain interacts with BAP1.
PTM: Phosphorylated in response to IR, UV, and various stimuli that cause checkpoint activation, probably by ATM or ATR.
POLYMORPHISM: There is evidence that the presence of the rare form of Gln-356-Arg and Leu-871-Pro polymorphisms may be associated with an increased risk for developing ovarian cancer.
DISEASE: Defects in BRCA1 are a cause of genetic susceptibility to breast cancer (BC) [MIM:113705, 114480]. BC is an extremely common malignancy, affecting one in eight women during their lifetime. A positive family history has been identified as major contributor to risk of development of the disease, and this link is striking for early-onset breast cancer. Mutations in BRCA1 are thought to be responsible for 45% of inherited breast cancer. Moreover, BRCA1 carriers have a 4-fold increased risk of colon cancer, whereas male carriers face a 3-fold increased risk of prostate cancer. Cells lacking BRCA1 show defects in DNA repair by homologous recombination.
DISEASE: Defects in BRCA1 are a cause of susceptibility to familial breast-ovarian cancer type 1 (BROVCA1) [MIM:604370]. Mutations in BRCA1 are thought to be responsible for more than 80% of inherited breast-ovarian cancer.
DISEASE: Defects in BRCA1 are a cause of genetic susceptibility to ovarian cancer [MIM:113705].
SIMILARITY: Contains 2 BRCT domains.
SIMILARITY: Contains 1 RING-type zinc finger.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/BRCA1ID163ch17q21.html";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=BRCA1";.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/brca1/";.
WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and polymorphism database; URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=BRCA1";.
WEB RESOURCE: Name=Wikipedia; Note=BRCA1 entry; URL="http://en.wikipedia.org/wiki/BRCA1";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U14680; AAA73985.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L78833; AAC37594.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U64805; AAC00049.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF005068; AAB61673.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY273801; AAP12647.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00027277; -.
IPI00185298; -.
IPI00218982; -.
IPI00375507; -.
IPI00909467; -.

PIR

A58881; A58881.

RefSeq

NP_009225.1; -.
NP_009226.1; -.
NP_009227.1; -.
NP_009228.1; -.
NP_009235.2; -.

UniGene

Hs.194143

3D structure databases

PDB

1JM7; NMR; -; A=1-110.	[ExPASy / RCSB / EBI]
1JNX; X-ray; 2.50 A; X=1646-1859.	[ExPASy / RCSB / EBI]
1N5O; X-ray; 2.80 A; X=1646-1859.	[ExPASy / RCSB / EBI]
1OQA; NMR; -; A=1755-1863.	[ExPASy / RCSB / EBI]
1T15; X-ray; 1.85 A; A=1649-1859.	[ExPASy / RCSB / EBI]
1T29; X-ray; 2.30 A; A=1646-1859.	[ExPASy / RCSB / EBI]
1T2U; X-ray; 2.80 A; A=1646-1859.	[ExPASy / RCSB / EBI]
1T2V; X-ray; 3.30 A; A/B/C/D/E=1646-1859.	[ExPASy / RCSB / EBI]
1Y98; X-ray; 2.50 A; A=1646-1859.	[ExPASy / RCSB / EBI]
2ING; X-ray; 3.60 A; X=1649-1859.	[ExPASy / RCSB / EBI]
3COJ; X-ray; 3.21 A; A/B/C/D/E/F/G/X=1646-1859.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1JM7; -.
1JNX; -.
1N5O; -.
1OQA; -.
1T15; -.
1T29; -.
1T2U; -.
1T2V; -.
1Y98; -.
2ING; -.
3COJ; -.

DisProt

DP00238; -.

ModBase

P38398.

Protein-protein interaction databases

DIP

DIP:5971N; -.

IntAct

P38398; 42.

PTM databases

PhosphoSite

P38398; -.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_a_pathway; Aurora A signaling.
bard1pathway; BARD1 signaling events.
ar_pathway; Coregulation of Androgen receptor activity.
hnf3apathway; FOXA1 transcription factor network.

Reactome

REACT_216; DNA Repair.

Organism-specific databases

GC17M038450; -.

HIX0039035; -.

HGNC:1100; BRCA1.

CAB001946; -.

113705; gene. [NCBI / EBI]
114480; phenotype. [NCBI / EBI]
604370; phenotype. [NCBI / EBI]

Orphanet

145; Breast cancer, familial.
1331; Prostate cancer, familial.

PharmGKB

PA25411; -.

Gene expression databases

P38398; -.

P38398; -.

HS_BRCA1; -.

ENSG00000012048; Homo sapiens.

Ontologies

GO:0070531;	Cellular component: BRCA1-A complex (inferred from direct assay from UniProtKB).
GO:0031436;	Cellular component: BRCA1-BARD1 complex (inferred from direct assay from UniProtKB).
GO:0008274;	Cellular component: gamma-tubulin ring complex (non-traceable author statement from UniProtKB).
GO:0005654;	Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0030529;	Cellular component: ribonucleoprotein complex (inferred from direct assay from MGI).
GO:0050681;	Molecular function: androgen receptor binding (non-traceable author statement from UniProtKB).
GO:0019899;	Molecular function: enzyme binding (inferred from physical interaction from UniProtKB).
GO:0042802;	Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0016874;	Molecular function: ligase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0003713;	Molecular function: transcription coactivator activity (non-traceable author statement from UniProtKB).
GO:0015631;	Molecular function: tubulin binding (non-traceable author statement from UniProtKB).
GO:0008270;	Molecular function: zinc ion binding (traceable author statement from ProtInc).
GO:0030521;	Biological process: androgen receptor signaling pathway (non-traceable author statement from UniProtKB).
GO:0006915;	Biological process: apoptosis (traceable author statement from UniProtKB).
GO:0007059;	Biological process: chromosome segregation (inferred from mutant phenotype from UniProtKB).
GO:0006978;	Biological process: DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator (traceable author statement from UniProtKB).
GO:0008630;	Biological process: DNA damage response, signal transduction resulting in induction of apoptosis (inferred from direct assay from MGI).
GO:0000724;	Biological process: double-strand break repair via homologous recombination (inferred from direct assay from HGNC).
GO:0006633;	Biological process: fatty acid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0031572;	Biological process: G2/M transition DNA damage checkpoint (inferred from mutant phenotype from UniProtKB).
GO:0019941;	Biological process: modification-dependent protein catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0045786;	Biological process: negative regulation of cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0046600;	Biological process: negative regulation of centriole replication (non-traceable author statement from UniProtKB).
GO:0045717;	Biological process: negative regulation of fatty acid biosynthetic process (inferred from mutant phenotype from UniProtKB).
GO:0016481;	Biological process: negative regulation of transcription (inferred from direct assay from UniProtKB).
GO:0045739;	Biological process: positive regulation of DNA repair (inferred from mutant phenotype from UniProtKB).
GO:0031398;	Biological process: positive regulation of protein ubiquitination (inferred from direct assay from UniProtKB).
GO:0045893;	Biological process: positive regulation of transcription, DNA-dependent (non-traceable author statement from UniProtKB).
GO:0006301;	Biological process: postreplication repair (inferred from direct assay from HGNC).
GO:0016567;	Biological process: protein ubiquitination (non-traceable author statement from UniProtKB).
GO:0042127;	Biological process: regulation of cell proliferation (traceable author statement from UniProtKB).
GO:0006357;	Biological process: regulation of transcription from RNA polymerase II promoter (traceable author statement from ProtInc).
GO:0006359;	Biological process: regulation of transcription from RNA polymerase III promoter (traceable author statement from UniProtKB).
GO:0043627;	Biological process: response to estrogen stimulus (inferred from direct assay from UniProtKB).
GO:0010212;	Biological process: response to ionizing radiation (inferred from mutant phenotype from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR011364; BRCA1.
IPR001357; BRCT.
IPR002378; Brst_cancerI.
IPR018957; Znf_C3HC4_RING-type.
IPR001841; Znf_RING.
IPR017907; Znf_RING_CS.
Graphical view of domain structure.

PANTHER

PTHR13763; BRCA1; 1.

Pfam

PF00533; BRCT; 2.
PF00097; zf-C3HC4; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001734; BRCA1; 1.

PRINTS

PR00493; BRSTCANCERI.

SMART

SM00292; BRCT; 2.
SM00184; RING; 1.
SMART graphical view of domain structure.

PROSITE

PS50172; BRCT; 2.
PS00518; ZF_RING_1; 1.
PS50089; ZF_RING_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P38398; -.

Genome annotation databases

Ensembl

ENSG00000012048; Homo sapiens. [Contig view]

GeneID

672; -.

KEGG

hsa:672; -.

Phylogenomic databases

HOGENOM

P38398; -.

HOVERGEN

P38398; -.

OMA

P38398; CMLKLLN.

Other

2752; -.

P38398; -.

BRCA1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative initiation; Alternative splicing; Anti-oncogene; Cell cycle; Cytoplasm; Direct protein sequencing; Disease mutation; DNA damage; DNA repair; DNA-binding; Fatty acid biosynthesis; Ligase; Lipid synthesis; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Repeat; Ubl conjugation pathway; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1863`	`1863`	`Breast cancer type 1 susceptibility protein.`	`PRO_0000055830`
`DOMAIN`	`1642 1736`	`95`	`BRCT 1.`
`DOMAIN`	`1756 1855`	`100`	`BRCT 2.`
`ZN_FING`	`24 65`	`42`	`RING-type.`
`COMPBIAS`	`651 654`	`4`	`Poly-Lys.`
`MOD_RES`	`395 395`		`Phosphoserine.`
`MOD_RES`	`398 398`		`Phosphoserine.`
`MOD_RES`	`403 403`		`Phosphoserine.`
`MOD_RES`	`753 753`		`Phosphoserine.`
`MOD_RES`	`840 840`		`Phosphoserine (By similarity).`
`MOD_RES`	`1143 1143`		`Phosphoserine; by ATR; in vitro.`
`MOD_RES`	`1211 1211`		`Phosphoserine.`
`MOD_RES`	`1212 1212`		`Phosphoserine.`
`MOD_RES`	`1217 1217`		`Phosphoserine.`
`MOD_RES`	`1218 1218`		`Phosphoserine.`
`MOD_RES`	`1239 1239`		`Phosphoserine.`
`MOD_RES`	`1245 1245`		`Phosphoserine.`
`MOD_RES`	`1280 1280`		`Phosphoserine; by ATR; in vitro.`
`MOD_RES`	`1330 1330`		`Phosphoserine.`
`MOD_RES`	`1336 1336`		`Phosphoserine.`
`MOD_RES`	`1342 1342`		`Phosphoserine.`
`MOD_RES`	`1387 1387`		`Phosphoserine; by ATM and ATR.`
`MOD_RES`	`1394 1394`		`Phosphothreonine; by ATR; in vitro.`
`MOD_RES`	`1423 1423`		`Phosphoserine; by ATM and ATR.`
`MOD_RES`	`1457 1457`		`Phosphoserine; by ATR; in vitro.`
`MOD_RES`	`1466 1466`		`Phosphoserine.`
`MOD_RES`	`1524 1524`		`Phosphoserine; by ATM.`
`MOD_RES`	`1542 1542`		`Phosphoserine.`
`MOD_RES`	`1700 1700`		`Phosphothreonine.`
`MOD_RES`	`1720 1720`		`Phosphothreonine.`
`VAR_SEQ`	`1 17`		`Missing (in isoform 4).`	`VSP_035396`
`VAR_SEQ`	`71 71`		`R -> M (in isoform 2).`	`VSP_035397`
`VAR_SEQ`	`224 1365`		`Missing (in isoform 5).`	`VSP_035398`
`VAR_SEQ`	`264 1366`		`Missing (in isoform 3).`	`VSP_035399`
`VARIANT`	`10 10`	`1`	`E -> K (in BC and BROVCA1).`	`VAR_020679`
`VARIANT`	`11 11`	`1`	`V -> A (unclassified).`	`VAR_007754`
`VARIANT`	`21 21`	`1`	`I -> V (unclassified).`	`VAR_007755`
`VARIANT`	`22 22`	`1`	`L -> S (in BC).`	`VAR_007756`
`VARIANT`	`23 23`	`1`	`E -> K (in BC and BROVCA1).`	`VAR_020680`
`VARIANT`	`30 30`	`1`	`L -> F (in a breast cancer sample; somatic mutation).`	`VAR_035947`
`VARIANT`	`61 61`	`1`	`C -> G (in BC and ovarian cancer; no interaction with BAP1; dbSNP:rs28897672 [NCBI]).`	`VAR_007757`
`VARIANT`	`64 64`	`1`	`C -> G (in BC; no interaction with BAP1).`	`VAR_007758`
`VARIANT`	`64 64`	`1`	`C -> Y (unclassified; dbSNP:rs55851803 [NCBI]).`	`VAR_007759`
`VARIANT`	`71 71`	`1`	`R -> K (in BC; unknown pathological significance).`	`VAR_020681`
`VARIANT`	`153 153`	`1`	`S -> R (in dbSNP:rs28897674 [NCBI]).`	`VAR_052077`
`VARIANT`	`227 227`	`1`	`E -> K (in ovarian cancer; could be a polymorphism).`	`VAR_008759`
`VARIANT`	`239 239`	`1`	`H -> R.`	`VAR_007760`
`VARIANT`	`271 271`	`1`	`V -> M (in BC).`	`VAR_007761`
`VARIANT`	`275 275`	`1`	`G -> S (in dbSNP:rs8176153 [NCBI]).`	`VAR_019944`
`VARIANT`	`346 346`	`1`	`P -> S (in BC; could be a polymorphism).`	`VAR_008760`
`VARIANT`	`356 356`	`1`	`Q -> R (common polymorphism; dbSNP:rs1799950 [NCBI]).`	`VAR_007762`
`VARIANT`	`369 369`	`1`	`Missing (in BC).`	`VAR_007763`
`VARIANT`	`379 379`	`1`	`I -> M (unclassified; dbSNP:rs56128296 [NCBI]).`	`VAR_007764`
`VARIANT`	`461 461`	`1`	`F -> L (in BC; dbSNP:rs56046357 [NCBI]).`	`VAR_007765`
`VARIANT`	`465 465`	`1`	`Y -> D (in BC).`	`VAR_007766`
`VARIANT`	`507 507`	`1`	`R -> I (unclassified).`	`VAR_007767`
`VARIANT`	`552 552`	`1`	`G -> V (in BC).`	`VAR_007768`
`VARIANT`	`656 656`	`1`	`N -> I.`	`VAR_020682`
`VARIANT`	`693 693`	`1`	`D -> N (rare polymorphism; dbSNP:rs4986850 [NCBI]).`	`VAR_007769`
`VARIANT`	`723 723`	`1`	`N -> D (in dbSNP:rs4986845 [NCBI]).`	`VAR_020110`
`VARIANT`	`749 749`	`1`	`D -> Y (in BC).`	`VAR_020683`
`VARIANT`	`758 758`	`1`	`L -> F (in a breast cancer sample; somatic mutation).`	`VAR_035948`
`VARIANT`	`772 772`	`1`	`V -> A (rare polymorphism).`	`VAR_007770`
`VARIANT`	`778 778`	`1`	`G -> C (in a breast cancer sample; somatic mutation).`	`VAR_035949`
`VARIANT`	`820 820`	`1`	`K -> E (rare polymorphism).`	`VAR_007771`
`VARIANT`	`826 826`	`1`	`T -> K (in BC).`	`VAR_007772`
`VARIANT`	`835 835`	`1`	`H -> Y (in BROVCA1; unknown pathological significance).`	`VAR_020684`
`VARIANT`	`841 841`	`1`	`R -> W (in BROVCA1; could be a rare polymorphism; dbSNP:rs1800709 [NCBI]).`	`VAR_007773`
`VARIANT`	`856 856`	`1`	`Y -> H (in a patient with sporadic breast cancer; unknown pathological significance).`	`VAR_020685`
`VARIANT`	`866 866`	`1`	`R -> Q (in BC; unknown pathological significance).`	`VAR_020686`
`VARIANT`	`871 871`	`1`	`P -> L (common polymorphism; dbSNP:rs799917 [NCBI]).`	`VAR_007774`
`VARIANT`	`888 888`	`1`	`H -> Y (in BC; unknown pathological significance).`	`VAR_020687`
`VARIANT`	`892 892`	`1`	`L -> S (in BC).`	`VAR_007775`
`VARIANT`	`925 925`	`1`	`I -> L (in dbSNP:rs4986847 [NCBI]).`	`VAR_021913`
`VARIANT`	`960 960`	`1`	`G -> D (in BC).`	`VAR_007776`
`VARIANT`	`989 989`	`1`	`F -> S (in dbSNP:rs4986848 [NCBI]).`	`VAR_020111`
`VARIANT`	`1008 1008`	`1`	`M -> I (common polymorphism; dbSNP:rs1800704 [NCBI]).`	`VAR_007777`
`VARIANT`	`1025 1025`	`1`	`T -> I (in BC).`	`VAR_007778`
`VARIANT`	`1038 1038`	`1`	`E -> G (common polymorphism; dbSNP:rs16941 [NCBI]).`	`VAR_007779`
`VARIANT`	`1040 1040`	`1`	`S -> N (rare polymorphism; dbSNP:rs4986852 [NCBI]).`	`VAR_007780`
`VARIANT`	`1047 1047`	`1`	`V -> A (in BC).`	`VAR_007781`
`VARIANT`	`1060 1060`	`1`	`E -> A.`	`VAR_020688`
`VARIANT`	`1139 1139`	`1`	`S -> I (in BC; unknown pathological significance).`	`VAR_020689`
`VARIANT`	`1140 1140`	`1`	`S -> G (in dbSNP:rs2227945 [NCBI]).`	`VAR_019945`
`VARIANT`	`1150 1150`	`1`	`P -> S (in BC).`	`VAR_007782`
`VARIANT`	`1183 1183`	`1`	`K -> R (common polymorphism; dbSNP:rs16942 [NCBI]).`	`VAR_007783`
`VARIANT`	`1187 1187`	`1`	`S -> I (in BC and BROVCA1).`	`VAR_020690`
`VARIANT`	`1200 1200`	`1`	`Q -> H (in BC and BROVCA1).`	`VAR_020691`
`VARIANT`	`1204 1204`	`1`	`R -> I (in BC).`	`VAR_020692`
`VARIANT`	`1207 1207`	`1`	`K -> N (in BC).`	`VAR_020693`
`VARIANT`	`1210 1210`	`1`	`E -> G (in BC; unknown pathological significance).`	`VAR_020694`
`VARIANT`	`1217 1217`	`1`	`S -> Y (in BC and BROVCA1).`	`VAR_020695`
`VARIANT`	`1219 1219`	`1`	`E -> D (unclassified).`	`VAR_007784`
`VARIANT`	`1226 1226`	`1`	`F -> L (in BROVCA1).`	`VAR_020696`
`VARIANT`	`1236 1236`	`1`	`N -> K (in dbSNP:rs28897687 [NCBI]).`	`VAR_052078`
`VARIANT`	`1243 1243`	`1`	`R -> G (in BROVCA1).`	`VAR_020697`
`VARIANT`	`1250 1250`	`1`	`E -> K (in dbSNP:rs28897686 [NCBI]).`	`VAR_052079`
`VARIANT`	`1297 1297`	`1`	`S -> P (in BC; unknown pathological significance).`	`VAR_020698`
`VARIANT`	`1347 1347`	`1`	`R -> G.`	`VAR_007785`
`VARIANT`	`1406 1406`	`1`	`K -> N (polymorphism; dbSNP:rs1800707 [NCBI]).`	`VAR_008761`
`VARIANT`	`1411 1411`	`1`	`M -> T (in ovarian cancer; unknown pathological significance).`	`VAR_020699`
`VARIANT`	`1431 1431`	`1`	`S -> P.`	`VAR_007786`
`VARIANT`	`1443 1443`	`1`	`R -> G (rare polymorphism).`	`VAR_007787`
`VARIANT`	`1443 1443`	`1`	`R -> Q (in dbSNP:rs4986849 [NCBI]).`	`VAR_020112`
`VARIANT`	`1512 1512`	`1`	`S -> I (in dbSNP:rs1800744 [NCBI]).`	`VAR_007788`
`VARIANT`	`1561 1561`	`1`	`T -> I (unclassified).`	`VAR_007789`
`VARIANT`	`1606 1606`	`1`	`K -> E (unclassified).`	`VAR_007790`
`VARIANT`	`1613 1613`	`1`	`S -> G (common polymorphism; dbSNP:rs1799966 [NCBI]).`	`VAR_007791`
`VARIANT`	`1620 1620`	`1`	`T -> A (in dbSNP:rs8176219 [NCBI]).`	`VAR_019946`
`VARIANT`	`1628 1628`	`1`	`M -> T (in some patients with sporadic breast cancer; unknown pathological significance; dbSNP:rs4986854 [NCBI]).`	`VAR_007793`
`VARIANT`	`1628 1628`	`1`	`M -> V (unclassified).`	`VAR_007792`
`VARIANT`	`1637 1637`	`1`	`P -> L (rare polymorphism).`	`VAR_007794`
`VARIANT`	`1641 1641`	`1`	`A -> P (in ovarian cancer; could be a polymorphism; dbSNP:rs1800726 [NCBI]).`	`VAR_008762`
`VARIANT`	`1652 1652`	`1`	`M -> I (rare polymorphism; dbSNP:rs1799967 [NCBI]).`	`VAR_007795 [3D]`
`VARIANT`	`1662 1662`	`1`	`F -> C (in dbSNP:rs28897695 [NCBI]).`	`VAR_052080 [3D]`
`VARIANT`	`1665 1665`	`1`	`V -> M.`	`VAR_020700 [3D]`
`VARIANT`	`1690 1690`	`1`	`K -> Q (in some patients with sporadic breast cancer; unknown pathological significance).`	`VAR_020701 [3D]`
`VARIANT`	`1692 1692`	`1`	`D -> N (in ovarian cancer; could be a polymorphism).`	`VAR_008763 [3D]`
`VARIANT`	`1697 1697`	`1`	`C -> R (in ovarian cancer).`	`VAR_020702 [3D]`
`VARIANT`	`1699 1699`	`1`	`R -> W (in ovarian cancer).`	`VAR_020703 [3D]`
`VARIANT`	`1708 1708`	`1`	`A -> E (in BC; abolishes ACACA binding).`	`VAR_007796 [3D]`
`VARIANT`	`1713 1713`	`1`	`V -> G.`	`VAR_007797 [3D]`
`VARIANT`	`1749 1749`	`1`	`P -> R (in ovarian cancer; could be a polymorphism; abolishes ACACA binding and reduces BRIP1 binding).`	`VAR_007798 [3D]`
`VARIANT`	`1775 1775`	`1`	`M -> R (in BC; abolishes ACACA and BRIP1 binding).`	`VAR_007799 [3D]`
`VARIANT`	`1776 1776`	`1`	`P -> S (in ovarian cancer; could be a polymorphism; dbSNP:rs1800757 [NCBI]).`	`VAR_008764 [3D]`
`VARIANT`	`1786 1786`	`1`	`L -> P (in BROVCA1; unknown pathological significance).`	`VAR_020704 [3D]`
`VARIANT`	`1812 1812`	`1`	`P -> S (in ovarian cancer; could be a polymorphism; dbSNP:rs1800751 [NCBI]).`	`VAR_008765 [3D]`
`MUTAGEN`	`71 71`		`R->G: No effect on interaction with BAP1.`
`MUTAGEN`	`1143 1143`		`S->A: Reduces in vitro phosphorylation by ATR.`
`MUTAGEN`	`1239 1239`		`S->A: No effect on in vitro phosphorylation by ATR.`
`MUTAGEN`	`1280 1280`		`S->A: Reduces in vitro phosphorylation by ATR.`
`MUTAGEN`	`1298 1298`		`S->A: No effect on in vitro phosphorylation by ATR.`
`MUTAGEN`	`1330 1330`		`S->A: No effect on in vitro phosphorylation by ATR.`
`MUTAGEN`	`1387 1387`		`S->A: Loss of IR-induced S-phase checkpoint. Reduces in vitro phosphorylation by ATR.`
`MUTAGEN`	`1394 1394`		`T->A: Reduces in vitro phosphorylation by ATR.`
`MUTAGEN`	`1423 1423`		`S->A: Inhibition of the IR-induced G2 arrest. Reduces phosphorylation by ATR.`
`MUTAGEN`	`1457 1457`		`S->A: Reduces in vitro phosphorylation by ATR.`
`MUTAGEN`	`1466 1466`		`S->A: No effect on in vitro phosphorylation by ATR.`
`MUTAGEN`	`1524 1524`		`S->A: No change in IR S-phase delay; when associated with A-1387. No effect on in vitro phosphorylation by ATR.`
`MUTAGEN`	`1720 1720`		`T->A: No effect on in vitro phosphorylation by ATR.`
`MUTAGEN`	`1755 1755`		`S->A: No effect on in vitro phosphorylation by ATR.`
`CONFLICT`	`89 89`		`I -> T (in Ref. 4; AAB61673).`
`CONFLICT`	`148 148`		`Missing (in Ref. 4; AAB61673).`
`CONFLICT`	`253 253`		`A -> V (in Ref. 3; AAC00049).`
`CONFLICT`	`1077 1077`		`G -> R (in Ref. 4; AAB61673).`
`CONFLICT`	`1426 1426`		`S -> P (in Ref. 3; AAC00049).`
`CONFLICT`	`1453 1453`		`Missing (in Ref. 3; AAC00049).`
`HELIX`	`3 5`	`3`
`HELIX`	`8 21`	`14`
`STRAND`	`25 27`	`3`
`HELIX`	`46 53`	`8`
`STRAND`	`54 58`	`5`
`TURN`	`62 64`	`3`
`TURN`	`70 72`	`3`
`STRAND`	`78 80`	`3`
`HELIX`	`81 96`	`16`
`STRAND`	`1651 1656`	`6`
`HELIX`	`1659 1672`	`14`
`STRAND`	`1686 1689`	`4`
`STRAND`	`1695 1697`	`3`
`HELIX`	`1701 1708`	`8`
`STRAND`	`1712 1715`	`4`
`HELIX`	`1717 1724`	`8`
`HELIX`	`1731 1734`	`4`
`TURN`	`1740 1742`	`3`
`HELIX`	`1748 1753`	`6`
`TURN`	`1760 1763`	`4`
`STRAND`	`1765 1768`	`4`
`STRAND`	`1773 1775`	`3`
`HELIX`	`1777 1786`	`10`
`HELIX`	`1795 1797`	`3`
`STRAND`	`1806 1810`	`5`
`HELIX`	`1812 1814`	`3`
`HELIX`	`1819 1822`	`4`
`TURN`	`1825 1827`	`3`
`STRAND`	`1832 1834`	`3`
`HELIX`	`1835 1844`	`10`
`HELIX`	`1851 1853`	`3`

Sequence information

Length: 1863 AA [This is the length of the unprocessed precursor]

Molecular weight: 207721 Da [This is the MW of the unprocessed precursor]

CRC64: 89C6D83FF56312AF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDLSALRVEE VQNVINAMQK ILECPICLEL IKEPVSTKCD HIFCKFCMLK LLNQKKGPSQ 

        70         80         90        100        110        120 
CPLCKNDITK RSLQESTRFS QLVEELLKII CAFQLDTGLE YANSYNFAKK ENNSPEHLKD 

       130        140        150        160        170        180 
EVSIIQSMGY RNRAKRLLQS EPENPSLQET SLSVQLSNLG TVRTLRTKQR IQPQKTSVYI 

       190        200        210        220        230        240 
ELGSDSSEDT VNKATYCSVG DQELLQITPQ GTRDEISLDS AKKAACEFSE TDVTNTEHHQ 

       250        260        270        280        290        300 
PSNNDLNTTE KRAAERHPEK YQGSSVSNLH VEPCGTNTHA SSLQHENSSL LLTKDRMNVE 

       310        320        330        340        350        360 
KAEFCNKSKQ PGLARSQHNR WAGSKETCND RRTPSTEKKV DLNADPLCER KEWNKQKLPC 

       370        380        390        400        410        420 
SENPRDTEDV PWITLNSSIQ KVNEWFSRSD ELLGSDDSHD GESESNAKVA DVLDVLNEVD 

       430        440        450        460        470        480 
EYSGSSEKID LLASDPHEAL ICKSERVHSK SVESNIEDKI FGKTYRKKAS LPNLSHVTEN 

       490        500        510        520        530        540 
LIIGAFVTEP QIIQERPLTN KLKRKRRPTS GLHPEDFIKK ADLAVQKTPE MINQGTNQTE 

       550        560        570        580        590        600 
QNGQVMNITN SGHENKTKGD SIQNEKNPNP IESLEKESAF KTKAEPISSS ISNMELELNI 

       610        620        630        640        650        660 
HNSKAPKKNR LRRKSSTRHI HALELVVSRN LSPPNCTELQ IDSCSSSEEI KKKKYNQMPV 

       670        680        690        700        710        720 
RHSRNLQLME GKEPATGAKK SNKPNEQTSK RHDSDTFPEL KLTNAPGSFT KCSNTSELKE 

       730        740        750        760        770        780 
FVNPSLPREE KEEKLETVKV SNNAEDPKDL MLSGERVLQT ERSVESSSIS LVPGTDYGTQ 

       790        800        810        820        830        840 
ESISLLEVST LGKAKTEPNK CVSQCAAFEN PKGLIHGCSK DNRNDTEGFK YPLGHEVNHS 

       850        860        870        880        890        900 
RETSIEMEES ELDAQYLQNT FKVSKRQSFA PFSNPGNAEE ECATFSAHSG SLKKQSPKVT 

       910        920        930        940        950        960 
FECEQKEENQ GKNESNIKPV QTVNITAGFP VVGQKDKPVD NAKCSIKGGS RFCLSSQFRG 

       970        980        990       1000       1010       1020 
NETGLITPNK HGLLQNPYRI PPLFPIKSFV KTKCKKNLLE ENFEEHSMSP EREMGNENIP 

      1030       1040       1050       1060       1070       1080 
STVSTISRNN IRENVFKEAS SSNINEVGSS TNEVGSSINE IGSSDENIQA ELGRNRGPKL 

      1090       1100       1110       1120       1130       1140 
NAMLRLGVLQ PEVYKQSLPG SNCKHPEIKK QEYEEVVQTV NTDFSPYLIS DNLEQPMGSS 

      1150       1160       1170       1180       1190       1200 
HASQVCSETP DDLLDDGEIK EDTSFAENDI KESSAVFSKS VQKGELSRSP SPFTHTHLAQ 

      1210       1220       1230       1240       1250       1260 
GYRRGAKKLE SSEENLSSED EELPCFQHLL FGKVNNIPSQ STRHSTVATE CLSKNTEENL 

      1270       1280       1290       1300       1310       1320 
LSLKNSLNDC SNQVILAKAS QEHHLSEETK CSASLFSSQC SELEDLTANT NTQDPFLIGS 

      1330       1340       1350       1360       1370       1380 
SKQMRHQSES QGVGLSDKEL VSDDEERGTG LEENNQEEQS MDSNLGEAAS GCESETSVSE 

      1390       1400       1410       1420       1430       1440 
DCSGLSSQSD ILTTQQRDTM QHNLIKLQQE MAELEAVLEQ HGSQPSNSYP SIISDSSALE 

      1450       1460       1470       1480       1490       1500 
DLRNPEQSTS EKAVLTSQKS SEYPISQNPE GLSADKFEVS ADSSTSKNKE PGVERSSPSK 

      1510       1520       1530       1540       1550       1560 
CPSLDDRWYM HSCSGSLQNR NYPSQEELIK VVDVEEQQLE ESGPHDLTET SYLPRQDLEG 

      1570       1580       1590       1600       1610       1620 
TPYLESGISL FSDDPESDPS EDRAPESARV GNIPSSTSAL KVPQLKVAES AQSPAAAHTT 

      1630       1640       1650       1660       1670       1680 
DTAGYNAMEE SVSREKPELT ASTERVNKRM SMVVSGLTPE EFMLVYKFAR KHHITLTNLI 

      1690       1700       1710       1720       1730       1740 
TEETTHVVMK TDAEFVCERT LKYFLGIAGG KWVVSYFWVT QSIKERKMLN EHDFEVRGDV 

      1750       1760       1770       1780       1790       1800 
VNGRNHQGPK RARESQDRKI FRGLEICCYG PFTNMPTDQL EWMVQLCGAS VVKELSSFTL 

      1810       1820       1830       1840       1850       1860 
GTGVHPIVVV QPDAWTEDNG FHAIGQMCEA PVVTREWVLD SVALYQCQEL DTYLIPQIPH 


SHY

P38398 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools