Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Breast cancer type 2 susceptibility protein (Fanconi anemia group D1 protein)

 BRCA2_HUMAN             Reviewed;        3418 AA.
P51587; O00183; O15008; Q13879; Q5TBJ7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
11-NOV-2015, sequence version 3.
30-AUG-2017, entry version 197.
RecName: Full=Breast cancer type 2 susceptibility protein;
AltName: Full=Fanconi anemia group D1 protein;
Name=BRCA2; Synonyms=FACD, FANCD1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8524414; DOI=10.1038/378789a0;
Wooster R., Bignell G., Lancaster J., Swift S., Seal S., Mangion J.,
Collins N., Gregory S., Gumbs C., Micklem G., Barfoot R., Hamoudi R.,
Patel S., Rice C., Biggs P., Hashim Y., Smith A., Connor F.,
Arason A., Gudmundsson J., Ficenec D., Kelsell D., Ford D., Tonin P.,
Bishop D.T., Spurr N.K., Ponder B.A.J., Eeles R., Peto J., Devilee P.,
Cornelisse C., Lynch H., Narod S., Lenoir G., Egilsson V.,
Barkadottir R.B., Easton D.F., Bentley D.R., Futreal P.A.,
Ashworth A., Stratton M.R.;
"Identification of the breast cancer susceptibility gene BRCA2.";
Nature 378:789-792(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS HIS-372 AND PHE-599.
PubMed=8589730; DOI=10.1038/ng0396-333;
Tavtigian S.V., Simard J., Rommens J., Couch F., Shattuck-Eidens D.,
Neuhausen S., Merajver S., Thorlacius S., Offit K., Stoppa-Lyonnet D.,
Belanger C., Bell R., Berry S., Bogden R., Chen Q., Davis T.,
Dumont M., Frye C., Hattier T., Jammulapati S., Janecki T., Jiang P.,
Kehrer R., Leblanc J.-F., Mitchell J.T., McArthur-Morrison J.,
Nguyen K., Peng Y., Samson C., Schroeder M., Snyder S.C., Steele L.,
Stringfellow M., Stroup C., Swedlund B., Swensen J., Teng D.,
Thomas A., Tran T., Tran T., Tranchant M., Weaver-Feldhaus J.,
Wong A.K.C., Shizuya H., Eyfjord J.E., Cannon-Albright L., Labrie F.,
Skolnick M.H., Weber B., Kamb A., Goldar D.E.;
"The complete BRCA2 gene and mutations in chromosome 13q-linked
kindreds.";
Nat. Genet. 12:333-337(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-289; GLN-322;
HIS-372; VAL-784; SER-929; PHE-976; ILE-987; ASP-991; ASN-1561;
LYS-1880; MET-1915; PHE-2138; ARG-2162; ARG-2440; VAL-2466; THR-2490;
PRO-2835; ALA-2856; PHE-2944; THR-2951; ILE-3244 AND VAL-3412.
NIEHS SNPs program;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[5]
INVOLVEMENT IN PNCA2.
PubMed=9140390; DOI=10.1038/ng0597-17;
Ozcelik H., Schmocker B., Di Nicola N., Shi X.H., Langer B., Moore M.,
Taylor B.R., Narod S.A., Darlington G., Andrulis I.L., Gallinger S.,
Redston M.;
"Germline BRCA2 6174delT mutations in Ashkenazi Jewish pancreatic
cancer patients.";
Nat. Genet. 16:17-18(1997).
[6]
INTERACTION WITH SEM1.
PubMed=10373512; DOI=10.1128/MCB.19.7.4633;
Marston N.J., Richards W.J., Hughes D., Bertwistle D., Marshall C.J.,
Ashworth A.;
"Interaction between the product of the breast cancer susceptibility
gene BRCA2 and DSS1, a protein functionally conserved from yeast to
mammals.";
Mol. Cell. Biol. 19:4633-4642(1999).
[7]
FUNCTION, AND INTERACTION WITH FANCD2.
PubMed=15115758; DOI=10.1093/hmg/ddh135;
Hussain S., Wilson J.B., Medhurst A.L., Hejna J., Witt E., Ananth S.,
Davies A., Masson J.-Y., Moses R., West S.C., de Winter J.P.,
Ashworth A., Jones N.J., Mathew C.G.;
"Direct interaction of FANCD2 with BRCA2 in DNA damage response
pathways.";
Hum. Mol. Genet. 13:1241-1248(2004).
[8]
FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH FANCD2.
PubMed=15199141; DOI=10.1128/MCB.24.13.5850-5862.2004;
Wang X.Z., Andreassen P.R., D'Andrea A.D.;
"Functional interaction of monoubiquitinated FANCD2 and BRCA2/FANCD1
in chromatin.";
Mol. Cell. Biol. 24:5850-5862(2004).
[9]
UBIQUITINATION, DEUBIQUITINATION, AND INTERACTION WITH USP11.
PubMed=15314155; DOI=10.1128/MCB.24.17.7444-7455.2004;
Schoenfeld A.R., Apgar S., Dolios G., Wang R., Aaronson S.A.;
"BRCA2 is ubiquitinated in vivo and interacts with USP11, a
deubiquitinating enzyme that exhibits prosurvival function in the
cellular response to DNA damage.";
Mol. Cell. Biol. 24:7444-7455(2004).
[10]
INVOLVEMENT IN GLM3.
PubMed=15689453; DOI=10.1136/jmg.2004.022673;
The famillial Wilms tumor collaboration;
Reid S., Renwick A., Seal S., Baskcomb L., Barfoot R., Jayatilake H.,
Pritchard-Jones K., Stratton M.R., Ridolfi-Luethy A., Rahman N.;
"Biallelic BRCA2 mutations are associated with multiple malignancies
in childhood including familial Wilms tumour.";
J. Med. Genet. 42:147-151(2005).
[11]
FUNCTION.
PubMed=15671039; DOI=10.1074/jbc.M414669200;
Ohashi A., Zdzienicka M.Z., Chen J., Couch F.J.;
"FANCD2 functions independently of BRCA2 and RAD51 associated
homologous recombination in response to DNA damage.";
J. Biol. Chem. 280:14877-14883(2005).
[12]
PHOSPHORYLATION AT SER-3291 BY CDK2, INTERACTION WITH RAD51, AND
MUTAGENESIS OF SER-3291.
PubMed=15800615; DOI=10.1038/nature03404;
Esashi F., Christ N., Gannon J., Liu Y., Hunt T., Jasin M., West S.C.;
"CDK-dependent phosphorylation of BRCA2 as a regulatory mechanism for
recombinational repair.";
Nature 434:598-604(2005).
[13]
INTERACTION WITH WDR16.
PubMed=15967112; DOI=10.1593/neo.04544;
Silva F.P., Hamamoto R., Nakamura Y., Furukawa Y.;
"WDRPUH, a novel WD-repeat-containing protein, is highly expressed in
human hepatocellular carcinoma and involved in cell proliferation.";
Neoplasia 7:348-355(2005).
[14]
INTERACTION WITH PALB2, AND CHARACTERIZATION OF VARIANTS BC ARG-25;
CYS-31 AND ARG-31.
PubMed=16793542; DOI=10.1016/j.molcel.2006.05.022;
Xia B., Sheng Q., Nakanishi K., Ohashi A., Wu J., Christ N., Liu X.,
Jasin M., Couch F.J., Livingston D.M.;
"Control of BRCA2 cellular and clinical functions by a nuclear
partner, PALB2.";
Mol. Cell 22:719-729(2006).
[15]
INTERACTION WITH SEM1.
PubMed=16205630; DOI=10.1038/sj.onc.1209153;
Li J., Zou C., Bai Y., Wazer D.E., Band V., Gao Q.;
"DSS1 is required for the stability of BRCA2.";
Oncogene 25:1186-1194(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-755, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[17]
INTERACTION WITH FANCD2; FANCG AND XRCC3.
PubMed=18212739; DOI=10.1038/sj.onc.1211034;
Wilson J.B., Yamamoto K., Marriott A.S., Hussain S., Sung P.,
Hoatlin M.E., Mathew C.G., Takata M., Thompson L.H., Kupfer G.M.,
Jones N.J.;
"FANCG promotes formation of a newly identified protein complex
containing BRCA2, FANCD2 and XRCC3.";
Oncogene 27:3641-3652(2008).
[18]
FUNCTION IN RAD51-DEPENDENT DNA REPAIR, PHOSPHORYLATION AT THR-3387 BY
CHEK1 AND CHEK2, MUTAGENESIS OF THR-3387, AND INTERACTION WITH RAD51.
PubMed=18317453; DOI=10.1038/onc.2008.17;
Bahassi E.M., Ovesen J.L., Riesenberg A.L., Bernstein W.Z.,
Hasty P.E., Stambrook P.J.;
"The checkpoint kinases Chk1 and Chk2 regulate the functional
associations between hBRCA2 and Rad51 in response to DNA damage.";
Oncogene 27:3977-3985(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A BRCA
COMPLEX WITH BRCA1 AND PALB2.
PubMed=19369211; DOI=10.1073/pnas.0811159106;
Sy S.M., Huen M.S., Chen J.;
"PALB2 is an integral component of the BRCA complex required for
homologous recombination repair.";
Proc. Natl. Acad. Sci. U.S.A. 106:7155-7160(2009).
[20]
FUNCTION, AND INTERACTION WITH RAD51.
PubMed=20729859; DOI=10.1038/nsmb.1904;
Liu J., Doty T., Gibson B., Heyer W.D.;
"Human BRCA2 protein promotes RAD51 filament formation on RPA-covered
single-stranded DNA.";
Nat. Struct. Mol. Biol. 17:1260-1262(2010).
[21]
FUNCTION, AND SUBUNIT.
PubMed=20729858; DOI=10.1038/nsmb.1905;
Thorslund T., McIlwraith M.J., Compton S.A., Lekomtsev S.,
Petronczki M., Griffith J.D., West S.C.;
"The breast cancer tumor suppressor BRCA2 promotes the specific
targeting of RAD51 to single-stranded DNA.";
Nat. Struct. Mol. Biol. 17:1263-1265(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH
RAD51 AND DMC1.
PubMed=20729832; DOI=10.1038/nature09399;
Jensen R.B., Carreira A., Kowalczykowski S.C.;
"Purified human BRCA2 stimulates RAD51-mediated recombination.";
Nature 467:678-683(2010).
[23]
FUNCTION, AND INTERACTION WITH ROCK2 AND NPM1.
PubMed=21084279; DOI=10.1158/0008-5472.CAN-10-0030;
Wang H.F., Takenaka K., Nakanishi A., Miki Y.;
"BRCA2 and nucleophosmin coregulate centrosome amplification and form
a complex with the Rho effector kinase ROCK2.";
Cancer Res. 71:68-77(2011).
[24]
SUBCELLULAR LOCATION.
PubMed=21276791; DOI=10.1016/j.yexcr.2011.01.021;
Cappelli E., Townsend S., Griffin C., Thacker J.;
"Homologous recombination proteins are associated with centrosomes and
are required for mitotic stability.";
Exp. Cell Res. 317:1203-1213(2011).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-445; SER-492;
SER-1970; THR-2035; SER-2095 AND SER-3319, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
INTERACTION WITH SEM1, CHARACTERIZATION OF VARIANT BC HIS-2723,
MUTAGENESIS OF TRP-2725, NUCLEAR EXPORT SIGNAL, AND SUBCELLULAR
LOCATION.
PubMed=24013206; DOI=10.1038/nsmb.2666;
Jeyasekharan A.D., Liu Y., Hattori H., Pisupati V., Jonsdottir A.B.,
Rajendra E., Lee M., Sundaramoorthy E., Schlachter S., Kaminski C.F.,
Ofir-Rosenfeld Y., Sato K., Savill J., Ayoub N., Venkitaraman A.R.;
"A cancer-associated BRCA2 mutation reveals masked nuclear export
signals controlling localization.";
Nat. Struct. Mol. Biol. 20:1191-1198(2013).
[27]
INTERACTION WITH PALB2, AND IDENTIFICATION IN A PALB2-CONTAINING HR
COMPLEX.
PubMed=24141787; DOI=10.1038/onc.2013.421;
Park J.Y., Singh T.R., Nassar N., Zhang F., Freund M., Hanenberg H.,
Meetei A.R., Andreassen P.R.;
"Breast cancer-associated missense mutants of the PALB2 WD40 domain,
which directly binds RAD51C, RAD51 and BRCA2, disrupt DNA repair.";
Oncogene 33:4803-4812(2014).
[28]
FUNCTION, AND INTERACTION WITH POLH.
PubMed=24485656; DOI=10.1016/j.celrep.2014.01.009;
Buisson R., Niraj J., Pauty J., Maity R., Zhao W., Coulombe Y.,
Sung P., Masson J.Y.;
"Breast cancer proteins PALB2 and BRCA2 stimulate polymerase eta in
recombination-associated DNA synthesis at blocked replication forks.";
Cell Rep. 6:553-564(2014).
[29]
FUNCTION IN R-LOOP PROCESSING, AND INTERACTION WITH SEM1 AND PCID2.
PubMed=24896180; DOI=10.1038/nature13374;
Bhatia V., Barroso S.I., Garcia-Rubio M.L., Tumini E.,
Herrera-Moyano E., Aguilera A.;
"BRCA2 prevents R-loop accumulation and associates with TREX-2 mRNA
export factor PCID2.";
Nature 511:362-365(2014).
[30]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1519-1551 IN COMPLEX WITH
RAD51.
PubMed=12442171; DOI=10.1038/nature01230;
Pellegrini L., Yu D.S., Lo T., Anand S., Lee M., Blundell T.L.,
Venkitaraman A.R.;
"Insights into DNA recombination from the structure of a RAD51-BRCA2
complex.";
Nature 420:287-293(2002).
[31]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 21-39 IN COMPLEX WITH PALB2.
PubMed=19609323; DOI=10.1038/embor.2009.126;
Oliver A.W., Swift S., Lord C.J., Ashworth A., Pearl L.H.;
"Structural basis for recruitment of BRCA2 by PALB2.";
EMBO Rep. 10:990-996(2009).
[32]
VARIANT OVARIAN CANCER HIS-2787, AND VARIANTS HIS-372; MET-1915 AND
VAL-2466.
PubMed=8665505;
Takahashi H., Chiu H.-C., Bandera C.A., Behbakht K., Liu P.C.,
Couch F.J., Weber B.L., LiVolsi V.A., Furusato M., Rebane B.A.,
Cardonick A., Benjamin I., Morgan M.A., King S.A., Mikuta J.J.,
Rubin S.C., Boyd J.;
"Mutations of the BRCA2 gene in ovarian carcinomas.";
Cancer Res. 56:2738-2741(1996).
[33]
VARIANTS HIS-372; ASP-991; SER-1147; MET-1915 AND CYS-2034.
PubMed=8673091; DOI=10.1038/ng0596-123;
Couch F.J., Farid L.M., Deshano M.L., Tavtigian S.V., Calzone K.,
Campeau L., Peng Y., Bogden B., Chen Q., Neuhausen S.,
Shattuck-Eidens D., Godwin A.K., Daly M., Radford D.M., Sedlacek S.,
Rommens J., Simard J., Garber J., Merajver S., Weber B.L.;
"BRCA2 germline mutations in male breast cancer cases and breast
cancer families.";
Nat. Genet. 13:123-125(1996).
[34]
VARIANT GLU-3095.
PubMed=8640235; DOI=10.1038/ng0696-238;
Lancaster J.M., Wooster R., Mangion J., Phelan C.M., Cochran C.,
Gumbs C., Seal S., Barfoot R., Collins N., Bignell G., Patel S.,
Hamoudi R., Larsson C., Wiseman R.W., Berchuck A., Iglehart J.D.,
Marks J.R., Ashworth A., Stratton M.R., Futreal P.A.;
"BRCA2 mutations in primary breast and ovarian cancers.";
Nat. Genet. 13:238-240(1996).
[35]
VARIANTS.
PubMed=8640236; DOI=10.1038/ng0696-241;
Teng D.H.-F., Bogden R., Mitchell J., Baumgard M., Bell R., Berry S.,
Davis T., Ha P.C., Kehrer R., Jammulapati S., Chen Q., Offit K.,
Skolnick M.H., Tavtigian S.V., Jhanwar S., Swedlund B., Wong A.K.C.,
Kamb A.;
"Low incidence of BRCA2 mutations in breast carcinoma and other
cancers.";
Nat. Genet. 13:241-244(1996).
[36]
VARIANT BC ASN-2415.
PubMed=8640237; DOI=10.1038/ng0696-245;
Miki Y., Katagiri T., Kasumi F., Yoshimoto T., Nakamura Y.;
"Mutation analysis in the BRCA2 gene in primary breast cancers.";
Nat. Genet. 13:245-247(1996).
[37]
VARIANT BC ASP-2089, AND VARIANT VAL-3412.
PubMed=9150152;
Vehmanen P., Friedman L.S., Eerola H., Sarantaus L., Pyrhoenen S.,
Ponder B.A.J., Muhonen T., Nevanlinna H.;
"A low proportion of BRCA2 mutations in Finnish breast cancer
families.";
Am. J. Hum. Genet. 60:1050-1058(1997).
[38]
VARIANT BC/PANCREAS CANCER TRP-554.
PubMed=9654203; DOI=10.1007/s004390050738;
Ganguly T., Dhulipala R., Godmilow L., Ganguly A.;
"High throughput fluorescence-based conformation-sensitive gel
electrophoresis (F-CSGE) identifies six unique BRCA2 mutations and an
overall low incidence of BRCA2 mutations in high-risk BRCA1-negative
breast cancer families.";
Hum. Genet. 102:549-556(1998).
[39]
VARIANTS BC LEU-32; ARG-53; LEU-81; ARG-201; ALA-211; SER-222 AND
THR-3118.
PubMed=9609997; DOI=10.1007/s100380050035;
Katagiri T., Kasumi F., Yoshimoto M., Nomizu T., Asaishi K., Abe R.,
Tsuchiya A., Sugano M., Takai S., Yoneda M., Fukutomi T., Nanba K.,
Makita M., Okazaki H., Hirata K., Okazaki M., Furutsuma Y.,
Morishita Y., Iino Y., Karino T., Ayabe H., Hara S., Kajiwara T.,
Houga S., Shimizu T., Toda M., Yamazaki Y., Uchida T., Kunitomo K.,
Sonoo H., Kurebayashi J., Shimotsuma K., Nakamura Y., Miki Y.;
"High proportion of missense mutations of the BRCA1 and BRCA2 genes in
Japanese breast cancer families.";
J. Hum. Genet. 43:42-48(1998).
[40]
VARIANTS OVARIAN CANCER PRO-75; HIS-2502 AND HIS-3098.
PubMed=10486320; DOI=10.1086/302583;
Gayther S.A., Russell P., Harrington P., Antoniou A.C., Easton D.F.,
Ponder B.A.J.;
"The contribution of germline BRCA1 and BRCA2 mutations to familial
ovarian cancer: no evidence for other ovarian cancer-susceptibility
genes.";
Am. J. Hum. Genet. 65:1021-1029(1999).
[41]
VARIANTS HIS-289; HIS-372; ASP-991 AND VAL-3412.
PubMed=10323242; DOI=10.1007/s004390050936;
Li S.S.-L., Tseng H.-M., Yang T.-P., Liu C.-H., Teng S.-J.,
Huang H.-W., Chen L.-M., Kao H.-W., Chen J.H., Tseng J.-N., Chen A.,
Hou M.-F., Huang T.-J., Chang H.-T., Mok K.-T., Tsai J.-H.;
"Molecular characterization of germline mutations in the BRCA1 and
BRCA2 genes from breast cancer families in Taiwan.";
Hum. Genet. 104:201-204(1999).
[42]
VARIANTS BC, AND VARIANTS.
PubMed=9971877; DOI=10.1093/hmg/8.3.413;
Wagner T.M.U., Hirtenlehner K., Shen P., Moeslinger R., Muhr D.,
Fleischmann E., Concin H., Doeller W., Haid A., Lang A.H., Mayer P.,
Petru E., Ropp E., Langbauer G., Kubista E., Scheiner O.,
Underhill P., Mountain J., Stierer M., Zielinski C., Oefner P.;
"Global sequence diversity of BRCA2: analysis of 71 breast cancer
families and 95 control individuals of worldwide populations.";
Hum. Mol. Genet. 8:413-423(1999).
[43]
VARIANT BC ARG-326, AND VARIANT ILE-2728.
PubMed=10399947;
DOI=10.1002/(SICI)1097-0215(19990730)82:3<325::AID-IJC3>3.0.CO;2-G;
Sinilnikova O.M., Egan K.M., Quinn J.L., Boutrand L., Lenoir G.M.,
Stoppa-Lyonnet D., Desjardins L., Levy C., Goldgar D., Gragoudas E.S.;
"Germline brca2 sequence variants in patients with ocular melanoma.";
Int. J. Cancer 82:325-328(1999).
[44]
VARIANT HIS-372.
PubMed=11062481; DOI=10.1038/81691;
Healey C.S., Dunning A.M., Teare M.D., Chase D., Parker L., Burn J.,
Chang-Claude J., Mannermaa A., Kataja V., Huntsman D.G.,
Pharoah P.D.P., Luben R.N., Easton D.F., Ponder B.A.J.;
"A common variant in BRCA2 is associated with both breast cancer risk
and prenatal viability.";
Nat. Genet. 26:362-364(2000).
[45]
VARIANTS BC MET-729; ILE-2515 AND ILE-2728, AND VARIANTS HIS-289;
HIS-372; ASP-991; MET-1915 AND VAL-3412.
PubMed=10978364; DOI=10.1136/jmg.37.9.e17;
Plaschke J., Commer T., Jacobi C., Schackert H.K., Chang-Claude J.;
"BRCA2 germline mutations among early onset breast cancer patients
unselected for family history of the disease.";
J. Med. Genet. 37:E17-E17(2000).
[46]
VARIANTS BC ASN-1179; ILE-3124 AND GLU-3196, AND VARIANT TYR-1420.
PubMed=11139248;
DOI=10.1002/1098-1004(2001)17:1<73::AID-HUMU12>3.3.CO;2-F;
Kwiatkowska E., Teresiak M., Lamperska K.M., Karczewska A.,
Breborowicz D., Stawicka M., Godlewski D., Krzyzosiak W.J.,
Mackiewicz A.;
"BRCA2 germline mutations in male breast cancer patients in the Polish
population.";
Hum. Mutat. 17:73-73(2001).
[47]
VARIANTS BC THR-505; TYR-1730; HIS-2135 AND CYS-2222, AND VARIANT
LYS-1880.
PubMed=11241844; DOI=10.1002/humu.7;
Edwards S.M., Kote-Jarai Z., Hamoudi R., Eeles R.A.;
"An improved high throughput heteroduplex mutation detection system
for screening BRCA2 mutations-fluorescent mutation detection (F-MD).";
Hum. Mutat. 17:220-232(2001).
[48]
VARIANT BC ARG-2722.
PubMed=12145750; DOI=10.1086/342192;
Fackenthal J.D., Cartegni L., Krainer A.R., Olopade O.I.;
"BRCA2 T2722R is a deleterious allele that causes exon skipping.";
Am. J. Hum. Genet. 71:625-631(2002).
[49]
ERRATUM.
Fackenthal J.D., Cartegni L., Krainer A.R., Olopade O.I.;
Am. J. Hum. Genet. 73:1477-1477(2002).
[50]
VARIANTS BC CYS-2072; CYS-2094 AND ASN-2128.
PubMed=12373604; DOI=10.1038/sj.bjc.6600562;
Jakubowska A., Nej K., Huzarski T., Scott R.J., Lubinski J.;
"BRCA2 gene mutations in families with aggregations of breast and
stomach cancers.";
Br. J. Cancer 87:888-891(2002).
[51]
VARIANT THR-192.
PubMed=12097290;
Murphy K.M., Brune K.A., Griffin C., Sollenberger J.E., Petersen G.M.,
Bansal R., Hruban R.H., Kern S.E.;
"Evaluation of candidate genes MAP2K4, MADH4, ACVR1B, and BRCA2 in
familial pancreatic cancer: deleterious BRCA2 mutations in 17%.";
Cancer Res. 62:3789-3793(2002).
[52]
VARIANTS HIS-118; SER-315; ILE-1988; CYS-2842 AND SER-3300.
PubMed=11948123;
Hu N., Li G., Li W.-J., Wang C., Goldstein A.M., Tang Z.-Z.,
Roth M.J., Dawsey S.M., Huang J., Wang Q.-H., Ding T., Giffen C.,
Taylor P.R., Emmert-Buck M.R.;
"Infrequent mutation in the BRCA2 gene in esophageal squamous cell
carcinoma.";
Clin. Cancer Res. 8:1121-1126(2002).
[53]
VARIANTS ALA-598; TYR-1420; CYS-2034; ILE-2728 AND THR-2951.
PubMed=12215251; DOI=10.1089/10906570260199375;
Deffenbaugh A.M., Frank T.S., Hoffman M., Cannon-Albright L.,
Neuhausen S.L.;
"Characterization of common BRCA1 and BRCA2 variants.";
Genet. Test. 6:119-121(2002).
[54]
VARIANTS ASP-1593 AND SER-2706.
PubMed=12442273; DOI=10.1002/humu.9082;
Saxena S., Szabo C.I., Chopin S., Barjhoux L., Sinilnikova O.,
Lenoir G., Goldgar D.E., Bhatanager D.;
"BRCA1 and BRCA2 in Indian breast cancer patients.";
Hum. Mutat. 20:473-474(2002).
[55]
VARIANT BC ASN-2729, AND VARIANT VAL-3412.
PubMed=12442274; DOI=10.1002/humu.9083;
Zhi X., Szabo C., Chopin S., Suter N., Wang Q.-S., Ostrander E.A.,
Sinilnikova O.M., Lenoir G.M., Goldgar D., Shi Y.-R.;
"BRCA1 and BRCA2 sequence variants in Chinese breast cancer
families.";
Hum. Mutat. 20:474-474(2002).
[56]
VARIANTS BC CYS-42; ARG-613; LEU-2118; LEU-2293 AND ARG-2793, AND
VARIANT ILE-3374.
PubMed=12442275; DOI=10.1002/humu.9084;
Ruiz-Flores P., Sinilnikova O.M., Badzioch M.,
Calderon-Garciduenas A.L., Chopin S., Fabrice O.,
Gonzalez-Guerrero J.F., Szabo C., Lenoir G., Goldgar D.E.,
Barrera-Saldana H.A.;
"BRCA1 and BRCA2 mutation analysis of early-onset and familial breast
cancer cases in Mexico.";
Hum. Mutat. 20:474-475(2002).
[57]
VARIANTS BC TYR-1580 AND MET-1915.
PubMed=11948477; DOI=10.1002/ijc.10289;
Kwiatkowska E., Teresiak M., Breborowicz D., Mackiewicz A.;
"Somatic mutations in the BRCA2 gene and high frequency of allelic
loss of BRCA2 in sporadic male breast cancer.";
Int. J. Cancer 98:943-945(2002).
[58]
INVOLVEMENT IN FANCD1.
PubMed=12065746; DOI=10.1126/science.1073834;
Howlett N.G., Taniguchi T., Olson S., Cox B., Waisfisz Q.,
de Die-Smulders C., Persky N., Grompe M., Joenje H., Pals G.,
Ikeda H., Fox E.A., D'Andrea A.D.;
"Biallelic inactivation of BRCA2 in Fanconi anemia.";
Science 297:606-609(2002).
[59]
VARIANTS HIS-289; HIS-372; GLY-462; ASP-991; SER-1279; TYR-1420;
ASP-1771 AND VAL-2466.
PubMed=12552570; DOI=10.1002/humu.9110;
Hadjisavvas A., Charalambous E., Adamou A., Christodoulou C.G.,
Kyriacou K.;
"BRCA2 germline mutations in Cypriot patients with familial
breast/ovarian cancer.";
Hum. Mutat. 21:171-171(2003).
[60]
VARIANTS BC ILE-431; LYS-1036; ARG-1106 AND VAL-1524.
PubMed=12938098; DOI=10.1002/humu.9174;
Meyer P., Voigtlaender T., Bartram C.R., Klaes R.;
"Twenty-three novel BRCA1 and BRCA2 sequence alterations in breast
and/or ovarian cancer families in Southern Germany.";
Hum. Mutat. 22:259-259(2003).
[61]
VARIANTS PRO-582; PHE-1522 AND VAL-2044.
PubMed=12624724; DOI=10.1007/s100380300020;
Sakayori M., Kawahara M., Shiraishi K., Nomizu T., Shimada A.,
Kudo T., Abe R., Ohuchi N., Takenoshita S., Kanamaru R., Ishioka C.;
"Evaluation of the diagnostic accuracy of the stop codon (SC) assay
for identifying protein-truncating mutations in the BRCA1and
BRCA2genes in familial breast cancer.";
J. Hum. Genet. 48:130-137(2003).
[62]
VARIANTS CYS-2034 AND GLU-3076.
PubMed=12569143; DOI=10.1093/jnci/95.3.214;
Hahn S.A., Greenhalf B., Ellis I., Sina-Frey M., Rieder H., Korte B.,
Gerdes B., Kress R., Ziegler A., Raeburn J.A., Campra D.,
Gruetzmann R., Rehder H., Rothmund M., Schmiegel W., Neoptolemos J.P.,
Bartsch D.K.;
"BRCA2 germline mutations in familial pancreatic carcinoma.";
J. Natl. Cancer Inst. 95:214-221(2003).
[63]
VARIANT FANCD1 PRO-2510.
PubMed=14670928; DOI=10.1182/blood-2003-06-1970;
Hirsch B., Shimamura A., Moreau L., Baldinger S., Hag-alshiekh M.,
Bostrom B., Sencer S., D'Andrea A.D.;
"Association of biallelic BRCA2/FANCD1 mutations with spontaneous
chromosomal instability and solid tumors of childhood.";
Blood 103:2554-2559(2004).
[64]
VARIANTS BC SER-60; ARG-405; HIS-448; GLY-462; GLY-2275; ARG-2353;
LYS-2488; HIS-2723; ASN-2950; ILE-3013 AND HIS-3098, AND VARIANTS
ASP-991; ALA-2856 AND VAL-3412.
PubMed=15026808; DOI=10.1038/sj.bjc.6601656;
Claes K., Poppe B., Coene I., De Paepe A., Messiaen L.;
"BRCA1 and BRCA2 germline mutation spectrum and frequencies in Belgian
breast/ovarian cancer families.";
Br. J. Cancer 90:1244-1251(2004).
[65]
VARIANTS BC ILE-64; GLY-462; ASN-1690; ASP-1771; MET-1887; MET-1915
AND GLU-2456, AND VARIANTS HIS-289; HIS-372; ASP-991; SER-1279;
TYR-1420; CYS-2108 AND VAL-2466.
PubMed=15172753; DOI=10.1016/j.cancergencyto.2003.09.020;
Hadjisavvas A., Charalambous E., Adamou A., Neuhausen S.L.,
Christodoulou C.G., Kyriacou K.;
"Hereditary breast and ovarian cancer in Cyprus: identification of a
founder BRCA2 mutation.";
Cancer Genet. Cytogenet. 151:152-156(2004).
[66]
VARIANT OVARIAN CANCER CYS-42, AND VARIANTS SER-3063 AND VAL-3412.
PubMed=14746861; DOI=10.1016/j.ejca.2003.09.016;
Malander S., Ridderheim M., Masbaeck A., Loman N., Kristoffersson U.,
Olsson H., Nilbert M., Borg A.;
"One in 10 ovarian cancer patients carry germ line BRCA1 or BRCA2
mutations: results of a prospective study in Southern Sweden.";
Eur. J. Cancer 40:422-428(2004).
[67]
VARIANTS BC ILE-1679; ALA-1804; LYS-1901 AND LEU-2096.
PubMed=14722926; DOI=10.1002/humu.9213;
Valarmathi M.T., Sawhney M., Deo S.S.V., Shukla N.K., Das S.N.;
"Novel germline mutations in the BRCA1 and BRCA2 genes in Indian
breast and breast-ovarian cancer families.";
Hum. Mutat. 23:205-205(2004).
[68]
VARIANT ALA-225, AND CHARACTERIZATION OF VARIANT ALA-225.
PubMed=15300854; DOI=10.1002/humu.9267;
Sharp A., Pichert G., Lucassen A., Eccles D.;
"RNA analysis reveals splicing mutations and loss of expression
defects in MLH1 and BRCA1.";
Hum. Mutat. 24:272-272(2004).
[69]
VARIANTS BC THR-1445; VAL-1929 AND ALA-2031, AND VARIANTS HIS-289;
HIS-372; VAL-784; ASP-991 AND VAL-3412.
PubMed=15365993; DOI=10.1002/humu.9275;
Seo J.H., Cho D.-Y., Ahn S.-H., Yoon K.-S., Kang C.-S., Cho H.M.,
Lee H.S., Choe J.J., Choi C.W., Kim B.S., Shin S.W., Kim Y.H.,
Kim J.S., Son G.-S., Lee J.-B., Koo B.H.;
"BRCA1 and BRCA2 germline mutations in Korean patients with sporadic
breast cancer.";
Hum. Mutat. 24:350-350(2004).
[70]
VARIANTS LEU-1172; TYR-1420; PHE-2944; ASN-2950 AND ILE-3013.
PubMed=15635067; DOI=10.1136/jmg.2004.025056;
Kim S.-W., Lee C.S., Fey J.V., Borgen P.I., Boyd J.;
"Prevalence of BRCA2 mutations in a hospital based series of
unselected breast cancer cases.";
J. Med. Genet. 42:E5-E5(2005).
[71]
VARIANTS HIS-2336; CYS-2502; CYS-2626; PHE-2627; PRO-2653; LYS-2659;
VAL-2663; ARG-2722; GLY-2723; ASP-2748 AND GLU-3095.
PubMed=17924331; DOI=10.1086/521032;
Easton D.F., Deffenbaugh A.M., Pruss D., Frye C., Wenstrup R.J.,
Allen-Brady K., Tavtigian S.V., Monteiro A.N.A., Iversen E.S.,
Couch F.J., Goldgar D.E.;
"A systematic genetic assessment of 1,433 sequence variants of unknown
clinical significance in the BRCA1 and BRCA2 breast cancer-
predisposition genes.";
Am. J. Hum. Genet. 81:873-883(2007).
[72]
VARIANTS FANCD1 HIS-2336 AND CYS-2626.
PubMed=16825431; DOI=10.1136/jmg.2006.043257;
Alter B.P., Rosenberg P.S., Brody L.C.;
"Clinical and molecular features associated with biallelic mutations
in FANCD1/BRCA2.";
J. Med. Genet. 44:1-9(2007).
[73]
CHARACTERIZATION OF VARIANTS VAL-2663; GLY-2723 AND TRP-3052.
PubMed=20513136; DOI=10.1002/humu.21267;
Walker L.C., Whiley P.J., Couch F.J., Farrugia D.J., Healey S.,
Eccles D.M., Lin F., Butler S.A., Goff S.A., Thompson B.A.,
Lakhani S.R., Da Silva L.M., Tavtigian S.V., Goldgar D.E., Brown M.A.,
Spurdle A.B.;
"Detection of splicing aberrations caused by BRCA1 and BRCA2 sequence
variants encoding missense substitutions: implications for prediction
of pathogenicity.";
Hum. Mutat. 31:E1484-E1505(2010).
[74]
CHARACTERIZATION OF VARIANTS FANCD1 HIS-2336; PRO-2510 AND CYS-2626,
CHARACTERIZATION OF VARIANTS THR-2490 AND ASN-2729, FUNCTION, AND
INTERACTION WITH SEM1.
PubMed=21719596; DOI=10.1182/blood-2010-12-324541;
Biswas K., Das R., Alter B.P., Kuznetsov S.G., Stauffer S.,
North S.L., Burkett S., Brody L.C., Meyer S., Byrd R.A., Sharan S.K.;
"A comprehensive functional characterization of BRCA2 variants
associated with Fanconi anemia using mouse ES cell-based assay.";
Blood 118:2430-2442(2011).
[75]
VARIANTS LEU-606 AND TYR-1420.
PubMed=26566883; DOI=10.1136/jmedgenet-2015-103179;
Rafiullah R., Aslamkhan M., Paramasivam N., Thiel C., Mustafa G.,
Wiemann S., Schlesner M., Wade R.C., Rappold G.A., Berkel S.;
"Homozygous missense mutation in the LMAN2L gene segregates with
intellectual disability in a large consanguineous Pakistani family.";
J. Med. Genet. 53:138-144(2016).
-!- FUNCTION: Involved in double-strand break repair and/or homologous
recombination. Binds RAD51 and potentiates recombinational DNA
repair by promoting assembly of RAD51 onto single-stranded DNA
(ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded
DNA, enabling RAD51 to displace replication protein-A (RPA) from
ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP
hydrolysis. Part of a PALB2-scaffolded HR complex containing
RAD51C and which is thought to play a role in DNA repair by HR.
May participate in S phase checkpoint activation. Binds
selectively to ssDNA, and to ssDNA in tailed duplexes and
replication fork structures. May play a role in the extension step
after strand invasion at replication-dependent DNA double-strand
breaks; together with PALB2 is involved in both POLH localization
at collapsed replication forks and DNA polymerization activity. In
concert with NPM1, regulates centrosome duplication. Interacts
with the TREX-2 complex (transcription and export complex 2)
subunits PCID2 and SEM1, and is required to prevent R-loop-
associated DNA damage and thus transcription-associated genomic
instability. Silencing of BRCA2 promotes R-loop accumulation at
actively transcribed genes in replicating and non-replicating
cells, suggesting that BRCA2 mediates the control of R-loop
associated genomic instability, independently of its known role in
homologous recombination (PubMed:24896180).
{ECO:0000269|PubMed:15115758, ECO:0000269|PubMed:15199141,
ECO:0000269|PubMed:15671039, ECO:0000269|PubMed:18317453,
ECO:0000269|PubMed:20729832, ECO:0000269|PubMed:20729858,
ECO:0000269|PubMed:20729859, ECO:0000269|PubMed:21084279,
ECO:0000269|PubMed:21719596, ECO:0000269|PubMed:24485656,
ECO:0000269|PubMed:24896180}.
-!- SUBUNIT: Monomer and dimer. Interacts with RAD51; regulates RAD51
recruitment and function at sites of DNA repair. Interacts with
WDR16, USP11, DMC1, ROCK2 and NPM1. Interacts with SEM1; the
interaction masks a nuclear export signal in BRCA2. Interacts with
both nonubiquitinated and monoubiquitinated FANCD2; this complex
also includes XRCC3 and phosphorylated FANCG. Part of a BRCA
complex containing BRCA1, BRCA2 and PALB2. Interacts directly with
PALB2 which may serve as a scaffold for a HR complex containing
PALB2, BRCA2, RAD51C, RAD51 and XRCC3. Interacts with BRCA1 only
in the presence of PALB2 which serves as the bridging protein.
Interacts with POLH; the interaction is direct. Interacts with the
TREX-2 complex subunits PCID2 and SEM1 (PubMed:24896180,
PubMed:21719596). {ECO:0000269|PubMed:10373512,
ECO:0000269|PubMed:12442171, ECO:0000269|PubMed:15115758,
ECO:0000269|PubMed:15199141, ECO:0000269|PubMed:15314155,
ECO:0000269|PubMed:15800615, ECO:0000269|PubMed:15967112,
ECO:0000269|PubMed:16205630, ECO:0000269|PubMed:16793542,
ECO:0000269|PubMed:18212739, ECO:0000269|PubMed:18317453,
ECO:0000269|PubMed:19369211, ECO:0000269|PubMed:19609323,
ECO:0000269|PubMed:20729832, ECO:0000269|PubMed:20729858,
ECO:0000269|PubMed:20729859, ECO:0000269|PubMed:21084279,
ECO:0000269|PubMed:21719596, ECO:0000269|PubMed:24013206,
ECO:0000269|PubMed:24141787, ECO:0000269|PubMed:24485656,
ECO:0000269|PubMed:24896180}.
-!- INTERACTION:
Q14565:DMC1; NbExp=11; IntAct=EBI-79792, EBI-930865;
Q9BXW9:FANCD2; NbExp=16; IntAct=EBI-79792, EBI-359343;
Q9BXW9-2:FANCD2; NbExp=3; IntAct=EBI-79792, EBI-596878;
Q9P0W2:HMG20B; NbExp=8; IntAct=EBI-79792, EBI-713401;
Q86YC2:PALB2; NbExp=15; IntAct=EBI-79792, EBI-1222653;
Q9NTI5:PDS5B; NbExp=26; IntAct=EBI-79792, EBI-1175604;
Q9Y253:POLH; NbExp=6; IntAct=EBI-79792, EBI-2827270;
Q06609:RAD51; NbExp=36; IntAct=EBI-79792, EBI-297202;
P60896:SEM1; NbExp=8; IntAct=EBI-79792, EBI-79819;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24013206,
ECO:0000305|PubMed:21276791}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:21276791}.
-!- TISSUE SPECIFICITY: Highest levels of expression in breast and
thymus, with slightly lower levels in lung, ovary and spleen.
-!- PTM: Phosphorylated by ATM upon irradiation-induced DNA damage.
Phosphorylation by CHEK1 and CHEK2 regulates interaction with
RAD51. Phosphorylation at Ser-3291 by CDK1 and CDK2 is low in S
phase when recombination is active, but increases as cells
progress towards mitosis; this phosphorylation prevents homologous
recombination-dependent repair during S phase and G2 by inhibiting
RAD51 binding. {ECO:0000269|PubMed:15199141,
ECO:0000269|PubMed:15800615, ECO:0000269|PubMed:18317453}.
-!- PTM: Ubiquitinated in the absence of DNA damage; this does not
lead to proteasomal degradation. In contrast, ubiquitination in
response to DNA damage leads to proteasomal degradation.
{ECO:0000269|PubMed:15314155}.
-!- DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy
originating from breast epithelial tissue. Breast neoplasms can be
distinguished by their histologic pattern. Invasive ductal
carcinoma is by far the most common type. Breast cancer is
etiologically and genetically heterogeneous. Important genetic
factors have been indicated by familial occurrence and bilateral
involvement. Mutations at more than one locus can be involved in
different families or even in the same case.
{ECO:0000269|PubMed:10399947, ECO:0000269|PubMed:10978364,
ECO:0000269|PubMed:11139248, ECO:0000269|PubMed:11241844,
ECO:0000269|PubMed:11948477, ECO:0000269|PubMed:12145750,
ECO:0000269|PubMed:12373604, ECO:0000269|PubMed:12442274,
ECO:0000269|PubMed:12442275, ECO:0000269|PubMed:12938098,
ECO:0000269|PubMed:14722926, ECO:0000269|PubMed:15026808,
ECO:0000269|PubMed:15172753, ECO:0000269|PubMed:15365993,
ECO:0000269|PubMed:16793542, ECO:0000269|PubMed:24013206,
ECO:0000269|PubMed:8640237, ECO:0000269|PubMed:9150152,
ECO:0000269|PubMed:9609997, ECO:0000269|PubMed:9654203,
ECO:0000269|PubMed:9971877}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Pancreatic cancer 2 (PNCA2) [MIM:613347]: A malignant
neoplasm of the pancreas. Tumors can arise from both the exocrine
and endocrine portions of the pancreas, but 95% of them develop
from the exocrine portion, including the ductal epithelium, acinar
cells, connective tissue, and lymphatic tissue.
{ECO:0000269|PubMed:9140390}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Breast-ovarian cancer, familial, 2 (BROVCA2)
[MIM:612555]: A condition associated with familial predisposition
to cancer of the breast and ovaries. Characteristic features in
affected families are an early age of onset of breast cancer
(often before age 50), increased chance of bilateral cancers
(cancer that develop in both breasts, or both ovaries,
independently), frequent occurrence of breast cancer among men,
increased incidence of tumors of other specific organs, such as
the prostate. Note=Disease susceptibility is associated with
variations affecting the gene represented in this entry.
-!- DISEASE: Fanconi anemia complementation group D1 (FANCD1)
[MIM:605724]: A disorder affecting all bone marrow elements and
resulting in anemia, leukopenia and thrombopenia. It is associated
with cardiac, renal and limb malformations, dermal pigmentary
changes, and a predisposition to the development of malignancies.
At the cellular level it is associated with hypersensitivity to
DNA-damaging agents, chromosomal instability (increased chromosome
breakage) and defective DNA repair. {ECO:0000269|PubMed:12065746,
ECO:0000269|PubMed:14670928, ECO:0000269|PubMed:16825431,
ECO:0000269|PubMed:21719596}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Glioma 3 (GLM3) [MIM:613029]: Gliomas are benign or
malignant central nervous system neoplasms derived from glial
cells. They comprise astrocytomas and glioblastoma multiforme that
are derived from astrocytes, oligodendrogliomas derived from
oligodendrocytes and ependymomas derived from ependymocytes.
{ECO:0000269|PubMed:15689453}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=Fanconi Anemia Mutation Database;
URL="http://www2.rockefeller.edu/fanconi/genes/jumpd1";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/brca2/";
-!- WEB RESOURCE: Name=Wikipedia; Note=BRCA2 entry;
URL="https://en.wikipedia.org/wiki/BRCA2";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BRCA2ID164ch13q13.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X95152; CAA64484.1; -; Genomic_DNA.
EMBL; X95153; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95154; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95155; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95156; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95157; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95158; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95159; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95160; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95161; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95162; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95163; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95164; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95165; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95166; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95167; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95168; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95169; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95170; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95171; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95172; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95173; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95174; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95175; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95176; CAA64484.1; JOINED; Genomic_DNA.
EMBL; X95177; CAA64484.1; JOINED; Genomic_DNA.
EMBL; U43746; AAB07223.1; -; mRNA.
EMBL; AY436640; AAQ97181.1; -; Genomic_DNA.
EMBL; AL137247; CAI13195.1; -; Genomic_DNA.
EMBL; AL445212; CAI13195.1; JOINED; Genomic_DNA.
EMBL; AL445212; CAI40479.1; -; Genomic_DNA.
EMBL; AL137247; CAI40479.1; JOINED; Genomic_DNA.
EMBL; Z74739; CAA98995.2; -; Genomic_DNA.
EMBL; Z73359; CAA97728.1; -; Genomic_DNA.
CCDS; CCDS9344.1; -.
PIR; G02334; G02334.
RefSeq; NP_000050.2; NM_000059.3.
UniGene; Hs.34012; -.
PDB; 1N0W; X-ray; 1.70 A; B=1517-1551.
PDB; 3EU7; X-ray; 2.20 A; X=21-39.
PDBsum; 1N0W; -.
PDBsum; 3EU7; -.
ProteinModelPortal; P51587; -.
SMR; P51587; -.
BioGrid; 107142; 94.
DIP; DIP-24214N; -.
ELM; P51587; -.
IntAct; P51587; 28.
MINT; MINT-1540184; -.
STRING; 9606.ENSP00000369497; -.
iPTMnet; P51587; -.
PhosphoSitePlus; P51587; -.
BioMuta; BRCA2; -.
DMDM; 14424438; -.
EPD; P51587; -.
PaxDb; P51587; -.
PeptideAtlas; P51587; -.
PRIDE; P51587; -.
DNASU; 675; -.
Ensembl; ENST00000380152; ENSP00000369497; ENSG00000139618.
Ensembl; ENST00000544455; ENSP00000439902; ENSG00000139618.
GeneID; 675; -.
KEGG; hsa:675; -.
UCSC; uc001uub.2; human.
CTD; 675; -.
DisGeNET; 675; -.
GeneCards; BRCA2; -.
GeneReviews; BRCA2; -.
HGNC; HGNC:1101; BRCA2.
HPA; HPA026815; -.
MalaCards; BRCA2; -.
MIM; 114480; phenotype.
MIM; 600185; gene.
MIM; 605724; phenotype.
MIM; 612555; phenotype.
MIM; 613029; phenotype.
MIM; 613347; phenotype.
neXtProt; NX_P51587; -.
Orphanet; 1333; Familial pancreatic carcinoma.
Orphanet; 1331; Familial prostate cancer.
Orphanet; 84; Fanconi anemia.
Orphanet; 145; Hereditary breast and ovarian cancer syndrome.
Orphanet; 227535; Hereditary breast cancer.
Orphanet; 213524; Hereditary site-specific ovarian cancer syndrome.
Orphanet; 319462; Inherited cancer-predisposing syndrome due to biallelic BRCA2 mutations.
PharmGKB; PA25412; -.
eggNOG; KOG4751; Eukaryota.
eggNOG; ENOG410Y06W; LUCA.
HOGENOM; HOG000139693; -.
HOVERGEN; HBG050731; -.
InParanoid; P51587; -.
KO; K08775; -.
OrthoDB; EOG091G0C79; -.
TreeFam; TF105041; -.
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-HSA-912446; Meiotic recombination.
SignaLink; P51587; -.
SIGNOR; P51587; -.
EvolutionaryTrace; P51587; -.
GeneWiki; BRCA2; -.
GenomeRNAi; 675; -.
PRO; PR:P51587; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000139618; -.
CleanEx; HS_BRCA2; -.
ExpressionAtlas; P51587; baseline and differential.
Genevisible; P51587; HS.
GO; GO:0033593; C:BRCA2-MAGE-D1 complex; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000800; C:lateral element; IDA:MGI.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
GO; GO:0043015; F:gamma-tubulin binding; IPI:UniProtKB.
GO; GO:0010484; F:H3 histone acetyltransferase activity; IDA:UniProtKB.
GO; GO:0010485; F:H4 histone acetyltransferase activity; IDA:UniProtKB.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IDA:MGI.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0007569; P:cell aging; IEA:Ensembl.
GO; GO:0051298; P:centrosome duplication; IMP:UniProtKB.
GO; GO:0000910; P:cytokinesis; IDA:UniProtKB.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IEA:Ensembl.
GO; GO:0000731; P:DNA synthesis involved in DNA repair; TAS:Reactome.
GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
GO; GO:0070200; P:establishment of protein localization to telomere; IDA:BHF-UCL.
GO; GO:0008585; P:female gonad development; IEA:Ensembl.
GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
GO; GO:0001833; P:inner cell mass cell proliferation; IEA:Ensembl.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IMP:BHF-UCL.
GO; GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; IDA:UniProtKB.
GO; GO:0006289; P:nucleotide-excision repair; IMP:UniProtKB.
GO; GO:0001556; P:oocyte maturation; IEA:Ensembl.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0032465; P:regulation of cytokinesis; IEA:Ensembl.
GO; GO:0048478; P:replication fork protection; IEA:Ensembl.
GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
GO; GO:0010225; P:response to UV-C; IEA:Ensembl.
GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0000732; P:strand displacement; TAS:Reactome.
GO; GO:0000722; P:telomere maintenance via recombination; IEA:Ensembl.
InterPro; IPR015525; BRCA2.
InterPro; IPR015252; BRCA2_hlx.
InterPro; IPR015187; BRCA2_OB_1.
InterPro; IPR015188; BRCA2_OB_3.
InterPro; IPR002093; BRCA2_repeat.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR015205; Tower_dom.
PANTHER; PTHR11289; PTHR11289; 1.
Pfam; PF09169; BRCA-2_helical; 1.
Pfam; PF09103; BRCA-2_OB1; 1.
Pfam; PF09104; BRCA-2_OB3; 1.
Pfam; PF00634; BRCA2; 8.
Pfam; PF09121; Tower; 1.
PIRSF; PIRSF002397; BRCA2; 1.
SMART; SM01341; Tower; 1.
SUPFAM; SSF50249; SSF50249; 4.
SUPFAM; SSF81872; SSF81872; 1.
PROSITE; PS50138; BRCA2_REPEAT; 8.
1: Evidence at protein level;
3D-structure; Cell cycle; Complete proteome; Cytoplasm; Cytoskeleton;
Disease mutation; DNA damage; DNA recombination; DNA repair;
DNA-binding; Fanconi anemia; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Tumor suppressor; Ubl conjugation.
CHAIN 1 3418 Breast cancer type 2 susceptibility
protein.
/FTId=PRO_0000064984.
REPEAT 1002 1036 BRCA2 1.
REPEAT 1212 1246 BRCA2 2.
REPEAT 1421 1455 BRCA2 3.
REPEAT 1517 1551 BRCA2 4.
REPEAT 1664 1698 BRCA2 5.
REPEAT 1837 1871 BRCA2 6.
REPEAT 1971 2005 BRCA2 7.
REPEAT 2051 2085 BRCA2 8.
REGION 1 40 Interaction with PALB2.
REGION 639 1000 Interaction with NPM1.
{ECO:0000269|PubMed:21084279}.
REGION 1338 1781 Interaction with POLH.
{ECO:0000269|PubMed:24485656}.
REGION 1410 1595 Required for stimulation of POLH DNA
polymerization activity.
REGION 2350 2545 Interaction with FANCD2.
REGION 2481 2832 Interaction with SEM1.
{ECO:0000269|PubMed:10373512,
ECO:0000269|PubMed:16205630}.
MOTIF 2682 2698 Nuclear export signal; masked by
interaction with SEM1.
{ECO:0000269|PubMed:24013206}.
MOD_RES 70 70 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 445 445 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 755 755 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 1970 1970 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2035 2035 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2095 2095 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 3291 3291 Phosphoserine; by CDK1 and CDK2.
{ECO:0000269|PubMed:15800615}.
MOD_RES 3319 3319 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 3387 3387 Phosphothreonine; by CHEK1 and CHEK2.
{ECO:0000269|PubMed:18317453}.
VARIANT 25 25 G -> R (in BC; abolishes interaction with
PALB2). {ECO:0000269|PubMed:16793542}.
/FTId=VAR_028167.
VARIANT 31 31 W -> C (in BC; abolishes interaction with
PALB2). {ECO:0000269|PubMed:16793542}.
/FTId=VAR_028168.
VARIANT 31 31 W -> R (in BC; abolishes interaction with
PALB2). {ECO:0000269|PubMed:16793542}.
/FTId=VAR_028169.
VARIANT 32 32 F -> L (in BC).
{ECO:0000269|PubMed:9609997}.
/FTId=VAR_005085.
VARIANT 42 42 Y -> C (in BC and ovarian cancer; unknown
pathological significance;
dbSNP:rs4987046).
{ECO:0000269|PubMed:12442275,
ECO:0000269|PubMed:14746861}.
/FTId=VAR_020705.
VARIANT 53 53 K -> R (in BC).
{ECO:0000269|PubMed:9609997}.
/FTId=VAR_005086.
VARIANT 60 60 N -> S (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:15026808}.
/FTId=VAR_020706.
VARIANT 64 64 T -> I (in BC).
{ECO:0000269|PubMed:15172753}.
/FTId=VAR_032712.
VARIANT 75 75 A -> P (in ovarian cancer and renal
cancer; unknown pathological
significance; dbSNP:rs28897701).
{ECO:0000269|PubMed:10486320}.
/FTId=VAR_005087.
VARIANT 81 81 F -> L (in BC).
{ECO:0000269|PubMed:9609997}.
/FTId=VAR_005088.
VARIANT 108 108 N -> H.
/FTId=VAR_008766.
VARIANT 118 118 R -> H (in one patient with esophageal
carcinoma).
{ECO:0000269|PubMed:11948123}.
/FTId=VAR_032713.
VARIANT 192 192 M -> T (in one patient with pancreatic
cancer). {ECO:0000269|PubMed:12097290}.
/FTId=VAR_032714.
VARIANT 201 201 P -> R (in BC).
{ECO:0000269|PubMed:9609997}.
/FTId=VAR_005089.
VARIANT 211 211 V -> A (in BC).
{ECO:0000269|PubMed:9609997}.
/FTId=VAR_005090.
VARIANT 222 222 P -> S (in BC).
{ECO:0000269|PubMed:9609997}.
/FTId=VAR_005091.
VARIANT 225 225 T -> A (in one patient with BC; normal
RNA expression and splicing).
{ECO:0000269|PubMed:15300854}.
/FTId=VAR_032715.
VARIANT 289 289 N -> H (common polymorphism; was
originally thought to be linked to
ovarian cancer; dbSNP:rs766173).
{ECO:0000269|PubMed:10323242,
ECO:0000269|PubMed:10978364,
ECO:0000269|PubMed:12552570,
ECO:0000269|PubMed:15172753,
ECO:0000269|PubMed:15365993,
ECO:0000269|Ref.3}.
/FTId=VAR_005092.
VARIANT 315 315 C -> S (in one patient with esophageal
carcinoma; dbSNP:rs79483201).
{ECO:0000269|PubMed:11948123}.
/FTId=VAR_032716.
VARIANT 322 322 K -> Q (in dbSNP:rs11571640).
{ECO:0000269|Ref.3}.
/FTId=VAR_018908.
VARIANT 326 326 S -> R (in BC; dbSNP:rs28897706).
{ECO:0000269|PubMed:10399947}.
/FTId=VAR_032717.
VARIANT 327 327 K -> E (in BC; unknown pathological
significance).
/FTId=VAR_008767.
VARIANT 355 355 V -> L (in lung cancer).
/FTId=VAR_005093.
VARIANT 372 372 N -> H (common polymorphism; may be
associated with an increased risk of
breast cancer; dbSNP:rs144848).
{ECO:0000269|PubMed:10323242,
ECO:0000269|PubMed:10978364,
ECO:0000269|PubMed:11062481,
ECO:0000269|PubMed:12552570,
ECO:0000269|PubMed:15057823,
ECO:0000269|PubMed:15172753,
ECO:0000269|PubMed:15365993,
ECO:0000269|PubMed:8665505,
ECO:0000269|PubMed:8673091,
ECO:0000269|Ref.3}.
/FTId=VAR_005094.
VARIANT 405 405 G -> R (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:15026808}.
/FTId=VAR_020707.
VARIANT 431 431 T -> I (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:12938098}.
/FTId=VAR_020708.
VARIANT 448 448 R -> H (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:15026808}.
/FTId=VAR_020709.
VARIANT 462 462 E -> G (in BC; unknown pathological
significance; dbSNP:rs56403624).
{ECO:0000269|PubMed:12552570,
ECO:0000269|PubMed:15026808,
ECO:0000269|PubMed:15172753}.
/FTId=VAR_020710.
VARIANT 505 505 I -> T (in BC; dbSNP:rs28897708).
{ECO:0000269|PubMed:11241844}.
/FTId=VAR_032718.
VARIANT 513 513 K -> R (in dbSNP:rs28897709).
/FTId=VAR_056751.
VARIANT 554 554 C -> W (in BC and pancreas cancer).
{ECO:0000269|PubMed:9654203}.
/FTId=VAR_005095.
VARIANT 582 582 T -> P (in dbSNP:rs80358457).
{ECO:0000269|PubMed:12624724}.
/FTId=VAR_008768.
VARIANT 598 598 T -> A (in dbSNP:rs28897710).
{ECO:0000269|PubMed:12215251}.
/FTId=VAR_020711.
VARIANT 599 599 S -> F (in dbSNP:rs1046984).
{ECO:0000269|PubMed:8589730}.
/FTId=VAR_035436.
VARIANT 606 606 P -> L. {ECO:0000269|PubMed:26566883}.
/FTId=VAR_076440.
VARIANT 613 613 L -> R (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:12442275}.
/FTId=VAR_020712.
VARIANT 630 630 T -> I (in ovarian cancer).
/FTId=VAR_005096.
VARIANT 707 707 D -> Y (in dbSNP:rs80358487).
/FTId=VAR_008769.
VARIANT 728 728 D -> A (in BC).
/FTId=VAR_005097.
VARIANT 729 729 I -> M (in BC).
{ECO:0000269|PubMed:10978364}.
/FTId=VAR_032719.
VARIANT 784 784 M -> V (in dbSNP:rs11571653).
{ECO:0000269|PubMed:15365993,
ECO:0000269|Ref.3}.
/FTId=VAR_008770.
VARIANT 886 886 N -> I.
/FTId=VAR_008771.
VARIANT 929 929 L -> S (in dbSNP:rs2227943).
{ECO:0000269|Ref.3}.
/FTId=VAR_018909.
VARIANT 935 935 D -> N (in BC; unknown pathological
significance; dbSNP:rs28897716).
/FTId=VAR_008772.
VARIANT 976 976 S -> F (in dbSNP:rs11571656).
{ECO:0000269|Ref.3}.
/FTId=VAR_018910.
VARIANT 982 982 I -> L (in dbSNP:rs28897717).
/FTId=VAR_056752.
VARIANT 987 987 N -> I (in dbSNP:rs2227944).
{ECO:0000269|Ref.3}.
/FTId=VAR_018911.
VARIANT 991 991 N -> D (common polymorphism;
dbSNP:rs1799944).
{ECO:0000269|PubMed:10323242,
ECO:0000269|PubMed:10978364,
ECO:0000269|PubMed:12552570,
ECO:0000269|PubMed:15026808,
ECO:0000269|PubMed:15172753,
ECO:0000269|PubMed:15365993,
ECO:0000269|PubMed:8673091,
ECO:0000269|Ref.3}.
/FTId=VAR_005098.
VARIANT 1036 1036 E -> K (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:12938098}.
/FTId=VAR_020713.
VARIANT 1106 1106 S -> R (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:12938098}.
/FTId=VAR_020714.
VARIANT 1147 1147 N -> S (in dbSNP:rs1799951).
{ECO:0000269|PubMed:8673091}.
/FTId=VAR_005099.
VARIANT 1172 1172 S -> L (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:15635067}.
/FTId=VAR_032720.
VARIANT 1179 1179 S -> N (in BC).
{ECO:0000269|PubMed:11139248}.
/FTId=VAR_020715.
VARIANT 1279 1279 N -> S. {ECO:0000269|PubMed:12552570,
ECO:0000269|PubMed:15172753}.
/FTId=VAR_020716.
VARIANT 1286 1286 Missing.
/FTId=VAR_008773.
VARIANT 1290 1290 C -> Y (in dbSNP:rs41293485).
/FTId=VAR_008774.
VARIANT 1302 1302 Missing (in BC).
/FTId=VAR_005100.
VARIANT 1414 1414 T -> M (in dbSNP:rs70953664).
/FTId=VAR_008775.
VARIANT 1420 1420 D -> Y (in dbSNP:rs28897727).
{ECO:0000269|PubMed:11139248,
ECO:0000269|PubMed:12215251,
ECO:0000269|PubMed:12552570,
ECO:0000269|PubMed:15172753,
ECO:0000269|PubMed:15635067,
ECO:0000269|PubMed:26566883}.
/FTId=VAR_008776.
VARIANT 1445 1445 K -> T (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:15365993}.
/FTId=VAR_020717.
VARIANT 1513 1513 D -> N.
/FTId=VAR_008777.
VARIANT 1522 1522 L -> F (in one patient with BC).
{ECO:0000269|PubMed:12624724}.
/FTId=VAR_032721.
VARIANT 1524 1524 F -> V (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:12938098}.
/FTId=VAR_020718.
VARIANT 1529 1529 G -> R (in bladder cancer;
dbSNP:rs28897728).
/FTId=VAR_005101.
VARIANT 1542 1542 V -> M (in dbSNP:rs28897729).
/FTId=VAR_056753.
VARIANT 1561 1561 H -> N (in dbSNP:rs2219594).
{ECO:0000269|Ref.3}.
/FTId=VAR_018912.
VARIANT 1580 1580 C -> Y (in BC; somatic mutation).
{ECO:0000269|PubMed:11948477}.
/FTId=VAR_020719.
VARIANT 1593 1593 E -> D. {ECO:0000269|PubMed:12442273}.
/FTId=VAR_008778.
VARIANT 1643 1643 V -> A (in dbSNP:rs28897731).
/FTId=VAR_056754.
VARIANT 1679 1679 T -> I (in BC).
{ECO:0000269|PubMed:14722926}.
/FTId=VAR_020720.
VARIANT 1690 1690 K -> N (in BC).
{ECO:0000269|PubMed:15172753}.
/FTId=VAR_032722.
VARIANT 1730 1730 N -> Y (in BC).
{ECO:0000269|PubMed:11241844}.
/FTId=VAR_032723.
VARIANT 1771 1771 G -> D (in BC; unknown pathological
significance; dbSNP:rs80358755).
{ECO:0000269|PubMed:12552570,
ECO:0000269|PubMed:15172753}.
/FTId=VAR_008779.
VARIANT 1804 1804 V -> A (in BC).
{ECO:0000269|PubMed:14722926}.
/FTId=VAR_020721.
VARIANT 1805 1805 N -> S (in dbSNP:rs80358765).
/FTId=VAR_008780.
VARIANT 1880 1880 N -> K (polymorphism; was originally
thought to be linked to breast cancer;
dbSNP:rs11571657).
{ECO:0000269|PubMed:11241844,
ECO:0000269|Ref.3}.
/FTId=VAR_005102.
VARIANT 1887 1887 T -> M (in BC).
{ECO:0000269|PubMed:15172753}.
/FTId=VAR_032724.
VARIANT 1901 1901 E -> K (in BC).
{ECO:0000269|PubMed:14722926}.
/FTId=VAR_020722.
VARIANT 1902 1902 D -> N (in dbSNP:rs4987048).
/FTId=VAR_008781.
VARIANT 1915 1915 T -> M (may be a rare polymorphism;
somatic mutation; dbSNP:rs4987117).
{ECO:0000269|PubMed:10978364,
ECO:0000269|PubMed:11948477,
ECO:0000269|PubMed:15172753,
ECO:0000269|PubMed:8665505,
ECO:0000269|PubMed:8673091,
ECO:0000269|Ref.3}.
/FTId=VAR_005103.
VARIANT 1929 1929 I -> V (in BC; unknown pathological
significance; dbSNP:rs79538375).
{ECO:0000269|PubMed:15365993}.
/FTId=VAR_020723.
VARIANT 1979 1979 S -> R (in dbSNP:rs28897737).
/FTId=VAR_056755.
VARIANT 1988 1988 V -> I (in one patient with esophageal
carcinoma; somatic mutation).
{ECO:0000269|PubMed:11948123}.
/FTId=VAR_032725.
VARIANT 2031 2031 T -> A (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:15365993}.
/FTId=VAR_020724.
VARIANT 2034 2034 R -> C (in dbSNP:rs1799954).
{ECO:0000269|PubMed:12215251,
ECO:0000269|PubMed:12569143,
ECO:0000269|PubMed:8673091}.
/FTId=VAR_005104.
VARIANT 2044 2044 G -> V (in one patient with BC;
dbSNP:rs56191579).
{ECO:0000269|PubMed:12624724}.
/FTId=VAR_032726.
VARIANT 2072 2072 S -> C (in BC).
{ECO:0000269|PubMed:12373604}.
/FTId=VAR_020725.
VARIANT 2074 2074 H -> N (in dbSNP:rs34309943).
/FTId=VAR_008782.
VARIANT 2089 2089 E -> D (in BC).
{ECO:0000269|PubMed:9150152}.
/FTId=VAR_008783.
VARIANT 2094 2094 Y -> C (in BC).
{ECO:0000269|PubMed:12373604}.
/FTId=VAR_020726.
VARIANT 2096 2096 P -> L (in BC).
{ECO:0000269|PubMed:14722926}.
/FTId=VAR_020727.
VARIANT 2108 2108 R -> C (in dbSNP:rs55794205).
{ECO:0000269|PubMed:15172753}.
/FTId=VAR_032727.
VARIANT 2116 2116 H -> R (in dbSNP:rs55953736).
/FTId=VAR_061563.
VARIANT 2118 2118 V -> L (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:12442275}.
/FTId=VAR_020728.
VARIANT 2128 2128 K -> N (in BC).
{ECO:0000269|PubMed:12373604}.
/FTId=VAR_020729.
VARIANT 2135 2135 N -> H (in BC).
{ECO:0000269|PubMed:11241844}.
/FTId=VAR_032728.
VARIANT 2138 2138 V -> F (in dbSNP:rs11571659).
{ECO:0000269|Ref.3}.
/FTId=VAR_008784.
VARIANT 2162 2162 K -> R (in dbSNP:rs11571660).
{ECO:0000269|Ref.3}.
/FTId=VAR_018913.
VARIANT 2222 2222 Y -> C (in BC).
{ECO:0000269|PubMed:11241844}.
/FTId=VAR_032729.
VARIANT 2238 2238 D -> E (in dbSNP:rs28897742).
/FTId=VAR_056756.
VARIANT 2274 2274 G -> V (in BC).
/FTId=VAR_005105.
VARIANT 2275 2275 E -> G (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:15026808}.
/FTId=VAR_020730.
VARIANT 2293 2293 F -> L (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:12442275}.
/FTId=VAR_020731.
VARIANT 2336 2336 R -> H (in FANCD1; affects protein
splicing and expression; decreases
homologous recombination-mediated DNA
repair; dbSNP:rs28897743).
{ECO:0000269|PubMed:16825431,
ECO:0000269|PubMed:17924331,
ECO:0000269|PubMed:21719596}.
/FTId=VAR_032730.
VARIANT 2336 2336 R -> Q (in dbSNP:rs28897743).
/FTId=VAR_056757.
VARIANT 2353 2353 G -> R (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:15026808}.
/FTId=VAR_020732.
VARIANT 2415 2415 H -> N (in BC).
{ECO:0000269|PubMed:8640237}.
/FTId=VAR_005106.
VARIANT 2421 2421 Q -> H (in BC).
/FTId=VAR_005107.
VARIANT 2440 2440 H -> R (in dbSNP:rs4986860).
{ECO:0000269|Ref.3}.
/FTId=VAR_018914.
VARIANT 2447 2447 N -> D (in dbSNP:rs4986859).
/FTId=VAR_056758.
VARIANT 2456 2456 Q -> E (in BC).
{ECO:0000269|PubMed:15172753}.
/FTId=VAR_032731.
VARIANT 2466 2466 A -> V (polymorphism; was originally
thought to be linked to ovarian cancer).
{ECO:0000269|PubMed:12552570,
ECO:0000269|PubMed:15057823,
ECO:0000269|PubMed:15172753,
ECO:0000269|PubMed:8665505,
ECO:0000269|Ref.3}.
/FTId=VAR_008785.
VARIANT 2480 2480 L -> V (in dbSNP:rs80358965).
/FTId=VAR_008786.
VARIANT 2488 2488 R -> K (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:15026808}.
/FTId=VAR_020733.
VARIANT 2490 2490 I -> T (polymorphism; no effect on
homologous recombination-mediated DNA
repair; no effect on interaction with
SEM1; dbSNP:rs11571707).
{ECO:0000269|PubMed:21719596,
ECO:0000269|Ref.3}.
/FTId=VAR_008787.
VARIANT 2502 2502 R -> C (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:17924331}.
/FTId=VAR_063911.
VARIANT 2502 2502 R -> H (in ovarian cancer; unknown
pathological significance).
{ECO:0000269|PubMed:10486320}.
/FTId=VAR_008788.
VARIANT 2510 2510 L -> P (in FANCD1; hypersensitive to DNA
damage; disrupts interaction with SEM1).
{ECO:0000269|PubMed:14670928,
ECO:0000269|PubMed:21719596}.
/FTId=VAR_032732.
VARIANT 2515 2515 T -> I (in BC; unknown pathological
significance; dbSNP:rs28897744).
{ECO:0000269|PubMed:10978364}.
/FTId=VAR_008789.
VARIANT 2626 2626 W -> C (in FANCD1; hypersensitive to DNA
damage; no effect on interaction with
SEM1). {ECO:0000269|PubMed:16825431,
ECO:0000269|PubMed:17924331,
ECO:0000269|PubMed:21719596}.
/FTId=VAR_032733.
VARIANT 2627 2627 I -> F (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:17924331}.
/FTId=VAR_063912.
VARIANT 2653 2653 L -> P (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:17924331}.
/FTId=VAR_063913.
VARIANT 2659 2659 R -> K (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:17924331}.
/FTId=VAR_063914.
VARIANT 2663 2663 E -> V (could be associated with cancer
susceptibility; major splicing aberration
identified with this mutant;
multifactorial likelihood analysis
provides evidence for pathogenicity).
{ECO:0000269|PubMed:17924331,
ECO:0000269|PubMed:20513136}.
/FTId=VAR_063915.
VARIANT 2686 2686 L -> P (in dbSNP:rs28897746).
/FTId=VAR_056759.
VARIANT 2706 2706 N -> S. {ECO:0000269|PubMed:12442273}.
/FTId=VAR_020734.
VARIANT 2722 2722 T -> R (in BC).
{ECO:0000269|PubMed:12145750,
ECO:0000269|PubMed:17924331}.
/FTId=VAR_018661.
VARIANT 2723 2723 D -> G (could be associated with cancer
susceptibility; has abrogated function
consistent with pathogenicity; major
splicing aberration identified with this
mutant). {ECO:0000269|PubMed:17924331,
ECO:0000269|PubMed:20513136}.
/FTId=VAR_063916.
VARIANT 2723 2723 D -> H (in BC; unknown pathological
significance; disrupts interaction with
SEM1 promoting interaction with XPO1 and
BRCA2 cytoplasmic localization; in
heterozygous state promotes RAD51
cytoplasmic localization).
{ECO:0000269|PubMed:15026808,
ECO:0000269|PubMed:24013206}.
/FTId=VAR_020735.
VARIANT 2728 2728 V -> I (in BC; dbSNP:rs28897749).
{ECO:0000269|PubMed:10399947,
ECO:0000269|PubMed:10978364,
ECO:0000269|PubMed:12215251}.
/FTId=VAR_020736.
VARIANT 2729 2729 K -> N (in BC; unknown pathological
significance; no effect on homologous
recombination-mediated DNA repair; no
effect on interaction with SEM1;
dbSNP:rs80359065).
{ECO:0000269|PubMed:12442274,
ECO:0000269|PubMed:21719596}.
/FTId=VAR_020737.
VARIANT 2748 2748 G -> D (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:17924331}.
/FTId=VAR_063917.
VARIANT 2787 2787 R -> H (in ovarian cancer; somatic
mutation). {ECO:0000269|PubMed:8665505}.
/FTId=VAR_008790.
VARIANT 2792 2792 L -> P (in dbSNP:rs28897751).
/FTId=VAR_056760.
VARIANT 2793 2793 G -> R (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:12442275}.
/FTId=VAR_020738.
VARIANT 2835 2835 S -> P (in dbSNP:rs11571746).
{ECO:0000269|Ref.3}.
/FTId=VAR_018915.
VARIANT 2842 2842 R -> C (in one patient with esophageal
carcinoma; somatic mutation).
{ECO:0000269|PubMed:11948123}.
/FTId=VAR_032734.
VARIANT 2856 2856 E -> A (in dbSNP:rs11571747).
{ECO:0000269|PubMed:15026808,
ECO:0000269|Ref.3}.
/FTId=VAR_018916.
VARIANT 2944 2944 I -> F (in dbSNP:rs4987047).
{ECO:0000269|PubMed:15635067,
ECO:0000269|Ref.3}.
/FTId=VAR_008791.
VARIANT 2950 2950 K -> N (in BC; unknown pathological
significance; dbSNP:rs28897754).
{ECO:0000269|PubMed:15026808,
ECO:0000269|PubMed:15635067}.
/FTId=VAR_020739.
VARIANT 2951 2951 A -> T (in dbSNP:rs11571769).
{ECO:0000269|PubMed:12215251,
ECO:0000269|Ref.3}.
/FTId=VAR_008792.
VARIANT 2969 2969 V -> M (in dbSNP:rs59004709).
/FTId=VAR_008793.
VARIANT 3013 3013 T -> I (in BC; unknown pathological
significance; dbSNP:rs28897755).
{ECO:0000269|PubMed:15026808,
ECO:0000269|PubMed:15635067}.
/FTId=VAR_020740.
VARIANT 3052 3052 R -> W (could be associated with cancer
susceptibility; has abrogated function
consistent with pathogenicity;
multifactorial likelihood analysis
provides evidence for pathogenicity).
{ECO:0000269|PubMed:20513136}.
/FTId=VAR_063918.
VARIANT 3063 3063 P -> S (in a patient with ovarian cancer;
unknown pathological significance).
{ECO:0000269|PubMed:14746861}.
/FTId=VAR_020741.
VARIANT 3076 3076 G -> E. {ECO:0000269|PubMed:12569143}.
/FTId=VAR_020742.
VARIANT 3095 3095 D -> E (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:17924331,
ECO:0000269|PubMed:8640235}.
/FTId=VAR_005108.
VARIANT 3098 3098 Y -> H (in BC and ovarian cancer; unknown
pathological significance;
dbSNP:rs41293521).
{ECO:0000269|PubMed:10486320,
ECO:0000269|PubMed:15026808}.
/FTId=VAR_008794.
VARIANT 3101 3101 L -> R (in dbSNP:rs28897758).
/FTId=VAR_056761.
VARIANT 3103 3103 I -> M (in melanoma).
/FTId=VAR_005109.
VARIANT 3118 3118 M -> T (in BC).
{ECO:0000269|PubMed:9609997}.
/FTId=VAR_005110.
VARIANT 3124 3124 N -> I (in BC).
{ECO:0000269|PubMed:11139248}.
/FTId=VAR_020743.
VARIANT 3196 3196 K -> E (in BC; dbSNP:rs80359228).
{ECO:0000269|PubMed:11139248}.
/FTId=VAR_020744.
VARIANT 3244 3244 V -> I (in dbSNP:rs11571831).
{ECO:0000269|Ref.3}.
/FTId=VAR_018917.
VARIANT 3257 3257 K -> R.
/FTId=VAR_008795.
VARIANT 3276 3276 R -> S.
/FTId=VAR_008796.
VARIANT 3300 3300 P -> S (in one patient with esophageal
carcinoma).
{ECO:0000269|PubMed:11948123}.
/FTId=VAR_032735.
VARIANT 3357 3357 T -> R (in BC).
/FTId=VAR_005111.
VARIANT 3374 3374 T -> I (in dbSNP:rs56309455).
{ECO:0000269|PubMed:12442275}.
/FTId=VAR_020745.
VARIANT 3412 3412 I -> V (polymorphism; was originally
thought to be associated with breast
cancer; dbSNP:rs1801426).
{ECO:0000269|PubMed:10323242,
ECO:0000269|PubMed:10978364,
ECO:0000269|PubMed:12442274,
ECO:0000269|PubMed:14746861,
ECO:0000269|PubMed:15026808,
ECO:0000269|PubMed:15365993,
ECO:0000269|PubMed:9150152,
ECO:0000269|Ref.3}.
/FTId=VAR_005112.
MUTAGEN 2725 2725 W->A: Disrupts interaction with SEM1.
{ECO:0000269|PubMed:24013206}.
MUTAGEN 3291 3291 S->E: Impaired interaction with RAD51.
{ECO:0000269|PubMed:15800615}.
MUTAGEN 3387 3387 T->A: Loss of phosphorylation by CHEK1
and CHEK2 (in vitro).
{ECO:0000269|PubMed:18317453}.
CONFLICT 758 758 S -> N (in Ref. 1; CAA64484).
{ECO:0000305}.
CONFLICT 1761 1762 GY -> RI (in Ref. 1; CAA64484).
{ECO:0000305}.
CONFLICT 1767 1767 K -> N (in Ref. 1; CAA64484).
{ECO:0000305}.
CONFLICT 2536 2536 S -> P (in Ref. 4; CAA98995).
{ECO:0000305}.
CONFLICT 3216 3216 L -> LVS (in Ref. 4; CAA97728).
{ECO:0000305}.
HELIX 31 35 {ECO:0000244|PDB:3EU7}.
HELIX 1520 1522 {ECO:0000244|PDB:1N0W}.
HELIX 1536 1541 {ECO:0000244|PDB:1N0W}.
TURN 1542 1546 {ECO:0000244|PDB:1N0W}.
SEQUENCE 3418 AA; 384202 MW; 6A0B3B7B332153EB CRC64;
MPIGSKERPT FFEIFKTRCN KADLGPISLN WFEELSSEAP PYNSEPAEES EHKNNNYEPN
LFKTPQRKPS YNQLASTPII FKEQGLTLPL YQSPVKELDK FKLDLGRNVP NSRHKSLRTV
KTKMDQADDV SCPLLNSCLS ESPVVLQCTH VTPQRDKSVV CGSLFHTPKF VKGRQTPKHI
SESLGAEVDP DMSWSSSLAT PPTLSSTVLI VRNEEASETV FPHDTTANVK SYFSNHDESL
KKNDRFIASV TDSENTNQRE AASHGFGKTS GNSFKVNSCK DHIGKSMPNV LEDEVYETVV
DTSEEDSFSL CFSKCRTKNL QKVRTSKTRK KIFHEANADE CEKSKNQVKE KYSFVSEVEP
NDTDPLDSNV ANQKPFESGS DKISKEVVPS LACEWSQLTL SGLNGAQMEK IPLLHISSCD
QNISEKDLLD TENKRKKDFL TSENSLPRIS SLPKSEKPLN EETVVNKRDE EQHLESHTDC
ILAVKQAISG TSPVASSFQG IKKSIFRIRE SPKETFNASF SGHMTDPNFK KETEASESGL
EIHTVCSQKE DSLCPNLIDN GSWPATTTQN SVALKNAGLI STLKKKTNKF IYAIHDETSY
KGKKIPKDQK SELINCSAQF EANAFEAPLT FANADSGLLH SSVKRSCSQN DSEEPTLSLT
SSFGTILRKC SRNETCSNNT VISQDLDYKE AKCNKEKLQL FITPEADSLS CLQEGQCEND
PKSKKVSDIK EEVLAAACHP VQHSKVEYSD TDFQSQKSLL YDHENASTLI LTPTSKDVLS
NLVMISRGKE SYKMSDKLKG NNYESDVELT KNIPMEKNQD VCALNENYKN VELLPPEKYM
RVASPSRKVQ FNQNTNLRVI QKNQEETTSI SKITVNPDSE ELFSDNENNF VFQVANERNN
LALGNTKELH ETDLTCVNEP IFKNSTMVLY GDTGDKQATQ VSIKKDLVYV LAEENKNSVK
QHIKMTLGQD LKSDISLNID KIPEKNNDYM NKWAGLLGPI SNHSFGGSFR TASNKEIKLS
EHNIKKSKMF FKDIEEQYPT SLACVEIVNT LALDNQKKLS KPQSINTVSA HLQSSVVVSD
CKNSHITPQM LFSKQDFNSN HNLTPSQKAE ITELSTILEE SGSQFEFTQF RKPSYILQKS
TFEVPENQMT ILKTTSEECR DADLHVIMNA PSIGQVDSSK QFEGTVEIKR KFAGLLKNDC
NKSASGYLTD ENEVGFRGFY SAHGTKLNVS TEALQKAVKL FSDIENISEE TSAEVHPISL
SSSKCHDSVV SMFKIENHND KTVSEKNNKC QLILQNNIEM TTGTFVEEIT ENYKRNTENE
DNKYTAASRN SHNLEFDGSD SSKNDTVCIH KDETDLLFTD QHNICLKLSG QFMKEGNTQI
KEDLSDLTFL EVAKAQEACH GNTSNKEQLT ATKTEQNIKD FETSDTFFQT ASGKNISVAK
ESFNKIVNFF DQKPEELHNF SLNSELHSDI RKNKMDILSY EETDIVKHKI LKESVPVGTG
NQLVTFQGQP ERDEKIKEPT LLGFHTASGK KVKIAKESLD KVKNLFDEKE QGTSEITSFS
HQWAKTLKYR EACKDLELAC ETIEITAAPK CKEMQNSLNN DKNLVSIETV VPPKLLSDNL
CRQTENLKTS KSIFLKVKVH ENVEKETAKS PATCYTNQSP YSVIENSALA FYTSCSRKTS
VSQTSLLEAK KWLREGIFDG QPERINTADY VGNYLYENNS NSTIAENDKN HLSEKQDTYL
SNSSMSNSYS YHSDEVYNDS GYLSKNKLDS GIEPVLKNVE DQKNTSFSKV ISNVKDANAY
PQTVNEDICV EELVTSSSPC KNKNAAIKLS ISNSNNFEVG PPAFRIASGK IVCVSHETIK
KVKDIFTDSF SKVIKENNEN KSKICQTKIM AGCYEALDDS EDILHNSLDN DECSTHSHKV
FADIQSEEIL QHNQNMSGLE KVSKISPCDV SLETSDICKC SIGKLHKSVS SANTCGIFST
ASGKSVQVSD ASLQNARQVF SEIEDSTKQV FSKVLFKSNE HSDQLTREEN TAIRTPEHLI
SQKGFSYNVV NSSAFSGFST ASGKQVSILE SSLHKVKGVL EEFDLIRTEH SLHYSPTSRQ
NVSKILPRVD KRNPEHCVNS EMEKTCSKEF KLSNNLNVEG GSSENNHSIK VSPYLSQFQQ
DKQQLVLGTK VSLVENIHVL GKEQASPKNV KMEIGKTETF SDVPVKTNIE VCSTYSKDSE
NYFETEAVEI AKAFMEDDEL TDSKLPSHAT HSLFTCPENE EMVLSNSRIG KRRGEPLILV
GEPSIKRNLL NEFDRIIENQ EKSLKASKST PDGTIKDRRL FMHHVSLEPI TCVPFRTTKE
RQEIQNPNFT APGQEFLSKS HLYEHLTLEK SSSNLAVSGH PFYQVSATRN EKMRHLITTG
RPTKVFVPPF KTKSHFHRVE QCVRNINLEE NRQKQNIDGH GSDDSKNKIN DNEIHQFNKN
NSNQAAAVTF TKCEEEPLDL ITSLQNARDI QDMRIKKKQR QRVFPQPGSL YLAKTSTLPR
ISLKAAVGGQ VPSACSHKQL YTYGVSKHCI KINSKNAESF QFHTEDYFGK ESLWTGKGIQ
LADGGWLIPS NDGKAGKEEF YRALCDTPGV DPKLISRIWV YNHYRWIIWK LAAMECAFPK
EFANRCLSPE RVLLQLKYRY DTEIDRSRRS AIKKIMERDD TAAKTLVLCV SDIISLSANI
SETSSNKTSS ADTQKVAIIE LTDGWYAVKA QLDPPLLAVL KNGRLTVGQK IILHGAELVG
SPDACTPLEA PESLMLKISA NSTRPARWYT KLGFFPDPRP FPLPLSSLFS DGGNVGCVDV
IIQRAYPIQW MEKTSSGLYI FRNEREEEKE AAKYVEAQQK RLEALFTKIQ EEFEEHEENT
TKPYLPSRAL TRQQVRALQD GAELYEAVKN AADPAYLEGY FSEEQLRALN NHRQMLNDKK
QAQIQLEIRK AMESAEQKEQ GLSRDVTTVW KLRIVSYSKK EKDSVILSIW RPSSDLYSLL
TEGKRYRIYH LATSKSKSKS ERANIQLAAT KKTQYQQLPV SDEILFQIYQ PREPLHFSKF
LDPDFQPSCS EVDLIGFVVS VVKKTGLAPF VYLSDECYNL LAIKFWIDLN EDIIKPHMLI
AASNLQWRPE SKSGLLTLFA GDFSVFSASP KEGHFQETFN KMKNTVENID ILCNEAENKL
MHILHANDPK WSTPTKDCTS GPYTAQIIPG TGNKLLMSSP NCEIYYQSPL SLCMAKRKSV
STPVSAQMTS KSCKGEKEID DQKNCKKRRA LDFLSRLPLP PPVSPICTFV SPAAQKAFQP
PRSCGTKYET PIKKKELNSP QMTPFKKFNE ISLLESNSIA DEELALINTQ ALLSGSTGEK
QFISVSESTR TAPTSSEDYL RLKRRCTTSL IKEQESSQAS TEECEKNKQD TITTKKYI


Related products :

Catalog number Product name Quantity
U1364h CLIA BRCA2,Breast cancer type 2 susceptibility protein,FACD,FANCD1,Fanconi anemia group D1 protein,Homo sapiens,Human 96T
E1364h ELISA kit BRCA2,Breast cancer type 2 susceptibility protein,FACD,FANCD1,Fanconi anemia group D1 protein,Homo sapiens,Human 96T
E1364h ELISA BRCA2,Breast cancer type 2 susceptibility protein,FACD,FANCD1,Fanconi anemia group D1 protein,Homo sapiens,Human 96T
U1364m CLIA Brca2,Breast cancer type 2 susceptibility protein homolog,Fancd1,Fanconi anemia group D1 protein homolog,Mouse,Mus musculus 96T
U1364r CLIA Brca2,Breast cancer type 2 susceptibility protein homolog,Fancd1,Fanconi anemia group D1 protein homolog,Rat,Rattus norvegicus 96T
E1364r ELISA Brca2,Breast cancer type 2 susceptibility protein homolog,Fancd1,Fanconi anemia group D1 protein homolog,Rat,Rattus norvegicus 96T
E1364m ELISA kit Brca2,Breast cancer type 2 susceptibility protein homolog,Fancd1,Fanconi anemia group D1 protein homolog,Mouse,Mus musculus 96T
E1364r ELISA kit Brca2,Breast cancer type 2 susceptibility protein homolog,Fancd1,Fanconi anemia group D1 protein homolog,Rat,Rattus norvegicus 96T
E1364m ELISA Brca2,Breast cancer type 2 susceptibility protein homolog,Fancd1,Fanconi anemia group D1 protein homolog,Mouse,Mus musculus 96T
EIAAB14414 FAAP95,FANCB,Fanconi anemia group B protein,Fanconi anemia-associated polypeptide of 95 kDa,Homo sapiens,Human,Protein FACB
EIAAB14432 ATP-dependent RNA helicase FANCM,FAAP250,FANCM,Fanconi anemia group M protein,Fanconi anemia-associated polypeptide of 250 kDa,Homo sapiens,Human,KIAA1596,Protein FACM,Protein Hef ortholog
EIAAB14430 E3 ubiquitin-protein ligase FANCL,FAAP43,FANCL,Fanconi anemia group L protein,Fanconi anemia-associated polypeptide of 43 kDa,Homo sapiens,Human,PHF9
NB100-182 Fanconi anemia group D2 protein 0.05 ml
GTX25064 Fanconi anemia group E protein 100 µg
GTX25065 Fanconi anemia group C protein 100 µg
GTX25360 Fanconi anemia group D2 protein 100 µl
AP06115PU-N Fanconi anemia group D2 protein 100 µg
GTX70299 Fanconi anemia group D2 protein 0.1 mg
GTX25063 Fanconi anemia group A protein 100 µg
GTX70315 Fanconi anemia group C protein 0.1 mg
NB100-316 Fanconi anemia group D2 protein 0.1 ml
GTX30142 Fanconi anemia group D2 protein 50 µl
NB100-411 Fanconi anemia group D2 protein 0.1 ml
EH1088 Breast cancer type 1 susceptibility protein Elisa Kit 96T
EH1532 Breast cancer type 2 susceptibility protein Elisa Kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur