RAD51_HUMAN
ID RAD51_HUMAN Reviewed; 339 AA.
AC Q06609; B0FXP0; B2R8T6; Q6FHX9; Q6ZNA8; Q9BV60;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 233.
DE RecName: Full=DNA repair protein RAD51 homolog 1 {ECO:0000305};
DE Short=HsRAD51;
DE Short=hRAD51;
DE AltName: Full=RAD51 homolog A;
GN Name=RAD51 {ECO:0000312|HGNC:HGNC:9817}; Synonyms=RAD51A, RECA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8358431; DOI=10.1038/ng0793-239;
RA Shinohara A., Ogawa H., Matsuda Y., Ushio N., Ikeo K., Ogawa T.;
RT "Cloning of human, mouse and fission yeast recombination genes homologous
RT to RAD51 and recA.";
RL Nat. Genet. 4:239-243(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=8479919; DOI=10.1093/nar/21.7.1665;
RA Yoshimura Y., Morita T., Yamamoto A., Matsushiro A.;
RT "Cloning and sequence of the human RecA-like gene cDNA.";
RL Nucleic Acids Res. 21:1665-1665(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10493508;
RA Schmutte C., Tombline G., Rhiem K., Sadoff M.M., Schmutzler R.,
RA von Deimling A., Fishel R.;
RT "Characterization of the human Rad51 genomic locus and examination of
RT tumors with 15q14-15 loss of heterozygosity (LOH).";
RL Cancer Res. 59:4564-4569(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11535547;
RA Wang W.W., Spurdle A.B., Kolachana P., Bove B., Modan B., Ebbers S.M.,
RA Suthers G., Tucker M.A., Kaufman D.J., Doody M.M., Tarone R.E., Daly M.,
RA Levavi H., Pierce H., Chetrit A., Yechezkel G.H., Chenevix-Trench G.,
RA Offit K., Godwin A.K., Struewing J.P.;
RT "A single nucleotide polymorphism in the 5' untranslated region of RAD51
RT and risk of cancer among BRCA1/2 mutation carriers.";
RL Cancer Epidemiol. Biomarkers Prev. 10:955-960(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION OF ISOFORMS 1 AND 3,
RP TISSUE SPECIFICITY (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION (ISOFORMS 1 AND
RP 3), AND MUTAGENESIS (ISOFORM 3).
RX PubMed=18417535; DOI=10.1093/nar/gkn171;
RA Park J.Y., Yoo H.W., Kim B.R., Park R., Choi S.Y., Kim Y.;
RT "Identification of a novel human Rad51 variant that promotes DNA strand
RT exchange.";
RL Nucleic Acids Res. 36:3226-3234(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP CHARACTERIZATION.
RX PubMed=7988572; DOI=10.1002/j.1460-2075.1994.tb06914.x;
RA Benson F.E., Stasiak A., West S.C.;
RT "Purification and characterization of the human Rad51 protein, an analogue
RT of E. coli RecA.";
RL EMBO J. 13:5764-5771(1994).
RN [13]
RP INTERACTION WITH RAD54L.
RX PubMed=9321665; DOI=10.1093/nar/25.20.4106;
RA Golub E.I., Kovalenko O.V., Gupta R.C., Ward D.C., Radding C.M.;
RT "Interaction of human recombination proteins Rad51 and Rad54.";
RL Nucleic Acids Res. 25:4106-4110(1997).
RN [14]
RP INTERACTION WITH RAD51AP1.
RX PubMed=9396801; DOI=10.1093/nar/25.24.4946;
RA Kovalenko O.V., Golub E.I., Bray-Ward P., Ward D.C., Radding C.M.;
RT "A novel nucleic acid-binding protein that interacts with human rad51
RT recombinase.";
RL Nucleic Acids Res. 25:4946-4953(1997).
RN [15]
RP INTERACTION WITH RAD51AP1, AND SUBCELLULAR LOCATION.
RX PubMed=9192668; DOI=10.1073/pnas.94.13.6927;
RA Mizuta R., LaSalle J.M., Cheng H.-L., Shinohara A., Ogawa H.,
RA Copeland N.G., Jenkins N.A., Lalande M., Alt F.W.;
RT "RAB22 and RAB163/mouse BRCA2: proteins that specifically interact with the
RT RAD51 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6927-6932(1997).
RN [16]
RP INTERACTION WITH ABL1, AND PHOSPHORYLATION AT TYR-54.
RX PubMed=9461559; DOI=10.1074/jbc.273.7.3799;
RA Yuan Z.M., Huang Y., Ishiko T., Nakada S., Utsugisawa T., Kharbanda S.,
RA Wang R., Sung P., Shinohara A., Weichselbaum R., Kufe D.;
RT "Regulation of Rad51 function by c-Abl in response to DNA damage.";
RL J. Biol. Chem. 273:3799-3802(1998).
RN [17]
RP INTERACTION WITH RAD54B.
RX PubMed=10851248; DOI=10.1074/jbc.m910306199;
RA Tanaka K., Hiramoto T., Fukuda T., Miyagawa K.;
RT "A novel human Rad54 homologue, Rad54B, associates with Rad51.";
RL J. Biol. Chem. 275:26316-26321(2000).
RN [18]
RP FUNCTION.
RX PubMed=12205100; DOI=10.1074/jbc.m208004200;
RA Sigurdsson S., Van Komen S., Petukhova G., Sung P.;
RT "Homologous DNA pairing by human recombination factors Rad51 and Rad54.";
RL J. Biol. Chem. 277:42790-42794(2002).
RN [19]
RP INTERACTION WITH XRCC3.
RX PubMed=11842113; DOI=10.1093/nar/30.4.1009;
RA Liu N., Schild D., Thelen M.P., Thompson L.H.;
RT "Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs
RT in human cells.";
RL Nucleic Acids Res. 30:1009-1015(2002).
RN [20]
RP INTERACTION WITH RAD51B AND RAD51C.
RX PubMed=12427746; DOI=10.1074/jbc.m211038200;
RA Lio Y.-C., Mazin A.V., Kowalczykowski S.C., Chen D.J.;
RT "Complex formation by the human Rad51B and Rad51C DNA repair proteins and
RT their activities in vitro.";
RL J. Biol. Chem. 278:2469-2478(2003).
RN [21]
RP SELF-ASSOCIATION, INTERACTION WITH BRCA2, AND MUTAGENESIS OF
RP 208-SER-ALA-209.
RX PubMed=14580352; DOI=10.1016/s1097-2765(03)00394-0;
RA Yu D.S., Sonoda E., Takeda S., Huang C.L., Pellegrini L., Blundell T.L.,
RA Venkitaraman A.R.;
RT "Dynamic control of Rad51 recombinase by self-association and interaction
RT with BRCA2.";
RL Mol. Cell 12:1029-1041(2003).
RN [22]
RP SUBCELLULAR LOCATION.
RX PubMed=16215984; DOI=10.1002/jcb.20640;
RA Bennett B.T., Knight K.L.;
RT "Cellular localization of human Rad51C and regulation of ubiquitin-mediated
RT proteolysis of Rad51.";
RL J. Cell. Biochem. 96:1095-1109(2005).
RN [23]
RP INTERACTION WITH CHEK1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-309,
RP AND MUTAGENESIS OF THR-309.
RX PubMed=15665856; DOI=10.1038/ncb1212;
RA Soerensen C.S., Hansen L.T., Dziegielewski J., Syljuaesen R.G., Lundin C.,
RA Bartek J., Helleday T.;
RT "The cell-cycle checkpoint kinase Chk1 is required for mammalian homologous
RT recombination repair.";
RL Nat. Cell Biol. 7:195-201(2005).
RN [24]
RP INTERACTION WITH RAD51AP2.
RX PubMed=16990250; DOI=10.1093/nar/gkl665;
RA Kovalenko O.V., Wiese C., Schild D.;
RT "RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a
RT conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51.";
RL Nucleic Acids Res. 34:5081-5092(2006).
RN [25]
RP INTERACTION WITH NABP2.
RX PubMed=18449195; DOI=10.1038/nature06883;
RA Richard D.J., Bolderson E., Cubeddu L., Wadsworth R.I.M., Savage K.,
RA Sharma G.G., Nicolette M.L., Tsvetanov S., McIlwraith M.J., Pandita R.K.,
RA Takeda S., Hay R.T., Gautier J., West S.C., Paull T.T., Pandita T.K.,
RA White M.F., Khanna K.K.;
RT "Single-stranded DNA-binding protein hSSB1 is critical for genomic
RT stability.";
RL Nature 453:677-681(2008).
RN [26]
RP SUBCELLULAR LOCATION.
RX PubMed=19783859; DOI=10.1074/jbc.m109.024646;
RA Gildemeister O.S., Sage J.M., Knight K.L.;
RT "Cellular redistribution of Rad51 in response to DNA damage: novel role for
RT Rad51C.";
RL J. Biol. Chem. 284:31945-31952(2009).
RN [27]
RP INTERACTION WITH RECQL5, AND FUNCTION.
RX PubMed=20348101; DOI=10.1074/jbc.m110.110478;
RA Schwendener S., Raynard S., Paliwal S., Cheng A., Kanagaraj R.,
RA Shevelev I., Stark J.M., Sung P., Janscak P.;
RT "Physical interaction of RECQ5 helicase with RAD51 facilitates its anti-
RT recombinase activity.";
RL J. Biol. Chem. 285:15739-15745(2010).
RN [28]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=20413593; DOI=10.1074/jbc.m109.099846;
RA Sage J.M., Gildemeister O.S., Knight K.L.;
RT "Discovery of a novel function for human Rad51: maintenance of the
RT mitochondrial genome.";
RL J. Biol. Chem. 285:18984-18990(2010).
RN [29]
RP INTERACTION WITH RPA1.
RX PubMed=20705237; DOI=10.1016/j.molcel.2010.07.021;
RA Dou H., Huang C., Singh M., Carpenter P.B., Yeh E.T.;
RT "Regulation of DNA repair through desumoylation and sumoylation of
RT replication protein A complex.";
RL Mol. Cell 39:333-345(2010).
RN [30]
RP INTERACTION WITH POLN.
RX PubMed=19995904; DOI=10.1128/mcb.01124-09;
RA Moldovan G.L., Madhavan M.V., Mirchandani K.D., McCaffrey R.M.,
RA Vinciguerra P., D'Andrea A.D.;
RT "DNA polymerase POLN participates in cross-link repair and homologous
RT recombination.";
RL Mol. Cell. Biol. 30:1088-1096(2010).
RN [31]
RP INTERACTION WITH RECQL5, AND FUNCTION.
RX PubMed=20231364; DOI=10.1128/mcb.01583-09;
RA Islam M.N., Fox D. III, Guo R., Enomoto T., Wang W.;
RT "RecQL5 promotes genome stabilization through two parallel mechanisms--
RT interacting with RNA polymerase II and acting as a helicase.";
RL Mol. Cell. Biol. 30:2460-2472(2010).
RN [32]
RP INTERACTION WITH RPA2, AND SUBCELLULAR LOCATION.
RX PubMed=20154705; DOI=10.1038/nsmb.1769;
RA Lee D.H., Pan Y., Kanner S., Sung P., Borowiec J.A., Chowdhury D.;
RT "A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair
RT via homologous recombination.";
RL Nat. Struct. Mol. Biol. 17:365-372(2010).
RN [33]
RP INTERACTION WITH PALB2.
RX PubMed=20871615; DOI=10.1038/nsmb.1915;
RA Buisson R., Dion-Cote A.M., Coulombe Y., Launay H., Cai H., Stasiak A.Z.,
RA Stasiak A., Xia B., Masson J.Y.;
RT "Cooperation of breast cancer proteins PALB2 and piccolo BRCA2 in
RT stimulating homologous recombination.";
RL Nat. Struct. Mol. Biol. 17:1247-1254(2010).
RN [34]
RP SUBCELLULAR LOCATION.
RX PubMed=21276791; DOI=10.1016/j.yexcr.2011.01.021;
RA Cappelli E., Townsend S., Griffin C., Thacker J.;
RT "Homologous recombination proteins are associated with centrosomes and are
RT required for mitotic stability.";
RL Exp. Cell Res. 317:1203-1213(2011).
RN [35]
RP INTERACTION WITH SWI5 AND SFR1.
RX PubMed=21252223; DOI=10.1074/jbc.m110.207290;
RA Yuan J., Chen J.;
RT "The role of human SWI5-MEI5 complex in homologous recombination repair.";
RL J. Biol. Chem. 286:9888-9893(2011).
RN [36]
RP INTERACTION WITH SWSAP1.
RX PubMed=21965664; DOI=10.1074/jbc.m111.271080;
RA Liu T., Wan L., Wu Y., Chen J., Huang J.;
RT "hSWS1.SWSAP1 is an evolutionarily conserved complex required for efficient
RT homologous recombination repair.";
RL J. Biol. Chem. 286:41758-41766(2011).
RN [37]
RP INVOLVEMENT IN MRMV2.
RX PubMed=22305526; DOI=10.1016/j.ajhg.2011.12.002;
RA Depienne C., Bouteiller D., Meneret A., Billot S., Groppa S., Klebe S.,
RA Charbonnier-Beaupel F., Corvol J.C., Saraiva J.P., Brueggemann N.,
RA Bhatia K., Cincotta M., Brochard V., Flamand-Roze C., Carpentier W.,
RA Meunier S., Marie Y., Gaussen M., Stevanin G., Wehrle R., Vidailhet M.,
RA Klein C., Dusart I., Brice A., Roze E.;
RT "RAD51 haploinsufficiency causes congenital mirror movements in humans.";
RL Am. J. Hum. Genet. 90:301-307(2012).
RN [38]
RP INTERACTION WITH PARPBP.
RX PubMed=22153967; DOI=10.1016/j.molcel.2011.11.010;
RA Moldovan G.L., Dejsuphong D., Petalcorin M.I., Hofmann K., Takeda S.,
RA Boulton S.J., D'Andrea A.D.;
RT "Inhibition of homologous recombination by the PCNA-interacting protein
RT PARI.";
RL Mol. Cell 45:75-86(2012).
RN [39]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [40]
RP INTERACTION WITH MCM9 AND MCM8, AND SUBCELLULAR LOCATION.
RX PubMed=23401855; DOI=10.1128/mcb.01503-12;
RA Park J., Long D.T., Lee K.Y., Abbas T., Shibata E., Negishi M., Luo Y.,
RA Schimenti J.C., Gambus A., Walter J.C., Dutta A.;
RT "The MCM8-MCM9 complex promotes RAD51 recruitment at DNA damage sites to
RT facilitate homologous recombination.";
RL Mol. Cell. Biol. 33:1632-1644(2013).
RN [41]
RP MUTAGENESIS OF 208-SER-ALA-209, AND NUCLEAR EXPORT SIGNAL.
RX PubMed=24013206; DOI=10.1038/nsmb.2666;
RA Jeyasekharan A.D., Liu Y., Hattori H., Pisupati V., Jonsdottir A.B.,
RA Rajendra E., Lee M., Sundaramoorthy E., Schlachter S., Kaminski C.F.,
RA Ofir-Rosenfeld Y., Sato K., Savill J., Ayoub N., Venkitaraman A.R.;
RT "A cancer-associated BRCA2 mutation reveals masked nuclear export signals
RT controlling localization.";
RL Nat. Struct. Mol. Biol. 20:1191-1198(2013).
RN [42]
RP INTERACTION WITH FBH1, UBIQUITINATION AT LYS-58 AND LYS-64, AND MUTAGENESIS
RP OF LYS-58 AND LYS-64.
RX PubMed=23393192; DOI=10.1093/nar/gkt056;
RA Masuda-Ozawa T., Hoang T., Seo Y.S., Chen L.F., Spies M.;
RT "Single-molecule sorting reveals how ubiquitylation affects substrate
RT recognition and activities of FBH1 helicase.";
RL Nucleic Acids Res. 41:3576-3587(2013).
RN [43]
RP FUNCTION, INTERACTION WITH PALB2, AND IDENTIFICATION IN A PALB2-CONTAINING
RP HR COMPLEX.
RX PubMed=24141787; DOI=10.1038/onc.2013.421;
RA Park J.Y., Singh T.R., Nassar N., Zhang F., Freund M., Hanenberg H.,
RA Meetei A.R., Andreassen P.R.;
RT "Breast cancer-associated missense mutants of the PALB2 WD40 domain, which
RT directly binds RAD51C, RAD51 and BRCA2, disrupt DNA repair.";
RL Oncogene 33:4803-4812(2014).
RN [44]
RP FUNCTION, INTERACTION WITH FIGNL1; RAD51AP1 AND SWI5, SUBCELLULAR LOCATION,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23754376; DOI=10.1073/pnas.1220662110;
RA Yuan J., Chen J.;
RT "FIGNL1-containing protein complex is required for efficient homologous
RT recombination repair.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:10640-10645(2013).
RN [45]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH BLM AND SPIDR, INTERACTION WITH
RP SPIDR, AND SUBCELLULAR LOCATION.
RX PubMed=23509288; DOI=10.1073/pnas.1220921110;
RA Wan L., Han J., Liu T., Dong S., Xie F., Chen H., Huang J.;
RT "Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase
RT with homologous recombination repair.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:10646-10651(2013).
RN [46]
RP FUNCTION, INVOLVEMENT IN FANCR, VARIANT FANCR PRO-131, AND CHARACTERIZATION
RP OF VARIANT FANCR PRO-131.
RX PubMed=26253028; DOI=10.1016/j.molcel.2015.07.009;
RA Wang A.T., Kim T., Wagner J.E., Conti B.A., Lach F.P., Huang A.L.,
RA Molina H., Sanborn E.M., Zierhut H., Cornes B.K., Abhyankar A., Sougnez C.,
RA Gabriel S.B., Auerbach A.D., Kowalczykowski S.C., Smogorzewska A.;
RT "A dominant mutation in human RAD51 reveals its function in DNA interstrand
RT crosslink repair independent of homologous recombination.";
RL Mol. Cell 59:478-490(2015).
RN [47]
RP INTERACTION WITH POLQ.
RX PubMed=25642963; DOI=10.1038/nature14184;
RA Ceccaldi R., Liu J.C., Amunugama R., Hajdu I., Primack B., Petalcorin M.I.,
RA O'Connor K.W., Konstantinopoulos P.A., Elledge S.J., Boulton S.J.,
RA Yusufzai T., D'Andrea A.D.;
RT "Homologous-recombination-deficient tumours are dependent on Poltheta-
RT mediated repair.";
RL Nature 518:258-262(2015).
RN [48]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MMS22L.
RX PubMed=27797818; DOI=10.15252/embj.201593132;
RA Piwko W., Mlejnkova L.J., Mutreja K., Ranjha L., Stafa D., Smirnov A.,
RA Brodersen M.M., Zellweger R., Sturzenegger A., Janscak P., Lopes M.,
RA Peter M., Cejka P.;
RT "The MMS22L-TONSL heterodimer directly promotes RAD51-dependent
RT recombination upon replication stress.";
RL EMBO J. 35:2584-2601(2016).
RN [49]
RP IDENTIFICATION IN THE HRR COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=26833090; DOI=10.1016/j.molcel.2015.12.026;
RA Trego K.S., Groesser T., Davalos A.R., Parplys A.C., Zhao W., Nelson M.R.,
RA Hlaing A., Shih B., Rydberg B., Pluth J.M., Tsai M.S., Hoeijmakers J.H.J.,
RA Sung P., Wiese C., Campisi J., Cooper P.K.;
RT "Non-catalytic Roles for XPG with BRCA1 and BRCA2 in Homologous
RT Recombination and Genome Stability.";
RL Mol. Cell 61:535-546(2016).
RN [50]
RP FUNCTION, INTERACTION WITH RFWD3, AND UBIQUITINATION.
RX PubMed=28575658; DOI=10.1016/j.molcel.2017.04.022;
RA Inano S., Sato K., Katsuki Y., Kobayashi W., Tanaka H., Nakajima K.,
RA Nakada S., Miyoshi H., Knies K., Takaori-Kondo A., Schindler D., Ishiai M.,
RA Kurumizaka H., Takata M.;
RT "RFWD3-mediated ubiquitination promotes timely removal of both RPA and
RT RAD51 from dna damage sites to facilitate homologous recombination.";
RL Mol. Cell 66:622-634(2017).
RN [51]
RP FUNCTION, INTERACTION WITH ATAD5 RFC-LIKE COMPLEX; ATAD5 AND WDR48, AND
RP SUBCELLULAR LOCATION.
RX PubMed=31844045; DOI=10.1038/s41467-019-13667-4;
RA Park S.H., Kang N., Song E., Wie M., Lee E.A., Hwang S., Lee D., Ra J.S.,
RA Park I.B., Park J., Kang S., Park J.H., Hohng S., Lee K.Y., Myung K.;
RT "ATAD5 promotes replication restart by regulating RAD51 and PCNA in
RT response to replication stress.";
RL Nat. Commun. 10:5718-5718(2019).
RN [52]
RP INTERACTION WITH HELQ.
RX PubMed=34937945; DOI=10.1038/s41586-021-04261-0;
RA Anand R., Buechelmaier E., Belan O., Newton M., Vancevska A.,
RA Kaczmarczyk A., Takaki T., Rueda D.S., Powell S.N., Boulton S.J.;
RT "HELQ is a dual-function DSB repair enzyme modulated by RPA and RAD51.";
RL Nature 601:268-273(2022).
RN [53]
RP STRUCTURE BY NMR OF 1-114.
RX PubMed=10390347; DOI=10.1006/jmbi.1999.2904;
RA Aihara H., Ito Y., Kurumizaka H., Yokoyama S., Shibata T.;
RT "The N-terminal domain of the human Rad51 protein binds DNA: structure and
RT a DNA binding surface as revealed by NMR.";
RL J. Mol. Biol. 290:495-504(1999).
RN [54]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 97-339 IN COMPLEX WITH BRCA2,
RP FUNCTION, SUBUNIT, MUTAGENESIS OF PHE-86 AND ALA-89, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH BRCA2.
RX PubMed=12442171; DOI=10.1038/nature01230;
RA Pellegrini L., Yu D.S., Lo T., Anand S., Lee M., Blundell T.L.,
RA Venkitaraman A.R.;
RT "Insights into DNA recombination from the structure of a RAD51-BRCA2
RT complex.";
RL Nature 420:287-293(2002).
RN [55]
RP VARIANT BC GLN-150.
RX PubMed=10807537; DOI=10.1007/s100380050199;
RA Kato M., Yano K., Matsuo F., Saito H., Katagiri T., Kurumizaka H.,
RA Yoshimoto M., Kasumi F., Akiyama F., Sakamoto G., Nagawa H., Nakamura Y.,
RA Miki Y.;
RT "Identification of Rad51 alteration in patients with bilateral breast
RT cancer.";
RL J. Hum. Genet. 45:133-137(2000).
RN [56]
RP INVOLVEMENT IN FANCR, VARIANT FANCR THR-293, CHARACTERIZATION OF VARIANT
RP FANCR THR-293, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26681308; DOI=10.1038/ncomms9829;
RA Ameziane N., May P., Haitjema A., van de Vrugt H.J.,
RA van Rossum-Fikkert S.E., Ristic D., Williams G.J., Balk J., Rockx D.,
RA Li H., Rooimans M.A., Oostra A.B., Velleuer E., Dietrich R.,
RA Bleijerveld O.B., Maarten Altelaar A.F., Meijers-Heijboer H., Joenje H.,
RA Glusman G., Roach J., Hood L., Galas D., Wyman C., Balling R.,
RA den Dunnen J., de Winter J.P., Kanaar R., Gelinas R., Dorsman J.C.;
RT "A novel Fanconi anaemia subtype associated with a dominant-negative
RT mutation in RAD51.";
RL Nat. Commun. 6:8829-8829(2015).
RN [57]
RP CHARACTERIZATION OF VARIANT BC GLN-150.
RX PubMed=25539919; DOI=10.1093/nar/gku1337;
RA Chen J., Morrical M.D., Donigan K.A., Weidhaas J.B., Sweasy J.B.,
RA Averill A.M., Tomczak J.A., Morrical S.W.;
RT "Tumor-associated mutations in a conserved structural motif alter physical
RT and biochemical properties of human RAD51 recombinase.";
RL Nucleic Acids Res. 43:1098-1111(2015).
CC -!- FUNCTION: Plays an important role in homologous strand exchange, a key
CC step in DNA repair through homologous recombination (HR)
CC (PubMed:18417535, PubMed:20348101, PubMed:12205100, PubMed:20231364,
CC PubMed:23754376, PubMed:23509288, PubMed:28575658, PubMed:26681308).
CC Binds to single-stranded DNA in an ATP-dependent manner to form
CC nucleoprotein filaments which are essential for the homology search and
CC strand exchange (PubMed:18417535, PubMed:20348101, PubMed:12205100,
CC PubMed:20231364, PubMed:23754376, PubMed:23509288, PubMed:28575658,
CC PubMed:26681308). Catalyzes the recognition of homology and strand
CC exchange between homologous DNA partners to form a joint molecule
CC between a processed DNA break and the repair template (PubMed:18417535,
CC PubMed:20348101, PubMed:12205100, PubMed:20231364, PubMed:23754376,
CC PubMed:23509288, PubMed:28575658, PubMed:26681308). Recruited to
CC resolve stalled replication forks during replication stress
CC (PubMed:27797818, PubMed:31844045). Part of a PALB2-scaffolded HR
CC complex containing BRCA2 and RAD51C and which is thought to play a role
CC in DNA repair by HR (PubMed:24141787, PubMed:12442171). Plays a role in
CC regulating mitochondrial DNA copy number under conditions of oxidative
CC stress in the presence of RAD51C and XRCC3 (PubMed:20413593). Also
CC involved in interstrand cross-link repair (PubMed:26253028).
CC {ECO:0000269|PubMed:12205100, ECO:0000269|PubMed:12442171,
CC ECO:0000269|PubMed:18417535, ECO:0000269|PubMed:20231364,
CC ECO:0000269|PubMed:20348101, ECO:0000269|PubMed:20413593,
CC ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:23754376,
CC ECO:0000269|PubMed:24141787, ECO:0000269|PubMed:26253028,
CC ECO:0000269|PubMed:26681308, ECO:0000269|PubMed:27797818,
CC ECO:0000269|PubMed:28575658, ECO:0000269|PubMed:31844045}.
CC -!- SUBUNIT: Forms linear homooligomers, giving rise to a RAD51
CC nucleoprotein filament, which is essential for strand-pairing reactions
CC during DNA recombination. Interacts with BRCA1 and either directly or
CC indirectly with p53. Interacts with XRCC3, RAD54L and RAD54B. Interacts
CC with the BCDX2 subcomplex RAD51C:RAD51B. Component of the homologous
CC recombination repair (HR) complex composed of ERCC5/XPG, BRCA2, PALB2,
CC DSS1 and RAD51 (PubMed:26833090). Interacts directly with PALB2 which
CC may serve as a scaffold for a HR complex containing PALB2, BRCA2,
CC RAD51C, RAD51 and XRCC3. Interacts with RAD51AP1 and RAD51AP2.
CC Interacts with CHEK1, and this may require prior phosphorylation of
CC CHEK1. Interacts with the MND1-PSMC3IP heterodimer. Found in a complex,
CC at least composed of BLM, RAD51 and SPIDR; the complex formation is
CC mediated by SPIDR. Interacts with SPIDR; the interaction is direct and
CC recruits RAD51 to DNA damage sites. Interacts with FIGNL1 (via N-
CC terminal one-half region); the interaction is direct. Interacts with
CC RAD51AP1 (via C-terminal region); the interaction is direct. Interacts
CC with NABP2, RPA1, PALB2 and RAD51. Interacts with SWI5/C9orf119, and at
CC lower level with SFR1/MEIR5. Interacts with hyperphosphorylated RPA2;
CC this interaction is necessary for efficient recruitment to chromatin in
CC response to DNA damage. Interacts with SWSAP1; involved in homologous
CC recombination repair. Interacts with PARPBP, BRCA2 and RECQL5; these
CC interactions interfere with the formation of the RAD51-DNA homologous
CC recombination structure. Interacts with POLQ; POLQ acts as an inhibitor
CC of homology-recombination repair (HR) pathway by limiting RAD51
CC accumulation at resected ends (PubMed:25642963). Interacts with FBH1
CC (PubMed:23393192). Interacts with POLN (PubMed:19995904). Interacts
CC with RFWD3 (PubMed:28575658). Interacts with the MCM8-MCM9 complex; the
CC interaction recruits RAD51 to DNA damage sites (PubMed:23401855).
CC Component of a multiprotein complex with MEIOB and SPATA22. Interacts
CC with the complex BRME1:HSF2BP:BRCA2 (By similarity). Interacts with
CC HELQ; stimulating HELQ DNA helicase activity and ability to unwing DNA
CC (PubMed:34937945). Interacts with MMS22L; the interaction is direct and
CC promotes recruitment of RAD51 to sites of DNA damage (PubMed:27797818).
CC Interacts with the ATAD5 RFC-like complex (PubMed:31844045). Within the
CC ATAD5 RFC-like complex, interacts with ATAD5 (via N-terminus); the
CC interaction is direct and enhanced under replication stress
CC (PubMed:31844045). Interacts with WDR48; the interaction is enhanced
CC under replication stress (PubMed:31844045).
CC {ECO:0000250|UniProtKB:Q08297, ECO:0000269|PubMed:10851248,
CC ECO:0000269|PubMed:11842113, ECO:0000269|PubMed:12427746,
CC ECO:0000269|PubMed:12442171, ECO:0000269|PubMed:14580352,
CC ECO:0000269|PubMed:15665856, ECO:0000269|PubMed:16990250,
CC ECO:0000269|PubMed:18449195, ECO:0000269|PubMed:19995904,
CC ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:20231364,
CC ECO:0000269|PubMed:20348101, ECO:0000269|PubMed:20705237,
CC ECO:0000269|PubMed:20871615, ECO:0000269|PubMed:21252223,
CC ECO:0000269|PubMed:21965664, ECO:0000269|PubMed:22153967,
CC ECO:0000269|PubMed:23393192, ECO:0000269|PubMed:23401855,
CC ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:23754376,
CC ECO:0000269|PubMed:24141787, ECO:0000269|PubMed:25642963,
CC ECO:0000269|PubMed:26833090, ECO:0000269|PubMed:27797818,
CC ECO:0000269|PubMed:28575658, ECO:0000269|PubMed:31844045,
CC ECO:0000269|PubMed:34937945, ECO:0000269|PubMed:9192668,
CC ECO:0000269|PubMed:9321665, ECO:0000269|PubMed:9396801,
CC ECO:0000269|PubMed:9461559}.
CC -!- INTERACTION:
CC Q06609; P51587: BRCA2; NbExp=46; IntAct=EBI-297202, EBI-79792;
CC Q06609; O14757: CHEK1; NbExp=3; IntAct=EBI-297202, EBI-974488;
CC Q06609; Q00341: HDLBP; NbExp=2; IntAct=EBI-297202, EBI-1049478;
CC Q06609; Q13007: IL24; NbExp=2; IntAct=EBI-297202, EBI-3915542;
CC Q06609; Q96KN1: LRATD2; NbExp=4; IntAct=EBI-297202, EBI-9057780;
CC Q06609; Q14676: MDC1; NbExp=3; IntAct=EBI-297202, EBI-495644;
CC Q06609; P11245: NAT2; NbExp=4; IntAct=EBI-297202, EBI-9057228;
CC Q06609; Q9BZ95: NSD3; NbExp=4; IntAct=EBI-297202, EBI-3390132;
CC Q06609; Q86YC2: PALB2; NbExp=8; IntAct=EBI-297202, EBI-1222653;
CC Q06609; O75417-1: POLQ; NbExp=3; IntAct=EBI-297202, EBI-16141065;
CC Q06609; Q06609: RAD51; NbExp=11; IntAct=EBI-297202, EBI-297202;
CC Q06609; Q96B01-2: RAD51AP1; NbExp=6; IntAct=EBI-297202, EBI-1178743;
CC Q06609; Q96B01-3: RAD51AP1; NbExp=6; IntAct=EBI-297202, EBI-1178748;
CC Q06609; O43502: RAD51C; NbExp=6; IntAct=EBI-297202, EBI-2267048;
CC Q06609; P43351: RAD52; NbExp=3; IntAct=EBI-297202, EBI-706448;
CC Q06609; Q14159: SPIDR; NbExp=6; IntAct=EBI-297202, EBI-11318692;
CC Q06609; Q6NVH7: SWSAP1; NbExp=2; IntAct=EBI-297202, EBI-5281637;
CC Q06609; P04637: TP53; NbExp=2; IntAct=EBI-297202, EBI-366083;
CC Q06609; O43542: XRCC3; NbExp=5; IntAct=EBI-297202, EBI-2849976;
CC Q06609-1; P51587: BRCA2; NbExp=12; IntAct=EBI-15557721, EBI-79792;
CC Q06609-1; Q06609-1: RAD51; NbExp=4; IntAct=EBI-15557721, EBI-15557721;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12442171,
CC ECO:0000269|PubMed:15665856, ECO:0000269|PubMed:18417535,
CC ECO:0000269|PubMed:19783859, ECO:0000269|PubMed:23401855,
CC ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:26681308,
CC ECO:0000269|PubMed:26833090, ECO:0000269|PubMed:9192668}. Cytoplasm
CC {ECO:0000269|PubMed:16215984, ECO:0000269|PubMed:26681308}. Cytoplasm,
CC perinuclear region. Mitochondrion matrix {ECO:0000269|PubMed:20413593}.
CC Chromosome {ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:27797818,
CC ECO:0000269|PubMed:31844045}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:21276791}.
CC Note=Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon
CC induction of DNA damage (PubMed:20154705). DNA damage induces an
CC increase in nuclear levels (PubMed:20154705). Together with FIGNL1,
CC redistributed in discrete nuclear DNA damage-induced foci after
CC ionizing radiation (IR) or camptothecin (CPT) treatment
CC (PubMed:23754376). Accumulated at sites of DNA damage in a SPIDR-
CC dependent manner (PubMed:23509288). Recruited at sites of DNA damage in
CC a MCM9-MCM8-dependent manner (PubMed:23401855). Colocalizes with
CC ERCC5/XPG to nuclear foci in S phase (PubMed:26833090). Recruited to
CC stalled replication forks during replication stress by the TONSL-MMS22L
CC complex, as well as ATAD5 and WDR48 in an ATR-dependent manner
CC (PubMed:27797818, PubMed:31844045). {ECO:0000269|PubMed:20154705,
CC ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:23509288,
CC ECO:0000269|PubMed:23754376, ECO:0000269|PubMed:26833090,
CC ECO:0000269|PubMed:27797818, ECO:0000269|PubMed:31844045}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q06609-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q06609-2; Sequence=VSP_005556;
CC Name=3;
CC IsoId=Q06609-3; Sequence=VSP_041724, VSP_041725;
CC Name=4;
CC IsoId=Q06609-4; Sequence=VSP_043655;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis and thymus, followed by
CC small intestine, placenta, colon, pancreas and ovary. Weakly expressed
CC in breast.
CC -!- INDUCTION: Stress-induced increase in the mitochondrial levels is seen.
CC {ECO:0000269|PubMed:20413593}.
CC -!- DOMAIN: The nuclear localization may reside in the C-terminus (between
CC 259 and 339 AA).
CC -!- PTM: Ubiquitinated by the SCF(FBH1) E3 ubiquitin ligase complex,
CC regulating RAD51 subcellular location and preventing its association
CC with DNA. Ubiquitinated by RFWD3 in response to DNA damage:
CC ubiquitination leads to degradation by the proteasome, promoting
CC homologous recombination (PubMed:28575658).
CC {ECO:0000269|PubMed:23393192, ECO:0000269|PubMed:28575658}.
CC -!- PTM: Phosphorylated. Phosphorylation of Thr-309 by CHEK1 may enhance
CC association with chromatin at sites of DNA damage and promote DNA
CC repair by homologous recombination. Phosphorylation by ABL1 inhibits
CC function. {ECO:0000269|PubMed:15665856, ECO:0000269|PubMed:9461559}.
CC -!- DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy
CC originating from breast epithelial tissue. Breast neoplasms can be
CC distinguished by their histologic pattern. Invasive ductal carcinoma is
CC by far the most common type. Breast cancer is etiologically and
CC genetically heterogeneous. Important genetic factors have been
CC indicated by familial occurrence and bilateral involvement. Mutations
CC at more than one locus can be involved in different families or even in
CC the same case. {ECO:0000269|PubMed:10807537,
CC ECO:0000269|PubMed:25539919}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry.
CC -!- DISEASE: Mirror movements 2 (MRMV2) [MIM:614508]: A disorder
CC characterized by contralateral involuntary movements that mirror
CC voluntary ones. While mirror movements are occasionally found in young
CC children, persistence beyond the age of 10 is abnormal. Mirror
CC movements occur more commonly in the upper extremities.
CC {ECO:0000269|PubMed:22305526}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Fanconi anemia, complementation group R (FANCR) [MIM:617244]:
CC A disorder affecting all bone marrow elements and resulting in anemia,
CC leukopenia and thrombopenia. It is associated with cardiac, renal and
CC limb malformations, dermal pigmentary changes, and a predisposition to
CC the development of malignancies. At the cellular level it is associated
CC with hypersensitivity to DNA-damaging agents, chromosomal instability
CC (increased chromosome breakage) and defective DNA repair.
CC {ECO:0000269|PubMed:26253028, ECO:0000269|PubMed:26681308}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 3]: Mutagenesis of Arg-264 to Ala inhibits
CC nuclear localization. Mutagenesis of Lys-264 to Gln inhibits nuclear
CC localization. Deletion of 254-Arg-Lys-255 inhibits nuclear
CC localization. {ECO:0000269|PubMed:18417535}.
CC -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rad51/";
CC ---------------------------------------------------------------------------
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DR EMBL; D13804; BAA02962.1; -; mRNA.
DR EMBL; D14134; BAA03189.1; -; mRNA.
DR EMBL; AF165094; AAD49705.1; -; Genomic_DNA.
DR EMBL; AF165088; AAD49705.1; JOINED; Genomic_DNA.
DR EMBL; AF165089; AAD49705.1; JOINED; Genomic_DNA.
DR EMBL; AF165090; AAD49705.1; JOINED; Genomic_DNA.
DR EMBL; AF165091; AAD49705.1; JOINED; Genomic_DNA.
DR EMBL; AF165092; AAD49705.1; JOINED; Genomic_DNA.
DR EMBL; AF165093; AAD49705.1; JOINED; Genomic_DNA.
DR EMBL; AF233744; AAF69145.1; -; Genomic_DNA.
DR EMBL; AF233740; AAF69145.1; JOINED; Genomic_DNA.
DR EMBL; AF233741; AAF69145.1; JOINED; Genomic_DNA.
DR EMBL; AF233742; AAF69145.1; JOINED; Genomic_DNA.
DR EMBL; AF236021; AAF69145.1; JOINED; Genomic_DNA.
DR EMBL; AF233743; AAF69145.1; JOINED; Genomic_DNA.
DR EMBL; EU362635; ABY59731.1; -; mRNA.
DR EMBL; AY196785; AAN87149.1; -; Genomic_DNA.
DR EMBL; AK131299; BAD18467.1; -; mRNA.
DR EMBL; AK291969; BAF84658.1; -; mRNA.
DR EMBL; AK313503; BAG36283.1; -; mRNA.
DR EMBL; CR536559; CAG38796.1; -; mRNA.
DR EMBL; AC012476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471125; EAW92434.1; -; Genomic_DNA.
DR EMBL; CH471125; EAW92432.1; -; Genomic_DNA.
DR EMBL; CH471125; EAW92435.1; -; Genomic_DNA.
DR EMBL; BC001459; AAH01459.1; -; mRNA.
DR CCDS; CCDS10062.1; -. [Q06609-1]
DR CCDS; CCDS53931.1; -. [Q06609-4]
DR CCDS; CCDS53932.1; -. [Q06609-3]
DR PIR; I58295; I58295.
DR RefSeq; NP_001157741.1; NM_001164269.1. [Q06609-4]
DR RefSeq; NP_001157742.1; NM_001164270.1. [Q06609-3]
DR RefSeq; NP_002866.2; NM_002875.4. [Q06609-1]
DR RefSeq; NP_597994.3; NM_133487.3. [Q06609-4]
DR RefSeq; XP_006720689.1; XM_006720626.3. [Q06609-1]
DR RefSeq; XP_011520159.1; XM_011521857.2. [Q06609-1]
DR RefSeq; XP_011520160.1; XM_011521858.2. [Q06609-1]
DR RefSeq; XP_011520161.1; XM_011521859.2. [Q06609-1]
DR RefSeq; XP_011520162.1; XM_011521860.2. [Q06609-1]
DR RefSeq; XP_011520163.1; XM_011521861.2. [Q06609-3]
DR PDB; 1B22; NMR; -; A=1-114.
DR PDB; 1N0W; X-ray; 1.70 A; A=97-339.
DR PDB; 5H1B; EM; 4.40 A; A/B/C=1-339.
DR PDB; 5H1C; EM; 4.50 A; A/B/C=1-339.
DR PDB; 5JZC; EM; 4.20 A; A/B/C/D/E/F/G=1-339.
DR PDB; 5NP7; EM; 4.20 A; A/B/C/D/E/F/G=1-339.
DR PDB; 5NWL; X-ray; 3.93 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-339.
DR PDB; 7C9A; EM; 3.43 A; A/B/C=1-339.
DR PDB; 7EJC; EM; 2.97 A; A/B/C=1-339.
DR PDB; 7EJE; EM; 3.98 A; A/B/C=1-339.
DR PDBsum; 1B22; -.
DR PDBsum; 1N0W; -.
DR PDBsum; 5H1B; -.
DR PDBsum; 5H1C; -.
DR PDBsum; 5JZC; -.
DR PDBsum; 5NP7; -.
DR PDBsum; 5NWL; -.
DR PDBsum; 7C9A; -.
DR PDBsum; 7EJC; -.
DR PDBsum; 7EJE; -.
DR AlphaFoldDB; Q06609; -.
DR BMRB; Q06609; -.
DR SMR; Q06609; -.
DR BioGRID; 111825; 235.
DR ComplexPortal; CPX-955; BRCC ubiquitin ligase complex.
DR CORUM; Q06609; -.
DR DIP; DIP-462N; -.
DR ELM; Q06609; -.
DR IntAct; Q06609; 129.
DR MINT; Q06609; -.
DR BindingDB; Q06609; -.
DR ChEMBL; CHEMBL2034807; -.
DR DrugBank; DB12742; Amuvatinib.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR iPTMnet; Q06609; -.
DR PhosphoSitePlus; Q06609; -.
DR BioMuta; RAD51; -.
DR DMDM; 548663; -.
DR EPD; Q06609; -.
DR jPOST; Q06609; -.
DR MassIVE; Q06609; -.
DR MaxQB; Q06609; -.
DR PeptideAtlas; Q06609; -.
DR PRIDE; Q06609; -.
DR ProteomicsDB; 58464; -. [Q06609-1]
DR ProteomicsDB; 58465; -. [Q06609-2]
DR ProteomicsDB; 58466; -. [Q06609-3]
DR ProteomicsDB; 58467; -. [Q06609-4]
DR Antibodypedia; 4162; 970 antibodies from 45 providers.
DR DNASU; 5888; -.
DR Ensembl; ENST00000267868.8; ENSP00000267868.3; ENSG00000051180.17. [Q06609-1]
DR Ensembl; ENST00000382643.7; ENSP00000372088.3; ENSG00000051180.17. [Q06609-4]
DR Ensembl; ENST00000423169.6; ENSP00000406602.2; ENSG00000051180.17. [Q06609-3]
DR Ensembl; ENST00000532743.6; ENSP00000433924.2; ENSG00000051180.17. [Q06609-1]
DR Ensembl; ENST00000557850.5; ENSP00000454176.1; ENSG00000051180.17. [Q06609-2]
DR Ensembl; ENST00000645673.2; ENSP00000493712.2; ENSG00000051180.17. [Q06609-4]
DR GeneID; 5888; -.
DR KEGG; hsa:5888; -.
DR MANE-Select; ENST00000267868.8; ENSP00000267868.3; NM_002875.5; NP_002866.2.
DR UCSC; uc001zmi.5; human. [Q06609-1]
DR CTD; 5888; -.
DR DisGeNET; 5888; -.
DR GeneCards; RAD51; -.
DR GeneReviews; RAD51; -.
DR HGNC; HGNC:9817; RAD51.
DR HPA; ENSG00000051180; Tissue enhanced (lymphoid tissue, testis).
DR MalaCards; RAD51; -.
DR MIM; 114480; phenotype.
DR MIM; 179617; gene.
DR MIM; 614508; phenotype.
DR MIM; 617244; phenotype.
DR neXtProt; NX_Q06609; -.
DR OpenTargets; ENSG00000051180; -.
DR Orphanet; 238722; Familial congenital mirror movements.
DR Orphanet; 84; Fanconi anemia.
DR Orphanet; 145; Hereditary breast and ovarian cancer syndrome.
DR PharmGKB; PA34176; -.
DR VEuPathDB; HostDB:ENSG00000051180; -.
DR GeneTree; ENSGT00940000156157; -.
DR HOGENOM; CLU_041732_3_0_1; -.
DR InParanoid; Q06609; -.
DR OMA; TFRIYLR; -.
DR OrthoDB; 877394at2759; -.
DR PhylomeDB; Q06609; -.
DR TreeFam; TF101218; -.
DR BRENDA; 3.6.4.B7; 2681.
DR PathwayCommons; Q06609; -.
DR Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
DR Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR Reactome; R-HSA-912446; Meiotic recombination.
DR Reactome; R-HSA-9701192; Defective HDR through Homologous Recombination (HRR) due to BRCA1 loss-of-function.
DR Reactome; R-HSA-9704331; Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function.
DR Reactome; R-HSA-9704646; Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function.
DR Reactome; R-HSA-9709570; Impaired BRCA2 binding to RAD51.
DR Reactome; R-HSA-9709603; Impaired BRCA2 binding to PALB2.
DR SignaLink; Q06609; -.
DR SIGNOR; Q06609; -.
DR BioGRID-ORCS; 5888; 773 hits in 1097 CRISPR screens.
DR ChiTaRS; RAD51; human.
DR EvolutionaryTrace; Q06609; -.
DR GeneWiki; RAD51; -.
DR GenomeRNAi; 5888; -.
DR Pharos; Q06609; Tchem.
DR PRO; PR:Q06609; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q06609; protein.
DR Bgee; ENSG00000051180; Expressed in buccal mucosa cell and 129 other tissues.
DR ExpressionAtlas; Q06609; baseline and differential.
DR Genevisible; Q06609; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0000793; C:condensed chromosome; ISS:UniProtKB.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000800; C:lateral element; IDA:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
DR GO; GO:0000152; C:nuclear ubiquitin ligase complex; IDA:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IDA:MGI.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0070182; F:DNA polymerase binding; IPI:UniProtKB.
DR GO; GO:0000150; F:DNA strand exchange activity; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0072757; P:cellular response to camptothecin; IDA:UniProtKB.
DR GO; GO:0072719; P:cellular response to cisplatin; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
DR GO; GO:0072711; P:cellular response to hydroxyurea; IEA:Ensembl.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0000730; P:DNA recombinase assembly; IMP:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; TAS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IC:ComplexPortal.
DR GO; GO:0036297; P:interstrand cross-link repair; IMP:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; ISS:UniProtKB.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IEA:InterPro.
DR GO; GO:0051106; P:positive regulation of DNA ligation; IDA:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IC:ComplexPortal.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IC:ComplexPortal.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IDA:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0031297; P:replication fork processing; IDA:UniProtKB.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IEA:Ensembl.
DR GO; GO:1904631; P:response to glucoside; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0042148; P:strand invasion; IBA:GO_Central.
DR GO; GO:0000722; P:telomere maintenance via recombination; ISS:BHF-UCL.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; ISS:BHF-UCL.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR DisProt; DP01622; -.
DR Gene3D; 3.40.50.300; -; 1.
DR IDEAL; IID00241; -.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011941; DNA_recomb/repair_Rad51.
DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033925; Rad51_DMC1_RadA.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR Pfam; PF08423; Rad51; 1.
DR PIRSF; PIRSF005856; Rad51; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47794; SSF47794; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02239; recomb_RAD51; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Chromosome;
KW Cytoplasm; Cytoskeleton; Disease variant; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Fanconi anemia; Isopeptide bond; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..339
FT /note="DNA repair protein RAD51 homolog 1"
FT /id="PRO_0000122932"
FT DOMAIN 48..77
FT /note="HhH"
FT REGION 184..257
FT /note="Interaction with PALB2"
FT MOTIF 245..260
FT /note="Nuclear export signal; masked by the interaction
FT with BRCA2"
FT /evidence="ECO:0000305|PubMed:24013206"
FT BINDING 127..134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 54
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:9461559"
FT MOD_RES 309
FT /note="Phosphothreonine; by CHEK1"
FT /evidence="ECO:0000269|PubMed:15665856"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23393192"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23393192"
FT VAR_SEQ 76..114
FT /note="AEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQ -> TESRSVARL
FT ECNSVILVYCTLRLSGSSDSPASASRVVGTT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043655"
FT VAR_SEQ 77..173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_005556"
FT VAR_SEQ 259..284
FT /note="FGVAVVITNQVVAQVDGAAMFAADPK -> IVSEERKRGNQNLQNLRLSLSS
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18417535"
FT /id="VSP_041724"
FT VAR_SEQ 285..339
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18417535"
FT /id="VSP_041725"
FT VARIANT 131
FT /note="T -> P (in FANCR; causes dominant negative loss of
FT function in interstrand cross-link repair; shows high basal
FT DNA-independent ATPase activity; results in decreased DNA
FT binding)"
FT /evidence="ECO:0000269|PubMed:26253028"
FT /id="VAR_076870"
FT VARIANT 150
FT /note="R -> Q (in BC; decreased ATPase activity in the
FT presence of stoichiometric ss-DNA concentrations with
FT respect to RAD51; 3 to 4-fold decrease of affinity for ATP;
FT dbSNP:rs121917739)"
FT /evidence="ECO:0000269|PubMed:10807537,
FT ECO:0000269|PubMed:25539919"
FT /id="VAR_010899"
FT VARIANT 293
FT /note="A -> T (in FANCR; dominant negative; impaired
FT function in DNA repair via homologous recombination;
FT impaired DNA-binding and formation of nucleoprotein
FT filaments; impaired DNA-dependent ATPase activity; no
FT effect on subcellular location; dbSNP:rs1057519413)"
FT /evidence="ECO:0000269|PubMed:26681308"
FT /id="VAR_076593"
FT MUTAGEN 58
FT /note="K->R: Impaired ubiquitination; when associated with
FT R-64."
FT /evidence="ECO:0000269|PubMed:23393192"
FT MUTAGEN 64
FT /note="K->R: Impaired ubiquitination; when associated with
FT R-58."
FT /evidence="ECO:0000269|PubMed:23393192"
FT MUTAGEN 86
FT /note="F->A: Loss of homooligomerization."
FT /evidence="ECO:0000269|PubMed:12442171"
FT MUTAGEN 89
FT /note="A->E: Loss of homooligomerization."
FT /evidence="ECO:0000269|PubMed:12442171"
FT MUTAGEN 208..209
FT /note="SA->LE: Disrupts interaction with BRCA2, no effect
FT on homooligomerization, promotes interaction with XPO1 and
FT cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:14580352,
FT ECO:0000269|PubMed:24013206"
FT MUTAGEN 309
FT /note="T->A: Confers hypersensitivity to hydroxyurea."
FT /evidence="ECO:0000269|PubMed:15665856"
FT CONFLICT 313
FT /note="K -> Q (in Ref. 1; BAA02962)"
FT /evidence="ECO:0000305"
FT HELIX 25..30
FT /evidence="ECO:0007829|PDB:7C9A"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:7C9A"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:7C9A"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1B22"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:7C9A"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:1B22"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:7C9A"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:7C9A"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:7C9A"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:7C9A"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:1N0W"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1N0W"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1N0W"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:1N0W"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:7C9A"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:1N0W"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1N0W"
FT STRAND 154..164
FT /evidence="ECO:0007829|PDB:1N0W"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:1N0W"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:1N0W"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:1N0W"
FT HELIX 197..213
FT /evidence="ECO:0007829|PDB:1N0W"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:1N0W"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:7C9A"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:1N0W"
FT HELIX 238..259
FT /evidence="ECO:0007829|PDB:1N0W"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:1N0W"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:7C9A"
FT HELIX 289..295
FT /evidence="ECO:0007829|PDB:7C9A"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:1N0W"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:1N0W"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:7C9A"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:1N0W"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:1N0W"
SQ SEQUENCE 339 AA; 36966 MW; 26578E6206DEDEDA CRC64;
MAMQMQLEAN ADTSVEEESF GPQPISRLEQ CGINANDVKK LEEAGFHTVE AVAYAPKKEL
INIKGISEAK ADKILAEAAK LVPMGFTTAT EFHQRRSEII QITTGSKELD KLLQGGIETG
SITEMFGEFR TGKTQICHTL AVTCQLPIDR GGGEGKAMYI DTEGTFRPER LLAVAERYGL
SGSDVLDNVA YARAFNTDHQ TQLLYQASAM MVESRYALLI VDSATALYRT DYSGRGELSA
RQMHLARFLR MLLRLADEFG VAVVITNQVV AQVDGAAMFA ADPKKPIGGN IIAHASTTRL
YLRKGRGETR ICKIYDSPCL PEAEAMFAIN ADGVGDAKD
