RA51B_HUMAN
ID RA51B_HUMAN Reviewed; 384 AA.
AC O15315; O60914; O75210; Q3Y4F8; Q6FHX8; Q86SY3; Q86SY4; Q86TR0; Q86U92;
AC Q86U93; Q86U94; Q8N6H4; Q9UPL5;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=DNA repair protein RAD51 homolog 2;
DE Short=R51H2;
DE AltName: Full=RAD51 homolog B;
DE Short=Rad51B;
DE AltName: Full=RAD51-like protein 1;
GN Name=RAD51B; Synonyms=RAD51L1, REC2;
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 2).
RX PubMed=9207106; DOI=10.1073/pnas.94.14.7417;
RA Rice M.C., Smith S.T., Bullrich F., Havre P., Kmiec E.B.;
RT "Isolation of human and mouse genes based on homology to REC2, a
RT recombinational repair gene from the fungus Ustilago maydis.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7417-7422(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=9441753; DOI=10.1006/geno.1997.5062;
RA Albala J.S., Thelen M.P., Prange C.K., Fan W., Christensen M.,
RA Thompson L.H., Lennon G.G.;
RT "Identification of a novel human RAD51 homolog, RAD51B.";
RL Genomics 46:476-479(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=9512535; DOI=10.1093/nar/26.7.1653;
RA Cartwright R., Dunn A.M., Simpson P.J., Tambini C.E., Thacker J.;
RT "Isolation of novel human and mouse genes of the recA/RAD51 recombination-
RT repair gene family.";
RL Nucleic Acids Res. 26:1653-1659(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-9; CYS-82; TRP-172;
RP CYS-180; ARG-243 AND ALA-250.
RG NIEHS SNPs program;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 253-310, AND CHROMOSOMAL TRANSLOCATION WITH
RP HMGA2.
RX PubMed=12649198;
RA Quade B.J., Weremowicz S., Neskey D.M., Vanni R., Ladd C., Dal Cin P.,
RA Morton C.C.;
RT "Fusion transcripts involving HMGA2 are not a common molecular mechanism in
RT uterine leiomyomata with rearrangements in 12q15.";
RL Cancer Res. 63:1351-1358(2003).
RN [11]
RP FUNCTION, AND IDENTIFICATION IN THE BCDX2 COMPLEX WITH RAD51C; RAD51D AND
RP XRCC2.
RX PubMed=11751635; DOI=10.1101/gad.947001;
RA Masson J.Y., Tarsounas M.C., Stasiak A.Z., Stasiak A., Shah R.,
RA McIlwraith M.J., Benson F.E., West S.C.;
RT "Identification and purification of two distinct complexes containing the
RT five RAD51 paralogs.";
RL Genes Dev. 15:3296-3307(2001).
RN [12]
RP FUNCTION, AND INTERACTION WITH RAD51C.
RX PubMed=11751636; DOI=10.1101/gad.935501;
RA Sigurdsson S., Van Komen S., Bussen W., Schild D., Albala J.S., Sung P.;
RT "Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-
RT catalyzed DNA strand exchange.";
RL Genes Dev. 15:3308-3318(2001).
RN [13]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D AND XRCC2.
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 [14]
RP INTERACTION WITH RAD51C, AND SUBUNIT.
RX PubMed=11744692; DOI=10.1074/jbc.m108306200;
RA Miller K.A., Yoshikawa D.M., McConnell I.R., Clark R., Schild D.,
RA Albala J.S.;
RT "RAD51C interacts with RAD51B and is central to a larger protein complex in
RT vivo exclusive of RAD51.";
RL J. Biol. Chem. 277:8406-8411(2002).
RN [15]
RP IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D AND XRCC2.
RX PubMed=11842112; DOI=10.1093/nar/30.4.1001;
RA Wiese C., Collins D.W., Albala J.S., Thompson L.H., Kronenberg A.,
RA Schild D.;
RT "Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human
RT cells.";
RL Nucleic Acids Res. 30:1001-1008(2002).
RN [16]
RP INTERACTION WITH RAD51 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 [17]
RP CHROMOSOMAL TRANSLOCATION WITH HMGA2.
RX PubMed=9892177;
RA Schoenmakers E.F.P.M., Huysmans C., Van de Ven W.J.M.;
RT "Allelic knockout of novel splice variants of human recombination repair
RT gene RAD51B in t(12;14) uterine leiomyomas.";
RL Cancer Res. 59:19-23(1999).
RN [18]
RP CHROMOSOMAL TRANSLOCATION WITH HMGA1.
RX PubMed=11978964; DOI=10.1159/000057011;
RA Blank C., Schoenmakers E.F.P.M., Rogalla P., Huys E.H., van Rijk A.A.,
RA Drieschner N., Bullerdiek J.;
RT "Intragenic breakpoint within RAD51L1 in a t(6;14)(p21.3;q24) of a
RT pulmonary chondroid hamartoma.";
RL Cytogenet. Cell Genet. 95:17-19(2001).
RN [19]
RP FUNCTION.
RX PubMed=12441335; DOI=10.1074/jbc.m210899200;
RA Yokoyama H., Kurumizaka H., Ikawa S., Yokoyama S., Shibata T.;
RT "Holliday junction binding activity of the human Rad51B protein.";
RL J. Biol. Chem. 278:2767-2772(2003).
RN [20]
RP INTERACTION WITH RAD51C.
RX PubMed=14704354; DOI=10.1093/nar/gkg925;
RA Miller K.A., Sawicka D., Barsky D., Albala J.S.;
RT "Domain mapping of the Rad51 paralog protein complexes.";
RL Nucleic Acids Res. 32:169-178(2004).
RN [21]
RP PHOSPHORYLATION BY BCR-ABL, AND MUTAGENESIS OF PRO-326.
RX PubMed=19657362; DOI=10.1038/leu.2009.164;
RA Slupianek A., Jozwiakowski S.K., Gurdek E., Skorski T.;
RT "BCR/ABL kinase interacts with and phosphorylates the RAD51 paralog,
RT RAD51B.";
RL Leukemia 23:2308-2310(2009).
RN [22]
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 [23]
RP FUNCTION IN MITOTIC CELL PROGRESSION.
RX PubMed=23108668; DOI=10.1242/jcs.114595;
RA Rodrigue A., Coulombe Y., Jacquet K., Gagne J.P., Roques C., Gobeil S.,
RA Poirier G., Masson J.Y.;
RT "The RAD51 paralogs ensure cellular protection against mitotic defects and
RT aneuploidy.";
RL J. Cell Sci. 126:348-359(2013).
RN [24]
RP FUNCTION OF THE BCDX2 COMPLEX.
RX PubMed=23149936; DOI=10.1128/mcb.00465-12;
RA Chun J., Buechelmaier E.S., Powell S.N.;
RT "Rad51 paralog complexes BCDX2 and CX3 act at different stages in the
RT BRCA1-BRCA2-dependent homologous recombination pathway.";
RL Mol. Cell. Biol. 33:387-395(2013).
RN [25]
RP INTERACTION WITH HELQ.
RX PubMed=24005041; DOI=10.1093/nar/gkt676;
RA Luebben S.W., Kawabata T., Akre M.K., Lee W.L., Johnson C.S.,
RA O'Sullivan M.G., Shima N.;
RT "Helq acts in parallel to Fancc to suppress replication-associated genome
RT instability.";
RL Nucleic Acids Res. 41:10283-10297(2013).
RN [26]
RP ELECTRON MICROSCOPY OF THE BCDX2 COMPLEX, AND DNA-BINDING OF THE BCDX2
RP COMPLEX.
RX PubMed=20207730; DOI=10.1074/jbc.m109.074286;
RA Compton S.A., Ozgur S., Griffith J.D.;
RT "Ring-shaped Rad51 paralog protein complexes bind Holliday junctions and
RT replication forks as visualized by electron microscopy.";
RL J. Biol. Chem. 285:13349-13356(2010).
CC -!- FUNCTION: Involved in the homologous recombination repair (HRR) pathway
CC of double-stranded DNA breaks arising during DNA replication or induced
CC by DNA-damaging agents. May promote the assembly of presynaptic RAD51
CC nucleoprotein filaments. Binds single-stranded DNA and double-stranded
CC DNA and has DNA-dependent ATPase activity. Part of the RAD51 paralog
CC protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR
CC pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment
CC and upstream of RAD51 recruitment. BCDX2 binds predominantly to the
CC intersection of the four duplex arms of the Holliday junction and to
CC junction of replication forks. The BCDX2 complex was originally
CC reported to bind single-stranded DNA, single-stranded gaps in duplex
CC DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex
CC RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase activity
CC suggesting an involvement in early stages of the HR pathway.
CC {ECO:0000269|PubMed:11751635, ECO:0000269|PubMed:11751636,
CC ECO:0000269|PubMed:11842113, ECO:0000269|PubMed:12441335,
CC ECO:0000269|PubMed:23108668, ECO:0000269|PubMed:23149936}.
CC -!- SUBUNIT: Part of the BCDX2 complex consisting of RAD51B, RAD51C, RAD51D
CC and XRCC2; the complex has a ring-like structure arranged into a flat
CC disc around a central channel (PubMed:11744692, PubMed:11751635,
CC PubMed:11751636, PubMed:11842112, PubMed:11842113, PubMed:12427746,
CC PubMed:14704354). The BCDX2 subcomplex RAD51B:RAD51C interacts with
CC RAD51 (PubMed:11744692, PubMed:11751635, PubMed:11751636,
CC PubMed:11842112, PubMed:11842113, PubMed:12427746, PubMed:14704354).
CC Interacts with SWSAP1; involved in homologous recombination repair
CC (PubMed:21965664). Interacts with HELQ (PubMed:24005041).
CC {ECO:0000269|PubMed:11744692, ECO:0000269|PubMed:11751635,
CC ECO:0000269|PubMed:11751636, ECO:0000269|PubMed:11842112,
CC ECO:0000269|PubMed:11842113, ECO:0000269|PubMed:12427746,
CC ECO:0000269|PubMed:14704354, ECO:0000269|PubMed:21965664,
CC ECO:0000269|PubMed:24005041}.
CC -!- INTERACTION:
CC O15315; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-2824089, EBI-10175124;
CC O15315; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2824089, EBI-16439278;
CC O15315; O43502: RAD51C; NbExp=12; IntAct=EBI-2824089, EBI-2267048;
CC O15315; O75771: RAD51D; NbExp=5; IntAct=EBI-2824089, EBI-1055693;
CC O15315; Q86UA6: RPAIN; NbExp=3; IntAct=EBI-2824089, EBI-3907663;
CC O15315; Q6NVH7: SWSAP1; NbExp=2; IntAct=EBI-2824089, EBI-5281637;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=O15315-3; Sequence=Displayed;
CC Name=2; Synonyms=RAD51L1a;
CC IsoId=O15315-1; Sequence=VSP_008819;
CC Name=3; Synonyms=RAD51L1b;
CC IsoId=O15315-2; Sequence=VSP_008818;
CC Name=4;
CC IsoId=O15315-4; Sequence=VSP_008820;
CC Name=5;
CC IsoId=O15315-5; Sequence=VSP_008817, VSP_008818;
CC -!- TISSUE SPECIFICITY: Expressed in a wide range of tissues.
CC -!- PTM: Phosphorylated on tyrosine residues by BCR-ABL.
CC {ECO:0000269|PubMed:19657362}.
CC -!- DISEASE: Note=A chromosomal aberration involving RAD51B is found in
CC pulmonary chondroid hamartoma. Translocation t(6;14)(p21;q23-24) with
CC HMGA1. {ECO:0000269|PubMed:11978964}.
CC -!- DISEASE: Note=A chromosomal aberration involving RAD51B is found in
CC uterine leiomyoma. Translocation t(12;14)(q15;q23-24) with HMGA2.
CC {ECO:0000269|PubMed:12649198, ECO:0000269|PubMed:9892177}.
CC -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD62357.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD66573.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rad51l1/";
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DR EMBL; U92074; AAB63358.1; -; mRNA.
DR EMBL; U84138; AAC39723.1; -; mRNA.
DR EMBL; Y15571; CAA75680.1; -; mRNA.
DR EMBL; BX161515; CAD61950.1; -; mRNA.
DR EMBL; BX248061; CAD62357.1; ALT_INIT; mRNA.
DR EMBL; BX248766; CAD66573.1; ALT_INIT; mRNA.
DR EMBL; DQ160197; AAZ85144.1; -; Genomic_DNA.
DR EMBL; AC004518; AAC32426.1; -; Genomic_DNA.
DR EMBL; AC004518; AAC32425.1; -; Genomic_DNA.
DR EMBL; CR536560; CAG38797.1; -; mRNA.
DR EMBL; CH471061; EAW80957.1; -; Genomic_DNA.
DR EMBL; BC030219; AAH30219.1; -; mRNA.
DR EMBL; AY138857; AAN60542.1; -; mRNA.
DR EMBL; AY138858; AAN60543.1; -; mRNA.
DR EMBL; AY138859; AAN60544.1; -; mRNA.
DR CCDS; CCDS9789.1; -. [O15315-3]
DR CCDS; CCDS9790.1; -. [O15315-2]
DR RefSeq; NP_001308746.1; NM_001321817.1. [O15315-5]
DR RefSeq; NP_002868.1; NM_002877.5. [O15315-1]
DR RefSeq; NP_598193.2; NM_133509.3. [O15315-3]
DR RefSeq; NP_598194.1; NM_133510.3. [O15315-2]
DR AlphaFoldDB; O15315; -.
DR SMR; O15315; -.
DR BioGRID; 111827; 41.
DR CORUM; O15315; -.
DR DIP; DIP-41246N; -.
DR IntAct; O15315; 16.
DR MINT; O15315; -.
DR STRING; 9606.ENSP00000419471; -.
DR iPTMnet; O15315; -.
DR PhosphoSitePlus; O15315; -.
DR BioMuta; RAD51B; -.
DR EPD; O15315; -.
DR jPOST; O15315; -.
DR MassIVE; O15315; -.
DR MaxQB; O15315; -.
DR PaxDb; O15315; -.
DR PeptideAtlas; O15315; -.
DR PRIDE; O15315; -.
DR ProteomicsDB; 48575; -. [O15315-3]
DR ProteomicsDB; 48576; -. [O15315-1]
DR ProteomicsDB; 48577; -. [O15315-2]
DR ProteomicsDB; 48578; -. [O15315-4]
DR ProteomicsDB; 48579; -. [O15315-5]
DR TopDownProteomics; O15315-2; -. [O15315-2]
DR Antibodypedia; 4257; 301 antibodies from 36 providers.
DR DNASU; 5890; -.
DR Ensembl; ENST00000471583.6; ENSP00000418859.1; ENSG00000182185.19. [O15315-2]
DR Ensembl; ENST00000487270.5; ENSP00000419471.1; ENSG00000182185.19. [O15315-3]
DR Ensembl; ENST00000488612.5; ENSP00000420061.1; ENSG00000182185.19. [O15315-4]
DR GeneID; 5890; -.
DR KEGG; hsa:5890; -.
DR MANE-Select; ENST00000471583.6; ENSP00000418859.1; NM_133510.4; NP_598194.1. [O15315-2]
DR UCSC; uc001xkd.4; human. [O15315-3]
DR CTD; 5890; -.
DR DisGeNET; 5890; -.
DR GeneCards; RAD51B; -.
DR HGNC; HGNC:9822; RAD51B.
DR HPA; ENSG00000182185; Low tissue specificity.
DR MIM; 150699; phenotype.
DR MIM; 602948; gene.
DR neXtProt; NX_O15315; -.
DR OpenTargets; ENSG00000182185; -.
DR PharmGKB; PA34178; -.
DR VEuPathDB; HostDB:ENSG00000182185; -.
DR eggNOG; KOG1433; Eukaryota.
DR GeneTree; ENSGT00940000160169; -.
DR HOGENOM; CLU_013059_0_0_1; -.
DR InParanoid; O15315; -.
DR OMA; QLQGNMK; -.
DR OrthoDB; 1345899at2759; -.
DR PhylomeDB; O15315; -.
DR TreeFam; TF101219; -.
DR PathwayCommons; O15315; -.
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-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-9709603; Impaired BRCA2 binding to PALB2.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; O15315; -.
DR SIGNOR; O15315; -.
DR BioGRID-ORCS; 5890; 102 hits in 1081 CRISPR screens.
DR ChiTaRS; RAD51B; human.
DR GeneWiki; RAD51L1; -.
DR GenomeRNAi; 5890; -.
DR Pharos; O15315; Tbio.
DR PRO; PR:O15315; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O15315; protein.
DR Bgee; ENSG00000182185; Expressed in sural nerve and 125 other tissues.
DR ExpressionAtlas; O15315; baseline and differential.
DR Genevisible; O15315; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0033063; C:Rad51B-Rad51C-Rad51D-XRCC2 complex; IDA:UniProtKB.
DR GO; GO:0005657; C:replication fork; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:UniProtKB.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0001832; P:blastocyst growth; IEA:Ensembl.
DR GO; GO:0006310; P:DNA recombination; TAS:ProtInc.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0007131; P:reciprocal meiotic recombination; TAS:ProtInc.
DR GO; GO:0061053; P:somite development; IEA:Ensembl.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033925; Rad51_DMC1_RadA.
DR InterPro; IPR030548; RAD51B.
DR InterPro; IPR020588; RecA_ATP-bd.
DR PANTHER; PTHR46456; PTHR46456; 1.
DR Pfam; PF08423; Rad51; 1.
DR PIRSF; PIRSF005856; Rad51; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50162; RECA_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chromosomal rearrangement; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..384
FT /note="DNA repair protein RAD51 homolog 2"
FT /id="PRO_0000122939"
FT REGION 1..75
FT /note="Interaction with RAD51C"
FT BINDING 108..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT SITE 252..253
FT /note="Breakpoint for translocation to form HMGA2-RAD51B"
FT VAR_SEQ 1..119
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_008817"
FT VAR_SEQ 346..384
FT /note="ETTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF -> AYGNS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:9207106,
FT ECO:0000303|PubMed:9441753, ECO:0000303|Ref.6"
FT /id="VSP_008819"
FT VAR_SEQ 346..384
FT /note="ETTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF -> GQEKP (in
FT isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:9512535, ECO:0000303|Ref.4"
FT /id="VSP_008818"
FT VAR_SEQ 347..384
FT /note="TTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF -> FWHICISGFS
FT IQNRLKENES (in isoform 4)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_008820"
FT VARIANT 9
FT /note="V -> M (in dbSNP:rs34583846)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_025243"
FT VARIANT 82
FT /note="F -> C (in dbSNP:rs35282642)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_025244"
FT VARIANT 172
FT /note="L -> W (in dbSNP:rs34094401)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_025245"
FT VARIANT 180
FT /note="Y -> C (in dbSNP:rs28910275)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_025246"
FT VARIANT 207
FT /note="V -> L (in dbSNP:rs28908168)"
FT /id="VAR_035437"
FT VARIANT 243
FT /note="K -> R (in dbSNP:rs34594234)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_025247"
FT VARIANT 250
FT /note="S -> A (in dbSNP:rs33929366)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_025248"
FT VARIANT 365
FT /note="P -> R (in dbSNP:rs28908468)"
FT /id="VAR_051730"
FT MUTAGEN 326
FT /note="P->L: Abolishes interaction with BCR-ABL SH3
FT domain."
FT /evidence="ECO:0000269|PubMed:19657362"
FT CONFLICT 281
FT /note="S -> P (in Ref. 9; AAN60542/AAN60543/AAN60544)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 42196 MW; DB0B9AE82F44A52B CRC64;
MGSKKLKRVG LSQELCDRLS RHQILTCQDF LCLSPLELMK VTGLSYRGVH ELLCMVSRAC
APKMQTAYGI KAQRSADFSP AFLSTTLSAL DEALHGGVAC GSLTEITGPP GCGKTQFCIM
MSILATLPTN MGGLEGAVVY IDTESAFSAE RLVEIAESRF PRYFNTEEKL LLTSSKVHLY
RELTCDEVLQ RIESLEEEII SKGIKLVILD SVASVVRKEF DAQLQGNLKE RNKFLAREAS
SLKYLAEEFS IPVILTNQIT THLSGALASQ ADLVSPADDL SLSEGTSGSS CVIAALGNTW
SHSVNTRLIL QYLDSERRQI LIAKSPLAPF TSFVYTIKEE GLVLQETTFC SVTQAELNWA
PEILPPQPPE QLGLQMCHHT QLIF
