RA51C_HUMAN
ID RA51C_HUMAN Reviewed; 376 AA.
AC O43502; O43503; Q3B783;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=DNA repair protein RAD51 homolog 3;
DE Short=R51H3;
DE AltName: Full=RAD51 homolog C;
DE AltName: Full=RAD51-like protein 2;
GN Name=RAD51C; Synonyms=RAD51L2;
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] (ISOFORMS 1 AND 2).
RX PubMed=9469824; DOI=10.1093/nar/26.5.1179;
RA Dosanjh M.K., Collins D.W., Fan W., Lennon G.G., Albala J.S., Shen Z.,
RA Schild D.;
RT "Isolation and characterization of RAD51C, a new human member of the RAD51
RT family of related genes.";
RL Nucleic Acids Res. 26:1179-1184(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-144; CYS-249 AND
RP ALA-287.
RG NIEHS SNPs program;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP IDENTIFICATION IN THE BCDX2 COMPLEX WITH RAD51B; RAD51D AND XRCC2, AND
RP IDENTIFICATION IN THE CX3 COMPLEX WITH XRCC3.
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 [7]
RP FUNCTION, AND INTERACTION WITH RAD51B.
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 [8]
RP INTERACTION WITH RAD51B, 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 [9]
RP IDENTIFICATION IN A COMPLEX WITH RAD51B; 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 [10]
RP IDENTIFICATION IN A COMPLEX WITH RAD51B; RAD51D AND XRCC2, AND INTERACTION
RP 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 [11]
RP INTERACTION WITH RAD51 AND RAD51B.
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 [12]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-131.
RX PubMed=12966089; DOI=10.1074/jbc.m308621200;
RA French C.A., Tambini C.E., Thacker J.;
RT "Identification of functional domains in the RAD51L2 (RAD51C) protein and
RT its requirement for gene conversion.";
RL J. Biol. Chem. 278:45445-45450(2003).
RN [13]
RP INTERACTION WITH RAD51B; RAD51D AND XRCC3.
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 [14]
RP FUNCTION, AND MUTAGENESIS OF LYS-131.
RX PubMed=14716019; DOI=10.1126/science.1093037;
RA Liu Y., Masson J.Y., Shah R., O'Regan P., West S.C.;
RT "RAD51C is required for Holliday junction processing in mammalian cells.";
RL Science 303:243-246(2004).
RN [15]
RP FUNCTION, AND 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 [16]
RP FUNCTION, AND INTERACTION WITH RAD51.
RX PubMed=16395335; DOI=10.1038/sj.emboj.7600914;
RA Rodrigue A., Lafrance M., Gauthier M.C., McDonald D., Hendzel M.,
RA West S.C., Jasin M., Masson J.Y.;
RT "Interplay between human DNA repair proteins at a unique double-strand
RT break in vivo.";
RL EMBO J. 25:222-231(2006).
RN [17]
RP FUNCTION, AND 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 [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19451272; DOI=10.1083/jcb.200811079;
RA Badie S., Liao C., Thanasoula M., Barber P., Hill M.A., Tarsounas M.;
RT "RAD51C facilitates checkpoint signaling by promoting CHK2
RT phosphorylation.";
RL J. Cell Biol. 185:587-600(2009).
RN [19]
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 [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
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 [22]
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 [23]
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP FUNCTION OF THE BCDX2 COMPLEX, AND FUNCTION OF THE CX3 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 [26]
RP INTERACTION WITH BRCA2; RAD51 AND PALB2, IDENTIFICATION IN A
RP PALB2-CONTAINING HR COMPLEX, CHARACTERIZATION OF VARIANT BROVCA3 PHE-138,
RP CHARACTERIZATION OF VARIANT ASN-159, AND CHARACTERIZATION OF VARIANT FANCO
RP HIS-258.
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 [27]
RP ELECTRON MICROSCOPY OF THE BCDX2 AND CX3 COMPLEXES, AND DNA-BINDING OF THE
RP BCDX2 AND CX3 COMPLEXES.
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).
RN [28]
RP VARIANT FANCO HIS-258, AND CHARACTERIZATION OF VARIANT FANCO HIS-258.
RX PubMed=20400963; DOI=10.1038/ng.570;
RA Vaz F., Hanenberg H., Schuster B., Barker K., Wiek C., Erven V.,
RA Neveling K., Endt D., Kesterton I., Autore F., Fraternali F., Freund M.,
RA Hartmann L., Grimwade D., Roberts R.G., Schaal H., Mohammed S., Rahman N.,
RA Schindler D., Mathew C.G.;
RT "Mutation of the RAD51C gene in a Fanconi anemia-like disorder.";
RL Nat. Genet. 42:406-409(2010).
RN [29]
RP VARIANTS ARG-3; THR-126; ASN-159; ALA-169; SER-264; VAL-264; ALA-287 AND
RP GLN-366, AND VARIANTS BROVCA3 VAL-125 AND PHE-138.
RX PubMed=20400964; DOI=10.1038/ng.569;
RA Meindl A., Hellebrand H., Wiek C., Erven V., Wappenschmidt B.,
RA Niederacher D., Freund M., Lichtner P., Hartmann L., Schaal H., Ramser J.,
RA Honisch E., Kubisch C., Wichmann H.E., Kast K., Deissler H., Engel C.,
RA Muller-Myhsok B., Neveling K., Kiechle M., Mathew C.G., Schindler D.,
RA Schmutzler R.K., Hanenberg H.;
RT "Germline mutations in breast and ovarian cancer pedigrees establish RAD51C
RT as a human cancer susceptibility gene.";
RL Nat. Genet. 42:410-414(2010).
RN [30]
RP VARIANTS LEU-52; PHE-103 DEL; VAL-114; THR-126; ALA-169; THR-175; CYS-249;
RP VAL-262 AND SER-264, AND VARIANTS BROVCA3 GLU-162; PRO-178 AND ALA-287.
RX PubMed=21990120; DOI=10.1002/humu.21625;
RG Kathleen Cuningham foundation consortium for research into familial breast cancer (kConFab);
RA Thompson E.R., Boyle S.E., Johnson J., Ryland G.L., Sawyer S., Choong D.Y.,
RA Chenevix-Trench G., Trainer A.H., Lindeman G.J., Mitchell G., James P.A.,
RA Campbell I.G.;
RT "Analysis of RAD51C germline mutations in high-risk breast and ovarian
RT cancer families and ovarian cancer patients.";
RL Hum. Mutat. 33:95-99(2012).
CC -!- FUNCTION: Essential for the homologous recombination (HR) pathway of
CC DNA repair. Involved in the homologous recombination repair (HRR)
CC pathway of double-stranded DNA breaks arising during DNA replication or
CC induced by DNA-damaging agents. Part of the RAD51 paralog protein
CC complexes BCDX2 and CX3 which act at different stages of the BRCA1-
CC BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 seems to act
CC downstream of BRCA2 recruitment and upstream of RAD51 recruitment; CX3
CC seems to act downstream of RAD51 recruitment; both complexes bind
CC predominantly to the intersection of the four duplex arms of the
CC Holliday junction (HJ) and to junction of replication forks. The BCDX2
CC complex was originally reported to bind single-stranded DNA, single-
CC stranded gaps in duplex DNA and specifically to nicks in duplex DNA.
CC The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA-
CC dependent ATPase activity suggesting an involvement in early stages of
CC the HR pathway. Involved in RAD51 foci formation in response to DNA
CC damage suggesting an involvement in early stages of HR probably in the
CC invasion step. Has an early function in DNA repair in facilitating
CC phosphorylation of the checkpoint kinase CHEK2 and thereby transduction
CC of the damage signal, leading to cell cycle arrest and HR activation.
CC Participates in branch migration and HJ resolution and thus is
CC important for processing HR intermediates late in the DNA repair
CC process; the function may be linked to the CX3 complex. Part of a
CC PALB2-scaffolded HR complex containing BRCA2 and which is thought to
CC play a role in DNA repair by HR. Protects RAD51 from ubiquitin-mediated
CC degradation that is enhanced following DNA damage. Plays a role in
CC regulating mitochondrial DNA copy number under conditions of oxidative
CC stress in the presence of RAD51 and XRCC3. Contributes to DNA cross-
CC link resistance, sister chromatid cohesion and genomic stability.
CC Involved in maintaining centrosome number in mitosis.
CC {ECO:0000269|PubMed:14716019, ECO:0000269|PubMed:16215984,
CC ECO:0000269|PubMed:16395335, ECO:0000269|PubMed:19451272,
CC ECO:0000269|PubMed:19783859, ECO:0000269|PubMed:20413593,
CC ECO:0000269|PubMed:23108668, ECO:0000269|PubMed:23149936}.
CC -!- SUBUNIT: Part of the RAD51 paralog protein complexes BCDX2 and CX3; the
CC complexes have a ring-like structure arranged into a flat disc around a
CC central channel (PubMed:12427746, PubMed:11751635, PubMed:11751636,
CC PubMed:11842112, PubMed:11842113, PubMed:14704354). The BCDX2 complex
CC consits of RAD51B, RAD51C, RAD51D and XRCC2; the CX3 complex consists
CC of RAD51C and XRCC3 (PubMed:11751635, PubMed:11842113,
CC PubMed:14704354). The BCDX2 subcomplex RAD51B:RAD51C interacts with
CC RAD51 (PubMed:12427746, PubMed:16395335). Interacts with SWSAP1;
CC involved in homologous recombination repair (PubMed:21965664).
CC Interacts directly with PALB2 which may serve as a scaffold for a HR
CC complex containing PALB2, BRCA2, RAD51C, RAD51 and XRCC3
CC (PubMed:24141787). Interacts with HELQ (PubMed:24005041).
CC {ECO:0000269|PubMed:11751635, ECO:0000269|PubMed:11751636,
CC ECO:0000269|PubMed:11842112, ECO:0000269|PubMed:11842113,
CC ECO:0000269|PubMed:12427746, ECO:0000269|PubMed:14704354,
CC ECO:0000269|PubMed:16395335, ECO:0000269|PubMed:21965664,
CC ECO:0000269|PubMed:24005041, ECO:0000269|PubMed:24141787}.
CC -!- INTERACTION:
CC O43502; Q8TDG4: HELQ; NbExp=6; IntAct=EBI-2267048, EBI-2802156;
CC O43502; Q86YC2: PALB2; NbExp=10; IntAct=EBI-2267048, EBI-1222653;
CC O43502; Q06609: RAD51; NbExp=6; IntAct=EBI-2267048, EBI-297202;
CC O43502; O15315: RAD51B; NbExp=12; IntAct=EBI-2267048, EBI-2824089;
CC O43502; O75771: RAD51D; NbExp=6; IntAct=EBI-2267048, EBI-1055693;
CC O43502; Q6NVH7: SWSAP1; NbExp=2; IntAct=EBI-2267048, EBI-5281637;
CC O43502; O43543: XRCC2; NbExp=3; IntAct=EBI-2267048, EBI-3918457;
CC O43502; O43542: XRCC3; NbExp=11; IntAct=EBI-2267048, EBI-2849976;
CC O43502-2; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-14233893, EBI-742688;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12966089,
CC ECO:0000269|PubMed:16215984}. Cytoplasm {ECO:0000269|PubMed:16215984}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:16215984}.
CC Mitochondrion {ECO:0000269|PubMed:20413593}. Note=DNA damage induces an
CC increase in nuclear levels. Accumulates in DNA damage induced nuclear
CC foci or RAD51C foci which is formed during the S or G2 phase of cell
CC cycle. Accumulation at DNA lesions requires the presence of NBN/NBS1,
CC ATM and RPA.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43502-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43502-2; Sequence=VSP_043656, VSP_043657;
CC -!- TISSUE SPECIFICITY: Expressed in a variety of tissues, with highest
CC expression in testis, heart muscle, spleen and prostate.
CC -!- INDUCTION: Stress-induced increase in the mitochondrial levels is seen.
CC {ECO:0000269|PubMed:20413593}.
CC -!- DISEASE: Fanconi anemia complementation group O (FANCO) [MIM:613390]: A
CC 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:20400963, ECO:0000269|PubMed:24141787}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Breast-ovarian cancer, familial, 3 (BROVCA3) [MIM:613399]: A
CC condition associated with familial predisposition to cancer of the
CC breast and ovaries. Characteristic features in affected families are an
CC early age of onset of breast cancer (often before age 50), increased
CC chance of bilateral cancers (cancer that develop in both breasts, or
CC both ovaries, independently), frequent occurrence of breast cancer
CC among men, increased incidence of tumors of other specific organs, such
CC as the prostate. {ECO:0000269|PubMed:20400964,
CC ECO:0000269|PubMed:21990120, ECO:0000269|PubMed:24141787}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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/rad51c/";
CC -!- WEB RESOURCE: Name=RAD51 homolog C (S.cerevisiae) (RAD51C); Note=Leiden
CC Open Variation Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/RAD51C";
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DR EMBL; AF029669; AAC39604.1; -; mRNA.
DR EMBL; AF029670; AAC39605.1; -; mRNA.
DR EMBL; AY623112; AAT38108.1; -; Genomic_DNA.
DR EMBL; AC011195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94432.1; -; Genomic_DNA.
DR EMBL; BC107753; AAI07754.1; -; mRNA.
DR CCDS; CCDS11611.1; -. [O43502-1]
DR CCDS; CCDS45745.1; -. [O43502-2]
DR RefSeq; NP_002867.1; NM_002876.3. [O43502-2]
DR RefSeq; NP_478123.1; NM_058216.2. [O43502-1]
DR AlphaFoldDB; O43502; -.
DR SMR; O43502; -.
DR BioGRID; 111826; 53.
DR CORUM; O43502; -.
DR DIP; DIP-41247N; -.
DR IntAct; O43502; 20.
DR MINT; O43502; -.
DR STRING; 9606.ENSP00000336701; -.
DR GlyGen; O43502; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43502; -.
DR PhosphoSitePlus; O43502; -.
DR BioMuta; RAD51C; -.
DR CPTAC; CPTAC-3250; -.
DR CPTAC; CPTAC-3287; -.
DR EPD; O43502; -.
DR jPOST; O43502; -.
DR MassIVE; O43502; -.
DR MaxQB; O43502; -.
DR PaxDb; O43502; -.
DR PeptideAtlas; O43502; -.
DR PRIDE; O43502; -.
DR ProteomicsDB; 48995; -. [O43502-1]
DR ProteomicsDB; 48996; -. [O43502-2]
DR Antibodypedia; 18441; 390 antibodies from 35 providers.
DR CPTC; O43502; 2 antibodies.
DR DNASU; 5889; -.
DR Ensembl; ENST00000337432.9; ENSP00000336701.4; ENSG00000108384.15. [O43502-1]
DR Ensembl; ENST00000421782.3; ENSP00000391450.2; ENSG00000108384.15. [O43502-2]
DR GeneID; 5889; -.
DR KEGG; hsa:5889; -.
DR MANE-Select; ENST00000337432.9; ENSP00000336701.4; NM_058216.3; NP_478123.1.
DR UCSC; uc002iwt.3; human. [O43502-1]
DR CTD; 5889; -.
DR DisGeNET; 5889; -.
DR GeneCards; RAD51C; -.
DR GeneReviews; RAD51C; -.
DR HGNC; HGNC:9820; RAD51C.
DR HPA; ENSG00000108384; Low tissue specificity.
DR MalaCards; RAD51C; -.
DR MIM; 602774; gene.
DR MIM; 613390; phenotype.
DR MIM; 613399; phenotype.
DR neXtProt; NX_O43502; -.
DR OpenTargets; ENSG00000108384; -.
DR Orphanet; 84; Fanconi anemia.
DR Orphanet; 145; Hereditary breast and ovarian cancer syndrome.
DR PharmGKB; PA34177; -.
DR VEuPathDB; HostDB:ENSG00000108384; -.
DR eggNOG; KOG1434; Eukaryota.
DR GeneTree; ENSGT00940000156805; -.
DR InParanoid; O43502; -.
DR OMA; RLILYWN; -.
DR OrthoDB; 1345899at2759; -.
DR PhylomeDB; O43502; -.
DR TreeFam; TF101220; -.
DR PathwayCommons; O43502; -.
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-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-9709603; Impaired BRCA2 binding to PALB2.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; O43502; -.
DR SIGNOR; O43502; -.
DR BioGRID-ORCS; 5889; 537 hits in 1089 CRISPR screens.
DR ChiTaRS; RAD51C; human.
DR GeneWiki; RAD51C; -.
DR GenomeRNAi; 5889; -.
DR Pharos; O43502; Tbio.
DR PRO; PR:O43502; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O43502; protein.
DR Bgee; ENSG00000108384; Expressed in right testis and 198 other tissues.
DR ExpressionAtlas; O43502; baseline and differential.
DR Genevisible; O43502; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0033063; C:Rad51B-Rad51C-Rad51D-XRCC2 complex; IDA:UniProtKB.
DR GO; GO:0033065; C:Rad51C-XRCC3 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:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0006310; P:DNA recombination; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0007066; P:female meiosis sister chromatid cohesion; IEA:Ensembl.
DR GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
DR GO; GO:0000707; P:meiotic DNA recombinase assembly; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0007062; P:sister chromatid cohesion; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0000722; P:telomere maintenance via recombination; IEA:Ensembl.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 1.
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; IPR020588; RecA_ATP-bd.
DR Pfam; PF08423; Rad51; 1.
DR PIRSF; PIRSF005856; Rad51; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50162; RECA_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Disease variant; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Fanconi anemia; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..376
FT /note="DNA repair protein RAD51 homolog 3"
FT /id="PRO_0000122941"
FT REGION 1..126
FT /note="Required for Holliday junction resolution activity"
FT REGION 79..136
FT /note="Interaction with RAD51B, RAD51D and XRCC3"
FT /evidence="ECO:0000269|PubMed:14704354"
FT MOTIF 366..370
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT BINDING 125..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 135
FT /note="C -> W (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9469824"
FT /id="VSP_043656"
FT VAR_SEQ 136..376
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9469824"
FT /id="VSP_043657"
FT VARIANT 3
FT /note="G -> R (in dbSNP:rs376403182)"
FT /evidence="ECO:0000269|PubMed:20400964"
FT /id="VAR_063837"
FT VARIANT 52
FT /note="I -> L (in dbSNP:rs730881927)"
FT /evidence="ECO:0000269|PubMed:21990120"
FT /id="VAR_068014"
FT VARIANT 103
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:21990120"
FT /id="VAR_068015"
FT VARIANT 114
FT /note="G -> V (in dbSNP:rs1555593767)"
FT /evidence="ECO:0000269|PubMed:21990120"
FT /id="VAR_068016"
FT VARIANT 125
FT /note="G -> V (in BROVCA3; dbSNP:rs267606998)"
FT /evidence="ECO:0000269|PubMed:20400964"
FT /id="VAR_063838"
FT VARIANT 126
FT /note="A -> T (in dbSNP:rs61758784)"
FT /evidence="ECO:0000269|PubMed:20400964,
FT ECO:0000269|PubMed:21990120"
FT /id="VAR_063839"
FT VARIANT 138
FT /note="L -> F (in BROVCA3; reduces interaction with BRCA2
FT and to a lesser extent with PALB2 and RAD51;
FT dbSNP:rs267606999)"
FT /evidence="ECO:0000269|PubMed:20400964,
FT ECO:0000269|PubMed:24141787"
FT /id="VAR_063840"
FT VARIANT 144
FT /note="I -> T (in dbSNP:rs28363307)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_020518"
FT VARIANT 159
FT /note="D -> N (reduces interaction with BRCA2 and to a
FT lesser extent with PALB2 and RAD51)"
FT /evidence="ECO:0000269|PubMed:20400964,
FT ECO:0000269|PubMed:24141787"
FT /id="VAR_063841"
FT VARIANT 162
FT /note="G -> E (in BROVCA3; dbSNP:rs35151472)"
FT /evidence="ECO:0000269|PubMed:21990120"
FT /id="VAR_068017"
FT VARIANT 169
FT /note="V -> A (in dbSNP:rs587780256)"
FT /evidence="ECO:0000269|PubMed:20400964,
FT ECO:0000269|PubMed:21990120"
FT /id="VAR_063842"
FT VARIANT 175
FT /note="A -> T (in dbSNP:rs587780838)"
FT /evidence="ECO:0000269|PubMed:21990120"
FT /id="VAR_068018"
FT VARIANT 178
FT /note="Q -> P (in BROVCA3)"
FT /evidence="ECO:0000269|PubMed:21990120"
FT /id="VAR_068019"
FT VARIANT 249
FT /note="R -> C (in dbSNP:rs28363311)"
FT /evidence="ECO:0000269|PubMed:21990120, ECO:0000269|Ref.2"
FT /id="VAR_020519"
FT VARIANT 258
FT /note="R -> H (in FANCO; possibly hypomorphic allele;
FT reduces interaction with BRCA2 and to a lesser extent with
FT PALB2 and RAD51; dbSNP:rs267606997)"
FT /evidence="ECO:0000269|PubMed:20400963,
FT ECO:0000269|PubMed:24141787"
FT /id="VAR_064032"
FT VARIANT 262
FT /note="L -> V (in dbSNP:rs149331537)"
FT /evidence="ECO:0000269|PubMed:21990120"
FT /id="VAR_068020"
FT VARIANT 264
FT /note="G -> S (in dbSNP:rs147241704)"
FT /evidence="ECO:0000269|PubMed:20400964,
FT ECO:0000269|PubMed:21990120"
FT /id="VAR_063843"
FT VARIANT 264
FT /note="G -> V (in dbSNP:rs1283065191)"
FT /evidence="ECO:0000269|PubMed:20400964"
FT /id="VAR_063844"
FT VARIANT 287
FT /note="T -> A (in BROVCA3; dbSNP:rs28363317)"
FT /evidence="ECO:0000269|PubMed:20400964,
FT ECO:0000269|PubMed:21990120, ECO:0000269|Ref.2"
FT /id="VAR_020520"
FT VARIANT 366
FT /note="R -> Q (in dbSNP:rs577852020)"
FT /evidence="ECO:0000269|PubMed:20400964"
FT /id="VAR_063845"
FT MUTAGEN 131
FT /note="K->A: Significant loss of function; abolishes
FT Holliday junction resolution activity."
FT /evidence="ECO:0000269|PubMed:12966089,
FT ECO:0000269|PubMed:14716019"
FT MUTAGEN 131
FT /note="K->R: Partial loss of function."
FT /evidence="ECO:0000269|PubMed:12966089,
FT ECO:0000269|PubMed:14716019"
SQ SEQUENCE 376 AA; 42190 MW; 3AAADD3C1C0851E0 CRC64;
MRGKTFRFEM QRDLVSFPLS PAVRVKLVSA GFQTAEELLE VKPSELSKEV GISKAEALET
LQIIRRECLT NKPRYAGTSE SHKKCTALEL LEQEHTQGFI ITFCSALDDI LGGGVPLMKT
TEICGAPGVG KTQLCMQLAV DVQIPECFGG VAGEAVFIDT EGSFMVDRVV DLATACIQHL
QLIAEKHKGE EHRKALEDFT LDNILSHIYY FRCRDYTELL AQVYLLPDFL SEHSKVRLVI
VDGIAFPFRH DLDDLSLRTR LLNGLAQQMI SLANNHRLAV ILTNQMTTKI DRNQALLVPA
LGESWGHAAT IRLIFHWDRK QRLATLYKSP SQKECTVLFQ IKPQGFRDTV VTSACSLQTE
GSLSTRKRSR DPEEEL
