RA51D_HUMAN
ID RA51D_HUMAN Reviewed; 328 AA.
AC O75771; B4DJU7; E1P637; O43537; O60355; O75196; O75847; O75848; O76073;
AC O76085; O94908; Q9UFU5;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=DNA repair protein RAD51 homolog 4;
DE AltName: Full=R51H3;
DE AltName: Full=RAD51 homolog D;
DE AltName: Full=RAD51-like protein 3;
DE AltName: Full=TRAD;
GN Name=RAD51D; Synonyms=RAD51L3;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9570954; DOI=10.1006/geno.1998.5226;
RA Pittman D.L., Weinberg L.R., Schimenti J.C.;
RT "Identification, characterization, and genetic mapping of Rad51d, a new
RT mouse and human RAD51/RecA-related gene.";
RL Genomics 49:103-111(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING (ISOFORMS 2; 3; 4; 5;
RP 6 AND 7).
RC TISSUE=Brain;
RX PubMed=10092526; DOI=10.1006/bbrc.1999.0413;
RA Kawabata M., Saeki K.;
RT "Multiple alternative transcripts of the human homologue of the mouse
RT TRAD/R51H3/RAD51D gene, a member of the recA/RAD51 gene family.";
RL Biochem. Biophys. Res. Commun. 257:156-162(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-24; GLN-165; THR-225;
RP GLN-232 AND GLY-233.
RG NIEHS SNPs program;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
RC TISSUE=Thalamus;
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 [6]
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 [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 156-328.
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP FUNCTION, AND INTERACTION WITH XRCC2.
RX PubMed=10871607; DOI=10.1074/jbc.m002075200;
RA Braybrooke J.P., Spink K.G., Thacker J., Hickson I.D.;
RT "The RAD51 family member, RAD51L3, is a DNA-stimulated ATPase that forms a
RT complex with XRCC2.";
RL J. Biol. Chem. 275:29100-29106(2000).
RN [11]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D AND 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 SUBUNIT.
RX PubMed=11834724; DOI=10.1074/jbc.m105719200;
RA Kurumizaka H., Ikawa S., Nakada M., Enomoto R., Kagawa W., Kinebuchi T.,
RA Yamazoe M., Yokoyama S., Shibata T.;
RT "Homologous pairing and ring and filament structure formation activities of
RT the human Xrcc2*Rad51D complex.";
RL J. Biol. Chem. 277:14315-14320(2002).
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 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 FUNCTION OF THE BCDX2 COMPLEX, AND INTERACTION WITH BLM AND XRCC2.
RX PubMed=12975363; DOI=10.1074/jbc.m308838200;
RA Braybrooke J.P., Li J.L., Wu L., Caple F., Benson F.E., Hickson I.D.;
RT "Functional interaction between the Bloom's syndrome helicase and the RAD51
RT paralog, RAD51L3 (RAD51D).";
RL J. Biol. Chem. 278:48357-48366(2003).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15109494; DOI=10.1016/s0092-8674(04)00337-x;
RA Tarsounas M., Munoz P., Claas A., Smiraldo P.G., Pittman D.L., Blasco M.A.,
RA West S.C.;
RT "Telomere maintenance requires the RAD51D recombination/repair protein.";
RL Cell 117:337-347(2004).
RN [18]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [19]
RP INTERACTION WITH ZSWIM7 AND XRCC2.
RX PubMed=16710300; DOI=10.1038/sj.emboj.7601141;
RA Martin V., Chahwan C., Gao H., Blais V., Wohlschlegel J., Yates J.R. III,
RA McGowan C.H., Russell P.;
RT "Sws1 is a conserved regulator of homologous recombination in eukaryotic
RT cells.";
RL EMBO J. 25:2564-2574(2006).
RN [20]
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 [21]
RP INTERACTION WITH SWSAP1 AND ZSWIM7.
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 INVOLVEMENT IN BROVCA4.
RX PubMed=21822267; DOI=10.1038/ng.893;
RA Loveday C., Turnbull C., Ramsay E., Hughes D., Ruark E., Frankum J.R.,
RA Bowden G., Kalmyrzaev B., Warren-Perry M., Snape K., Adlard J.W.,
RA Barwell J., Berg J., Brady A.F., Brewer C., Brice G., Chapman C., Cook J.,
RA Davidson R., Donaldson A., Douglas F., Greenhalgh L., Henderson A.,
RA Izatt L., Kumar A., Lalloo F., Miedzybrodzka Z., Morrison P.J.,
RA Paterson J., Porteous M., Rogers M.T., Shanley S., Walker L., Eccles D.,
RA Evans D.G., Renwick A., Seal S., Lord C.J., Ashworth A., Reis-Filho J.S.,
RA Antoniou A.C., Rahman N.;
RT "Germline mutations in RAD51D confer susceptibility to ovarian cancer.";
RL Nat. Genet. 43:879-882(2011).
RN [23]
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 [24]
RP STRUCTURE BY NMR OF 1-83, AND DNA-BINDING.
RX PubMed=21111057; DOI=10.1016/j.biocel.2010.11.014;
RA Kim Y.M., Choi B.S.;
RT "Structural and functional characterization of the N-terminal domain of
RT human Rad51D.";
RL Int. J. Biochem. Cell Biol. 43:416-422(2011).
RN [25]
RP VARIANT SER-9.
RX PubMed=27932480; DOI=10.1681/asn.2016040387;
RG NephroS;
RG UK study of Nephrotic Syndrome;
RA Bierzynska A., Soderquest K., Dean P., Colby E., Rollason R., Jones C.,
RA Inward C.D., McCarthy H.J., Simpson M.A., Lord G.M., Williams M.,
RA Welsh G.I., Koziell A.B., Saleem M.A.;
RT "MAGI2 mutations cause congenital nephrotic syndrome.";
RL J. Am. Soc. Nephrol. 28:1614-1621(2017).
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. Bind to single-stranded DNA (ssDNA) and has
CC DNA-dependent ATPase activity. Part of the RAD51 paralog protein
CC complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon
CC DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of
CC RAD51 recruitment. BCDX2 binds predominantly to the intersection of the
CC four duplex arms of the Holliday junction and to junction of
CC replication forks. The BCDX2 complex was originally reported to bind
CC single-stranded DNA, single-stranded gaps in duplex DNA and
CC specifically to nicks in duplex DNA. Involved in telomere maintenance.
CC The BCDX2 subcomplex XRCC2:RAD51D can stimulate Holliday junction
CC resolution by BLM. {ECO:0000269|PubMed:10871607,
CC ECO:0000269|PubMed:11751635, ECO:0000269|PubMed:11834724,
CC ECO:0000269|PubMed:11842113, ECO:0000269|PubMed:12975363,
CC ECO:0000269|PubMed:15109494, 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. In the absence of DNA, the BCDX2
CC subcomplex XRCC2:RAD51D formed a multimeric ring structure; in the
CC presence of single-stranded DNA it formed a filamentous structure with
CC the ssDNA. Interacts with SWSAP1 and ZSWIM7; involved in homologous
CC recombination repair. Interacts with BLM; required for stimulation of
CC BLM activity by the BCDX2 subcomplex XRCC2:RAD51D.
CC {ECO:0000269|PubMed:10871607, ECO:0000269|PubMed:11744692,
CC ECO:0000269|PubMed:11751635, ECO:0000269|PubMed:11834724,
CC ECO:0000269|PubMed:11842112, ECO:0000269|PubMed:11842113,
CC ECO:0000269|PubMed:12975363, ECO:0000269|PubMed:16710300,
CC ECO:0000269|PubMed:21965664}.
CC -!- INTERACTION:
CC O75771; Q9Y2J4: AMOTL2; NbExp=8; IntAct=EBI-1055693, EBI-746752;
CC O75771; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-1055693, EBI-10187270;
CC O75771; P54132: BLM; NbExp=4; IntAct=EBI-1055693, EBI-621372;
CC O75771; Q6P1W5: C1orf94; NbExp=6; IntAct=EBI-1055693, EBI-946029;
CC O75771; Q8N5R6: CCDC33; NbExp=3; IntAct=EBI-1055693, EBI-740841;
CC O75771; Q9UK58: CCNL1; NbExp=3; IntAct=EBI-1055693, EBI-2836773;
CC O75771; Q6P2R3: CEP57L1; NbExp=3; IntAct=EBI-1055693, EBI-12696312;
CC O75771; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-1055693, EBI-10181988;
CC O75771; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-1055693, EBI-2349927;
CC O75771; P57678: GEMIN4; NbExp=3; IntAct=EBI-1055693, EBI-356700;
CC O75771; O75031: HSF2BP; NbExp=3; IntAct=EBI-1055693, EBI-7116203;
CC O75771; Q8IYA8: IHO1; NbExp=6; IntAct=EBI-1055693, EBI-8638439;
CC O75771; Q13422: IKZF1; NbExp=5; IntAct=EBI-1055693, EBI-745305;
CC O75771; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-1055693, EBI-11522367;
CC O75771; Q9UKT9: IKZF3; NbExp=11; IntAct=EBI-1055693, EBI-747204;
CC O75771; Q9H079: KATNBL1; NbExp=3; IntAct=EBI-1055693, EBI-715394;
CC O75771; F5H3M2: KIFC3; NbExp=3; IntAct=EBI-1055693, EBI-11953930;
CC O75771; Q9BVG8: KIFC3; NbExp=4; IntAct=EBI-1055693, EBI-2125614;
CC O75771; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-1055693, EBI-14069005;
CC O75771; P19012: KRT15; NbExp=7; IntAct=EBI-1055693, EBI-739566;
CC O75771; P48059-3: LIMS1; NbExp=3; IntAct=EBI-1055693, EBI-12864460;
CC O75771; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-1055693, EBI-739832;
CC O75771; Q9BRK4: LZTS2; NbExp=9; IntAct=EBI-1055693, EBI-741037;
CC O75771; Q9UPT6: MAPK8IP3; NbExp=3; IntAct=EBI-1055693, EBI-717887;
CC O75771; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1055693, EBI-16439278;
CC O75771; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-1055693, EBI-10271199;
CC O75771; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-1055693, EBI-79165;
CC O75771; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-1055693, EBI-302345;
CC O75771; Q8WUT1: POLDIP3; NbExp=3; IntAct=EBI-1055693, EBI-10276663;
CC O75771; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-1055693, EBI-3957793;
CC O75771; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-1055693, EBI-11320284;
CC O75771; O15315: RAD51B; NbExp=5; IntAct=EBI-1055693, EBI-2824089;
CC O75771; O43502: RAD51C; NbExp=6; IntAct=EBI-1055693, EBI-2267048;
CC O75771; Q5RL73: RBM48; NbExp=3; IntAct=EBI-1055693, EBI-473821;
CC O75771; Q04864-2: REL; NbExp=3; IntAct=EBI-1055693, EBI-10829018;
CC O75771; O60504: SORBS3; NbExp=3; IntAct=EBI-1055693, EBI-741237;
CC O75771; Q9H0A9-2: SPATC1L; NbExp=3; IntAct=EBI-1055693, EBI-11995806;
CC O75771; O75558: STX11; NbExp=3; IntAct=EBI-1055693, EBI-714135;
CC O75771; Q6NVH7: SWSAP1; NbExp=2; IntAct=EBI-1055693, EBI-5281637;
CC O75771; P15884-3: TCF4; NbExp=3; IntAct=EBI-1055693, EBI-13636688;
CC O75771; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-1055693, EBI-11139477;
CC O75771; Q08117-2: TLE5; NbExp=3; IntAct=EBI-1055693, EBI-11741437;
CC O75771; Q14142: TRIM14; NbExp=3; IntAct=EBI-1055693, EBI-2820256;
CC O75771; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-1055693, EBI-9090990;
CC O75771; Q9Y2B5: VPS9D1; NbExp=3; IntAct=EBI-1055693, EBI-9031083;
CC O75771; O43543: XRCC2; NbExp=38; IntAct=EBI-1055693, EBI-3918457;
CC O75771; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-1055693, EBI-12287587;
CC O75771; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-1055693, EBI-14104088;
CC O75771; Q6P1L6: ZNF343; NbExp=3; IntAct=EBI-1055693, EBI-10252492;
CC O75771; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-1055693, EBI-10251462;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome. Chromosome, telomere.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=TRAD;
CC IsoId=O75771-1; Sequence=Displayed;
CC Name=2; Synonyms=TRAD-D1, D2;
CC IsoId=O75771-2; Sequence=VSP_005558, VSP_005559;
CC Name=3; Synonyms=TRAD-D3;
CC IsoId=O75771-3; Sequence=VSP_005560;
CC Name=4; Synonyms=TRAD-D4;
CC IsoId=O75771-4; Sequence=VSP_005561;
CC Name=5; Synonyms=TRAD-D5;
CC IsoId=O75771-5; Sequence=VSP_005562;
CC Name=6; Synonyms=TRAD-D6, D7;
CC IsoId=O75771-6; Sequence=VSP_005563, VSP_005564;
CC Name=7; Synonyms=TRAD-D8;
CC IsoId=O75771-7; Sequence=VSP_005565, VSP_005566;
CC Name=8;
CC IsoId=O75771-8; Sequence=VSP_043658;
CC -!- TISSUE SPECIFICITY: Expressed in colon, prostate, spleen, testis,
CC ovary, thymus and small intestine. Weakly expressed in leukocytes.
CC -!- DISEASE: Breast-ovarian cancer, familial, 4 (BROVCA4) [MIM:614291]: 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:21822267}. Note=Disease
CC susceptibility is associated with variants affecting the gene
CC represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
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/rad51l3/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RAD51L3ID347ch17q12.html";
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DR EMBL; Y15572; CAA75681.1; -; mRNA.
DR EMBL; AF034956; AAC39719.1; -; mRNA.
DR EMBL; AB013341; BAA25914.1; -; mRNA.
DR EMBL; AB016223; BAA31747.1; -; mRNA.
DR EMBL; AB016224; BAA31748.1; -; mRNA.
DR EMBL; AB016225; BAA31749.1; -; mRNA.
DR EMBL; AB018360; BAA33779.1; -; mRNA.
DR EMBL; AB018361; BAA33780.1; -; mRNA.
DR EMBL; AB018362; BAA33781.1; -; mRNA.
DR EMBL; AB018363; BAA33782.1; -; mRNA.
DR EMBL; AB020412; BAA34690.1; -; mRNA.
DR EMBL; AY623116; AAT38112.1; -; Genomic_DNA.
DR EMBL; AK296241; BAG58959.1; -; mRNA.
DR EMBL; AC022916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471147; EAW80181.1; -; Genomic_DNA.
DR EMBL; CH471147; EAW80184.1; -; Genomic_DNA.
DR EMBL; CH471147; EAW80196.1; -; Genomic_DNA.
DR EMBL; BC014422; AAH14422.1; -; mRNA.
DR EMBL; AL117459; CAB55937.1; -; mRNA.
DR CCDS; CCDS11287.1; -. [O75771-1]
DR CCDS; CCDS11288.1; -. [O75771-3]
DR CCDS; CCDS45646.1; -. [O75771-8]
DR PIR; T17247; T17247.
DR RefSeq; NP_001136043.1; NM_001142571.1. [O75771-8]
DR RefSeq; NP_002869.3; NM_002878.3. [O75771-1]
DR RefSeq; NP_598332.1; NM_133629.2. [O75771-3]
DR PDB; 2KZ3; NMR; -; A=1-83.
DR PDBsum; 2KZ3; -.
DR AlphaFoldDB; O75771; -.
DR BMRB; O75771; -.
DR SMR; O75771; -.
DR BioGRID; 111829; 88.
DR CORUM; O75771; -.
DR DIP; DIP-24265N; -.
DR IntAct; O75771; 67.
DR MINT; O75771; -.
DR iPTMnet; O75771; -.
DR PhosphoSitePlus; O75771; -.
DR BioMuta; RAD51D; -.
DR EPD; O75771; -.
DR jPOST; O75771; -.
DR MassIVE; O75771; -.
DR MaxQB; O75771; -.
DR PaxDb; O75771; -.
DR PeptideAtlas; O75771; -.
DR PRIDE; O75771; -.
DR ProteomicsDB; 50183; -. [O75771-1]
DR ProteomicsDB; 50184; -. [O75771-2]
DR ProteomicsDB; 50185; -. [O75771-3]
DR ProteomicsDB; 50186; -. [O75771-4]
DR ProteomicsDB; 50187; -. [O75771-5]
DR ProteomicsDB; 50188; -. [O75771-6]
DR ProteomicsDB; 50189; -. [O75771-7]
DR ProteomicsDB; 50190; -. [O75771-8]
DR Antibodypedia; 15549; 376 antibodies from 33 providers.
DR DNASU; 5892; -.
DR Ensembl; ENST00000335858.11; ENSP00000338408.6; ENSG00000185379.21. [O75771-3]
DR Ensembl; ENST00000345365.11; ENSP00000338790.6; ENSG00000185379.21. [O75771-1]
DR Ensembl; ENST00000394589.8; ENSP00000378090.4; ENSG00000185379.21. [O75771-1]
DR Ensembl; ENST00000586044.5; ENSP00000465584.1; ENSG00000185379.21. [O75771-2]
DR Ensembl; ENST00000587977.5; ENSP00000466587.1; ENSG00000185379.21. [O75771-6]
DR Ensembl; ENST00000588594.5; ENSP00000465366.1; ENSG00000185379.21. [O75771-2]
DR Ensembl; ENST00000590016.5; ENSP00000466399.1; ENSG00000185379.21. [O75771-8]
DR GeneID; 5892; -.
DR KEGG; hsa:5892; -.
DR MANE-Select; ENST00000345365.11; ENSP00000338790.6; NM_002878.4; NP_002869.3.
DR UCSC; uc002hir.4; human. [O75771-1]
DR CTD; 5892; -.
DR DisGeNET; 5892; -.
DR GeneCards; RAD51D; -.
DR HGNC; HGNC:9823; RAD51D.
DR HPA; ENSG00000185379; Low tissue specificity.
DR MalaCards; RAD51D; -.
DR MIM; 602954; gene.
DR MIM; 614291; phenotype.
DR neXtProt; NX_O75771; -.
DR OpenTargets; ENSG00000185379; -.
DR Orphanet; 1331; Familial prostate cancer.
DR Orphanet; 145; Hereditary breast and ovarian cancer syndrome.
DR PharmGKB; PA34179; -.
DR VEuPathDB; HostDB:ENSG00000185379; -.
DR eggNOG; KOG1433; Eukaryota.
DR eggNOG; KOG4275; Eukaryota.
DR GeneTree; ENSGT00940000159095; -.
DR HOGENOM; CLU_058452_0_0_1; -.
DR InParanoid; O75771; -.
DR OMA; QRIHTFR; -.
DR OrthoDB; 1214879at2759; -.
DR PhylomeDB; O75771; -.
DR PathwayCommons; O75771; -.
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-6796648; TP53 Regulates Transcription of DNA Repair Genes.
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 SignaLink; O75771; -.
DR BioGRID-ORCS; 5892; 464 hits in 1094 CRISPR screens.
DR GeneWiki; RAD51L3; -.
DR GenomeRNAi; 5892; -.
DR Pharos; O75771; Tbio.
DR PRO; PR:O75771; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O75771; protein.
DR Bgee; ENSG00000185379; Expressed in sperm and 112 other tissues.
DR ExpressionAtlas; O75771; baseline and differential.
DR Genevisible; O75771; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; IMP:FlyBase.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
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:0036297; P:interstrand cross-link repair; IEA:Ensembl.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0042148; P:strand invasion; IDA:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; IMP:UniProtKB.
DR GO; GO:0000722; P:telomere maintenance via recombination; IMP:BHF-UCL.
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; IPR020588; RecA_ATP-bd.
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 3D-structure; Alternative splicing; ATP-binding; Chromosome; Cytoplasm;
KW Cytoskeleton; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Nucleotide-binding; Nucleus; Reference proteome; Telomere.
FT CHAIN 1..328
FT /note="DNA repair protein RAD51 homolog 4"
FT /id="PRO_0000122942"
FT REGION 1..83
FT /note="preferentially binds ssDNA"
FT BINDING 107..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 49..88
FT /note="ALVALRRVLLAQFSAFPVNGADLYEELKTSTAILSTGIGS -> TWRAHSSG
FT NLGGLQLPQVPAGRSWSGVRNALKKAGLGHGGTDGLSLNAFDERGTAVSTSR (in
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043658"
FT VAR_SEQ 49
FT /note="A -> S (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005558"
FT VAR_SEQ 50..328
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005559"
FT VAR_SEQ 50..161
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_005560"
FT VAR_SEQ 88..118
FT /note="SLDKLLDAGLYTGEVTEIVGGPGSGKTQVCL -> RHGGRTQVGTWEDCSCL
FT RSPQGDRGVGSGML (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_005563"
FT VAR_SEQ 88..101
FT /note="SLDKLLDAGLYTGE -> RQKLSGGSRWCMHL (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_005562"
FT VAR_SEQ 116..160
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_005561"
FT VAR_SEQ 119..328
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_005564"
FT VAR_SEQ 193..212
FT /note="VTGSSGTVKVVVVDSVTAVV -> DGIPEHLNHIPHCLHVHLPC (in
FT isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_005565"
FT VAR_SEQ 213..328
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_005566"
FT VARIANT 9
FT /note="C -> S (in dbSNP:rs140825795)"
FT /evidence="ECO:0000269|PubMed:27932480"
FT /id="VAR_079271"
FT VARIANT 24
FT /note="R -> S (in dbSNP:rs28363257)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_020560"
FT VARIANT 165
FT /note="R -> Q (in dbSNP:rs4796033)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_020561"
FT VARIANT 225
FT /note="A -> T (in dbSNP:rs28363282)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_020562"
FT VARIANT 232
FT /note="R -> Q (in dbSNP:rs28363283)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_020563"
FT VARIANT 233
FT /note="E -> G (in dbSNP:rs28363284)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_020564"
FT CONFLICT 231
FT /note="A -> V (in Ref. 9; CAB55937)"
FT /evidence="ECO:0000305"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:2KZ3"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:2KZ3"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:2KZ3"
FT HELIX 47..61
FT /evidence="ECO:0007829|PDB:2KZ3"
SQ SEQUENCE 328 AA; 35049 MW; 6038DA9356DF354A CRC64;
MGVLRVGLCP GLTEEMIQLL RSHRIKTVVD LVSADLEEVA QKCGLSYKAL VALRRVLLAQ
FSAFPVNGAD LYEELKTSTA ILSTGIGSLD KLLDAGLYTG EVTEIVGGPG SGKTQVCLCM
AANVAHGLQQ NVLYVDSNGG LTASRLLQLL QAKTQDEEEQ AEALRRIQVV HAFDIFQMLD
VLQELRGTVA QQVTGSSGTV KVVVVDSVTA VVSPLLGGQQ REGLALMMQL ARELKTLARD
LGMAVVVTNH ITRDRDSGRL KPALGRSWSF VPSTRILLDT IEGAGASGGR RMACLAKSSR
QPTGFQEMVD IGTWGTSEQS ATLQGDQT
