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DNA repair protein RAD51 homolog 4 (R51H3) (RAD51 homolog D) (RAD51-like protein 3) (TRAD)

 RA51D_HUMAN             Reviewed;         328 AA.
O75771; B4DJU7; E1P637; O43537; O60355; O75196; O75847; O75848;
O76073; O76085; O94908; Q9UFU5;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
12-SEP-2018, entry version 179.
RecName: Full=DNA repair protein RAD51 homolog 4;
AltName: Full=R51H3;
AltName: Full=RAD51 homolog D;
AltName: Full=RAD51-like protein 3;
AltName: Full=TRAD;
Name=RAD51D; Synonyms=RAD51L3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9512535; DOI=10.1093/nar/26.7.1653;
Cartwright R., Dunn A.M., Simpson P.J., Tambini C.E., Thacker J.;
"Isolation of novel human and mouse genes of the recA/RAD51
recombination-repair gene family.";
Nucleic Acids Res. 26:1653-1659(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9570954; DOI=10.1006/geno.1998.5226;
Pittman D.L., Weinberg L.R., Schimenti J.C.;
"Identification, characterization, and genetic mapping of Rad51d, a
new mouse and human RAD51/RecA-related gene.";
Genomics 49:103-111(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING (ISOFORMS 2; 3;
4; 5; 6 AND 7).
TISSUE=Brain;
PubMed=10092526; DOI=10.1006/bbrc.1999.0413;
Kawabata M., Saeki K.;
"Multiple alternative transcripts of the human homologue of the mouse
TRAD/R51H3/RAD51D gene, a member of the recA/RAD51 gene family.";
Biochem. Biophys. Res. Commun. 257:156-162(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-24; GLN-165;
THR-225; GLN-232 AND GLY-233.
NIEHS SNPs program;
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 156-328.
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[10]
FUNCTION, AND INTERACTION WITH XRCC2.
PubMed=10871607; DOI=10.1074/jbc.M002075200;
Braybrooke J.P., Spink K.G., Thacker J., Hickson I.D.;
"The RAD51 family member, RAD51L3, is a DNA-stimulated ATPase that
forms a complex with XRCC2.";
J. Biol. Chem. 275:29100-29106(2000).
[11]
FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D AND
XRCC2.
PubMed=11751635; DOI=10.1101/gad.947001;
Masson J.Y., Tarsounas M.C., Stasiak A.Z., Stasiak A., Shah R.,
McIlwraith M.J., Benson F.E., West S.C.;
"Identification and purification of two distinct complexes containing
the five RAD51 paralogs.";
Genes Dev. 15:3296-3307(2001).
[12]
FUNCTION, AND SUBUNIT.
PubMed=11834724; DOI=10.1074/jbc.M105719200;
Kurumizaka H., Ikawa S., Nakada M., Enomoto R., Kagawa W.,
Kinebuchi T., Yamazoe M., Yokoyama S., Shibata T.;
"Homologous pairing and ring and filament structure formation
activities of the human Xrcc2*Rad51D complex.";
J. Biol. Chem. 277:14315-14320(2002).
[13]
FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D AND
XRCC2.
PubMed=11842113; DOI=10.1093/nar/30.4.1009;
Liu N., Schild D., Thelen M.P., Thompson L.H.;
"Involvement of Rad51C in two distinct protein complexes of Rad51
paralogs in human cells.";
Nucleic Acids Res. 30:1009-1015(2002).
[14]
SUBUNIT.
PubMed=11744692; DOI=10.1074/jbc.M108306200;
Miller K.A., Yoshikawa D.M., McConnell I.R., Clark R., Schild D.,
Albala J.S.;
"RAD51C interacts with RAD51B and is central to a larger protein
complex in vivo exclusive of RAD51.";
J. Biol. Chem. 277:8406-8411(2002).
[15]
IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D AND XRCC2.
PubMed=11842112; DOI=10.1093/nar/30.4.1001;
Wiese C., Collins D.W., Albala J.S., Thompson L.H., Kronenberg A.,
Schild D.;
"Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human
cells.";
Nucleic Acids Res. 30:1001-1008(2002).
[16]
FUNCTION OF THE BCDX2 COMPLEX, AND INTERACTION WITH BLM AND XRCC2.
PubMed=12975363; DOI=10.1074/jbc.M308838200;
Braybrooke J.P., Li J.L., Wu L., Caple F., Benson F.E., Hickson I.D.;
"Functional interaction between the Bloom's syndrome helicase and the
RAD51 paralog, RAD51L3 (RAD51D).";
J. Biol. Chem. 278:48357-48366(2003).
[17]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15109494; DOI=10.1016/S0092-8674(04)00337-X;
Tarsounas M., Munoz P., Claas A., Smiraldo P.G., Pittman D.L.,
Blasco M.A., West S.C.;
"Telomere maintenance requires the RAD51D recombination/repair
protein.";
Cell 117:337-347(2004).
[18]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[19]
INTERACTION WITH ZSWIM7 AND XRCC2.
PubMed=16710300; DOI=10.1038/sj.emboj.7601141;
Martin V., Chahwan C., Gao H., Blais V., Wohlschlegel J.,
Yates J.R. III, McGowan C.H., Russell P.;
"Sws1 is a conserved regulator of homologous recombination in
eukaryotic cells.";
EMBO J. 25:2564-2574(2006).
[20]
SUBCELLULAR LOCATION.
PubMed=21276791; DOI=10.1016/j.yexcr.2011.01.021;
Cappelli E., Townsend S., Griffin C., Thacker J.;
"Homologous recombination proteins are associated with centrosomes and
are required for mitotic stability.";
Exp. Cell Res. 317:1203-1213(2011).
[21]
INTERACTION WITH SWSAP1 AND ZSWIM7.
PubMed=21965664; DOI=10.1074/jbc.M111.271080;
Liu T., Wan L., Wu Y., Chen J., Huang J.;
"hSWS1.SWSAP1 is an evolutionarily conserved complex required for
efficient homologous recombination repair.";
J. Biol. Chem. 286:41758-41766(2011).
[22]
INVOLVEMENT IN BROVCA4.
PubMed=21822267; DOI=10.1038/ng.893;
Loveday C., Turnbull C., Ramsay E., Hughes D., Ruark E., Frankum J.R.,
Bowden G., Kalmyrzaev B., Warren-Perry M., Snape K., Adlard J.W.,
Barwell J., Berg J., Brady A.F., Brewer C., Brice G., Chapman C.,
Cook J., Davidson R., Donaldson A., Douglas F., Greenhalgh L.,
Henderson A., Izatt L., Kumar A., Lalloo F., Miedzybrodzka Z.,
Morrison P.J., Paterson J., Porteous M., Rogers M.T., Shanley S.,
Walker L., Eccles D., Evans D.G., Renwick A., Seal S., Lord C.J.,
Ashworth A., Reis-Filho J.S., Antoniou A.C., Rahman N.;
"Germline mutations in RAD51D confer susceptibility to ovarian
cancer.";
Nat. Genet. 43:879-882(2011).
[23]
FUNCTION OF THE BCDX2 COMPLEX.
PubMed=23149936; DOI=10.1128/MCB.00465-12;
Chun J., Buechelmaier E.S., Powell S.N.;
"Rad51 paralog complexes BCDX2 and CX3 act at different stages in the
BRCA1-BRCA2-dependent homologous recombination pathway.";
Mol. Cell. Biol. 33:387-395(2013).
[24]
STRUCTURE BY NMR OF 1-83, AND DNA-BINDING.
PubMed=21111057; DOI=10.1016/j.biocel.2010.11.014;
Kim Y.M., Choi B.S.;
"Structural and functional characterization of the N-terminal domain
of human Rad51D.";
Int. J. Biochem. Cell Biol. 43:416-422(2011).
[25]
VARIANT SER-9.
PubMed=27932480; DOI=10.1681/ASN.2016040387;
NephroS;
UK study of Nephrotic Syndrome;
Bierzynska A., Soderquest K., Dean P., Colby E., Rollason R.,
Jones C., Inward C.D., McCarthy H.J., Simpson M.A., Lord G.M.,
Williams M., Welsh G.I., Koziell A.B., Saleem M.A.;
"MAGI2 mutations cause congenital nephrotic syndrome.";
J. Am. Soc. Nephrol. 28:1614-1621(2017).
-!- FUNCTION: Involved in the homologous recombination repair (HRR)
pathway of double-stranded DNA breaks arising during DNA
replication or induced by DNA-damaging agents. Bind to single-
stranded DNA (ssDNA) and has DNA-dependent ATPase activity. Part
of the Rad21 paralog protein complex BCDX2 which acts in the
BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts
downstream of BRCA2 recruitment and upstream of RAD51 recruitment.
BCDX2 binds predominantly to the intersection of the four duplex
arms of the Holliday junction and to junction of replication
forks. The BCDX2 complex was originally reported to bind single-
stranded DNA, single-stranded gaps in duplex DNA and specifically
to nicks in duplex DNA. Involved in telomere maintenance. The
BCDX2 subcomplex XRCC2:RAD51D can stimulate Holliday junction
resolution by BLM. {ECO:0000269|PubMed:10871607,
ECO:0000269|PubMed:11751635, ECO:0000269|PubMed:11834724,
ECO:0000269|PubMed:11842113, ECO:0000269|PubMed:12975363,
ECO:0000269|PubMed:15109494, ECO:0000269|PubMed:23149936}.
-!- SUBUNIT: Part of the BCDX2 complex consisting of RAD51B, RAD51C,
RAD51D and XRCC2; the complex has a ring-like structure arranged
into a flat disc around a central channel. In the absence of DNA,
the BCDX2 subcomplex XRCC2:RAD51D formed a multimeric ring
structure; in the presence of single-stranded DNA it formed a
filamentous structure with the ssDNA. Interacts with SWSAP1 and
ZSWIM7; involved in homologous recombination repair. Interacts
with BLM; required for stimulation of BLM activity by the BCDX2
subcomplex XRCC2:RAD51D. {ECO:0000269|PubMed:10871607,
ECO:0000269|PubMed:11744692, ECO:0000269|PubMed:11751635,
ECO:0000269|PubMed:11834724, ECO:0000269|PubMed:11842112,
ECO:0000269|PubMed:11842113, ECO:0000269|PubMed:12975363,
ECO:0000269|PubMed:16710300, ECO:0000269|PubMed:21965664}.
-!- INTERACTION:
Q9Y2J4:AMOTL2; NbExp=6; IntAct=EBI-1055693, EBI-746752;
Q9Y2J4-4:AMOTL2; NbExp=3; IntAct=EBI-1055693, EBI-10187270;
P54132:BLM; NbExp=4; IntAct=EBI-1055693, EBI-621372;
Q6P1W5:C1orf94; NbExp=6; IntAct=EBI-1055693, EBI-946029;
Q8IYA8:CCDC36; NbExp=5; IntAct=EBI-1055693, EBI-8638439;
Q6P2R3:CEP57L1; NbExp=3; IntAct=EBI-1055693, EBI-12696312;
Q8IYX8-2:CEP57L1; NbExp=3; IntAct=EBI-1055693, EBI-10181988;
Q5JST6:EFHC2; NbExp=3; IntAct=EBI-1055693, EBI-2349927;
Q13422:IKZF1; NbExp=4; IntAct=EBI-1055693, EBI-745305;
Q13422-7:IKZF1; NbExp=3; IntAct=EBI-1055693, EBI-11522367;
Q9UKT9:IKZF3; NbExp=8; IntAct=EBI-1055693, EBI-747204;
F5H3M2:KIFC3; NbExp=3; IntAct=EBI-1055693, EBI-11953930;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-1055693, EBI-2125614;
P19012:KRT15; NbExp=6; IntAct=EBI-1055693, EBI-739566;
Q8TBB1:LNX1; NbExp=6; IntAct=EBI-1055693, EBI-739832;
Q9BRK4:LZTS2; NbExp=8; IntAct=EBI-1055693, EBI-741037;
Q9GZV8:PRDM14; NbExp=3; IntAct=EBI-1055693, EBI-3957793;
O15315:RAD51B; NbExp=5; IntAct=EBI-1055693, EBI-2824089;
O43502:RAD51C; NbExp=6; IntAct=EBI-1055693, EBI-2267048;
Q6NVH7:SWSAP1; NbExp=2; IntAct=EBI-1055693, EBI-5281637;
O43543:XRCC2; NbExp=29; IntAct=EBI-1055693, EBI-3918457;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome.
Chromosome, telomere.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1; Synonyms=TRAD;
IsoId=O75771-1; Sequence=Displayed;
Name=2; Synonyms=TRAD-D1, D2;
IsoId=O75771-2; Sequence=VSP_005558, VSP_005559;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=3; Synonyms=TRAD-D3;
IsoId=O75771-3; Sequence=VSP_005560;
Name=4; Synonyms=TRAD-D4;
IsoId=O75771-4; Sequence=VSP_005561;
Name=5; Synonyms=TRAD-D5;
IsoId=O75771-5; Sequence=VSP_005562;
Name=6; Synonyms=TRAD-D6, D7;
IsoId=O75771-6; Sequence=VSP_005563, VSP_005564;
Name=7; Synonyms=TRAD-D8;
IsoId=O75771-7; Sequence=VSP_005565, VSP_005566;
Name=8;
IsoId=O75771-8; Sequence=VSP_043658;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in colon, prostate, spleen, testis,
ovary, thymus and small intestine. Weakly expressed in leukocytes.
-!- DISEASE: Breast-ovarian cancer, familial, 4 (BROVCA4)
[MIM:614291]: A condition associated with familial predisposition
to cancer of the breast and ovaries. Characteristic features in
affected families are an early age of onset of breast cancer
(often before age 50), increased chance of bilateral cancers
(cancer that develop in both breasts, or both ovaries,
independently), frequent occurrence of breast cancer among men,
increased incidence of tumors of other specific organs, such as
the prostate. {ECO:0000269|PubMed:21822267}. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/rad51l3/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RAD51L3ID347ch17q12.html";
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EMBL; Y15572; CAA75681.1; -; mRNA.
EMBL; AF034956; AAC39719.1; -; mRNA.
EMBL; AB013341; BAA25914.1; -; mRNA.
EMBL; AB016223; BAA31747.1; -; mRNA.
EMBL; AB016224; BAA31748.1; -; mRNA.
EMBL; AB016225; BAA31749.1; -; mRNA.
EMBL; AB018360; BAA33779.1; -; mRNA.
EMBL; AB018361; BAA33780.1; -; mRNA.
EMBL; AB018362; BAA33781.1; -; mRNA.
EMBL; AB018363; BAA33782.1; -; mRNA.
EMBL; AB020412; BAA34690.1; -; mRNA.
EMBL; AY623116; AAT38112.1; -; Genomic_DNA.
EMBL; AK296241; BAG58959.1; -; mRNA.
EMBL; AC022916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471147; EAW80181.1; -; Genomic_DNA.
EMBL; CH471147; EAW80184.1; -; Genomic_DNA.
EMBL; CH471147; EAW80196.1; -; Genomic_DNA.
EMBL; BC014422; AAH14422.1; -; mRNA.
EMBL; AL117459; CAB55937.1; -; mRNA.
CCDS; CCDS11287.1; -. [O75771-1]
CCDS; CCDS11288.1; -. [O75771-3]
CCDS; CCDS45646.1; -. [O75771-8]
PIR; T17247; T17247.
RefSeq; NP_001136043.1; NM_001142571.1. [O75771-8]
RefSeq; NP_002869.3; NM_002878.3. [O75771-1]
RefSeq; NP_598332.1; NM_133629.2. [O75771-3]
UniGene; Hs.631757; -.
PDB; 2KZ3; NMR; -; A=1-83.
PDBsum; 2KZ3; -.
ProteinModelPortal; O75771; -.
SMR; O75771; -.
BioGrid; 111829; 41.
CORUM; O75771; -.
DIP; DIP-24265N; -.
IntAct; O75771; 55.
MINT; O75771; -.
STRING; 9606.ENSP00000466834; -.
iPTMnet; O75771; -.
PhosphoSitePlus; O75771; -.
BioMuta; RAD51D; -.
EPD; O75771; -.
MaxQB; O75771; -.
PaxDb; O75771; -.
PeptideAtlas; O75771; -.
PRIDE; O75771; -.
ProteomicsDB; 50183; -.
ProteomicsDB; 50184; -. [O75771-2]
ProteomicsDB; 50185; -. [O75771-3]
ProteomicsDB; 50186; -. [O75771-4]
ProteomicsDB; 50187; -. [O75771-5]
ProteomicsDB; 50188; -. [O75771-6]
ProteomicsDB; 50189; -. [O75771-7]
ProteomicsDB; 50190; -. [O75771-8]
DNASU; 5892; -.
Ensembl; ENST00000335858; ENSP00000338408; ENSG00000185379. [O75771-3]
Ensembl; ENST00000345365; ENSP00000338790; ENSG00000185379. [O75771-1]
Ensembl; ENST00000394589; ENSP00000378090; ENSG00000185379. [O75771-1]
Ensembl; ENST00000586044; ENSP00000465584; ENSG00000185379. [O75771-2]
Ensembl; ENST00000587977; ENSP00000466587; ENSG00000185379. [O75771-6]
Ensembl; ENST00000588594; ENSP00000465366; ENSG00000185379. [O75771-2]
Ensembl; ENST00000590016; ENSP00000466399; ENSG00000185379. [O75771-8]
GeneID; 5892; -.
KEGG; hsa:5892; -.
UCSC; uc002hir.4; human. [O75771-1]
CTD; 5892; -.
DisGeNET; 5892; -.
EuPathDB; HostDB:ENSG00000185379.20; -.
GeneCards; RAD51D; -.
HGNC; HGNC:9823; RAD51D.
MalaCards; RAD51D; -.
MIM; 602954; gene.
MIM; 614291; phenotype.
neXtProt; NX_O75771; -.
OpenTargets; ENSG00000185379; -.
Orphanet; 145; Hereditary breast and ovarian cancer syndrome.
PharmGKB; PA34179; -.
eggNOG; KOG1433; Eukaryota.
eggNOG; KOG4275; Eukaryota.
eggNOG; ENOG41101VR; LUCA.
GeneTree; ENSGT00860000133731; -.
HOGENOM; HOG000049134; -.
HOVERGEN; HBG057455; -.
InParanoid; O75771; -.
KO; K10871; -.
OMA; CSLSYKA; -.
OrthoDB; EOG091G0SEJ; -.
PhylomeDB; O75771; -.
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
GeneWiki; RAD51L3; -.
GenomeRNAi; 5892; -.
PRO; PR:O75771; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000185379; Expressed in 128 organ(s), highest expression level in sperm.
ExpressionAtlas; O75771; baseline and differential.
Genevisible; O75771; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0033063; C:Rad51B-Rad51C-Rad51D-XRCC2 complex; IDA:UniProtKB.
GO; GO:0005657; C:replication fork; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
GO; GO:0000150; F:recombinase activity; IBA:GO_Central.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; TAS:ProtInc.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
GO; GO:0036297; P:interstrand cross-link repair; IEA:Ensembl.
GO; GO:0000707; P:meiotic DNA recombinase assembly; IBA:GO_Central.
GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
GO; GO:0006289; P:nucleotide-excision repair; IEA:Ensembl.
GO; GO:0007131; P:reciprocal meiotic recombination; TAS:ProtInc.
GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
GO; GO:0010212; P:response to ionizing radiation; IBA:GO_Central.
GO; GO:0042148; P:strand invasion; IDA:UniProtKB.
GO; GO:0000723; P:telomere maintenance; IMP:UniProtKB.
CDD; cd01123; Rad51_DMC1_radA; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
InterPro; IPR016467; DNA_recomb/repair_RecA-like.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR033925; Rad51_DMC1_RadA.
InterPro; IPR020588; RecA_ATP-bd.
Pfam; PF08423; Rad51; 1.
PIRSF; PIRSF005856; Rad51; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50162; RECA_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Chromosome;
Complete proteome; Cytoplasm; Cytoskeleton; DNA damage;
DNA recombination; DNA repair; DNA-binding; Nucleotide-binding;
Nucleus; Polymorphism; Reference proteome; Telomere.
CHAIN 1 328 DNA repair protein RAD51 homolog 4.
/FTId=PRO_0000122942.
NP_BIND 107 114 ATP. {ECO:0000255}.
REGION 1 83 preferentially binds ssDNA.
COMPBIAS 200 205 Poly-Val.
VAR_SEQ 49 88 ALVALRRVLLAQFSAFPVNGADLYEELKTSTAILSTGIGS
-> TWRAHSSGNLGGLQLPQVPAGRSWSGVRNALKKAGLGH
GGTDGLSLNAFDERGTAVSTSR (in isoform 8).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043658.
VAR_SEQ 49 49 A -> S (in isoform 2). {ECO:0000305}.
/FTId=VSP_005558.
VAR_SEQ 50 328 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_005559.
VAR_SEQ 50 161 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_005560.
VAR_SEQ 88 118 SLDKLLDAGLYTGEVTEIVGGPGSGKTQVCL -> RHGGRT
QVGTWEDCSCLRSPQGDRGVGSGML (in isoform 6).
{ECO:0000305}.
/FTId=VSP_005563.
VAR_SEQ 88 101 SLDKLLDAGLYTGE -> RQKLSGGSRWCMHL (in
isoform 5). {ECO:0000305}.
/FTId=VSP_005562.
VAR_SEQ 116 160 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_005561.
VAR_SEQ 119 328 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_005564.
VAR_SEQ 193 212 VTGSSGTVKVVVVDSVTAVV -> DGIPEHLNHIPHCLHVH
LPC (in isoform 7). {ECO:0000305}.
/FTId=VSP_005565.
VAR_SEQ 213 328 Missing (in isoform 7). {ECO:0000305}.
/FTId=VSP_005566.
VARIANT 9 9 C -> S (in dbSNP:rs140825795).
{ECO:0000269|PubMed:27932480}.
/FTId=VAR_079271.
VARIANT 24 24 R -> S (in dbSNP:rs28363257).
{ECO:0000269|Ref.4}.
/FTId=VAR_020560.
VARIANT 165 165 R -> Q (in dbSNP:rs4796033).
{ECO:0000269|Ref.4}.
/FTId=VAR_020561.
VARIANT 225 225 A -> T (in dbSNP:rs28363282).
{ECO:0000269|Ref.4}.
/FTId=VAR_020562.
VARIANT 232 232 R -> Q (in dbSNP:rs28363283).
{ECO:0000269|Ref.4}.
/FTId=VAR_020563.
VARIANT 233 233 E -> G (in dbSNP:rs28363284).
{ECO:0000269|Ref.4}.
/FTId=VAR_020564.
CONFLICT 231 231 A -> V (in Ref. 9; CAB55937).
{ECO:0000305}.
HELIX 14 22 {ECO:0000244|PDB:2KZ3}.
HELIX 28 31 {ECO:0000244|PDB:2KZ3}.
HELIX 36 43 {ECO:0000244|PDB:2KZ3}.
HELIX 47 61 {ECO:0000244|PDB:2KZ3}.
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


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