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O75771 (RA51D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein RAD51 homolog 4
Alternative name(s):
R51H3
RAD51 homolog D
RAD51-like protein 3
TRAD
Gene names
Name:RAD51D
Synonyms:RAD51L3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.17 Ref.23

Subunit structure

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. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.19 Ref.21

Subcellular location

Nucleus Probable. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Chromosometelomere Ref.17 Ref.20.

Tissue specificity

Expressed in colon, prostate, spleen, testis, ovary, thymus and small intestine. Weakly expressed in leukocytes.

Involvement in 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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.22

Sequence similarities

Belongs to the RecA family. RAD51 subfamily.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
   Cellular componentChromosome
Cytoplasm
Cytoskeleton
Nucleus
Telomere
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.10. Source: GOC

DNA repair

Traceable author statement Ref.2. Source: ProtInc

double-strand break repair via homologous recombination

Inferred from mutant phenotype Ref.23. Source: UniProtKB

reciprocal meiotic recombination

Traceable author statement Ref.2. Source: ProtInc

strand invasion

Inferred from direct assay Ref.12. Source: UniProtKB

telomere maintenance

Inferred from mutant phenotype Ref.17. Source: UniProtKB

   Cellular_componentRad51B-Rad51C-Rad51D-XRCC2 complex

Inferred from direct assay Ref.11. Source: UniProtKB

centrosome

Inferred from direct assay Ref.20. Source: UniProtKB

chromosome, telomeric region

Inferred from direct assay Ref.17. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Traceable author statement Ref.2. Source: ProtInc

replication fork

Inferred from direct assay PubMed 20207730. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Traceable author statement Ref.2. Source: ProtInc

DNA-dependent ATPase activity

Inferred from direct assay Ref.10. Source: UniProtKB

gamma-tubulin binding

Inferred from direct assay Ref.20. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10749867Ref.10Ref.11Ref.13Ref.16Ref.19Ref.21PubMed 24141787. Source: IntAct

single-stranded DNA binding

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75771-1)

Also known as: TRAD;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O75771-2)

Also known as: TRAD-D1; D2;

The sequence of this isoform differs from the canonical sequence as follows:
     49-49: A → S
     50-328: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 3 (identifier: O75771-3)

Also known as: TRAD-D3;

The sequence of this isoform differs from the canonical sequence as follows:
     50-161: Missing.
Isoform 4 (identifier: O75771-4)

Also known as: TRAD-D4;

The sequence of this isoform differs from the canonical sequence as follows:
     116-160: Missing.
Isoform 5 (identifier: O75771-5)

Also known as: TRAD-D5;

The sequence of this isoform differs from the canonical sequence as follows:
     88-101: SLDKLLDAGLYTGE → RQKLSGGSRWCMHL
Isoform 6 (identifier: O75771-6)

Also known as: TRAD-D6; D7;

The sequence of this isoform differs from the canonical sequence as follows:
     88-118: SLDKLLDAGLYTGEVTEIVGGPGSGKTQVCL → RHGGRTQVGTWEDCSCLRSPQGDRGVGSGML
     119-328: Missing.
Isoform 7 (identifier: O75771-7)

Also known as: TRAD-D8;

The sequence of this isoform differs from the canonical sequence as follows:
     193-212: VTGSSGTVKVVVVDSVTAVV → DGIPEHLNHIPHCLHVHLPC
     213-328: Missing.
Isoform 8 (identifier: O75771-8)

The sequence of this isoform differs from the canonical sequence as follows:
     49-88: ALVALRRVLL...TAILSTGIGS → TWRAHSSGNL...ERGTAVSTSR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 328328DNA repair protein RAD51 homolog 4
PRO_0000122942

Regions

Nucleotide binding107 – 1148ATP Potential
Region1 – 8383Preferencially binds ssDNA
Compositional bias200 – 2056Poly-Val

Natural variations

Alternative sequence49 – 8840ALVAL…TGIGS → TWRAHSSGNLGGLQLPQVPA GRSWSGVRNALKKAGLGHGG TDGLSLNAFDERGTAVSTSR in isoform 8.
VSP_043658
Alternative sequence491A → S in isoform 2.
VSP_005558
Alternative sequence50 – 328279Missing in isoform 2.
VSP_005559
Alternative sequence50 – 161112Missing in isoform 3.
VSP_005560
Alternative sequence88 – 11831SLDKL…TQVCL → RHGGRTQVGTWEDCSCLRSP QGDRGVGSGML in isoform 6.
VSP_005563
Alternative sequence88 – 10114SLDKL…LYTGE → RQKLSGGSRWCMHL in isoform 5.
VSP_005562
Alternative sequence116 – 16045Missing in isoform 4.
VSP_005561
Alternative sequence119 – 328210Missing in isoform 6.
VSP_005564
Alternative sequence193 – 21220VTGSS…VTAVV → DGIPEHLNHIPHCLHVHLPC in isoform 7.
VSP_005565
Alternative sequence213 – 328116Missing in isoform 7.
VSP_005566
Natural variant241R → S. Ref.4
Corresponds to variant rs28363257 [ dbSNP | Ensembl ].
VAR_020560
Natural variant1651R → Q. Ref.4
Corresponds to variant rs4796033 [ dbSNP | Ensembl ].
VAR_020561
Natural variant2251A → T. Ref.4
Corresponds to variant rs28363282 [ dbSNP | Ensembl ].
VAR_020562
Natural variant2321R → Q. Ref.4
Corresponds to variant rs28363283 [ dbSNP | Ensembl ].
VAR_020563
Natural variant2331E → G. Ref.4
Corresponds to variant rs28363284 [ dbSNP | Ensembl ].
VAR_020564

Experimental info

Sequence conflict2311A → V in CAB55937. Ref.9

Secondary structure

......... 328
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (TRAD) [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 6038DA9356DF354A

FASTA32835,049
        10         20         30         40         50         60 
MGVLRVGLCP GLTEEMIQLL RSHRIKTVVD LVSADLEEVA QKCGLSYKAL VALRRVLLAQ 

        70         80         90        100        110        120 
FSAFPVNGAD LYEELKTSTA ILSTGIGSLD KLLDAGLYTG EVTEIVGGPG SGKTQVCLCM 

       130        140        150        160        170        180 
AANVAHGLQQ NVLYVDSNGG LTASRLLQLL QAKTQDEEEQ AEALRRIQVV HAFDIFQMLD 

       190        200        210        220        230        240 
VLQELRGTVA QQVTGSSGTV KVVVVDSVTA VVSPLLGGQQ REGLALMMQL ARELKTLARD 

       250        260        270        280        290        300 
LGMAVVVTNH ITRDRDSGRL KPALGRSWSF VPSTRILLDT IEGAGASGGR RMACLAKSSR 

       310        320 
QPTGFQEMVD IGTWGTSEQS ATLQGDQT 

« Hide

Isoform 2 (TRAD-D1) (D2) [UniParc].

Checksum: 0B2D7DC5AF7D3D70
Show »

FASTA495,387
Isoform 3 (TRAD-D3) [UniParc].

Checksum: 34C5B25933759EC0
Show »

FASTA21623,317
Isoform 4 (TRAD-D4) [UniParc].

Checksum: 77A839A78449DC78
Show »

FASTA28330,194
Isoform 5 (TRAD-D5) [UniParc].

Checksum: A494887924CB3834
Show »

FASTA32835,214
Isoform 6 (TRAD-D6) (D7) [UniParc].

Checksum: E7A605D379835E0A
Show »

FASTA11812,675
Isoform 7 (TRAD-D8) [UniParc].

Checksum: E2554F3D42E92D58
Show »

FASTA21222,975
Isoform 8 [UniParc].

Checksum: 7371C4C9882D629C
Show »

FASTA34837,014

References

« Hide 'large scale' references
[1]"Isolation of novel human and mouse genes of the recA/RAD51 recombination-repair gene family."
Cartwright R., Dunn A.M., Simpson P.J., Tambini C.E., Thacker J.
Nucleic Acids Res. 26:1653-1659(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Identification, characterization, and genetic mapping of Rad51d, a new mouse and human RAD51/RecA-related gene."
Pittman D.L., Weinberg L.R., Schimenti J.C.
Genomics 49:103-111(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Multiple alternative transcripts of the human homologue of the mouse TRAD/R51H3/RAD51D gene, a member of the recA/RAD51 gene family."
Kawabata M., Saeki K.
Biochem. Biophys. Res. Commun. 257:156-162(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING (ISOFORMS 2; 3; 4; 5; 6 AND 7).
Tissue: Brain.
[4]NIEHS SNPs program
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-24; GLN-165; THR-225; GLN-232 AND GLY-233.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
Tissue: Thalamus.
[6]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
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. expand/collapse author list , 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.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Skin.
[9]"The full-ORF clone resource of the German cDNA consortium."
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.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 156-328.
Tissue: Uterus.
[10]"The RAD51 family member, RAD51L3, is a DNA-stimulated ATPase that forms a complex with XRCC2."
Braybrooke J.P., Spink K.G., Thacker J., Hickson I.D.
J. Biol. Chem. 275:29100-29106(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH XRCC2.
[11]"Identification and purification of two distinct complexes containing the five RAD51 paralogs."
Masson J.Y., Tarsounas M.C., Stasiak A.Z., Stasiak A., Shah R., McIlwraith M.J., Benson F.E., West S.C.
Genes Dev. 15:3296-3307(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D AND XRCC2.
[12]"Homologous pairing and ring and filament structure formation activities of the human Xrcc2*Rad51D complex."
Kurumizaka H., Ikawa S., Nakada M., Enomoto R., Kagawa W., Kinebuchi T., Yamazoe M., Yokoyama S., Shibata T.
J. Biol. Chem. 277:14315-14320(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[13]"Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells."
Liu N., Schild D., Thelen M.P., Thompson L.H.
Nucleic Acids Res. 30:1009-1015(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D AND XRCC2.
[14]"RAD51C interacts with RAD51B and is central to a larger protein complex in vivo exclusive of RAD51."
Miller K.A., Yoshikawa D.M., McConnell I.R., Clark R., Schild D., Albala J.S.
J. Biol. Chem. 277:8406-8411(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[15]"Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human cells."
Wiese C., Collins D.W., Albala J.S., Thompson L.H., Kronenberg A., Schild D.
Nucleic Acids Res. 30:1001-1008(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D AND XRCC2.
[16]"Functional interaction between the Bloom's syndrome helicase and the RAD51 paralog, RAD51L3 (RAD51D)."
Braybrooke J.P., Li J.L., Wu L., Caple F., Benson F.E., Hickson I.D.
J. Biol. Chem. 278:48357-48366(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE BCDX2 COMPLEX, INTERACTION WITH BLM AND XRCC2.
[17]"Telomere maintenance requires the RAD51D recombination/repair protein."
Tarsounas M., Munoz P., Claas A., Smiraldo P.G., Pittman D.L., Blasco M.A., West S.C.
Cell 117:337-347(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[18]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[19]"Sws1 is a conserved regulator of homologous recombination in eukaryotic cells."
Martin V., Chahwan C., Gao H., Blais V., Wohlschlegel J., Yates J.R. III, McGowan C.H., Russell P.
EMBO J. 25:2564-2574(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZSWIM7 AND XRCC2.
[20]"Homologous recombination proteins are associated with centrosomes and are required for mitotic stability."
Cappelli E., Townsend S., Griffin C., Thacker J.
Exp. Cell Res. 317:1203-1213(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[21]"hSWS1.SWSAP1 is an evolutionarily conserved complex required for efficient homologous recombination repair."
Liu T., Wan L., Wu Y., Chen J., Huang J.
J. Biol. Chem. 286:41758-41766(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SWSAP1 AND ZSWIM7.
[22]"Germline mutations in RAD51D confer susceptibility to ovarian cancer."
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. expand/collapse author list , 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.
Nat. Genet. 43:879-882(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN BROVCA4.
[23]"Rad51 paralog complexes BCDX2 and CX3 act at different stages in the BRCA1-BRCA2-dependent homologous recombination pathway."
Chun J., Buechelmaier E.S., Powell S.N.
Mol. Cell. Biol. 33:387-395(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE BCDX2 COMPLEX.
[24]"Structural and functional characterization of the N-terminal domain of human Rad51D."
Kim Y.M., Choi B.S.
Int. J. Biochem. Cell Biol. 43:416-422(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-83, DNA-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y15572 mRNA. Translation: CAA75681.1.
AF034956 mRNA. Translation: AAC39719.1.
AB013341 mRNA. Translation: BAA25914.1.
AB016223 mRNA. Translation: BAA31747.1.
AB016224 mRNA. Translation: BAA31748.1.
AB016225 mRNA. Translation: BAA31749.1.
AB018360 mRNA. Translation: BAA33779.1.
AB018361 mRNA. Translation: BAA33780.1.
AB018362 mRNA. Translation: BAA33781.1.
AB018363 mRNA. Translation: BAA33782.1.
AB020412 mRNA. Translation: BAA34690.1.
AY623116 Genomic DNA. Translation: AAT38112.1.
AK296241 mRNA. Translation: BAG58959.1.
AC022916 Genomic DNA. No translation available.
CH471147 Genomic DNA. Translation: EAW80181.1.
CH471147 Genomic DNA. Translation: EAW80184.1.
CH471147 Genomic DNA. Translation: EAW80196.1.
BC014422 mRNA. Translation: AAH14422.1.
AL117459 mRNA. Translation: CAB55937.1.
CCDSCCDS11287.1. [O75771-1]
CCDS11288.1. [O75771-3]
CCDS45646.1. [O75771-8]
PIRT17247.
RefSeqNP_001136043.1. NM_001142571.1. [O75771-8]
NP_002869.3. NM_002878.3. [O75771-1]
NP_598332.1. NM_133629.2. [O75771-3]
UniGeneHs.631757.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KZ3NMR-A1-83[»]
ProteinModelPortalO75771.
SMRO75771. Positions 1-304.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111829. 10 interactions.
DIPDIP-24265N.
IntActO75771. 10 interactions.
MINTMINT-127795.

PTM databases

PhosphoSiteO75771.

Proteomic databases

MaxQBO75771.
PaxDbO75771.
PRIDEO75771.

Protocols and materials databases

DNASU5892.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335858; ENSP00000338408; ENSG00000185379. [O75771-3]
ENST00000345365; ENSP00000338790; ENSG00000185379. [O75771-1]
ENST00000357906; ENSP00000350581; ENSG00000185379. [O75771-6]
ENST00000360276; ENSP00000353417; ENSG00000185379. [O75771-4]
ENST00000394589; ENSP00000378090; ENSG00000185379. [O75771-1]
ENST00000586044; ENSP00000465584; ENSG00000185379. [O75771-2]
ENST00000587977; ENSP00000466587; ENSG00000185379. [O75771-6]
ENST00000588594; ENSP00000465366; ENSG00000185379. [O75771-2]
ENST00000590016; ENSP00000466399; ENSG00000185379. [O75771-8]
GeneID5892.
KEGGhsa:5892.
UCSCuc002hir.2. human. [O75771-1]
uc002his.2. human. [O75771-3]
uc010wcd.1. human. [O75771-8]

Organism-specific databases

CTD5892.
GeneCardsGC17M033427.
HGNCHGNC:9823. RAD51D.
MIM602954. gene.
614291. phenotype.
neXtProtNX_O75771.
Orphanet145. Hereditary breast and ovarian cancer syndrome.
PharmGKBPA34179.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0468.
HOGENOMHOG000049134.
HOVERGENHBG057455.
KOK10871.
OMACSLSYKA.
PhylomeDBO75771.

Gene expression databases

ArrayExpressO75771.
BgeeO75771.
GenevestigatorO75771.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR013632. DNA_recomb/repair_Rad51_C.
IPR016467. DNA_recomb/repair_RecA-like.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
[Graphical view]
PfamPF08423. Rad51. 1 hit.
[Graphical view]
PIRSFPIRSF005856. Rad51. 1 hit.
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS50162. RECA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRAD51L3.
GenomeRNAi5892.
NextBio22920.
PROO75771.
SOURCESearch...

Entry information

Entry nameRA51D_HUMAN
AccessionPrimary (citable) accession number: O75771
Secondary accession number(s): B4DJU7 expand/collapse secondary AC list , E1P637, O43537, O60355, O75196, O75847, O75848, O76073, O76085, O94908, Q9UFU5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM