O75771 (RA51D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	328 AA.
Sequence status	Complete.
Protein existence	Evidence 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. The BCDX2 complex binds single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. Ref.10 Ref.11
Subunit structure	Part of a BCDX2 complex consisting of RAD51B, RAD51C, RAD51D and XRCC2. Part of a complex consisting of RAD51B, RAD51C, RAD51D, XRCC2 and XRCC3. Interacts with SWSAP1 and ZSWIM7; involved in homologous recombination repair. Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16
Subcellular location	Nucleus Probable.
Tissue specificity	Expressed in colon, prostate, spleen, testis, ovary, thymus and small intestine. Weakly expressed in leukocytes.
Involvement in disease	Familial breast-ovarian cancer 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.17
Sequence similarities	Belongs to the RecA family. RAD51 subfamily.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding DNA-binding Nucleotide-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Traceable author statement Ref.2. Source: ProtInc reciprocal meiotic recombination Traceable author statement Ref.2. Source: ProtInc
Cellular_component	nucleus Traceable author statement Ref.2. Source: ProtInc
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Traceable author statement Ref.2. Source: ProtInc DNA-dependent ATPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SWSAP1	Q6NVH7	2	EBI-1055693,EBI-5281637

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 328

328

DNA repair protein RAD51 homolog 4

PRO_0000122942

Regions

Nucleotide binding

107 – 114

8

ATP Potential

Region

1 – 83

83

Preferencially binds ssDNA

Compositional bias

200 – 205

6

Poly-Val

Natural variations

Alternative sequence

49 – 88

40

ALVAL…TGIGS → TWRAHSSGNLGGLQLPQVPA GRSWSGVRNALKKAGLGHGG TDGLSLNAFDERGTAVSTSR in isoform 8.

VSP_043658

Alternative sequence

49

1

A → S in isoform 2.

VSP_005558

Alternative sequence

50 – 328

279

Missing in isoform 2.

VSP_005559

Alternative sequence

50 – 161

112

Missing in isoform 3.

VSP_005560

Alternative sequence

88 – 118

31

SLDKL…TQVCL → RHGGRTQVGTWEDCSCLRSP QGDRGVGSGML in isoform 6.

VSP_005563

Alternative sequence

88 – 101

14

SLDKL…LYTGE → RQKLSGGSRWCMHL in isoform 5.

VSP_005562

Alternative sequence

116 – 160

45

Missing in isoform 4.

VSP_005561

Alternative sequence

119 – 328

210

Missing in isoform 6.

VSP_005564

Alternative sequence

193 – 212

20

VTGSS…VTAVV → DGIPEHLNHIPHCLHVHLPC in isoform 7.

VSP_005565

Alternative sequence

213 – 328

116

Missing in isoform 7.

VSP_005566

Natural variant

24

1

R → S. Ref.4
Corresponds to variant rs28363257 [ dbSNP | Ensembl ].

VAR_020560

Natural variant

165

1

R → Q. Ref.4
Corresponds to variant rs4796033 [ dbSNP | Ensembl ].

VAR_020561

Natural variant

225

1

A → T. Ref.4
Corresponds to variant rs28363282 [ dbSNP | Ensembl ].

VAR_020562

Natural variant

232

1

R → Q. Ref.4
Corresponds to variant rs28363283 [ dbSNP | Ensembl ].

VAR_020563

Natural variant

233

1

E → G. Ref.4
Corresponds to variant rs28363284 [ dbSNP | Ensembl ].

VAR_020564

Experimental info

Sequence conflict

231

1

A → V in CAB55937. Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

328

Helix Strand Turn

Details...

Helix

14 – 22

9

Helix

28 – 31

4

Helix

36 – 43

8

Helix

47 – 61

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (TRAD) [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 6038DA9356DF354A	FASTA	328	35,049
	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
	Isoform 2 (TRAD-D1) (D2) [UniParc]. Checksum: 0B2D7DC5AF7D3D70	FASTA	49	5,387
	10 20 30 40 MGVLRVGLCP GLTEEMIQLL RSHRIKTVVD LVSADLEEVA QKCGLSYKS
	Isoform 3 (TRAD-D3) [UniParc]. Checksum: 34C5B25933759EC0	FASTA	216	23,317
	10 20 30 40 50 60 MGVLRVGLCP GLTEEMIQLL RSHRIKTVVD LVSADLEEVA QKCGLSYKAE ALRRIQVVHA 70 80 90 100 110 120 FDIFQMLDVL QELRGTVAQQ VTGSSGTVKV VVVDSVTAVV SPLLGGQQRE GLALMMQLAR 130 140 150 160 170 180 ELKTLARDLG MAVVVTNHIT RDRDSGRLKP ALGRSWSFVP STRILLDTIE GAGASGGRRM 190 200 210 ACLAKSSRQP TGFQEMVDIG TWGTSEQSAT LQGDQT
	Isoform 4 (TRAD-D4) [UniParc]. Checksum: 77A839A78449DC78	FASTA	283	30,194
	10 20 30 40 50 60 MGVLRVGLCP GLTEEMIQLL RSHRIKTVVD LVSADLEEVA QKCGLSYKAL VALRRVLLAQ 70 80 90 100 110 120 FSAFPVNGAD LYEELKTSTA ILSTGIGSLD KLLDAGLYTG EVTEIVGGPG SGKTQAEALR 130 140 150 160 170 180 RIQVVHAFDI FQMLDVLQEL RGTVAQQVTG SSGTVKVVVV DSVTAVVSPL LGGQQREGLA 190 200 210 220 230 240 LMMQLARELK TLARDLGMAV VVTNHITRDR DSGRLKPALG RSWSFVPSTR ILLDTIEGAG 250 260 270 280 ASGGRRMACL AKSSRQPTGF QEMVDIGTWG TSEQSATLQG DQT
	Isoform 5 (TRAD-D5) [UniParc]. Checksum: A494887924CB3834	FASTA	328	35,214
	10 20 30 40 50 60 MGVLRVGLCP GLTEEMIQLL RSHRIKTVVD LVSADLEEVA QKCGLSYKAL VALRRVLLAQ 70 80 90 100 110 120 FSAFPVNGAD LYEELKTSTA ILSTGIGRQK LSGGSRWCMH LVTEIVGGPG 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
	Isoform 6 (TRAD-D6) (D7) [UniParc]. Checksum: E7A605D379835E0A	FASTA	118	12,675
	10 20 30 40 50 60 MGVLRVGLCP GLTEEMIQLL RSHRIKTVVD LVSADLEEVA QKCGLSYKAL VALRRVLLAQ 70 80 90 100 110 FSAFPVNGAD LYEELKTSTA ILSTGIGRHG GRTQVGTWED CSCLRSPQGD RGVGSGML
	Isoform 7 (TRAD-D8) [UniParc]. Checksum: E2554F3D42E92D58	FASTA	212	22,975
	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 VLQELRGTVA QQDGIPEHLN HIPHCLHVHL PC
	Isoform 8 [UniParc]. Checksum: 7371C4C9882D629C	FASTA	348	37,014
	10 20 30 40 50 60 MGVLRVGLCP GLTEEMIQLL RSHRIKTVVD LVSADLEEVA QKCGLSYKTW RAHSSGNLGG 70 80 90 100 110 120 LQLPQVPAGR SWSGVRNALK KAGLGHGGTD GLSLNAFDER GTAVSTSRLD KLLDAGLYTG 130 140 150 160 170 180 EVTEIVGGPG SGKTQVCLCM AANVAHGLQQ NVLYVDSNGG LTASRLLQLL QAKTQDEEEQ 190 200 210 220 230 240 AEALRRIQVV HAFDIFQMLD VLQELRGTVA QQVTGSSGTV KVVVVDSVTA VVSPLLGGQQ 250 260 270 280 290 300 REGLALMMQL ARELKTLARD LGMAVVVTNH ITRDRDSGRL KPALGRSWSF VPSTRILLDT 310 320 330 340 IEGAGASGGR RMACLAKSSR QPTGFQEMVD IGTWGTSEQS ATLQGDQT

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"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.
[11]	"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.
[12]	"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: IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D; XRCC2 AND XRCC3.
[13]	"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.
[14]	"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).
[15]	"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.
[16]	"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.
[17]	"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. , 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.
[18]	"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.

Web resources

NIEHS-SNPs

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.

IPI

IPI00216381.
IPI00216382.
IPI00216383.
IPI00216384.
IPI00216386.
IPI00291454.
IPI00411326.
IPI00791891.

PIR

T17247.

RefSeq

NP_001136043.1. NM_001142571.1.
NP_002869.3. NM_002878.3.
NP_598332.1. NM_133629.2.

UniGene

Hs.631757.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KZ3	NMR	-	A	1-83	[»]

ProteinModelPortal

O75771.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24265N.

IntAct

O75771. 2 interactions.

MINT

MINT-127795.

PTM databases

PhosphoSite

O75771.

Proteomic databases

PaxDb

O75771.

PRIDE

O75771.

Protocols and materials databases

DNASU

5892.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000335858; ENSP00000338408; ENSG00000185379.
ENST00000345365; ENSP00000338790; ENSG00000185379.
ENST00000357906; ENSP00000350581; ENSG00000185379.
ENST00000360276; ENSP00000353417; ENSG00000185379.
ENST00000394589; ENSP00000378090; ENSG00000185379.
ENST00000586044; ENSP00000465584; ENSG00000185379.
ENST00000587977; ENSP00000466587; ENSG00000185379.
ENST00000588594; ENSP00000465366; ENSG00000185379.
ENST00000590016; ENSP00000466399; ENSG00000185379.

GeneID

5892.

KEGG

hsa:5892.

UCSC

uc002hir.2. human.
uc002his.2. human.

Organism-specific databases

CTD

5892.

GeneCards

GC17M033427.

HGNC

HGNC:9823. RAD51D.

MIM

602954. gene.
614291. phenotype.

neXtProt

NX_O75771.

Orphanet

145. Hereditary breast and ovarian cancer syndrome.

PharmGKB

PA34179.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0468.

HOGENOM

HOG000049134.

HOVERGEN

HBG057455.

KO

K10871.

OMA

QARTQDE.

OrthoDB

EOG4K0QP3.

PhylomeDB

O75771.

Gene expression databases

ArrayExpress

O75771.

Bgee

O75771.

Genevestigator

O75771.

GermOnline

ENSG00000185379. Homo sapiens.

Family and domain databases

InterPro

IPR003593. AAA+_ATPase.
IPR013632. DNA_recomb/repair_Rad51_C.
IPR016467. DNA_recomb/repair_RecA-like.
IPR020588. DNA_recomb_RecA/RadB_ATP-bd.
[Graphical view]

Pfam

PF08423. Rad51. 1 hit.
[Graphical view]

PIRSF

PIRSF005856. Rad51. 1 hit.

SMART

SM00382. AAA. 1 hit.
[Graphical view]

PROSITE

PS50162. RECA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

5892.

NextBio

22920.

SOURCE

Search...

Entry information

Entry name

RA51D_HUMAN

Accession

Primary (citable) accession number: O75771
Secondary accession number(s): B4DJU7 , 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:	May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.