Q06609 (RAD51_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA repair protein RAD51 homolog 1
Short name=HsRAD51
Short name=hRAD51

Alternative name(s):
RAD51 homolog A

Gene names

Name:	RAD51
Synonyms:	RAD51A, RECA

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May participate in a common DNA damage response pathway associated with the activation of homologous recombination and double-strand break repair. Binds to single and double stranded DNA and exhibits DNA-dependent ATPase activity. Underwinds duplex DNA and forms helical nucleoprotein filaments. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Ref.5 Ref.18 Ref.26
Subunit structure	Interacts with BRCA1, BRCA2 and either directly or indirectly with p53. Interacts with XRCC3, RAD54L and RAD54B. Part of a complex with RAD51C and RAD51B. Interacts with RAD51AP1 and RAD51AP2. Interacts with CHEK1, and this may require prior phosphorylation of CHEK1. Interacts with the MND1-PSMC3IP heterodimer By similarity. Interacts with OBFC2B. Interacts with RPA1, PALB2 and RAD51. Interacts with SWI5/C9orf119, and at lower level with SFR1/MEIR5. Interacts with hyperphosphorylated RPA2; this interaction is necessary for efficient recruitment to chromatin in response to DNA damage. Interacts with SWSAP1; involved in homologous recombination repair. Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.22 Ref.23 Ref.24 Ref.27 Ref.28 Ref.29 Ref.30
Subcellular location	Nucleus. Cytoplasm. Cytoplasm › perinuclear region. Mitochondrion matrix. Note: Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage. DNA damage induces an increase in nuclear levels. Ref.5 Ref.15 Ref.21 Ref.22 Ref.25 Ref.26 Ref.28
Tissue specificity	Highly expressed in testis and thymus, followed by small intestine, placenta, colon, pancreas and ovary. Weakly expressed in breast. Ref.5
Induction	Stress-induced increase in the mitochondrial levels is seen. Ref.26
Domain	The nuclear localization may reside in the C-terminus (between 259 and 339 AA).
Post-translational modification	Phosphorylated. Phosphorylation of Thr-309 by CHEK1 may enhance association with chromatin at sites of DNA damage and promote DNA repair by homologous recombination. Phosphorylation by ABL1 inhibits function. Ref.16 Ref.22
Involvement in disease	Defects in RAD51 are a cause of susceptibility to breast cancer (BC) [MIM:114480]. A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. Ref.33
Sequence similarities	Belongs to the RecA family. RAD51 subfamily. Contains 1 HhH domain.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair
Cellular component	Cytoplasm Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Ligand	ATP-binding DNA-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA recombinase assembly Traceable author statement. Source: Reactome DNA unwinding involved in replication Inferred from direct assay Ref.12. Source: UniProtKB mitotic recombination Traceable author statement. Source: ProtInc positive regulation of DNA ligation Inferred from direct assay. Source: UniProtKB protein homooligomerization Inferred from physical interaction. Source: UniProtKB reciprocal meiotic recombination Traceable author statement. Source: ProtInc
Cellular component	PML body Inferred from direct assay. Source: UniProtKB condensed nuclear chromosome Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.21Ref.5. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay Ref.21. Source: UniProtKB
Molecular function	ATP binding Inferred from direct assay. Source: MGI damaged DNA binding Inferred from electronic annotation. Source: InterPro double-stranded DNA binding Inferred from direct assay Ref.12. Source: UniProtKB identical protein binding Inferred from physical interaction. Source: IntAct protein C-terminus binding Inferred from physical interaction. Source: UniProtKB single-stranded DNA binding Inferred from direct assay Ref.12. Source: UniProtKB single-stranded DNA-dependent ATPase activity Inferred from direct assay Ref.12. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-297202,EBI-297202
BRCA2	P51587	19	EBI-297202,EBI-79792
CHEK1	O14757	3	EBI-297202,EBI-974488
RAD51AP1	Q96B01-2	4	EBI-297202,EBI-1178743
RAD51AP1	Q96B01-3	5	EBI-297202,EBI-1178748
RAD52	P43351	3	EBI-297202,EBI-706448
TP53	P04637	2	EBI-297202,EBI-366083

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q06609-1)

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: Q06609-2)

The sequence of this isoform differs from the canonical sequence as follows:
     77-173: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q06609-3)

The sequence of this isoform differs from the canonical sequence as follows:
     259-284: FGVAVVITNQVVAQVDGAAMFAADPK → IVSEERKRGNQNLQNLRLSLSS
     285-339: Missing.

Note: Mutagenesis of Arg-264 to Ala inhibits nuclear localization. Mutagenesis of Lys-264 to Gln inhibits nuclear localization. Deletion of 254-Arg-Lys-255 inhibits nuclear localization.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 339

339

DNA repair protein RAD51 homolog 1

PRO_0000122932

Regions

Domain

48 – 77

30

HhH

Nucleotide binding

127 – 134

8

ATP By similarity

Region

184 – 257

74

Interaction with PALB2

Amino acid modifications

Modified residue

54

1

Phosphotyrosine; by ABL1 Ref.16

Modified residue

309

1

Phosphothreonine; by CHEK1 Ref.22

Natural variations

Alternative sequence

77 – 173

97

Missing in isoform 2.

VSP_005556

Alternative sequence

259 – 284

26

FGVAV…AADPK → IVSEERKRGNQNLQNLRLSL SS in isoform 3.

VSP_041724

Alternative sequence

285 – 339

55

Missing in isoform 3.

VSP_041725

Natural variant

150

1

R → Q in BC; familial. Ref.33

VAR_010899

Experimental info

Mutagenesis

309

1

T → A: Confers hypersensitivity to hydroxyurea. Ref.22

Sequence conflict

313

1

K → Q in BAA02962. Ref.1

Secondary structure

1

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339

Helix Strand Turn

Details...

Helix

25 – 30

6

Helix

35 – 42

8

Helix

49 – 51

3

Beta strand

54 – 56

3

Helix

57 – 61

5

Turn

62 – 65

4

Helix

70 – 81

12

Helix

107 – 112

6

Turn

113 – 115

3

Beta strand

116 – 118

3

Beta strand

121 – 126

6

Helix

133 – 143

11

Helix

148 – 150

3

Beta strand

154 – 164

11

Helix

168 – 177

10

Helix

182 – 187

6

Beta strand

189 – 193

5

Helix

197 – 213

17

Beta strand

216 – 222

7

Helix

226 – 228

3

Helix

238 – 259

22

Beta strand

262 – 267

6

Beta strand

298 – 304

7

Beta strand

309 – 314

6

Beta strand

323 – 330

8

Beta strand

333 – 335

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 26578E6206DEDEDA	FASTA	339	36,966
	10 20 30 40 50 60 MAMQMQLEAN ADTSVEEESF GPQPISRLEQ CGINANDVKK LEEAGFHTVE AVAYAPKKEL 70 80 90 100 110 120 INIKGISEAK ADKILAEAAK LVPMGFTTAT EFHQRRSEII QITTGSKELD KLLQGGIETG 130 140 150 160 170 180 SITEMFGEFR TGKTQICHTL AVTCQLPIDR GGGEGKAMYI DTEGTFRPER LLAVAERYGL 190 200 210 220 230 240 SGSDVLDNVA YARAFNTDHQ TQLLYQASAM MVESRYALLI VDSATALYRT DYSGRGELSA 250 260 270 280 290 300 RQMHLARFLR MLLRLADEFG VAVVITNQVV AQVDGAAMFA ADPKKPIGGN IIAHASTTRL 310 320 330 YLRKGRGETR ICKIYDSPCL PEAEAMFAIN ADGVGDAKD
	Isoform 2 [UniParc]. Checksum: DFA9E12DC8429CA2	FASTA	242	26,351
	10 20 30 40 50 60 MAMQMQLEAN ADTSVEEESF GPQPISRLEQ CGINANDVKK LEEAGFHTVE AVAYAPKKEL 70 80 90 100 110 120 INIKGISEAK ADKILAVAER YGLSGSDVLD NVAYARAFNT DHQTQLLYQA SAMMVESRYA 130 140 150 160 170 180 LLIVDSATAL YRTDYSGRGE LSARQMHLAR FLRMLLRLAD EFGVAVVITN QVVAQVDGAA 190 200 210 220 230 240 MFAADPKKPI GGNIIAHAST TRLYLRKGRG ETRICKIYDS PCLPEAEAMF AINADGVGDA KD
	Isoform 3 [UniParc]. Checksum: 1DFA22F6C0926FC2	FASTA	280	31,001
	10 20 30 40 50 60 MAMQMQLEAN ADTSVEEESF GPQPISRLEQ CGINANDVKK LEEAGFHTVE AVAYAPKKEL 70 80 90 100 110 120 INIKGISEAK ADKILAEAAK LVPMGFTTAT EFHQRRSEII QITTGSKELD KLLQGGIETG 130 140 150 160 170 180 SITEMFGEFR TGKTQICHTL AVTCQLPIDR GGGEGKAMYI DTEGTFRPER LLAVAERYGL 190 200 210 220 230 240 SGSDVLDNVA YARAFNTDHQ TQLLYQASAM MVESRYALLI VDSATALYRT DYSGRGELSA 250 260 270 280 RQMHLARFLR MLLRLADEIV SEERKRGNQN LQNLRLSLSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA." Shinohara A., Ogawa H., Matsuda Y., Ushio N., Ikeo K., Ogawa T. Nat. Genet. 4:239-243(1993) [PubMed: 8358431] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Cloning and sequence of the human RecA-like gene cDNA." Yoshimura Y., Morita T., Yamamoto A., Matsushiro A. Nucleic Acids Res. 21:1665-1665(1993) [PubMed: 8479919] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Testis.
[3]	"Characterization of the human Rad51 genomic locus and examination of tumors with 15q14-15 loss of heterozygosity (LOH)." Schmutte C., Tombline G., Rhiem K., Sadoff M.M., Schmutzler R., von Deimling A., Fishel R. Cancer Res. 59:4564-4569(1999) [PubMed: 10493508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"A single nucleotide polymorphism in the 5' untranslated region of RAD51 and risk of cancer among BRCA1/2 mutation carriers." Wang W.W., Spurdle A.B., Kolachana P., Bove B., Modan B., Ebbers S.M., Suthers G., Tucker M.A., Kaufman D.J., Doody M.M., Tarone R.E., Daly M., Levavi H., Pierce H., Chetrit A., Yechezkel G.H., Chenevix-Trench G., Offit K., Godwin A.K., Struewing J.P. Cancer Epidemiol. Biomarkers Prev. 10:955-960(2001) [PubMed: 11535547] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Identification of a novel human Rad51 variant that promotes DNA strand exchange." Park J.Y., Yoo H.W., Kim B.R., Park R., Choi S.Y., Kim Y. Nucleic Acids Res. 36:3226-3234(2008) [PubMed: 18417535] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION OF ISOFORMS 1 AND 3, TISSUE SPECIFICITY (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), MUTAGENESIS (ISOFORM 3).
[6]	NIEHS SNPs program Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[8]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed: 16572171] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Placenta.
[11]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[12]	"Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA." Benson F.E., Stasiak A., West S.C. EMBO J. 13:5764-5771(1994) [PubMed: 7988572] [Abstract] Cited for: CHARACTERIZATION.
[13]	"Interaction of human recombination proteins Rad51 and Rad54." Golub E.I., Kovalenko O.V., Gupta R.C., Ward D.C., Radding C.M. Nucleic Acids Res. 25:4106-4110(1997) [PubMed: 9321665] [Abstract] Cited for: INTERACTION WITH RAD54L.
[14]	"A novel nucleic acid-binding protein that interacts with human rad51 recombinase." Kovalenko O.V., Golub E.I., Bray-Ward P., Ward D.C., Radding C.M. Nucleic Acids Res. 25:4946-4953(1997) [PubMed: 9396801] [Abstract] Cited for: INTERACTION WITH RAD51AP1.
[15]	"RAB22 and RAB163/mouse BRCA2: proteins that specifically interact with the RAD51 protein." Mizuta R., LaSalle J.M., Cheng H.-L., Shinohara A., Ogawa H., Copeland N.G., Jenkins N.A., Lalande M., Alt F.W. Proc. Natl. Acad. Sci. U.S.A. 94:6927-6932(1997) [PubMed: 9192668] [Abstract] Cited for: INTERACTION WITH RAD51AP1, SUBCELLULAR LOCATION.
[16]	"Regulation of Rad51 function by c-Abl in response to DNA damage." Yuan Z.M., Huang Y., Ishiko T., Nakada S., Utsugisawa T., Kharbanda S., Wang R., Sung P., Shinohara A., Weichselbaum R., Kufe D. J. Biol. Chem. 273:3799-3802(1998) [PubMed: 9461559] [Abstract] Cited for: INTERACTION WITH ABL1, PHOSPHORYLATION AT TYR-54.
[17]	"A novel human Rad54 homologue, Rad54B, associates with Rad51." Tanaka K., Hiramoto T., Fukuda T., Miyagawa K. J. Biol. Chem. 275:26316-26321(2000) [PubMed: 10851248] [Abstract] Cited for: INTERACTION WITH RAD54B.
[18]	"Homologous DNA pairing by human recombination factors Rad51 and Rad54." Sigurdsson S., Van Komen S., Petukhova G., Sung P. J. Biol. Chem. 277:42790-42794(2002) [PubMed: 12205100] [Abstract] Cited for: FUNCTION.
[19]	"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: 11842113] [Abstract] Cited for: INTERACTION WITH XRCC3.
[20]	"Complex formation by the human Rad51B and Rad51C DNA repair proteins and their activities in vitro." Lio Y.-C., Mazin A.V., Kowalczykowski S.C., Chen D.J. J. Biol. Chem. 278:2469-2478(2003) [PubMed: 12427746] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH RAD51B AND RAD51C.
[21]	"Cellular localization of human Rad51C and regulation of ubiquitin-mediated proteolysis of Rad51." Bennett B.T., Knight K.L. J. Cell. Biochem. 96:1095-1109(2005) [PubMed: 16215984] [Abstract] Cited for: SUBCELLULAR LOCATION.
[22]	"The cell-cycle checkpoint kinase Chk1 is required for mammalian homologous recombination repair." Soerensen C.S., Hansen L.T., Dziegielewski J., Syljuaesen R.G., Lundin C., Bartek J., Helleday T. Nat. Cell Biol. 7:195-201(2005) [PubMed: 15665856] [Abstract] Cited for: INTERACTION WITH CHEK1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-309, MUTAGENESIS OF THR-309.
[23]	"RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51." Kovalenko O.V., Wiese C., Schild D. Nucleic Acids Res. 34:5081-5092(2006) [PubMed: 16990250] [Abstract] Cited for: INTERACTION WITH RAD51AP2.
[24]	"Single-stranded DNA-binding protein hSSB1 is critical for genomic stability." Richard D.J., Bolderson E., Cubeddu L., Wadsworth R.I.M., Savage K., Sharma G.G., Nicolette M.L., Tsvetanov S., McIlwraith M.J., Pandita R.K., Takeda S., Hay R.T., Gautier J., West S.C., Paull T.T., Pandita T.K., White M.F., Khanna K.K. Nature 453:677-681(2008) [PubMed: 18449195] [Abstract] Cited for: INTERACTION WITH OBFC2B.
[25]	"Cellular redistribution of Rad51 in response to DNA damage: novel role for Rad51C." Gildemeister O.S., Sage J.M., Knight K.L. J. Biol. Chem. 284:31945-31952(2009) [PubMed: 19783859] [Abstract] Cited for: SUBCELLULAR LOCATION.
[26]	"Discovery of a novel function for human Rad51: maintenance of the mitochondrial genome." Sage J.M., Gildemeister O.S., Knight K.L. J. Biol. Chem. 285:18984-18990(2010) [PubMed: 20413593] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
[27]	"Regulation of DNA Repair through DeSUMOylation and SUMOylation of Replication Protein A Complex." Dou H., Huang C., Singh M., Carpenter P.B., Yeh E.T. Mol. Cell 39:333-345(2010) [PubMed: 20705237] [Abstract] Cited for: INTERACTION WITH RPA1.
[28]	"A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination." Lee D.H., Pan Y., Kanner S., Sung P., Borowiec J.A., Chowdhury D. Nat. Struct. Mol. Biol. 17:365-372(2010) [PubMed: 20154705] [Abstract] Cited for: INTERACTION WITH RPA2, SUBCELLULAR LOCATION.
[29]	"Cooperation of breast cancer proteins PALB2 and piccolo BRCA2 in stimulating homologous recombination." Buisson R., Dion-Cote A.M., Coulombe Y., Launay H., Cai H., Stasiak A.Z., Stasiak A., Xia B., Masson J.Y. Nat. Struct. Mol. Biol. 17:1247-1254(2010) [PubMed: 20871615] [Abstract] Cited for: INTERACTION WITH PALB2.
[30]	"The role of human SWI5-MEI5 complex in homologous recombination repair." Yuan J., Chen J. J. Biol. Chem. 286:9888-9893(2011) [PubMed: 21252223] [Abstract] Cited for: INTERACTION WITH SWI5 AND SFR1.
[31]	"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: 21965664] [Abstract] Cited for: INTERACTION WITH SWSAP1.
[32]	"The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR." Aihara H., Ito Y., Kurumizaka H., Yokoyama S., Shibata T. J. Mol. Biol. 290:495-504(1999) [PubMed: 10390347] [Abstract] Cited for: STRUCTURE BY NMR OF 1-114.
[33]	"Identification of Rad51 alteration in patients with bilateral breast cancer." Kato M., Yano K., Matsuo F., Saito H., Katagiri T., Kurumizaka H., Yoshimoto M., Kasumi F., Akiyama F., Sakamoto G., Nagawa H., Nakamura Y., Miki Y. J. Hum. Genet. 45:133-137(2000) [PubMed: 10807537] [Abstract] Cited for: VARIANT BC GLN-150.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D13804 mRNA. Translation: BAA02962.1.
D14134 mRNA. Translation: BAA03189.1.
AF165094 , AF165088, AF165089, AF165090, AF165091, AF165092, AF165093 Genomic DNA. Translation: AAD49705.1.
AF233744 , AF233740, AF233741, AF233742, AF236021, AF233743 Genomic DNA. Translation: AAF69145.1.
EU362635 mRNA. Translation: ABY59731.1.
AY196785 Genomic DNA. Translation: AAN87149.1.
AK313503 mRNA. Translation: BAG36283.1.
CH471125 Genomic DNA. Translation: EAW92434.1.
BC001459 mRNA. Translation: AAH01459.1.
CR536559 mRNA. Translation: CAG38796.1.
AC012476 Genomic DNA. No translation available.
AC022405 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92432.1.

IPI

IPI00032201.
IPI00220649.
IPI01010370.

PIR

I58295.

RefSeq

NP_001157742.1. NM_001164270.1.
NP_002866.2. NM_002875.4.
NP_597994.3. NM_133487.3.

UniGene

Hs.631709.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B22	NMR	-	A	1-114	[»]
1N0W	X-ray	1.70	A	97-339	[»]

ProteinModelPortal

Q06609.

SMR

Q06609. Positions 16-339.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-462N.

IntAct

Q06609. 24 interactions.

MINT

MINT-1374477.

STRING

Q06609.

PTM databases

PhosphoSite

Q06609.

Polymorphism databases

DMDM

548663.

Proteomic databases

PRIDE

Q06609.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000267868; ENSP00000267868; ENSG00000051180.
ENST00000423169; ENSP00000406602; ENSG00000051180.

GeneID

5888.

KEGG

hsa:5888.

UCSC

uc001zmi.2. human.
uc010bbv.1. human.

Organism-specific databases

CTD

5888.

GeneCards

GC15P040987.

H-InvDB

HIX0012136.

HGNC

HGNC:9817. RAD51.

HPA

CAB010381.

MIM

114480. phenotype.
179617. gene.

neXtProt

NX_Q06609.

Orphanet

145. Hereditary breast and ovarian cancer syndrome.

PharmGKB

PA34176.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06903.

HOVERGEN

HBG001504.

OMA

SAMMAES.

OrthoDB

EOG47H5QB.

PhylomeDB

Q06609.

Enzyme and pathway databases

Pathway_Interaction_DB

bard1pathway. BARD1 signaling events.

Reactome

REACT_111183. Meiosis.
REACT_216. DNA Repair.

Gene expression databases

ArrayExpress

Q06609.

Bgee

Q06609.

CleanEx

HS_RAD51.

Genevestigator

Q06609.

GermOnline

ENSG00000051180. Homo sapiens.

Family and domain databases

InterPro

IPR003593. ATPase_AAA+_core.
IPR011941. DNA_recomb/repair_Rad51.
IPR013632. DNA_recomb/repair_Rad51_C.
IPR016467. DNA_recomb/repair_RecA-like.
IPR020588. DNA_recomb_RecA/RadB_ATP-bd.
IPR010995. DNA_repair_Rad51/TF_NusA_a-hlx.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]

KO

K04482.

PANTHER

PTHR22942:SF12. PTHR22942:SF12. 1 hit.

Pfam

PF08423. Rad51. 1 hit.
[Graphical view]

PIRSF

PIRSF005856. Rad51. 1 hit.

SMART

SM00382. AAA. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]

SUPFAM

SSF47794. Rad51_N. 1 hit.

TIGRFAMs

TIGR02239. Recomb_RAD51. 1 hit.

PROSITE

PS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

22896.

PMAP-CutDB

Q06609.

SOURCE

Search...

Entry information

Entry name

RAD51_HUMAN

Accession

Primary (citable) accession number: Q06609
Secondary accession number(s): B0FXP0 , B2R8T6, Q6FHX9, Q9BV60

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	January 25, 2012
This is version 137 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.