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Q06609 (RAD51_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates 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. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. 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 Ref.27 Ref.29 Ref.39 Ref.40 Ref.42

Subunit structure

Forms linear homooligomers, giving rise to a RAD51 nucleoprotein filament, which is essential for strand-pairing reactions during DNA recombination. Interacts with BRCA1 and either directly or indirectly with p53. Interacts with XRCC3, RAD54L and RAD54B. Interacts with the BCDX2 subcomplex RAD51C:RAD51B. Interacts directly with PALB2 which may serve as a scaffold for a HR complex containing PALB2, BRCA2, RAD51C, RAD51 and XRCC3. Interacts with RAD51AP1 and RAD51AP2. Interacts with CHEK1, and this may require prior phosphorylation of CHEK1. Interacts with the MND1-PSMC3IP heterodimer. Found in a complex, at least composed of BLM, RAD51 and SPIDR; the complex formation is mediated by SPIDR. Interacts with SPIDR; the interaction is direct and recruits RAD51 to DNA damage sites. Interacts with FIGNL1 (via N-terminus one-half region); the interaction is direct. Interacts with RAD51AP1 (via C-terminus region); the interaction is direct. Interacts with NABP2, 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. Interacts with PARPBP, BRCA2 and RECQL5; these interactions interfere with the formation of the RAD51-DNA homologous recombination structure. Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31 Ref.33 Ref.34 Ref.36 Ref.38 Ref.39 Ref.40 Ref.42

Subcellular location

Nucleus. Cytoplasm. Cytoplasmperinuclear region. Mitochondrion matrix. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage. DNA damage induces an increase in nuclear levels. Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a SPIDR-dependent manner. Ref.5 Ref.15 Ref.21 Ref.22 Ref.25 Ref.27 Ref.30 Ref.32 Ref.39 Ref.40 Ref.42

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.27

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

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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.43

Mirror movements 2 (MRMV2) [MIM:614508]: A disorder characterized by contralateral involuntary movements that mirror voluntary ones. While mirror movements are occasionally found in young children, persistence beyond the age of 10 is abnormal. Mirror movements occur more commonly in the upper extremities.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.35

Sequence similarities

Belongs to the RecA family. RAD51 subfamily.

Contains 1 HhH domain.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
   Cellular componentCytoplasm
Cytoskeleton
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   LigandATP-binding
DNA-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.12PubMed 8929543. Source: GOC

DNA recombinase assembly

Traceable author statement. Source: Reactome

DNA recombination

Traceable author statement Ref.12. Source: UniProtKB

DNA repair

Traceable author statement. Source: Reactome

DNA unwinding involved in DNA replication

Inferred from direct assay Ref.12. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from direct assay Ref.40. Source: UniProtKB

cellular response to camptothecin

Inferred from direct assay Ref.40. Source: UniProtKB

cellular response to ionizing radiation

Inferred from direct assay Ref.40Ref.39. Source: UniProtKB

double-strand break repair

Traceable author statement. Source: Reactome

double-strand break repair via homologous recombination

Inferred from mutant phenotype Ref.40. Source: UniProtKB

meiotic nuclear division

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic recombination

Traceable author statement Ref.1. Source: ProtInc

positive regulation of DNA ligation

Inferred from direct assay PubMed 8929543. Source: UniProtKB

protein homooligomerization

Inferred from physical interaction Ref.42. Source: UniProtKB

reciprocal meiotic recombination

Traceable author statement Ref.1. Source: ProtInc

regulation of double-strand break repair via homologous recombination

Inferred from direct assay Ref.39. Source: UniProtKB

   Cellular_componentPML body

Inferred from direct assay PubMed 11309417. Source: UniProtKB

condensed chromosome

Inferred from sequence or structural similarity. Source: UniProtKB

condensed nuclear chromosome

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.21. Source: UniProtKB

lateral element

Inferred from electronic annotation. Source: Ensembl

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay Ref.27. Source: UniProtKB

nuclear chromosome

Inferred from direct assay Ref.39. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.42Ref.21Ref.5. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.21. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay PubMed 16428451. Source: MGI

DNA polymerase binding

Inferred from physical interaction PubMed 19995904. Source: UniProt

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 Ref.42Ref.14. Source: IntAct

protein C-terminus binding

Inferred from physical interaction PubMed 17515903. 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.12PubMed 8929543. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 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.
Isoform 4 (identifier: Q06609-4)

The sequence of this isoform differs from the canonical sequence as follows:
     76-114: AEAAKLVPMG...GSKELDKLLQ → TESRSVARLE...ASASRVVGTT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.37
Chain2 – 339338DNA repair protein RAD51 homolog 1
PRO_0000122932

Regions

Domain48 – 7730HhH
Nucleotide binding127 – 1348ATP By similarity
Region184 – 25774Interaction with PALB2

Amino acid modifications

Modified residue21N-acetylalanine Ref.37
Modified residue541Phosphotyrosine; by ABL1 Ref.16
Modified residue3091Phosphothreonine; by CHEK1 Ref.22

Natural variations

Alternative sequence76 – 11439AEAAK…DKLLQ → TESRSVARLECNSVILVYCT LRLSGSSDSPASASRVVGTT in isoform 4.
VSP_043655
Alternative sequence77 – 17397Missing in isoform 2.
VSP_005556
Alternative sequence259 – 28426FGVAV…AADPK → IVSEERKRGNQNLQNLRLSL SS in isoform 3.
VSP_041724
Alternative sequence285 – 33955Missing in isoform 3.
VSP_041725
Natural variant1501R → Q in BC; familial. Ref.43
Corresponds to variant rs121917739 [ dbSNP | Ensembl ].
VAR_010899

Experimental info

Mutagenesis861F → A: Loss of homooligomerization. Ref.42
Mutagenesis891A → E: Loss of homooligomerization. Ref.42
Mutagenesis3091T → A: Confers hypersensitivity to hydroxyurea. Ref.22
Sequence conflict3131K → Q in BAA02962. Ref.1

Secondary structure

................................................. 339
Helix Strand Turn

Details...

Sequences

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

Last modified June 1, 1994. Version 1.
Checksum: 26578E6206DEDEDA

FASTA33936,966
        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 

« Hide

Isoform 2 [UniParc].

Checksum: DFA9E12DC8429CA2
Show »

FASTA24226,351
Isoform 3 [UniParc].

Checksum: 1DFA22F6C0926FC2
Show »

FASTA28031,001
Isoform 4 [UniParc].

Checksum: D8E2AAD35400FB04
Show »

FASTA34036,780

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. 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] (ISOFORMS 1 AND 4).
Tissue: Brain.
[8]"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).
[9]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"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 2).
Tissue: Placenta.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: INTERACTION 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NABP2.
[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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[26]"Physical interaction of RECQ5 helicase with RAD51 facilitates its anti-recombinase activity."
Schwendener S., Raynard S., Paliwal S., Cheng A., Kanagaraj R., Shevelev I., Stark J.M., Sung P., Janscak P.
J. Biol. Chem. 285:15739-15745(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RECQL5, FUNCTION.
[27]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
[28]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RPA1.
[29]"RecQL5 promotes genome stabilization through two parallel mechanisms--interacting with RNA polymerase II and acting as a helicase."
Islam M.N., Fox D. III, Guo R., Enomoto T., Wang W.
Mol. Cell. Biol. 30:2460-2472(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RECQL5, FUNCTION.
[30]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RPA2, SUBCELLULAR LOCATION.
[31]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PALB2.
[32]"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.
[33]"The role of human SWI5-MEI5 complex in homologous recombination repair."
Yuan J., Chen J.
J. Biol. Chem. 286:9888-9893(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SWI5 AND SFR1.
[34]"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.
[35]"RAD51 haploinsufficiency causes congenital mirror movements in humans."
Depienne C., Bouteiller D., Meneret A., Billot S., Groppa S., Klebe S., Charbonnier-Beaupel F., Corvol J.C., Saraiva J.P., Brueggemann N., Bhatia K., Cincotta M., Brochard V., Flamand-Roze C., Carpentier W., Meunier S., Marie Y., Gaussen M. expand/collapse author list , Stevanin G., Wehrle R., Vidailhet M., Klein C., Dusart I., Brice A., Roze E.
Am. J. Hum. Genet. 90:301-307(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MRMV2.
[36]"Inhibition of homologous recombination by the PCNA-interacting protein PARI."
Moldovan G.L., Dejsuphong D., Petalcorin M.I., Hofmann K., Takeda S., Boulton S.J., D'Andrea A.D.
Mol. Cell 45:75-86(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARPBP.
[37]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[38]"Breast cancer-associated missense mutants of the PALB2 WD40 domain, which directly binds RAD51C, RAD51 and BRCA2, disrupt DNA repair."
Park J.Y., Singh T.R., Nassar N., Zhang F., Freund M., Hanenberg H., Meetei A.R., Andreassen P.R.
Oncogene 0:0-0(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PALB2, IDENTIFICATION IN A PALB2-CONTAINING HR COMPLEX.
[39]"FIGNL1-containing protein complex is required for efficient homologous recombination repair."
Yuan J., Chen J.
Proc. Natl. Acad. Sci. U.S.A. 110:10640-10645(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FIGNL1; RAD51AP1 AND SWI5, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[40]"Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase with homologous recombination repair."
Wan L., Han J., Liu T., Dong S., Xie F., Chen H., Huang J.
Proc. Natl. Acad. Sci. U.S.A. 110:10646-10651(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH BLM AND SPIDR, INTERACTION WITH SPIDR, SUBCELLULAR LOCATION.
[41]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-114.
[42]"Insights into DNA recombination from the structure of a RAD51-BRCA2 complex."
Pellegrini L., Yu D.S., Lo T., Anand S., Lee M., Blundell T.L., Venkitaraman A.R.
Nature 420:287-293(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 97-339 IN COMPLEX WITH BRCA2, FUNCTION, SUBUNIT, MUTAGENESIS OF PHE-86 AND ALA-89, SUBCELLULAR LOCATION, INTERACTION WITH BRCA2.
[43]"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] [Europe PMC] [Abstract]
Cited for: VARIANT BC GLN-150.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13804 mRNA. Translation: BAA02962.1.
D14134 mRNA. Translation: BAA03189.1.
AF165094 expand/collapse EMBL AC list , AF165088, AF165089, AF165090, AF165091, AF165092, AF165093 Genomic DNA. Translation: AAD49705.1.
AF233744 expand/collapse EMBL AC list , AF233740, AF233741, AF233742, AF236021, AF233743 Genomic DNA. Translation: AAF69145.1.
EU362635 mRNA. Translation: ABY59731.1.
AY196785 Genomic DNA. Translation: AAN87149.1.
AK131299 mRNA. Translation: BAD18467.1.
AK291969 mRNA. Translation: BAF84658.1.
AK313503 mRNA. Translation: BAG36283.1.
CR536559 mRNA. Translation: CAG38796.1.
AC012476 Genomic DNA. No translation available.
AC022405 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92434.1.
CH471125 Genomic DNA. Translation: EAW92432.1.
CH471125 Genomic DNA. Translation: EAW92435.1.
BC001459 mRNA. Translation: AAH01459.1.
PIRI58295.
RefSeqNP_001157741.1. NM_001164269.1.
NP_001157742.1. NM_001164270.1.
NP_002866.2. NM_002875.4.
NP_597994.3. NM_133487.3.
UniGeneHs.631709.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B22NMR-A1-114[»]
1N0WX-ray1.70A97-339[»]
ProteinModelPortalQ06609.
SMRQ06609. Positions 16-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111825. 60 interactions.
DIPDIP-462N.
IntActQ06609. 31 interactions.
MINTMINT-1374477.
STRING9606.ENSP00000267868.

Chemistry

BindingDBQ06609.
ChEMBLCHEMBL2034807.

PTM databases

PhosphoSiteQ06609.

Polymorphism databases

DMDM548663.

Proteomic databases

PaxDbQ06609.
PRIDEQ06609.

Protocols and materials databases

DNASU5888.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000267868; ENSP00000267868; ENSG00000051180. [Q06609-1]
ENST00000382643; ENSP00000372088; ENSG00000051180. [Q06609-4]
ENST00000423169; ENSP00000406602; ENSG00000051180. [Q06609-3]
ENST00000532743; ENSP00000433924; ENSG00000051180. [Q06609-4]
ENST00000557850; ENSP00000454176; ENSG00000051180. [Q06609-2]
GeneID5888.
KEGGhsa:5888.
UCSCuc001zmi.4. human. [Q06609-1]
uc001zml.4. human. [Q06609-4]
uc010bbw.3. human. [Q06609-3]

Organism-specific databases

CTD5888.
GeneCardsGC15P040987.
HGNCHGNC:9817. RAD51.
HPACAB010381.
HPA039310.
MIM114480. phenotype.
179617. gene.
614508. phenotype.
neXtProtNX_Q06609.
Orphanet238722. Familial congenital mirror movements.
145. Hereditary breast and ovarian cancer syndrome.
PharmGKBPA34176.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0468.
HOGENOMHOG000227426.
HOVERGENHBG001504.
KOK04482.
OMAMMAESRY.
PhylomeDBQ06609.
TreeFamTF101218.

Enzyme and pathway databases

ReactomeREACT_111183. Meiosis.
REACT_216. DNA Repair.
SignaLinkQ06609.

Gene expression databases

ArrayExpressQ06609.
BgeeQ06609.
CleanExHS_RAD51.
GenevestigatorQ06609.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR011941. DNA_recomb/repair_Rad51.
IPR013632. DNA_recomb/repair_Rad51_C.
IPR016467. DNA_recomb/repair_RecA-like.
IPR010995. DNA_repair_Rad51/TF_NusA_a-hlx.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]
PANTHERPTHR22942:SF12. PTHR22942:SF12. 1 hit.
PfamPF08423. Rad51. 1 hit.
[Graphical view]
PIRSFPIRSF005856. Rad51. 1 hit.
SMARTSM00382. AAA. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMSSF47794. SSF47794. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR02239. recomb_RAD51. 1 hit.
PROSITEPS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAD51. human.
EvolutionaryTraceQ06609.
GeneWikiRAD51.
GenomeRNAi5888.
NextBio22896.
PMAP-CutDBQ06609.
PROQ06609.
SOURCESearch...

Entry information

Entry nameRAD51_HUMAN
AccessionPrimary (citable) accession number: Q06609
Secondary accession number(s): B0FXP0 expand/collapse secondary AC list , B2R8T6, Q6FHX9, Q6ZNA8, Q9BV60
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 161 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 15

Human chromosome 15: entries, gene names and cross-references to MIM