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RAD51 recombinase
A filament of Rad51 based on PDB: 1SZP .[1]
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols RAD51 ; BRCC5; HRAD51; HsRad51; HsT16930; MRMV2; RAD51A; RECA
External IDs OMIM179617 MGI97890 HomoloGene2155 GeneCards: RAD51 Gene
RNA expression pattern
PBB GE RAD51 205024 s at tn.png
PBB GE RAD51 205023 at tn.png
More reference expression data
Species Human Mouse
Entrez 5888 19361
Ensembl ENSG00000051180 ENSMUSG00000027323
UniProt Q06609 Q08297
RefSeq (mRNA) NM_001164269 NM_011234
RefSeq (protein) NP_001157741 NP_035364
Location (UCSC) Chr 15:
40.99 – 41.02 Mb
Chr 2:
119.11 – 119.15 Mb
PubMed search [1] [2]

RAD51 is a eukaryote gene. The protein encoded by this gene is a member of the RAD51 protein family which assist in repair of DNA double strand breaks. RAD51 family members are homologous to the bacterial RecA, Archaeal RadA and yeast Rad51.[2] The protein is highly conserved in most eukaryotes, from yeast to humans.[3]


Two alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported. Transcript variants utilizing alternative polyA signals exist.


In humans, RAD51 is a 339-amino acid protein that plays a major role in homologous recombination of DNA during double strand break repair. In this process, an ATP dependent DNA strand exchange takes place in which a template strand invades base-paired strands of homologous DNA molecules. RAD51 is involved in the search for homology and strand pairing stages of the process.

Unlike other proteins involved in DNA metabolism, the RecA/Rad51 family forms a helical nucleoprotein filament on DNA.[4]

This protein can interact with the ssDNA-binding protein RPA, BRCA2, PALB2[5] and RAD52.

The structural basis for Rad51 filament formation and its functional mechanism still remain poorly understood. However, recent studies using fluorescent labeled Rad51[6] has indicated that Rad51 fragments elongate via multiple nucleation events followed by growth, with the total fragment terminating when it reaches about 2 μm in length. Disassociation of Rad51 from dsDNA, however, is slow and incomplete, suggesting that there is a separate mechanism that accomplishes this.


This protein is also found to interact with PALB2[5] and BRCA2, which may be important for the cellular response to DNA damage. BRCA2 is shown to regulate both the intracellular localization and DNA-binding ability of this protein. Loss of these controls following BRCA2 inactivation may be a key event leading to genomic instability and tumorigenesis.[7]

The Rad51 gene is located on chromosome 15 and several alterations of the gene have been associated with an increased risk of developing breast cancer. The breast cancer susceptibility protein BRCA2 and PALB2 controls the function of Rad51 in the pathway for DNA repair by homologous recombination.[5][8] Increased RAD51 expression levels have been identified in metastatic canine mammary carcinoma, indicating that genomic instability plays an important role in the carcinogenesis of this tumor type.[9][10][11][12]


In mammals, seven recA-like genes have been identified: Rad51, Rad51L1/B, Rad51L2/C, Rad51L3/D, XRCC2, XRCC3, and DMC1/Lim15.[13] All of these proteins, with the exception of meiosis-specific DMC1, are essential for development in mammals. Rad51 is a member of the RecA-like NTPases.


RAD51 has been shown to interact with BRE,[14] RAD54,[15] RAD54B,[16] Ataxia telangiectasia mutated,[17] BRCC3,[14] BARD1,[14] BRCA2,[14][18][19][20][21][22][23][24][8][25][26][27][28] UBE2I,[29][30] Abl gene,[17] BRCA1,[14][27][31][32] RAD52,[17] DMC1,[33] P53[14][34][35] and Bloom syndrome protein.[36]


  1. ^ Conway AB, Lynch TW, Zhang Y, Fortin GS, Fung CW, Symington LS, Rice PA. (2004). "Crystal structure of a Rad51 filament". Nat Struct Mol Biol 11 (8): 791–6. doi:10.1038/nsmb795. PMID 15235592. 
  2. ^ Shinohara A., Ogawa H., & Ogawa T. (1992). "Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein". Cell 69 (3): 457–70. doi:10.1016/0092-8674(92)90447-K. PMID 1581961. 
  3. ^ Shinohara A., Ogawa H., Matsuda Y., Ushio N., Ikeo K. & Ogawa T. (1993). "Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA". Nature Genetics 4 (3): 239–243. doi:10.1038/ng0793-239. PMID 8358431. 
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  5. ^ a b c Buisson R, Dion-Côté A.M et al. (2010). "Cooperation of breast cancer proteins PALB2 and piccolo BRCA2 in stimulating homologous recombination.". Nature Structural & molecular biology 17 (10): 1247–54. doi:10.1038/nsmb.1915. PMID 20871615. 
  6. ^ Hilario J, Amitani I, Baskin RJ, Kowalczykowski SC (January 2009). "Direct imaging of human Rad51 nucleoprotein dynamics on individual DNA molecules". Proc. Natl. Acad. Sci. U.S.A. 106 (2): 361–8. doi:10.1073/pnas.0811965106. PMC 2613362. PMID 19122145. 
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