RAD52

RAD52 homolog (S. cerevisiae)
File:PBB Protein RAD52 image.jpg PDB rendering based on 1h2i.
Available structures PDB List of PDB id codes 1h2i​, 1kn0​
Identifiers
Symbols	RAD52 ;
External IDs	Template:OMIM5
Gene ontology Molecular function Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE RAD52 205647 at tn.png
File:PBB GE RAD52 210630 s at tn.png
File:PBB GE RAD52 211904 x at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

RAD52 homolog (S. cerevisiae), also known as RAD52, is a human gene.

The protein encoded by this gene shares similarity with Saccharomyces cerevisiae Rad52, a protein important for DNA double-strand break repair and homologous recombination. This gene product was shown to bind single-stranded DNA ends, and mediate the DNA-DNA interaction necessary for the annealing of complementary DNA strands. It was also found to interact with DNA recombination protein RAD51, which suggested its role in RAD51 related DNA recombination and repair.

Further reading

• Muris DF, Bezzubova O, Buerstedde JM; et al. (1994). "Cloning of human and mouse genes homologous to RAD52, a yeast gene involved in DNA repair and recombination". Mutat. Res. 315 (3): 295–305. PMID 7526206.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Shen Z, Denison K, Lobb R; et al. (1995). "The human and mouse homologs of the yeast RAD52 gene: cDNA cloning, sequence analysis, assignment to human chromosome 12p12.2-p13, and mRNA expression in mouse tissues". Genomics. 25 (1): 199–206. PMID 7774919.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Park MS (1995). "Expression of human RAD52 confers resistance to ionizing radiation in mammalian cells". J. Biol. Chem. 270 (26): 15467–70. PMID 7797537.
• Shen Z, Pardington-Purtymun PE, Comeaux JC; et al. (1997). "UBL1, a human ubiquitin-like protein associating with human RAD51/RAD52 proteins". Genomics. 36 (2): 271–9. doi:10.1006/geno.1996.0462. PMID 8812453.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Shen Z, Pardington-Purtymun PE, Comeaux JC; et al. (1997). "Associations of UBE2I with RAD52, UBL1, p53, and RAD51 proteins in a yeast two-hybrid system". Genomics. 37 (2): 183–6. doi:10.1006/geno.1996.0540. PMID 8921390.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Chen G, Yuan SS, Liu W; et al. (1999). "Radiation-induced assembly of Rad51 and Rad52 recombination complex requires ATM and c-Abl". J. Biol. Chem. 274 (18): 12748–52. PMID 10212258.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kito K, Wada H, Yeh ET, Kamitani T (2000). "Identification of novel isoforms of human RAD52". Biochim. Biophys. Acta. 1489 (2–3): 303–14. PMID 10673031.CS1 maint: Multiple names: authors list (link)
• Stasiak AZ, Larquet E, Stasiak A; et al. (2000). "The human Rad52 protein exists as a heptameric ring". Curr. Biol. 10 (6): 337–40. PMID 10744977.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Parsons CA, Baumann P, Van Dyck E, West SC (2000). "Precise binding of single-stranded DNA termini by human RAD52 protein". EMBO J. 19 (15): 4175–81. doi:10.1093/emboj/19.15.4175. PMID 10921897.CS1 maint: Multiple names: authors list (link)
• Mer G, Bochkarev A, Gupta R; et al. (2000). "Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA". Cell. 103 (3): 449–56. PMID 11081631.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ranatunga W, Jackson D, Flowers II RA, Borgstahl GE (2001). "Human RAD52 protein has extreme thermal stability". Biochemistry. 40 (29): 8557–62. PMID 11456495.CS1 maint: Multiple names: authors list (link)
• Van Dyck E, Stasiak AZ, Stasiak A, West SC (2002). "Visualization of recombination intermediates produced by RAD52-mediated single-strand annealing". EMBO Rep. 2 (10): 905–9. doi:10.1093/embo-reports/kve201. PMID 11571269.CS1 maint: Multiple names: authors list (link)
• Kim PM, Allen C, Wagener BM; et al. (2001). "Overexpression of human RAD51 and RAD52 reduces double-strand break-induced homologous recombination in mammalian cells". Nucleic Acids Res. 29 (21): 4352–60. PMID 11691922.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yáñez RJ, Porter AC (2002). "Differential effects of Rad52p overexpression on gene targeting and extrachromosomal homologous recombination in a human cell line". Nucleic Acids Res. 30 (3): 740–8. PMID 11809887.
• Jackson D, Dhar K, Wahl JK; et al. (2002). "Analysis of the human replication protein A:Rad52 complex: evidence for crosstalk between RPA32, RPA70, Rad52 and DNA". J. Mol. Biol. 321 (1): 133–48. PMID 12139939.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kagawa W, Kurumizaka H, Ishitani R; et al. (2002). "Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form". Mol. Cell. 10 (2): 359–71. PMID 12191481.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Singleton MR, Wentzell LM, Liu Y; et al. (2002). "Structure of the single-strand annealing domain of human RAD52 protein". Proc. Natl. Acad. Sci. U.S.A. 99 (21): 13492–7. doi:10.1073/pnas.212449899. PMID 12370410.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Liu J, Meng X, Shen Z (2002). "Association of human RAD52 protein with transcription factors". Biochem. Biophys. Res. Commun. 297 (5): 1191–6. PMID 12372413.CS1 maint: Multiple names: authors list (link)
• Han J, Hankinson SE, De Vivo I; et al. (2002). "No association between a stop codon polymorphism in RAD52 and breast cancer risk". Cancer Epidemiol. Biomarkers Prev. 11 (10 Pt 1): 1138–9. PMID 12376524.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kitao H, Yuan ZM (2003). "Regulation of ionizing radiation-induced Rad52 nuclear foci formation by c-Abl-mediated phosphorylation". J. Biol. Chem. 277 (50): 48944–8. doi:10.1074/jbc.M208151200. PMID 12379650.