RAD52

RAD52 homolog (S. cerevisiae)

PDB rendering based on 1h2i.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1H2I, 1KN0

Identifiers

External IDs

OMIM: 600392 HomoloGene: 31118 GeneCards: RAD52 Gene

Gene ontology
Molecular function	• DNA binding • protein binding • identical protein binding
Cellular component	• nucleus • nucleoplasm
Biological process	• double-strand break repair via homologous recombination • DNA recombinase assembly • DNA repair • double-strand break repair • DNA recombination
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

ENSG00000002016

ENSMUSG00000030166

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 12:
1.02 – 1.1 Mb

Chr 6:
119.9 – 119.92 Mb

PubMed search

RAD52 homolog (S. cerevisiae), also known as RAD52, is a protein which in humans is encoded by the RAD52 gene.^[1]^[2]

Function

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.^[2]

Interactions

RAD52 has been shown to interact with RAD51.^[3] The Rad52 will ease the loading of Rad51 on ssDNA by interfering with the RPA protein.

References

↑ Shen Z, Denison K, Lobb R, Gatewood JM, Chen DJ (January 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. doi:10.1016/0888-7543(95)80126-7. PMID 7774919.
↑ 2.0 2.1 "Entrez Gene: RAD52 RAD52 homolog (S. cerevisiae)".
↑ Chen, G; Yuan S S, Liu W, Xu Y, Trujillo K, Song B, Cong F, Goff S P, Wu Y, Arlinghaus R, Baltimore D, Gasser P J, Park M S, Sung P, Lee E Y (Apr 1999). "Radiation-induced assembly of Rad51 and Rad52 recombination complex requires ATM and c-Abl". J. Biol. Chem. (UNITED STATES) 274 (18): 12748–52. doi:10.1074/jbc.274.18.12748. ISSN 0021-9258. PMID 10212258.

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. doi:10.1016/0921-8777(94)90040-x. PMID 7526206.
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. doi:10.1016/0888-7543(95)80126-7. PMID 7774919.
Park MS (1995). "Expression of human RAD52 confers resistance to ionizing radiation in mammalian cells.". J. Biol. Chem. 270 (26): 15467–70. doi:10.1074/jbc.270.26.15467. 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.
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.
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. doi:10.1074/jbc.274.18.12748. PMID 10212258.
Kito K, Wada H, Yeh ET, Kamitani T (2000). "Identification of novel isoforms of human RAD52.". Biochim. Biophys. Acta 1489 (2–3): 303–14. doi:10.1016/s0167-4781(99)00214-6. PMID 10673031.
Stasiak AZ, Larquet E, Stasiak A et al. (2000). "The human Rad52 protein exists as a heptameric ring". Curr. Biol. 10 (6): 337–40. doi:10.1016/S0960-9822(00)00385-7. PMID 10744977.
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. PMC 306603. PMID 10921897.
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. doi:10.1016/S0092-8674(00)00136-7. PMID 11081631.
Ranatunga W, Jackson D, Flowers II RA, Borgstahl GE (2001). "Human RAD52 protein has extreme thermal stability". Biochemistry 40 (29): 8557–62. doi:10.1021/bi0155089. PMID 11456495.
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. PMC 1084079. PMID 11571269.
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. doi:10.1093/nar/29.21.4352. PMC 60192. PMID 11691922.
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. doi:10.1093/nar/30.3.740. PMC 100286. 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. doi:10.1016/S0022-2836(02)00541-7. PMID 12139939.
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. doi:10.1016/S1097-2765(02)00587-7. PMID 12191481.
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. PMC 129701. PMID 12370410.
Liu J, Meng X, Shen Z (2002). "Association of human RAD52 protein with transcription factors". Biochem. Biophys. Res. Commun. 297 (5): 1191–6. doi:10.1016/S0006-291X(02)02353-7. PMID 12372413.
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.
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.

PDB gallery

1h2i: HUMAN RAD52 PROTEIN, N-TERMINAL DOMAIN

1kn0: Crystal Structure of the human Rad52 protein