RAD52

From Wikipedia, the free encyclopedia

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
Cellular component	• nucleus • nucleoplasm
Biological process	• double-strand break repair via homologous recombination • DNA recombinase assembly • DNA repair • double-strand break repair • mitotic recombination • reciprocal meiotic 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]

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. Cite uses deprecated parameters (help)

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.
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. 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

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