RAD52

RAD52 homolog, DNA repair protein

PDB rendering based on 1h2i.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1H2I, 1KN0

Identifiers

Symbol

RAD52

External IDs

OMIM: 600392 HomoloGene: 31118 GeneCards: RAD52 Gene

Gene ontology
Molecular function	• DNA binding • damaged DNA binding • protein binding • identical protein binding
Cellular component	• nucleus • nucleoplasm • protein complex
Biological process	• double-strand break repair via homologous recombination • DNA recombinase assembly • DNA repair • double-strand break repair • DNA recombination • mitotic recombination • cellular response to DNA damage stimulus • DNA double-strand break processing involved in repair via single-strand annealing • protein sumoylation • cellular response to oxidative stress • post-translational protein modification • cellular protein metabolic process • regulation of nucleotide-excision repair
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 12:
0.91 – 0.99 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 (Jan 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.
1 2 "Entrez Gene: RAD52 RAD52 homolog (S. cerevisiae)".
↑ Chen G, Yuan SS, Liu W, Xu Y, Trujillo K, Song B, Cong F, Goff SP, Wu Y, Arlinghaus R, Baltimore D, Gasser PJ, Park MS, Sung P, Lee EY (Apr 1999). "Radiation-induced assembly of Rad51 and Rad52 recombination complex requires ATM and c-Abl". The Journal of Biological Chemistry 274 (18): 12748–52. doi:10.1074/jbc.274.18.12748. PMID 10212258.

Muris DF, Bezzubova O, Buerstedde JM, Vreeken K, Balajee AS, Osgood CJ, Troelstra C, Hoeijmakers JH, Ostermann K, Schmidt H (Nov 1994). "Cloning of human and mouse genes homologous to RAD52, a yeast gene involved in DNA repair and recombination". Mutation Research 315 (3): 295–305. doi:10.1016/0921-8777(94)90040-x. PMID 7526206.
Shen Z, Denison K, Lobb R, Gatewood JM, Chen DJ (Jan 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 (Jun 1995). "Expression of human RAD52 confers resistance to ionizing radiation in mammalian cells". The Journal of Biological Chemistry 270 (26): 15467–70. doi:10.1074/jbc.270.26.15467. PMID 7797537.
Shen Z, Pardington-Purtymun PE, Comeaux JC, Moyzis RK, Chen DJ (Sep 1996). "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, Moyzis RK, Chen DJ (Oct 1996). "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, Xu Y, Trujillo K, Song B, Cong F, Goff SP, Wu Y, Arlinghaus R, Baltimore D, Gasser PJ, Park MS, Sung P, Lee EY (Apr 1999). "Radiation-induced assembly of Rad51 and Rad52 recombination complex requires ATM and c-Abl". The Journal of Biological Chemistry 274 (18): 12748–52. doi:10.1074/jbc.274.18.12748. PMID 10212258.
Kito K, Wada H, Yeh ET, Kamitani T (Dec 1999). "Identification of novel isoforms of human RAD52". Biochimica Et Biophysica Acta 1489 (2-3): 303–14. doi:10.1016/s0167-4781(99)00214-6. PMID 10673031.
Stasiak AZ, Larquet E, Stasiak A, Müller S, Engel A, Van Dyck E, West SC, Egelman EH (Mar 2000). "The human Rad52 protein exists as a heptameric ring". Current Biology 10 (6): 337–40. doi:10.1016/S0960-9822(00)00385-7. PMID 10744977.
Parsons CA, Baumann P, Van Dyck E, West SC (Aug 2000). "Precise binding of single-stranded DNA termini by human RAD52 protein". The EMBO Journal 19 (15): 4175–81. doi:10.1093/emboj/19.15.4175. PMC 306603. PMID 10921897.
Mer G, Bochkarev A, Gupta R, Bochkareva E, Frappier L, Ingles CJ, Edwards AM, Chazin WJ (Oct 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 (Jul 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 (Oct 2001). "Visualization of recombination intermediates produced by RAD52-mediated single-strand annealing". EMBO Reports 2 (10): 905–9. doi:10.1093/embo-reports/kve201. PMC 1084079. PMID 11571269.
Kim PM, Allen C, Wagener BM, Shen Z, Nickoloff JA (Nov 2001). "Overexpression of human RAD51 and RAD52 reduces double-strand break-induced homologous recombination in mammalian cells". Nucleic Acids Research 29 (21): 4352–60. doi:10.1093/nar/29.21.4352. PMC 60192. PMID 11691922.
Yáñez RJ, Porter AC (Feb 2002). "Differential effects of Rad52p overexpression on gene targeting and extrachromosomal homologous recombination in a human cell line". Nucleic Acids Research 30 (3): 740–8. doi:10.1093/nar/30.3.740. PMC 100286. PMID 11809887.
Jackson D, Dhar K, Wahl JK, Wold MS, Borgstahl GE (Aug 2002). "Analysis of the human replication protein A:Rad52 complex: evidence for crosstalk between RPA32, RPA70, Rad52 and DNA". Journal of Molecular Biology 321 (1): 133–48. doi:10.1016/S0022-2836(02)00541-7. PMID 12139939.
Kagawa W, Kurumizaka H, Ishitani R, Fukai S, Nureki O, Shibata T, Yokoyama S (Aug 2002). "Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form". Molecular Cell 10 (2): 359–71. doi:10.1016/S1097-2765(02)00587-7. PMID 12191481.
Singleton MR, Wentzell LM, Liu Y, West SC, Wigley DB (Oct 2002). "Structure of the single-strand annealing domain of human RAD52 protein". Proceedings of the National Academy of Sciences of the United States of America 99 (21): 13492–7. doi:10.1073/pnas.212449899. PMC 129701. PMID 12370410.
Liu J, Meng X, Shen Z (Oct 2002). "Association of human RAD52 protein with transcription factors". Biochemical and Biophysical Research Communications 297 (5): 1191–6. doi:10.1016/S0006-291X(02)02353-7. PMID 12372413.
Han J, Hankinson SE, De Vivo I, Colditz GA, Hunter DJ (Oct 2002). "No association between a stop codon polymorphism in RAD52 and breast cancer risk". Cancer Epidemiology, Biomarkers & Prevention 11 (10 Pt 1): 1138–9. PMID 12376524.
Kitao H, Yuan ZM (Dec 2002). "Regulation of ionizing radiation-induced Rad52 nuclear foci formation by c-Abl-mediated phosphorylation". The Journal of Biological Chemistry 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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RAD52

Function

Interactions

References

Further reading