RPA2

From Wikipedia, the free encyclopedia

Replication protein A2, 32kDa

PDB rendering based on 1dpu.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1DPU, 1L1O, 1QUQ, 1Z1D, 2PI2, 2PQA, 2Z6K, 3KDF

Identifiers

Symbols

RPA2; REPA2; RPA32

External IDs

OMIM: 179836 MGI: 1339939 HomoloGene: 37712 GeneCards: RPA2 Gene

Gene Ontology
Molecular function	• single-stranded DNA binding • protein binding • protein phosphatase binding • protein N-terminus binding
Cellular component	• nucleus • nucleoplasm • DNA replication factor A complex • nucleolus • PML body
Biological process	• cell cycle checkpoint • G1/S transition of mitotic cell cycle • S phase of mitotic cell cycle • mitotic cell cycle • nucleotide-excision repair, DNA damage removal • telomere maintenance via recombination • telomere maintenance • double-strand break repair via homologous recombination • DNA recombinase assembly • DNA replication • DNA-dependent DNA replication • DNA strand elongation involved in DNA replication • DNA repair • transcription-coupled nucleotide-excision repair • nucleotide-excision repair • nucleotide-excision repair, DNA gap filling • double-strand break repair • regulation of double-strand break repair via homologous recombination • telomere maintenance via semi-conservative replication
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
28.22 – 28.24 Mb

Chr 4:
132.77 – 132.78 Mb

PubMed search

Replication protein A 32 kDa subunit is a protein that in humans is encoded by the RPA2 gene.^[1]^[2]

Interactions

RPA2 has been shown to interact with Ku70,^[3] Replication protein A1,^[3]^[4] RPA3,^[4]^[5] DNA-PKcs,^[3] STAT3,^[6] Cyclin O,^[7] MEN1,^[8] TP53BP1^[9] and Uracil-DNA glycosylase.^[10]

References

↑ Umbricht CB, Erdile LF, Jabs EW, Kelly TJ (April 1993). "Cloning, overexpression, and genomic mapping of the 14-kDa subunit of human replication protein A". J Biol Chem 268 (9): 6131–8. PMID 8454588.
↑ "Entrez Gene: RPA2 Replication protein A2, 32kDa".
↑ 3.0 3.1 3.2 Shao, R G; Cao C X, Zhang H, Kohn K W, Wold M S, Pommier Y (March 1999). "Replication-mediated DNA damage by camptothecin induces phosphorylation of RPA by DNA-dependent protein kinase and dissociates RPA:DNA-PK complexes". EMBO J. (ENGLAND) 18 (5): 1397–406. doi:10.1093/emboj/18.5.1397. ISSN 0261-4189. PMC 1171229. PMID 10064605. Cite uses deprecated parameters (help)
↑ 4.0 4.1 Bochkareva, Elena; Korolev Sergey, Lees-Miller Susan P, Bochkarev Alexey (April 2002). "Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA". EMBO J. (England) 21 (7): 1855–63. doi:10.1093/emboj/21.7.1855. ISSN 0261-4189. PMC 125950. PMID 11927569. Cite uses deprecated parameters (help)
↑ Bochkareva, E; Frappier L, Edwards A M, Bochkarev A (February 1998). "The RPA32 subunit of human replication protein A contains a single-stranded DNA-binding domain". J. Biol. Chem. (UNITED STATES) 273 (7): 3932–6. doi:10.1074/jbc.273.7.3932. ISSN 0021-9258. PMID 9461578. Cite uses deprecated parameters (help)
↑ Kim, J; Kim D, Chung J (2000). "Replication protein a 32 kDa subunit (RPA p32) binds the SH2 domain of STAT3 and regulates its transcriptional activity". Cell Biol. Int. (ENGLAND) 24 (7): 467–73. doi:10.1006/cbir.2000.0525. ISSN 1065-6995. PMID 10875894. Cite uses deprecated parameters (help)
↑ Otterlei, M; Warbrick E, Nagelhus T A, Haug T, Slupphaug G, Akbari M, Aas P A, Steinsbekk K, Bakke O, Krokan H E (July 1999). "Post-replicative base excision repair in replication foci". EMBO J. (ENGLAND) 18 (13): 3834–44. doi:10.1093/emboj/18.13.3834. ISSN 0261-4189. PMC 1171460. PMID 10393198. Cite uses deprecated parameters (help)
↑ Sukhodolets, Karen E; Hickman Alison B, Agarwal Sunita K, Sukhodolets Maxim V, Obungu Victor H, Novotny Elizabeth A, Crabtree Judy S, Chandrasekharappa Settara C, Collins Francis S, Spiegel Allen M, Burns A Lee, Marx Stephen J (January 2003). "The 32-kilodalton subunit of replication protein A interacts with menin, the product of the MEN1 tumor suppressor gene". Mol. Cell. Biol. (United States) 23 (2): 493–509. doi:10.1128/MCB.23.2.493-509.2003. ISSN 0270-7306. PMC 151531. PMID 12509449. Cite uses deprecated parameters (help)
↑ Yoo, Eunjae; Kim Byung U, Lee Seung Youn, Cho Chae Hyun, Chung Jay H, Lee Chang-Hun (August 2005). "53BP1 is associated with replication protein A and is required for RPA2 hyperphosphorylation following DNA damage". Oncogene (England) 24 (35): 5423–30. doi:10.1038/sj.onc.1208710. ISSN 0950-9232. PMID 15856006. Cite uses deprecated parameters (help)
↑ Nagelhus, T A; Haug T, Singh K K, Keshav K F, Skorpen F, Otterlei M, Bharati S, Lindmo T, Benichou S, Benarous R, Krokan H E (March 1997). "A sequence in the N-terminal region of human uracil-DNA glycosylase with homology to XPA interacts with the C-terminal part of the 34-kDa subunit of replication protein A". J. Biol. Chem. (UNITED STATES) 272 (10): 6561–6. doi:10.1074/jbc.272.10.6561. ISSN 0021-9258. PMID 9045683. Cite uses deprecated parameters (help)

Dutta A, Stillman B (1992). "cdc2 family kinases phosphorylate a human cell DNA replication factor, RPA, and activate DNA replication.". EMBO J. 11 (6): 2189–99. PMC 556686. PMID 1318195.
Erdile LF, Wold MS, Kelly TJ (1990). "The primary structure of the 32-kDa subunit of human replication protein A.". J. Biol. Chem. 265 (6): 3177–82. PMID 2406247.
Li L, Lu X, Peterson CA, Legerski RJ (1995). "An interaction between the DNA repair factor XPA and replication protein A appears essential for nucleotide excision repair.". Mol. Cell. Biol. 15 (10): 5396–402. PMC 230789. PMID 7565690.
Umbricht CB, Griffin CA, Hawkins AL, et al. (1994). "High-resolution genomic mapping of the three human replication protein A genes (RPA1, RPA2, and RPA3).". Genomics 20 (2): 249–57. doi:10.1006/geno.1994.1161. PMID 8020972.
Nagelhus TA, Haug T, Singh KK, et al. (1997). "A sequence in the N-terminal region of human uracil-DNA glycosylase with homology to XPA interacts with the C-terminal part of the 34-kDa subunit of replication protein A.". J. Biol. Chem. 272 (10): 6561–6. doi:10.1074/jbc.272.10.6561. PMID 9045683.
Amacker M, Hottiger M, Mossi R, Hübscher U (1997). "HIV-1 nucleocapsid protein and replication protein A influence the strand displacement DNA synthesis of lentiviral reverse transcriptase.". AIDS 11 (4): 534–6. PMID 9084803.
Niu H, Erdjument-Bromage H, Pan ZQ, et al. (1997). "Mapping of amino acid residues in the p34 subunit of human single-stranded DNA-binding protein phosphorylated by DNA-dependent protein kinase and Cdc2 kinase in vitro.". J. Biol. Chem. 272 (19): 12634–41. doi:10.1074/jbc.272.19.12634. PMID 9139719.
Zernik-Kobak M, Vasunia K, Connelly M, et al. (1997). "Sites of UV-induced phosphorylation of the p34 subunit of replication protein A from HeLa cells.". J. Biol. Chem. 272 (38): 23896–904. doi:10.1074/jbc.272.38.23896. PMID 9295339.
Bochkareva E, Frappier L, Edwards AM, Bochkarev A (1998). "The RPA32 subunit of human replication protein A contains a single-stranded DNA-binding domain.". J. Biol. Chem. 273 (7): 3932–6. doi:10.1074/jbc.273.7.3932. PMID 9461578.
Shao RG, Cao CX, Zhang H, et al. (1999). "Replication-mediated DNA damage by camptothecin induces phosphorylation of RPA by DNA-dependent protein kinase and dissociates RPA:DNA-PK complexes.". EMBO J. 18 (5): 1397–406. doi:10.1093/emboj/18.5.1397. PMC 1171229. PMID 10064605.
Otterlei M, Warbrick E, Nagelhus TA, et al. (1999). "Post-replicative base excision repair in replication foci.". EMBO J. 18 (13): 3834–44. doi:10.1093/emboj/18.13.3834. PMC 1171460. PMID 10393198.
Bochkarev A, Bochkareva E, Frappier L, Edwards AM (1999). "The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding.". EMBO J. 18 (16): 4498–504. doi:10.1093/emboj/18.16.4498. PMC 1171524. PMID 10449415.
Lao Y, Gomes XV, Ren Y, et al. (2000). "Replication protein A interactions with DNA. III. Molecular basis of recognition of damaged DNA.". Biochemistry 39 (5): 850–9. doi:10.1021/bi991704s. PMID 10653628.
Costello JF, Frühwald MC, Smiraglia DJ, et al. (2000). "Aberrant CpG-island methylation has non-random and tumour-type-specific patterns.". Nat. Genet. 24 (2): 132–8. doi:10.1038/72785. PMID 10655057.
Kim J, Kim D, Chung J (2000). "Replication protein a 32 kDa subunit (RPA p32) binds the SH2 domain of STAT3 and regulates its transcriptional activity.". Cell Biol. Int. 24 (7): 467–73. doi:10.1006/cbir.2000.0525. PMID 10875894.
Cho JM, Song DJ, Bergeron J, et al. (2000). "RBT1, a novel transcriptional co-activator, binds the second subunit of replication protein A.". Nucleic Acids Res. 28 (18): 3478–85. doi:10.1093/nar/28.18.3478. PMC 110737. PMID 10982866.
Brush GS, Kelly TJ (2000). "Phosphorylation of the replication protein A large subunit in the Saccharomyces cerevisiae checkpoint response.". Nucleic Acids Res. 28 (19): 3725–32. doi:10.1093/nar/28.19.3725. PMC 110765. PMID 11000264.
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.
Habel JE, Ohren JF, Borgstahl GE (2001). "Dynamic light-scattering analysis of full-length human RPA14/32 dimer: purification, crystallization and self-association.". Acta Crystallogr. D Biol. Crystallogr. 57 (Pt 2): 254–9. doi:10.1107/S0907444900015225. PMID 11173472.

PDB gallery

1dpu: SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF HUMAN RPA32 COMPLEXED WITH UNG2(73-88)

1l1o: Structure of the human Replication Protein A (RPA) trimerization core

1quq: COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32

1z1d: Structural Model for the interaction between RPA32 C-terminal domain and SV40 T antigen origin binding domain.

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RPA2

Interactions

References

Further reading