Replication protein A2

Replication protein A 32 kDa subunit is a protein that in humans is encoded by the RPA2 gene.

RPA2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1DPU, 1L1O, 1QUQ, 1Z1D, 2PI2, 2PQA, 2Z6K, 3KDF, 4MQV, 4OU0
Identifiers
Aliases	RPA2, REPA2, RP-A p32, RP-A p34, RPA32, replication protein A2
External IDs	OMIM: 179836; MGI: 1339939; HomoloGene: 37712; GeneCards: RPA2; OMA:RPA2 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1p35.3 Start 27,891,524 bp End 27,914,746 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4|4 D2.3 Start 132,495,643 bp End 132,506,063 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone granulocyte ganglionic eminence right testis left testis gastrocnemius muscle Achilles tendon right uterine tube gonad tibialis anterior muscle Top expressed in somite fetal liver hematopoietic progenitor cell primitive streak embryo ventricular zone mandibular prominence endocardial cushion abdominal wall germ layer ectoderm More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA binding protein N-terminus binding single-stranded DNA binding damaged DNA binding protein binding enzyme binding protein phosphatase binding ubiquitin protein ligase binding G-rich strand telomeric DNA binding double-stranded DNA binding sequence-specific DNA binding Cellular component site of double-strand break PML body nucleoplasm telomere DNA replication factor A complex chromatin nucleus nuclear body condensed nuclear chromosome Biological process nucleotide-excision repair, DNA gap filling DNA recombination interstrand cross-link repair regulation of double-strand break repair via homologous recombination error-free translesion synthesis G1 phase error-prone translesion synthesis cellular response to DNA damage stimulus DNA replication mitotic G1 DNA damage checkpoint signaling regulation of DNA damage checkpoint regulation of cellular response to heat DNA mismatch repair translesion synthesis transcription-coupled nucleotide-excision repair nucleotide-excision repair, DNA incision base-excision repair nucleotide-excision repair nucleotide-excision repair, preincision complex stabilization regulation of signal transduction by p53 class mediator DNA repair double-strand break repair via homologous recombination nucleotide-excision repair, preincision complex assembly nucleotide-excision repair, DNA incision, 5'-to lesion nucleotide-excision repair, DNA incision, 3'-to lesion protein localization to chromosome telomere maintenance telomere maintenance via semi-conservative replication G1/S transition of mitotic cell cycle telomere maintenance via recombination DNA topological change DNA unwinding involved in DNA replication mitotic recombination telomere maintenance via telomerase reciprocal meiotic recombination heteroduplex formation positive regulation of helicase activity Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6118 19891 Ensembl ENSG00000117748 ENSMUSG00000028884 UniProt P15927 Q62193 RefSeq (mRNA) NM_001286076 NM_001297558 NM_002946 NM_001355128 NM_001355129 NM_011284 RefSeq (protein) NP_001273005 NP_001284487 NP_002937 NP_001342057 NP_001342058 n/a Location (UCSC) Chr 1: 27.89 – 27.91 Mb Chr 4: 132.5 – 132.51 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Interactions

RPA2 has been shown to interact with:

• Cyclin O,
• DNA-PKcs,
• Ku70,
• MEN1,
• RPA3,
• Replication protein A1,
• STAT3,
• TP53BP1 and
• Uracil-DNA glycosylase.

See also

• Single-stranded binding protein
• Replication protein A
• Replication protein A1
• Replication protein A3

Further reading

• Dutta A, Stillman B (Jun 1992). "cdc2 family kinases phosphorylate a human cell DNA replication factor, RPA, and activate DNA replication". The EMBO Journal. 11 (6): 2189–99. doi:10.1002/j.1460-2075.1992.tb05278.x. PMC 556686. PMID 1318195.2189-99&rft.date=1992-06&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC556686#id-name=PMC&rft_id=info:pmid/1318195&rft_id=info:doi/10.1002/j.1460-2075.1992.tb05278.x&rft.aulast=Dutta&rft.aufirst=A&rft.au=Stillman, B&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC556686&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• Erdile LF, Wold MS, Kelly TJ (Feb 1990). "The primary structure of the 32-kDa subunit of human replication protein A". The Journal of Biological Chemistry. 265 (6): 3177–82. doi:10.1016/S0021-9258(19)39750-9. PMID 2406247.3177-82&rft.date=1990-02&rft_id=info:doi/10.1016/S0021-9258(19)39750-9&rft_id=info:pmid/2406247&rft.aulast=Erdile&rft.aufirst=LF&rft.au=Wold, MS&rft.au=Kelly, TJ&rft_id=https://doi.org/10.1016%2FS0021-9258%2819%2939750-9&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• Li L, Lu X, Peterson CA, Legerski RJ (Oct 1995). "An interaction between the DNA repair factor XPA and replication protein A appears essential for nucleotide excision repair". Molecular and Cellular Biology. 15 (10): 5396–402. doi:10.1128/mcb.15.10.5396. PMC 230789. PMID 7565690.5396-402&rft.date=1995-10&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC230789#id-name=PMC&rft_id=info:pmid/7565690&rft_id=info:doi/10.1128/mcb.15.10.5396&rft.aulast=Li&rft.aufirst=L&rft.au=Lu, X&rft.au=Peterson, CA&rft.au=Legerski, RJ&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC230789&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• Umbricht CB, Griffin CA, Hawkins AL, Grzeschik KH, O'Connell P, Leach R, Green ED, Kelly TJ (Mar 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 8020972.249-57&rft.date=1994-03&rft_id=info:doi/10.1006/geno.1994.1161&rft_id=info:pmid/8020972&rft.aulast=Umbricht&rft.aufirst=CB&rft.au=Griffin, CA&rft.au=Hawkins, AL&rft.au=Grzeschik, KH&rft.au=O'Connell, P&rft.au=Leach, R&rft.au=Green, ED&rft.au=Kelly, TJ&rft_id=https://doi.org/10.1006%2Fgeno.1994.1161&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• Nagelhus TA, Haug T, Singh KK, Keshav KF, Skorpen F, Otterlei M, Bharati S, Lindmo T, Benichou S, Benarous R, Krokan HE (Mar 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". The Journal of Biological Chemistry. 272 (10): 6561–6. doi:10.1074/jbc.272.10.6561. PMID 9045683.6561-6&rft.date=1997-03&rft_id=info:doi/10.1074/jbc.272.10.6561&rft_id=info:pmid/9045683&rft.aulast=Nagelhus&rft.aufirst=TA&rft.au=Haug, T&rft.au=Singh, KK&rft.au=Keshav, KF&rft.au=Skorpen, F&rft.au=Otterlei, M&rft.au=Bharati, S&rft.au=Lindmo, T&rft.au=Benichou, S&rft.au=Benarous, R&rft.au=Krokan, HE&rft_id=https://doi.org/10.1074%2Fjbc.272.10.6561&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• Amacker M, Hottiger M, Mossi R, Hübscher U (Mar 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 9084803.534-6&rft.date=1997-03&rft_id=info:pmid/9084803&rft.aulast=Amacker&rft.aufirst=M&rft.au=Hottiger, M&rft.au=Mossi, R&rft.au=Hübscher, U&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• Niu H, Erdjument-Bromage H, Pan ZQ, Lee SH, Tempst P, Hurwitz J (May 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". The Journal of Biological Chemistry. 272 (19): 12634–41. doi:10.1074/jbc.272.19.12634. PMID 9139719.12634-41&rft.date=1997-05&rft_id=info:doi/10.1074/jbc.272.19.12634&rft_id=info:pmid/9139719&rft.aulast=Niu&rft.aufirst=H&rft.au=Erdjument-Bromage, H&rft.au=Pan, ZQ&rft.au=Lee, SH&rft.au=Tempst, P&rft.au=Hurwitz, J&rft_id=https://doi.org/10.1074%2Fjbc.272.19.12634&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• Zernik-Kobak M, Vasunia K, Connelly M, Anderson CW, Dixon K (Sep 1997). "Sites of UV-induced phosphorylation of the p34 subunit of replication protein A from HeLa cells". The Journal of Biological Chemistry. 272 (38): 23896–904. doi:10.1074/jbc.272.38.23896. PMID 9295339.23896-904&rft.date=1997-09&rft_id=info:doi/10.1074/jbc.272.38.23896&rft_id=info:pmid/9295339&rft.aulast=Zernik-Kobak&rft.aufirst=M&rft.au=Vasunia, K&rft.au=Connelly, M&rft.au=Anderson, CW&rft.au=Dixon, K&rft_id=https://doi.org/10.1074%2Fjbc.272.38.23896&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• Bochkareva E, Frappier L, Edwards AM, Bochkarev A (Feb 1998). "The RPA32 subunit of human replication protein A contains a single-stranded DNA-binding domain". The Journal of Biological Chemistry. 273 (7): 3932–6. doi:10.1074/jbc.273.7.3932. PMID 9461578.3932-6&rft.date=1998-02&rft_id=info:doi/10.1074/jbc.273.7.3932&rft_id=info:pmid/9461578&rft.aulast=Bochkareva&rft.aufirst=E&rft.au=Frappier, L&rft.au=Edwards, AM&rft.au=Bochkarev, A&rft_id=https://doi.org/10.1074%2Fjbc.273.7.3932&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• Shao RG, Cao CX, Zhang H, Kohn KW, Wold MS, Pommier Y (Mar 1999). "Replication-mediated DNA damage by camptothecin induces phosphorylation of RPA by DNA-dependent protein kinase and dissociates RPA:DNA-PK complexes". The EMBO Journal. 18 (5): 1397–406. doi:10.1093/emboj/18.5.1397. PMC 1171229. PMID 10064605.1397-406&rft.date=1999-03&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171229#id-name=PMC&rft_id=info:pmid/10064605&rft_id=info:doi/10.1093/emboj/18.5.1397&rft.aulast=Shao&rft.aufirst=RG&rft.au=Cao, CX&rft.au=Zhang, H&rft.au=Kohn, KW&rft.au=Wold, MS&rft.au=Pommier, Y&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171229&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• Otterlei M, Warbrick E, Nagelhus TA, Haug T, Slupphaug G, Akbari M, Aas PA, Steinsbekk K, Bakke O, Krokan HE (Jul 1999). "Post-replicative base excision repair in replication foci". The EMBO Journal. 18 (13): 3834–44. doi:10.1093/emboj/18.13.3834. PMC 1171460. PMID 10393198.3834-44&rft.date=1999-07&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171460#id-name=PMC&rft_id=info:pmid/10393198&rft_id=info:doi/10.1093/emboj/18.13.3834&rft.aulast=Otterlei&rft.aufirst=M&rft.au=Warbrick, E&rft.au=Nagelhus, TA&rft.au=Haug, T&rft.au=Slupphaug, G&rft.au=Akbari, M&rft.au=Aas, PA&rft.au=Steinsbekk, K&rft.au=Bakke, O&rft.au=Krokan, HE&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171460&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• Bochkarev A, Bochkareva E, Frappier L, Edwards AM (Aug 1999). "The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding". The EMBO Journal. 18 (16): 4498–504. doi:10.1093/emboj/18.16.4498. PMC 1171524. PMID 10449415.4498-504&rft.date=1999-08&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171524#id-name=PMC&rft_id=info:pmid/10449415&rft_id=info:doi/10.1093/emboj/18.16.4498&rft.aulast=Bochkarev&rft.aufirst=A&rft.au=Bochkareva, E&rft.au=Frappier, L&rft.au=Edwards, AM&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171524&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• Lao Y, Gomes XV, Ren Y, Taylor JS, Wold MS (Feb 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 10653628.850-9&rft.date=2000-02&rft_id=info:doi/10.1021/bi991704s&rft_id=info:pmid/10653628&rft.aulast=Lao&rft.aufirst=Y&rft.au=Gomes, XV&rft.au=Ren, Y&rft.au=Taylor, JS&rft.au=Wold, MS&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• Costello JF, Frühwald MC, Smiraglia DJ, Rush LJ, Robertson GP, Gao X, Wright FA, Feramisco JD, Peltomäki P, Lang JC, Schuller DE, Yu L, Bloomfield CD, Caligiuri MA, Yates A, Nishikawa R, Su Huang H, Petrelli NJ, Zhang X, O'Dorisio MS, Held WA, Cavenee WK, Plass C (Feb 2000). "Aberrant CpG-island methylation has non-random and tumour-type-specific patterns". Nature Genetics. 24 (2): 132–8. doi:10.1038/72785. PMID 10655057. S2CID 6273676.132-8&rft.date=2000-02&rft_id=https://api.semanticscholar.org/CorpusID:6273676#id-name=S2CID&rft_id=info:pmid/10655057&rft_id=info:doi/10.1038/72785&rft.aulast=Costello&rft.aufirst=JF&rft.au=Frühwald, MC&rft.au=Smiraglia, DJ&rft.au=Rush, LJ&rft.au=Robertson, GP&rft.au=Gao, X&rft.au=Wright, FA&rft.au=Feramisco, JD&rft.au=Peltomäki, P&rft.au=Lang, JC&rft.au=Schuller, DE&rft.au=Yu, L&rft.au=Bloomfield, CD&rft.au=Caligiuri, MA&rft.au=Yates, A&rft.au=Nishikawa, R&rft.au=Su Huang, H&rft.au=Petrelli, NJ&rft.au=Zhang, X&rft.au=O'Dorisio, MS&rft.au=Held, WA&rft.au=Cavenee, WK&rft.au=Plass, C&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• 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 Biology International. 24 (7): 467–73. doi:10.1006/cbir.2000.0525. PMID 10875894. S2CID 23783745.467-73&rft.date=2000&rft_id=https://api.semanticscholar.org/CorpusID:23783745#id-name=S2CID&rft_id=info:pmid/10875894&rft_id=info:doi/10.1006/cbir.2000.0525&rft.aulast=Kim&rft.aufirst=J&rft.au=Kim, D&rft.au=Chung, J&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• Cho JM, Song DJ, Bergeron J, Benlimame N, Wold MS, Alaoui-Jamali MA (Sep 2000). "RBT1, a novel transcriptional co-activator, binds the second subunit of replication protein A". Nucleic Acids Research. 28 (18): 3478–85. doi:10.1093/nar/28.18.3478. PMC 110737. PMID 10982866.3478-85&rft.date=2000-09&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC110737#id-name=PMC&rft_id=info:pmid/10982866&rft_id=info:doi/10.1093/nar/28.18.3478&rft.aulast=Cho&rft.aufirst=JM&rft.au=Song, DJ&rft.au=Bergeron, J&rft.au=Benlimame, N&rft.au=Wold, MS&rft.au=Alaoui-Jamali, MA&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC110737&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• Brush GS, Kelly TJ (Oct 2000). "Phosphorylation of the replication protein A large subunit in the Saccharomyces cerevisiae checkpoint response". Nucleic Acids Research. 28 (19): 3725–32. doi:10.1093/nar/28.19.3725. PMC 110765. PMID 11000264.3725-32&rft.date=2000-10&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC110765#id-name=PMC&rft_id=info:pmid/11000264&rft_id=info:doi/10.1093/nar/28.19.3725&rft.aulast=Brush&rft.aufirst=GS&rft.au=Kelly, TJ&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC110765&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• 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. S2CID 16640087.449-56&rft.date=2000-10&rft_id=https://api.semanticscholar.org/CorpusID:16640087#id-name=S2CID&rft_id=info:pmid/11081631&rft_id=info:doi/10.1016/S0092-8674(00)00136-7&rft.aulast=Mer&rft.aufirst=G&rft.au=Bochkarev, A&rft.au=Gupta, R&rft.au=Bochkareva, E&rft.au=Frappier, L&rft.au=Ingles, CJ&rft.au=Edwards, AM&rft.au=Chazin, WJ&rft_id=https://doi.org/10.1016%2FS0092-8674%2800%2900136-7&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">
• Habel JE, Ohren JF, Borgstahl GE (Feb 2001). "Dynamic light-scattering analysis of full-length human RPA14/32 dimer: purification, crystallization and self-association". Acta Crystallographica Section D. 57 (Pt 2): 254–9. doi:10.1107/S0907444950015225. PMID 11173472.254-9&rft.date=2001-02&rft_id=info:doi/10.1107/S0907444950015225&rft_id=info:pmid/11173472&rft.aulast=Habel&rft.aufirst=JE&rft.au=Ohren, JF&rft.au=Borgstahl, GE&rft_id=https://doi.org/10.1107%2FS0907444950015225&rfr_id=info:sid/en.wikipedia.org:Replication protein A2" class="Z3988">