Replication protein A2

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
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1p35.3 Start 27,891,524 bp [1] End 27,914,746 bp [1]
Gene location (Mouse) Chr. Chromosome 4 (mouse) [2] Band 4|4 D2.3 Start 132,495,643 bp [2] End 132,506,063 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ganglionic eminence gastrocnemius muscle Achilles tendon right uterine tube tibialis anterior muscle lymph node gallbladder prefrontal cortex islet of Langerhans right coronary artery Top expressed in somite primitive streak endocardial cushion abdominal wall germ layer ectoderm otic placode maxillary prominence dermis morula 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 [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Replication protein A 32 kDa subunit is a protein that in humans is encoded by the RPA2 gene. ^{[5] [6]}

Interactions

RPA2 has been shown to interact with:

• Cyclin O, ^[7]
• DNA-PKcs, ^[8]
• Ku70, ^[8]
• MEN1, ^[9]
• RPA3, ^{[10] [11]}
• Replication protein A1, ^{[8] [10]}
• STAT3, ^[12]
• TP53BP1 ^[13] and
• Uracil-DNA glycosylase. ^[14]

See also

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

References

1. GRCh38: Ensembl release 89: ENSG00000117748 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028884 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Umbricht CB, Erdile LF, Jabs EW, Kelly TJ (Mar 1993). "Cloning, overexpression, and genomic mapping of the 14-kDa subunit of human replication protein A". The Journal of Biological Chemistry. 268 (9): 6131–8. doi: 10.1016/S0021-9258(18)53229-4 . PMID   8454588.
6. "Entrez Gene: RPA2 Replication protein A2, 32kDa".
7. 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.
8. 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.
9. Sukhodolets KE, Hickman AB, Agarwal SK, Sukhodolets MV, Obungu VH, Novotny EA, Crabtree JS, Chandrasekharappa SC, Collins FS, Spiegel AM, Burns AL, Marx SJ (Jan 2003). "The 32-kilodalton subunit of replication protein A interacts with menin, the product of the MEN1 tumor suppressor gene". Molecular and Cellular Biology. 23 (2): 493–509. doi:10.1128/mcb.23.2.493-509.2003. PMC   151531 . PMID   12509449.
10. Bochkareva E, Korolev S, Lees-Miller SP, Bochkarev A (Apr 2002). "Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA". The EMBO Journal. 21 (7): 1855–63. doi:10.1093/emboj/21.7.1855. PMC   125950 . PMID   11927569.
11. 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.
12. 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.
13. Yoo E, Kim BU, Lee SY, Cho CH, Chung JH, Lee CH (Aug 2005). "53BP1 is associated with replication protein A and is required for RPA2 hyperphosphorylation following DNA damage". Oncogene. 24 (35): 5423–30. doi: 10.1038/sj.onc.1208710 . PMID   15856006.
14. 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.

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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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/S0907444900015225 . PMID   11173472.