RPA2

Replication protein A2, 32kDa

PDB rendering based on 1dpu.

Available structures
PDB	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	• DNA binding • single-stranded DNA binding • protein binding • protein phosphatase binding • protein N-terminus binding
Cellular component	• nucleus • nucleoplasm • 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 • M/G1 transition 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 • DNA recombination • 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:
132.32 – 132.33 Mb

PubMed search

[1]

[2]

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,^[5]^[4] 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 (Apr 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". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6118.
^ ^a ^b ^c Shao, R G; Cao C X, Zhang H, Kohn K W, Wold M S, 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". EMBO J. (ENGLAND) 18 (5): 1397–406. doi:10.1093/emboj/18.5.1397. ISSN 0261-4189. PMC 1171229. PMID 10064605. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171229.
^ ^a ^b Bochkareva, Elena; Korolev Sergey, Lees-Miller Susan P, Bochkarev Alexey (Apr. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125950.
^ Bochkareva, E; Frappier L, Edwards A M, Bochkarev A (Feb. 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.
^ 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.
^ Otterlei, M; Warbrick E, Nagelhus T A, Haug T, Slupphaug G, Akbari M, Aas P A, Steinsbekk K, Bakke O, Krokan H E (Jul. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171460.
^ 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 (Jan. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=151531.
^ Yoo, Eunjae; Kim Byung U, Lee Seung Youn, Cho Chae Hyun, Chung Jay H, Lee Chang-Hun (Aug. 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.
^ 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 (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". J. Biol. Chem. (UNITED STATES) 272 (10): 6561–6. doi:10.1074/jbc.272.10.6561. ISSN 0021-9258. PMID 9045683.

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=556686.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=230789.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171229.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171460.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171524.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=110737.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=110765.
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.

RPA2

Interactions

References

Further reading