Replication protein A2

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

RPA2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRPA2, REPA2, RP-A p32, RP-A p34, RPA32, replication protein A2
External IDsOMIM: 179836 MGI: 1339939 HomoloGene: 37712 GeneCards: RPA2
Gene location (Human)
Chr.Chromosome 1 (human)[1]
Band1p35.3Start27,891,524 bp[1]
End27,914,746 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
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 MbChr 4: 132.77 – 132.78 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Interactions

RPA2 has been shown to interact with:

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See also

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. 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.
  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

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