Article · Wikipedia archive · Last revised Jul 3, 2026

Replication protein A3

Replication protein A 14 kDa subunit is a protein that in humans is encoded by the RPA3 gene. RPA is a single-stranded DNA-binding protein that is conserved in eukaryotes and plays essential roles in the metabolism of nucleic acids. Unlike helicase, RPA does not separate strands but binds and protects exposed single-stranded DNA to prevent secondary structure formation and degradation. RPA is usually considered to be the functional equivalent of bacterial single-stranded DNA-binding proteins (SSB), although it is much more complex structurally in eukaryotic cells.

Last revised
Jul 3, 2026
Read time
≈ 6 min
Length
1,335 w
Citations
19
Source
RPA3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRPA3, REPA3, RP-A p14, replication protein A3
External IDsOMIM: 179837; MGI: 1915490; HomoloGene: 68285; GeneCards: RPA3; OMA:RPA3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002947

NM_026632

RefSeq (protein)

NP_002938

NP_080908

Location (UCSC)Chr 7: 7.64 – 7.72 MbChr 6: 8.26 – 8.26 Mb
PubMed search34
Wikidata
View/Edit HumanView/Edit Mouse

Replication protein A 14 kDa subunit is a protein that in humans is encoded by the RPA3 gene.56 RPA is a single-stranded DNA-binding protein that is conserved in eukaryotes and plays essential roles in the metabolism of nucleic acids.7 Unlike helicase, RPA does not separate strands but binds and protects exposed single-stranded DNA to prevent secondary structure formation and degradation.8 RPA is usually considered to be the functional equivalent of bacterial single-stranded DNA-binding proteins (SSB), although it is much more complex structurally in eukaryotic cells.9


Interactions

RPA3 has been shown to interact with replication protein A11011 and replication protein A2.1011 Together, they form a heterotrimeric complex that contributes to the direct binding of single-stranded DNA during replication, homologous recombination, nucleoetide excision repair, and mismatch repair.12 RPA3 can directly contact ssDNA on the 3' side of a substrate, and this polarity is crucial for the positioning and stability of nucleases that are involved in excision repair13

See also

See also

References

References

  1. GRCh38: Ensembl release 89: ENSG00000106399Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000012483Ensembl, 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: RPA3 replication protein A3, 14kDa".
  7. Salas, Tonatiuh Romero; Petruseva, Irina; Lavrik, Olga; Saintomé, Carole (1 January 2009). "Evidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNA". Nucleic Acids Research. 37 (1): 38–46. doi:10.1093/nar/gkn895. PMC 2615627. PMID 19010961.
  8. Chen, Ran; Marc S, Wold (2014). "Replication protein A: single-stranded DNA's first responder: dynamic DNA-interactions allow replication protein A to direct single-strand DNA intermediates into different pathways for synthesis or repair". BioEssays: News and Reviews in Molecular, Cellular and Developmental Biology. 36, 12 (12): 1156–1161. doi:10.1002/bies.201400107. PMC 4629251. PMID 25171654.
  9. Iftode, C; Daniely, Y; Borowiec, J.A (1999). "Replication protein A (RPA): the eukaryotic SSB". Critical Reviews in Biochemistry and Molecular Biology. 34 (3): 141–180. doi:10.1080/10409239991209255. PMID 10473346.
  10. 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.
  11. 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.
  12. Madru, C; Martínez-Carranza, M (2023). "A-binding mechanism and evolution of replication protein A". Nature Communications. 14 (1) 2326. Bibcode:2023NatCo..14.2326M. doi:10.1038/s41467-023-38048-w. PMC 10122647. PMID 37087464.
  13. de Laat, W. L; Appeldoorn, E; Sugasawa, K; Weterings, E; Hoeijmakers, J. H; Jaspers, N. G (15 August 1998). "DNA-binding polarity of human replication protein A positions nucleases in nucleotide excision repair". Genes & Development. 12 (16): 2598–2609. doi:10.1101/gad.12.16.2598. PMC 317078. PMID 9716411.
Further reading

Further reading