Replication protein A3

RPA3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1L1O, 1QUQ, 2PI2, 2PQA, 2Z6K, 3KDF
Identifiers
Aliases	RPA3, REPA3, RP-A p14, replication protein A3
External IDs	OMIM: 179837; MGI: 1915490; HomoloGene: 68285; GeneCards: RPA3; OMA:RPA3 - orthologs
Gene location (Human) Chr. Chromosome 7 (human) Band 7p21.3 Start 7,636,518 bp End 7,718,607 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6|6 A1 Start 8,255,936 bp End 8,259,173 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in bronchial epithelial cell beta cell trabecular bone embryo ventricular zone bone marrow olfactory zone of nasal mucosa nasal epithelium ganglionic eminence mucosa of transverse colon Top expressed in medial ganglionic eminence otic placode zygote yolk sac thymus dermis mandibular prominence maxillary prominence embryo ventricular zone More reference expression data BioGPS More reference expression data
Gene ontology Molecular function single-stranded DNA binding DNA binding damaged DNA binding protein binding Cellular component nucleus nucleoplasm DNA replication factor A complex site of double-strand break Biological process DNA recombination translesion synthesis DNA replication nucleotide-excision repair, DNA gap filling transcription-coupled nucleotide-excision repair regulation of cell population proliferation nucleotide-excision repair, DNA incision error-free translesion synthesis cellular response to DNA damage stimulus regulation of mitotic cell cycle regulation of cellular response to heat interstrand cross-link repair error-prone translesion synthesis nucleotide-excision repair, DNA incision, 5'-to lesion nucleotide-excision repair, preincision complex stabilization nucleotide-excision repair DNA repair base-excision repair double-strand break repair via homologous recombination nucleotide-excision repair, preincision complex assembly telomere maintenance telomere maintenance via semi-conservative replication G1/S transition of mitotic cell cycle DNA mismatch repair nucleotide-excision repair, DNA incision, 3'-to lesion regulation of signal transduction by p53 class mediator Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6119 68240 Ensembl ENSG00000106399 ENSMUSG00000012483 UniProt P35244 Q9CQ71 RefSeq (mRNA) NM_002947 NM_026632 RefSeq (protein) NP_002938 NP_080908 Location (UCSC) Chr 7: 7.64 – 7.72 Mb Chr 6: 8.26 – 8.26 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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.

Interactions

RPA3 has been shown to interact with replication protein A1 and replication protein A2. 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. 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 repair

See also

• Single-stranded binding protein
• Replication protein A
• Replication protein A1
• Replication protein A2

Further reading

• Iftode C, Daniely Y, Borowiec JA (1999). "Replication protein A (RPA): the eukaryotic SSB". Critical Reviews in Biochemistry and Molecular Biology. 34 (3): 141–80. doi:10.1080/10409239991209255. PMID 10473346.
• Keshav KF, Chen C, Dutta A (Jun 1995). "Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A complex". Molecular and Cellular Biology. 15 (6): 3119–28. doi:10.1128/mcb.15.6.3119. PMC 230543. PMID 7760808.
• 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.
• 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.
• 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.
• Sanger Centre, The; Washington University Genome Sequencing Cente, The (Nov 1998). "Toward a complete human genome sequence". Genome Research. 8 (11): 1097–108. doi:10.1101/gr.8.11.1097. PMID 9847074.
• 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. Bibcode:2001AcCrD..57..254H. doi:10.1107/S0907444900015225. PMID 11173472.
• 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.
• Kneissl M, Pütter V, Szalay AA, Grummt F (Mar 2003). "Interaction and assembly of murine pre-replicative complex proteins in yeast and mouse cells". Journal of Molecular Biology. 327 (1): 111–28. doi:10.1016/S0022-2836(03)00079-2. PMID 12614612.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1) 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
• Sankaranarayanan P, Schomay TE, Aiello KA, Alter O (April 2015). "Tensor GSVD of patient- and platform-matched tumor and normal DNA copy-number profiles uncovers chromosome arm-wide patterns of tumor-exclusive platform-consistent alterations encoding for cell transformation and predicting ovarian cancer survival". PLOS ONE. 10 (4) e0121396. Bibcode:2015PLoSO..1021396S. doi:10.1371/journal.pone.0121396. PMC 4398562. PMID 25875127. AAAS EurekAlert! Press Release and NAE Podcast Feature.