RPA3

Replication protein A3, 14kDa
PDB rendering based on 1l1o.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1L1O​, 1QUQ​, 2PI2​, 2PQA​, 2Z6K​, 3KDF​
Identifiers
Symbols	RPA3 ; REPA3
External IDs	OMIM: 179837 MGI: 1915490 HomoloGene: 68285 GeneCards: RPA3 Gene
Gene ontology Molecular function • damaged DNA binding • single-stranded DNA binding • protein binding Cellular component • nucleoplasm • DNA replication factor A complex Biological process • G1/S 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 strand elongation involved in DNA replication • DNA repair • transcription-coupled nucleotide-excision repair • base-excision repair • nucleotide-excision repair • nucleotide-excision repair, DNA gap filling • mismatch repair • double-strand break repair • regulation of mitotic cell cycle • translesion synthesis • telomere maintenance via semi-conservative replication • cellular response to heat • regulation of cell proliferation • error-prone translesion synthesis • DNA damage response, detection of DNA damage • error-free translesion synthesis • regulation of cellular response to heat Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
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

Replication protein A 14 kDa subunit is a protein that in humans is encoded by the RPA3 gene.^[1][2]

Interactions

RPA3 has been shown to interact with Replication protein A1^[3][4] and RPA2.^[3][4]

References

1. 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.
2. "Entrez Gene: RPA3 replication protein A3, 14kDa".
3. 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.
4. 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.

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.
• "Toward a complete human genome sequence". Genome Research 8 (11): 1097–108. Nov 1998. 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.
• 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, Biological Crystallography 57 (Pt 2): 254–9. 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. doi:10.1038/nature04209. PMID 16189514.
• 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. doi:10.1371/journal.pone.0121396. PMID 25875127. AAAS EurekAlert! Press Release and NAE Podcast Feature.