RFC3

Replication factor C (activator 1) 3, 38kDa
Identifiers
Symbols	RFC3 ; RFC38
External IDs	OMIM: 600405 MGI: 1916513 HomoloGene: 2188 GeneCards: RFC3 Gene
Gene ontology Molecular function • DNA binding • DNA clamp loader activity • protein binding • ATPase activity Cellular component • nucleoplasm • DNA replication factor C complex Biological process • mitotic cell cycle • telomere maintenance via recombination • telomere maintenance • DNA synthesis involved in DNA repair • DNA replication • DNA-dependent 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 • translesion synthesis • telomere maintenance via semi-conservative replication • error-prone translesion synthesis • DNA damage response, detection of DNA damage • response to organophosphorus • error-free translesion synthesis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5983	69263
Ensembl	ENSG00000133119	ENSMUSG00000033970
UniProt	P40938	Q8R323
RefSeq (mRNA)	NM_002915	NM_027009
RefSeq (protein)	NP_002906	NP_081285
Location (UCSC)	Chr 13: 33.82 – 33.97 Mb	Chr 5: 151.64 – 151.65 Mb
PubMed search

Replication factor C subunit 3 is a protein that in humans is encoded by the RFC3 gene.^[1][2]

Function

The elongation of primed DNA templates by DNA polymerase delta and DNA polymerase epsilon requires the accessory proteins proliferating cell nuclear antigen (PCNA) and replication factor C (RFC). RFC, also named activator 1, is a protein complex consisting of five distinct subunits of 140, 40, 38, 37, and 36 kDa. This gene encodes the 38 kDa subunit. This subunit is essential for the interaction between the 140 kDa subunit and the core complex that consists of the 36, 37, and 40 kDa subunits. Alternatively spliced transcript variants encoding distinct isoforms have been described.^[2]

Interactions

RFC3 has been shown to interact with:

• BRD4,^[3]
• CHTF18,^[4][5]
• PCNA,^[5][6]
• RFC1,^[7][8][9] and
• RFC4.^[7][8]

References

1. Okumura K, Nogami M, Taguchi H, Dean FB, Chen M, Pan ZQ, Hurwitz J, Shiratori A, Murakami Y, Ozawa K (Jan 1995). "Assignment of the 36.5-kDa (RFC5), 37-kDa (RFC4), 38-kDa (RFC3), and 40-kDa (RFC2) subunit genes of human replication factor C to chromosome bands 12q24.2-q24.3, 3q27, 13q12.3-q13, and 7q11.23". Genomics 25 (1): 274–8. doi:10.1016/0888-7543(95)80135-9. PMID 7774928.
2. "Entrez Gene: RFC3 replication factor C (activator 1) 3, 38kDa".
3. Maruyama T, Farina A, Dey A, Cheong J, Bermudez VP, Tamura T, Sciortino S, Shuman J, Hurwitz J, Ozato K (Sep 2002). "A Mammalian bromodomain protein, brd4, interacts with replication factor C and inhibits progression to S phase". Molecular and Cellular Biology 22 (18): 6509–20. doi:10.1128/mcb.22.18.6509-6520.2002. PMC 135621. PMID 12192049.
4. Bermudez VP, Maniwa Y, Tappin I, Ozato K, Yokomori K, Hurwitz J (Sep 2003). "The alternative Ctf18-Dcc1-Ctf8-replication factor C complex required for sister chromatid cohesion loads proliferating cell nuclear antigen onto DNA". Proceedings of the National Academy of Sciences of the United States of America 100 (18): 10237–42. doi:10.1073/pnas.1434308100. PMC 193545. PMID 12930902.
5. Merkle CJ, Karnitz LM, Henry-Sánchez JT, Chen J (Aug 2003). "Cloning and characterization of hCTF18, hCTF8, and hDCC1. Human homologs of a Saccharomyces cerevisiae complex involved in sister chromatid cohesion establishment". The Journal of Biological Chemistry 278 (32): 30051–6. doi:10.1074/jbc.M211591200. PMID 12766176.
6. Ohta S, Shiomi Y, Sugimoto K, Obuse C, Tsurimoto T (Oct 2002). "A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-5 complex as a novel PCNA-binding protein". The Journal of Biological Chemistry 277 (43): 40362–7. doi:10.1074/jbc.M206194200. PMID 12171929.
7. Ellison V, Stillman B (Mar 1998). "Reconstitution of recombinant human replication factor C (RFC) and identification of an RFC subcomplex possessing DNA-dependent ATPase activity". The Journal of Biological Chemistry 273 (10): 5979–87. doi:10.1074/jbc.273.10.5979. PMID 9488738.
8. Uhlmann F, Cai J, Flores-Rozas H, Dean FB, Finkelstein J, O'Donnell M, Hurwitz J (Jun 1996). "In vitro reconstitution of human replication factor C from its five subunits". Proceedings of the National Academy of Sciences of the United States of America 93 (13): 6521–6. doi:10.1073/pnas.93.13.6521. PMC 39056. PMID 8692848.
9. Tomida J, Masuda Y, Hiroaki H, Ishikawa T, Song I, Tsurimoto T, Tateishi S, Shiomi T, Kamei Y, Kim J, Kamiya K, Vaziri C, Ohmori H, Todo T (Apr 2008). "DNA damage-induced ubiquitylation of RFC2 subunit of replication factor C complex". The Journal of Biological Chemistry 283 (14): 9071–9. doi:10.1074/jbc.M709835200. PMC 2431014. PMID 18245774.

Further reading

• Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• O'Donnell M, Onrust R, Dean FB, Chen M, Hurwitz J (Jan 1993). "Homology in accessory proteins of replicative polymerases--E. coli to humans". Nucleic Acids Research 21 (1): 1–3. doi:10.1093/nar/21.1.1. PMC 309057. PMID 8441605.
• Uhlmann F, Cai J, Flores-Rozas H, Dean FB, Finkelstein J, O'Donnell M, Hurwitz J (Jun 1996). "In vitro reconstitution of human replication factor C from its five subunits". Proceedings of the National Academy of Sciences of the United States of America 93 (13): 6521–6. doi:10.1073/pnas.93.13.6521. PMC 39056. PMID 8692848.
• Uhlmann F, Cai J, Gibbs E, O'Donnell M, Hurwitz J (Apr 1997). "Deletion analysis of the large subunit p140 in human replication factor C reveals regions required for complex formation and replication activities". The Journal of Biological Chemistry 272 (15): 10058–64. doi:10.1074/jbc.272.15.10058. PMID 9092549.
• Cujec TP, Cho H, Maldonado E, Meyer J, Reinberg D, Peterlin BM (Apr 1997). "The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme". Molecular and Cellular Biology 17 (4): 1817–23. PMC 232028. PMID 9121429.
• Cai J, Gibbs E, Uhlmann F, Phillips B, Yao N, O'Donnell M, Hurwitz J (Jul 1997). "A complex consisting of human replication factor C p40, p37, and p36 subunits is a DNA-dependent ATPase and an intermediate in the assembly of the holoenzyme". The Journal of Biological Chemistry 272 (30): 18974–81. doi:10.1074/jbc.272.30.18974. PMID 9228079.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Ellison V, Stillman B (Mar 1998). "Reconstitution of recombinant human replication factor C (RFC) and identification of an RFC subcomplex possessing DNA-dependent ATPase activity". The Journal of Biological Chemistry 273 (10): 5979–87. doi:10.1074/jbc.273.10.5979. PMID 9488738.
• Zhang G, Gibbs E, Kelman Z, O'Donnell M, Hurwitz J (Mar 1999). "Studies on the interactions between human replication factor C and human proliferating cell nuclear antigen". Proceedings of the National Academy of Sciences of the United States of America 96 (5): 1869–74. doi:10.1073/pnas.96.5.1869. PMC 26703. PMID 10051561.
• Rauen M, Burtelow MA, Dufault VM, Karnitz LM (Sep 2000). "The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9". The Journal of Biological Chemistry 275 (38): 29767–71. doi:10.1074/jbc.M005782200. PMID 10884395.
• Lindsey-Boltz LA, Bermudez VP, Hurwitz J, Sancar A (Sep 2001). "Purification and characterization of human DNA damage checkpoint Rad complexes". Proceedings of the National Academy of Sciences of the United States of America 98 (20): 11236–41. doi:10.1073/pnas.201373498. PMC 58713. PMID 11572977.
• Griffith JD, Lindsey-Boltz LA, Sancar A (May 2002). "Structures of the human Rad17-replication factor C and checkpoint Rad 9-1-1 complexes visualized by glycerol spray/low voltage microscopy". The Journal of Biological Chemistry 277 (18): 15233–6. doi:10.1074/jbc.C200129200. PMID 11907025.
• Ohta S, Shiomi Y, Sugimoto K, Obuse C, Tsurimoto T (Oct 2002). "A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-5 complex as a novel PCNA-binding protein". The Journal of Biological Chemistry 277 (43): 40362–7. doi:10.1074/jbc.M206194200. PMID 12171929.
• Maruyama T, Farina A, Dey A, Cheong J, Bermudez VP, Tamura T, Sciortino S, Shuman J, Hurwitz J, Ozato K (Sep 2002). "A Mammalian bromodomain protein, brd4, interacts with replication factor C and inhibits progression to S phase". Molecular and Cellular Biology 22 (18): 6509–20. doi:10.1128/MCB.22.18.6509-6520.2002. PMC 135621. PMID 12192049.
• Merkle CJ, Karnitz LM, Henry-Sánchez JT, Chen J (Aug 2003). "Cloning and characterization of hCTF18, hCTF8, and hDCC1. Human homologs of a Saccharomyces cerevisiae complex involved in sister chromatid cohesion establishment". The Journal of Biological Chemistry 278 (32): 30051–6. doi:10.1074/jbc.M211591200. PMID 12766176.
• Bermudez VP, Maniwa Y, Tappin I, Ozato K, Yokomori K, Hurwitz J (Sep 2003). "The alternative Ctf18-Dcc1-Ctf8-replication factor C complex required for sister chromatid cohesion loads proliferating cell nuclear antigen onto DNA". Proceedings of the National Academy of Sciences of the United States of America 100 (18): 10237–42. doi:10.1073/pnas.1434308100. PMC 193545. PMID 12930902.
• Zou L, Liu D, Elledge SJ (Nov 2003). "Replication protein A-mediated recruitment and activation of Rad17 complexes". Proceedings of the National Academy of Sciences of the United States of America 100 (24): 13827–32. doi:10.1073/pnas.2336100100. PMC 283506. PMID 14605214.