RFC3

Replication factor C subunit 3 is a protein that in humans is encoded by the RFC3 gene.

RFC3
Identifiers
Aliases	RFC3, RFC38, replication factor C subunit 3
External IDs	OMIM: 600405; MGI: 1916513; HomoloGene: 2188; GeneCards: RFC3; OMA:RFC3 - orthologs
Gene location (Human) Chr. Chromosome 13 (human) Band 13q13.2 Start 33,818,069 bp End 33,966,558 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5|5 G3 Start 151,566,221 bp End 151,574,707 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gonad ventricular zone embryo ganglionic eminence secondary oocyte testicle right adrenal cortex left adrenal gland left adrenal cortex appendix Top expressed in medial ganglionic eminence abdominal wall maxillary prominence mandibular prominence embryo embryo epiblast ventricular zone otic placode endocardial cushion More reference expression data BioGPS More reference expression data
Gene ontology Molecular function single-stranded DNA helicase activity ATPase activity protein binding DNA binding DNA clamp loader activity Cellular component Ctf18 RFC-like complex nucleoplasm DNA replication factor C complex nucleus Biological process nucleotide-excision repair, DNA gap filling DNA synthesis involved in DNA repair error-free translesion synthesis DNA strand elongation involved in DNA replication error-prone translesion synthesis positive regulation of DNA-directed DNA polymerase activity response to organophosphorus translesion synthesis transcription-coupled nucleotide-excision repair nucleotide-excision repair, DNA incision DNA replication nucleotide-excision repair, DNA incision, 5'-to lesion telomere maintenance via semi-conservative replication DNA-dependent DNA replication regulation of signal transduction by p53 class mediator Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5983 69263 Ensembl ENSG00000133119 ENSMUSG00000033970 UniProt P40938 Q8R323 RefSeq (mRNA) NM_002915 NM_181558 NM_027009 RefSeq (protein) NP_002906 NP_853536 NP_081285 Location (UCSC) Chr 13: 33.82 – 33.97 Mb Chr 5: 151.57 – 151.57 Mb PubMed search
Wikidata
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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.

Interactions

RFC3 has been shown to interact with:

• BRD4,
• CHTF18,
• PCNA,
• RFC1, and
• RFC4.

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. Bibcode:1996PNAS...93.6521U. 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. doi:10.1128/MCB.17.4.1817. 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. Bibcode:1999PNAS...96.1869Z. 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. Bibcode:2001PNAS...9811236L. 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. Bibcode:2003PNAS..10010237B. 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. Bibcode:2003PNAS..10013827Z. doi:10.1073/pnas.2336100100. PMC 283506. PMID 14605214.