RFC2

Replication factor C (activator 1) 2, 40kDa
Identifiers
Symbols	RFC2 ; RFC40
External IDs	OMIM: 600404 MGI: 1341868 HomoloGene: 6885 GeneCards: RFC2 Gene
Gene ontology Molecular function • DNA clamp loader activity • protein binding • ATP binding Cellular component • nucleoplasm • DNA replication factor C complex • Golgi apparatus Biological process • mitotic cell cycle • telomere maintenance via recombination • telomere maintenance • 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 • error-free translesion synthesis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5982	19718
Ensembl	ENSG00000049541	ENSMUSG00000023104
UniProt	P35250	Q9WUK4
RefSeq (mRNA)	NM_001278791	NM_020022
RefSeq (protein)	NP_001265720	NP_064406
Location (UCSC)	Chr 7: 74.23 – 74.25 Mb	Chr 5: 134.58 – 134.6 Mb
PubMed search

Replication factor C subunit 2 is a protein that in humans is encoded by the RFC2 gene.^[1][2][3]

Function

The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins, proliferating cell nuclear antigen (PCNA) and replication factor C (RFC). RFC, also called activator 1, is a protein complex consisting of five distinct subunits of 145, 40, 38, 37, and 36.5 kD. This gene encodes the 40 kD subunit, which has been shown to be responsible for binding ATP. Deletion of this gene has been associated with Williams syndrome. Alternatively spliced transcript variants encoding distinct isoforms have been described.^[3]

Interactions

RFC2 has been shown to interact with BRD4,^[4] CHTF18,^[5][6] PCNA,^[7][8][9] RFC4^[7][10] and RFC5.^[7][10]

References

1. Chen M, Pan ZQ, Hurwitz J (Apr 1992). "Sequence and expression in Escherichia coli of the 40-kDa subunit of activator 1 (replication factor C) of HeLa cells". Proceedings of the National Academy of Sciences of the United States of America 89 (7): 2516–20. doi:10.1073/pnas.89.7.2516. PMC 48692. PMID 1313560.
2. 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.
3. "Entrez Gene: RFC2 replication factor C (activator 1) 2, 40kDa".
4. 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.
5. 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.
6. 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.
7. 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.
8. Pan ZQ, Chen M, Hurwitz J (Jan 1993). "The subunits of activator 1 (replication factor C) carry out multiple functions essential for proliferating-cell nuclear antigen-dependent DNA synthesis". Proceedings of the National Academy of Sciences of the United States of America 90 (1): 6–10. doi:10.1073/pnas.90.1.6. PMC 45588. PMID 8093561.
9. 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.
10. Cai J, Yao N, Gibbs E, Finkelstein J, Phillips B, O'Donnell M, Hurwitz J (Sep 1998). "ATP hydrolysis catalyzed by human replication factor C requires participation of multiple subunits". Proceedings of the National Academy of Sciences of the United States of America 95 (20): 11607–12. doi:10.1073/pnas.95.20.11607. PMC 21688. PMID 9751713.

Further reading

• Pan ZQ, Chen M, Hurwitz J (Jan 1993). "The subunits of activator 1 (replication factor C) carry out multiple functions essential for proliferating-cell nuclear antigen-dependent DNA synthesis". Proceedings of the National Academy of Sciences of the United States of America 90 (1): 6–10. doi:10.1073/pnas.90.1.6. PMC 45588. PMID 8093561.
• Peoples R, Perez-Jurado L, Wang YK, Kaplan P, Francke U (Jun 1996). "The gene for replication factor C subunit 2 (RFC2) is within the 7q11.23 Williams syndrome deletion". American Journal of Human Genetics 58 (6): 1370–3. PMC 1915059. PMID 8651315.
• 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.
• Osborne LR, Martindale D, Scherer SW, Shi XM, Huizenga J, Heng HH, Costa T, Pober B, Lew L, Brinkman J, Rommens J, Koop B, Tsui LC (Sep 1996). "Identification of genes from a 500-kb region at 7q11.23 that is commonly deleted in Williams syndrome patients". Genomics 36 (2): 328–36. doi:10.1006/geno.1996.0469. PMID 8812460.
• 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.
• 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.
• Wang Y, Cortez D, Yazdi P, Neff N, Elledge SJ, Qin J (Apr 2000). "BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures". Genes & Development 14 (8): 927–39. doi:10.1101/gad.14.8.927. PMC 316544. PMID 10783165.
• Martindale DW, Wilson MD, Wang D, Burke RD, Chen X, Duronio V, Koop BF (Oct 2000). "Comparative genomic sequence analysis of the Williams syndrome region (LIMK1-RFC2) of human chromosome 7q11.23". Mammalian Genome 11 (10): 890–8. doi:10.1007/s003350010166. PMID 11003705.
• 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.
• Nieborowska-Skorska M, Hoser G, Kossev P, Wasik MA, Skorski T (Jun 2002). "Complementary functions of the antiapoptotic protein A1 and serine/threonine kinase pim-1 in the BCR/ABL-mediated leukemogenesis". Blood 99 (12): 4531–9. doi:10.1182/blood.V99.12.4531. PMID 12036885.
• 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.