The protein encoded by this gene is the large subunit of replication factor C, which is a five subunit DNA polymerase accessory protein. Replication factor C is a DNA-dependent ATPase that is required for eukaryotic DNA replication and repair. The protein acts as an activator of DNA polymerases, binds to the 3' end of primers, and promotes coordinated synthesis of both strands. It also may have a role in telomere stability.[2]
↑Anderson LA, Perkins ND (Aug 2002). "The large subunit of replication factor C interacts with the histone deacetylase, HDAC1". J. Biol. Chem. 277 (33): 29550–4. doi:10.1074/jbc.M200513200. PMID12045192.
↑Mossi R, Jónsson ZO, Allen BL, Hardin SH, Hübscher U (Jan 1997). "Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen". J. Biol. Chem. 272 (3): 1769–76. doi:10.1074/jbc.272.3.1769. PMID8999859.
↑van der Kuip H, Carius B, Haque SJ, Williams BR, Huber C, Fischer T (Apr 1999). "The DNA-binding subunit p140 of replication factor C is upregulated in cycling cells and associates with G1 phase cell cycle regulatory proteins". J. Mol. Med. 77 (4): 386–92. doi:10.1007/s001090050365. PMID10353443.
↑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". J. Biol. Chem. 277 (43): 40362–7. doi:10.1074/jbc.M206194200. PMID12171929.
↑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". J. Biol. Chem. 273 (10): 5979–87. doi:10.1074/jbc.273.10.5979. PMID9488738.
Lu Y, Riegel AT (1994). "The human DNA-binding protein, PO-GA, is homologous to the large subunit of mouse replication factor C: regulation by alternate 3' processing of mRNA". Gene. 145 (2): 261–5. doi:10.1016/0378-1119(94)90017-5. PMID7914507.
Lu Y, Zeft AS, Riegel AT (1993). "Cloning and expression of a novel human DNA binding protein, PO-GA". Biochem. Biophys. Res. Commun. 193 (2): 779–86. doi:10.1006/bbrc.1993.1693. PMID8512577.
Uchiumi F, Ohta T, Tanuma S (1997). "Replication factor C recognizes 5'-phosphate ends of telomeres". Biochem. Biophys. Res. Commun. 229 (1): 310–5. doi:10.1006/bbrc.1996.1798. PMID8954124.
Mossi R, Jónsson ZO, Allen BL, Hardin SH, Hübscher U (1997). "Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen". J. Biol. Chem. 272 (3): 1769–76. doi:10.1074/jbc.272.3.1769. PMID8999859.
Ubeda M, Habener JF (1997). "The large subunit of the DNA replication complex C (DSEB/RF-C140) cleaved and inactivated by caspase-3 (CPP32/YAMA) during Fas-induced apoptosis". J. Biol. Chem. 272 (31): 19562–8. doi:10.1074/jbc.272.31.19562. PMID9235961.
Ellison V, Stillman B (1998). "Reconstitution of recombinant human replication factor C (RFC) and identification of an RFC subcomplex possessing DNA-dependent ATPase activity". J. Biol. Chem. 273 (10): 5979–87. doi:10.1074/jbc.273.10.5979. PMID9488738.
Coll JM, Hickey RJ, Cronkey EA, Jiang HY, Schnaper L, Lee MY, Uitto L, Syvaoja JE, Malkas LH (1998). "Mapping specific protein-protein interactions within the core component of the breast cell DNA synthesome". Oncol. Res. 9 (11–12): 629–39. PMID9563011.
van der Kuip H, Carius B, Haque SJ, Williams BR, Huber C, Fischer T (1999). "The DNA-binding subunit p140 of replication factor C is upregulated in cycling cells and associates with G1 phase cell cycle regulatory proteins". J. Mol. Med. 77 (4): 386–92. doi:10.1007/s001090050365. PMID10353443.
Anderson LA, Perkins ND (2002). "The large subunit of replication factor C interacts with the histone deacetylase, HDAC1". J. Biol. Chem. 277 (33): 29550–4. doi:10.1074/jbc.M200513200. PMID12045192.
Ohta S, Shiomi Y, Sugimoto K, Obuse C, Tsurimoto T (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". J. Biol. Chem. 277 (43): 40362–7. doi:10.1074/jbc.M206194200. PMID12171929.