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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Replication factor C subunit 1''' is a [[protein]] that in humans is encoded by the ''RFC1'' [[gene]].<ref name="pmid8114700">{{cite journal | vauthors = Luckow B, Bunz F, Stillman B, Lichter P, Schütz G | title = Cloning, expression, and chromosomal localization of the 140-kilodalton subunit of replication factor C from mice and humans | journal = Mol Cell Biol | volume = 14 | issue = 3 | pages = 1626–34 | date = Mar 1994 | pmid = 8114700 | pmc = 358521 | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RFC1 replication factor C (activator 1) 1, 145kDa| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5981| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Replication factor C (activator 1) 1, 145kDa
| HGNCid = 9969
| Symbol = RFC1
| AltSymbols =; A1; MGC51786; MHCBFB; PO-GA; RECC1; RFC; RFC140
| OMIM = 102579
| ECnumber = 
| Homologene = 2187
| MGIid = 97891
| GeneAtlas_image1 = PBB_GE_RFC1_208021_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_RFC1_209085_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008047 |text = enzyme activator activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0017111 |text = nucleoside-triphosphatase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005663 |text = DNA replication factor C complex}}
| Process = {{GNF_GO|id=GO:0006261 |text = DNA-dependent DNA replication}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007004 |text = telomere maintenance via telomerase}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5981
    | Hs_Ensembl = ENSG00000035928
    | Hs_RefseqProtein = NP_002904
    | Hs_RefseqmRNA = NM_002913
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 4
    | Hs_GenLoc_start = 38965471
    | Hs_GenLoc_end = 39044390
    | Hs_Uniprot = P35251
    | Mm_EntrezGene = 19687
    | Mm_Ensembl = ENSMUSG00000029191
    | Mm_RefseqmRNA = NM_011258
    | Mm_RefseqProtein = NP_035388
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 65542198
    | Mm_GenLoc_end = 65598665
    | Mm_Uniprot = Q3UJT6
  }}
}}
'''Replication factor C (activator 1) 1, 145kDa''', also known as '''RFC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RFC1 replication factor C (activator 1) 1, 145kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5981| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="entrez" />
{{PBB_Summary
 
| section_title =
==Interactions==
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: RFC1 replication factor C (activator 1) 1, 145kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5981| accessdate = }}</ref>
RFC1 has been shown to [[Protein-protein interaction|interact]] with:
}}
* [[BRD4]],<ref name = pmid12192049>{{cite journal | vauthors = Maruyama T, Farina A, Dey A, Cheong J, Bermudez VP, Tamura T, Sciortino S, Shuman J, Hurwitz J, Ozato K | title = A Mammalian bromodomain protein, brd4, interacts with replication factor C and inhibits progression to S phase | journal = Mol. Cell. Biol. | volume = 22 | issue = 18 | pages = 6509–20 | date = Sep 2002 | pmid = 12192049 | pmc = 135621 | doi =  10.1128/mcb.22.18.6509-6520.2002}}</ref>
* [[HDAC1]],<ref name = pmid12045192>{{cite journal | vauthors = Anderson LA, Perkins ND | title = The large subunit of replication factor C interacts with the histone deacetylase, HDAC1 | journal = J. Biol. Chem. | volume = 277 | issue = 33 | pages = 29550–4 | date = Aug 2002 | pmid = 12045192 | doi = 10.1074/jbc.M200513200 }}</ref>
* [[PCNA]],<ref name = pmid12192049/><ref name = pmid8861969>{{cite journal | vauthors = Fotedar R, Mossi R, Fitzgerald P, Rousselle T, Maga G, Brickner H, Messier H, Kasibhatla S, Hübscher U, Fotedar A | title = A conserved domain of the large subunit of replication factor C binds PCNA and acts like a dominant negative inhibitor of DNA replication in mammalian cells | journal = EMBO J. | volume = 15 | issue = 16 | pages = 4423–33 | date = Aug 1996 | pmid = 8861969 | pmc = 452166 | doi =  }}</ref><ref name = pmid8999859>{{cite journal | vauthors = Mossi R, Jónsson ZO, Allen BL, Hardin SH, Hübscher U | title = Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen | journal = J. Biol. Chem. | volume = 272 | issue = 3 | pages = 1769–76 | date = Jan 1997 | pmid = 8999859 | doi =  10.1074/jbc.272.3.1769}}</ref><ref name = pmid10353443>{{cite journal | vauthors = van der Kuip H, Carius B, Haque SJ, Williams BR, Huber C, Fischer T | title = The DNA-binding subunit p140 of replication factor C is upregulated in cycling cells and associates with G1 phase cell cycle regulatory proteins | journal = J. Mol. Med. | volume = 77 | issue = 4 | pages = 386–92 | date = Apr 1999 | pmid = 10353443 | doi =  10.1007/s001090050365}}</ref><ref name = pmid12171929>{{cite journal | vauthors = Ohta S, Shiomi Y, Sugimoto K, Obuse C, Tsurimoto T | title = 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 | journal = J. Biol. Chem. | volume = 277 | issue = 43 | pages = 40362–7 | date = Oct 2002 | pmid = 12171929 | doi = 10.1074/jbc.M206194200 }}</ref>
* [[RELA]]<ref name = pmid12509469>{{cite journal | vauthors = Anderson LA, Perkins ND | title = Regulation of RelA (p65) function by the large subunit of replication factor C | journal = Mol. Cell. Biol. | volume = 23 | issue = 2 | pages = 721–32 | date = Jan 2003 | pmid = 12509469 | pmc = 151544 | doi =  10.1128/mcb.23.2.721-732.2003}}</ref>  and
* [[RFC3]].<ref name = pmid9488738>{{cite journal | vauthors = Ellison V, Stillman B | title = Reconstitution of recombinant human replication factor C (RFC) and identification of an RFC subcomplex possessing DNA-dependent ATPase activity | journal = J. Biol. Chem. | volume = 273 | issue = 10 | pages = 5979–87 | date = Mar 1998 | pmid = 9488738 | doi =  10.1074/jbc.273.10.5979}}</ref><ref name = pmid8692848>{{cite journal | vauthors = Uhlmann F, Cai J, Flores-Rozas H, Dean FB, Finkelstein J, O'Donnell M, Hurwitz J | title = In vitro reconstitution of human replication factor C from its five subunits | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 93 | issue = 13 | pages = 6521–6 | date = Jun 1996 | pmid = 8692848 | pmc = 39056 | doi = 10.1073/pnas.93.13.6521}}</ref><ref name = pmid18245774>{{cite journal | vauthors = 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 | title = DNA damage-induced ubiquitylation of RFC2 subunit of replication factor C complex | journal = J. Biol. Chem. | volume = 283 | issue = 14 | pages = 9071–9 | date = Apr 2008 | pmid = 18245774 | pmc = 2431014 | doi = 10.1074/jbc.M709835200 }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal | vauthors = Lu Y, Riegel AT | title = 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 | journal = Gene | volume = 145 | issue = 2 | pages = 261–5 | year = 1994 | pmid = 7914507 | doi = 10.1016/0378-1119(94)90017-5 }}
| citations =
*{{cite journal | vauthors = Bunz F, Kobayashi R, Stillman B | title = cDNAs encoding the large subunit of human replication factor C | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 90 | issue = 23 | pages = 11014–8 | year = 1994 | pmid = 8248204 | pmc = 47912 | doi = 10.1073/pnas.90.23.11014 }}
*{{cite journal | author=Lu Y, Riegel AT |title=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. |journal=Gene |volume=145 |issue= 2 |pages= 261-5 |year= 1994 |pmid= 7914507 |doi= }}
*{{cite journal | vauthors = Lu Y, Zeft AS, Riegel AT | title = Cloning and expression of a novel human DNA binding protein, PO-GA | journal = Biochem. Biophys. Res. Commun. | volume = 193 | issue = 2 | pages = 779–86 | year = 1993 | pmid = 8512577 | doi = 10.1006/bbrc.1993.1693 }}
*{{cite journal | author=Luckow B, Bunz F, Stillman B, ''et al.'' |title=Cloning, expression, and chromosomal localization of the 140-kilodalton subunit of replication factor C from mice and humans. |journal=Mol. Cell. Biol. |volume=14 |issue= 3 |pages= 1626-34 |year= 1994 |pmid= 8114700 |doi= }}
*{{cite journal | vauthors = Uhlmann F, Cai J, Flores-Rozas H, Dean FB, Finkelstein J, O'Donnell M, Hurwitz J | title = In vitro reconstitution of human replication factor C from its five subunits | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 93 | issue = 13 | pages = 6521–6 | year = 1996 | pmid = 8692848 | pmc = 39056 | doi = 10.1073/pnas.93.13.6521 }}
*{{cite journal | author=Bunz F, Kobayashi R, Stillman B |title=cDNAs encoding the large subunit of human replication factor C. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 23 |pages= 11014-8 |year= 1994 |pmid= 8248204 |doi= }}
*{{cite journal | vauthors = Fotedar R, Mossi R, Fitzgerald P, Rousselle T, Maga G, Brickner H, Messier H, Kasibhatla S, Hübscher U, Fotedar A | title = A conserved domain of the large subunit of replication factor C binds PCNA and acts like a dominant negative inhibitor of DNA replication in mammalian cells | journal = EMBO J. | volume = 15 | issue = 16 | pages = 4423–33 | year = 1996 | pmid = 8861969 | pmc = 452166 | doi =  }}
*{{cite journal | author=Lu Y, Zeft AS, Riegel AT |title=Cloning and expression of a novel human DNA binding protein, PO-GA. |journal=Biochem. Biophys. Res. Commun. |volume=193 |issue= 2 |pages= 779-86 |year= 1993 |pmid= 8512577 |doi= 10.1006/bbrc.1993.1693 }}
*{{cite journal | vauthors = Uchiumi F, Ohta T, Tanuma S | title = Replication factor C recognizes 5'-phosphate ends of telomeres | journal = Biochem. Biophys. Res. Commun. | volume = 229 | issue = 1 | pages = 310–5 | year = 1997 | pmid = 8954124 | doi = 10.1006/bbrc.1996.1798 }}
*{{cite journal | author=Uhlmann F, Cai J, Flores-Rozas H, ''et al.'' |title=In vitro reconstitution of human replication factor C from its five subunits. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 13 |pages= 6521-6 |year= 1996 |pmid= 8692848 |doi=  }}
*{{cite journal | vauthors = Mossi R, Jónsson ZO, Allen BL, Hardin SH, Hübscher U | title = Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen | journal = J. Biol. Chem. | volume = 272 | issue = 3 | pages = 1769–76 | year = 1997 | pmid = 8999859 | doi = 10.1074/jbc.272.3.1769 }}
*{{cite journal | author=Fotedar R, Mossi R, Fitzgerald P, ''et al.'' |title=A conserved domain of the large subunit of replication factor C binds PCNA and acts like a dominant negative inhibitor of DNA replication in mammalian cells. |journal=EMBO J. |volume=15 |issue= 16 |pages= 4423-33 |year= 1996 |pmid= 8861969 |doi= }}
*{{cite journal | vauthors = Cujec TP, Cho H, Maldonado E, Meyer J, Reinberg D, Peterlin BM | title = The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme | journal = Mol. Cell. Biol. | volume = 17 | issue = 4 | pages = 1817–23 | year = 1997 | pmid = 9121429 | pmc = 232028 | doi =  }}
*{{cite journal | author=Uchiumi F, Ohta T, Tanuma S |title=Replication factor C recognizes 5'-phosphate ends of telomeres. |journal=Biochem. Biophys. Res. Commun. |volume=229 |issue= 1 |pages= 310-5 |year= 1997 |pmid= 8954124 |doi= }}
*{{cite journal | vauthors = Ubeda M, Habener JF | title = The large subunit of the DNA replication complex C (DSEB/RF-C140) cleaved and inactivated by caspase-3 (CPP32/YAMA) during Fas-induced apoptosis | journal = J. Biol. Chem. | volume = 272 | issue = 31 | pages = 19562–8 | year = 1997 | pmid = 9235961 | doi = 10.1074/jbc.272.31.19562 }}
*{{cite journal | author=Mossi R, Jónsson ZO, Allen BL, ''et al.'' |title=Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen. |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 1769-76 |year= 1997 |pmid= 8999859 |doi=  }}
*{{cite journal | vauthors = Rhéaume E, Cohen LY, Uhlmann F, Lazure C, Alam A, Hurwitz J, Sékaly RP, Denis F | title = The large subunit of replication factor C is a substrate for caspase-3 in vitro and is cleaved by a caspase-3-like protease during Fas-mediated apoptosis | journal = EMBO J. | volume = 16 | issue = 21 | pages = 6346–54 | year = 1998 | pmid = 9351817 | pmc = 1170241 | doi = 10.1093/emboj/16.21.6346 }}
*{{cite journal | author=Cujec TP, Cho H, Maldonado E, ''et al.'' |title=The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme. |journal=Mol. Cell. Biol. |volume=17 |issue= 4 |pages= 1817-23 |year= 1997 |pmid= 9121429 |doi= }}
*{{cite journal | vauthors = Ellison V, Stillman B | title = Reconstitution of recombinant human replication factor C (RFC) and identification of an RFC subcomplex possessing DNA-dependent ATPase activity | journal = J. Biol. Chem. | volume = 273 | issue = 10 | pages = 5979–87 | year = 1998 | pmid = 9488738 | doi = 10.1074/jbc.273.10.5979 }}
*{{cite journal | author=Ubeda M, Habener JF |title=The large subunit of the DNA replication complex C (DSEB/RF-C140) cleaved and inactivated by caspase-3 (CPP32/YAMA) during Fas-induced apoptosis. |journal=J. Biol. Chem. |volume=272 |issue= 31 |pages= 19562-8 |year= 1997 |pmid= 9235961 |doi= }}
*{{cite journal | vauthors = Coll JM, Hickey RJ, Cronkey EA, Jiang HY, Schnaper L, Lee MY, Uitto L, Syvaoja JE, Malkas LH | title = Mapping specific protein-protein interactions within the core component of the breast cell DNA synthesome | journal = Oncol. Res. | volume = 9 | issue = 11–12 | pages = 629–39 | year = 1998 | pmid = 9563011 | doi =  }}
*{{cite journal | author=Rhéaume E, Cohen LY, Uhlmann F, ''et al.'' |title=The large subunit of replication factor C is a substrate for caspase-3 in vitro and is cleaved by a caspase-3-like protease during Fas-mediated apoptosis. |journal=EMBO J. |volume=16 |issue= 21 |pages= 6346-54 |year= 1998 |pmid= 9351817 |doi= 10.1093/emboj/16.21.6346 }}
*{{cite journal | vauthors = Allen BL, Uhlmann F, Gaur LK, Mulder BA, Posey KL, Jones LB, Hardin SH | title = DNA recognition properties of the N-terminal DNA binding domain within the large subunit of replication factor C | journal = Nucleic Acids Res. | volume = 26 | issue = 17 | pages = 3877–82 | year = 1998 | pmid = 9705493 | pmc = 147807 | doi = 10.1093/nar/26.17.3877 }}
*{{cite journal | author=Ellison V, Stillman B |title=Reconstitution of recombinant human replication factor C (RFC) and identification of an RFC subcomplex possessing DNA-dependent ATPase activity. |journal=J. Biol. Chem. |volume=273 |issue= 10 |pages= 5979-87 |year= 1998 |pmid= 9488738 |doi=  }}
*{{cite journal | vauthors = van der Kuip H, Carius B, Haque SJ, Williams BR, Huber C, Fischer T | title = The DNA-binding subunit p140 of replication factor C is upregulated in cycling cells and associates with G1 phase cell cycle regulatory proteins | journal = J. Mol. Med. | volume = 77 | issue = 4 | pages = 386–92 | year = 1999 | pmid = 10353443 | doi = 10.1007/s001090050365 }}
*{{cite journal | author=Coll JM, Hickey RJ, Cronkey EA, ''et al.'' |title=Mapping specific protein-protein interactions within the core component of the breast cell DNA synthesome. |journal=Oncol. Res. |volume=9 |issue= 11-12 |pages= 629-39 |year= 1998 |pmid= 9563011 |doi= }}
*{{cite journal | vauthors = Wang Y, Cortez D, Yazdi P, Neff N, Elledge SJ, Qin J | title = BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures | journal = Genes Dev. | volume = 14 | issue = 8 | pages = 927–39 | year = 2000 | pmid = 10783165 | pmc = 316544 | doi =  10.1101/gad.14.8.927}}
*{{cite journal  | author=Allen BL, Uhlmann F, Gaur LK, ''et al.'' |title=DNA recognition properties of the N-terminal DNA binding domain within the large subunit of replication factor C. |journal=Nucleic Acids Res. |volume=26 |issue= 17 |pages= 3877-82 |year= 1998 |pmid= 9705493 |doi= }}
*{{cite journal | vauthors = Yazdi PT, Wang Y, Zhao S, Patel N, Lee EY, Qin J | title = SMC1 is a downstream effector in the ATM/NBS1 branch of the human S-phase checkpoint | journal = Genes Dev. | volume = 16 | issue = 5 | pages = 571–82 | year = 2002 | pmid = 11877377 | pmc = 155356 | doi = 10.1101/gad.970702 }}
*{{cite journal | author=van der Kuip H, Carius B, Haque SJ, ''et al.'' |title=The DNA-binding subunit p140 of replication factor C is upregulated in cycling cells and associates with G1 phase cell cycle regulatory proteins. |journal=J. Mol. Med. |volume=77 |issue= 4 |pages= 386-92 |year= 1999 |pmid= 10353443 |doi=  }}
*{{cite journal | vauthors = Anderson LA, Perkins ND | title = The large subunit of replication factor C interacts with the histone deacetylase, HDAC1 | journal = J. Biol. Chem. | volume = 277 | issue = 33 | pages = 29550–4 | year = 2002 | pmid = 12045192 | doi = 10.1074/jbc.M200513200 }}
*{{cite journal | author=Wang Y, Cortez D, Yazdi P, ''et al.'' |title=BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures. |journal=Genes Dev. |volume=14 |issue= 8 |pages= 927-39 |year= 2000 |pmid= 10783165 |doi= }}
*{{cite journal | vauthors = Ohta S, Shiomi Y, Sugimoto K, Obuse C, Tsurimoto T | title = 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 | journal = J. Biol. Chem. | volume = 277 | issue = 43 | pages = 40362–7 | year = 2002 | pmid = 12171929 | doi = 10.1074/jbc.M206194200 }}
*{{cite journal | author=Yazdi PT, Wang Y, Zhao S, ''et al.'' |title=SMC1 is a downstream effector in the ATM/NBS1 branch of the human S-phase checkpoint. |journal=Genes Dev. |volume=16 |issue= 5 |pages= 571-82 |year= 2002 |pmid= 11877377 |doi= 10.1101/gad.970702 }}
*{{cite journal | vauthors = Maruyama T, Farina A, Dey A, Cheong J, Bermudez VP, Tamura T, Sciortino S, Shuman J, Hurwitz J, Ozato K | title = A Mammalian Bromodomain Protein, Brd4, Interacts with Replication Factor C and Inhibits Progression to S Phase | journal = Mol. Cell. Biol. | volume = 22 | issue = 18 | pages = 6509–20 | year = 2002 | pmid = 12192049 | pmc = 135621 | doi = 10.1128/MCB.22.18.6509-6520.2002 }}
*{{cite journal | author=Anderson LA, Perkins ND |title=The large subunit of replication factor C interacts with the histone deacetylase, HDAC1. |journal=J. Biol. Chem. |volume=277 |issue= 33 |pages= 29550-4 |year= 2002 |pmid= 12045192 |doi= 10.1074/jbc.M200513200 }}
*{{cite journal | author=Ohta S, Shiomi Y, Sugimoto K, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=277 |issue= 43 |pages= 40362-7 |year= 2002 |pmid= 12171929 |doi= 10.1074/jbc.M206194200 }}
*{{cite journal  | author=Maruyama T, Farina A, Dey A, ''et al.'' |title=A Mammalian bromodomain protein, brd4, interacts with replication factor C and inhibits progression to S phase. |journal=Mol. Cell. Biol. |volume=22 |issue= 18 |pages= 6509-20 |year= 2002 |pmid= 12192049 |doi=  }}
}}
{{refend}}
{{refend}}
{{protein-stub}}
{{WikiDoc Sources}}

Revision as of 09:08, 10 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Replication factor C subunit 1 is a protein that in humans is encoded by the RFC1 gene.[1][2]

Function

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]

Interactions

RFC1 has been shown to interact with:

References

  1. ↑ Luckow B, Bunz F, Stillman B, Lichter P, Schütz G (Mar 1994). "Cloning, expression, and chromosomal localization of the 140-kilodalton subunit of replication factor C from mice and humans". Mol Cell Biol. 14 (3): 1626–34. PMC 358521. PMID 8114700.
  2. ↑ 2.0 2.1 "Entrez Gene: RFC1 replication factor C (activator 1) 1, 145kDa".
  3. ↑ 3.0 3.1 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". Mol. Cell. Biol. 22 (18): 6509–20. doi:10.1128/mcb.22.18.6509-6520.2002. PMC 135621. PMID 12192049.
  4. ↑ 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. PMID 12045192.
  5. ↑ Fotedar R, Mossi R, Fitzgerald P, Rousselle T, Maga G, Brickner H, Messier H, Kasibhatla S, Hübscher U, Fotedar A (Aug 1996). "A conserved domain of the large subunit of replication factor C binds PCNA and acts like a dominant negative inhibitor of DNA replication in mammalian cells". EMBO J. 15 (16): 4423–33. PMC 452166. PMID 8861969.
  6. ↑ 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. PMID 8999859.
  7. ↑ 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. PMID 10353443.
  8. ↑ 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. PMID 12171929.
  9. ↑ Anderson LA, Perkins ND (Jan 2003). "Regulation of RelA (p65) function by the large subunit of replication factor C". Mol. Cell. Biol. 23 (2): 721–32. doi:10.1128/mcb.23.2.721-732.2003. PMC 151544. PMID 12509469.
  10. ↑ 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. PMID 9488738.
  11. ↑ 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". Proc. Natl. Acad. Sci. U.S.A. 93 (13): 6521–6. doi:10.1073/pnas.93.13.6521. PMC 39056. PMID 8692848.
  12. ↑ 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". J. Biol. Chem. 283 (14): 9071–9. doi:10.1074/jbc.M709835200. PMC 2431014. PMID 18245774.

Further reading

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