RFC1

2EBU, 2K6G, 2K7F - Identifiers
Symbol
RFC1; A1; MHCBFB; PO-GA; RECC1; RFC; RFC140
External ID
OMIM: 102579 MGI: 97891 HomoloGene: 2187 GeneCards: RFC1 Gene
Gene ontology
Function
• DNA binding
• DNA clamp loader activity • • double -stranded DNA binding • • protein binding • • ATP binding • • enzyme activator activity • • protein domain specific binding • • sequence-specific DNA binding
Cell component • • nucleus
• nucleoplasm • DNA replication factor C complex • nucleolus • Golgi apparatus • cell junction • extracellular vesicular exosome
Biological process • • negative regulation of transcription from RNA polymerase II promoter • • mitotic cell cycle • • telomere maintenance via recombination • • telomere maintenance • • ATP catabolic process • • DNA-dependent DNA replication • • DNA strand elongation involved in DNA replication • • DNA repair
• transcription-coupled nucleotide-ex cision repair • • nucleotide-excision repair
• nucleotide-excision repair, DNA gap filling
• transcription, DNA-templated
• telomere maintenance via telomerase
• telomere maintenance via semi-conservative replication
• positive regulation of catalytic activity
• positive regulation of transcription, DNA-templated
Sources: Amigo / QuickGO
RNA expression profile
More information
Orthologists
View
Human - Mouse - Entrez - 5981 - 19687 - Ensembl - ENSG00000035928 - ENSMUSG00000029191 - UniProt - P35251 - P35601 - RefSeq (mRNA)
NM_001204747 - NM_011258 - RefSeq (protein) - NP_001191676 - NP_035388 - Locus (UCSC)
Chr 4: 39.39 - 39.37 Mb
Chr 5:
65.26 - 65.34 Mb
PubMed Search
[1]
[2]
Template: view • discussion • edit
Replication factor C subunit CA 1 - a protein encoded by a human gene RFC1. [1] [2]
Contents
1 Function
2 Interactions
3 Notes
4 Literature
Function
The protein encoded by this gene is a large subunit of replication factor C, which is a subunit of five accessory DNA polymerase proteins. Replication factor C is a DNA-dependent ATPase, which is required for eukaryotic replication and DNA repair. The protein acts as an activator of DNA polymerases, binds to the 3'-ends of the primers, and also contributes to the coordinated synthesis of both strands. It can also play a role in telomere stability. [2]
Interactions
RFC1 has been found to interact with:
BRD4, [3]
HDAC1, [4]
PCNA, [3] [5] [6] [ 7] [8]
RELA [9] and
RFC3. [10] [11] [12]
Notes
↑ 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. PMID 8114700.
↑ 1 2 Entrez Gene: RFC1 replication factor C (activator 1) 1, 145kDa.
↑ 1 2 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. PMID 12192049.
↑ 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.
↑ 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. PMID 8861969.
↑ 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.
↑ 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.
↑ 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.
↑ 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. PMID 12509469.
↑ 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.
↑ 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. PMID 8692848.
↑ 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. PMID 18245774.
References: 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. PMID 7914507.
Bunz F, Kobayashi R, Stillman B (1994). "CDNAs encoding the large subunit of human replication factor C". Proc. Natl. Acad Sci. U.S.A. 90 (23): 11014–8. DOI: 10.1073 / pnas.90.23.11014. PMID 8248204.
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. 1993.13693. PMID 8512577.
Uhlmann F, Cai J, Flores-Rozas H, Dean FB, Finkelstein J, O'Donnell M, Hurwitz J (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. PMID 8692848.
Fotedar R, Mossi R, Fitzgerald P, Rousselle T, Maga G, Brickner H, Messier H, Kasibhatla S, Hübscher U, Fotedar A (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. PMID 8861969. 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. PMID 8954124.
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. PMID 8999859.
Cujec TP, Cho H, Maldonado E, Meyer J, Reinberg D, Peterlin BM (1997). "The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme." Mol. Cell. Biol. 17 (4): 1817–23. PMID 9121429. 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. PMID 9235961.
Rhéaume E, Cohen LY, Uhlmann F, Lazure C, Alam A, Hurwitz J, Sékaly RP, Denis F (1998). "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." EMBO J. 16 (21): 6346-54. DOI: 10.1093 / emboj / 16.21.6346. PMID 9351817.
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. PMID 9488738.
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. PMID 9563011.
Allen BL, Uhlmann F, Gaur LK, Mulder BA, Posey KL, Jones LB, Hardin SH (1998). "DNA recognition properties of the N-terminal DNA binding domain within the large subunit of replication factor C." Nucleic Acids Res. 26 (17): 3877–82. DOI: 10.1093 / nar / 26.17.3877. PMID 9705493.
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. PMID 10353443.
Wang Y, Cortez D, Yazdi P, Neff N, Elledge SJ, Qin J (2000). "BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures." Genes Dev. 14 (8): 927–39. PMID 10783165.
Yazdi PT, Wang Y, Zhao S, Patel N, Lee EY, Qin J (2002). "SMC1 is a downstream effector in the ATM / NBS1 branch of the human S-phase checkpoint." Genes Dev. 16 (5): 571–82. DOI: 10.1101 / gad. 970702. PMID 11877377.
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. PMID 12045192.
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. PMID 12171929.
Maruyama T, Farina A, Dey A, Cheong J, Bermudez VP, Tamura T, Sciortino S, Shuman J, Hurwitz J, Ozato K (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. PMID 12192049.


RFC1

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