RFC1_HUMAN
ID RFC1_HUMAN Reviewed; 1148 AA.
AC P35251; A8K6E7; Q5XKF5; Q6PKU0; Q86V41; Q86V46;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 4.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Replication factor C subunit 1;
DE AltName: Full=Activator 1 140 kDa subunit;
DE Short=A1 140 kDa subunit;
DE AltName: Full=Activator 1 large subunit;
DE AltName: Full=Activator 1 subunit 1;
DE AltName: Full=DNA-binding protein PO-GA;
DE AltName: Full=Replication factor C 140 kDa subunit;
DE Short=RF-C 140 kDa subunit;
DE Short=RFC140;
DE AltName: Full=Replication factor C large subunit;
GN Name=RFC1; Synonyms=RFC140;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 469-480;
RP 571-580 AND 678-700.
RX PubMed=8248204; DOI=10.1073/pnas.90.23.11014;
RA Bunz F., Kobayashi R., Stillman B.;
RT "cDNAs encoding the large subunit of human replication factor C.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11014-11018(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT LEU-613.
RX PubMed=8512577; DOI=10.1006/bbrc.1993.1693;
RA Lu Y., Zeft A.S., Riegel A.T.;
RT "Cloning and expression of a novel human DNA binding protein, PO-GA.";
RL Biochem. Biophys. Res. Commun. 193:779-786(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2), AND VARIANT LEU-613.
RX PubMed=7914507; DOI=10.1016/0378-1119(94)90017-5;
RA Lu Y., Riegel A.T.;
RT "The human DNA-binding protein, PO-GA, is homologous to the large subunit
RT of mouse replication factor C: regulation by alternate 3' processing of
RT mRNA.";
RL Gene 145:261-265(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2), AND VARIANT LEU-613.
RC TISSUE=Hepatoma;
RA Rajavashisth T.B., Tripathi S.;
RT "Molecular cloning of a DNA binding protein from human hepatoma cells.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-598; ASP-692; LYS-955
RP AND LEU-1146.
RG NIEHS SNPs program;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Skin, Testis, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH PCNA.
RX PubMed=8999859; DOI=10.1074/jbc.272.3.1769;
RA Mossi R., Jonsson Z.O., Allen B.L., Hardin S.H., Huebscher U.;
RT "Replication factor C interacts with the C-terminal side of proliferating
RT cell nuclear antigen.";
RL J. Biol. Chem. 272:1769-1776(1997).
RN [10]
RP DNA-BINDING.
RX PubMed=9705493; DOI=10.1093/nar/26.17.3877;
RA Allen B.L., Uhlmann F., Gaur L.K., Mulder B.A., Posey K.L., Jones L.B.,
RA Hardin S.H.;
RT "DNA recognition properties of the N-terminal DNA binding domain within the
RT large subunit of replication factor C.";
RL Nucleic Acids Res. 26:3877-3882(1998).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69 AND SER-71, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-71; SER-73; SER-108;
RP THR-110; SER-156; THR-161; SER-164; SER-173; SER-190; SER-281; SER-283;
RP SER-312; SER-1104 AND SER-1106, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-71; SER-156; THR-161;
RP THR-163; SER-164 AND SER-173, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67; SER-69; SER-71; SER-108;
RP THR-110; SER-156; SER-173; SER-190; SER-312 AND SER-368, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67; SER-69; SER-71; SER-190
RP AND SER-368, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-71; SER-156; THR-161;
RP SER-190 AND SER-1104, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-50, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [23]
RP INVOLVEMENT IN CANVAS.
RX PubMed=31230722; DOI=10.1016/j.ajhg.2019.05.016;
RA Rafehi H., Szmulewicz D.J., Bennett M.F., Sobreira N.L.M., Pope K.,
RA Smith K.R., Gillies G., Diakumis P., Dolzhenko E., Eberle M.A.,
RA Barcina M.G., Breen D.P., Chancellor A.M., Cremer P.D., Delatycki M.B.,
RA Fogel B.L., Hackett A., Halmagyi G.M., Kapetanovic S., Lang A., Mossman S.,
RA Mu W., Patrikios P., Perlman S.L., Rosemergy I., Storey E., Watson S.R.D.,
RA Wilson M.A., Zee D.S., Valle D., Amor D.J., Bahlo M., Lockhart P.J.;
RT "Bioinformatics-Based Identification of Expanded Repeats: A Non-reference
RT Intronic Pentamer Expansion in RFC1 Causes CANVAS.";
RL Am. J. Hum. Genet. 105:151-165(2019).
RN [24]
RP INVOLVEMENT IN CANVAS.
RX PubMed=30926972; DOI=10.1038/s41588-019-0372-4;
RA Cortese A., Simone R., Sullivan R., Vandrovcova J., Tariq H., Yau W.Y.,
RA Humphrey J., Jaunmuktane Z., Sivakumar P., Polke J., Ilyas M.,
RA Tribollet E., Tomaselli P.J., Devigili G., Callegari I., Versino M.,
RA Salpietro V., Efthymiou S., Kaski D., Wood N.W., Andrade N.S., Buglo E.,
RA Rebelo A., Rossor A.M., Bronstein A., Fratta P., Marques W.J., Zuechner S.,
RA Reilly M.M., Houlden H.;
RT "Biallelic expansion of an intronic repeat in RFC1 is a common cause of
RT late-onset ataxia.";
RL Nat. Genet. 51:649-658(2019).
RN [25]
RP STRUCTURE BY NMR OF 392-496.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the BRCT domain from human replication factor C
RT large subunit 1.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: The elongation of primed DNA templates by DNA polymerase
CC delta and epsilon requires the action of the accessory proteins PCNA
CC and activator 1. This subunit binds to the primer-template junction.
CC Binds the PO-B transcription element as well as other GA rich DNA
CC sequences. Could play a role in DNA transcription regulation as well as
CC DNA replication and/or repair. Can bind single- or double-stranded DNA.
CC {ECO:0000269|PubMed:8999859}.
CC -!- FUNCTION: Interacts with C-terminus of PCNA. 5' phosphate residue is
CC required for binding of the N-terminal DNA-binding domain to duplex
CC DNA, suggesting a role in recognition of non-primer template DNA
CC structures during replication and/or repair.
CC {ECO:0000269|PubMed:8999859}.
CC -!- SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can
CC form a complex either with RFC1 or with RAD17. The former interacts
CC with PCNA in the presence of ATP, while the latter has ATPase activity
CC but is not stimulated by PCNA. {ECO:0000269|PubMed:8999859}.
CC -!- INTERACTION:
CC P35251; P35250: RFC2; NbExp=4; IntAct=EBI-476616, EBI-476409;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P35251-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35251-2; Sequence=VSP_008443;
CC -!- TISSUE SPECIFICITY: Wide tissue distribution. Undetectable in placental
CC tissue.
CC -!- DISEASE: Cerebellar ataxia, neuropathy, and vestibular areflexia
CC syndrome (CANVAS) [MIM:614575]: An autosomal recessive neurologic
CC disease characterized by imbalance, cerebellar ataxia, impaired
CC vestibular function, and non-length-dependent sensory deficit.
CC {ECO:0000269|PubMed:30926972, ECO:0000269|PubMed:31230722}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. The disease is caused by intronic AAGGG repeat expansions in
CC intron 2. {ECO:0000269|PubMed:30926972, ECO:0000269|PubMed:31230722}.
CC -!- MISCELLANEOUS: [Isoform 2]: Alternative use of an acceptor site.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rfc1/";
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DR EMBL; L23320; AAA16121.1; -; mRNA.
DR EMBL; Z22642; CAA80355.1; -; mRNA.
DR EMBL; AF040250; AAB99788.1; -; mRNA.
DR EMBL; AY600371; AAS94325.1; -; Genomic_DNA.
DR EMBL; AK291612; BAF84301.1; -; mRNA.
DR EMBL; CH471069; EAW92923.1; -; Genomic_DNA.
DR EMBL; BC035297; AAH35297.1; -; mRNA.
DR EMBL; BC051751; AAH51751.1; -; mRNA.
DR EMBL; BC051786; AAH51786.1; -; mRNA.
DR CCDS; CCDS3450.1; -. [P35251-2]
DR CCDS; CCDS56329.1; -. [P35251-1]
DR PIR; A49651; A49651.
DR PIR; JN0599; JN0599.
DR RefSeq; NP_001191676.1; NM_001204747.1. [P35251-1]
DR RefSeq; NP_002904.3; NM_002913.4. [P35251-2]
DR PDB; 2EBU; NMR; -; A=392-496.
DR PDB; 2K6G; NMR; -; A=375-480.
DR PDB; 2K7F; NMR; -; A=375-480.
DR PDB; 6VVO; EM; 3.40 A; A=556-1148.
DR PDBsum; 2EBU; -.
DR PDBsum; 2K6G; -.
DR PDBsum; 2K7F; -.
DR PDBsum; 6VVO; -.
DR AlphaFoldDB; P35251; -.
DR BMRB; P35251; -.
DR SMR; P35251; -.
DR BioGRID; 111913; 188.
DR ComplexPortal; CPX-415; DNA replication factor C complex.
DR CORUM; P35251; -.
DR IntAct; P35251; 57.
DR MINT; P35251; -.
DR STRING; 9606.ENSP00000371321; -.
DR iPTMnet; P35251; -.
DR PhosphoSitePlus; P35251; -.
DR BioMuta; RFC1; -.
DR DMDM; 56757608; -.
DR EPD; P35251; -.
DR jPOST; P35251; -.
DR MassIVE; P35251; -.
DR MaxQB; P35251; -.
DR PaxDb; P35251; -.
DR PeptideAtlas; P35251; -.
DR PRIDE; P35251; -.
DR ProteomicsDB; 55016; -. [P35251-1]
DR ProteomicsDB; 55017; -. [P35251-2]
DR Antibodypedia; 4019; 267 antibodies from 31 providers.
DR DNASU; 5981; -.
DR Ensembl; ENST00000349703.7; ENSP00000261424.4; ENSG00000035928.17. [P35251-2]
DR Ensembl; ENST00000381897.5; ENSP00000371321.1; ENSG00000035928.17. [P35251-1]
DR GeneID; 5981; -.
DR KEGG; hsa:5981; -.
DR MANE-Select; ENST00000349703.7; ENSP00000261424.4; NM_002913.5; NP_002904.3. [P35251-2]
DR UCSC; uc003gtx.3; human. [P35251-1]
DR CTD; 5981; -.
DR DisGeNET; 5981; -.
DR GeneCards; RFC1; -.
DR HGNC; HGNC:9969; RFC1.
DR HPA; ENSG00000035928; Low tissue specificity.
DR MalaCards; RFC1; -.
DR MIM; 102579; gene.
DR MIM; 614575; phenotype.
DR neXtProt; NX_P35251; -.
DR OpenTargets; ENSG00000035928; -.
DR Orphanet; 504476; Cerebellar ataxia with neuropathy and bilateral vestibular areflexia syndrome.
DR PharmGKB; PA34338; -.
DR VEuPathDB; HostDB:ENSG00000035928; -.
DR eggNOG; KOG1968; Eukaryota.
DR GeneTree; ENSGT00730000111066; -.
DR HOGENOM; CLU_003574_0_0_1; -.
DR InParanoid; P35251; -.
DR OMA; PVGAENC; -.
DR OrthoDB; 307415at2759; -.
DR PhylomeDB; P35251; -.
DR TreeFam; TF105722; -.
DR BRENDA; 3.6.4.B8; 2681.
DR PathwayCommons; P35251; -.
DR Reactome; R-HSA-110312; Translesion synthesis by REV1.
DR Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-HSA-110320; Translesion Synthesis by POLH.
DR Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-HSA-5655862; Translesion synthesis by POLK.
DR Reactome; R-HSA-5656121; Translesion synthesis by POLI.
DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-69091; Polymerase switching.
DR SignaLink; P35251; -.
DR SIGNOR; P35251; -.
DR BioGRID-ORCS; 5981; 299 hits in 1084 CRISPR screens.
DR ChiTaRS; RFC1; human.
DR EvolutionaryTrace; P35251; -.
DR GeneWiki; RFC1; -.
DR GenomeRNAi; 5981; -.
DR Pharos; P35251; Tbio.
DR PRO; PR:P35251; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P35251; protein.
DR Bgee; ENSG00000035928; Expressed in calcaneal tendon and 189 other tissues.
DR ExpressionAtlas; P35251; baseline and differential.
DR Genevisible; P35251; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005663; C:DNA replication factor C complex; IDA:UniProtKB.
DR GO; GO:0031391; C:Elg1 RFC-like complex; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; TAS:ProtInc.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003689; F:DNA clamp loader activity; IEA:InterPro.
DR GO; GO:0061860; F:DNA clamp unloader activity; IMP:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0090618; P:DNA clamp unloading; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006261; P:DNA-templated DNA replication; TAS:ProtInc.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0007004; P:telomere maintenance via telomerase; TAS:ProtInc.
DR Gene3D; 3.40.50.10190; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR013725; DNA_replication_fac_RFC1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012178; RFC1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF08519; RFC1; 1.
DR PIRSF; PIRSF036578; RFC1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; ATP-binding;
KW Direct protein sequencing; DNA replication; DNA-binding; Isopeptide bond;
KW Neuropathy; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..1148
FT /note="Replication factor C subunit 1"
FT /id="PRO_0000121772"
FT DOMAIN 402..492
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 46..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1120..1124
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 46..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1110
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 650..657
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 67
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 163
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35601"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35601"
FT MOD_RES 1104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 50
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364"
FT VAR_SEQ 630
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8512577"
FT /id="VSP_008443"
FT VARIANT 598
FT /note="I -> V (in dbSNP:rs2066791)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_014860"
FT VARIANT 613
FT /note="R -> L (in dbSNP:rs1057747)"
FT /evidence="ECO:0000269|PubMed:7914507,
FT ECO:0000269|PubMed:8512577, ECO:0000269|Ref.4"
FT /id="VAR_016986"
FT VARIANT 692
FT /note="E -> D (in dbSNP:rs11932767)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020657"
FT VARIANT 955
FT /note="Q -> K (in dbSNP:rs17335452)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020658"
FT VARIANT 1146
FT /note="S -> L (in dbSNP:rs17288828)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020659"
FT CONFLICT 326
FT /note="E -> K (in Ref. 1; AAA16121)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="S -> N (in Ref. 8; AAH51786)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="A -> S (in Ref. 2, 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="G -> N (in Ref. 2, 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="A -> R (in Ref. 2, 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 1076
FT /note="S -> A (in Ref. 2, 3 and 4)"
FT /evidence="ECO:0000305"
FT HELIX 380..386
FT /evidence="ECO:0007829|PDB:2K6G"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:2K6G"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:2EBU"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:2EBU"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:2EBU"
FT HELIX 423..432
FT /evidence="ECO:0007829|PDB:2EBU"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:2K6G"
FT STRAND 447..450
FT /evidence="ECO:0007829|PDB:2EBU"
FT HELIX 457..465
FT /evidence="ECO:0007829|PDB:2EBU"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:2EBU"
FT HELIX 472..481
FT /evidence="ECO:0007829|PDB:2EBU"
FT HELIX 586..589
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 607..616
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 645..650
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 657..667
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 671..675
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 683..689
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 691..694
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 699..701
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 715..719
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 722..724
FT /evidence="ECO:0007829|PDB:6VVO"
FT TURN 729..732
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 733..742
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 748..751
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 758..761
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 764..766
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 767..771
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 777..791
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 797..806
FT /evidence="ECO:0007829|PDB:6VVO"
FT TURN 807..809
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 811..826
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 848..854
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 859..861
FT /evidence="ECO:0007829|PDB:6VVO"
FT TURN 862..864
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 867..875
FT /evidence="ECO:0007829|PDB:6VVO"
FT TURN 878..880
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 881..888
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 889..891
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 901..927
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 934..941
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 944..948
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 962..981
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 990..992
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 993..1012
FT /evidence="ECO:0007829|PDB:6VVO"
FT TURN 1014..1016
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 1017..1027
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 1032..1039
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 1057..1065
FT /evidence="ECO:0007829|PDB:6VVO"
SQ SEQUENCE 1148 AA; 128255 MW; 485F0332FB56819B CRC64;
MDIRKFFGVI PSGKKLVSET VKKNEKTKSD EETLKAKKGI KEIKVNSSRK EDDFKQKQPS
KKKRIIYDSD SESEETLQVK NAKKPPEKLP VSSKPGKISR QDPVTYISET DEEDDFMCKK
AASKSKENGR STNSHLGTSN MKKNEENTKT KNKPLSPIKL TPTSVLDYFG TGSVQRSNKK
MVASKRKELS QNTDESGLND EAIAKQLQLD EDAELERQLH EDEEFARTLA MLDEEPKTKK
ARKDTEAGET FSSVQANLSK AEKHKYPHKV KTAQVSDERK SYSPRKQSKY ESSKESQQHS
KSSADKIGEV SSPKASSKLA IMKRKEESSY KEIEPVASKR KENAIKLKGE TKTPKKTKSS
PAKKESVSPE DSEKKRTNYQ AYRSYLNREG PKALGSKEIP KGAENCLEGL IFVITGVLES
IERDEAKSLI ERYGGKVTGN VSKKTNYLVM GRDSGQSKSD KAAALGTKII DEDGLLNLIR
TMPGKKSKYE IAVETEMKKE SKLERTPQKN VQGKRKISPS KKESESKKSR PTSKRDSLAK
TIKKETDVFW KSLDFKEQVA EETSGDSKAR NLADDSSENK VENLLWVDKY KPTSLKTIIG
QQGDQSCANK LLRWLRNWQK SSSEDKKHAA KFGKFSGKDD GSSFKAALLS GPPGVGKTTT
ASLVCQELGY SYVELNASDT RSKSSLKAIV AESLNNTSIK GFYSNGAASS VSTKHALIMD
EVDGMAGNED RGGIQELIGL IKHTKIPIIC MCNDRNHPKI RSLVHYCFDL RFQRPRVEQI
KGAMMSIAFK EGLKIPPPAM NEIILGANQD IRQVLHNLSM WCARSKALTY DQAKADSHRA
KKDIKMGPFD VARKVFAAGE ETAHMSLVDK SDLFFHDYSI APLFVQENYI HVKPVAAGGD
MKKHLMLLSR AADSICDGDL VDSQIRSKQN WSLLPAQAIY ASVLPGELMR GYMTQFPTFP
SWLGKHSSTG KHDRIVQDLA LHMSLRTYSS KRTVNMDYLS LLRDALVQPL TSQGVDGVQD
VVALMDTYYL MKEDFENIME ISSWGGKPSP FSKLDPKVKA AFTRAYNKEA HLTPYSLQAI
KASRHSTSPS LDSEYNEELN EDDSQSDEKD QDAIETDAMI KKKTKSSKPS KPEKDKEPRK
GKGKSSKK
