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   27-MAR-2024, entry version 234.
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/";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 235.
DR   ComplexPortal; CPX-415; DNA replication factor C complex.
DR   CORUM; P35251; -.
DR   IntAct; P35251; 60.
DR   MINT; P35251; -.
DR   STRING; 9606.ENSP00000371321; -.
DR   GlyGen; P35251; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P35251; -.
DR   PhosphoSitePlus; P35251; -.
DR   SwissPalm; P35251; -.
DR   BioMuta; RFC1; -.
DR   DMDM; 56757608; -.
DR   EPD; P35251; -.
DR   jPOST; P35251; -.
DR   MassIVE; P35251; -.
DR   MaxQB; P35251; -.
DR   PaxDb; 9606-ENSP00000371321; -.
DR   PeptideAtlas; P35251; -.
DR   ProteomicsDB; 55016; -. [P35251-1]
DR   ProteomicsDB; 55017; -. [P35251-2]
DR   Pumba; P35251; -.
DR   Antibodypedia; 4019; 300 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   AGR; HGNC:9969; -.
DR   CTD; 5981; -.
DR   DisGeNET; 5981; -.
DR   GeneCards; RFC1; -.
DR   GeneReviews; 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; LICNERN; -.
DR   OrthoDB; 6297at2759; -.
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; 307 hits in 1160 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 190 other cell types or tissues.
DR   ExpressionAtlas; P35251; baseline and differential.
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: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:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IDA:ComplexPortal.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:0007004; P:telomere maintenance via telomerase; TAS:ProtInc.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd17752; BRCT_RFC1; 1.
DR   CDD; cd18140; HLD_clamp_RFC; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   InterPro; IPR047854; RFC_lid.
DR   PANTHER; PTHR23389; CHROMOSOME TRANSMISSION FIDELITY FACTOR 18; 1.
DR   PANTHER; PTHR23389:SF36; REPLICATION FACTOR C SUBUNIT 1; 1.
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; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   Genevisible; P35251; HS.
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
//