ID RFC5_HUMAN Reviewed; 340 AA. AC P40937; A8MZ62; B3KSX8; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 04-NOV-2026, entry version 227. DE RecName: Full=Replication factor C subunit 5; DE AltName: Full=Activator 1 36 kDa subunit; DE Short=A1 36 kDa subunit; DE AltName: Full=Activator 1 subunit 5; DE AltName: Full=Replication factor C 36 kDa subunit; DE Short=RF-C 36 kDa subunit; DE Short=RFC36; GN Name=RFC5; 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). RX PubMed=8441605; DOI=10.1093/nar/21.1.1; RA O'Donnell M., Onrust R., Dean F.B., Chen M., Hurwitz J.; RT "Homology in accessory proteins of replicative polymerases -- E. coli to RT humans."; RL Nucleic Acids Res. 21:1-3(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-13. RG NIEHS SNPs program; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Amygdala; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle, and Skin; 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 [6] 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 [7] RP FUNCTION, AND SUBUNIT. RX PubMed=9488738; DOI=10.1074/jbc.273.10.5979; RA Ellison V., Stillman B.; RT "Reconstitution of recombinant human replication factor C (RFC) and RT identification of an RFC subcomplex possessing DNA-dependent ATPase RT activity."; RL J. Biol. Chem. 273:5979-5987(1998). RN [8] RP INTERACTION WITH RAD17. RX PubMed=11572977; DOI=10.1073/pnas.201373498; RA Lindsey-Boltz L.A., Bermudez V.P., Hurwitz J., Sancar A.; RT "Purification and characterization of human DNA damage checkpoint Rad RT complexes."; RL Proc. Natl. Acad. Sci. U.S.A. 98:11236-11241(2001). RN [9] 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 [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [11] RP IDENTIFICATION BY 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). CC -!- FUNCTION: Subunit of the replication factor C (RFC) complex which acts CC during elongation of primed DNA templates by DNA polymerases delta and CC epsilon, and is necessary for ATP-dependent loading of proliferating CC cell nuclear antigen (PCNA) onto primed DNA. CC {ECO:0000269|PubMed:8999859, ECO:0000269|PubMed:9488738}. CC -!- SUBUNIT: Subunit of the RFC complex, an heteropentameric complex CC consisting of a large subunit RFC1 and four small subunits RFC2, RFC3, CC RFC4 and RFC5; the RFC complex interacts with PCNA (PubMed:8999859, CC PubMed:9488738). Forms an heterotetrameric complex with RFC2, RFC3 and CC RFC4; this complex has ATPase activity but is not stimulated by PCNA CC (PubMed:9488738). The heterotetramer of subunits RFC2, RFC3, RFC4 and CC RFC5 interacts with RAD17 (PubMed:11572977). CC {ECO:0000269|PubMed:11572977, ECO:0000269|PubMed:8999859, CC ECO:0000269|PubMed:9488738}. CC -!- INTERACTION: CC P40937; Q03989: ARID5A; NbExp=3; IntAct=EBI-712376, EBI-948603; CC P40937; Q13490: BIRC2; NbExp=3; IntAct=EBI-712376, EBI-514538; CC P40937; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-712376, EBI-2548012; CC P40937; P24863: CCNC; NbExp=5; IntAct=EBI-712376, EBI-395261; CC P40937; A8MTA8-2: CIMIP2B; NbExp=3; IntAct=EBI-712376, EBI-12160437; CC P40937; Q96D03: DDIT4L; NbExp=5; IntAct=EBI-712376, EBI-742054; CC P40937; A0A0C4DGQ7: EML2; NbExp=3; IntAct=EBI-712376, EBI-12112376; CC P40937; Q96B26: EXOSC8; NbExp=3; IntAct=EBI-712376, EBI-371922; CC P40937; O76011: KRT34; NbExp=3; IntAct=EBI-712376, EBI-1047093; CC P40937; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-712376, EBI-11742507; CC P40937; Q9HAF1: MEAF6; NbExp=3; IntAct=EBI-712376, EBI-399266; CC P40937; O15049: N4BP3; NbExp=5; IntAct=EBI-712376, EBI-2512055; CC P40937; Q15742: NAB2; NbExp=8; IntAct=EBI-712376, EBI-8641936; CC P40937; Q13285: NR5A1; NbExp=3; IntAct=EBI-712376, EBI-874629; CC P40937; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-712376, EBI-10293968; CC P40937; P35249: RFC4; NbExp=26; IntAct=EBI-712376, EBI-476655; CC P40937; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-712376, EBI-745958; CC P40937; O00635: TRIM38; NbExp=8; IntAct=EBI-712376, EBI-2130415; CC P40937; Q99598: TSNAX; NbExp=3; IntAct=EBI-712376, EBI-21353855; CC P40937; Q6GPH4: XAF1; NbExp=3; IntAct=EBI-712376, EBI-2815120; CC P40937; P98170: XIAP; NbExp=9; IntAct=EBI-712376, EBI-517127; CC P40937; P17023: ZNF19; NbExp=5; IntAct=EBI-712376, EBI-12884200; CC P40937; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-712376, EBI-743265; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P40937-1; Sequence=Displayed; CC Name=2; CC IsoId=P40937-2; Sequence=VSP_043067; CC -!- SIMILARITY: Belongs to the activator 1 small subunits family. CC {ECO:0000305}. 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; L07540; AAB09784.1; -; mRNA. DR EMBL; AY254323; AAO63493.1; -; Genomic_DNA. DR EMBL; AK094575; BAG52890.1; -; mRNA. DR EMBL; AC131159; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001866; AAH01866.1; -; mRNA. DR EMBL; BC013961; AAH13961.1; -; mRNA. DR CCDS; CCDS41843.2; -. [P40937-2] DR CCDS; CCDS9185.1; -. [P40937-1] DR RefSeq; NP_001123584.1; NM_001130112.4. DR RefSeq; NP_001123585.1; NM_001130113.3. [P40937-2] DR RefSeq; NP_031396.1; NM_007370.7. [P40937-1] DR RefSeq; NP_853556.2; NM_181578.5. [P40937-2] DR PDB; 6VVO; EM; 3.40 A; C=1-340. DR PDB; 7Z6H; EM; 3.59 A; G=2-340. DR PDB; 8UI7; EM; 4.20 A; C=1-340. DR PDB; 8UI8; EM; 3.10 A; C=1-340. DR PDB; 8UI9; EM; 3.50 A; C=1-340. DR PDB; 8UII; EM; 3.04 A; C=1-340. DR PDB; 8UMT; EM; 3.33 A; C=1-340. DR PDB; 8UMU; EM; 3.16 A; C=1-340. DR PDB; 8UMV; EM; 2.75 A; C=1-340. DR PDB; 8UMW; EM; 2.93 A; C=1-340. DR PDB; 8UMY; EM; 2.83 A; C=1-340. DR PDB; 8UN0; EM; 3.00 A; C=1-340. DR PDB; 8UNJ; EM; 3.35 A; C=1-340. DR PDB; 8ZWO; EM; 2.99 A; C=1-340. DR PDB; 9IIN; EM; 3.20 A; C=1-340. DR PDB; 9UIQ; EM; 3.20 A; C=19-338. DR AlphaFoldDB; P40937; -. DR EMDB; EMD-14527; -. DR EMDB; EMD-21405; -. DR EMDB; EMD-42287; -. DR EMDB; EMD-42288; -. DR EMDB; EMD-42289; -. DR EMDB; EMD-42295; -. DR EMDB; EMD-42383; -. DR EMDB; EMD-42384; -. DR EMDB; EMD-42385; -. DR EMDB; EMD-42386; -. DR EMDB; EMD-42388; -. DR EMDB; EMD-42389; -. DR EMDB; EMD-42406; -. DR EMDB; EMD-60534; -. DR EMDB; EMD-60598; -. DR EMDB; EMD-64201; -. DR SMR; P40937; -. DR BioGRID; 111917; 233. DR ComplexPortal; CPX-26030; DNA replication factor C complex, ATAD5 variant. DR ComplexPortal; CPX-26356; DNA replication factor C complex, CHTF18 variant. DR ComplexPortal; CPX-415; DNA replication factor C complex, RFC1 variant. DR ComplexPortal; CPX-7931; DNA replication factor C complex, RAD17 variant. DR CORUM; P40937; -. DR DIP; DIP-36433N; -. DR FunCoup; P40937; 2494. DR IntAct; P40937; 124. DR NDEx; IQUERY-CP-RFC5; 11 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000408295; -. DR BindingDB; P40937; -. DR ChEMBL; CHEMBL4296000; -. DR GlyCosmos; P40937; 1 site, 1 glycan. DR GlyGen; P40937; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; P40937; -. DR MetOSite; P40937; -. DR PhosphoSitePlus; P40937; -. DR BioMuta; RFC5; -. DR DMDM; 728777; -. DR jPOST; P40937; -. DR MassIVE; P40937; -. DR PaxDb; 9606-ENSP00000408295; -. DR PeptideAtlas; P40937; -. DR ProteomicsDB; 55389; -. [P40937-1] DR ProteomicsDB; 55390; -. [P40937-2] DR Pumba; P40937; -. DR Antibodypedia; 18857; 141 antibodies from 32 providers. DR DNASU; 5985; -. DR Ensembl; ENST00000392542.6; ENSP00000376325.2; ENSG00000111445.15. [P40937-2] DR Ensembl; ENST00000454402.7; ENSP00000408295.2; ENSG00000111445.15. [P40937-1] DR Ensembl; ENST00000900837.1; ENSP00000570896.1; ENSG00000111445.15. [P40937-1] DR GeneID; 5985; -. DR KEGG; hsa:5985; -. DR MANE-Select; ENST00000454402.7; ENSP00000408295.2; NM_007370.7; NP_031396.1. DR UCSC; uc001twq.4; human. [P40937-1] DR AGR; HGNC:9973; -. DR ClinPGx; PA34342; -. DR CTD; 5985; -. DR DisGeNET; 5985; -. DR GeneCards; RFC5; -. DR HGNC; HGNC:9973; RFC5. DR HPA; ENSG00000111445; Low tissue specificity. DR MIM; 600407; gene. DR OpenTargets; ENSG00000111445; -. DR VEuPathDB; HostDB:ENSG00000111445; -. DR eggNOG; KOG0990; Eukaryota. DR GeneTree; ENSGT00550000075072; -. DR HOGENOM; CLU_042324_2_0_1; -. DR InParanoid; P40937; -. DR OMA; AADHPYD; -. DR OrthoDB; 10254700at2759; -. DR PAN-GO; P40937; 5 GO annotations based on evolutionary models. DR PhylomeDB; P40937; -. DR BRENDA; 3.6.4.B8; 2681. DR PathwayCommons; P40937; -. 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-176187; Activation of ATR in response to replication stress. 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-5685938; HDR through Single Strand Annealing (SSA). DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR). DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends. DR Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange. 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-6804756; Regulation of TP53 Activity through Phosphorylation. DR Reactome; R-HSA-69091; Polymerase switching. DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint. DR Reactome; R-HSA-9709570; Impaired BRCA2 binding to RAD51. DR Reactome; R-HSA-9968295; Somatic hypermutation of immunoglobulin genes by error-prone mismatch repair (MMR). DR Reactome; R-HSA-9968297; Somatic hypermutation of immunoglobulin genes by error-prone base excision repair (BER). DR SignaLink; P40937; -. DR SIGNOR; P40937; -. DR Agora; ENSG00000111445; -. DR BioGRID-ORCS; 5985; 811 hits in 1165 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR ChiTaRS; RFC5; human. DR GeneWiki; RFC5; -. DR GenomeRNAi; 5985; -. DR Pharos; P40937; Tbio. DR PRO; PR:P40937; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P40937; protein. DR Bgee; ENSG00000111445; Expressed in pons and 220 other cell types or tissues. DR ExpressionAtlas; P40937; baseline and differential. DR GO; GO:0031390; C:Ctf18 RFC-like complex; IDA:UniProtKB. DR GO; GO:0005663; C:DNA replication factor C complex; IDA:UniProtKB. DR GO; GO:0031391; C:Elg1 RFC-like complex; NAS:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0031389; C:Rad17 RFC-like complex; IPI:ComplexPortal. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0019899; F:enzyme binding; NAS:UniProtKB. DR GO; GO:0006281; P:DNA repair; IBA:GO_Central. DR GO; GO:0006260; P:DNA replication; NAS:UniProtKB. DR GO; GO:0000076; P:DNA replication checkpoint signaling; NAS:ComplexPortal. DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:ComplexPortal. DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IDA:UniProtKB. DR CDD; cd00009; AAA; 1. DR CDD; cd18140; HLD_clamp_RFC; 1. DR FunFam; 3.40.50.300:FF:001637; replication factor C subunit 2 isoform X2; 1. DR FunFam; 1.10.8.60:FF:000028; Replication factor C subunit 5; 1. DR FunFam; 1.20.272.10:FF:000004; Replication factor C subunit 5; 1. DR FunFam; 3.40.50.300:FF:001987; replication factor C subunit 5 isoform X2; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 1.20.272.10; -; 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; IPR008921; DNA_pol3_clamp-load_cplx_C. DR InterPro; IPR050238; DNA_Rep/Repair_Clamp_Loader. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR013748; Rep_factorC_C. DR InterPro; IPR047854; RFC_lid. DR NCBIfam; NF001679; PRK00440.1; 1. DR PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1. DR PANTHER; PTHR11669:SF9; REPLICATION FACTOR C SUBUNIT 5; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF21960; RCF1-5-like_lid; 1. DR Pfam; PF08542; Rep_fac_C; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW DNA replication; Nucleotide-binding; Nucleus; Proteomics identification; KW Reference proteome. FT CHAIN 1..340 FT /note="Replication factor C subunit 5" FT /id="PRO_0000121751" FT BINDING 60..67 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT VAR_SEQ 1..22 FT /note="METSALKQQEQPAATKIRNLPW -> M (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043067" FT VARIANT 13 FT /note="A -> T (in dbSNP:rs5745796)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_018749" FT HELIX 5..10 FT /evidence="ECO:0007829|PDB:8UI8" FT STRAND 16..18 FT /evidence="ECO:0007829|PDB:8UI8" FT HELIX 22..25 FT /evidence="ECO:0007829|PDB:8UMV" FT HELIX 31..33 FT /evidence="ECO:0007829|PDB:8UMY" FT HELIX 38..49 FT /evidence="ECO:0007829|PDB:8UMV" FT STRAND 56..59 FT /evidence="ECO:0007829|PDB:8UMV" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:8UMV" FT HELIX 67..77 FT /evidence="ECO:0007829|PDB:8UMV" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:8UMT" FT HELIX 83..86 FT /evidence="ECO:0007829|PDB:8UMV" FT STRAND 87..90 FT /evidence="ECO:0007829|PDB:8UMV" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:8ZWO" FT STRAND 96..98 FT /evidence="ECO:0007829|PDB:8UI8" FT HELIX 101..105 FT /evidence="ECO:0007829|PDB:8UMV" FT HELIX 106..110 FT /evidence="ECO:0007829|PDB:8UMV" FT STRAND 114..116 FT /evidence="ECO:0007829|PDB:8UMV" FT STRAND 120..124 FT /evidence="ECO:0007829|PDB:8UMV" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:8UMV" FT HELIX 132..144 FT /evidence="ECO:0007829|PDB:8UMV" FT TURN 145..148 FT /evidence="ECO:0007829|PDB:8UMV" FT STRAND 149..156 FT /evidence="ECO:0007829|PDB:8UMV" FT HELIX 158..160 FT /evidence="ECO:0007829|PDB:8UMV" FT HELIX 163..168 FT /evidence="ECO:0007829|PDB:8UMV" FT STRAND 169..173 FT /evidence="ECO:0007829|PDB:8UMV" FT HELIX 175..178 FT /evidence="ECO:0007829|PDB:8UII" FT HELIX 179..193 FT /evidence="ECO:0007829|PDB:8UMV" FT HELIX 199..209 FT /evidence="ECO:0007829|PDB:8UMV" FT HELIX 213..226 FT /evidence="ECO:0007829|PDB:8UMV" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:8UMV" FT HELIX 232..239 FT /evidence="ECO:0007829|PDB:8UMV" FT HELIX 244..256 FT /evidence="ECO:0007829|PDB:8UMV" FT HELIX 259..273 FT /evidence="ECO:0007829|PDB:8UMV" FT HELIX 277..288 FT /evidence="ECO:0007829|PDB:8UMV" FT HELIX 295..311 FT /evidence="ECO:0007829|PDB:8UMV" FT TURN 313..315 FT /evidence="ECO:0007829|PDB:8UMU" FT HELIX 318..339 FT /evidence="ECO:0007829|PDB:8UMV" SQ SEQUENCE 340 AA; 38497 MW; E31E7B8C79933BCE CRC64; METSALKQQE QPAATKIRNL PWVEKYRPQT LNDLISHQDI LSTIQKFINE DRLPHLLLYG PPGTGKTSTI LACAKQLYKD KEFGSMVLEL NASDDRGIDI IRGPILSFAS TRTIFKKGFK LVILDEADAM TQDAQNALRR VIEKFTENTR FCLICNYLSK IIPALQSRCT RFRFGPLTPE LMVPRLEHVV EEEKVDISED GMKALVTLSS GDMRRALNIL QSTNMAFGKV TEETVYTCTG HPLKSDIANI LDWMLNQDFT TAYRNITELK TLKGLALHDI LTEIHLFVHR VDFPSSVRIH LLTKMADIEY RLSVGTNEKI QLSSLIAAFQ VTRDLIVAEA //