ID PCNA_YEAST Reviewed; 258 AA. AC P15873; D6VQ89; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 27-MAR-2024, entry version 214. DE RecName: Full=Proliferating cell nuclear antigen; DE Short=PCNA; GN Name=POL30; OrderedLocusNames=YBR088C; ORFNames=YBR0811; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-41 AND RP 231-240. RX PubMed=1970160; DOI=10.1093/nar/18.2.261; RA Bauer G.A., Burgess P.M.J.; RT "Molecular cloning, structure and expression of the yeast proliferating RT cell nuclear antigen gene."; RL Nucleic Acids Res. 18:261-265(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7900426; DOI=10.1002/yea.320101014; RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.; RT "Analysis of a 70 kb region on the right arm of yeast chromosome II."; RL Yeast 10:1363-1381(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [6] RP FUNCTION, AND INTERACTION WITH RAD30. RX PubMed=11545742; DOI=10.1016/s1097-2765(01)00319-7; RA Haracska L., Kondratick C.M., Unk I., Prakash S., Prakash L.; RT "Interaction with PCNA is essential for yeast DNA polymerase eta RT function."; RL Mol. Cell 8:407-415(2001). RN [7] RP FUNCTION, SUMOYLATION AT LYS-127 AND LYS-164, UBIQUITINATION AT LYS-164, RP AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=12226657; DOI=10.1038/nature00991; RA Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S.; RT "RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin RT and SUMO."; RL Nature 419:135-141(2002). RN [8] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-127 AND LYS-164, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=15166219; DOI=10.1074/jbc.m404173200; RA Zhou W., Ryan J.J., Zhou H.; RT "Global analyses of sumoylated proteins in Saccharomyces cerevisiae. RT Induction of protein sumoylation by cellular stresses."; RL J. Biol. Chem. 279:32262-32268(2004). RN [9] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=EJY251-11b; RX PubMed=15542864; DOI=10.1074/mcp.m400154-mcp200; RA Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D., RA Gygi S.P.; RT "A proteomic strategy for gaining insights into protein sumoylation in RT yeast."; RL Mol. Cell. Proteomics 4:246-254(2005). RN [10] RP INTERACTION WITH MCM10. RX PubMed=16782870; DOI=10.1128/mcb.02062-05; RA Das-Bradoo S., Ricke R.M., Bielinsky A.-K.; RT "Interaction between PCNA and diubiquitinated Mcm10 is essential for cell RT growth in budding yeast."; RL Mol. Cell. Biol. 26:4806-4817(2006). RN [11] RP DEUBIQUITINATION BY UBP10, AND INTERACTION WITH UBP10. RX PubMed=22829782; DOI=10.1371/journal.pgen.1002826; RA Gallego-Sanchez A., Andres S., Conde F., San-Segundo P.A., Bueno A.; RT "Reversal of PCNA ubiquitylation by Ubp10 in Saccharomyces cerevisiae."; RL PLoS Genet. 8:E1002826-E1002826(2012). RN [12] RP IDENTIFICATION BY MASS 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 [13] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=8001157; DOI=10.1016/0092-8674(94)90014-0; RA Krishna T.S., Kong X.P., Gary S., Burgers P.M., Kuriyan J.; RT "Crystal structure of the eukaryotic DNA polymerase processivity factor RT PCNA."; RL Cell 79:1233-1243(1994). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH RFC1; RCF2; RCF3; RP RCF4 AND RCF5. RX PubMed=15201901; DOI=10.1038/nature02585; RA Bowman G.D., O'Donnell M., Kuriyan J.; RT "Structural analysis of a eukaryotic sliding DNA clamp-clamp loader RT complex."; RL Nature 429:724-730(2004). CC -!- FUNCTION: This protein is an auxiliary protein of DNA polymerase delta CC and is involved in the control of eukaryotic DNA replication by CC increasing the polymerase's processibility during elongation of the CC leading strand. Involved in DNA repair. {ECO:0000269|PubMed:11545742, CC ECO:0000269|PubMed:12226657}. CC -!- SUBUNIT: Homotrimer (PubMed:15201901). Interacts with RAD30 CC (PubMed:11545742). Interacts with MCM10 (PubMed:16782870). Interacts CC with UBP10 (PubMed:22829782). {ECO:0000269|PubMed:11545742, CC ECO:0000269|PubMed:15201901, ECO:0000269|PubMed:16782870, CC ECO:0000269|PubMed:22829782}. CC -!- INTERACTION: CC P15873; P43605: ECO1; NbExp=2; IntAct=EBI-12993, EBI-22988; CC P15873; Q12050: ELG1; NbExp=9; IntAct=EBI-12993, EBI-32195; CC P15873; P32354: MCM10; NbExp=4; IntAct=EBI-12993, EBI-5965; CC P15873; Q03834: MSH6; NbExp=5; IntAct=EBI-12993, EBI-11383; CC P15873; P15873: POL30; NbExp=10; IntAct=EBI-12993, EBI-12993; CC P15873; P47110: POL32; NbExp=4; IntAct=EBI-12993, EBI-6084; CC P15873; P26793: RAD27; NbExp=7; IntAct=EBI-12993, EBI-14693; CC P15873; Q04049: RAD30; NbExp=7; IntAct=EBI-12993, EBI-36214; CC P15873; Q12495: RLF2; NbExp=3; IntAct=EBI-12993, EBI-3913; CC P15873; Q12306: SMT3; NbExp=6; IntAct=EBI-12993, EBI-17490; CC P15873; P12954: SRS2; NbExp=10; IntAct=EBI-12993, EBI-18110; CC P15873; P12887: UNG1; NbExp=4; IntAct=EBI-12993, EBI-2097931; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- PTM: Sumoylated on Lys-164, and to a lesser extent on Lys-127 by the CC UBC9/SIZ1 complex during S-phase; which impairs ubiquitination and CC function in DNA repair. {ECO:0000269|PubMed:12226657, CC ECO:0000269|PubMed:15166219, ECO:0000269|PubMed:15542864}. CC -!- PTM: Monoubiquitinated on Lys-164 by the UBC2/RAD18 complex upon DNA CC damage, and then polyubiquitinated through 'Lys-63'-linkage by CC UBC13/MMS2. Ubiquitination is required for UBC2-mediated DNA repair. CC {ECO:0000269|PubMed:12226657}. CC -!- PTM: Lys-164 is deubiquitinated by UBP10 (PubMed:22829782). CC {ECO:0000269|PubMed:22829782}. CC -!- SIMILARITY: Belongs to the PCNA family. {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; X16676; CAA34664.1; -; Genomic_DNA. DR EMBL; X78993; CAA55594.1; -; Genomic_DNA. DR EMBL; Z35957; CAA85038.1; -; Genomic_DNA. DR EMBL; AY557715; AAS56041.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07209.1; -; Genomic_DNA. DR PIR; S22851; WMBYET. DR RefSeq; NP_009645.1; NM_001178436.1. DR PDB; 1PLQ; X-ray; 2.30 A; A=1-258. DR PDB; 1PLR; X-ray; 3.00 A; A=1-258. DR PDB; 1SXJ; X-ray; 2.85 A; F/G/H=1-258. DR PDB; 2OD8; X-ray; 2.80 A; A=1-258. DR PDB; 3F1W; X-ray; 2.90 A; A=1-258. DR PDB; 3GPM; X-ray; 3.80 A; A=1-258. DR PDB; 3GPN; X-ray; 2.50 A; A=1-258. DR PDB; 3L0W; X-ray; 2.80 A; A=1-163. DR PDB; 3L0X; X-ray; 3.00 A; A=1-163, B=165-258. DR PDB; 3L10; X-ray; 2.80 A; A=1-163. DR PDB; 3PGE; X-ray; 2.80 A; A=165-258, B=1-163. DR PDB; 3V60; X-ray; 2.60 A; B=1-258. DR PDB; 3V61; X-ray; 2.80 A; B=1-258. DR PDB; 3V62; X-ray; 2.90 A; B/E=1-258. DR PDB; 4L60; X-ray; 3.00 A; A=1-256. DR PDB; 4L6P; X-ray; 2.68 A; A/B/C=1-258. DR PDB; 4YHR; X-ray; 2.95 A; A=1-258. DR PDB; 5JNE; X-ray; 2.85 A; D/H=1-258. DR PDB; 5T9D; X-ray; 3.27 A; A/B/C=2-258. DR PDB; 5V7K; X-ray; 3.05 A; A=1-258. DR PDB; 5V7L; X-ray; 3.20 A; A=1-258. DR PDB; 5V7M; X-ray; 1.93 A; A=1-258. DR PDB; 5ZUT; X-ray; 2.82 A; A=1-258. DR PDB; 6CX2; X-ray; 3.10 A; A=1-258. DR PDB; 6CX3; X-ray; 3.10 A; A=1-258. DR PDB; 6CX4; X-ray; 3.08 A; A=1-258. DR PDB; 6D0Q; X-ray; 2.80 A; A=1-258. DR PDB; 6D0R; X-ray; 2.86 A; A=1-258. DR PDB; 6E49; X-ray; 2.90 A; A/B/C=1-258. DR PDB; 6W9W; X-ray; 2.65 A; A=1-254. DR PDB; 6WAC; X-ray; 2.90 A; A=1-253. DR PDB; 7KC0; EM; 3.20 A; E/F/G=1-258. DR PDB; 7TFH; EM; 3.09 A; F/G/H=1-258. DR PDB; 7TFI; EM; 3.41 A; F/G/H=1-258. DR PDB; 7TFJ; EM; 3.30 A; F/G/H=1-258. DR PDB; 7THJ; EM; 3.80 A; F/G/H=1-258. DR PDB; 7THV; EM; 4.00 A; F/G/H=1-258. DR PDB; 7TI8; EM; 3.50 A; F/G/H=1-258. DR PDB; 7TIB; EM; 3.40 A; F/G/H=1-258. DR PDB; 7TIC; EM; 3.90 A; F/G/H=1-258. DR PDB; 7TID; EM; 3.30 A; F/G/H=1-258. DR PDB; 7TKU; EM; 4.00 A; F/G/H=1-258. DR PDB; 7U19; EM; 3.70 A; F/G/H=1-258. DR PDB; 7U1A; EM; 3.30 A; F/G/H=1-258. DR PDB; 7U1P; EM; 3.00 A; F/G/H=1-258. DR PDB; 8DQX; EM; 2.10 A; F/G/H=1-258. DR PDB; 8DQZ; EM; 2.92 A; F/G/H=1-258. DR PDB; 8DR0; EM; 2.42 A; F/G/H=1-258. DR PDB; 8DR1; EM; 2.14 A; F/G/H=1-258. DR PDB; 8DR3; EM; 2.20 A; F/G/H=1-258. DR PDB; 8DR4; EM; 2.45 A; F/G/H=1-258. DR PDB; 8DR5; EM; 2.76 A; F/G/H=1-258. DR PDB; 8DR6; EM; 2.39 A; F/G/H=1-258. DR PDB; 8DR7; EM; 2.70 A; F/G/H=1-258. DR PDBsum; 1PLQ; -. DR PDBsum; 1PLR; -. DR PDBsum; 1SXJ; -. DR PDBsum; 2OD8; -. DR PDBsum; 3F1W; -. DR PDBsum; 3GPM; -. DR PDBsum; 3GPN; -. DR PDBsum; 3L0W; -. DR PDBsum; 3L0X; -. DR PDBsum; 3L10; -. DR PDBsum; 3PGE; -. DR PDBsum; 3V60; -. DR PDBsum; 3V61; -. DR PDBsum; 3V62; -. DR PDBsum; 4L60; -. DR PDBsum; 4L6P; -. DR PDBsum; 4YHR; -. DR PDBsum; 5JNE; -. DR PDBsum; 5T9D; -. DR PDBsum; 5V7K; -. DR PDBsum; 5V7L; -. DR PDBsum; 5V7M; -. DR PDBsum; 5ZUT; -. DR PDBsum; 6CX2; -. DR PDBsum; 6CX3; -. DR PDBsum; 6CX4; -. DR PDBsum; 6D0Q; -. DR PDBsum; 6D0R; -. DR PDBsum; 6E49; -. DR PDBsum; 6W9W; -. DR PDBsum; 6WAC; -. DR PDBsum; 7KC0; -. DR PDBsum; 7TFH; -. DR PDBsum; 7TFI; -. DR PDBsum; 7TFJ; -. DR PDBsum; 7THJ; -. DR PDBsum; 7THV; -. DR PDBsum; 7TI8; -. DR PDBsum; 7TIB; -. DR PDBsum; 7TIC; -. DR PDBsum; 7TID; -. DR PDBsum; 7TKU; -. DR PDBsum; 7U19; -. DR PDBsum; 7U1A; -. DR PDBsum; 7U1P; -. DR PDBsum; 8DQX; -. DR PDBsum; 8DQZ; -. DR PDBsum; 8DR0; -. DR PDBsum; 8DR1; -. DR PDBsum; 8DR3; -. DR PDBsum; 8DR4; -. DR PDBsum; 8DR5; -. DR PDBsum; 8DR6; -. DR PDBsum; 8DR7; -. DR AlphaFoldDB; P15873; -. DR EMDB; EMD-22803; -. DR EMDB; EMD-25568; -. DR EMDB; EMD-25569; -. DR EMDB; EMD-25614; -. DR EMDB; EMD-25615; -. DR EMDB; EMD-25616; -. DR EMDB; EMD-25617; -. DR EMDB; EMD-25753; -. DR EMDB; EMD-25872; -. DR EMDB; EMD-25873; -. DR EMDB; EMD-25874; -. DR EMDB; EMD-26297; -. DR EMDB; EMD-26298; -. DR EMDB; EMD-26302; -. DR EMDB; EMD-27663; -. DR EMDB; EMD-27666; -. DR EMDB; EMD-27668; -. DR EMDB; EMD-27669; -. DR EMDB; EMD-27670; -. DR EMDB; EMD-27672; -. DR SASBDB; P15873; -. DR SMR; P15873; -. DR BioGRID; 32794; 480. DR ComplexPortal; CPX-544; PCNA homotrimer. DR DIP; DIP-2417N; -. DR IntAct; P15873; 36. DR MINT; P15873; -. DR STRING; 4932.YBR088C; -. DR iPTMnet; P15873; -. DR MaxQB; P15873; -. DR PaxDb; 4932-YBR088C; -. DR PeptideAtlas; P15873; -. DR TopDownProteomics; P15873; -. DR EnsemblFungi; YBR088C_mRNA; YBR088C; YBR088C. DR GeneID; 852385; -. DR KEGG; sce:YBR088C; -. DR AGR; SGD:S000000292; -. DR SGD; S000000292; POL30. DR VEuPathDB; FungiDB:YBR088C; -. DR eggNOG; KOG1636; Eukaryota. DR GeneTree; ENSGT00390000004965; -. DR HOGENOM; CLU_043978_3_0_1; -. DR InParanoid; P15873; -. DR OMA; EMKLINM; -. DR OrthoDB; 118939at2759; -. DR BioCyc; YEAST:G3O-29055-MONOMER; -. DR Reactome; R-SCE-4615885; SUMOylation of DNA replication proteins. DR Reactome; R-SCE-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha). DR Reactome; R-SCE-69091; Polymerase switching. DR Reactome; R-SCE-69166; Removal of the Flap Intermediate. DR Reactome; R-SCE-69183; Processive synthesis on the lagging strand. DR BioGRID-ORCS; 852385; 9 hits in 10 CRISPR screens. DR EvolutionaryTrace; P15873; -. DR PRO; PR:P15873; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; P15873; Protein. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0043626; C:PCNA complex; IPI:SGD. DR GO; GO:0005657; C:replication fork; IDA:SGD. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IDA:SGD. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0070987; P:error-free translesion synthesis; IGI:SGD. DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IGI:SGD. DR GO; GO:0006273; P:lagging strand elongation; IDA:SGD. DR GO; GO:0006272; P:leading strand elongation; IDA:SGD. DR GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IMP:SGD. DR GO; GO:0000710; P:meiotic mismatch repair; IMP:SGD. DR GO; GO:0006298; P:mismatch repair; IMP:SGD. DR GO; GO:0000278; P:mitotic cell cycle; IGI:SGD. DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IGI:SGD. DR GO; GO:0006289; P:nucleotide-excision repair; IMP:SGD. DR GO; GO:0051054; P:positive regulation of DNA metabolic process; IDA:SGD. DR GO; GO:0045739; P:positive regulation of DNA repair; IMP:ComplexPortal. DR GO; GO:0045740; P:positive regulation of DNA replication; IDA:ComplexPortal. DR GO; GO:0006301; P:postreplication repair; IMP:SGD. DR GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IMP:SGD. DR GO; GO:0031509; P:subtelomeric heterochromatin formation; IMP:SGD. DR GO; GO:0019985; P:translesion synthesis; IBA:GO_Central. DR CDD; cd00577; PCNA; 1. DR Gene3D; 3.10.150.10; DNA Polymerase III, subunit A, domain 2; 2. DR HAMAP; MF_00317; DNApol_clamp_arch; 1. DR InterPro; IPR046938; DNA_clamp_sf. DR InterPro; IPR000730; Pr_cel_nuc_antig. DR InterPro; IPR022649; Pr_cel_nuc_antig_C. DR InterPro; IPR022659; Pr_cel_nuc_antig_CS. DR InterPro; IPR022648; Pr_cel_nuc_antig_N. DR NCBIfam; TIGR00590; pcna; 1. DR PANTHER; PTHR11352; PROLIFERATING CELL NUCLEAR ANTIGEN; 1. DR PANTHER; PTHR11352:SF0; PROLIFERATING CELL NUCLEAR ANTIGEN; 1. DR Pfam; PF02747; PCNA_C; 1. DR Pfam; PF00705; PCNA_N; 1. DR PRINTS; PR00339; PCNACYCLIN. DR SUPFAM; SSF55979; DNA clamp; 2. DR PROSITE; PS01251; PCNA_1; 1. DR PROSITE; PS00293; PCNA_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; DNA damage; DNA repair; KW DNA replication; DNA-binding; Isopeptide bond; Nucleus; Reference proteome; KW Ubl conjugation. FT CHAIN 1..258 FT /note="Proliferating cell nuclear antigen" FT /id="PRO_0000149176" FT DNA_BIND 61..80 FT /evidence="ECO:0000255" FT CROSSLNK 127 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:15166219" FT CROSSLNK 164 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000269|PubMed:15166219, FT ECO:0000269|PubMed:15542864" FT CROSSLNK 164 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000269|PubMed:12226657" FT STRAND 2..7 FT /evidence="ECO:0007829|PDB:5V7M" FT HELIX 9..17 FT /evidence="ECO:0007829|PDB:5V7M" FT TURN 18..22 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 24..31 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 34..40 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:5ZUT" FT STRAND 46..53 FT /evidence="ECO:0007829|PDB:5V7M" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 57..64 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 66..71 FT /evidence="ECO:0007829|PDB:5V7M" FT HELIX 72..79 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:5V7K" FT STRAND 84..92 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 97..104 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 106..109 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 111..117 FT /evidence="ECO:0007829|PDB:5V7M" FT HELIX 122..124 FT /evidence="ECO:0007829|PDB:3V62" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:7KC0" FT STRAND 134..140 FT /evidence="ECO:0007829|PDB:5V7M" FT HELIX 141..152 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 156..163 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 166..173 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 176..182 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 185..187 FT /evidence="ECO:0007829|PDB:1SXJ" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:3V60" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 195..201 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 203..208 FT /evidence="ECO:0007829|PDB:5V7M" FT HELIX 209..215 FT /evidence="ECO:0007829|PDB:5V7M" FT HELIX 216..220 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 223..229 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 235..241 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 244..250 FT /evidence="ECO:0007829|PDB:5V7M" FT STRAND 254..256 FT /evidence="ECO:0007829|PDB:1PLQ" SQ SEQUENCE 258 AA; 28916 MW; 9B56C5851621DDDC CRC64; MLEAKFEEAS LFKRIIDGFK DCVQLVNFQC KEDGIIAQAV DDSRVLLVSL EIGVEAFQEY RCDHPVTLGM DLTSLSKILR CGNNTDTLTL IADNTPDSII LLFEDTKKDR IAEYSLKLMD IDADFLKIEE LQYDSTLSLP SSEFSKIVRD LSQLSDSINI MITKETIKFV ADGDIGSGSV IIKPFVDMEH PETSIKLEMD QPVDLTFGAK YLLDIIKGSS LSDRVGIRLS SEAPALFQFD LKSGFLQFFL APKFNDEE //