ID PCNA_HUMAN Reviewed; 261 AA. AC P12004; B2R897; D3DW02; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 27-MAR-2024, entry version 251. DE RecName: Full=Proliferating cell nuclear antigen; DE Short=PCNA; DE AltName: Full=Cyclin; GN Name=PCNA; 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]. RX PubMed=2882507; DOI=10.1073/pnas.84.6.1575; RA Almendral J.M., Huebsch D., Blundell P.A., Macdonald-Bravo H., Bravo R.; RT "Cloning and sequence of the human nuclear protein cyclin: homology with RT DNA-binding proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 84:1575-1579(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2565339; DOI=10.1016/s0021-9258(18)83257-4; RA Travali S., Ku D.H., Rizzo M.G., Ottavio L., Baserga R., Calabretta B.; RT "Structure of the human gene for the proliferating cell nuclear antigen."; RL J. Biol. Chem. 264:7466-7472(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [6] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone marrow, and Lung; 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 [8] RP PROTEIN SEQUENCE OF 1-26. RX PubMed=2882422; DOI=10.1038/326471a0; RA Prelich G., Kostura M., Marshak D.R., Mathews M.B., Stillman B.; RT "The cell-cycle regulated proliferating cell nuclear antigen is required RT for SV40 DNA replication in vitro."; RL Nature 326:471-475(1987). RN [9] RP PROTEIN SEQUENCE OF 169-181, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [10] RP INTERACTION WITH ERCC5/XPG. RX PubMed=9305916; DOI=10.1074/jbc.272.39.24522; RA Gary R., Ludwig D.L., Cornelius H.L., MacInnes M.A., Park M.S.; RT "The DNA repair endonuclease XPG binds to proliferating cell nuclear RT antigen (PCNA) and shares sequence elements with the PCNA-binding regions RT of FEN-1 and cyclin-dependent kinase inhibitor p21."; RL J. Biol. Chem. 272:24522-24529(1997). RN [11] RP INTERACTION WITH DNMT1. RX PubMed=9302295; DOI=10.1126/science.277.5334.1996; RA Chuang L.S.-H., Ian H.-I., Koh T.-W., Ng H.-H., Xu G., Li B.F.L.; RT "Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for RT p21WAF1."; RL Science 277:1996-2000(1997). RN [12] RP INTERACTION WITH CDC6. RX PubMed=9566895; DOI=10.1128/mcb.18.5.2758; RA Saha P., Chen J., Thome K.C., Lawlis S.J., Hou Z.H., Hendricks M., RA Parvin J.D., Dutta A.; RT "Human CDC6/Cdc18 associates with Orc1 and cyclin-cdk and is selectively RT eliminated from the nucleus at the onset of S phase."; RL Mol. Cell. Biol. 18:2758-2767(1998). RN [13] RP INTERACTION WITH POLD3 AND CDKN1A, AND MUTAGENESIS OF 43-SER--VAL-45; RP 125-GLN--ILE-128; 188-VAL--LYS-190 AND 251-LEU--LYS-254. RX PubMed=11595739; DOI=10.1074/jbc.m106990200; RA Ducoux M., Urbach S., Baldacci G., Huebscher U., Koundrioukoff S., RA Christensen J., Hughes P.; RT "Mediation of proliferating cell nuclear antigen (PCNA)-dependent DNA RT replication through a conserved p21(Cip1)-like PCNA-binding motif present RT in the third subunit of human DNA polymerase delta."; RL J. Biol. Chem. 276:49258-49266(2001). RN [14] RP INTERACTION WITH APEX2. RX PubMed=11376153; DOI=10.1093/nar/29.11.2349; RA Tsuchimoto D., Sakai Y., Sakumi K., Nishioka K., Sasaki M., Fujiwara T., RA Nakabeppu Y.; RT "Human APE2 protein is mostly localized in the nuclei and to some extent in RT the mitochondria, while nuclear APE2 is partly associated with RT proliferating cell nuclear antigen."; RL Nucleic Acids Res. 29:2349-2360(2001). RN [15] RP INTERACTION WITH POLK. RX PubMed=11784855; DOI=10.1128/mcb.22.3.784-791.2002; RA Haracska L., Unk I., Johnson R.E., Phillips B.B., Hurwitz J., Prakash L., RA Prakash S.; RT "Stimulation of DNA synthesis activity of human DNA polymerase kappa by RT PCNA."; RL Mol. Cell. Biol. 22:784-791(2002). RN [16] RP INTERACTION WITH DNTTIP2. RX PubMed=12786946; DOI=10.1046/j.1365-2443.2003.00656.x; RA Fujita K., Shimazaki N., Ohta Y., Kubota T., Ibe S., Toji S., Tamai K., RA Fujisaki S., Hayano T., Koiwai O.; RT "Terminal deoxynucleotidyltransferase forms a ternary complex with a novel RT chromatin remodeling protein with 82 kDa and core histone."; RL Genes Cells 8:559-571(2003). RN [17] RP INTERACTION WITH POLDIP2. RC TISSUE=Placenta; RX PubMed=12522211; DOI=10.1074/jbc.m208694200; RA Liu L., Rodriguez-Belmonte E.M., Mazloum N., Xie B., Lee M.Y.W.T.; RT "Identification of a novel protein, PDIP38, that interacts with the p50 RT subunit of DNA polymerase delta and proliferating cell nuclear antigen."; RL J. Biol. Chem. 278:10041-10047(2003). RN [18] RP INTERACTION WITH EXO1. RX PubMed=15225546; DOI=10.1016/j.molcel.2004.06.016; RA Dzantiev L., Constantin N., Genschel J., Iyer R.R., Burgers P.M., RA Modrich P.; RT "A defined human system that supports bidirectional mismatch-provoked RT excision."; RL Mol. Cell 15:31-41(2004). RN [19] RP UBIQUITINATION, AND INTERACTION WITH POLH. RX PubMed=15149598; DOI=10.1016/s1097-2765(04)00259-x; RA Kannouche P.L., Wing J., Lehmann A.R.; RT "Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a RT possible mechanism for the polymerase switch in response to DNA damage."; RL Mol. Cell 14:491-500(2004). RN [20] RP INTERACTION WITH BAZ1B AND SMARCA5. RX PubMed=15543136; DOI=10.1038/ncb1196; RA Poot R.A., Bozhenok L., van den Berg D.L.C., Steffensen S., Ferreira F., RA Grimaldi M., Gilbert N., Ferreira J., Varga-Weisz P.D.; RT "The Williams syndrome transcription factor interacts with PCNA to target RT chromatin remodelling by ISWI to replication foci."; RL Nat. Cell Biol. 6:1236-1244(2004). RN [21] RP INTERACTION WITH POLD1; POLD3 AND POLD4. RX PubMed=16510448; DOI=10.1074/jbc.m600322200; RA Li H., Xie B., Zhou Y., Rahmeh A., Trusa S., Zhang S., Gao Y., Lee E.Y., RA Lee M.Y.; RT "Functional roles of p12, the fourth subunit of human DNA polymerase RT delta."; RL J. Biol. Chem. 281:14748-14755(2006). RN [22] RP INTERACTION WITH SHPRH, UBIQUITINATION AT LYS-164, AND MUTAGENESIS OF RP LYS-164. RX PubMed=17130289; DOI=10.1083/jcb.200606145; RA Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K.; RT "Human SHPRH suppresses genomic instability through proliferating cell RT nuclear antigen polyubiquitination."; RL J. Cell Biol. 175:703-708(2006). RN [23] RP INTERACTION WITH CDT1. RX PubMed=16949367; DOI=10.1016/j.molcel.2006.08.010; RA Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.; RT "A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is RT required for S phase destruction of the replication factor Cdt1."; RL Mol. Cell 23:709-721(2006). RN [24] RP PHOSPHORYLATION AT TYR-211 BY EGFR, MUTAGENESIS OF TYR-211, AND INTERACTION RP WITH EGFR. RX PubMed=17115032; DOI=10.1038/ncb1501; RA Wang S.C., Nakajima Y., Yu Y.L., Xia W., Chen C.T., Yang C.C., RA McIntush E.W., Li L.Y., Hawke D.H., Kobayashi R., Hung M.C.; RT "Tyrosine phosphorylation controls PCNA function through protein RT stability."; RL Nat. Cell Biol. 8:1359-1368(2006). RN [25] RP UBIQUITINATION AT LYS-164, AND MUTAGENESIS OF LYS-164. RX PubMed=17108083; DOI=10.1073/pnas.0608595103; RA Unk I., Hajdu I., Fatyol K., Szakal B., Blastyak A., Bermudez V., RA Hurwitz J., Prakash L., Prakash S., Haracska L.; RT "Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent RT polyubiquitylation of proliferating cell nuclear antigen."; RL Proc. Natl. Acad. Sci. U.S.A. 103:18107-18112(2006). RN [26] RP UBIQUITINATION. RX PubMed=18948756; DOI=10.4161/cc.7.21.6949; RA Zhang S., Chea J., Meng X., Zhou Y., Lee E.Y.C., Lee M.Y.W.T.; RT "PCNA is ubiquitinated by RNF8."; RL Cell Cycle 7:3399-3404(2008). RN [27] RP INTERACTION WITH CDKN1A. RX PubMed=18794347; DOI=10.1101/gad.1676108; RA Abbas T., Sivaprasad U., Terai K., Amador V., Pagano M., Dutta A.; RT "PCNA-dependent regulation of p21 ubiquitylation and degradation via the RT CRL4Cdt2 ubiquitin ligase complex."; RL Genes Dev. 22:2496-2506(2008). RN [28] RP INTERACTION WITH POLB. RX PubMed=19336415; DOI=10.1093/nar/gkp201; RA Guo Z., Zheng L., Dai H., Zhou M., Xu H., Shen B.; RT "Human DNA polymerase beta polymorphism, Arg137Gln, impairs its polymerase RT activity and interaction with PCNA and the cellular base excision repair RT capacity."; RL Nucleic Acids Res. 37:3431-3441(2009). RN [29] RP INTERACTION WITH DDX11. RX PubMed=18499658; DOI=10.1074/jbc.m802696200; RA Farina A., Shin J.H., Kim D.H., Bermudez V.P., Kelman Z., Seo Y.S., RA Hurwitz J.; RT "Studies with the human cohesin establishment factor, ChlR1. Association of RT ChlR1 with Ctf18-RFC and Fen1."; RL J. Biol. Chem. 283:20925-20936(2008). RN [30] RP INTERACTION WITH CDKN1A. RX PubMed=18703516; DOI=10.1074/jbc.m806045200; RA Nishitani H., Shiomi Y., Iida H., Michishita M., Takami T., Tsurimoto T.; RT "CDK inhibitor p21 is degraded by a proliferating cell nuclear antigen- RT coupled Cul4-DDB1Cdt2 pathway during S phase and after UV irradiation."; RL J. Biol. Chem. 283:29045-29052(2008). RN [31] RP FUNCTION, AND INTERACTION WITH APEX2. RX PubMed=19443450; DOI=10.1093/nar/gkp357; RA Burkovics P., Hajdu I., Szukacsov V., Unk I., Haracska L.; RT "Role of PCNA-dependent stimulation of 3'-phosphodiesterase and 3'-5' RT exonuclease activities of human Ape2 in repair of oxidative DNA damage."; RL Nucleic Acids Res. 37:4247-4255(2009). RN [32] RP UBIQUITINATION, AND INTERACTION WITH HLTF. RX PubMed=18316726; DOI=10.1073/pnas.0800563105; RA Unk I., Hajdu I., Fatyol K., Hurwitz J., Yoon J.-H., Prakash L., RA Prakash S., Haracska L.; RT "Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear RT antigen polyubiquitination."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3768-3773(2008). RN [33] RP UBIQUITINATION, FUNCTION, INTERACTION WITH HLTF AND SHPRH, AND MUTAGENESIS RP OF LYS-164. RX PubMed=18719106; DOI=10.1073/pnas.0805685105; RA Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X., Moinova H., RA Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.; RT "Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH RT prevents genomic instability from stalled replication forks."; RL Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008). RN [34] RP INTERACTION WITH NUDT15, AND ACETYLATION AT LYS-14. RX PubMed=19419956; DOI=10.1074/jbc.m109.015289; RA Yu Y., Cai J.-P., Tu B., Wu L., Zhao Y., Liu X., Li L., McNutt M.A., RA Feng J., He Q., Yang Y., Wang H., Sekiguchi M., Zhu W.-G.; RT "Proliferating cell nuclear antigen is protected from degradation by RT forming a complex with MutT Homolog2."; RL J. Biol. Chem. 284:19310-19320(2009). RN [35] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-77; LYS-80 AND LYS-248, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [36] RP INTERACTION WITH ATAD5. RX PubMed=20147293; DOI=10.1074/jbc.m109.092544; RA Lee K.Y., Yang K., Cohn M.A., Sikdar N., D'Andrea A.D., Myung K.; RT "Human ELG1 regulates the level of ubiquitinated proliferating cell nuclear RT antigen (PCNA) through Its interactions with PCNA and USP1."; RL J. Biol. Chem. 285:10362-10369(2010). RN [37] RP INTERACTION WITH MAPK15. RX PubMed=20733054; DOI=10.1083/jcb.201002124; RA Groehler A.L., Lannigan D.A.; RT "A chromatin-bound kinase, ERK8, protects genomic integrity by inhibiting RT HDM2-mediated degradation of the DNA clamp PCNA."; RL J. Cell Biol. 190:575-586(2010). RN [38] RP UBIQUITINATION, AND MUTAGENESIS OF LYS-164. RX PubMed=20129063; DOI=10.1016/j.molcel.2009.12.018; RA Terai K., Abbas T., Jazaeri A.A., Dutta A.; RT "CRL4(Cdt2) E3 ubiquitin ligase monoubiquitinates PCNA to promote RT translesion DNA synthesis."; RL Mol. Cell 37:143-149(2010). RN [39] RP UBIQUITINATION IN RESPONSE TO UV IRRADIATION. RX PubMed=20227374; DOI=10.1016/j.molcel.2010.02.009; RA Ogi T., Limsirichaikul S., Overmeer R.M., Volker M., Takenaka K., RA Cloney R., Nakazawa Y., Niimi A., Miki Y., Jaspers N.G., Mullenders L.H., RA Yamashita S., Fousteri M.I., Lehmann A.R.; RT "Three DNA polymerases, recruited by different mechanisms, carry out NER RT repair synthesis in human cells."; RL Mol. Cell 37:714-727(2010). RN [40] RP INTERACTION WITH POLN. RX PubMed=19995904; DOI=10.1128/mcb.01124-09; RA Moldovan G.L., Madhavan M.V., Mirchandani K.D., McCaffrey R.M., RA Vinciguerra P., D'Andrea A.D.; RT "DNA polymerase POLN participates in cross-link repair and homologous RT recombination."; RL Mol. Cell. Biol. 30:1088-1096(2010). RN [41] RP INTERACTION WITH SETMAR. RX PubMed=20457750; DOI=10.1093/nar/gkq339; RA De Haro L.P., Wray J., Williamson E.A., Durant S.T., Corwin L., RA Gentry A.C., Osheroff N., Lee S.H., Hromas R., Nickoloff J.A.; RT "Metnase promotes restart and repair of stalled and collapsed replication RT forks."; RL Nucleic Acids Res. 38:5681-5691(2010). RN [42] 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 [43] RP INTERACTION WITH SMARCAD1. RX PubMed=21549307; DOI=10.1016/j.molcel.2011.02.036; RA Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N., RA Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P., RA Mermoud J.E.; RT "Maintenance of silent chromatin through replication requires SWI/SNF-like RT chromatin remodeler SMARCAD1."; RL Mol. Cell 42:285-296(2011). RN [44] RP INTERACTION WITH PCLAF. RX PubMed=21628590; DOI=10.1073/pnas.1106136108; RA Emanuele M.J., Ciccia A., Elia A.E., Elledge S.J.; RT "Proliferating cell nuclear antigen (PCNA)-associated KIAA0101/PAF15 RT protein is a cell cycle-regulated anaphase-promoting complex/cyclosome RT substrate."; RL Proc. Natl. Acad. Sci. U.S.A. 108:9845-9850(2011). RN [45] RP INTERACTION WITH POLD3. RX PubMed=22148433; DOI=10.1021/bi201638e; RA Rahmeh A.A., Zhou Y., Xie B., Li H., Lee E.Y., Lee M.Y.; RT "Phosphorylation of the p68 subunit of Pol delta acts as a molecular switch RT to regulate its interaction with PCNA."; RL Biochemistry 51:416-424(2012). RN [46] RP INTERACTION WITH PARPBP, AND SUMOYLATION. RX PubMed=22153967; DOI=10.1016/j.molcel.2011.11.010; RA Moldovan G.L., Dejsuphong D., Petalcorin M.I., Hofmann K., Takeda S., RA Boulton S.J., D'Andrea A.D.; RT "Inhibition of homologous recombination by the PCNA-interacting protein RT PARI."; RL Mol. Cell 45:75-86(2012). RN [47] RP INTERACTION WITH SPRTN. RX PubMed=22681887; DOI=10.1016/j.molcel.2012.05.020; RA Centore R.C., Yazinski S.A., Tse A., Zou L.; RT "Spartan/C1orf124, a reader of PCNA ubiquitylation and a regulator of UV- RT induced DNA damage response."; RL Mol. Cell 46:625-635(2012). RN [48] RP INTERACTION WITH ZRANB3. RX PubMed=22759634; DOI=10.1101/gad.193516.112; RA Weston R., Peeters H., Ahel D.; RT "ZRANB3 is a structure-specific ATP-dependent endonuclease involved in RT replication stress response."; RL Genes Dev. 26:1558-1572(2012). RN [49] RP INTERACTION WITH ZRANB3. RX PubMed=22705370; DOI=10.1016/j.molcel.2012.05.025; RA Yuan J., Ghosal G., Chen J.; RT "The HARP-like domain-containing protein AH2/ZRANB3 binds to PCNA and RT participates in cellular response to replication stress."; RL Mol. Cell 47:410-421(2012). RN [50] RP INTERACTION WITH PCLAF. RX PubMed=23000965; DOI=10.1038/ncb2579; RA Povlsen L.K., Beli P., Wagner S.A., Poulsen S.L., Sylvestersen K.B., RA Poulsen J.W., Nielsen M.L., Bekker-Jensen S., Mailand N., Choudhary C.; RT "Systems-wide analysis of ubiquitylation dynamics reveals a key role for RT PAF15 ubiquitylation in DNA-damage bypass."; RL Nat. Cell Biol. 14:1089-1098(2012). RN [51] RP INTERACTION WITH ZRANB3. RX PubMed=22704558; DOI=10.1016/j.molcel.2012.05.024; RA Ciccia A., Nimonkar A.V., Hu Y., Hajdu I., Achar Y.J., Izhar L., RA Petit S.A., Adamson B., Yoon J.C., Kowalczykowski S.C., Livingston D.M., RA Haracska L., Elledge S.J.; RT "Polyubiquitinated PCNA recruits the ZRANB3 translocase to maintain genomic RT integrity after replication stress."; RL Mol. Cell 47:396-409(2012). RN [52] RP INTERACTION WITH CDKN1C. RX PubMed=22634751; DOI=10.1038/ng.2275; RA Arboleda V.A., Lee H., Parnaik R., Fleming A., Banerjee A., RA Ferraz-de-Souza B., Delot E.C., Rodriguez-Fernandez I.A., Braslavsky D., RA Bergada I., Dell'Angelica E.C., Nelson S.F., Martinez-Agosto J.A., RA Achermann J.C., Vilain E.; RT "Mutations in the PCNA-binding domain of CDKN1C cause IMAGe syndrome."; RL Nat. Genet. 44:788-792(2012). RN [53] RP INTERACTION WITH ANKRD17. RX PubMed=23711367; DOI=10.1016/j.febslet.2013.05.037; RA Menning M., Kufer T.A.; RT "A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and RT Nod2-mediated inflammatory responses."; RL FEBS Lett. 587:2137-2142(2013). RN [54] RP INTERACTION WITH FBH1. RX PubMed=23677613; DOI=10.1093/nar/gkt397; RA Bacquin A., Pouvelle C., Siaud N., Perderiset M., Salome-Desnoulez S., RA Tellier-Lebegue C., Lopez B., Charbonnier J.B., Kannouche P.L.; RT "The helicase FBH1 is tightly regulated by PCNA via CRL4(Cdt2)-mediated RT proteolysis in human cells."; RL Nucleic Acids Res. 41:6501-6513(2013). RN [55] RP INTERACTION WITH RTEL1, AND SUBCELLULAR LOCATION. RX PubMed=24115439; DOI=10.1126/science.1241779; RA Vannier J.B., Sandhu S., Petalcorin M.I., Wu X., Nabi Z., Ding H., RA Boulton S.J.; RT "RTEL1 is a replisome-associated helicase that promotes telomere and RT genome-wide replication."; RL Science 342:239-242(2013). RN [56] RP FUNCTION, AND INTERACTION WITH PARP10. RX PubMed=24695737; DOI=10.1074/jbc.m114.556340; RA Nicolae C.M., Aho E.R., Vlahos A.H., Choe K.N., De S., Karras G.I., RA Moldovan G.L.; RT "The ADP-ribosyltransferase PARP10/ARTD10 interacts with proliferating cell RT nuclear antigen (PCNA) and is required for DNA damage tolerance."; RL J. Biol. Chem. 289:13627-13637(2014). RN [57] RP INVOLVEMENT IN ATLD2, INTERACTION WITH FEN1; LIG1 AND ERCC5, VARIANT ATLD2 RP ILE-228, AND CHARACTERIZATION OF VARIANT ATDL2 ILE-228. RX PubMed=24911150; DOI=10.1172/jci74593; RA Baple E.L., Chambers H., Cross H.E., Fawcett H., Nakazawa Y., Chioza B.A., RA Harlalka G.V., Mansour S., Sreekantan-Nair A., Patton M.A., RA Muggenthaler M., Rich P., Wagner K., Coblentz R., Stein C.K., Last J.I., RA Taylor A.M., Jackson A.P., Ogi T., Lehmann A.R., Green C.M., Crosby A.H.; RT "Hypomorphic PCNA mutation underlies a human DNA repair disorder."; RL J. Clin. Invest. 124:3137-3146(2014). RN [58] 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). RN [59] RP INTERACTION WITH FAM111A. RX PubMed=24561620; DOI=10.1038/ncb2918; RA Alabert C., Bukowski-Wills J.C., Lee S.B., Kustatscher G., Nakamura K., RA de Lima Alves F., Menard P., Mejlvang J., Rappsilber J., Groth A.; RT "Nascent chromatin capture proteomics determines chromatin dynamics during RT DNA replication and identifies unknown fork components."; RL Nat. Cell Biol. 16:281-293(2014). RN [60] RP FUNCTION, TRIMERIZATION, INTERACTION WITH CREBBP; EP300 AND POLD1, RP ACETYLATION, UBIQUITINATION, ASSOCIATION WITH CHROMATIN, AND MUTAGENESIS OF RP LYS-13; LYS-14; LYS-20; LYS-77 AND LYS-80. RX PubMed=24939902; DOI=10.1093/nar/gku533; RA Cazzalini O., Sommatis S., Tillhon M., Dutto I., Bachi A., Rapp A., RA Nardo T., Scovassi A.I., Necchi D., Cardoso M.C., Stivala L.A., RA Prosperi E.; RT "CBP and p300 acetylate PCNA to link its degradation with nucleotide RT excision repair synthesis."; RL Nucleic Acids Res. 42:8433-8448(2014). RN [61] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [62] RP METHYLATION. RX PubMed=25732820; DOI=10.1016/j.celrep.2015.01.054; RA Perry J.J., Ballard G.D., Albert A.E., Dobrolecki L.E., Malkas L.H., RA Hoelz D.J.; RT "Human C6orf211 encodes Armt1, a protein carboxyl methyltransferase that RT targets PCNA and is linked to the DNA damage response."; RL Cell Rep. 10:1288-1296(2015). RN [63] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164, 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 [64] RP INTERACTION WITH ALKBH2, AND MUTAGENESIS OF 43-SER--VAL-45; RP 125-GLN--ILE-128 AND 188-VAL--LYS-190. RX PubMed=26408825; DOI=10.1016/j.dnarep.2015.09.008; RA Fu D., Samson L.D., Huebscher U., van Loon B.; RT "The interaction between ALKBH2 DNA repair enzyme and PCNA is direct, RT mediated by the hydrophobic pocket of PCNA and perturbed in naturally- RT occurring ALKBH2 variants."; RL DNA Repair 35:13-18(2015). RN [65] RP INTERACTION WITH HERPES VIRUS 8 PROTEIN LANA1 (MICROBIAL INFECTION). RX PubMed=26223641; DOI=10.1128/jvi.01524-15; RA Sun Z., Jha H.C., Robertson E.S.; RT "Bub1 in Complex with LANA Recruits PCNA To Regulate Kaposi's Sarcoma- RT Associated Herpesvirus Latent Replication and DNA Translesion Synthesis."; RL J. Virol. 89:10206-10218(2015). RN [66] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [67] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [68] RP INTERACTION WITH TRAIP. RX PubMed=27462463; DOI=10.1038/celldisc.2016.16; RA Feng W., Guo Y., Huang J., Deng Y., Zang J., Huen M.S.; RT "TRAIP regulates replication fork recovery and progression via PCNA."; RL Cell Discov. 2:16016-16016(2016). RN [69] RP INTERACTION WITH POLB. RX PubMed=26760506; DOI=10.18632/oncotarget.6849; RA Zhou T., Pan F., Cao Y., Han Y., Zhao J., Sun H., Zhou X., Wu X., He L., RA Hu Z., Chen H., Shen B., Guo Z.; RT "R152C DNA Pol beta mutation impairs base excision repair and induces RT cellular transformation."; RL Oncotarget 7:6902-6915(2016). RN [70] RP INTERACTION WITH SDE2. RX PubMed=27906959; DOI=10.1371/journal.pgen.1006465; RA Jo U., Cai W., Wang J., Kwon Y., D'Andrea A.D., Kim H.; RT "PCNA-dependent cleavage and degradation of SDE2 regulates response to RT replication stress."; RL PLoS Genet. 12:E1006465-E1006465(2016). RN [71] RP INTERACTION WITH DONSON. RX PubMed=28191891; DOI=10.1038/ng.3790; RA Reynolds J.J., Bicknell L.S., Carroll P., Higgs M.R., Shaheen R., RA Murray J.E., Papadopoulos D.K., Leitch A., Murina O., Tarnauskaite Z., RA Wessel S.R., Zlatanou A., Vernet A., von Kriegsheim A., Mottram R.M., RA Logan C.V., Bye H., Li Y., Brean A., Maddirevula S., Challis R.C., RA Skouloudaki K., Almoisheer A., Alsaif H.S., Amar A., Prescott N.J., RA Bober M.B., Duker A., Faqeih E., Seidahmed M.Z., Al Tala S., Alswaid A., RA Ahmed S., Al-Aama J.Y., Altmueller J., Al Balwi M., Brady A.F., Chessa L., RA Cox H., Fischetto R., Heller R., Henderson B.D., Hobson E., Nuernberg P., RA Percin E.F., Peron A., Spaccini L., Quigley A.J., Thakur S., Wise C.A., RA Yoon G., Alnemer M., Tomancak P., Yigit G., Taylor A.M., Reijns M.A., RA Simpson M.A., Cortez D., Alkuraya F.S., Mathew C.G., Jackson A.P., RA Stewart G.S.; RT "Mutations in DONSON disrupt replication fork stability and cause RT microcephalic dwarfism."; RL Nat. Genet. 49:537-549(2017). RN [72] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164 AND LYS-254, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [73] RP INTERACTION WITH DDI2. RX PubMed=29290612; DOI=10.1016/j.molcel.2017.11.035; RA Kottemann M.C., Conti B.A., Lach F.P., Smogorzewska A.; RT "Removal of RTF2 from Stalled Replisomes Promotes Maintenance of Genome RT Integrity."; RL Mol. Cell 69:24-35.E5(2018). RN [74] RP INTERACTION WITH HMCES. RX PubMed=30554877; DOI=10.1016/j.cell.2018.10.055; RA Mohni K.N., Wessel S.R., Zhao R., Wojciechowski A.C., Luzwick J.W., RA Layden H., Eichman B.F., Thompson P.S., Mehta K.P.M., Cortez D.; RT "HMCES maintains genome integrity by shielding abasic sites in single- RT strand DNA."; RL Cell 176:144-153(2019). RN [75] RP FUNCTION. RX PubMed=35585232; DOI=10.1038/s41586-022-04759-1; RA Baris Y., Taylor M.R.G., Aria V., Yeeles J.T.P.; RT "Fast and efficient DNA replication with purified human proteins."; RL Nature 606:204-210(2022). RN [76] RP INTERACTION WITH DDUP. RX PubMed=35849344; DOI=10.1093/nar/gkac611; RA Yu R., Hu Y., Zhang S., Li X., Tang M., Yang M., Wu X., Li Z., Liao X., RA Xu Y., Li M., Chen S., Qian W., Gong L.Y., Song L., Li J.; RT "LncRNA CTBP1-DT-encoded microprotein DDUP sustains DNA damage response RT signalling to trigger dual DNA repair mechanisms."; RL Nucleic Acids Res. 50:8060-8079(2022). RN [77] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=8861913; DOI=10.1016/s0092-8674(00)81347-1; RA Gulbis J.M., Kelman Z., Hurwitz J., O'Donnell M., Kuriyan J.; RT "Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human RT PCNA."; RL Cell 87:297-306(1996). RN [78] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH FEN1. RX PubMed=15616578; DOI=10.1038/sj.emboj.7600519; RA Sakurai S., Kitano K., Yamaguchi H., Hamada K., Okada K., Fukuda K., RA Uchida M., Ohtsuka E., Morioka H., Hakoshima T.; RT "Structural basis for recruitment of human flap endonuclease 1 to PCNA."; RL EMBO J. 24:683-693(2005). RN [79] {ECO:0007744|PDB:5IY4} RP X-RAY CRYSTALLOGRAPHY (2.94 ANGSTROMS) IN COMPLEX WITH SPRTN. RX PubMed=27084448; DOI=10.1016/j.bbrc.2016.04.053; RA Wang Y., Xu M., Jiang T.; RT "Crystal structure of human PCNA in complex with the PIP box of DVC1."; RL Biochem. Biophys. Res. Commun. 474:264-270(2016). RN [80] {ECO:0007744|PDB:4ZTD} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-254 IN COMPLEX WITH TRAIP. RX PubMed=26711499; DOI=10.1083/jcb.201506071; RA Hoffmann S., Smedegaard S., Nakamura K., Mortuza G.B., Raschle M., RA Ibanez de Opakua A., Oka Y., Feng Y., Blanco F.J., Mann M., Montoya G., RA Groth A., Bekker-Jensen S., Mailand N.; RT "TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability RT after replication stress."; RL J. Cell Biol. 212:63-75(2016). RN [81] {ECO:0007744|PDB:5YCO} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), INTERACTION WITH UHRF2, AND RP MUTAGENESIS OF MET-40; ILE-128; TYR-250 AND ALA-252. RX PubMed=28951215; DOI=10.1016/j.bbrc.2017.09.102; RA Chen W., Wu M., Hang T., Wang C., Zhang X., Zang J.; RT "Structure insights into the molecular mechanism of the interaction between RT UHRF2 and PCNA."; RL Biochem. Biophys. Res. Commun. 494:575-580(2017). CC -!- FUNCTION: Auxiliary protein of DNA polymerase delta and epsilon, is CC involved in the control of eukaryotic DNA replication by increasing the CC polymerase's processibility during elongation of the leading strand CC (PubMed:35585232). Induces a robust stimulatory effect on the 3'-5' CC exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic CC (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order CC to be able to stimulate APEX2. Plays a key role in DNA damage response CC (DDR) by being conveniently positioned at the replication fork to CC coordinate DNA replication with DNA repair and DNA damage tolerance CC pathways (PubMed:24939902). Acts as a loading platform to recruit DDR CC proteins that allow completion of DNA replication after DNA damage and CC promote postreplication repair: Monoubiquitinated PCNA leads to CC recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked CC polyubiquitination of PCNA is involved in error-free pathway and CC employs recombination mechanisms to synthesize across the lesion CC (PubMed:24695737). {ECO:0000269|PubMed:18719106, CC ECO:0000269|PubMed:19443450, ECO:0000269|PubMed:24695737, CC ECO:0000269|PubMed:24939902, ECO:0000269|PubMed:35585232}. CC -!- SUBUNIT: Homotrimer (PubMed:24939902). Interacts with p300/EP300; the CC interaction occurs on chromatin in UV-irradiated damaged cells CC (PubMed:24939902). Interacts with CREBBP (via transactivation domain CC and C-terminus); the interaction occurs on chromatin in UV-irradiated CC damaged cells (PubMed:24939902). Directly interacts with POLD1, POLD3 CC and POLD4 subunits of the DNA polymerase delta complex, POLD3 being the CC major interacting partner; the interaction with POLD3 is inhibited by CC CDKN1A/p21(CIP1) (PubMed:11595739, PubMed:16510448, PubMed:22148433, CC PubMed:24939902). Forms a complex with activator 1 heteropentamer in CC the presence of ATP. Interacts with EXO1, POLH, POLK, DNMT1, ERCC5, CC FEN1, CDC6 and POLDIP2 (PubMed:9305916, PubMed:9302295, PubMed:9566895, CC PubMed:11784855, PubMed:12522211, PubMed:15225546, PubMed:15149598, CC PubMed:24911150, PubMed:15616578, PubMed:26760506). Interacts with POLB CC (PubMed:19336415, PubMed:26760506). Interacts with APEX2; this CC interaction is triggered by reactive oxygen species and increased by CC misincorporation of uracil in nuclear DNA (PubMed:11376153, CC PubMed:19443450). Forms a ternary complex with DNTTIP2 and core histone CC (PubMed:12786946). Interacts with KCTD10 and PPP1R15A (By similarity). CC Interacts with SMARCA5/SNF2H (PubMed:15543136). Interacts with CC BAZ1B/WSTF; the interaction is direct and is required for BAZ1B/WSTF CC binding to replication foci during S phase (PubMed:15543136). Interacts CC with HLTF and SHPRH (PubMed:17130289, PubMed:18316726, CC PubMed:18719106). Interacts with NUDT15; this interaction is disrupted CC in response to UV irradiation and acetylation (PubMed:19419956). CC Interacts with CDKN1A/p21(CIP1) and CDT1; interacts via their PIP-box CC which also recruits the DCX(DTL) complex. The interaction with CDKN1A CC inhibits POLD3 binding (PubMed:11595739, PubMed:16949367, CC PubMed:18794347, PubMed:18703516). Interacts with DDX11 CC (PubMed:18499658). Interacts with EGFR; positively regulates PCNA CC (PubMed:17115032). Interacts with PARPBP (PubMed:22153967). Interacts CC (when ubiquitinated) with SPRTN; leading to enhance RAD18-mediated PCNA CC ubiquitination (PubMed:22681887, PubMed:27084448). Interacts (when CC polyubiquitinated) with ZRANB3 (PubMed:22704558, PubMed:22705370, CC PubMed:22759634). Interacts with SMARCAD1 (PubMed:21549307). Interacts CC with CDKN1C (PubMed:22634751). Interacts with PCLAF (via PIP-box) CC (PubMed:21628590, PubMed:23000965). Interacts with RTEL1 (via PIP-box); CC the interaction is direct and essential for the suppression of telomere CC fragility (PubMed:24115439). Interacts with FAM111A (via PIP-box); the CC interaction is direct and required for PCNA loading on chromatin CC binding (PubMed:24561620). Interacts with LIG1 (PubMed:24911150). CC Interacts with SETMAR (PubMed:20457750). Interacts with ANKRD17 CC (PubMed:23711367). Interacts with FBXO18/FBH1 (via PIP-box); the CC interaction recruits the DCX(DTL) complex and promotes ubiquitination CC and degradation of FBXO18/FBH1 (PubMed:23677613). Interacts with POLN CC (PubMed:19995904). Interacts with SDE2 (via PIP-box); the interaction CC is direct and prevents ultraviolet light induced monoubiquitination CC (PubMed:27906959). Component of the replisome complex composed of at CC least DONSON, MCM2, MCM7, PCNA and TICRR; interaction at least with CC PCNA occurs during DNA replication (PubMed:28191891). Interacts with CC MAPK15; the interaction is chromatin binding dependent and prevents CC MDM2-mediated PCNA destruction by inhibiting the association of PCNA CC with MDM2 (PubMed:20733054). Interacts with PARP10 (via PIP-box) CC (PubMed:24695737). Interacts with DDI2 (PubMed:29290612). Interacts CC with HMCES (via PIP-box) (PubMed:30554877). Interacts with TRAIP (via CC PIP-box) (PubMed:27462463, PubMed:26711499). Interacts with UHRF2 CC (PubMed:28951215). Interacts with ALKBH2; this interaction is enhanced CC during the S-phase of the cell cycle. Interacts with ATAD5; the CC interaction promotes USP1-mediated PCNA deubiquitination CC (PubMed:20147293). Interacts with DNA damage up-regulated protein DDUP CC (PubMed:35849344). {ECO:0000250|UniProtKB:P04961, CC ECO:0000250|UniProtKB:P17918, ECO:0000269|PubMed:11376153, CC ECO:0000269|PubMed:11595739, ECO:0000269|PubMed:11784855, CC ECO:0000269|PubMed:12522211, ECO:0000269|PubMed:12786946, CC ECO:0000269|PubMed:15149598, ECO:0000269|PubMed:15225546, CC ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:15616578, CC ECO:0000269|PubMed:16510448, ECO:0000269|PubMed:16949367, CC ECO:0000269|PubMed:17115032, ECO:0000269|PubMed:17130289, CC ECO:0000269|PubMed:18316726, ECO:0000269|PubMed:18499658, CC ECO:0000269|PubMed:18703516, ECO:0000269|PubMed:18719106, CC ECO:0000269|PubMed:18794347, ECO:0000269|PubMed:19336415, CC ECO:0000269|PubMed:19419956, ECO:0000269|PubMed:19443450, CC ECO:0000269|PubMed:19995904, ECO:0000269|PubMed:20147293, CC ECO:0000269|PubMed:20457750, ECO:0000269|PubMed:20733054, CC ECO:0000269|PubMed:21549307, ECO:0000269|PubMed:21628590, CC ECO:0000269|PubMed:22148433, ECO:0000269|PubMed:22153967, CC ECO:0000269|PubMed:22634751, ECO:0000269|PubMed:22681887, CC ECO:0000269|PubMed:22704558, ECO:0000269|PubMed:22705370, CC ECO:0000269|PubMed:22759634, ECO:0000269|PubMed:23000965, CC ECO:0000269|PubMed:23677613, ECO:0000269|PubMed:23711367, CC ECO:0000269|PubMed:24115439, ECO:0000269|PubMed:24561620, CC ECO:0000269|PubMed:24695737, ECO:0000269|PubMed:24911150, CC ECO:0000269|PubMed:24939902, ECO:0000269|PubMed:26408825, CC ECO:0000269|PubMed:26760506, ECO:0000269|PubMed:27084448, CC ECO:0000269|PubMed:27462463, ECO:0000269|PubMed:27906959, CC ECO:0000269|PubMed:28191891, ECO:0000269|PubMed:29290612, CC ECO:0000269|PubMed:30554877, ECO:0000269|PubMed:35849344, CC ECO:0000269|PubMed:9302295, ECO:0000269|PubMed:9305916, CC ECO:0000269|PubMed:9566895}. CC -!- SUBUNIT: (Microbial infection) Interacts with herpes virus 8 protein CC LANA1. {ECO:0000269|PubMed:26223641}. CC -!- INTERACTION: CC P12004; P04075: ALDOA; NbExp=3; IntAct=EBI-358311, EBI-709613; CC P12004; P03950: ANG; NbExp=4; IntAct=EBI-358311, EBI-525291; CC P12004; P07355: ANXA2; NbExp=2; IntAct=EBI-358311, EBI-352622; CC P12004; P61769: B2M; NbExp=3; IntAct=EBI-358311, EBI-714718; CC P12004; P38936: CDKN1A; NbExp=37; IntAct=EBI-358311, EBI-375077; CC P12004; P42771: CDKN2A; NbExp=8; IntAct=EBI-358311, EBI-375053; CC P12004; Q9H211: CDT1; NbExp=2; IntAct=EBI-358311, EBI-456953; CC P12004; Q13111: CHAF1A; NbExp=4; IntAct=EBI-358311, EBI-1020839; CC P12004; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-358311, EBI-11522780; CC P12004; P68104: EEF1A1; NbExp=2; IntAct=EBI-358311, EBI-352162; CC P12004; P06733: ENO1; NbExp=3; IntAct=EBI-358311, EBI-353877; CC P12004; P39748: FEN1; NbExp=19; IntAct=EBI-358311, EBI-707816; CC P12004; P04406: GAPDH; NbExp=3; IntAct=EBI-358311, EBI-354056; CC P12004; Q14527: HLTF; NbExp=2; IntAct=EBI-358311, EBI-1045161; CC P12004; Q9H160: ING2; NbExp=3; IntAct=EBI-358311, EBI-389787; CC P12004; Q9H063: MAF1; NbExp=4; IntAct=EBI-358311, EBI-720354; CC P12004; P20585: MSH3; NbExp=6; IntAct=EBI-358311, EBI-1164205; CC P12004; O95944: NCR2; NbExp=7; IntAct=EBI-358311, EBI-14058375; CC P12004; P61970: NUTF2; NbExp=3; IntAct=EBI-358311, EBI-591778; CC P12004; Q15004: PCLAF; NbExp=5; IntAct=EBI-358311, EBI-10971436; CC P12004; P12004: PCNA; NbExp=11; IntAct=EBI-358311, EBI-358311; CC P12004; P18669: PGAM1; NbExp=2; IntAct=EBI-358311, EBI-717905; CC P12004; P00558: PGK1; NbExp=2; IntAct=EBI-358311, EBI-709599; CC P12004; P28340: POLD1; NbExp=3; IntAct=EBI-358311, EBI-716569; CC P12004; P49005: POLD2; NbExp=3; IntAct=EBI-358311, EBI-372354; CC P12004; Q15054: POLD3; NbExp=7; IntAct=EBI-358311, EBI-864956; CC P12004; Q9HCU8: POLD4; NbExp=4; IntAct=EBI-358311, EBI-864968; CC P12004; P30041: PRDX6; NbExp=2; IntAct=EBI-358311, EBI-2255129; CC P12004; Q9UBF6: RNF7; NbExp=3; IntAct=EBI-358311, EBI-398632; CC P12004; Q86TU7: SETD3; NbExp=3; IntAct=EBI-358311, EBI-2908049; CC P12004; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-358311, EBI-10262251; CC P12004; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-358311, EBI-742688; CC P12004; A2RU14: TMEM218; NbExp=4; IntAct=EBI-358311, EBI-10173151; CC P12004; P60174: TPI1; NbExp=2; IntAct=EBI-358311, EBI-717475; CC P12004; Q5FWF4: ZRANB3; NbExp=8; IntAct=EBI-358311, EBI-13954615; CC P12004; Q8TE30; NbExp=6; IntAct=EBI-358311, EBI-8874509; CC P12004; Q9Z111: Gadd45g; Xeno; NbExp=9; IntAct=EBI-358311, EBI-1173616; CC P12004; Q1K9H5: PB1; Xeno; NbExp=2; IntAct=EBI-358311, EBI-6050669; CC P12004; B4URF7: PB2; Xeno; NbExp=2; IntAct=EBI-358311, EBI-6050648; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15543136, CC ECO:0000269|PubMed:24115439, ECO:0000269|PubMed:24939902}. CC Note=Colocalizes with CREBBP, EP300 and POLD1 to sites of DNA damage CC (PubMed:24939902). Forms nuclear foci representing sites of ongoing DNA CC replication and vary in morphology and number during S phase CC (PubMed:15543136). Co-localizes with SMARCA5/SNF2H and BAZ1B/WSTF at CC replication foci during S phase (PubMed:15543136). Together with APEX2, CC is redistributed in discrete nuclear foci in presence of oxidative DNA CC damaging agents. {ECO:0000269|PubMed:15543136, CC ECO:0000269|PubMed:24939902}. CC -!- PTM: Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes CC chromatin-associated PCNA. {ECO:0000269|PubMed:17115032}. CC -!- PTM: Acetylated by CREBBP and p300/EP300; preferentially acetylated by CC CREBBP on Lys-80, Lys-13 and Lys-14 and on Lys-77 by p300/EP300 upon CC loading on chromatin in response to UV irradiation (PubMed:24939902, CC PubMed:19419956). Lysine acetylation disrupts association with CC chromatin, hence promoting PCNA ubiquitination and proteasomal CC degradation in response to UV damage in a CREBBP- and EP300-dependent CC manner (PubMed:24939902). Acetylation disrupts interaction with NUDT15 CC and promotes degradation (PubMed:19419956). CC {ECO:0000269|PubMed:24939902}. CC -!- PTM: Ubiquitinated (PubMed:24939902, PubMed:20227374). Following DNA CC damage, can be either monoubiquitinated to stimulate direct bypass of CC DNA lesions by specialized DNA polymerases or polyubiquitinated to CC promote recombination-dependent DNA synthesis across DNA lesions by CC template switching mechanisms. Following induction of replication CC stress, monoubiquitinated by the UBE2B-RAD18 complex on Lys-164, CC leading to recruit translesion (TLS) polymerases, which are able to CC synthesize across DNA lesions in a potentially error-prone manner. An CC error-free pathway also exists and requires non-canonical CC polyubiquitination on Lys-164 through 'Lys-63' linkage of ubiquitin CC moieties by the E2 complex UBE2N-UBE2V2 and the E3 ligases, HLTF, RNF8 CC and SHPRH. This error-free pathway, also known as template switching, CC employs recombination mechanisms to synthesize across the lesion, using CC as a template the undamaged, newly synthesized strand of the sister CC chromatid. Monoubiquitination at Lys-164 also takes place in undamaged CC proliferating cells, and is mediated by the DCX(DTL) complex, leading CC to enhance PCNA-dependent translesion DNA synthesis. Sumoylated during CC S phase. {ECO:0000269|PubMed:15149598, ECO:0000269|PubMed:17108083, CC ECO:0000269|PubMed:17130289, ECO:0000269|PubMed:18316726, CC ECO:0000269|PubMed:18719106, ECO:0000269|PubMed:18948756, CC ECO:0000269|PubMed:20129063, ECO:0000269|PubMed:20227374, CC ECO:0000269|PubMed:22153967, ECO:0000269|PubMed:24939902}. CC -!- PTM: Methylated on glutamate residues by ARMT1/C6orf211. CC {ECO:0000269|PubMed:25732820}. CC -!- DISEASE: Ataxia-telangiectasia-like disorder 2 (ATLD2) [MIM:615919]: A CC neurodegenerative disorder due to defects in DNA excision repair. ATLD2 CC is characterized by developmental delay, ataxia, sensorineural hearing CC loss, short stature, cutaneous and ocular telangiectasia, and CC photosensitivity. {ECO:0000269|PubMed:24911150}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Antibodies against PCNA are present in sera from CC patients with systemic lupus erythematosus. CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/pcna/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=PCNA entry; CC URL="https://en.wikipedia.org/wiki/PCNA"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/41670/PCNA"; 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; M15796; AAA35736.1; -; mRNA. DR EMBL; J04718; AAA60040.1; -; Genomic_DNA. DR EMBL; AF527838; AAM78556.1; -; Genomic_DNA. DR EMBL; AK313286; BAG36094.1; -; mRNA. DR EMBL; AL121924; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471133; EAX10428.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10429.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10430.1; -; Genomic_DNA. DR EMBL; BC000491; AAH00491.1; -; mRNA. DR EMBL; BC062439; AAH62439.1; -; mRNA. DR CCDS; CCDS13087.1; -. DR PIR; A27445; WMHUET. DR RefSeq; NP_002583.1; NM_002592.2. DR RefSeq; NP_872590.1; NM_182649.1. DR PDB; 1AXC; X-ray; 2.60 A; A/C/E=1-261. DR PDB; 1U76; X-ray; 2.60 A; A/C/E=1-261. DR PDB; 1U7B; X-ray; 1.88 A; A=1-261. DR PDB; 1UL1; X-ray; 2.90 A; A/B/C=1-261. DR PDB; 1VYJ; X-ray; 2.80 A; A/C/E/G/I/K=1-261. DR PDB; 1VYM; X-ray; 2.30 A; A/B/C=1-261. DR PDB; 1W60; X-ray; 3.15 A; A/B=1-261. DR PDB; 2ZVK; X-ray; 2.70 A; A/B/C=1-261. DR PDB; 2ZVL; X-ray; 2.50 A; A/B/C/D/E/F=1-261. DR PDB; 2ZVM; X-ray; 2.30 A; A/B/C=1-261. DR PDB; 3JA9; EM; 22.00 A; A/B/C=1-261. DR PDB; 3P87; X-ray; 2.99 A; A/B/C/D/E/F=1-261. DR PDB; 3TBL; X-ray; 2.90 A; A/B/C=1-261. DR PDB; 3VKX; X-ray; 2.10 A; A=1-261. DR PDB; 3WGW; X-ray; 2.80 A; A/B=1-261. DR PDB; 4D2G; X-ray; 2.65 A; A/B/C=1-261. DR PDB; 4RJF; X-ray; 2.01 A; A/C/E=1-261. DR PDB; 4ZTD; X-ray; 2.20 A; A/B/C=2-254. DR PDB; 5E0T; X-ray; 2.67 A; A/B/C=1-261. DR PDB; 5E0U; X-ray; 1.93 A; A/B/C=1-261. DR PDB; 5E0V; X-ray; 2.07 A; A/B=1-261. DR PDB; 5IY4; X-ray; 2.94 A; A/C/E=1-261. DR PDB; 5MAV; X-ray; 2.58 A; A/B/C/D/E/F=1-261. DR PDB; 5MLO; X-ray; 1.96 A; A/C/E=1-261. DR PDB; 5MLW; X-ray; 2.45 A; A/C/E=1-261. DR PDB; 5MOM; X-ray; 2.27 A; A/B/C=1-258. DR PDB; 5YCO; X-ray; 2.20 A; A/B/C/D=1-261. DR PDB; 5YD8; X-ray; 2.30 A; X/Y/Z=1-261. DR PDB; 6CBI; X-ray; 2.75 A; A/B/C/D/E/F=1-261. DR PDB; 6EHT; X-ray; 3.20 A; A/B=1-254, C=1-255. DR PDB; 6FCM; X-ray; 2.80 A; A/C/E=1-261. DR PDB; 6FCN; X-ray; 3.22 A; A/C/E=1-261. DR PDB; 6GIS; X-ray; 2.82 A; A/B/C=1-261. DR PDB; 6GWS; X-ray; 2.90 A; A/B/C=1-261. DR PDB; 6HVO; X-ray; 2.10 A; A/B/C=1-261. DR PDB; 6K3A; X-ray; 2.30 A; A/C/E=1-261. DR PDB; 6QC0; X-ray; 3.50 A; A/C/E=1-261. DR PDB; 6QCG; X-ray; 3.40 A; A/B/C/D/E/F=1-261. DR PDB; 6S1M; EM; 4.27 A; E/F/G=1-261. DR PDB; 6S1N; EM; 4.86 A; E/F/G=1-261. DR PDB; 6S1O; EM; 8.10 A; E/F/G=1-261. DR PDB; 6TNY; EM; 3.08 A; E/F/G=1-261. DR PDB; 6TNZ; EM; 4.05 A; E/F/G=1-261. DR PDB; 6VVO; EM; 3.40 A; F/G/H=1-261. DR PDB; 7EFA; X-ray; 2.70 A; A=1-261. DR PDB; 7KQ0; X-ray; 2.40 A; A/C/E=1-259. DR PDB; 7KQ1; X-ray; 3.30 A; A/C/E=1-259. DR PDB; 7M5L; X-ray; 3.00 A; A/B/C=1-258. DR PDB; 7M5M; X-ray; 3.00 A; A/B/C=1-259. DR PDB; 7M5N; X-ray; 3.11 A; A/B/C=1-259. DR PDB; 7NV0; EM; 3.40 A; B/C/D=1-261. DR PDB; 7NV1; EM; 6.40 A; B/C/D=1-261. DR PDB; 7QNZ; EM; 4.58 A; B/C/D=1-261. DR PDB; 7QO1; EM; 4.40 A; B/F/G=1-261. DR PDB; 8B8T; EM; 4.20 A; E/F/G=1-255. DR PDB; 8COB; X-ray; 2.73 A; A/C/E=1-261. DR PDB; 8E84; X-ray; 3.10 A; A/B/C=1-261. DR PDB; 8F5Q; X-ray; 1.90 A; A/C/E=1-259. DR PDB; 8GL9; X-ray; 2.81 A; A/B/C/D=1-261. DR PDB; 8GLA; X-ray; 3.77 A; A/B/C/D=1-261. DR PDBsum; 1AXC; -. DR PDBsum; 1U76; -. DR PDBsum; 1U7B; -. DR PDBsum; 1UL1; -. DR PDBsum; 1VYJ; -. DR PDBsum; 1VYM; -. DR PDBsum; 1W60; -. DR PDBsum; 2ZVK; -. DR PDBsum; 2ZVL; -. DR PDBsum; 2ZVM; -. DR PDBsum; 3JA9; -. DR PDBsum; 3P87; -. DR PDBsum; 3TBL; -. DR PDBsum; 3VKX; -. DR PDBsum; 3WGW; -. DR PDBsum; 4D2G; -. DR PDBsum; 4RJF; -. DR PDBsum; 4ZTD; -. DR PDBsum; 5E0T; -. DR PDBsum; 5E0U; -. DR PDBsum; 5E0V; -. DR PDBsum; 5IY4; -. DR PDBsum; 5MAV; -. DR PDBsum; 5MLO; -. DR PDBsum; 5MLW; -. DR PDBsum; 5MOM; -. DR PDBsum; 5YCO; -. DR PDBsum; 5YD8; -. DR PDBsum; 6CBI; -. DR PDBsum; 6EHT; -. DR PDBsum; 6FCM; -. DR PDBsum; 6FCN; -. DR PDBsum; 6GIS; -. DR PDBsum; 6GWS; -. DR PDBsum; 6HVO; -. DR PDBsum; 6K3A; -. DR PDBsum; 6QC0; -. DR PDBsum; 6QCG; -. DR PDBsum; 6S1M; -. DR PDBsum; 6S1N; -. DR PDBsum; 6S1O; -. DR PDBsum; 6TNY; -. DR PDBsum; 6TNZ; -. DR PDBsum; 6VVO; -. DR PDBsum; 7EFA; -. DR PDBsum; 7KQ0; -. DR PDBsum; 7KQ1; -. DR PDBsum; 7M5L; -. DR PDBsum; 7M5M; -. DR PDBsum; 7M5N; -. DR PDBsum; 7NV0; -. DR PDBsum; 7NV1; -. DR PDBsum; 7QNZ; -. DR PDBsum; 7QO1; -. DR PDBsum; 8B8T; -. DR PDBsum; 8COB; -. DR PDBsum; 8E84; -. DR PDBsum; 8F5Q; -. DR PDBsum; 8GL9; -. DR PDBsum; 8GLA; -. DR AlphaFoldDB; P12004; -. DR BMRB; P12004; -. DR EMDB; EMD-10080; -. DR EMDB; EMD-10081; -. DR EMDB; EMD-10082; -. DR EMDB; EMD-10539; -. DR EMDB; EMD-10540; -. DR EMDB; EMD-12601; -. DR EMDB; EMD-12602; -. DR EMDB; EMD-15921; -. DR EMDB; EMD-21405; -. DR SASBDB; P12004; -. DR SMR; P12004; -. DR BioGRID; 111142; 498. DR ComplexPortal; CPX-538; PCNA homotrimer. DR CORUM; P12004; -. DR DIP; DIP-1098N; -. DR ELM; P12004; -. DR IntAct; P12004; 436. DR MINT; P12004; -. DR STRING; 9606.ENSP00000368458; -. DR BindingDB; P12004; -. DR ChEMBL; CHEMBL2346488; -. DR DrugBank; DB00945; Acetylsalicylic acid. DR DrugBank; DB00279; Liothyronine. DR DrugCentral; P12004; -. DR MoonDB; P12004; Predicted. DR GlyCosmos; P12004; 1 site, 1 glycan. DR GlyGen; P12004; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P12004; -. DR MetOSite; P12004; -. DR PhosphoSitePlus; P12004; -. DR SwissPalm; P12004; -. DR BioMuta; PCNA; -. DR DMDM; 129694; -. DR CPTAC; CPTAC-1224; -. DR CPTAC; CPTAC-1225; -. DR CPTAC; CPTAC-3242; -. DR CPTAC; CPTAC-3243; -. DR CPTAC; CPTAC-3244; -. DR CPTAC; CPTAC-3245; -. DR CPTAC; CPTAC-558; -. DR CPTAC; CPTAC-559; -. DR CPTAC; CPTAC-722; -. DR EPD; P12004; -. DR jPOST; P12004; -. DR MassIVE; P12004; -. DR MaxQB; P12004; -. DR PaxDb; 9606-ENSP00000368458; -. DR PeptideAtlas; P12004; -. DR ProteomicsDB; 52816; -. DR Pumba; P12004; -. DR TopDownProteomics; P12004; -. DR ABCD; P12004; 1 sequenced antibody. DR Antibodypedia; 3769; 3055 antibodies from 54 providers. DR CPTC; P12004; 4 antibodies. DR DNASU; 5111; -. DR Ensembl; ENST00000379143.10; ENSP00000368438.5; ENSG00000132646.11. DR Ensembl; ENST00000379160.3; ENSP00000368458.3; ENSG00000132646.11. DR GeneID; 5111; -. DR KEGG; hsa:5111; -. DR MANE-Select; ENST00000379143.10; ENSP00000368438.5; NM_182649.2; NP_872590.1. DR UCSC; uc002wlp.4; human. DR AGR; HGNC:8729; -. DR CTD; 5111; -. DR DisGeNET; 5111; -. DR GeneCards; PCNA; -. DR HGNC; HGNC:8729; PCNA. DR HPA; ENSG00000132646; Tissue enhanced (bone). DR MalaCards; PCNA; -. DR MIM; 176740; gene. DR MIM; 615919; phenotype. DR neXtProt; NX_P12004; -. DR OpenTargets; ENSG00000132646; -. DR Orphanet; 438134; PCNA-related progressive neurodegenerative photosensitivity syndrome. DR PharmGKB; PA263; -. DR VEuPathDB; HostDB:ENSG00000132646; -. DR eggNOG; KOG1636; Eukaryota. DR GeneTree; ENSGT00390000004965; -. DR HOGENOM; CLU_043978_3_0_1; -. DR InParanoid; P12004; -. DR OMA; EMKLINM; -. DR OrthoDB; 118939at2759; -. DR PhylomeDB; P12004; -. DR TreeFam; TF313441; -. DR PathwayCommons; P12004; -. 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-1362277; Transcription of E2F targets under negative control by DREAM complex. DR Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere. DR Reactome; R-HSA-174414; Processive synthesis on the C-strand of the telomere. DR Reactome; R-HSA-174417; Telomere C-strand (Lagging Strand) Synthesis. DR Reactome; R-HSA-174437; Removal of the Flap Intermediate from the C-strand. DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins. DR Reactome; R-HSA-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha). DR Reactome; R-HSA-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta). 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-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest. DR Reactome; R-HSA-69091; Polymerase switching. DR Reactome; R-HSA-69166; Removal of the Flap Intermediate. DR Reactome; R-HSA-69183; Processive synthesis on the lagging strand. DR Reactome; R-HSA-69205; G1/S-Specific Transcription. DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins. DR SignaLink; P12004; -. DR SIGNOR; P12004; -. DR BioGRID-ORCS; 5111; 865 hits in 1151 CRISPR screens. DR ChiTaRS; PCNA; human. DR EvolutionaryTrace; P12004; -. DR GeneWiki; Proliferating_cell_nuclear_antigen; -. DR GenomeRNAi; 5111; -. DR Pharos; P12004; Tchem. DR PRO; PR:P12004; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; P12004; Protein. DR Bgee; ENSG00000132646; Expressed in oocyte and 198 other cell types or tissues. DR GO; GO:0005813; C:centrosome; IDA:MGI. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL. DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005652; C:nuclear lamina; IEA:Ensembl. DR GO; GO:0043596; C:nuclear replication fork; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0043626; C:PCNA complex; IDA:UniProtKB. DR GO; GO:0070557; C:PCNA-p21 complex; IDA:UniProtKB. DR GO; GO:0005657; C:replication fork; IDA:MGI. DR GO; GO:0030894; C:replisome; TAS:BHF-UCL. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB. DR GO; GO:0032139; F:dinucleotide insertion or deletion binding; IDA:BHF-UCL. DR GO; GO:0070182; F:DNA polymerase binding; IPI:UniProtKB. DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IBA:GO_Central. DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL. DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0032405; F:MutLalpha complex binding; IDA:HGNC-UCL. DR GO; GO:0030331; F:nuclear estrogen receptor binding; IEA:Ensembl. DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB. DR GO; GO:0000701; F:purine-specific mismatch base pair DNA N-glycosylase activity; IDA:BHF-UCL. DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB. DR GO; GO:0006287; P:base-excision repair, gap-filling; IEA:Ensembl. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl. DR GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB. DR GO; GO:0044849; P:estrous cycle; IEA:Ensembl. DR GO; GO:0007507; P:heart development; IEA:Ensembl. DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central. DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl. DR GO; GO:0006298; P:mismatch repair; IDA:BHF-UCL. DR GO; GO:1902990; P:mitotic telomere maintenance via semi-conservative replication; ISS:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0032077; P:positive regulation of deoxyribonuclease activity; IDA:UniProtKB. DR GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB. DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:UniProtKB. DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IMP:UniProtKB. DR GO; GO:0031297; P:replication fork processing; ISS:BHF-UCL. DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl. DR GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:1902065; P:response to L-glutamate; IEA:Ensembl. DR GO; GO:0019985; P:translesion synthesis; IDA:UniProtKB. DR CDD; cd00577; PCNA; 1. DR Gene3D; 3.70.10.10; -; 1. DR HAMAP; MF_00317; DNApol_clamp_arch; 1. DR IDEAL; IID00022; -. 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. DR SWISS-2DPAGE; P12004; -. DR Genevisible; P12004; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Deafness; Direct protein sequencing; KW Disease variant; DNA damage; DNA repair; DNA replication; DNA-binding; KW Dwarfism; Host-virus interaction; Isopeptide bond; Methylation; KW Neurodegeneration; Nucleus; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT CHAIN 1..261 FT /note="Proliferating cell nuclear antigen" FT /id="PRO_0000149158" FT DNA_BIND 61..80 FT /evidence="ECO:0000255" FT REGION 7..100 FT /note="Interaction with NUDT15" FT /evidence="ECO:0000269|PubMed:19419956" FT MOD_RES 14 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:19419956" FT MOD_RES 77 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 80 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 211 FT /note="Phosphotyrosine; by EGFR" FT /evidence="ECO:0000269|PubMed:17115032" FT MOD_RES 248 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 164 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 164 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000269|PubMed:17108083, FT ECO:0000269|PubMed:17130289" FT CROSSLNK 254 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 228 FT /note="S -> I (in ATLD2; a hypomorphic mutation affecting FT DNA repair in response to UV; results in significantly FT decreased interaction with FEN1, LIG1 and ERCC5; FT dbSNP:rs369958038)" FT /evidence="ECO:0000269|PubMed:24911150" FT /id="VAR_071871" FT MUTAGEN 13 FT /note="K->R: Inhibits acetylation, recruitment to DNA FT damage sites, inducible ubiquitination and protein FT degradation, DNA replication and repair synthesis FT efficiencies, but homotrimer formation, nuclear recruitment FT to DNA damage sites, interactions with CREBBP, EP300 and FT POLD1 are similar as the wild-type; in association with FT R-14; R-20; R-77 and R-80." FT /evidence="ECO:0000269|PubMed:24939902" FT MUTAGEN 14 FT /note="K->R: Inhibits acetylation, recruitment to DNA FT damage sites, inducible ubiquitination and protein FT degradation, DNA replication and repair synthesis FT efficiencies, but homotrimer formation, nuclear recruitment FT to DNA damage sites, interactions with CREBBP, EP300 and FT POLD1 are similar as the wild-type; in association with FT R-13; R-20; R-77 and R-80." FT /evidence="ECO:0000269|PubMed:24939902" FT MUTAGEN 20 FT /note="K->R: Inhibits acetylation, recruitment to DNA FT damage sites, inducible ubiquitination and protein FT degradation, DNA replication and repair synthesis FT efficiencies, but homotrimer formation, nuclear recruitment FT to DNA damage sites, interactions with CREBBP, EP300 and FT POLD1 are similar as the wild-type; in association with FT R-13; R-14; R-77 and R-80." FT /evidence="ECO:0000269|PubMed:24939902" FT MUTAGEN 40 FT /note="M->A: Complete loss of interaction with UHRF2." FT /evidence="ECO:0000269|PubMed:11595739" FT MUTAGEN 43..45 FT /note="SHV->AAA: No effect on POLD3-binding. Impairs FT binding to ALKBH2." FT /evidence="ECO:0000269|PubMed:11595739, FT ECO:0000269|PubMed:26408825" FT MUTAGEN 77 FT /note="K->A: Inhibits recruitment to DNA damage sites, but FT nuclear localization is similar as the wild-type; in FT association with A-80." FT /evidence="ECO:0000269|PubMed:24939902" FT MUTAGEN 77 FT /note="K->R: Inhibits acetylation, recruitment to DNA FT damage sites, inducible ubiquitination and protein FT degradation, DNA replication and repair synthesis FT efficiencies, but homotrimer formation, nuclear recruitment FT to DNA damage sites, interactions with CREBBP, EP300 and FT POLD1 are similar as the wild-type; in association with FT R-13; R-14; R-20 and R-80." FT /evidence="ECO:0000269|PubMed:24939902" FT MUTAGEN 80 FT /note="K->A: Inhibits recruitment to DNA damage sites, but FT nuclear localization is similar as the wild-type; in FT association with A-77." FT /evidence="ECO:0000269|PubMed:24939902" FT MUTAGEN 80 FT /note="K->R: Inhibits acetylation, recruitment to DNA FT damage sites, inducible ubiquitination and protein FT degradation, DNA replication and repair synthesis FT efficiencies, but homotrimer formation, nuclear recruitment FT to DNA damage sites, interactions with CREBBP, EP300 and FT POLD1 are similar as the wild-type; in association with FT R-13; R-14; R-20 and R-77." FT /evidence="ECO:0000269|PubMed:24939902" FT MUTAGEN 125..128 FT /note="QLGI->AAAA: Strong decrease in POLD3-binding. FT Impairs binding to ALKBH2." FT /evidence="ECO:0000269|PubMed:11595739, FT ECO:0000269|PubMed:26408825" FT MUTAGEN 128 FT /note="I->A: Complete loss of interaction with UHRF2." FT /evidence="ECO:0000269|PubMed:11595739" FT MUTAGEN 164 FT /note="K->R: Abolishes ubiquitination. No effect on FT interaction with SHPRH." FT /evidence="ECO:0000269|PubMed:17108083, FT ECO:0000269|PubMed:17130289, ECO:0000269|PubMed:18719106, FT ECO:0000269|PubMed:20129063" FT MUTAGEN 188..190 FT /note="VDK->AAA: No effect on POLD3-binding. No effect on FT ALKBH2-binding." FT /evidence="ECO:0000269|PubMed:11595739, FT ECO:0000269|PubMed:26408825" FT MUTAGEN 211 FT /note="Y->F: Alters chromatin-associated PCNA stability and FT its function in DNA replication and repair." FT /evidence="ECO:0000269|PubMed:17115032" FT MUTAGEN 250 FT /note="Y->A: Complete loss of interaction with UHRF2." FT /evidence="ECO:0000269|PubMed:11595739" FT MUTAGEN 251..254 FT /note="LAPK->AAAA: Decrease in POLD3-binding." FT /evidence="ECO:0000269|PubMed:11595739" FT MUTAGEN 252 FT /note="A->G: Complete loss of interaction with UHRF2." FT /evidence="ECO:0000269|PubMed:11595739" FT STRAND 2..7 FT /evidence="ECO:0007829|PDB:1U7B" FT HELIX 10..20 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 24..31 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 34..40 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 44..53 FT /evidence="ECO:0007829|PDB:1U7B" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 57..64 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 66..71 FT /evidence="ECO:0007829|PDB:1U7B" FT HELIX 72..79 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 87..92 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:1VYM" FT STRAND 97..104 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 106..108 FT /evidence="ECO:0007829|PDB:8F5Q" FT STRAND 111..117 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 121..126 FT /evidence="ECO:0007829|PDB:5E0U" FT STRAND 134..140 FT /evidence="ECO:0007829|PDB:1U7B" FT HELIX 141..152 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 156..163 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 166..173 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 176..182 FT /evidence="ECO:0007829|PDB:1U7B" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:5E0U" FT STRAND 196..201 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 203..208 FT /evidence="ECO:0007829|PDB:1U7B" FT HELIX 209..215 FT /evidence="ECO:0007829|PDB:1U7B" FT HELIX 216..221 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 223..229 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:1VYM" FT STRAND 235..241 FT /evidence="ECO:0007829|PDB:1U7B" FT TURN 242..244 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 245..251 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 254..256 FT /evidence="ECO:0007829|PDB:7KQ1" SQ SEQUENCE 261 AA; 28769 MW; E6F08E7EDBC48B00 CRC64; MFEARLVQGS ILKKVLEALK DLINEACWDI SSSGVNLQSM DSSHVSLVQL TLRSEGFDTY RCDRNLAMGV NLTSMSKILK CAGNEDIITL RAEDNADTLA LVFEAPNQEK VSDYEMKLMD LDVEQLGIPE QEYSCVVKMP SGEFARICRD LSHIGDAVVI SCAKDGVKFS ASGELGNGNI KLSQTSNVDK EEEAVTIEMN EPVQLTFALR YLNFFTKATP LSSTVTLSMS ADVPLVVEYK IADMGHLKYY LAPKIEDEEG S //