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Database: UniProt
Entry: P12004
LinkDB: P12004
Original site: P12004 
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   18-SEP-2019, entry version 226.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Bravo R.;
RT   "Cloning and sequence of the human nuclear protein cyclin: homology
RT   with 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;
RA   Travali S., Ku D.H., Rizzo M.G., Ottavio L., Baserga R.,
RA   Calabretta B.;
RT   "Structure of the human gene for the proliferating cell nuclear
RT   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA   Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA   Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA   Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA   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.,
RA   Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA   Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA   Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA   Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA   Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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
RT   required 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
RT   regions 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
RT   selectively 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
RT   present 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.,
RA   Fujiwara T., Nakabeppu Y.;
RT   "Human APE2 protein is mostly localized in the nuclei and to some
RT   extent in the mitochondria, while nuclear APE2 is partly associated
RT   with 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.,
RA   Prakash L., Prakash S.;
RT   "Stimulation of DNA synthesis activity of human DNA polymerase kappa
RT   by 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.,
RA   Tamai K., Fujisaki S., Hayano T., Koiwai O.;
RT   "Terminal deoxynucleotidyltransferase forms a ternary complex with a
RT   novel 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
RT   p50 subunit of DNA polymerase delta and proliferating cell nuclear
RT   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:
RT   a possible mechanism for the polymerase switch in response to DNA
RT   damage.";
RL   Mol. Cell 14:491-500(2004).
RN   [20]
RP   INTERACTION WITH BAZ1B.
RX   PubMed=15543136; DOI=10.1038/ncb1196;
RA   Poot R.A., Bozhenok L., van den Berg D.L.C., Steffensen S.,
RA   Ferreira F., Grimaldi M., Gilbert N., Ferreira J., Varga-Weisz P.D.;
RT   "The Williams syndrome transcription factor interacts with PCNA to
RT   target 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.,
RA   Lee E.Y., 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,
RT   which is required for S phase destruction of the replication factor
RT   Cdt1.";
RL   Mol. Cell 23:709-721(2006).
RN   [24]
RP   PHOSPHORYLATION AT TYR-211 BY EGFR, MUTAGENESIS OF TYR-211, AND
RP   INTERACTION 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
RT   the CRL4Cdt2 ubiquitin ligase complex.";
RL   Genes Dev. 22:2496-2506(2008).
RN   [28]
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.
RT   Association of ChlR1 with Ctf18-RFC and Fen1.";
RL   J. Biol. Chem. 283:20925-20936(2008).
RN   [29]
RP   INTERACTION WITH CDKN1A.
RX   PubMed=18703516; DOI=10.1074/jbc.m806045200;
RA   Nishitani H., Shiomi Y., Iida H., Michishita M., Takami T.,
RA   Tsurimoto T.;
RT   "CDK inhibitor p21 is degraded by a proliferating cell nuclear
RT   antigen-coupled Cul4-DDB1Cdt2 pathway during S phase and after UV
RT   irradiation.";
RL   J. Biol. Chem. 283:29045-29052(2008).
RN   [30]
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
RT   damage.";
RL   Nucleic Acids Res. 37:4247-4255(2009).
RN   [31]
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
RT   nuclear antigen polyubiquitination.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:3768-3773(2008).
RN   [32]
RP   UBIQUITINATION, FUNCTION, INTERACTION WITH HLTF AND SHPRH, AND
RP   MUTAGENESIS 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.,
RA   Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.;
RT   "Polyubiquitination of proliferating cell nuclear antigen by HLTF and
RT   SHPRH prevents genomic instability from stalled replication forks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008).
RN   [33]
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   [34]
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.,
RA   Walther T.C., 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   [35]
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
RT   inhibiting HDM2-mediated degradation of the DNA clamp PCNA.";
RL   J. Cell Biol. 190:575-586(2010).
RN   [36]
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   [37]
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.,
RA   Mullenders L.H., Yamashita S., Fousteri M.I., Lehmann A.R.;
RT   "Three DNA polymerases, recruited by different mechanisms, carry out
RT   NER repair synthesis in human cells.";
RL   Mol. Cell 37:714-727(2010).
RN   [38]
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   [39]
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
RT   replication forks.";
RL   Nucleic Acids Res. 38:5681-5691(2010).
RN   [40]
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.,
RA   Buerckstuemmer T., 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   [41]
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.,
RA   Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M.,
RA   Varga-Weisz P., Mermoud J.E.;
RT   "Maintenance of silent chromatin through replication requires SWI/SNF-
RT   like chromatin remodeler SMARCAD1.";
RL   Mol. Cell 42:285-296(2011).
RN   [42]
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   [43]
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
RT   switch to regulate its interaction with PCNA.";
RL   Biochemistry 51:416-424(2012).
RN   [44]
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
RT   protein PARI.";
RL   Mol. Cell 45:75-86(2012).
RN   [45]
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
RT   UV-induced DNA damage response.";
RL   Mol. Cell 46:625-635(2012).
RN   [46]
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   [47]
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   [48]
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.,
RA   Choudhary C.;
RT   "Systems-wide analysis of ubiquitylation dynamics reveals a key role
RT   for PAF15 ubiquitylation in DNA-damage bypass.";
RL   Nat. Cell Biol. 14:1089-1098(2012).
RN   [49]
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.,
RA   Livingston D.M., Haracska L., Elledge S.J.;
RT   "Polyubiquitinated PCNA recruits the ZRANB3 translocase to maintain
RT   genomic integrity after replication stress.";
RL   Mol. Cell 47:396-409(2012).
RN   [50]
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.,
RA   Braslavsky D., Bergada I., Dell'Angelica E.C., Nelson S.F.,
RA   Martinez-Agosto J.A., Achermann J.C., Vilain E.;
RT   "Mutations in the PCNA-binding domain of CDKN1C cause IMAGe
RT   syndrome.";
RL   Nat. Genet. 44:788-792(2012).
RN   [51]
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   [52]
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)-
RT   mediated proteolysis in human cells.";
RL   Nucleic Acids Res. 41:6501-6513(2013).
RN   [53]
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   [54]
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
RT   cell nuclear antigen (PCNA) and is required for DNA damage
RT   tolerance.";
RL   J. Biol. Chem. 289:13627-13637(2014).
RN   [55]
RP   INVOLVEMENT IN ATLD2, INTERACTION WITH FEN1; LIG1 AND ERCC5, VARIANT
RP   ATLD2 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.,
RA   Chioza B.A., Harlalka G.V., Mansour S., Sreekantan-Nair A.,
RA   Patton M.A., Muggenthaler M., Rich P., Wagner K., Coblentz R.,
RA   Stein C.K., Last J.I., Taylor A.M., Jackson A.P., Ogi T.,
RA   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   [56]
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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [57]
RP   INTERACTION WITH FAM111A.
RX   PubMed=24561620; DOI=10.1038/ncb2918;
RA   Alabert C., Bukowski-Wills J.C., Lee S.B., Kustatscher G.,
RA   Nakamura K., de Lima Alves F., Menard P., Mejlvang J., Rappsilber J.,
RA   Groth A.;
RT   "Nascent chromatin capture proteomics determines chromatin dynamics
RT   during DNA replication and identifies unknown fork components.";
RL   Nat. Cell Biol. 16:281-293(2014).
RN   [58]
RP   FUNCTION, TRIMERIZATION, INTERACTION WITH CREBBP; EP300 AND POLD1,
RP   ACETYLATION, UBIQUITINATION, ASSOCIATION WITH CHROMATIN, AND
RP   MUTAGENESIS OF 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   [59]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164, AND IDENTIFICATION BY
RP   MASS 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   [60]
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
RT   that targets PCNA and is linked to the DNA damage response.";
RL   Cell Rep. 10:1288-1296(2015).
RN   [61]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164, AND IDENTIFICATION BY
RP   MASS 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   [62]
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
RT   Synthesis.";
RL   J. Virol. 89:10206-10218(2015).
RN   [63]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164, AND IDENTIFICATION BY
RP   MASS 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
RT   replication stress reveals novel small ubiquitin-like modified target
RT   proteins and acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [64]
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.,
RA   Ayoub D., 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   [65]
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   [66]
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.,
RA   Alswaid A., Ahmed S., Al-Aama J.Y., Altmueller J., Al Balwi M.,
RA   Brady A.F., Chessa L., Cox H., Fischetto R., Heller R.,
RA   Henderson B.D., Hobson E., Nuernberg P., Percin E.F., Peron A.,
RA   Spaccini L., Quigley A.J., Thakur S., Wise C.A., Yoon G., Alnemer M.,
RA   Tomancak P., Yigit G., Taylor A.M., Reijns M.A., Simpson M.A.,
RA   Cortez D., Alkuraya F.S., Mathew C.G., Jackson A.P., Stewart G.S.;
RT   "Mutations in DONSON disrupt replication fork stability and cause
RT   microcephalic dwarfism.";
RL   Nat. Genet. 49:537-549(2017).
RN   [67]
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-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [68]
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
RT   Genome Integrity.";
RL   Mol. Cell 69:24-35.E5(2018).
RN   [69]
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   [70]
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
RT   human PCNA.";
RL   Cell 87:297-306(1996).
RN   [71]
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
RT   PCNA.";
RL   EMBO J. 24:683-693(2005).
CC   -!- FUNCTION: Auxiliary protein of DNA polymerase delta and is
CC       involved in the control of eukaryotic DNA replication by
CC       increasing the polymerase's processibility during elongation of
CC       the leading strand. Induces a robust stimulatory effect on the 3'-
CC       5' exonuclease and 3'-phosphodiesterase, but not apurinic-
CC       apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded
CC       onto DNA in order to be able to stimulate APEX2. Plays a key role
CC       in DNA damage response (DDR) by being conveniently positioned at
CC       the replication fork to coordinate DNA replication with DNA repair
CC       and DNA damage tolerance pathways (PubMed:24939902). Acts as a
CC       loading platform to recruit DDR proteins that allow completion of
CC       DNA replication after DNA damage and promote postreplication
CC       repair: Monoubiquitinated PCNA leads to recruitment of translesion
CC       (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of
CC       PCNA is involved in error-free pathway and employs recombination
CC       mechanisms to synthesize across the lesion (PubMed:24695737).
CC       {ECO:0000269|PubMed:18719106, ECO:0000269|PubMed:19443450,
CC       ECO:0000269|PubMed:24695737, ECO:0000269|PubMed:24939902}.
CC   -!- SUBUNIT: Homotrimer (PubMed:24939902). Interacts with p300/EP300;
CC       the interaction occurs on chromatin in UV-irradiated damaged cells
CC       (PubMed:24939902). Interacts with CREBBP (via transactivation
CC       domain and C-terminus); the interaction occurs on chromatin in UV-
CC       irradiated damaged cells (PubMed:24939902). Directly interacts
CC       with POLD1, POLD3 and POLD4 subunits of the DNA polymerase delta
CC       complex, POLD3 being the major interacting partner; the
CC       interaction with POLD3 is inhibited by CDKN1A/p21(CIP1)
CC       (PubMed:11595739, PubMed:16510448, PubMed:22148433,
CC       PubMed:24939902). Forms a complex with activator 1 heteropentamer
CC       in the presence of ATP. Interacts with EXO1, POLH, POLK, DNMT1,
CC       ERCC5, FEN1, CDC6 and POLDIP2 (PubMed:9305916, PubMed:9302295,
CC       PubMed:9566895, PubMed:11784855, PubMed:12522211, PubMed:15225546,
CC       PubMed:15149598, PubMed:24911150, PubMed:15616578). Interacts with
CC       APEX2; this interaction is triggered by reactive oxygen species
CC       and increased by misincorporation of uracil in nuclear DNA
CC       (PubMed:11376153, PubMed:19443450). Forms a ternary complex with
CC       DNTTIP2 and core histone (PubMed:12786946). Interacts with KCTD10
CC       and PPP1R15A (By similarity). Directly interacts with BAZ1B
CC       (PubMed:15543136). Interacts with HLTF and SHPRH (PubMed:17130289,
CC       PubMed:18316726, PubMed:18719106). Interacts with NUDT15; this
CC       interaction is disrupted in response to UV irradiation and
CC       acetylation (PubMed:19419956). Interacts with CDKN1A/p21(CIP1) and
CC       CDT1; interacts via their PIP-box which also recruits the DCX(DTL)
CC       complex. The interaction with CDKN1A inhibits POLD3 binding
CC       (PubMed:11595739, PubMed:16949367, PubMed:18794347,
CC       PubMed:18703516). Interacts with DDX11 (PubMed:18499658).
CC       Interacts with EGFR; positively regulates PCNA (PubMed:17115032).
CC       Interacts with PARPBP (PubMed:22153967). Interacts (when
CC       ubiquitinated) with SPRTN; leading to enhance RAD18-mediated PCNA
CC       ubiquitination (PubMed:22681887). Interacts (when
CC       polyubiquitinated) with ZRANB3 (PubMed:22704558, PubMed:22705370,
CC       PubMed:22759634). Interacts with SMARCAD1 (PubMed:21549307).
CC       Interacts with CDKN1C (PubMed:22634751). Interacts with PCLAF (via
CC       PIP-box) (PubMed:21628590, PubMed:23000965). Interacts with RTEL1
CC       (via PIP-box); the interaction is direct and essential for the
CC       suppression of telomere fragility (PubMed:24115439). Interacts
CC       with FAM111A (via PIP-box); the interaction is direct and required
CC       for PCNA loading on chromatin binding (PubMed:24561620). Interacts
CC       with LIG1 (PubMed:24911150). Interacts with SETMAR
CC       (PubMed:20457750). Interacts with ANKRD17 (PubMed:23711367).
CC       Interacts with FBXO18/FBH1 (via PIP-box); the interaction recruits
CC       the DCX(DTL) complex and promotes ubiquitination and degradation
CC       of FBXO18/FBH1 (PubMed:23677613). Interacts with POLN
CC       (PubMed:19995904). Interacts with SDE2 (via PIP-box); the
CC       interaction is direct and prevents ultraviolet light induced
CC       monoubiquitination (PubMed:27906959). Component of the replisome
CC       complex composed of at least DONSON, MCM2, MCM7, PCNA and TICRR;
CC       interaction at least with PCNA occurs during DNA replication
CC       (PubMed:28191891). Interacts with MAPK15; the interaction is
CC       chromatin binding dependent and prevents MDM2-mediated PCNA
CC       destruction by inhibiting the association of PCNA with MDM2
CC       (PubMed:20733054). Interacts with PARP10 (via PIP-box)
CC       (PubMed:24695737). Interacts with DDI2 (PubMed:29290612).
CC       Interacts with HMCES (via PIP-box) (PubMed:30554877).
CC       {ECO:0000250|UniProtKB:P04961, ECO:0000250|UniProtKB:P17918,
CC       ECO:0000269|PubMed:11376153, ECO:0000269|PubMed:11595739,
CC       ECO:0000269|PubMed:11784855, ECO:0000269|PubMed:12522211,
CC       ECO:0000269|PubMed:12786946, ECO:0000269|PubMed:15149598,
CC       ECO:0000269|PubMed:15225546, ECO:0000269|PubMed:15543136,
CC       ECO:0000269|PubMed:15616578, ECO:0000269|PubMed:16510448,
CC       ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:17115032,
CC       ECO:0000269|PubMed:17130289, ECO:0000269|PubMed:18316726,
CC       ECO:0000269|PubMed:18499658, ECO:0000269|PubMed:18703516,
CC       ECO:0000269|PubMed:18719106, ECO:0000269|PubMed:18794347,
CC       ECO:0000269|PubMed:19419956, ECO:0000269|PubMed:19443450,
CC       ECO:0000269|PubMed:19995904, ECO:0000269|PubMed:20457750,
CC       ECO:0000269|PubMed:20733054, ECO:0000269|PubMed:21549307,
CC       ECO:0000269|PubMed:21628590, ECO:0000269|PubMed:22148433,
CC       ECO:0000269|PubMed:22153967, ECO:0000269|PubMed:22634751,
CC       ECO:0000269|PubMed:22681887, ECO:0000269|PubMed:22704558,
CC       ECO:0000269|PubMed:22705370, ECO:0000269|PubMed:22759634,
CC       ECO:0000269|PubMed:23000965, ECO:0000269|PubMed:23677613,
CC       ECO:0000269|PubMed:23711367, ECO:0000269|PubMed:24115439,
CC       ECO:0000269|PubMed:24561620, ECO:0000269|PubMed:24695737,
CC       ECO:0000269|PubMed:24911150, ECO:0000269|PubMed:24939902,
CC       ECO:0000269|PubMed:27906959, ECO:0000269|PubMed:28191891,
CC       ECO:0000269|PubMed:29290612, ECO:0000269|PubMed:30554877,
CC       ECO:0000269|PubMed:9302295, ECO:0000269|PubMed:9305916,
CC       ECO:0000269|PubMed:9566895}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with herpes virus 8
CC       protein LANA1. {ECO:0000269|PubMed:26223641}.
CC   -!- INTERACTION:
CC       Self; NbExp=7; IntAct=EBI-358311, EBI-358311;
CC       Q8TE30:-; NbExp=6; IntAct=EBI-358311, EBI-8874509;
CC       P04075:ALDOA; NbExp=3; IntAct=EBI-358311, EBI-709613;
CC       P03950:ANG; NbExp=4; IntAct=EBI-358311, EBI-525291;
CC       P61769:B2M; NbExp=2; IntAct=EBI-358311, EBI-714718;
CC       P38936:CDKN1A; NbExp=31; IntAct=EBI-358311, EBI-375077;
CC       P42771:CDKN2A; NbExp=8; IntAct=EBI-358311, EBI-375053;
CC       Q9H211:CDT1; NbExp=2; IntAct=EBI-358311, EBI-456953;
CC       Q13111:CHAF1A; NbExp=4; IntAct=EBI-358311, EBI-1020839;
CC       P06733:ENO1; NbExp=3; IntAct=EBI-358311, EBI-353877;
CC       P39748:FEN1; NbExp=14; IntAct=EBI-358311, EBI-707816;
CC       Q9Z111:Gadd45g (xeno); NbExp=9; IntAct=EBI-358311, EBI-1173616;
CC       P04406:GAPDH; NbExp=3; IntAct=EBI-358311, EBI-354056;
CC       Q14527:HLTF; NbExp=2; IntAct=EBI-358311, EBI-1045161;
CC       Q9H160:ING2; NbExp=3; IntAct=EBI-358311, EBI-389787;
CC       P20585:MSH3; NbExp=5; IntAct=EBI-358311, EBI-1164205;
CC       O95944:NCR2; NbExp=7; IntAct=EBI-358311, EBI-14058375;
CC       Q1K9H5:PB1 (xeno); NbExp=2; IntAct=EBI-358311, EBI-6050669;
CC       B4URF7:PB2 (xeno); NbExp=2; IntAct=EBI-358311, EBI-6050648;
CC       Q15004:PCLAF; NbExp=4; IntAct=EBI-358311, EBI-10971436;
CC       P18669:PGAM1; NbExp=2; IntAct=EBI-358311, EBI-717905;
CC       P28340:POLD1; NbExp=3; IntAct=EBI-358311, EBI-716569;
CC       P49005:POLD2; NbExp=2; IntAct=EBI-358311, EBI-372354;
CC       Q15054:POLD3; NbExp=7; IntAct=EBI-358311, EBI-864956;
CC       Q9HCU8:POLD4; NbExp=4; IntAct=EBI-358311, EBI-864968;
CC       A2RU14:TMEM218; NbExp=3; IntAct=EBI-358311, EBI-10173151;
CC       P60174:TPI1; NbExp=2; IntAct=EBI-358311, EBI-717475;
CC       Q5FWF4:ZRANB3; NbExp=8; IntAct=EBI-358311, EBI-13954615;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24115439,
CC       ECO:0000269|PubMed:24939902}. Note=Colocalizes with CREBBP, EP300
CC       and POLD1 to sites of DNA damage (PubMed:24939902). Forms nuclear
CC       foci representing sites of ongoing DNA replication and vary in
CC       morphology and number during S phase. Together with APEX2, is
CC       redistributed in discrete nuclear foci in presence of oxidative
CC       DNA damaging agents. {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
CC       acetylated by CREBBP on Lys-80, Lys-13 and Lys-14 and on Lys-77 by
CC       p300/EP300 upon loading on chromatin in response to UV irradiation
CC       (PubMed:24939902, PubMed:19419956). Lysine acetylation disrupts
CC       association with chromatin, hence promoting PCNA ubiquitination
CC       and proteasomal degradation in response to UV damage in a
CC       CREBBP- and EP300-dependent manner (PubMed:24939902). Acetylation
CC       disrupts interaction with NUDT15 and promotes degradation
CC       (PubMed:19419956). {ECO:0000269|PubMed:24939902}.
CC   -!- PTM: Ubiquitinated (PubMed:24939902, PubMed:20227374). Following
CC       DNA damage, can be either monoubiquitinated to stimulate direct
CC       bypass of DNA lesions by specialized DNA polymerases or
CC       polyubiquitinated to promote recombination-dependent DNA synthesis
CC       across DNA lesions by template switching mechanisms. Following
CC       induction of replication stress, monoubiquitinated by the UBE2B-
CC       RAD18 complex on Lys-164, leading to recruit translesion (TLS)
CC       polymerases, which are able to synthesize across DNA lesions in a
CC       potentially error-prone manner. An error-free pathway also exists
CC       and requires non-canonical polyubiquitination on Lys-164 through
CC       'Lys-63' linkage of ubiquitin moieties by the E2 complex UBE2N-
CC       UBE2V2 and the E3 ligases, HLTF, RNF8 and SHPRH. This error-free
CC       pathway, also known as template switching, employs recombination
CC       mechanisms to synthesize across the lesion, using as a template
CC       the undamaged, newly synthesized strand of the sister chromatid.
CC       Monoubiquitination at Lys-164 also takes place in undamaged
CC       proliferating cells, and is mediated by the DCX(DTL) complex,
CC       leading to enhance PCNA-dependent translesion DNA synthesis.
CC       Sumoylated during S phase. {ECO:0000269|PubMed:15149598,
CC       ECO:0000269|PubMed:17108083, ECO:0000269|PubMed:17130289,
CC       ECO:0000269|PubMed:18316726, ECO:0000269|PubMed:18719106,
CC       ECO:0000269|PubMed:18948756, ECO:0000269|PubMed:20129063,
CC       ECO:0000269|PubMed:20227374, ECO:0000269|PubMed:22153967,
CC       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)
CC       [MIM:615919]: A neurodegenerative disorder due to defects in DNA
CC       excision repair. ATLD2 is characterized by developmental delay,
CC       ataxia, sensorineural hearing loss, short stature, cutaneous and
CC       ocular telangiectasia, and photosensitivity.
CC       {ECO:0000269|PubMed:24911150}. Note=The disease is caused by
CC       mutations 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
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/PCNAID41670ch20p12.html";
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   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   SMR; P12004; -.
DR   BioGrid; 111142; 332.
DR   ComplexPortal; CPX-538; PCNA homotrimer.
DR   CORUM; P12004; -.
DR   DIP; DIP-1098N; -.
DR   ELM; P12004; -.
DR   IntAct; P12004; 131.
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   iPTMnet; P12004; -.
DR   PhosphoSitePlus; P12004; -.
DR   SwissPalm; P12004; -.
DR   BioMuta; PCNA; -.
DR   DMDM; 129694; -.
DR   SWISS-2DPAGE; P12004; -.
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; P12004; -.
DR   PeptideAtlas; P12004; -.
DR   PRIDE; P12004; -.
DR   ProteomicsDB; 52816; -.
DR   TopDownProteomics; P12004; -.
DR   ABCD; P12004; -.
DR   DNASU; 5111; -.
DR   Ensembl; ENST00000379143; ENSP00000368438; ENSG00000132646.
DR   Ensembl; ENST00000379160; ENSP00000368458; ENSG00000132646.
DR   GeneID; 5111; -.
DR   KEGG; hsa:5111; -.
DR   UCSC; uc002wlp.4; human.
DR   CTD; 5111; -.
DR   DisGeNET; 5111; -.
DR   GeneCards; PCNA; -.
DR   HGNC; HGNC:8729; PCNA.
DR   HPA; CAB000148; -.
DR   HPA; HPA030521; -.
DR   HPA; HPA030522; -.
DR   HPA; HPA030523; -.
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   eggNOG; KOG1636; Eukaryota.
DR   eggNOG; COG0592; LUCA.
DR   GeneTree; ENSGT00390000004965; -.
DR   HOGENOM; HOG000211098; -.
DR   InParanoid; P12004; -.
DR   KO; K04802; -.
DR   OMA; KILRCAG; -.
DR   OrthoDB; 1012066at2759; -.
DR   PhylomeDB; P12004; -.
DR   TreeFam; TF313441; -.
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   ChiTaRS; PCNA; human.
DR   EvolutionaryTrace; P12004; -.
DR   GeneWiki; Proliferating_cell_nuclear_antigen; -.
DR   GenomeRNAi; 5111; -.
DR   Pharos; P12004; -.
DR   PRO; PR:P12004; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   Bgee; ENSG00000132646; Expressed in 228 organ(s), highest expression level in oocyte.
DR   Genevisible; P12004; HS.
DR   GO; GO:0005813; C:centrosome; IDA:MGI.
DR   GO; GO:0000785; C:chromatin; IDA:UniProtKB.
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:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0000784; C:nuclear chromosome, telomeric region; HDA:BHF-UCL.
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:0030331; F:estrogen receptor binding; IEA:Ensembl.
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.
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:0042769; P:DNA damage response, detection of DNA damage; TAS:Reactome.
DR   GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
DR   GO; GO:0070987; P:error-free translesion synthesis; TAS:Reactome.
DR   GO; GO:0042276; P:error-prone translesion synthesis; TAS:Reactome.
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:0006297; P:nucleotide-excision repair, DNA gap filling; TAS:Reactome.
DR   GO; GO:0033683; P:nucleotide-excision repair, DNA incision; TAS:Reactome.
DR   GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; TAS:Reactome.
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:0016567; P:protein ubiquitination; TAS:Reactome.
DR   GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; TAS:Reactome.
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:0000723; P:telomere maintenance; TAS:Reactome.
DR   GO; GO:0032201; P:telomere maintenance via semi-conservative replication; TAS:Reactome.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
DR   GO; GO:0019985; P:translesion synthesis; IDA:UniProtKB.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00317; DNApol_clamp_arch; 1.
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   Pfam; PF02747; PCNA_C; 1.
DR   Pfam; PF00705; PCNA_N; 1.
DR   PRINTS; PR00339; PCNACYCLIN.
DR   TIGRFAMs; TIGR00590; pcna; 1.
DR   PROSITE; PS01251; PCNA_1; 1.
DR   PROSITE; PS00293; PCNA_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome; Deafness;
KW   Direct protein sequencing; Disease mutation; DNA damage; DNA repair;
KW   DNA replication; DNA-binding; Dwarfism; Host-virus interaction;
KW   Isopeptide bond; Methylation; Neurodegeneration; Nucleus;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN         1    261       Proliferating cell nuclear antigen.
FT                                /FTId=PRO_0000149158.
FT   DNA_BIND     61     80       {ECO:0000255}.
FT   REGION        7    100       Interaction with NUDT15.
FT                                {ECO:0000269|PubMed:19419956}.
FT   MOD_RES      14     14       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:19419956}.
FT   MOD_RES      77     77       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES      80     80       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     211    211       Phosphotyrosine; by EGFR.
FT                                {ECO:0000269|PubMed:17115032}.
FT   MOD_RES     248    248       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   CROSSLNK    164    164       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate. {ECO:0000244|PubMed:25114211,
FT                                ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:25772364,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    164    164       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin);
FT                                alternate. {ECO:0000269|PubMed:17108083,
FT                                ECO:0000269|PubMed:17130289}.
FT   CROSSLNK    254    254       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   VARIANT     228    228       S -> I (in ATLD2; a hypomorphic mutation
FT                                affecting DNA repair in response to UV;
FT                                results in significantly decreased
FT                                interaction with FEN1, LIG1 and ERCC5;
FT                                dbSNP:rs369958038).
FT                                {ECO:0000269|PubMed:24911150}.
FT                                /FTId=VAR_071871.
FT   MUTAGEN      13     13       K->R: Inhibits acetylation, recruitment
FT                                to DNA damage sites, inducible
FT                                ubiquitination and protein degradation,
FT                                DNA replication and repair synthesis
FT                                efficiencies, but homotrimer formation,
FT                                nuclear recruitment to DNA damage sites,
FT                                interactions with CREBBP, EP300 and POLD1
FT                                are similar as the wild-type; in
FT                                association with R-14; R-20; R-77 and R-
FT                                80. {ECO:0000269|PubMed:24939902}.
FT   MUTAGEN      14     14       K->R: Inhibits acetylation, recruitment
FT                                to DNA damage sites, inducible
FT                                ubiquitination and protein degradation,
FT                                DNA replication and repair synthesis
FT                                efficiencies, but homotrimer formation,
FT                                nuclear recruitment to DNA damage sites,
FT                                interactions with CREBBP, EP300 and POLD1
FT                                are similar as the wild-type; in
FT                                association with R-13; R-20; R-77 and R-
FT                                80. {ECO:0000269|PubMed:24939902}.
FT   MUTAGEN      20     20       K->R: Inhibits acetylation, recruitment
FT                                to DNA damage sites, inducible
FT                                ubiquitination and protein degradation,
FT                                DNA replication and repair synthesis
FT                                efficiencies, but homotrimer formation,
FT                                nuclear recruitment to DNA damage sites,
FT                                interactions with CREBBP, EP300 and POLD1
FT                                are similar as the wild-type; in
FT                                association with R-13; R-14; R-77 and R-
FT                                80. {ECO:0000269|PubMed:24939902}.
FT   MUTAGEN      43     45       SHV->AAA: No effect on POLD3-binding.
FT                                {ECO:0000269|PubMed:11595739}.
FT   MUTAGEN      77     77       K->A: Inhibits recruitment to DNA damage
FT                                sites, but nuclear localization is
FT                                similar as the wild-type; in association
FT                                with A-80. {ECO:0000269|PubMed:24939902}.
FT   MUTAGEN      77     77       K->R: Inhibits acetylation, recruitment
FT                                to DNA damage sites, inducible
FT                                ubiquitination and protein degradation,
FT                                DNA replication and repair synthesis
FT                                efficiencies, but homotrimer formation,
FT                                nuclear recruitment to DNA damage sites,
FT                                interactions with CREBBP, EP300 and POLD1
FT                                are similar as the wild-type; in
FT                                association with R-13; R-14; R-20 and R-
FT                                80. {ECO:0000269|PubMed:24939902}.
FT   MUTAGEN      80     80       K->A: Inhibits recruitment to DNA damage
FT                                sites, but nuclear localization is
FT                                similar as the wild-type; in association
FT                                with A-77. {ECO:0000269|PubMed:24939902}.
FT   MUTAGEN      80     80       K->R: Inhibits acetylation, recruitment
FT                                to DNA damage sites, inducible
FT                                ubiquitination and protein degradation,
FT                                DNA replication and repair synthesis
FT                                efficiencies, but homotrimer formation,
FT                                nuclear recruitment to DNA damage sites,
FT                                interactions with CREBBP, EP300 and POLD1
FT                                are similar as the wild-type; in
FT                                association with R-13; R-14; R-20 and R-
FT                                77. {ECO:0000269|PubMed:24939902}.
FT   MUTAGEN     125    128       QLGI->AAAA: Strong decrease in POLD3-
FT                                binding. {ECO:0000269|PubMed:11595739}.
FT   MUTAGEN     164    164       K->R: Abolishes ubiquitination. No effect
FT                                on interaction with SHPRH.
FT                                {ECO:0000269|PubMed:17108083,
FT                                ECO:0000269|PubMed:17130289,
FT                                ECO:0000269|PubMed:18719106,
FT                                ECO:0000269|PubMed:20129063}.
FT   MUTAGEN     188    190       VDK->AAA: No effect on POLD3-binding.
FT                                {ECO:0000269|PubMed:11595739}.
FT   MUTAGEN     211    211       Y->F: Alters chromatin-associated PCNA
FT                                stability and its function in DNA
FT                                replication and repair.
FT                                {ECO:0000269|PubMed:17115032}.
FT   MUTAGEN     251    254       LAPK->AAAA: Decrease in POLD3-binding.
FT                                {ECO:0000269|PubMed:11595739}.
FT   STRAND        2      7       {ECO:0000244|PDB:1U7B}.
FT   HELIX        10     20       {ECO:0000244|PDB:1U7B}.
FT   STRAND       24     31       {ECO:0000244|PDB:1U7B}.
FT   STRAND       34     40       {ECO:0000244|PDB:1U7B}.
FT   STRAND       44     53       {ECO:0000244|PDB:1U7B}.
FT   HELIX        54     56       {ECO:0000244|PDB:1U7B}.
FT   STRAND       57     64       {ECO:0000244|PDB:1U7B}.
FT   STRAND       66     71       {ECO:0000244|PDB:1U7B}.
FT   HELIX        72     79       {ECO:0000244|PDB:1U7B}.
FT   STRAND       87     92       {ECO:0000244|PDB:1U7B}.
FT   STRAND       94     96       {ECO:0000244|PDB:1VYM}.
FT   STRAND       97    104       {ECO:0000244|PDB:1U7B}.
FT   STRAND      106    109       {ECO:0000244|PDB:4RJF}.
FT   STRAND      111    117       {ECO:0000244|PDB:1U7B}.
FT   STRAND      121    126       {ECO:0000244|PDB:5E0U}.
FT   STRAND      134    140       {ECO:0000244|PDB:1U7B}.
FT   HELIX       141    152       {ECO:0000244|PDB:1U7B}.
FT   STRAND      156    163       {ECO:0000244|PDB:1U7B}.
FT   STRAND      166    173       {ECO:0000244|PDB:1U7B}.
FT   STRAND      176    182       {ECO:0000244|PDB:1U7B}.
FT   HELIX       191    193       {ECO:0000244|PDB:5E0U}.
FT   STRAND      196    201       {ECO:0000244|PDB:1U7B}.
FT   STRAND      203    208       {ECO:0000244|PDB:1U7B}.
FT   HELIX       209    215       {ECO:0000244|PDB:1U7B}.
FT   HELIX       216    221       {ECO:0000244|PDB:1U7B}.
FT   STRAND      223    229       {ECO:0000244|PDB:1U7B}.
FT   STRAND      231    233       {ECO:0000244|PDB:1VYM}.
FT   STRAND      235    241       {ECO:0000244|PDB:1U7B}.
FT   TURN        242    244       {ECO:0000244|PDB:1U7B}.
FT   STRAND      245    251       {ECO:0000244|PDB:1U7B}.
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
//
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