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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   25-MAY-2022, entry version 241.
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 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   [29]
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   [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 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 nuclear
RT   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 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   [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., 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   [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 inhibiting
RT   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., 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   [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 replication
RT   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., 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   [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., 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   [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 switch
RT   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 protein
RT   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 UV-
RT   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., 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   [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., 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   [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., 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   [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)-mediated
RT   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 cell
RT   nuclear antigen (PCNA) and is required for DNA damage tolerance.";
RL   J. Biol. Chem. 289:13627-13637(2014).
RN   [55]
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   [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., 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   [57]
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   [58]
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   [59]
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   [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 that
RT   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 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   [62]
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   [63]
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   [64]
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   [65]
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   [66]
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   [67]
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   [68]
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   [69]
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   [70]
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   [71]
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   [72]
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   [73]
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   [74] {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   [75] {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   [76] {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 is involved in
CC       the control of eukaryotic DNA replication by increasing the
CC       polymerase's processibility during elongation of the leading strand.
CC       Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-
CC       phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease,
CC       APEX2 activities. Has to be loaded onto DNA in order to be able to
CC       stimulate APEX2. Plays a key role in DNA damage response (DDR) by being
CC       conveniently positioned at the replication fork to coordinate DNA
CC       replication with DNA repair and DNA damage tolerance pathways
CC       (PubMed:24939902). Acts as a loading platform to recruit DDR proteins
CC       that allow completion of DNA replication after DNA damage and promote
CC       postreplication repair: Monoubiquitinated PCNA leads to recruitment of
CC       translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination
CC       of 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; 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). 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. {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:19419956,
CC       ECO:0000269|PubMed:19443450, ECO:0000269|PubMed:19995904,
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:27084448, ECO:0000269|PubMed:27462463,
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 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="http://atlasgeneticsoncology.org/Genes/PCNAID41670ch20p12.html";
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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   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   AlphaFoldDB; P12004; -.
DR   BMRB; P12004; -.
DR   SASBDB; P12004; -.
DR   SMR; P12004; -.
DR   BioGRID; 111142; 409.
DR   ComplexPortal; CPX-538; PCNA homotrimer.
DR   CORUM; P12004; -.
DR   DIP; DIP-1098N; -.
DR   ELM; P12004; -.
DR   IntAct; P12004; 431.
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   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   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; 1 sequenced antibody.
DR   Antibodypedia; 3769; 2577 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   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; 1012066at2759; -.
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; 828 hits in 1071 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 237 other tissues.
DR   Genevisible; P12004; HS.
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: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: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-UCL.
DR   GO; GO:0008022; F:protein C-terminus binding; IMP:UniProtKB.
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   HAMAP; MF_00317; DNApol_clamp_arch; 1.
DR   IDEAL; IID00022; -.
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; 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 R-
FT                   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 R-
FT                   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 R-
FT                   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 R-
FT                   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 R-
FT                   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..109
FT                   /evidence="ECO:0007829|PDB:4RJF"
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
//
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