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Proliferating cell nuclear antigen (PCNA) (Cyclin)

 PCNA_HUMAN              Reviewed;         261 AA.
P12004; B2R897; D3DW02;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
30-AUG-2017, entry version 203.
RecName: Full=Proliferating cell nuclear antigen;
Short=PCNA;
AltName: Full=Cyclin;
Name=PCNA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2882507; DOI=10.1073/pnas.84.6.1575;
Almendral J.M., Huebsch D., Blundell P.A., Macdonald-Bravo H.,
Bravo R.;
"Cloning and sequence of the human nuclear protein cyclin: homology
with DNA-binding proteins.";
Proc. Natl. Acad. Sci. U.S.A. 84:1575-1579(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2565339;
Travali S., Ku D.H., Rizzo M.G., Ottavio L., Baserga R.,
Calabretta B.;
"Structure of the human gene for the proliferating cell nuclear
antigen.";
J. Biol. Chem. 264:7466-7472(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 1-26.
PubMed=2882422; DOI=10.1038/326471a0;
Prelich G., Kostura M., Marshak D.R., Mathews M.B., Stillman B.;
"The cell-cycle regulated proliferating cell nuclear antigen is
required for SV40 DNA replication in vitro.";
Nature 326:471-475(1987).
[9]
PROTEIN SEQUENCE OF 169-181, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[10]
INTERACTION WITH ERCC5/XPG.
PubMed=9305916; DOI=10.1074/jbc.272.39.24522;
Gary R., Ludwig D.L., Cornelius H.L., MacInnes M.A., Park M.S.;
"The DNA repair endonuclease XPG binds to proliferating cell nuclear
antigen (PCNA) and shares sequence elements with the PCNA-binding
regions of FEN-1 and cyclin-dependent kinase inhibitor p21.";
J. Biol. Chem. 272:24522-24529(1997).
[11]
INTERACTION WITH DNMT1.
PubMed=9302295; DOI=10.1126/science.277.5334.1996;
Chuang L.S.-H., Ian H.-I., Koh T.-W., Ng H.-H., Xu G., Li B.F.L.;
"Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for
p21WAF1.";
Science 277:1996-2000(1997).
[12]
INTERACTION WITH CDC6.
PubMed=9566895; DOI=10.1128/MCB.18.5.2758;
Saha P., Chen J., Thome K.C., Lawlis S.J., Hou Z.H., Hendricks M.,
Parvin J.D., Dutta A.;
"Human CDC6/Cdc18 associates with Orc1 and cyclin-cdk and is
selectively eliminated from the nucleus at the onset of S phase.";
Mol. Cell. Biol. 18:2758-2767(1998).
[13]
INTERACTION WITH POLD3 AND CDKN1A, AND MUTAGENESIS OF 43-SER--VAL-45;
125-GLN--ILE-128; 188-VAL--LYS-190 AND 251-LEU--LYS-254.
PubMed=11595739; DOI=10.1074/jbc.M106990200;
Ducoux M., Urbach S., Baldacci G., Huebscher U., Koundrioukoff S.,
Christensen J., Hughes P.;
"Mediation of proliferating cell nuclear antigen (PCNA)-dependent DNA
replication through a conserved p21(Cip1)-like PCNA-binding motif
present in the third subunit of human DNA polymerase delta.";
J. Biol. Chem. 276:49258-49266(2001).
[14]
INTERACTION WITH APEX2.
PubMed=11376153; DOI=10.1093/nar/29.11.2349;
Tsuchimoto D., Sakai Y., Sakumi K., Nishioka K., Sasaki M.,
Fujiwara T., Nakabeppu Y.;
"Human APE2 protein is mostly localized in the nuclei and to some
extent in the mitochondria, while nuclear APE2 is partly associated
with proliferating cell nuclear antigen.";
Nucleic Acids Res. 29:2349-2360(2001).
[15]
INTERACTION WITH POLK.
PubMed=11784855; DOI=10.1128/MCB.22.3.784-791.2002;
Haracska L., Unk I., Johnson R.E., Phillips B.B., Hurwitz J.,
Prakash L., Prakash S.;
"Stimulation of DNA synthesis activity of human DNA polymerase kappa
by PCNA.";
Mol. Cell. Biol. 22:784-791(2002).
[16]
INTERACTION WITH DNTTIP2.
PubMed=12786946; DOI=10.1046/j.1365-2443.2003.00656.x;
Fujita K., Shimazaki N., Ohta Y., Kubota T., Ibe S., Toji S.,
Tamai K., Fujisaki S., Hayano T., Koiwai O.;
"Terminal deoxynucleotidyltransferase forms a ternary complex with a
novel chromatin remodeling protein with 82 kDa and core histone.";
Genes Cells 8:559-571(2003).
[17]
INTERACTION WITH POLDIP2.
TISSUE=Placenta;
PubMed=12522211; DOI=10.1074/jbc.M208694200;
Liu L., Rodriguez-Belmonte E.M., Mazloum N., Xie B., Lee M.Y.W.T.;
"Identification of a novel protein, PDIP38, that interacts with the
p50 subunit of DNA polymerase delta and proliferating cell nuclear
antigen.";
J. Biol. Chem. 278:10041-10047(2003).
[18]
INTERACTION WITH EXO1.
PubMed=15225546; DOI=10.1016/j.molcel.2004.06.016;
Dzantiev L., Constantin N., Genschel J., Iyer R.R., Burgers P.M.,
Modrich P.;
"A defined human system that supports bidirectional mismatch-provoked
excision.";
Mol. Cell 15:31-41(2004).
[19]
UBIQUITINATION, AND INTERACTION WITH POLH.
PubMed=15149598; DOI=10.1016/S1097-2765(04)00259-X;
Kannouche P.L., Wing J., Lehmann A.R.;
"Interaction of human DNA polymerase eta with monoubiquitinated PCNA:
a possible mechanism for the polymerase switch in response to DNA
damage.";
Mol. Cell 14:491-500(2004).
[20]
INTERACTION WITH BAZ1B.
PubMed=15543136; DOI=10.1038/ncb1196;
Poot R.A., Bozhenok L., van den Berg D.L.C., Steffensen S.,
Ferreira F., Grimaldi M., Gilbert N., Ferreira J., Varga-Weisz P.D.;
"The Williams syndrome transcription factor interacts with PCNA to
target chromatin remodelling by ISWI to replication foci.";
Nat. Cell Biol. 6:1236-1244(2004).
[21]
INTERACTION WITH POLD1; POLD3 AND POLD4.
PubMed=16510448; DOI=10.1074/jbc.M600322200;
Li H., Xie B., Zhou Y., Rahmeh A., Trusa S., Zhang S., Gao Y.,
Lee E.Y., Lee M.Y.;
"Functional roles of p12, the fourth subunit of human DNA polymerase
delta.";
J. Biol. Chem. 281:14748-14755(2006).
[22]
INTERACTION WITH SHPRH, UBIQUITINATION AT LYS-164, AND MUTAGENESIS OF
LYS-164.
PubMed=17130289; DOI=10.1083/jcb.200606145;
Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K.;
"Human SHPRH suppresses genomic instability through proliferating cell
nuclear antigen polyubiquitination.";
J. Cell Biol. 175:703-708(2006).
[23]
INTERACTION WITH CDT1.
PubMed=16949367; DOI=10.1016/j.molcel.2006.08.010;
Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.;
"A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
which is required for S phase destruction of the replication factor
Cdt1.";
Mol. Cell 23:709-721(2006).
[24]
PHOSPHORYLATION AT TYR-211 BY EGFR, MUTAGENESIS OF TYR-211, AND
INTERACTION WITH EGFR.
PubMed=17115032; DOI=10.1038/ncb1501;
Wang S.C., Nakajima Y., Yu Y.L., Xia W., Chen C.T., Yang C.C.,
McIntush E.W., Li L.Y., Hawke D.H., Kobayashi R., Hung M.C.;
"Tyrosine phosphorylation controls PCNA function through protein
stability.";
Nat. Cell Biol. 8:1359-1368(2006).
[25]
UBIQUITINATION AT LYS-164, AND MUTAGENESIS OF LYS-164.
PubMed=17108083; DOI=10.1073/pnas.0608595103;
Unk I., Hajdu I., Fatyol K., Szakal B., Blastyak A., Bermudez V.,
Hurwitz J., Prakash L., Prakash S., Haracska L.;
"Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent
polyubiquitylation of proliferating cell nuclear antigen.";
Proc. Natl. Acad. Sci. U.S.A. 103:18107-18112(2006).
[26]
UBIQUITINATION.
PubMed=18948756; DOI=10.4161/cc.7.21.6949;
Zhang S., Chea J., Meng X., Zhou Y., Lee E.Y.C., Lee M.Y.W.T.;
"PCNA is ubiquitinated by RNF8.";
Cell Cycle 7:3399-3404(2008).
[27]
INTERACTION WITH CDKN1A.
PubMed=18794347; DOI=10.1101/gad.1676108;
Abbas T., Sivaprasad U., Terai K., Amador V., Pagano M., Dutta A.;
"PCNA-dependent regulation of p21 ubiquitylation and degradation via
the CRL4Cdt2 ubiquitin ligase complex.";
Genes Dev. 22:2496-2506(2008).
[28]
INTERACTION WITH DDX11.
PubMed=18499658; DOI=10.1074/jbc.M802696200;
Farina A., Shin J.H., Kim D.H., Bermudez V.P., Kelman Z., Seo Y.S.,
Hurwitz J.;
"Studies with the human cohesin establishment factor, ChlR1.
Association of ChlR1 with Ctf18-RFC and Fen1.";
J. Biol. Chem. 283:20925-20936(2008).
[29]
INTERACTION WITH CDKN1A.
PubMed=18703516; DOI=10.1074/jbc.M806045200;
Nishitani H., Shiomi Y., Iida H., Michishita M., Takami T.,
Tsurimoto T.;
"CDK inhibitor p21 is degraded by a proliferating cell nuclear
antigen-coupled Cul4-DDB1Cdt2 pathway during S phase and after UV
irradiation.";
J. Biol. Chem. 283:29045-29052(2008).
[30]
FUNCTION, AND INTERACTION WITH APEX2.
PubMed=19443450; DOI=10.1093/nar/gkp357;
Burkovics P., Hajdu I., Szukacsov V., Unk I., Haracska L.;
"Role of PCNA-dependent stimulation of 3'-phosphodiesterase and 3'-5'
exonuclease activities of human Ape2 in repair of oxidative DNA
damage.";
Nucleic Acids Res. 37:4247-4255(2009).
[31]
UBIQUITINATION, AND INTERACTION WITH HLTF.
PubMed=18316726; DOI=10.1073/pnas.0800563105;
Unk I., Hajdu I., Fatyol K., Hurwitz J., Yoon J.-H., Prakash L.,
Prakash S., Haracska L.;
"Human HLTF functions as a ubiquitin ligase for proliferating cell
nuclear antigen polyubiquitination.";
Proc. Natl. Acad. Sci. U.S.A. 105:3768-3773(2008).
[32]
UBIQUITINATION, FUNCTION, INTERACTION WITH HLTF AND SHPRH, AND
MUTAGENESIS OF LYS-164.
PubMed=18719106; DOI=10.1073/pnas.0805685105;
Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X.,
Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.;
"Polyubiquitination of proliferating cell nuclear antigen by HLTF and
SHPRH prevents genomic instability from stalled replication forks.";
Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008).
[33]
INTERACTION WITH NUDT15, AND ACETYLATION AT LYS-14.
PubMed=19419956; DOI=10.1074/jbc.M109.015289;
Yu Y., Cai J.-P., Tu B., Wu L., Zhao Y., Liu X., Li L., McNutt M.A.,
Feng J., He Q., Yang Y., Wang H., Sekiguchi M., Zhu W.-G.;
"Proliferating cell nuclear antigen is protected from degradation by
forming a complex with MutT Homolog2.";
J. Biol. Chem. 284:19310-19320(2009).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-77; LYS-80 AND LYS-248, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[35]
UBIQUITINATION, AND MUTAGENESIS OF LYS-164.
PubMed=20129063; DOI=10.1016/j.molcel.2009.12.018;
Terai K., Abbas T., Jazaeri A.A., Dutta A.;
"CRL4(Cdt2) E3 ubiquitin ligase monoubiquitinates PCNA to promote
translesion DNA synthesis.";
Mol. Cell 37:143-149(2010).
[36]
UBIQUITINATION IN RESPONSE TO UV IRRADIATION.
PubMed=20227374; DOI=10.1016/j.molcel.2010.02.009;
Ogi T., Limsirichaikul S., Overmeer R.M., Volker M., Takenaka K.,
Cloney R., Nakazawa Y., Niimi A., Miki Y., Jaspers N.G.,
Mullenders L.H., Yamashita S., Fousteri M.I., Lehmann A.R.;
"Three DNA polymerases, recruited by different mechanisms, carry out
NER repair synthesis in human cells.";
Mol. Cell 37:714-727(2010).
[37]
INTERACTION WITH POLN.
PubMed=19995904; DOI=10.1128/MCB.01124-09;
Moldovan G.L., Madhavan M.V., Mirchandani K.D., McCaffrey R.M.,
Vinciguerra P., D'Andrea A.D.;
"DNA polymerase POLN participates in cross-link repair and homologous
recombination.";
Mol. Cell. Biol. 30:1088-1096(2010).
[38]
INTERACTION WITH SETMAR.
PubMed=20457750; DOI=10.1093/nar/gkq339;
De Haro L.P., Wray J., Williamson E.A., Durant S.T., Corwin L.,
Gentry A.C., Osheroff N., Lee S.H., Hromas R., Nickoloff J.A.;
"Metnase promotes restart and repair of stalled and collapsed
replication forks.";
Nucleic Acids Res. 38:5681-5691(2010).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[40]
INTERACTION WITH SMARCAD1.
PubMed=21549307; DOI=10.1016/j.molcel.2011.02.036;
Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W.,
Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M.,
Varga-Weisz P., Mermoud J.E.;
"Maintenance of silent chromatin through replication requires SWI/SNF-
like chromatin remodeler SMARCAD1.";
Mol. Cell 42:285-296(2011).
[41]
INTERACTION WITH PCLAF.
PubMed=21628590; DOI=10.1073/pnas.1106136108;
Emanuele M.J., Ciccia A., Elia A.E., Elledge S.J.;
"Proliferating cell nuclear antigen (PCNA)-associated KIAA0101/PAF15
protein is a cell cycle-regulated anaphase-promoting complex/cyclosome
substrate.";
Proc. Natl. Acad. Sci. U.S.A. 108:9845-9850(2011).
[42]
INTERACTION WITH POLD3.
PubMed=22148433; DOI=10.1021/bi201638e;
Rahmeh A.A., Zhou Y., Xie B., Li H., Lee E.Y., Lee M.Y.;
"Phosphorylation of the p68 subunit of Pol delta acts as a molecular
switch to regulate its interaction with PCNA.";
Biochemistry 51:416-424(2012).
[43]
INTERACTION WITH PARPBP, AND SUMOYLATION.
PubMed=22153967; DOI=10.1016/j.molcel.2011.11.010;
Moldovan G.L., Dejsuphong D., Petalcorin M.I., Hofmann K., Takeda S.,
Boulton S.J., D'Andrea A.D.;
"Inhibition of homologous recombination by the PCNA-interacting
protein PARI.";
Mol. Cell 45:75-86(2012).
[44]
INTERACTION WITH SPRTN.
PubMed=22681887; DOI=10.1016/j.molcel.2012.05.020;
Centore R.C., Yazinski S.A., Tse A., Zou L.;
"Spartan/C1orf124, a reader of PCNA ubiquitylation and a regulator of
UV-induced DNA damage response.";
Mol. Cell 46:625-635(2012).
[45]
INTERACTION WITH ZRANB3.
PubMed=22759634; DOI=10.1101/gad.193516.112;
Weston R., Peeters H., Ahel D.;
"ZRANB3 is a structure-specific ATP-dependent endonuclease involved in
replication stress response.";
Genes Dev. 26:1558-1572(2012).
[46]
INTERACTION WITH ZRANB3.
PubMed=22705370; DOI=10.1016/j.molcel.2012.05.025;
Yuan J., Ghosal G., Chen J.;
"The HARP-like domain-containing protein AH2/ZRANB3 binds to PCNA and
participates in cellular response to replication stress.";
Mol. Cell 47:410-421(2012).
[47]
INTERACTION WITH PCLAF.
PubMed=23000965; DOI=10.1038/ncb2579;
Povlsen L.K., Beli P., Wagner S.A., Poulsen S.L., Sylvestersen K.B.,
Poulsen J.W., Nielsen M.L., Bekker-Jensen S., Mailand N.,
Choudhary C.;
"Systems-wide analysis of ubiquitylation dynamics reveals a key role
for PAF15 ubiquitylation in DNA-damage bypass.";
Nat. Cell Biol. 14:1089-1098(2012).
[48]
INTERACTION WITH ZRANB3.
PubMed=22704558; DOI=10.1016/j.molcel.2012.05.024;
Ciccia A., Nimonkar A.V., Hu Y., Hajdu I., Achar Y.J., Izhar L.,
Petit S.A., Adamson B., Yoon J.C., Kowalczykowski S.C.,
Livingston D.M., Haracska L., Elledge S.J.;
"Polyubiquitinated PCNA recruits the ZRANB3 translocase to maintain
genomic integrity after replication stress.";
Mol. Cell 47:396-409(2012).
[49]
INTERACTION WITH CDKN1C.
PubMed=22634751; DOI=10.1038/ng.2275;
Arboleda V.A., Lee H., Parnaik R., Fleming A., Banerjee A.,
Ferraz-de-Souza B., Delot E.C., Rodriguez-Fernandez I.A.,
Braslavsky D., Bergada I., Dell'Angelica E.C., Nelson S.F.,
Martinez-Agosto J.A., Achermann J.C., Vilain E.;
"Mutations in the PCNA-binding domain of CDKN1C cause IMAGe
syndrome.";
Nat. Genet. 44:788-792(2012).
[50]
INTERACTION WITH ANKRD17.
PubMed=23711367; DOI=10.1016/j.febslet.2013.05.037;
Menning M., Kufer T.A.;
"A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and
Nod2-mediated inflammatory responses.";
FEBS Lett. 587:2137-2142(2013).
[51]
INTERACTION WITH FBXO18.
PubMed=23677613; DOI=10.1093/nar/gkt397;
Bacquin A., Pouvelle C., Siaud N., Perderiset M., Salome-Desnoulez S.,
Tellier-Lebegue C., Lopez B., Charbonnier J.B., Kannouche P.L.;
"The helicase FBH1 is tightly regulated by PCNA via CRL4(Cdt2)-
mediated proteolysis in human cells.";
Nucleic Acids Res. 41:6501-6513(2013).
[52]
INTERACTION WITH RTEL1, AND SUBCELLULAR LOCATION.
PubMed=24115439; DOI=10.1126/science.1241779;
Vannier J.B., Sandhu S., Petalcorin M.I., Wu X., Nabi Z., Ding H.,
Boulton S.J.;
"RTEL1 is a replisome-associated helicase that promotes telomere and
genome-wide replication.";
Science 342:239-242(2013).
[53]
INVOLVEMENT IN ATLD2, INTERACTION WITH FEN1; LIG1 AND ERCC5, VARIANT
ATLD2 ILE-228, AND CHARACTERIZATION OF VARIANT ATDL2 ILE-228.
PubMed=24911150; DOI=10.1172/JCI74593;
Baple E.L., Chambers H., Cross H.E., Fawcett H., Nakazawa Y.,
Chioza B.A., Harlalka G.V., Mansour S., Sreekantan-Nair A.,
Patton M.A., Muggenthaler M., Rich P., Wagner K., Coblentz R.,
Stein C.K., Last J.I., Taylor A.M., Jackson A.P., Ogi T.,
Lehmann A.R., Green C.M., Crosby A.H.;
"Hypomorphic PCNA mutation underlies a human DNA repair disorder.";
J. Clin. Invest. 124:3137-3146(2014).
[54]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[55]
INTERACTION WITH FAM111A.
PubMed=24561620; DOI=10.1038/ncb2918;
Alabert C., Bukowski-Wills J.C., Lee S.B., Kustatscher G.,
Nakamura K., de Lima Alves F., Menard P., Mejlvang J., Rappsilber J.,
Groth A.;
"Nascent chromatin capture proteomics determines chromatin dynamics
during DNA replication and identifies unknown fork components.";
Nat. Cell Biol. 16:281-293(2014).
[56]
FUNCTION, TRIMERIZATION, INTERACTION WITH CREBBP; EP300 AND POLD1,
ACETYLATION, UBIQUITINATION, ASSOCIATION WITH CHROMATIN, AND
MUTAGENESIS OF LYS-13; LYS-14; LYS-20; LYS-77 AND LYS-80.
PubMed=24939902; DOI=10.1093/nar/gku533;
Cazzalini O., Sommatis S., Tillhon M., Dutto I., Bachi A., Rapp A.,
Nardo T., Scovassi A.I., Necchi D., Cardoso M.C., Stivala L.A.,
Prosperi E.;
"CBP and p300 acetylate PCNA to link its degradation with nucleotide
excision repair synthesis.";
Nucleic Acids Res. 42:8433-8448(2014).
[57]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[58]
METHYLATION.
PubMed=25732820; DOI=10.1016/j.celrep.2015.01.054;
Perry J.J., Ballard G.D., Albert A.E., Dobrolecki L.E., Malkas L.H.,
Hoelz D.J.;
"Human C6orf211 encodes Armt1, a protein carboxyl methyltransferase
that targets PCNA and is linked to the DNA damage response.";
Cell Rep. 10:1288-1296(2015).
[59]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[60]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[61]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[62]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164 AND LYS-254, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[63]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
PubMed=8861913; DOI=10.1016/S0092-8674(00)81347-1;
Gulbis J.M., Kelman Z., Hurwitz J., O'Donnell M., Kuriyan J.;
"Structure of the C-terminal region of p21(WAF1/CIP1) complexed with
human PCNA.";
Cell 87:297-306(1996).
[64]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH FEN1.
PubMed=15616578; DOI=10.1038/sj.emboj.7600519;
Sakurai S., Kitano K., Yamaguchi H., Hamada K., Okada K., Fukuda K.,
Uchida M., Ohtsuka E., Morioka H., Hakoshima T.;
"Structural basis for recruitment of human flap endonuclease 1 to
PCNA.";
EMBO J. 24:683-693(2005).
-!- FUNCTION: Auxiliary protein of DNA polymerase delta and is
involved in the control of eukaryotic DNA replication by
increasing the polymerase's processibility during elongation of
the leading strand. Induces a robust stimulatory effect on the 3'-
5' exonuclease and 3'-phosphodiesterase, but not apurinic-
apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded
onto DNA in order to be able to stimulate APEX2. Plays a key role
in DNA damage response (DDR) by being conveniently positioned at
the replication fork to coordinate DNA replication with DNA repair
and DNA damage tolerance pathways (PubMed:24939902). Acts as a
loading platform to recruit DDR proteins that allow completion of
DNA replication after DNA damage and promote postreplication
repair: Monoubiquitinated PCNA leads to recruitment of translesion
(TLS) polymerases, while 'Lys-63'-linked polyubiquitination of
PCNA is involved in error-free pathway and employs recombination
mechanisms to synthesize across the lesion.
{ECO:0000269|PubMed:18719106, ECO:0000269|PubMed:19443450,
ECO:0000269|PubMed:24939902}.
-!- SUBUNIT: Homotrimer (PubMed:24939902). Interacts with p300/EP300;
the interaction occurs on chromatin in UV-irradiated damaged cells
(PubMed:24939902). Interacts with CREBBP (via transactivation
domain and C-terminus); the interaction occurs on chromatin in UV-
irradiated damaged cells (PubMed:24939902). Directly interacts
with POLD1, POLD3 and POLD4 subunits of the DNA polymerase delta
complex, POLD3 being the major interacting partner; the
interaction with POLD3 is inhibited by CDKN1A/p21(CIP1)
(PubMed:11595739, PubMed:16510448, PubMed:22148433,
PubMed:24939902). Forms a complex with activator 1 heteropentamer
in the presence of ATP. Interacts with EXO1, POLH, POLK, DNMT1,
ERCC5, FEN1, CDC6 and POLDIP2 (PubMed:9305916, PubMed:9302295,
PubMed:9566895, PubMed:11784855, PubMed:12522211, PubMed:15225546,
PubMed:15149598, PubMed:24911150, PubMed:15616578). Interacts with
APEX2; this interaction is triggered by reactive oxygen species
and increased by misincorporation of uracil in nuclear DNA
(PubMed:11376153, PubMed:19443450). Forms a ternary complex with
DNTTIP2 and core histone (PubMed:12786946). Interacts with KCTD10
and PPP1R15A (By similarity). Directly interacts with BAZ1B
(PubMed:15543136). Interacts with HLTF and SHPRH (PubMed:17130289,
PubMed:18316726, PubMed:18719106). Interacts with NUDT15; this
interaction is disrupted in response to UV irradiation and
acetylation (PubMed:19419956). Interacts with CDKN1A/p21(CIP1) and
CDT1; interacts via their PIP-box which also recruits the DCX(DTL)
complex. The interaction with CDKN1A inhibits POLD3 binding
(PubMed:11595739, PubMed:16949367, PubMed:18794347,
PubMed:18703516). Interacts with DDX11 (PubMed:18499658).
Interacts with EGFR; positively regulates PCNA (PubMed:17115032).
Interacts with PARPBP (PubMed:22153967). Interacts (when
ubiquitinated) with SPRTN; leading to enhance RAD18-mediated PCNA
ubiquitination (PubMed:22681887). Interacts (when
polyubiquitinated) with ZRANB3 (PubMed:22704558, PubMed:22705370,
PubMed:22759634). Interacts with SMARCAD1 (PubMed:21549307).
Interacts with CDKN1C (PubMed:22634751). Interacts with PCLAF (via
PIP-box) (PubMed:21628590, PubMed:23000965). Interacts with RTEL1
(via PIP-box); the interaction is direct and essential for the
suppression of telomere fragility (PubMed:24115439). Interacts
with FAM111A (via PIP-box); the interaction is direct and required
for PCNA loading on chromatin binding (PubMed:24561620). Interacts
with LIG1 (PubMed:24911150). Interacts with SETMAR
(PubMed:20457750). Interacts with ANKRD17 (PubMed:23711367).
Interacts with FBXO18/FBH1 (via PIP-box); the interaction recruits
the DCX(DTL) complex and promotes ubiquitination and degradation
of FBXO18/FBH1 (PubMed:23677613). Interacts with POLN
(PubMed:19995904). {ECO:0000250|UniProtKB:P04961,
ECO:0000250|UniProtKB:P17918, ECO:0000269|PubMed:11376153,
ECO:0000269|PubMed:11595739, ECO:0000269|PubMed:11784855,
ECO:0000269|PubMed:12522211, ECO:0000269|PubMed:12786946,
ECO:0000269|PubMed:15149598, ECO:0000269|PubMed:15225546,
ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:15616578,
ECO:0000269|PubMed:16510448, ECO:0000269|PubMed:16949367,
ECO:0000269|PubMed:17115032, ECO:0000269|PubMed:17130289,
ECO:0000269|PubMed:18316726, ECO:0000269|PubMed:18499658,
ECO:0000269|PubMed:18703516, ECO:0000269|PubMed:18719106,
ECO:0000269|PubMed:18794347, ECO:0000269|PubMed:19419956,
ECO:0000269|PubMed:19443450, ECO:0000269|PubMed:19995904,
ECO:0000269|PubMed:20457750, ECO:0000269|PubMed:21549307,
ECO:0000269|PubMed:21628590, ECO:0000269|PubMed:22148433,
ECO:0000269|PubMed:22153967, ECO:0000269|PubMed:22634751,
ECO:0000269|PubMed:22681887, ECO:0000269|PubMed:22704558,
ECO:0000269|PubMed:22705370, ECO:0000269|PubMed:22759634,
ECO:0000269|PubMed:23000965, ECO:0000269|PubMed:23677613,
ECO:0000269|PubMed:23711367, ECO:0000269|PubMed:24115439,
ECO:0000269|PubMed:24561620, ECO:0000269|PubMed:24911150,
ECO:0000269|PubMed:24939902, ECO:0000269|PubMed:9302295,
ECO:0000269|PubMed:9305916, ECO:0000269|PubMed:9566895}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-358311, EBI-358311;
Q8TE30:-; NbExp=6; IntAct=EBI-358311, EBI-8874509;
P04075:ALDOA; NbExp=3; IntAct=EBI-358311, EBI-709613;
P38936:CDKN1A; NbExp=28; IntAct=EBI-358311, EBI-375077;
P42771:CDKN2A; NbExp=8; IntAct=EBI-358311, EBI-375053;
Q9H211:CDT1; NbExp=2; IntAct=EBI-358311, EBI-456953;
Q13111:CHAF1A; NbExp=4; IntAct=EBI-358311, EBI-1020839;
P06733:ENO1; NbExp=3; IntAct=EBI-358311, EBI-353877;
P39748:FEN1; NbExp=6; IntAct=EBI-358311, EBI-707816;
Q9Z111:Gadd45g (xeno); NbExp=9; IntAct=EBI-358311, EBI-1173616;
P04406:GAPDH; NbExp=3; IntAct=EBI-358311, EBI-354056;
Q9H160:ING2; NbExp=3; IntAct=EBI-358311, EBI-389787;
P20585:MSH3; NbExp=7; IntAct=EBI-358311, EBI-1164205;
Q1K9H5:PB1 (xeno); NbExp=2; IntAct=EBI-358311, EBI-6050669;
B4URF7:PB2 (xeno); NbExp=2; IntAct=EBI-358311, EBI-6050648;
Q15004:PCLAF; NbExp=3; IntAct=EBI-358311, EBI-10971436;
P18669:PGAM1; NbExp=2; IntAct=EBI-358311, EBI-717905;
P28340:POLD1; NbExp=3; IntAct=EBI-358311, EBI-716569;
P49005:POLD2; NbExp=2; IntAct=EBI-358311, EBI-372354;
Q15054:POLD3; NbExp=5; IntAct=EBI-358311, EBI-864956;
Q9HCU8:POLD4; NbExp=4; IntAct=EBI-358311, EBI-864968;
A2RU14:TMEM218; NbExp=3; IntAct=EBI-358311, EBI-10173151;
P60174:TPI1; NbExp=2; IntAct=EBI-358311, EBI-717475;
Q5FWF4:ZRANB3; NbExp=8; IntAct=EBI-358311, EBI-13954615;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24115439,
ECO:0000269|PubMed:24939902}. Note=Colocalizes with CREBBP, EP300
and POLD1 to sites of DNA damage (PubMed:24939902). Forms nuclear
foci representing sites of ongoing DNA replication and vary in
morphology and number during S phase. Together with APEX2, is
redistributed in discrete nuclear foci in presence of oxidative
DNA damaging agents. {ECO:0000269|PubMed:24939902}.
-!- PTM: Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes
chromatin-associated PCNA. {ECO:0000269|PubMed:17115032}.
-!- PTM: Acetylated by CREBBP and p300/EP300; preferentially
acetylated by CREBBP on Lys-80, Lys-13 and Lys-14 and on Lys-77 by
p300/EP300 upon loading on chromatin in response to UV irradiation
(PubMed:24939902, PubMed:19419956). Lysine acetylation disrupts
association with chromatin, hence promoting PCNA ubiquitination
and proteasomal degradation in response to UV damage in a
CREBBP- and EP300-dependent manner (PubMed:24939902). Acetylation
disrupts interaction with NUDT15 and promotes degradation
(PubMed:19419956). {ECO:0000269|PubMed:24939902}.
-!- PTM: Ubiquitinated (PubMed:24939902, PubMed:20227374). Following
DNA damage, can be either monoubiquitinated to stimulate direct
bypass of DNA lesions by specialized DNA polymerases or
polyubiquitinated to promote recombination-dependent DNA synthesis
across DNA lesions by template switching mechanisms. Following
induction of replication stress, monoubiquitinated by the UBE2B-
RAD18 complex on Lys-164, leading to recruit translesion (TLS)
polymerases, which are able to synthesize across DNA lesions in a
potentially error-prone manner. An error-free pathway also exists
and requires non-canonical polyubiquitination on Lys-164 through
'Lys-63' linkage of ubiquitin moieties by the E2 complex UBE2N-
UBE2V2 and the E3 ligases, HLTF, RNF8 and SHPRH. This error-free
pathway, also known as template switching, employs recombination
mechanisms to synthesize across the lesion, using as a template
the undamaged, newly synthesized strand of the sister chromatid.
Monoubiquitination at Lys-164 also takes place in undamaged
proliferating cells, and is mediated by the DCX(DTL) complex,
leading to enhance PCNA-dependent translesion DNA synthesis.
Sumoylated during S phase. {ECO:0000269|PubMed:15149598,
ECO:0000269|PubMed:17108083, ECO:0000269|PubMed:17130289,
ECO:0000269|PubMed:18316726, ECO:0000269|PubMed:18719106,
ECO:0000269|PubMed:18948756, ECO:0000269|PubMed:20129063,
ECO:0000269|PubMed:20227374, ECO:0000269|PubMed:22153967,
ECO:0000269|PubMed:24939902}.
-!- PTM: Methylated on glutamate residues by ARMT1/C6orf211.
{ECO:0000269|PubMed:25732820}.
-!- DISEASE: Ataxia-telangiectasia-like disorder 2 (ATLD2)
[MIM:615919]: A neurodegenerative disorder due to defects in DNA
excision repair. ATLD2 is characterized by developmental delay,
ataxia, sensorineural hearing loss, short stature, cutaneous and
ocular telangiectasia, and photosensitivity.
{ECO:0000269|PubMed:24911150}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Antibodies against PCNA are present in sera from
patients with systemic lupus erythematosus.
-!- SIMILARITY: Belongs to the PCNA family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/pcna/";
-!- WEB RESOURCE: Name=Wikipedia; Note=PCNA entry;
URL="https://en.wikipedia.org/wiki/PCNA";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PCNAID41670ch20p12.html";
-----------------------------------------------------------------------
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EMBL; M15796; AAA35736.1; -; mRNA.
EMBL; J04718; AAA60040.1; -; Genomic_DNA.
EMBL; AF527838; AAM78556.1; -; Genomic_DNA.
EMBL; AK313286; BAG36094.1; -; mRNA.
EMBL; AL121924; CAC27344.1; -; Genomic_DNA.
EMBL; CH471133; EAX10428.1; -; Genomic_DNA.
EMBL; CH471133; EAX10429.1; -; Genomic_DNA.
EMBL; CH471133; EAX10430.1; -; Genomic_DNA.
EMBL; BC000491; AAH00491.1; -; mRNA.
EMBL; BC062439; AAH62439.1; -; mRNA.
CCDS; CCDS13087.1; -.
PIR; A27445; WMHUET.
RefSeq; NP_002583.1; NM_002592.2.
RefSeq; NP_872590.1; NM_182649.1.
UniGene; Hs.147433; -.
UniGene; Hs.744934; -.
PDB; 1AXC; X-ray; 2.60 A; A/C/E=1-261.
PDB; 1U76; X-ray; 2.60 A; A/C/E=1-261.
PDB; 1U7B; X-ray; 1.88 A; A=1-261.
PDB; 1UL1; X-ray; 2.90 A; A/B/C=1-261.
PDB; 1VYJ; X-ray; 2.80 A; A/C/E/G/I/K=1-261.
PDB; 1VYM; X-ray; 2.30 A; A/B/C=1-261.
PDB; 1W60; X-ray; 3.15 A; A/B=1-261.
PDB; 2ZVK; X-ray; 2.70 A; A/B/C=1-261.
PDB; 2ZVL; X-ray; 2.50 A; A/B/C/D/E/F=1-261.
PDB; 2ZVM; X-ray; 2.30 A; A/B/C=1-261.
PDB; 3JA9; EM; 22.00 A; A/B/C=1-261.
PDB; 3P87; X-ray; 2.99 A; A/B/C/D/E/F=1-261.
PDB; 3TBL; X-ray; 2.90 A; A/B/C=1-261.
PDB; 3VKX; X-ray; 2.10 A; A=1-261.
PDB; 3WGW; X-ray; 2.80 A; A/B=1-261.
PDB; 4D2G; X-ray; 2.65 A; A/B/C=1-261.
PDB; 4RJF; X-ray; 2.01 A; A/C/E=1-261.
PDB; 4ZTD; X-ray; 2.20 A; A/B/C=2-254.
PDB; 5E0T; X-ray; 2.67 A; A/B/C=1-261.
PDB; 5E0U; X-ray; 1.93 A; A/B/C=1-261.
PDB; 5E0V; X-ray; 2.07 A; A/B=1-261.
PDB; 5IY4; X-ray; 2.94 A; A/C/E=1-261.
PDB; 5L7C; X-ray; 2.82 A; A/B/C=1-261.
PDB; 5MOM; X-ray; 2.27 A; A/B/C=1-258.
PDBsum; 1AXC; -.
PDBsum; 1U76; -.
PDBsum; 1U7B; -.
PDBsum; 1UL1; -.
PDBsum; 1VYJ; -.
PDBsum; 1VYM; -.
PDBsum; 1W60; -.
PDBsum; 2ZVK; -.
PDBsum; 2ZVL; -.
PDBsum; 2ZVM; -.
PDBsum; 3JA9; -.
PDBsum; 3P87; -.
PDBsum; 3TBL; -.
PDBsum; 3VKX; -.
PDBsum; 3WGW; -.
PDBsum; 4D2G; -.
PDBsum; 4RJF; -.
PDBsum; 4ZTD; -.
PDBsum; 5E0T; -.
PDBsum; 5E0U; -.
PDBsum; 5E0V; -.
PDBsum; 5IY4; -.
PDBsum; 5L7C; -.
PDBsum; 5MOM; -.
ProteinModelPortal; P12004; -.
SMR; P12004; -.
BioGrid; 111142; 291.
DIP; DIP-1098N; -.
ELM; P12004; -.
IntAct; P12004; 109.
MINT; MINT-5000943; -.
STRING; 9606.ENSP00000368438; -.
BindingDB; P12004; -.
ChEMBL; CHEMBL2346488; -.
iPTMnet; P12004; -.
PhosphoSitePlus; P12004; -.
SwissPalm; P12004; -.
BioMuta; PCNA; -.
DMDM; 129694; -.
SWISS-2DPAGE; P12004; -.
EPD; P12004; -.
MaxQB; P12004; -.
PaxDb; P12004; -.
PeptideAtlas; P12004; -.
PRIDE; P12004; -.
TopDownProteomics; P12004; -.
DNASU; 5111; -.
Ensembl; ENST00000379143; ENSP00000368438; ENSG00000132646.
Ensembl; ENST00000379160; ENSP00000368458; ENSG00000132646.
GeneID; 5111; -.
KEGG; hsa:5111; -.
UCSC; uc002wlp.4; human.
CTD; 5111; -.
DisGeNET; 5111; -.
GeneCards; PCNA; -.
HGNC; HGNC:8729; PCNA.
HPA; CAB000148; -.
HPA; HPA030521; -.
HPA; HPA030522; -.
HPA; HPA030523; -.
MalaCards; PCNA; -.
MIM; 176740; gene.
MIM; 615919; phenotype.
neXtProt; NX_P12004; -.
OpenTargets; ENSG00000132646; -.
PharmGKB; PA263; -.
eggNOG; KOG1636; Eukaryota.
eggNOG; COG0592; LUCA.
GeneTree; ENSGT00390000004965; -.
HOGENOM; HOG000211098; -.
HOVERGEN; HBG000947; -.
InParanoid; P12004; -.
KO; K04802; -.
OMA; SDGFDKY; -.
OrthoDB; EOG091G0GQ7; -.
PhylomeDB; P12004; -.
TreeFam; TF313441; -.
Reactome; R-HSA-110312; Translesion synthesis by REV1.
Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
Reactome; R-HSA-110320; Translesion Synthesis by POLH.
Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere.
Reactome; R-HSA-174414; Processive synthesis on the C-strand of the telomere.
Reactome; R-HSA-174417; Telomere C-strand (Lagging Strand) Synthesis.
Reactome; R-HSA-174437; Removal of the Flap Intermediate from the C-strand.
Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
Reactome; R-HSA-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
Reactome; R-HSA-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
Reactome; R-HSA-539107; Activation of E2F1 target genes at G1/S.
Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
Reactome; R-HSA-5655862; Translesion synthesis by POLK.
Reactome; R-HSA-5656121; Translesion synthesis by POLI.
Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
Reactome; R-HSA-5696400; Dual Incision in GG-NER.
Reactome; R-HSA-6782135; Dual incision in TC-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-HSA-69091; Polymerase switching.
Reactome; R-HSA-69166; Removal of the Flap Intermediate.
Reactome; R-HSA-69183; Processive synthesis on the lagging strand.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
SignaLink; P12004; -.
SIGNOR; P12004; -.
ChiTaRS; PCNA; human.
EvolutionaryTrace; P12004; -.
GeneWiki; Proliferating_cell_nuclear_antigen; -.
GenomeRNAi; 5111; -.
PRO; PR:P12004; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000132646; -.
CleanEx; HS_PCNA; -.
Genevisible; P12004; HS.
GO; GO:0005813; C:centrosome; IDA:MGI.
GO; GO:0005663; C:DNA replication factor C complex; TAS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0043596; C:nuclear replication fork; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043626; C:PCNA complex; IDA:UniProtKB.
GO; GO:0070557; C:PCNA-p21 complex; IDA:UniProtKB.
GO; GO:0005657; C:replication fork; IDA:MGI.
GO; GO:0030894; C:replisome; TAS:BHF-UCL.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
GO; GO:0032139; F:dinucleotide insertion or deletion binding; IDA:BHF-UCL.
GO; GO:0070182; F:DNA polymerase binding; IPI:UniProtKB.
GO; GO:0030337; F:DNA polymerase processivity factor activity; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0030331; F:estrogen receptor binding; IEA:Ensembl.
GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0032405; F:MutLalpha complex binding; IDA:HGNC.
GO; GO:0000701; F:purine-specific mismatch base pair DNA N-glycosylase activity; IDA:BHF-UCL.
GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
GO; GO:0042769; P:DNA damage response, detection of DNA damage; TAS:Reactome.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0006266; P:DNA ligation; TAS:Reactome.
GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
GO; GO:0070987; P:error-free translesion synthesis; TAS:Reactome.
GO; GO:0042276; P:error-prone translesion synthesis; TAS:Reactome.
GO; GO:0044849; P:estrous cycle; IEA:Ensembl.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0006298; P:mismatch repair; IDA:BHF-UCL.
GO; GO:1902990; P:mitotic telomere maintenance via semi-conservative replication; ISS:BHF-UCL.
GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; TAS:Reactome.
GO; GO:0033683; P:nucleotide-excision repair, DNA incision; TAS:Reactome.
GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; TAS:Reactome.
GO; GO:0032077; P:positive regulation of deoxyribonuclease activity; IDA:UniProtKB.
GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
GO; GO:0045740; P:positive regulation of DNA replication; IMP:UniProtKB.
GO; GO:0016925; P:protein sumoylation; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0031297; P:replication fork processing; ISS:BHF-UCL.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:1902065; P:response to L-glutamate; IEA:Ensembl.
GO; GO:0000723; P:telomere maintenance; TAS:Reactome.
GO; GO:0000722; P:telomere maintenance via recombination; TAS:Reactome.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
GO; GO:0019985; P:translesion synthesis; IDA:UniProtKB.
HAMAP; MF_00317; DNApol_clamp_arch; 1.
InterPro; IPR000730; Pr_cel_nuc_antig.
InterPro; IPR022649; Pr_cel_nuc_antig_C.
InterPro; IPR022659; Pr_cel_nuc_antig_CS.
InterPro; IPR022648; Pr_cel_nuc_antig_N.
PANTHER; PTHR11352:SF7; PTHR11352:SF7; 1.
Pfam; PF02747; PCNA_C; 1.
Pfam; PF00705; PCNA_N; 1.
PRINTS; PR00339; PCNACYCLIN.
TIGRFAMs; TIGR00590; pcna; 1.
PROSITE; PS01251; PCNA_1; 1.
PROSITE; PS00293; PCNA_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Deafness;
Direct protein sequencing; Disease mutation; DNA damage; DNA repair;
DNA replication; DNA-binding; Dwarfism; Isopeptide bond; Methylation;
Neurodegeneration; Nucleus; Phosphoprotein; Reference proteome;
Ubl conjugation.
CHAIN 1 261 Proliferating cell nuclear antigen.
/FTId=PRO_0000149158.
DNA_BIND 61 80 {ECO:0000255}.
REGION 7 100 Interaction with NUDT15.
{ECO:0000269|PubMed:19419956}.
MOD_RES 14 14 N6-acetyllysine.
{ECO:0000269|PubMed:19419956}.
MOD_RES 77 77 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 80 80 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 211 211 Phosphotyrosine; by EGFR.
{ECO:0000269|PubMed:17115032}.
MOD_RES 248 248 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 164 164 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 164 164 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:17108083,
ECO:0000269|PubMed:17130289}.
CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 228 228 S -> I (in ATLD2; a hypomorphic mutation
affecting DNA repair in response to UV;
results in significantly decreased
interaction with FEN1, LIG1 and ERCC5;
dbSNP:rs369958038).
{ECO:0000269|PubMed:24911150}.
/FTId=VAR_071871.
MUTAGEN 13 13 K->R: Inhibits acetylation, recruitment
to DNA damage sites, inducible
ubiquitination and protein degradation,
DNA replication and repair synthesis
efficiencies, but homotrimer formation,
nuclear recruitment to DNA damage sites,
interactions with CREBBP, EP300 and POLD1
are similar as the wild-type; in
association with R-14; R-20; R-77 and R-
80. {ECO:0000269|PubMed:24939902}.
MUTAGEN 14 14 K->R: Inhibits acetylation, recruitment
to DNA damage sites, inducible
ubiquitination and protein degradation,
DNA replication and repair synthesis
efficiencies, but homotrimer formation,
nuclear recruitment to DNA damage sites,
interactions with CREBBP, EP300 and POLD1
are similar as the wild-type; in
association with R-13; R-20; R-77 and R-
80. {ECO:0000269|PubMed:24939902}.
MUTAGEN 20 20 K->R: Inhibits acetylation, recruitment
to DNA damage sites, inducible
ubiquitination and protein degradation,
DNA replication and repair synthesis
efficiencies, but homotrimer formation,
nuclear recruitment to DNA damage sites,
interactions with CREBBP, EP300 and POLD1
are similar as the wild-type; in
association with R-13; R-14; R-77 and R-
80. {ECO:0000269|PubMed:24939902}.
MUTAGEN 43 45 SHV->AAA: No effect on POLD3-binding.
{ECO:0000269|PubMed:11595739}.
MUTAGEN 77 77 K->A: Inhibits recruitment to DNA damage
sites, but nuclear localization is
similar as the wild-type; in association
with A-80. {ECO:0000269|PubMed:24939902}.
MUTAGEN 77 77 K->R: Inhibits acetylation, recruitment
to DNA damage sites, inducible
ubiquitination and protein degradation,
DNA replication and repair synthesis
efficiencies, but homotrimer formation,
nuclear recruitment to DNA damage sites,
interactions with CREBBP, EP300 and POLD1
are similar as the wild-type; in
association with R-13; R-14; R-20 and R-
80. {ECO:0000269|PubMed:24939902}.
MUTAGEN 80 80 K->A: Inhibits recruitment to DNA damage
sites, but nuclear localization is
similar as the wild-type; in association
with A-77. {ECO:0000269|PubMed:24939902}.
MUTAGEN 80 80 K->R: Inhibits acetylation, recruitment
to DNA damage sites, inducible
ubiquitination and protein degradation,
DNA replication and repair synthesis
efficiencies, but homotrimer formation,
nuclear recruitment to DNA damage sites,
interactions with CREBBP, EP300 and POLD1
are similar as the wild-type; in
association with R-13; R-14; R-20 and R-
77. {ECO:0000269|PubMed:24939902}.
MUTAGEN 125 128 QLGI->AAAA: Strong decrease in POLD3-
binding. {ECO:0000269|PubMed:11595739}.
MUTAGEN 164 164 K->R: Abolishes ubiquitination. No effect
on interaction with SHPRH.
{ECO:0000269|PubMed:17108083,
ECO:0000269|PubMed:17130289,
ECO:0000269|PubMed:18719106,
ECO:0000269|PubMed:20129063}.
MUTAGEN 188 190 VDK->AAA: No effect on POLD3-binding.
{ECO:0000269|PubMed:11595739}.
MUTAGEN 211 211 Y->F: Alters chromatin-associated PCNA
stability and its function in DNA
replication and repair.
{ECO:0000269|PubMed:17115032}.
MUTAGEN 251 254 LAPK->AAAA: Decrease in POLD3-binding.
{ECO:0000269|PubMed:11595739}.
STRAND 2 7 {ECO:0000244|PDB:1U7B}.
HELIX 10 20 {ECO:0000244|PDB:1U7B}.
STRAND 24 31 {ECO:0000244|PDB:1U7B}.
STRAND 34 40 {ECO:0000244|PDB:1U7B}.
STRAND 44 53 {ECO:0000244|PDB:1U7B}.
HELIX 54 56 {ECO:0000244|PDB:1U7B}.
STRAND 57 64 {ECO:0000244|PDB:1U7B}.
STRAND 66 71 {ECO:0000244|PDB:1U7B}.
HELIX 72 79 {ECO:0000244|PDB:1U7B}.
STRAND 87 92 {ECO:0000244|PDB:1U7B}.
STRAND 94 96 {ECO:0000244|PDB:1VYM}.
STRAND 97 104 {ECO:0000244|PDB:1U7B}.
STRAND 106 109 {ECO:0000244|PDB:4RJF}.
STRAND 111 117 {ECO:0000244|PDB:1U7B}.
STRAND 121 126 {ECO:0000244|PDB:5E0U}.
STRAND 134 140 {ECO:0000244|PDB:1U7B}.
HELIX 141 152 {ECO:0000244|PDB:1U7B}.
STRAND 156 163 {ECO:0000244|PDB:1U7B}.
STRAND 166 173 {ECO:0000244|PDB:1U7B}.
STRAND 176 182 {ECO:0000244|PDB:1U7B}.
HELIX 191 193 {ECO:0000244|PDB:5E0U}.
STRAND 196 201 {ECO:0000244|PDB:1U7B}.
STRAND 203 208 {ECO:0000244|PDB:1U7B}.
HELIX 209 215 {ECO:0000244|PDB:1U7B}.
HELIX 216 221 {ECO:0000244|PDB:1U7B}.
STRAND 223 229 {ECO:0000244|PDB:1U7B}.
STRAND 231 233 {ECO:0000244|PDB:1VYM}.
STRAND 235 241 {ECO:0000244|PDB:1U7B}.
TURN 242 244 {ECO:0000244|PDB:1U7B}.
STRAND 245 251 {ECO:0000244|PDB:1U7B}.
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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