[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1073/pnas.84.6.1575; PubMed=2882507 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 GENOMIC DNA]. DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Bone marrow, and Lung; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[6]	PROTEIN SEQUENCE OF 1-26. DOI=10.1038/326471a0; PubMed=2882422 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[7]	PROTEIN SEQUENCE OF 169-181, AND MASS SPECTROMETRY. TISSUE=Fetal brain cortex; Lubec G., Chen W.-Q., Sun Y.; Submitted (DEC-2008) to UniProtKB.
[8]	INTERACTION WITH ERCC5/XPG. DOI=10.1074/jbc.272.39.24522; PubMed=9305916 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[9]	INTERACTION WITH DNMT1. DOI=10.1126/science.277.5334.1996; PubMed=9302295 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[10]	INTERACTION WITH CDC6. PubMed=9566895 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[11]	INTERACTION WITH APEX2. DOI=10.1093/nar/29.11.2349; PubMed=11376153 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[12]	INTERACTION WITH POLK. PubMed=11784855 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[13]	INTERACTION WITH DNTTIP2. DOI=10.1046/j.1365-2443.2003.00656.x; PubMed=12786946 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[14]	INTERACTION WITH POLDIP2. TISSUE=Placenta; DOI=10.1074/jbc.M208694200; PubMed=12522211 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[15]	INTERACTION WITH EXO1. DOI=10.1016/j.molcel.2004.06.016; PubMed=15225546 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[16]	UBIQUITINATION, AND INTERACTION WITH POLH. DOI=10.1016/S1097-2765(04)00259-X; PubMed=15149598 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[17]	INTERACTION WITH BAZ1B. DOI=10.1038/ncb1196; PubMed=15543136 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[18]	INTERACTION WITH POLD1; POLD3 AND POLD4. DOI=10.1074/jbc.M600322200; PubMed=16510448 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[19]	INTERACTION WITH SHPRH, UBIQUITINATION AT LYS-164, AND MUTAGENESIS OF LYS-164. DOI=10.1083/jcb.200606145; PubMed=17130289 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[20]	UBIQUITINATION AT LYS-164, AND MUTAGENESIS OF LYS-164. DOI=10.1073/pnas.0608595103; PubMed=17108083 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[21]	UBIQUITINATION. PubMed=18948756 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[22]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[23]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). DOI=10.1016/S0092-8674(00)81347-1; PubMed=8861913 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[24]	X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH PCNA. DOI=10.1038/sj.emboj.7600519; PubMed=15616578 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

FUNCTION: This protein is an 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.
SUBUNIT: Homotrimer. Interacts with KCTD10. Interacts with PPP1R15A (By similarity). Forms a complex with activator 1 heteropentamer in the presence of ATP. Interacts with POLH, POLK, DNMT1, ERCC5/XPG, FEN1, CDC6, APEX2 and POLDIP2. Interacts with EXO1 and SHPRH. Forms a ternary complex with DNTTIP2 and core histone. Interacts with POLD1, POLD3 and POLD4. Interacts with BAZ1B/WSTF; the interaction is direct.
INTERACTION:
Q99728:BARD1; NbExp=1; IntAct=EBI-358311, EBI-473181;
P38936:CDKN1A; NbExp=1; IntAct=EBI-358311, EBI-375077;
P42771:CDKN2A; NbExp=3; IntAct=EBI-358311, EBI-375053;
Q13111:CHAF1A; NbExp=1; IntAct=EBI-358311, EBI-1020839;
Q05048:CSTF1; NbExp=1; IntAct=EBI-358311, EBI-1789619;
P39748:FEN1; NbExp=2; IntAct=EBI-358311, EBI-707816;
Q9Z111:Gadd45g (xeno); NbExp=4; IntAct=EBI-358311, EBI-1173616;
P28340:POLD1; NbExp=1; IntAct=EBI-358311, EBI-716569;
P49005:POLD2; NbExp=1; IntAct=EBI-358311, EBI-372354;
Q15054:POLD3; NbExp=3; IntAct=EBI-358311, EBI-864956;
Q9HCU8:POLD4; NbExp=2; IntAct=EBI-358311, EBI-864968;
P36873-1:PPP1CC; NbExp=1; IntAct=EBI-358311, EBI-356289;
SUBCELLULAR LOCATION: Nucleus.
PTM: Upon methyl methanesulfonate-induced DNA damage, mono-ubiquitinated by the UBE2B-RAD18 complex on Lys-164. This induces non-canonical poly-ubiquitination on Lys-164 through 'Lys-63' linkage of ubiquitin moieties by the E2 complex UBE2N-UBE2V2 and the E3 ligases RNF8 and SHPRH, which are required for DNA repair.
DISEASE: Antibodies are present in sera from patients with systemic lupus erythematosus.
SIMILARITY: Belongs to the PCNA family.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/pcna/";.
WEB RESOURCE: Name=Wikipedia; Note=PCNA entry; URL="http://en.wikipedia.org/wiki/PCNA";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M15796; AAA35736.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J04718; AAA60040.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF527838; AAM78556.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121924; CAC27344.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000491; AAH00491.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC062439; AAH62439.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00021700; -.

PIR

A27445; WMHUET.

RefSeq

NP_002583.1; -.
NP_872590.1; -.

UniGene

Hs.147433

3D structure databases

PDB

1AXC; X-ray; 2.60 A; A/C/E=1-261.	[ExPASy / RCSB / EBI]
1U76; X-ray; 2.60 A; A/C/E=1-261.	[ExPASy / RCSB / EBI]
1U7B; X-ray; 1.88 A; A=1-261.	[ExPASy / RCSB / EBI]
1UL1; X-ray; 2.90 A; A/B/C=1-261.	[ExPASy / RCSB / EBI]
1VYJ; X-ray; 2.80 A; A/C/E/G/I/K=1-261.	[ExPASy / RCSB / EBI]
1VYM; X-ray; 2.30 A; A/B/C=1-261.	[ExPASy / RCSB / EBI]
1W60; X-ray; 3.15 A; A/B=1-261.	[ExPASy / RCSB / EBI]
2ZVK; X-ray; 2.70 A; A/B/C=1-261.	[ExPASy / RCSB / EBI]
2ZVL; X-ray; 2.50 A; A/B/C/D/E/F=1-261.	[ExPASy / RCSB / EBI]
2ZVM; X-ray; 2.30 A; A/B/C=1-261.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AXC; -.
1U76; -.
1U7B; -.
1UL1; -.
1VYJ; -.
1VYM; -.
1W60; -.
2ZVK; -.
2ZVL; -.
2ZVM; -.

ModBase

P12004.

Protein-protein interaction databases

DIP

DIP:1098N; -.

IntAct

P12004; 24.

PTM databases

PhosphoSite

P12004; -.

Enzyme and pathway databases

Pathway_Interaction_DB

bard1pathway; BARD1 signaling events.

Reactome

REACT_152; Cell Cycle, Mitotic.
REACT_216; DNA Repair.
REACT_383; DNA Replication.
REACT_7970; Telomere Maintenance.

2D gel databases

SWISS-2DPAGE

P12004; -.

Organism-specific databases

GC20M005043; -.

HIX0015618; -.

HGNC:8729; PCNA.

CAB000148; -.

176740; gene. [NCBI / EBI]

PharmGKB

PA263; -.

Gene expression databases

P12004; -.

P12004; -.

HS_PCNA; -.

ENSG00000132646; Homo sapiens.

Ontologies

GO:0005663;	Cellular component: DNA replication factor C complex (traceable author statement from UniProtKB).
GO:0005654;	Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0043626;	Cellular component: PCNA complex (inferred from electronic annotation from InterPro).
GO:0032139;	Molecular function: dinucleotide insertion or deletion binding (inferred from direct assay from UniProtKB).
GO:0030337;	Molecular function: DNA polymerase processivity factor activity (inferred from electronic annotation from InterPro).
GO:0032405;	Molecular function: MutLalpha complex binding (inferred from direct assay from HGNC).
GO:0000701;	Molecular function: purine-specific mismatch base pair DNA N-glycosylase activity (inferred from direct assay from UniProtKB).
GO:0008283;	Biological process: cell proliferation (traceable author statement from ProtInc).
GO:0006298;	Biological process: mismatch repair (inferred from direct assay from UniProtKB).
GO:0006297;	Biological process: nucleotide-excision repair, DNA gap filling (inferred from experiment from Reactome).
GO:0048015;	Biological process: phosphoinositide-mediated signaling (non-traceable author statement from UniProtKB).
GO:0006275;	Biological process: regulation of DNA replication (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000730; Pr_cel_nuc_antig.
Graphical view of domain structure.

PANTHER

PTHR11352; Pr_cel_nuc_antig; 1.

Pfam

PF02747; PCNA_C; 1.
PF00705; PCNA_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR00339; PCNACYCLIN.

ProDom

PD002673; Pr_cel_nuc_antig; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00590; pcna; 1.

PROSITE

PS01251; PCNA_1; 1.
PS00293; PCNA_2; 1.

Proteomic databases

PeptideAtlas

P12004; -.

PRIDE

P12004; -.

Genome annotation databases

Ensembl

ENSG00000132646; Homo sapiens. [Contig view]

GeneID

5111; -.

KEGG

hsa:5111; -.

Phylogenomic databases

HOVERGEN

P12004; -.

OMA

P12004; ICRDLSQ.

Other

19722; -.

PCNA; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; DNA replication; DNA-binding; Isopeptide bond; Nucleus; Systemic lupus erythematosus; Ubl conjugation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 261`	`261`	`Proliferating cell nuclear antigen.`	`PRO_0000149158`
`DNA_BIND`	`61 80`	`20`	`Potential.`
`CROSSLNK`	`164 164`		`Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).`
`MUTAGEN`	`164 164`		`K->R: Abolishes ubiquitination. No effect on interaction with SHPRH.`
`STRAND`	`2 7`	`6`
`HELIX`	`10 20`	`11`
`STRAND`	`24 31`	`8`
`STRAND`	`34 40`	`7`
`STRAND`	`44 53`	`10`
`HELIX`	`54 56`	`3`
`STRAND`	`57 64`	`8`
`STRAND`	`66 71`	`6`
`HELIX`	`72 79`	`8`
`STRAND`	`87 92`	`6`
`STRAND`	`97 104`	`8`
`STRAND`	`108 117`	`10`
`STRAND`	`134 140`	`7`
`HELIX`	`141 152`	`12`
`STRAND`	`156 163`	`8`
`STRAND`	`166 173`	`8`
`STRAND`	`176 182`	`7`
`STRAND`	`196 201`	`6`
`STRAND`	`203 208`	`6`
`HELIX`	`209 215`	`7`
`HELIX`	`216 221`	`6`
`STRAND`	`223 229`	`7`
`STRAND`	`235 241`	`7`
`TURN`	`242 244`	`3`
`STRAND`	`245 251`	`7`

Sequence information

Length: 261 AA [This is the length of the unprocessed precursor]

Molecular weight: 28769 Da [This is the MW of the unprocessed precursor]

CRC64: E6F08E7EDBC48B00 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFEARLVQGS ILKKVLEALK DLINEACWDI SSSGVNLQSM DSSHVSLVQL TLRSEGFDTY 

        70         80         90        100        110        120 
RCDRNLAMGV NLTSMSKILK CAGNEDIITL RAEDNADTLA LVFEAPNQEK VSDYEMKLMD 

       130        140        150        160        170        180 
LDVEQLGIPE QEYSCVVKMP SGEFARICRD LSHIGDAVVI SCAKDGVKFS ASGELGNGNI 

       190        200        210        220        230        240 
KLSQTSNVDK EEEAVTIEMN EPVQLTFALR YLNFFTKATP LSSTVTLSMS ADVPLVVEYK 

       250        260 
IADMGHLKYY LAPKIEDEEG S

P12004 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools