P12004 (PCNA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proliferating cell nuclear antigen
Short name=PCNA

Alternative name(s):
Cyclin

Gene names

Name:

PCNA

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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. 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. Ref.29 Ref.31
Subunit structure	Homotrimer By similarity. Forms a complex with activator 1 heteropentamer in the presence of ATP. Interacts with EXO1, POLH, POLK, DNMT1, ERCC5, FEN1, CDC6 and POLDIP2. Interacts with APEX2; this interaction is triggered by reactive oxygen species and increased by misincorporation of uracil in nuclear DNA. Forms a ternary complex with DNTTIP2 and core histone. Interacts with KCTD10 and PPP1R15A By similarity. Interacts with POLD1, POLD3 and POLD4. Interacts with BAZ1B; the interaction is direct. Interacts with HLTF and SHPRH. Interacts with NUDT15. Interaction is disrupted in response to UV irradiation and acetylation. Interacts with CDKN1A/p21(CIP1) and CDT1; interacts via their PIP-box which also recruits the DCX(DTL) complex. Interacts with DDX11. Interacts with EGFR; positively regulates PCNA. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32
Subcellular location	Nucleus. Note: 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.
Post-translational modification	Upon methyl methanesulfonate-induced DNA damage, mono-ubiquitinated by the UBE2B-RAD18 complex on Lys-164. This induces 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, which is required for DNA repair. 'Lys-63' polyubiquitination prevents genomic instability on DNA damage. 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. Acetylated in response to UV irradiation. Acetylation disrupts interaction with NUDT15 and promotes degradation. Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes chromatin-associated PCNA. Ref.23
Miscellaneous	Antibodies against PCNA are present in sera from patients with systemic lupus erythematosus.
Sequence similarities	Belongs to the PCNA family.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Ligand	DNA-binding
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA strand elongation involved in DNA replication Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome cell proliferation Traceable author statement. Source: ProtInc mismatch repair Inferred from direct assay. Source: BHF-UCL nucleotide-excision repair, DNA gap filling Traceable author statement. Source: Reactome phosphatidylinositol-mediated signaling Non-traceable author statement. Source: UniProtKB positive regulation of deoxyribonuclease activity Inferred from direct assay Ref.29. Source: UniProtKB regulation of DNA replication Inferred from electronic annotation. Source: InterPro regulation of transcription involved in G1/S phase of mitotic cell cycle Traceable author statement. Source: Reactome telomere maintenance via recombination Traceable author statement. Source: Reactome telomere maintenance via semi-conservative replication Traceable author statement. Source: Reactome transcription-coupled nucleotide-excision repair Traceable author statement. Source: Reactome translesion synthesis Inferred from direct assay Ref.34. Source: UniProtKB
Cellular component	DNA replication factor C complex Traceable author statement Ref.2. Source: UniProtKB PCNA complex Inferred from electronic annotation. Source: InterPro PCNA-p21 complex Inferred from direct assay Ref.26. Source: UniProtKB cytoplasm Inferred from direct assay. Source: HPA microtubule cytoskeleton Inferred from direct assay. Source: HPA nuclear replication fork Inferred from direct assay Ref.19. Source: BHF-UCL nucleoplasm Traceable author statement. Source: Reactome
Molecular function	DNA polymerase processivity factor activity Inferred from electronic annotation. Source: InterPro MutLalpha complex binding Inferred from direct assay. Source: HGNC dinucleotide insertion or deletion binding Inferred from direct assay. Source: BHF-UCL identical protein binding Inferred from physical interaction. Source: IntAct purine-specific mismatch base pair DNA N-glycosylase activity Inferred from direct assay. Source: BHF-UCL receptor tyrosine kinase binding Inferred from physical interaction Ref.23. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		4	EBI-358311,EBI-358311
CDKN1A	P38936	4	EBI-358311,EBI-375077
CDKN2A	P42771	8	EBI-358311,EBI-375053
CHAF1A	Q13111	2	EBI-358311,EBI-1020839
FEN1	P39748	4	EBI-358311,EBI-707816
Gadd45g	Q9Z111	9	EBI-358311,EBI-1173616	From a different organism.
POLD1	P28340	2	EBI-358311,EBI-716569
POLD3	Q15054	4	EBI-358311,EBI-864956
POLD4	Q9HCU8	4	EBI-358311,EBI-864968

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 261

261

Proliferating cell nuclear antigen

PRO_0000149158

Regions

DNA binding

61 – 80

20

Potential

Region

7 – 100

94

Interaction with NUDT15

Amino acid modifications

Modified residue

77

1

N6-acetyllysine Ref.33

Modified residue

80

1

N6-acetyllysine Ref.33

Modified residue

211

1

Phosphotyrosine; by EGFR Ref.23

Modified residue

248

1

N6-acetyllysine Ref.33

Cross-link

164

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.21 Ref.24

Experimental info

Mutagenesis

164

1

K → R: Abolishes ubiquitination. No effect on interaction with SHPRH. Ref.21 Ref.24 Ref.31 Ref.34

Mutagenesis

211

1

Y → F: Alters chromatin-associated PCNA stability and its function in DNA replication and repair. Ref.23

Secondary structure

1

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261

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Helix

10 – 20

11

Beta strand

24 – 31

8

Beta strand

34 – 40

7

Beta strand

44 – 53

10

Helix

54 – 56

3

Beta strand

57 – 64

8

Beta strand

66 – 71

6

Helix

72 – 79

8

Beta strand

87 – 92

6

Beta strand

97 – 104

8

Beta strand

108 – 117

10

Beta strand

134 – 140

7

Helix

141 – 152

12

Beta strand

156 – 163

8

Beta strand

166 – 173

8

Beta strand

176 – 182

7

Beta strand

196 – 201

6

Beta strand

203 – 208

6

Helix

209 – 215

7

Helix

216 – 221

6

Beta strand

223 – 229

7

Beta strand

235 – 241

7

Turn

242 – 244

3

Beta strand

245 – 251

7

Sequences

	Sequence		Length	Mass (Da)
	P12004 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: E6F08E7EDBC48B00	FASTA	261	28,769
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence of the human nuclear protein cyclin: homology with DNA-binding proteins." Almendral J.M., Huebsch D., Blundell P.A., Macdonald-Bravo H., Bravo R. Proc. Natl. Acad. Sci. U.S.A. 84:1575-1579(1987) [PubMed: 2882507] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure of the human gene for the proliferating cell nuclear antigen." Travali S., Ku D.H., Rizzo M.G., Ottavio L., Baserga R., Calabretta B. J. Biol. Chem. 264:7466-7472(1989) [PubMed: 2565339] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	NIEHS SNPs program Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skeletal muscle.
[5]	"The DNA sequence and comparative analysis of human chromosome 20." 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. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow and Lung.
[8]	"The cell-cycle regulated proliferating cell nuclear antigen is required for SV40 DNA replication in vitro." Prelich G., Kostura M., Marshak D.R., Mathews M.B., Stillman B. Nature 326:471-475(1987) [PubMed: 2882422] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-26.
[9]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 169-181, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[10]	"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." Gary R., Ludwig D.L., Cornelius H.L., MacInnes M.A., Park M.S. J. Biol. Chem. 272:24522-24529(1997) [PubMed: 9305916] [Abstract] Cited for: INTERACTION WITH ERCC5/XPG.
[11]	"Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1." Chuang L.S.-H., Ian H.-I., Koh T.-W., Ng H.-H., Xu G., Li B.F.L. Science 277:1996-2000(1997) [PubMed: 9302295] [Abstract] Cited for: INTERACTION WITH DNMT1.
[12]	"Human CDC6/Cdc18 associates with Orc1 and cyclin-cdk and is selectively eliminated from the nucleus at the onset of S phase." Saha P., Chen J., Thome K.C., Lawlis S.J., Hou Z.H., Hendricks M., Parvin J.D., Dutta A. Mol. Cell. Biol. 18:2758-2767(1998) [PubMed: 9566895] [Abstract] Cited for: INTERACTION WITH CDC6.
[13]	"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." Tsuchimoto D., Sakai Y., Sakumi K., Nishioka K., Sasaki M., Fujiwara T., Nakabeppu Y. Nucleic Acids Res. 29:2349-2360(2001) [PubMed: 11376153] [Abstract] Cited for: INTERACTION WITH APEX2.
[14]	"Stimulation of DNA synthesis activity of human DNA polymerase kappa by PCNA." Haracska L., Unk I., Johnson R.E., Phillips B.B., Hurwitz J., Prakash L., Prakash S. Mol. Cell. Biol. 22:784-791(2002) [PubMed: 11784855] [Abstract] Cited for: INTERACTION WITH POLK.
[15]	"Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone." Fujita K., Shimazaki N., Ohta Y., Kubota T., Ibe S., Toji S., Tamai K., Fujisaki S., Hayano T., Koiwai O. Genes Cells 8:559-571(2003) [PubMed: 12786946] [Abstract] Cited for: INTERACTION WITH DNTTIP2.
[16]	"Identification of a novel protein, PDIP38, that interacts with the p50 subunit of DNA polymerase delta and proliferating cell nuclear antigen." Liu L., Rodriguez-Belmonte E.M., Mazloum N., Xie B., Lee M.Y.W.T. J. Biol. Chem. 278:10041-10047(2003) [PubMed: 12522211] [Abstract] Cited for: INTERACTION WITH POLDIP2. Tissue: Placenta.
[17]	"A defined human system that supports bidirectional mismatch-provoked excision." Dzantiev L., Constantin N., Genschel J., Iyer R.R., Burgers P.M., Modrich P. Mol. Cell 15:31-41(2004) [PubMed: 15225546] [Abstract] Cited for: INTERACTION WITH EXO1.
[18]	"Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage." Kannouche P.L., Wing J., Lehmann A.R. Mol. Cell 14:491-500(2004) [PubMed: 15149598] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH POLH.
[19]	"The Williams syndrome transcription factor interacts with PCNA to target chromatin remodelling by ISWI to replication foci." 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. Nat. Cell Biol. 6:1236-1244(2004) [PubMed: 15543136] [Abstract] Cited for: INTERACTION WITH BAZ1B.
[20]	"Functional roles of p12, the fourth subunit of human DNA polymerase delta." Li H., Xie B., Zhou Y., Rahmeh A., Trusa S., Zhang S., Gao Y., Lee E.Y., Lee M.Y. J. Biol. Chem. 281:14748-14755(2006) [PubMed: 16510448] [Abstract] Cited for: INTERACTION WITH POLD1; POLD3 AND POLD4.
[21]	"Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination." Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K. J. Cell Biol. 175:703-708(2006) [PubMed: 17130289] [Abstract] Cited for: INTERACTION WITH SHPRH, UBIQUITINATION AT LYS-164, MUTAGENESIS OF LYS-164.
[22]	"A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1." Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C. Mol. Cell 23:709-721(2006) [PubMed: 16949367] [Abstract] Cited for: INTERACTION WITH CDT1.
[23]	"Tyrosine phosphorylation controls PCNA function through protein stability." 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. Nat. Cell Biol. 8:1359-1368(2006) [PubMed: 17115032] [Abstract] Cited for: PHOSPHORYLATION AT TYR-211 BY EGFR, MUTAGENESIS OF TYR-211, INTERACTION WITH EGFR.
[24]	"Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen." Unk I., Hajdu I., Fatyol K., Szakal B., Blastyak A., Bermudez V., Hurwitz J., Prakash L., Prakash S., Haracska L. Proc. Natl. Acad. Sci. U.S.A. 103:18107-18112(2006) [PubMed: 17108083] [Abstract] Cited for: UBIQUITINATION AT LYS-164, MUTAGENESIS OF LYS-164.
[25]	"PCNA is ubiquitinated by RNF8." Zhang S., Chea J., Meng X., Zhou Y., Lee E.Y.C., Lee M.Y.W.T. Cell Cycle 7:3399-3404(2008) [PubMed: 18948756] [Abstract] Cited for: UBIQUITINATION.
[26]	"PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex." Abbas T., Sivaprasad U., Terai K., Amador V., Pagano M., Dutta A. Genes Dev. 22:2496-2506(2008) [PubMed: 18794347] [Abstract] Cited for: INTERACTION WITH CDKN1A.
[27]	"Studies with the human cohesin establishment factor, ChlR1. Association of ChlR1 with Ctf18-RFC and Fen1." Farina A., Shin J.H., Kim D.H., Bermudez V.P., Kelman Z., Seo Y.S., Hurwitz J. J. Biol. Chem. 283:20925-20936(2008) [PubMed: 18499658] [Abstract] Cited for: INTERACTION WITH DDX11.
[28]	"CDK inhibitor p21 is degraded by a proliferating cell nuclear antigen-coupled Cul4-DDB1Cdt2 pathway during S phase and after UV irradiation." Nishitani H., Shiomi Y., Iida H., Michishita M., Takami T., Tsurimoto T. J. Biol. Chem. 283:29045-29052(2008) [PubMed: 18703516] [Abstract] Cited for: INTERACTION WITH CDKN1A.
[29]	"Role of PCNA-dependent stimulation of 3'-phosphodiesterase and 3'-5' exonuclease activities of human Ape2 in repair of oxidative DNA damage." Burkovics P., Hajdu I., Szukacsov V., Unk I., Haracska L. Nucleic Acids Res. 37:4247-4255(2009) [PubMed: 19443450] [Abstract] Cited for: FUNCTION, INTERACTION WITH APEX2.
[30]	"Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination." Unk I., Hajdu I., Fatyol K., Hurwitz J., Yoon J.-H., Prakash L., Prakash S., Haracska L. Proc. Natl. Acad. Sci. U.S.A. 105:3768-3773(2008) [PubMed: 18316726] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH HLTF.
[31]	"Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks." 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. Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008) [PubMed: 18719106] [Abstract] Cited for: UBIQUITINATION, FUNCTION, INTERACTION WITH HLTF AND SHPRH, MUTAGENESIS OF LYS-164.
[32]	"Proliferating cell nuclear antigen is protected from degradation by forming a complex with MutT Homolog2." 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. J. Biol. Chem. 284:19310-19320(2009) [PubMed: 19419956] [Abstract] Cited for: INTERACTION WITH NUDT15, ACETYLATION.
[33]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-77; LYS-80 AND LYS-248, MASS SPECTROMETRY.
[34]	"CRL4(Cdt2) E3 ubiquitin ligase monoubiquitinates PCNA to promote translesion DNA synthesis." Terai K., Abbas T., Jazaeri A.A., Dutta A. Mol. Cell 37:143-149(2010) [PubMed: 20129063] [Abstract] Cited for: UBIQUITINATION, MUTAGENESIS OF LYS-164.
[35]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]	"Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA." Gulbis J.M., Kelman Z., Hurwitz J., O'Donnell M., Kuriyan J. Cell 87:297-306(1996) [PubMed: 8861913] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[37]	"Structural basis for recruitment of human flap endonuclease 1 to PCNA." Sakurai S., Kitano K., Yamaguchi H., Hamada K., Okada K., Fukuda K., Uchida M., Ohtsuka E., Morioka H., Hakoshima T. EMBO J. 24:683-693(2005) [PubMed: 15616578] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH FEN1.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Wikipedia

PCNA entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M15796 mRNA. Translation: AAA35736.1.
J04718 Genomic DNA. Translation: AAA60040.1.
AF527838 Genomic DNA. Translation: AAM78556.1.
AK313286 mRNA. Translation: BAG36094.1.
AL121924 Genomic DNA. Translation: CAC27344.1.
CH471133 Genomic DNA. Translation: EAX10428.1.
CH471133 Genomic DNA. Translation: EAX10429.1.
CH471133 Genomic DNA. Translation: EAX10430.1.
BC000491 mRNA. Translation: AAH00491.1.
BC062439 mRNA. Translation: AAH62439.1.

IPI

IPI00021700.

PIR

WMHUET. A27445.

RefSeq

NP_002583.1. NM_002592.2.
NP_872590.1. NM_182649.1.

UniGene

Hs.147433.
Hs.728886.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AXC	X-ray	2.60	A/C/E	1-261	[»]
1U76	X-ray	2.60	A/C/E	1-261	[»]
1U7B	X-ray	1.88	A	1-261	[»]
1UL1	X-ray	2.90	A/B/C	1-261	[»]
1VYJ	X-ray	2.80	A/C/E/G/I/K	1-261	[»]
1VYM	X-ray	2.30	A/B/C	1-261	[»]
1W60	X-ray	3.15	A/B	1-261	[»]
2ZVK	X-ray	2.70	A/B/C	1-261	[»]
2ZVL	X-ray	2.50	A/B/C/D/E/F	1-261	[»]
2ZVM	X-ray	2.30	A/B/C	1-261	[»]
3P87	X-ray	2.99	A/B/C/D/E/F	1-261	[»]

ProteinModelPortal

P12004.

SMR

P12004. Positions 1-255.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1098N.

IntAct

P12004. 22 interactions.

MINT

MINT-5000943.

STRING

P12004.

PTM databases

PhosphoSite

P12004.

Polymorphism databases

DMDM

129694.

2D gel databases

SWISS-2DPAGE

P12004.

Proteomic databases

PeptideAtlas

P12004.

PRIDE

P12004.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000379143; ENSP00000368438; ENSG00000132646.
ENST00000379160; ENSP00000368458; ENSG00000132646.

GeneID

5111.

KEGG

hsa:5111.

UCSC

uc002wlp.1. human.

Organism-specific databases

CTD

5111.

GeneCards

GC20M005095.

H-InvDB

HIX0015618.

HGNC

HGNC:8729. PCNA.

HPA

CAB000148.
HPA030521.
HPA030522.
HPA030523.

MIM

176740. gene.

neXtProt

NX_P12004.

PharmGKB

PA263.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG19692.

HOGENOM

HBG749295.

HOVERGEN

HBG000947.

InParanoid

P12004.

OMA

KAQDNAD.

OrthoDB

EOG4933JJ.

PhylomeDB

P12004.

Enzyme and pathway databases

Pathway_Interaction_DB

bard1pathway. BARD1 signaling events.

Reactome

REACT_152. Cell Cycle, Mitotic.
REACT_216. DNA Repair.
REACT_22172. Chromosome Maintenance.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpress

P12004.

Bgee

P12004.

CleanEx

HS_PCNA.

Genevestigator

P12004.

GermOnline

ENSG00000132646. Homo sapiens.

Family and domain databases

InterPro

IPR000730. Pr_cel_nuc_antig.
IPR022649. Pr_cel_nuc_antig_C.
IPR022659. Pr_cel_nuc_antig_CS.
IPR022648. Pr_cel_nuc_antig_N.
[Graphical view]

KO

K04802.

PANTHER

PTHR11352. Pr_cel_nuc_antig. 1 hit.

Pfam

PF02747. PCNA_C. 1 hit.
PF00705. PCNA_N. 1 hit.
[Graphical view]

PRINTS

PR00339. PCNACYCLIN.

TIGRFAMs

TIGR00590. Pcna. 1 hit.

PROSITE

PS01251. PCNA_1. 1 hit.
PS00293. PCNA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

19722.

SOURCE

Search...

Entry information

Entry name

PCNA_HUMAN

Accession

Primary (citable) accession number: P12004
Secondary accession number(s): B2R897, D3DW02

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	December 14, 2011
This is version 142 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.