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Protein

Proliferating cell nuclear antigen

Gene

PCNA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.3 Publications

Miscellaneous

Antibodies against PCNA are present in sera from patients with systemic lupus erythematosus.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi61 – 80Sequence analysisAdd BLAST20

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding
Biological processDNA damage, DNA repair, DNA replication, Host-virus interaction

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-110312 Translesion synthesis by REV1
R-HSA-110314 Recognition of DNA damage by PCNA-containing replication complex
R-HSA-110320 Translesion Synthesis by POLH
R-HSA-1362277 Transcription of E2F targets under negative control by DREAM complex
R-HSA-174411 Polymerase switching on the C-strand of the telomere
R-HSA-174414 Processive synthesis on the C-strand of the telomere
R-HSA-174417 Telomere C-strand (Lagging Strand) Synthesis
R-HSA-174437 Removal of the Flap Intermediate from the C-strand
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-HSA-5358606 Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)
R-HSA-539107 Activation of E2F1 target genes at G1/S
R-HSA-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-HSA-5655862 Translesion synthesis by POLK
R-HSA-5656121 Translesion synthesis by POLI
R-HSA-5656169 Termination of translesion DNA synthesis
R-HSA-5685942 HDR through Homologous Recombination (HRR)
R-HSA-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER
R-HSA-5696400 Dual Incision in GG-NER
R-HSA-6782135 Dual incision in TC-NER
R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-6804114 TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest
R-HSA-69091 Polymerase switching
R-HSA-69166 Removal of the Flap Intermediate
R-HSA-69183 Processive synthesis on the lagging strand
R-HSA-8866654 E3 ubiquitin ligases ubiquitinate target proteins

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P12004

SIGNOR Signaling Network Open Resource

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SIGNORi
P12004

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P12004 Predicted

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Proliferating cell nuclear antigen
Short name:
PCNA
Alternative name(s):
Cyclin
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PCNA
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 20

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000132646.10

Human Gene Nomenclature Database

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HGNCi
HGNC:8729 PCNA

Online Mendelian Inheritance in Man (OMIM)

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MIMi
176740 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P12004

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Ataxia-telangiectasia-like disorder 2 (ATLD2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:615919
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071871228S → I in ATLD2; a hypomorphic mutation affecting DNA repair in response to UV; results in significantly decreased interaction with FEN1, LIG1 and ERCC5. 1 PublicationCorresponds to variant dbSNP:rs369958038EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi13K → 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. 1 Publication1
Mutagenesisi14K → 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. 1 Publication1
Mutagenesisi20K → 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. 1 Publication1
Mutagenesisi43 – 45SHV → AAA: No effect on POLD3-binding. 1 Publication3
Mutagenesisi77K → A: Inhibits recruitment to DNA damage sites, but nuclear localization is similar as the wild-type; in association with A-80. 1 Publication1
Mutagenesisi77K → 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. 1 Publication1
Mutagenesisi80K → A: Inhibits recruitment to DNA damage sites, but nuclear localization is similar as the wild-type; in association with A-77. 1 Publication1
Mutagenesisi80K → 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. 1 Publication1
Mutagenesisi125 – 128QLGI → AAAA: Strong decrease in POLD3-binding. 1 Publication4
Mutagenesisi164K → R: Abolishes ubiquitination. No effect on interaction with SHPRH. 4 Publications1
Mutagenesisi188 – 190VDK → AAA: No effect on POLD3-binding. 1 Publication3
Mutagenesisi211Y → F: Alters chromatin-associated PCNA stability and its function in DNA replication and repair. 1 Publication1
Mutagenesisi251 – 254LAPK → AAAA: Decrease in POLD3-binding. 1 Publication4

Keywords - Diseasei

Deafness, Disease mutation, Dwarfism, Neurodegeneration

Organism-specific databases

DisGeNET

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DisGeNETi
5111

MalaCards human disease database

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MalaCardsi
PCNA
MIMi615919 phenotype

Open Targets

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OpenTargetsi
ENSG00000132646

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
438134 PCNA-related progressive neurodegenerative photosensitivity syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA263

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2346488

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PCNA

Domain mapping of disease mutations (DMDM)

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DMDMi
129694

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001491581 – 261Proliferating cell nuclear antigenAdd BLAST261

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei14N6-acetyllysine1 Publication1
Modified residuei77N6-acetyllysineCombined sources1
Modified residuei80N6-acetyllysineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate2 Publications
Modified residuei211Phosphotyrosine; by EGFR1 Publication1
Modified residuei248N6-acetyllysineCombined sources1
Cross-linki254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes chromatin-associated PCNA.1 Publication
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).1 Publication
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.10 Publications
Methylated on glutamate residues by ARMT1/C6orf211.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P12004

MaxQB - The MaxQuant DataBase

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MaxQBi
P12004

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P12004

PeptideAtlas

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PeptideAtlasi
P12004

PRoteomics IDEntifications database

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PRIDEi
P12004

ProteomicsDB human proteome resource

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ProteomicsDBi
52816

Consortium for Top Down Proteomics

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TopDownProteomicsi
P12004

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P12004

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P12004

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P12004

SwissPalm database of S-palmitoylation events

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SwissPalmi
P12004

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000132646 Expressed in 228 organ(s), highest expression level in oocyte

CleanEx database of gene expression profiles

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CleanExi
HS_PCNA

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P12004 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB000148
HPA030521
HPA030522
HPA030523

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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). Interacts with SDE2 (via PIP-box); the interaction is direct and prevents ultraviolet light induced monoubiquitination (PubMed:27906959). Component of the replisome complex composed of at least DONSON, MCM2, MCM7, PCNA and TICRR; interaction at least with PCNA occurs during DNA replication (PubMed:28191891). Interacts with MAPK15; the interaction is chromatin binding dependent and prevents MDM2-mediated PCNA destruction by inhibiting the association of PCNA with MDM2 (PubMed:20733054).By similarity44 Publications
(Microbial infection) Interacts with herpes virus 8 protein LANA1.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111142, 301 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-538 PCNA homotrimer

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P12004

Database of interacting proteins

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DIPi
DIP-1098N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P12004

Protein interaction database and analysis system

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IntActi
P12004, 120 interactors

Molecular INTeraction database

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MINTi
P12004

STRING: functional protein association networks

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STRINGi
9606.ENSP00000368438

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P12004

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1261
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P12004

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P12004

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P12004

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni7 – 100Interaction with NUDT151 PublicationAdd BLAST94

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the PCNA family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1636 Eukaryota
COG0592 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000004965

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000211098

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000947

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P12004

KEGG Orthology (KO)

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KOi
K04802

Identification of Orthologs from Complete Genome Data

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OMAi
KILRCAG

Database of Orthologous Groups

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OrthoDBi
EOG091G0GQ7

Database for complete collections of gene phylogenies

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PhylomeDBi
P12004

TreeFam database of animal gene trees

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TreeFami
TF313441

Family and domain databases

HAMAP database of protein families

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HAMAPi
MF_00317 DNApol_clamp_arch, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000730 Pr_cel_nuc_antig
IPR022649 Pr_cel_nuc_antig_C
IPR022659 Pr_cel_nuc_antig_CS
IPR022648 Pr_cel_nuc_antig_N

The PANTHER Classification System

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PANTHERi
PTHR11352:SF0 PTHR11352:SF0, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02747 PCNA_C, 1 hit
PF00705 PCNA_N, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00339 PCNACYCLIN

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00590 pcna, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS01251 PCNA_1, 1 hit
PS00293 PCNA_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P12004-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFEARLVQGS ILKKVLEALK DLINEACWDI SSSGVNLQSM DSSHVSLVQL
60 70 80 90 100
TLRSEGFDTY RCDRNLAMGV NLTSMSKILK CAGNEDIITL RAEDNADTLA
110 120 130 140 150
LVFEAPNQEK VSDYEMKLMD LDVEQLGIPE QEYSCVVKMP SGEFARICRD
160 170 180 190 200
LSHIGDAVVI SCAKDGVKFS ASGELGNGNI KLSQTSNVDK EEEAVTIEMN
210 220 230 240 250
EPVQLTFALR YLNFFTKATP LSSTVTLSMS ADVPLVVEYK IADMGHLKYY
260
LAPKIEDEEG S
Length:261
Mass (Da):28,769
Last modified:October 1, 1989 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE6F08E7EDBC48B00
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071871228S → I in ATLD2; a hypomorphic mutation affecting DNA repair in response to UV; results in significantly decreased interaction with FEN1, LIG1 and ERCC5. 1 PublicationCorresponds to variant dbSNP:rs369958038EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
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 No translation available.
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

The Consensus CDS (CCDS) project

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CCDSi
CCDS13087.1

Protein sequence database of the Protein Information Resource

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PIRi
A27445 WMHUET

NCBI Reference Sequences

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RefSeqi
NP_002583.1, NM_002592.2
NP_872590.1, NM_182649.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.147433
Hs.744934

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000379143; ENSP00000368438; ENSG00000132646
ENST00000379160; ENSP00000368458; ENSG00000132646

Database of genes from NCBI RefSeq genomes

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GeneIDi
5111

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:5111

UCSC genome browser

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UCSCi
uc002wlp.4 human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs
Wikipedia

PCNA entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 No translation available.
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
CCDSiCCDS13087.1
PIRiA27445 WMHUET
RefSeqiNP_002583.1, NM_002592.2
NP_872590.1, NM_182649.1
UniGeneiHs.147433
Hs.744934

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AXCX-ray2.60A/C/E1-261[»]
1U76X-ray2.60A/C/E1-261[»]
1U7BX-ray1.88A1-261[»]
1UL1X-ray2.90A/B/C1-261[»]
1VYJX-ray2.80A/C/E/G/I/K1-261[»]
1VYMX-ray2.30A/B/C1-261[»]
1W60X-ray3.15A/B1-261[»]
2ZVKX-ray2.70A/B/C1-261[»]
2ZVLX-ray2.50A/B/C/D/E/F1-261[»]
2ZVMX-ray2.30A/B/C1-261[»]
3JA9electron microscopy22.00A/B/C1-261[»]
3P87X-ray2.99A/B/C/D/E/F1-261[»]
3TBLX-ray2.90A/B/C1-261[»]
3VKXX-ray2.10A1-261[»]
3WGWX-ray2.80A/B1-261[»]
4D2GX-ray2.65A/B/C1-261[»]
4RJFX-ray2.01A/C/E1-261[»]
4ZTDX-ray2.20A/B/C2-254[»]
5E0TX-ray2.67A/B/C1-261[»]
5E0UX-ray1.93A/B/C1-261[»]
5E0VX-ray2.07A/B1-261[»]
5IY4X-ray2.94A/C/E1-261[»]
5MAVX-ray2.58A/B/C/D/E/F1-261[»]
5MLOX-ray1.96A/C/E1-261[»]
5MLWX-ray2.45A/C/E1-261[»]
5MOMX-ray2.27A/B/C1-258[»]
5YCOX-ray2.20A/B/C/D1-261[»]
5YD8X-ray2.30X/Y/Z1-261[»]
6CBIX-ray2.75A/B/C/D/E/F1-261[»]
6EHTX-ray3.20A/B1-254[»]
C1-255[»]
6GISX-ray2.82A/B/C1-261[»]
6GWSX-ray2.90A/B/C1-261[»]
ProteinModelPortaliP12004
SMRiP12004
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111142, 301 interactors
ComplexPortaliCPX-538 PCNA homotrimer
CORUMiP12004
DIPiDIP-1098N
ELMiP12004
IntActiP12004, 120 interactors
MINTiP12004
STRINGi9606.ENSP00000368438

Chemistry databases

BindingDBiP12004
ChEMBLiCHEMBL2346488

Protein family/group databases

MoonDBiP12004 Predicted

PTM databases

iPTMnetiP12004
PhosphoSitePlusiP12004
SwissPalmiP12004

Polymorphism and mutation databases

BioMutaiPCNA
DMDMi129694

2D gel databases

SWISS-2DPAGEiP12004

Proteomic databases

EPDiP12004
MaxQBiP12004
PaxDbiP12004
PeptideAtlasiP12004
PRIDEiP12004
ProteomicsDBi52816
TopDownProteomicsiP12004

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5111
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379143; ENSP00000368438; ENSG00000132646
ENST00000379160; ENSP00000368458; ENSG00000132646
GeneIDi5111
KEGGihsa:5111
UCSCiuc002wlp.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5111
DisGeNETi5111
EuPathDBiHostDB:ENSG00000132646.10

GeneCards: human genes, protein and diseases

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GeneCardsi
PCNA
HGNCiHGNC:8729 PCNA
HPAiCAB000148
HPA030521
HPA030522
HPA030523
MalaCardsiPCNA
MIMi176740 gene
615919 phenotype
neXtProtiNX_P12004
OpenTargetsiENSG00000132646
Orphaneti438134 PCNA-related progressive neurodegenerative photosensitivity syndrome
PharmGKBiPA263

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1636 Eukaryota
COG0592 LUCA
GeneTreeiENSGT00390000004965
HOGENOMiHOG000211098
HOVERGENiHBG000947
InParanoidiP12004
KOiK04802
OMAiKILRCAG
OrthoDBiEOG091G0GQ7
PhylomeDBiP12004
TreeFamiTF313441

Enzyme and pathway databases

ReactomeiR-HSA-110312 Translesion synthesis by REV1
R-HSA-110314 Recognition of DNA damage by PCNA-containing replication complex
R-HSA-110320 Translesion Synthesis by POLH
R-HSA-1362277 Transcription of E2F targets under negative control by DREAM complex
R-HSA-174411 Polymerase switching on the C-strand of the telomere
R-HSA-174414 Processive synthesis on the C-strand of the telomere
R-HSA-174417 Telomere C-strand (Lagging Strand) Synthesis
R-HSA-174437 Removal of the Flap Intermediate from the C-strand
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-HSA-5358606 Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)
R-HSA-539107 Activation of E2F1 target genes at G1/S
R-HSA-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-HSA-5655862 Translesion synthesis by POLK
R-HSA-5656121 Translesion synthesis by POLI
R-HSA-5656169 Termination of translesion DNA synthesis
R-HSA-5685942 HDR through Homologous Recombination (HRR)
R-HSA-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER
R-HSA-5696400 Dual Incision in GG-NER
R-HSA-6782135 Dual incision in TC-NER
R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-6804114 TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest
R-HSA-69091 Polymerase switching
R-HSA-69166 Removal of the Flap Intermediate
R-HSA-69183 Processive synthesis on the lagging strand
R-HSA-8866654 E3 ubiquitin ligases ubiquitinate target proteins
SignaLinkiP12004
SIGNORiP12004

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
PCNA human
EvolutionaryTraceiP12004

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Proliferating_cell_nuclear_antigen

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
5111

Protein Ontology

More...
PROi
PR:P12004

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000132646 Expressed in 228 organ(s), highest expression level in oocyte
CleanExiHS_PCNA
GenevisibleiP12004 HS

Family and domain databases

HAMAPiMF_00317 DNApol_clamp_arch, 1 hit
InterProiView protein in InterPro
IPR000730 Pr_cel_nuc_antig
IPR022649 Pr_cel_nuc_antig_C
IPR022659 Pr_cel_nuc_antig_CS
IPR022648 Pr_cel_nuc_antig_N
PANTHERiPTHR11352:SF0 PTHR11352:SF0, 1 hit
PfamiView protein in Pfam
PF02747 PCNA_C, 1 hit
PF00705 PCNA_N, 1 hit
PRINTSiPR00339 PCNACYCLIN
TIGRFAMsiTIGR00590 pcna, 1 hit
PROSITEiView protein in PROSITE
PS01251 PCNA_1, 1 hit
PS00293 PCNA_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPCNA_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P12004
Secondary accession number(s): B2R897, D3DW02
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: December 5, 2018
This is version 218 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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