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Entry version 166 (03 Jul 2019)
Sequence version 1 (13 Aug 1987)
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Protein

Proliferating cell nuclear antigen

Gene

Pcna

Organism
Rattus norvegicus (Rat)
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. 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 (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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

<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 3

Organism-specific databases

Rat genome database

More...
RGDi
3269 Pcna

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<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_00001491611 – 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-acetyllysineBy similarity1
Modified residuei77N6-acetyllysineBy similarity1
Modified residuei80N6-acetyllysineBy similarity1
<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); alternateBy similarity
Cross-linki164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei211Phosphotyrosine; by EGFRBy similarity1
Modified residuei248N6-acetyllysineBy similarity1
Cross-linki254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

<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 (By similarity).By similarity
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. 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. Acetylation disrupts interaction with NUDT15 and promotes degradation (By similarity).By similarity
Ubiquitinated. 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 (By similarity).By similarity
Methylated on glutamate residues by ARMT1.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P04961

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

More...
PaxDbi
P04961

PRoteomics IDEntifications database

More...
PRIDEi
P04961

PTM databases

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

More...
PhosphoSitePlusi
P04961

<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

More...
Bgeei
ENSRNOG00000021264 Expressed in 9 organ(s), highest expression level in colon

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P04961 RN

<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.

Interacts with p300/EP300; the interaction occurs on chromatin in UV-irradiated damaged cells.

Interacts with CREBBP (via transactivation domain and C-terminus); the interaction occurs on chromatin in UV-irradiated damaged cells. 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).

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 (By similarity).

Interacts with KCTD10 (PubMed:15982757).

Interacts with PPP1R15A (By similarity). Directly interacts with BAZ1B.

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. The interaction with CDKN1A inhibits POLD3 binding.

Interacts with DDX11.

Interacts with EGFR; positively regulates PCNA.

Interacts with PARPBP.

Interacts (when ubiquitinated) with SPRTN; leading to enhance RAD18-mediated PCNA ubiquitination.

Interacts (when polyubiquitinated) with ZRANB3.

Interacts with SMARCAD1.

Interacts with CDKN1C.

Interacts with PCLAF (via PIP-box).

Interacts with RTEL1 (via PIP-box); the interaction is direct and essential for the suppression of telomere fragility.

Interacts with FAM111A (via PIP-box); the interaction is direct and required for PCNA loading on chromatin binding.

Interacts with LIG1.

Interacts with SETMAR.

Interacts with ANKRD17.

Interacts with FBXO18/FBH1 (via PIP-box); the interaction recruits the DCX(DTL) complex and promotes ubiquitination and degradation of FBXO18/FBH1.

Interacts with POLN (By similarity).

Interacts with SDE2 (via PIP-box); the interaction is direct and prevents ultraviolet light induced monoubiquitination (By similarity).

Component of the replisome complex composed of at least DONSON, MCM2, MCM7, PCNA and TICRR; interaction at least with PCNA occurs during DNA replication (By similarity).

Interacts with MAPK15; the interaction is chromatin binding dependent and prevents MDM2-mediated PCNA destruction by inhibiting the association of PCNA with MDM2.

Interacts with PARP10 (via PIP-box) (By similarity).

Interacts with DDI2 (By similarity).

Interacts with HMCES (via PIP-box) (By similarity).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
247765, 6 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-542 PCNA homotrimer

Protein interaction database and analysis system

More...
IntActi
P04961, 2 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000028887

<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

3D structure databases

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

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SMRi
P04961

Database of comparative protein structure models

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ModBasei
Search...

<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

<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

More...
HOGENOMi
HOG000211098

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P04961

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
1012066at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P04961

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

More...
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

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00339 PCNACYCLIN

TIGRFAMs; a protein family database

More...
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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

P04961-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFEARLIQGS ILKKVLEALK DLINEACWDI SSGGVNLQSM 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 EEEAVSIEMN
210 220 230 240 250
EPVQLTFALR YLNFFTKATP LSPTVTLSMS ADVPLVVEYK IADMGHLKYY
260
LAPKIEDEEG S
Length:261
Mass (Da):28,749
Last modified:August 13, 1987 - 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:iCE55E9BA46C50F07
GO

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
Y00047 mRNA Translation: CAA68261.1
BC060570 mRNA Translation: AAH60570.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A26631 WMRTET

NCBI Reference Sequences

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RefSeqi
NP_071776.1, NM_022381.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000028887; ENSRNOP00000028887; ENSRNOG00000021264

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
25737

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:25737

UCSC genome browser

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UCSCi
RGD:3269 rat

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00047 mRNA Translation: CAA68261.1
BC060570 mRNA Translation: AAH60570.1
PIRiA26631 WMRTET
RefSeqiNP_071776.1, NM_022381.3

3D structure databases

SMRiP04961
ModBaseiSearch...

Protein-protein interaction databases

BioGridi247765, 6 interactors
ComplexPortaliCPX-542 PCNA homotrimer
IntActiP04961, 2 interactors
STRINGi10116.ENSRNOP00000028887

PTM databases

PhosphoSitePlusiP04961

Proteomic databases

jPOSTiP04961
PaxDbiP04961
PRIDEiP04961

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000028887; ENSRNOP00000028887; ENSRNOG00000021264
GeneIDi25737
KEGGirno:25737
UCSCiRGD:3269 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5111
RGDi3269 Pcna

Phylogenomic databases

eggNOGiKOG1636 Eukaryota
COG0592 LUCA
GeneTreeiENSGT00390000004965
HOGENOMiHOG000211098
InParanoidiP04961
KOiK04802
OMAiKILRCAG
OrthoDBi1012066at2759
PhylomeDBiP04961
TreeFamiTF313441

Enzyme and pathway databases

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

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P04961

Gene expression databases

BgeeiENSRNOG00000021264 Expressed in 9 organ(s), highest expression level in colon
GenevisibleiP04961 RN

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
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

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_RAT
<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: P04961
<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: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 3, 2019
This is version 166 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

<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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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