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Entry version 124 (02 Dec 2020)
Sequence version 1 (27 Sep 2005)
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Protein

Proliferating cell nuclear antigen

Gene

PCNA

Organism
Bos taurus (Bovine)
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 transcript 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%5Fsection">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-BTA-110312, Translesion synthesis by REV1
R-BTA-110314, Recognition of DNA damage by PCNA-containing replication complex
R-BTA-110320, Translesion Synthesis by POLH
R-BTA-174411, Polymerase switching on the C-strand of the telomere
R-BTA-174414, Processive synthesis on the C-strand of the telomere
R-BTA-174417, Telomere C-strand (Lagging Strand) Synthesis
R-BTA-174437, Removal of the Flap Intermediate from the C-strand
R-BTA-4615885, SUMOylation of DNA replication proteins
R-BTA-5358565, Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-BTA-5651801, PCNA-Dependent Long Patch Base Excision Repair
R-BTA-5655862, Translesion synthesis by POLK
R-BTA-5656121, Translesion synthesis by POLI
R-BTA-5656169, Termination of translesion DNA synthesis
R-BTA-5685942, HDR through Homologous Recombination (HRR)
R-BTA-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER
R-BTA-5696400, Dual Incision in GG-NER
R-BTA-6782135, Dual incision in TC-NER
R-BTA-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-BTA-6804114, TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest
R-BTA-69091, Polymerase switching
R-BTA-69166, Removal of the Flap Intermediate
R-BTA-69183, Processive synthesis on the lagging strand
R-BTA-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%5Fand%5Ftaxonomy%5Fsection">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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 13

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:32635, 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002849171 – 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%5Fprocessing%5Fsection">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%5Fprocessing%5Fsection">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

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

More...
PaxDbi
Q3ZBW4

PRoteomics IDEntifications database

More...
PRIDEi
Q3ZBW4

<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
ENSBTAG00000006065, Expressed in spermatid and 19 other tissues

<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%5Fsection">'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%5Fsection">'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 and PPP1R15A (By similarity). Directly interacts with BAZ1B.

Interacts with HLTF and SHPRH.

Interacts with NUDT15; this 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).

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

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
172122, 12 interactors

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000007967

<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

More...
SMRi
Q3ZBW4

Database of comparative protein structure models

More...
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

More...
eggNOGi
KOG1636, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000004965

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_043978_3_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q3ZBW4

Identification of Orthologs from Complete Genome Data

More...
OMAi
EMKLINM

Database of Orthologous Groups

More...
OrthoDBi
1012066at2759

TreeFam database of animal gene trees

More...
TreeFami
TF313441

Family and domain databases

HAMAP database of protein families

More...
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

More...
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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q3ZBW4-1 [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 EEEAVAIEMN
210 220 230 240 250
EPVQLTFALR YLNFFTKATP LSPTVTLSMS ADVPLVVEYK IADMGHLKYY
260
LAPKIEDEEG S
Length:261
Mass (Da):28,749
Last modified:September 27, 2005 - 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:iD9D3E20EC7A8F9FD
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
BC103068 mRNA Translation: AAI03069.1

NCBI Reference Sequences

More...
RefSeqi
NP_001029666.1, NM_001034494.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSBTAT00000007967; ENSBTAP00000007967; ENSBTAG00000006065

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
515499

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:515499

<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
BC103068 mRNA Translation: AAI03069.1
RefSeqiNP_001029666.1, NM_001034494.1

3D structure databases

SMRiQ3ZBW4
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi172122, 12 interactors
STRINGi9913.ENSBTAP00000007967

Proteomic databases

PaxDbiQ3ZBW4
PRIDEiQ3ZBW4

Genome annotation databases

EnsembliENSBTAT00000007967; ENSBTAP00000007967; ENSBTAG00000006065
GeneIDi515499
KEGGibta:515499

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5111
VGNCiVGNC:32635, PCNA

Phylogenomic databases

eggNOGiKOG1636, Eukaryota
GeneTreeiENSGT00390000004965
HOGENOMiCLU_043978_3_0_1
InParanoidiQ3ZBW4
OMAiEMKLINM
OrthoDBi1012066at2759
TreeFamiTF313441

Enzyme and pathway databases

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

Gene expression databases

BgeeiENSBTAG00000006065, Expressed in spermatid and 19 other tissues

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

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_BOVIN
<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: Q3ZBW4
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: September 27, 2005
Last modified: December 2, 2020
This is version 124 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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