Proliferating cell nuclear antigen

<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

Regions

<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

• DNA binding Source: UniProtKB-KW
• DNA polymerase processivity factor activity Source: SGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "DNA polymerase delta is highly processive with proliferating cell nuclear antigen and undergoes collision release upon completing DNA."
    Langston L.D., O'Donnell M.
    J Biol Chem 283:29522-29531(2008) [PubMed] [Europe PMC] [Abstract]
  • "The yeast analog of mammalian cyclin/proliferating-cell nuclear antigen interacts with mammalian DNA polymerase delta."
    Bauer G.A., Burgers P.M.
    Proc Natl Acad Sci U S A 85:7506-7510(1988) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.6

    "Interaction with PCNA is essential for yeast DNA polymerase eta function."
    Haracska L., Kondratick C.M., Unk I., Prakash S., Prakash L.
    Mol. Cell 8:407-415(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH RAD30.
  • "The structure of a ring-opened proliferating cell nuclear antigen-replication factor C complex revealed by fluorescence energy transfer."
    Zhuang Z., Yoder B.L., Burgers P.M., Benkovic S.J.
    Proc Natl Acad Sci U S A 103:2546-2551(2006) [PubMed] [Europe PMC] [Abstract]
  • "Structure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchange."
    Freudenthal B.D., Gakhar L., Ramaswamy S., Washington M.T.
    Nat Struct Mol Biol 17:479-484(2010) [PubMed] [Europe PMC] [Abstract]
  • "Subtle alterations in PCNA-partner interactions severely impair DNA replication and repair."
    Fridman Y., Palgi N., Dovrat D., Ben-Aroya S., Hieter P., Aharoni A.
    PLoS Biol 8:e1000507-e1000507(2010) [PubMed] [Europe PMC] [Abstract]
  • "Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2."
    Armstrong A.A., Mohideen F., Lima C.D.
    Nature 483:59-63(2012) [PubMed] [Europe PMC] [Abstract]
  • Ref.13

    "Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA."
    Krishna T.S., Kong X.P., Gary S., Burgers P.M., Kuriyan J.
    Cell 79:1233-1243(1994) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

GO - Biological processⁱ

• chromatin silencing at telomere Source: SGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Rtt106p is a histone chaperone involved in heterochromatin-mediated silencing."
    Huang S., Zhou H., Katzmann D., Hochstrasser M., Atanasova E., Zhang Z.
    Proc. Natl. Acad. Sci. U.S.A. 102:13410-13415(2005) [PubMed] [Europe PMC] [Abstract]
• error-free translesion synthesis Source: SGD <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "PCNA monoubiquitylation and DNA polymerase eta ubiquitin-binding domain are required to prevent 8-oxoguanine-induced mutagenesis in Saccharomyces cerevisiae."
    van der Kemp P.A., de Padula M., Burguiere-Slezak G., Ulrich H.D., Boiteux S.
    Nucleic Acids Res 37:2549-2559(2009) [PubMed] [Europe PMC] [Abstract]
• establishment of mitotic sister chromatid cohesion Source: SGDInferred from genetic interactionⁱ
  • "PCNA controls establishment of sister chromatid cohesion during S phase."
    Moldovan G.L., Pfander B., Jentsch S.
    Mol Cell 23:723-732(2006) [PubMed] [Europe PMC] [Abstract]
• lagging strand elongation Source: SGDInferred from direct assayⁱ
  • "Lagging strand DNA synthesis at the eukaryotic replication fork involves binding and stimulation of FEN-1 by proliferating cell nuclear antigen."
    Li X., Li J., Harrington J., Lieber M.R., Burgers P.M.
    J Biol Chem 270:22109-22112(1995) [PubMed] [Europe PMC] [Abstract]
• leading strand elongation Source: SGDInferred from direct assayⁱ
  • "Saccharomyces cerevisiae replication factor C. I. Purification and characterization of its ATPase activity."
    Yoder B.L., Burgers P.M.
    J Biol Chem 266:22689-22697(1991) [PubMed] [Europe PMC] [Abstract]
• maintenance of DNA trinucleotide repeats Source: SGDInferred from mutant phenotypeⁱ
  • "Interactions among DNA ligase I, the flap endonuclease and proliferating cell nuclear antigen in the expansion and contraction of CAG repeat tracts in yeast."
    Refsland E.W., Livingston D.M.
    Genetics 171:923-934(2005) [PubMed] [Europe PMC] [Abstract]
• meiotic mismatch repair Source: SGDInferred from mutant phenotypeⁱ
  • "Role of proliferating cell nuclear antigen interactions in the mismatch repair-dependent processing of mitotic and meiotic recombination intermediates in yeast."
    Stone J.E., Ozbirn R.G., Petes T.D., Jinks-Robertson S.
    Genetics 178:1221-1236(2008) [PubMed] [Europe PMC] [Abstract]
• mismatch repair Source: SGDInferred from mutant phenotypeⁱ
  • "Requirement for PCNA in DNA mismatch repair at a step preceding DNA resynthesis."
    Umar A., Buermeyer A.B., Simon J.A., Thomas D.C., Clark A.B., Liskay R.M., Kunkel T.A.
    Cell 87:65-73(1996) [PubMed] [Europe PMC] [Abstract]
• mitotic cell cycle Source: SGDInferred from genetic interactionⁱ
  • "Proliferating cell nuclear antigen (pol30) mutations suppress cdc44 mutations and identify potential regions of interaction between the two encoded proteins."
    McAlear M.A., Howell E.A., Espenshade K.K., Holm C.
    Mol Cell Biol 14:4390-4397(1994) [PubMed] [Europe PMC] [Abstract]
• mitotic sister chromatid cohesion Source: SGDInferred from genetic interactionⁱ
  • "PCNA controls establishment of sister chromatid cohesion during S phase."
    Moldovan G.L., Pfander B., Jentsch S.
    Mol Cell 23:723-732(2006) [PubMed] [Europe PMC] [Abstract]
• nucleotide-excision repair Source: SGDInferred from mutant phenotypeⁱ
  • "The N-degron protein degradation strategy for investigating the function of essential genes: requirement for replication protein A and proliferating cell nuclear antigen proteins for nucleotide excision repair in yeast extracts."
    Huang W., Feaver W.J., Tomkinson A.E., Friedberg E.C.
    Mutat Res 408:183-194(1998) [PubMed] [Europe PMC] [Abstract]
• positive regulation of exodeoxyribonuclease activity Source: SGDInferred from direct assayⁱ
  • "Stimulation of 3'-->5' exonuclease and 3'-phosphodiesterase activities of yeast apn2 by proliferating cell nuclear antigen."
    Unk I., Haracska L., Gomes X.V., Burgers P.M., Prakash L., Prakash S.
    Mol Cell Biol 22:6480-6486(2002) [PubMed] [Europe PMC] [Abstract]
• positive regulation of exonuclease activity Source: SGDInferred from direct assayⁱ
  • "Apn2 resolves blocked 3' ends and suppresses Top1-induced mutagenesis at genomic rNMP sites."
    Li F., Wang Q., Seol J.H., Che J., Lu X., Shim E.Y., Lee S.E., Niu H.
    Nat Struct Mol Biol 26:155-163(2019) [PubMed] [Europe PMC] [Abstract]
• positive regulation of phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands Source: SGDInferred from direct assayⁱ
  • "Stimulation of 3'-->5' exonuclease and 3'-phosphodiesterase activities of yeast apn2 by proliferating cell nuclear antigen."
    Unk I., Haracska L., Gomes X.V., Burgers P.M., Prakash L., Prakash S.
    Mol Cell Biol 22:6480-6486(2002) [PubMed] [Europe PMC] [Abstract]
• postreplication repair Source: SGDInferred from mutant phenotypeⁱ
  • "Requirement of proliferating cell nuclear antigen in RAD6-dependent postreplicational DNA repair."
    Torres-Ramos C.A., Yoder B.L., Burgers P.M., Prakash S., Prakash L.
    Proc Natl Acad Sci U S A 93:9676-9681(1996) [PubMed] [Europe PMC] [Abstract]
• regulation of DNA replication Source: InterPro
• silent mating-type cassette heterochromatin assembly Source: SGDInferred from mutant phenotypeⁱ
  • "Rtt106p is a histone chaperone involved in heterochromatin-mediated silencing."
    Huang S., Zhou H., Katzmann D., Hochstrasser M., Atanasova E., Zhang Z.
    Proc. Natl. Acad. Sci. U.S.A. 102:13410-13415(2005) [PubMed] [Europe PMC] [Abstract]
• translesion synthesis Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

<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

Enzyme and pathway databases

<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

Organism-specific databases

<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

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

<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

Amino acid modifications

<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

Keywords - PTMⁱ

Proteomic databases

PTM databases

<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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• identical protein binding Source: IntActInferred from physical interactionⁱ
  • Ref.6

    "Interaction with PCNA is essential for yeast DNA polymerase eta function."
    Haracska L., Kondratick C.M., Unk I., Prakash S., Prakash L.
    Mol. Cell 8:407-415(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH RAD30.
  • "The structure of a ring-opened proliferating cell nuclear antigen-replication factor C complex revealed by fluorescence energy transfer."
    Zhuang Z., Yoder B.L., Burgers P.M., Benkovic S.J.
    Proc Natl Acad Sci U S A 103:2546-2551(2006) [PubMed] [Europe PMC] [Abstract]
  • "Structure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchange."
    Freudenthal B.D., Gakhar L., Ramaswamy S., Washington M.T.
    Nat Struct Mol Biol 17:479-484(2010) [PubMed] [Europe PMC] [Abstract]
  • "Subtle alterations in PCNA-partner interactions severely impair DNA replication and repair."
    Fridman Y., Palgi N., Dovrat D., Ben-Aroya S., Hieter P., Aharoni A.
    PLoS Biol 8:e1000507-e1000507(2010) [PubMed] [Europe PMC] [Abstract]
  • "Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2."
    Armstrong A.A., Mohideen F., Lima C.D.
    Nature 483:59-63(2012) [PubMed] [Europe PMC] [Abstract]
  • Ref.13

    "Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA."
    Krishna T.S., Kong X.P., Gary S., Burgers P.M., Kuriyan J.
    Cell 79:1233-1243(1994) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Protein-protein interaction databases

Miscellaneous databases

<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

3D structure databases

Miscellaneous databases

<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

Phylogenomic databases

Family and domain databases

<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.

        10         20         30         40         50
MLEAKFEEAS LFKRIIDGFK DCVQLVNFQC KEDGIIAQAV DDSRVLLVSL 
        60         70         80         90        100
EIGVEAFQEY RCDHPVTLGM DLTSLSKILR CGNNTDTLTL IADNTPDSII 
       110        120        130        140        150
LLFEDTKKDR IAEYSLKLMD IDADFLKIEE LQYDSTLSLP SSEFSKIVRD 
       160        170        180        190        200
LSQLSDSINI MITKETIKFV ADGDIGSGSV IIKPFVDMEH PETSIKLEMD 
       210        220        230        240        250
QPVDLTFGAK YLLDIIKGSS LSDRVGIRLS SEAPALFQFD LKSGFLQFFL 

APKFNDEE                                               

Sequence databases

Genome annotation databases

<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

• 100% Identity
• 90% Identity
• 50% Identity

<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

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

1. Yeast
   Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
2. Yeast chromosome II
   Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names
3. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
4. SIMILARITY comments
   Index of protein domains and families