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P15873 (PCNA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proliferating cell nuclear antigen

Short name=PCNA
Gene names
Name:POL30
Ordered Locus Names:YBR088C
ORF Names:YBR0811
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair. Ref.6 Ref.7

Subunit structure

Homotrimer. Interacts with RAD30 and MCM10. Ref.6 Ref.10

Subcellular location

Nucleus HAMAP-Rule MF_00317.

Post-translational modification

Sumoylated on Lys-164, and to a lesser extent on Lys-127 by the UBC9/SIZ1 complex during S-phase; which impairs ubiquitination and function in DNA repair. Ref.7

Monoubiquitinated on Lys-164 by the UBC2/RAD18 complex upon DNA damage, and then polyubiquitinated through 'Lys-63'-linkage by UBC13/MMS2. Ubiquitination is required for UBC2-mediated DNA repair. HAMAP-Rule MF_00317

Sequence similarities

Belongs to the PCNA family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
DNA replication
   Cellular componentNucleus
   LigandDNA-binding
   PTMIsopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin silencing at silent mating-type cassette

Inferred from mutant phenotype PubMed 16157874. Source: SGD

chromatin silencing at telomere

Inferred from mutant phenotype PubMed 16157874. Source: SGD

lagging strand elongation

Inferred from direct assay PubMed 7673186. Source: SGD

leading strand elongation

Inferred from direct assay PubMed 1682321. Source: SGD

meiotic mismatch repair

Inferred from mutant phenotype PubMed 18245822. Source: SGD

mismatch repair

Inferred from mutant phenotype PubMed 8858149. Source: SGD

mitotic sister chromatid cohesion

Inferred from genetic interaction PubMed 16934511. Source: SGD

nucleotide-excision repair

Inferred from mutant phenotype PubMed 9806417. Source: SGD

postreplication repair

Inferred from mutant phenotype PubMed 8790390. Source: SGD

regulation of DNA replication

Inferred from electronic annotation. Source: InterPro

   Cellular_componentPCNA complex

Traceable author statement PubMed 9745046. Source: SGD

nucleus

Inferred from direct assay PubMed 15282802. Source: SGD

replication fork

Traceable author statement PubMed 9759502. Source: SGD

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA polymerase processivity factor activity

Inferred from direct assay PubMed 18635534PubMed 2902631. Source: SGD

identical protein binding

Inferred from physical interaction Ref.6Ref.12. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 258258Proliferating cell nuclear antigen HAMAP-Rule MF_00317
PRO_0000149176

Regions

DNA binding61 – 8020 Potential

Amino acid modifications

Cross-link127Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.7 Ref.8
Cross-link164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.7 Ref.8 Ref.9
Cross-link164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate

Secondary structure

........................................................ 258
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15873 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 9B56C5851621DDDC

FASTA25828,916
        10         20         30         40         50         60 
MLEAKFEEAS LFKRIIDGFK DCVQLVNFQC KEDGIIAQAV DDSRVLLVSL EIGVEAFQEY 

        70         80         90        100        110        120 
RCDHPVTLGM DLTSLSKILR CGNNTDTLTL IADNTPDSII LLFEDTKKDR IAEYSLKLMD 

       130        140        150        160        170        180 
IDADFLKIEE LQYDSTLSLP SSEFSKIVRD LSQLSDSINI MITKETIKFV ADGDIGSGSV 

       190        200        210        220        230        240 
IIKPFVDMEH PETSIKLEMD QPVDLTFGAK YLLDIIKGSS LSDRVGIRLS SEAPALFQFD 

       250 
LKSGFLQFFL APKFNDEE 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, structure and expression of the yeast proliferating cell nuclear antigen gene."
Bauer G.A., Burgess P.M.J.
Nucleic Acids Res. 18:261-265(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-41 AND 231-240.
[2]"Analysis of a 70 kb region on the right arm of yeast chromosome II."
Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.
Yeast 10:1363-1381(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[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.
[7]"RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO."
Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S.
Nature 419:135-141(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUMOYLATION AT LYS-127 AND LYS-164, UBIQUITINATION AT LYS-164, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses."
Zhou W., Ryan J.J., Zhou H.
J. Biol. Chem. 279:32262-32268(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-127 AND LYS-164.
[9]"A proteomic strategy for gaining insights into protein sumoylation in yeast."
Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D., Gygi S.P.
Mol. Cell. Proteomics 4:246-254(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164.
Strain: EJY251-11b.
[10]"Interaction between PCNA and diubiquitinated Mcm10 is essential for cell growth in budding yeast."
Das-Bradoo S., Ricke R.M., Bielinsky A.-K.
Mol. Cell. Biol. 26:4806-4817(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MCM10.
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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).
[13]"Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex."
Bowman G.D., O'Donnell M., Kuriyan J.
Nature 429:724-730(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH RFC1; RCF2; RCF3; RCF4 AND RCF5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16676 Genomic DNA. Translation: CAA34664.1.
X78993 Genomic DNA. Translation: CAA55594.1.
Z35957 Genomic DNA. Translation: CAA85038.1.
AY557715 Genomic DNA. Translation: AAS56041.1.
BK006936 Genomic DNA. Translation: DAA07209.1.
PIRWMBYET. S22851.
RefSeqNP_009645.1. NM_001178436.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PLQX-ray2.30A1-258[»]
1PLRX-ray3.00A1-258[»]
1SXJX-ray2.85F/G/H1-258[»]
2OD8X-ray2.80A1-258[»]
3F1WX-ray2.90A1-258[»]
3GPMX-ray3.80A1-258[»]
3GPNX-ray2.50A1-258[»]
3L0WX-ray2.80A1-163[»]
3L0XX-ray3.00A1-163[»]
B165-258[»]
3L10X-ray2.80A1-163[»]
3PGEX-ray2.80A165-258[»]
B1-163[»]
3V60X-ray2.60B1-258[»]
3V61X-ray2.80B1-258[»]
3V62X-ray2.90B/E1-258[»]
4L60X-ray3.00A1-256[»]
ProteinModelPortalP15873.
SMRP15873. Positions 1-258.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32794. 222 interactions.
DIPDIP-2417N.
IntActP15873. 17 interactions.
MINTMINT-675752.
STRING4932.YBR088C.

Proteomic databases

PaxDbP15873.
PeptideAtlasP15873.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR088C; YBR088C; YBR088C.
GeneID852385.
KEGGsce:YBR088C.

Organism-specific databases

CYGDYBR088c.
SGDS000000292. POL30.

Phylogenomic databases

eggNOGCOG0592.
GeneTreeENSGT00390000004965.
HOGENOMHOG000211098.
KOK04802.
OMAYEMKLMN.
OrthoDBEOG7M3J9S.

Enzyme and pathway databases

BioCycYEAST:G3O-29055-MONOMER.

Gene expression databases

GenevestigatorP15873.

Family and domain databases

HAMAPMF_00317. DNApol_clamp_arch.
InterProIPR000730. Pr_cel_nuc_antig.
IPR022649. Pr_cel_nuc_antig_C.
IPR022659. Pr_cel_nuc_antig_CS.
IPR022648. Pr_cel_nuc_antig_N.
[Graphical view]
PANTHERPTHR11352. PTHR11352. 1 hit.
PfamPF02747. PCNA_C. 1 hit.
PF00705. PCNA_N. 1 hit.
[Graphical view]
PRINTSPR00339. PCNACYCLIN.
TIGRFAMsTIGR00590. pcna. 1 hit.
PROSITEPS01251. PCNA_1. 1 hit.
PS00293. PCNA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15873.
NextBio971192.
PROP15873.

Entry information

Entry namePCNA_YEAST
AccessionPrimary (citable) accession number: P15873
Secondary accession number(s): D6VQ89
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references