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P15873

- PCNA_YEAST

UniProt

P15873 - PCNA_YEAST

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Protein

Proliferating cell nuclear antigen

Gene

POL30

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi61 – 8020Sequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. DNA polymerase processivity factor activity Source: SGD
  3. identical protein binding Source: IntAct

GO - Biological processi

  1. chromatin silencing at silent mating-type cassette Source: SGD
  2. chromatin silencing at telomere Source: SGD
  3. error-free translesion synthesis Source: SGD
  4. establishment of mitotic sister chromatid cohesion Source: SGD
  5. lagging strand elongation Source: SGD
  6. leading strand elongation Source: SGD
  7. maintenance of DNA trinucleotide repeats Source: SGD
  8. meiotic mismatch repair Source: SGD
  9. mismatch repair Source: SGD
  10. mitotic cell cycle Source: SGD
  11. mitotic sister chromatid cohesion Source: SGD
  12. nucleotide-excision repair Source: SGD
  13. positive regulation of exodeoxyribonuclease activity Source: SGD
  14. positive regulation of phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands Source: SGD
  15. postreplication repair Source: SGD
  16. regulation of DNA replication Source: InterPro
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, DNA replication

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29055-MONOMER.
ReactomeiREACT_189247. G1/S-Specific Transcription.

Names & Taxonomyi

Protein namesi
Recommended name:
Proliferating cell nuclear antigen
Short name:
PCNA
Gene namesi
Name:POL30
Ordered Locus Names:YBR088C
ORF Names:YBR0811
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

CYGDiYBR088c.
SGDiS000000292. POL30.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: SGD
  2. PCNA complex Source: SGD
  3. replication fork Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 258258Proliferating cell nuclear antigenPRO_0000149176Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki127 – 127Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki164 – 164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki164 – 164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication

Post-translational modificationi

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.3 Publications
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.1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP15873.
PaxDbiP15873.
PeptideAtlasiP15873.

Expressioni

Gene expression databases

GenevestigatoriP15873.

Interactioni

Subunit structurei

Homotrimer. Interacts with RAD30 and MCM10.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-12993,EBI-12993
ELG1Q120509EBI-12993,EBI-32195
MCM10P323544EBI-12993,EBI-5965
RAD27P267933EBI-12993,EBI-14693
RAD30Q040493EBI-12993,EBI-36214
SMT3Q123066EBI-12993,EBI-17490
SRS2P1295410EBI-12993,EBI-18110

Protein-protein interaction databases

BioGridi32794. 224 interactions.
DIPiDIP-2417N.
IntActiP15873. 18 interactions.
MINTiMINT-675752.
STRINGi4932.YBR088C.

Structurei

Secondary structure

1
258
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87
Helixi9 – 1911
Turni20 – 223
Beta strandi24 – 318
Beta strandi34 – 407
Beta strandi44 – 5310
Helixi54 – 563
Beta strandi57 – 604
Beta strandi66 – 716
Helixi72 – 787
Turni83 – 853
Beta strandi86 – 927
Beta strandi97 – 1048
Beta strandi106 – 1094
Beta strandi111 – 1177
Helixi122 – 1243
Beta strandi134 – 1407
Helixi141 – 15212
Beta strandi156 – 1638
Beta strandi166 – 1727
Beta strandi177 – 1826
Beta strandi185 – 1873
Beta strandi188 – 1903
Helixi191 – 1933
Beta strandi195 – 2017
Beta strandi203 – 2086
Helixi209 – 2157
Helixi216 – 2205
Beta strandi223 – 2297
Beta strandi231 – 2333
Beta strandi235 – 2417
Beta strandi244 – 2507
Beta strandi254 – 2563

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP15873.
SMRiP15873. Positions 1-258.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15873.

Family & Domainsi

Sequence similaritiesi

Belongs to the PCNA family.Curated

Phylogenomic databases

eggNOGiCOG0592.
GeneTreeiENSGT00390000004965.
HOGENOMiHOG000211098.
InParanoidiP15873.
KOiK04802.
OMAiMKLMNLD.
OrthoDBiEOG7M3J9S.

Family and domain databases

HAMAPiMF_00317. DNApol_clamp_arch.
InterProiIPR000730. Pr_cel_nuc_antig.
IPR022649. Pr_cel_nuc_antig_C.
IPR022659. Pr_cel_nuc_antig_CS.
IPR022648. Pr_cel_nuc_antig_N.
[Graphical view]
PANTHERiPTHR11352. PTHR11352. 1 hit.
PfamiPF02747. PCNA_C. 1 hit.
PF00705. PCNA_N. 1 hit.
[Graphical view]
PRINTSiPR00339. PCNACYCLIN.
TIGRFAMsiTIGR00590. pcna. 1 hit.
PROSITEiPS01251. PCNA_1. 1 hit.
PS00293. PCNA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15873-1 [UniParc]FASTAAdd to Basket

« Hide

        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
Length:258
Mass (Da):28,916
Last modified:April 1, 1990 - v1
Checksum:i9B56C5851621DDDC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS22851. WMBYET.
RefSeqiNP_009645.1. NM_001178436.1.

Genome annotation databases

EnsemblFungiiYBR088C; YBR088C; YBR088C.
GeneIDi852385.
KEGGisce:YBR088C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S22851. WMBYET.
RefSeqi NP_009645.1. NM_001178436.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PLQ X-ray 2.30 A 1-258 [» ]
1PLR X-ray 3.00 A 1-258 [» ]
1SXJ X-ray 2.85 F/G/H 1-258 [» ]
2OD8 X-ray 2.80 A 1-258 [» ]
3F1W X-ray 2.90 A 1-258 [» ]
3GPM X-ray 3.80 A 1-258 [» ]
3GPN X-ray 2.50 A 1-258 [» ]
3L0W X-ray 2.80 A 1-163 [» ]
3L0X X-ray 3.00 A 1-163 [» ]
B 165-258 [» ]
3L10 X-ray 2.80 A 1-163 [» ]
3PGE X-ray 2.80 A 165-258 [» ]
B 1-163 [» ]
3V60 X-ray 2.60 B 1-258 [» ]
3V61 X-ray 2.80 B 1-258 [» ]
3V62 X-ray 2.90 B/E 1-258 [» ]
4L60 X-ray 3.00 A 1-256 [» ]
ProteinModelPortali P15873.
SMRi P15873. Positions 1-258.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32794. 224 interactions.
DIPi DIP-2417N.
IntActi P15873. 18 interactions.
MINTi MINT-675752.
STRINGi 4932.YBR088C.

Proteomic databases

MaxQBi P15873.
PaxDbi P15873.
PeptideAtlasi P15873.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YBR088C ; YBR088C ; YBR088C .
GeneIDi 852385.
KEGGi sce:YBR088C.

Organism-specific databases

CYGDi YBR088c.
SGDi S000000292. POL30.

Phylogenomic databases

eggNOGi COG0592.
GeneTreei ENSGT00390000004965.
HOGENOMi HOG000211098.
InParanoidi P15873.
KOi K04802.
OMAi MKLMNLD.
OrthoDBi EOG7M3J9S.

Enzyme and pathway databases

BioCyci YEAST:G3O-29055-MONOMER.
Reactomei REACT_189247. G1/S-Specific Transcription.

Miscellaneous databases

EvolutionaryTracei P15873.
NextBioi 971192.
PROi P15873.

Gene expression databases

Genevestigatori P15873.

Family and domain databases

HAMAPi MF_00317. DNApol_clamp_arch.
InterProi IPR000730. Pr_cel_nuc_antig.
IPR022649. Pr_cel_nuc_antig_C.
IPR022659. Pr_cel_nuc_antig_CS.
IPR022648. Pr_cel_nuc_antig_N.
[Graphical view ]
PANTHERi PTHR11352. PTHR11352. 1 hit.
Pfami PF02747. PCNA_C. 1 hit.
PF00705. PCNA_N. 1 hit.
[Graphical view ]
PRINTSi PR00339. PCNACYCLIN.
TIGRFAMsi TIGR00590. pcna. 1 hit.
PROSITEi PS01251. PCNA_1. 1 hit.
PS00293. PCNA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. 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. 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.

Entry informationi

Entry nameiPCNA_YEAST
AccessioniPrimary (citable) accession number: P15873
Secondary accession number(s): D6VQ89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 29, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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

External Data

Dasty 3