We will be switching to the new UniProt website on Tuesday, June 28. Please explore and share your feedback.
Take me to UniProt BETA
UniProtKB - P15873 (PCNA_YEAST)
Protein
Proliferating cell nuclear antigen
Gene
POL30
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
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 PublicationsRegions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
DNA bindingi | 61 – 80 | Sequence analysisAdd BLAST | 20 |
GO - Molecular functioni
- DNA binding Source: UniProtKB-KW
- DNA polymerase processivity factor activity Source: SGD
- identical protein binding Source: IntAct
GO - Biological processi
- error-free translesion synthesis Source: SGD
- establishment of mitotic sister chromatid cohesion Source: SGD
- lagging strand elongation Source: SGD
- leading strand elongation Source: SGD
- maintenance of DNA trinucleotide repeats Source: SGD
- meiotic mismatch repair Source: SGD
- mismatch repair Source: SGD
- mitotic cell cycle Source: SGD
- mitotic sister chromatid cohesion Source: SGD
- nucleotide-excision repair Source: SGD
- positive regulation of DNA repair Source: ComplexPortal
- positive regulation of DNA replication Source: ComplexPortal
- positive regulation of exodeoxyribonuclease activity Source: SGD
- positive regulation of exonuclease activity Source: SGD
- positive regulation of phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands Source: SGD
- postreplication repair Source: SGD
- silent mating-type cassette heterochromatin assembly Source: SGD
- subtelomeric heterochromatin assembly Source: SGD
- translesion synthesis Source: GO_Central
Keywordsi
Molecular function | DNA-binding |
Biological process | DNA damage, DNA repair, DNA replication |
Enzyme and pathway databases
Reactomei | R-SCE-110312, Translesion synthesis by REV1 R-SCE-110314, Recognition of DNA damage by PCNA-containing replication complex R-SCE-110320, Translesion Synthesis by POLH R-SCE-4615885, SUMOylation of DNA replication proteins R-SCE-5358565, Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) R-SCE-5655862, Translesion synthesis by POLK R-SCE-5656121, Translesion synthesis by POLI R-SCE-5656169, Termination of translesion DNA synthesis R-SCE-6782135, Dual incision in TC-NER R-SCE-69091, Polymerase switching R-SCE-69166, Removal of the Flap Intermediate R-SCE-69183, Processive synthesis on the lagging strand |
Names & Taxonomyi
Protein namesi | Recommended name: Proliferating cell nuclear antigenShort name: PCNA |
Gene namesi | Name:POL30 Ordered Locus Names:YBR088C ORF Names:YBR0811 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000000292, POL30 |
VEuPathDBi | FungiDB:YBR088C |
Subcellular locationi
Nucleus
Nucleus
- nucleus Source: SGD
- PCNA complex Source: SGD
Other locations
- chromosome, telomeric region Source: GOC
- replication fork Source: SGD
Keywords - Cellular componenti
NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000149176 | 1 – 258 | Proliferating cell nuclear antigenAdd BLAST | 258 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Cross-linki | 127 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication | ||
Cross-linki | 164 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate2 Publications | ||
Cross-linki | 164 | Glycyl 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
Lys-164 is deubiquitinated by UBP10 (PubMed:22829782).1 Publication
Keywords - PTMi
Isopeptide bond, Ubl conjugationProteomic databases
MaxQBi | P15873 |
PaxDbi | P15873 |
PRIDEi | P15873 |
TopDownProteomicsi | P15873 |
PTM databases
iPTMneti | P15873 |
Interactioni
Subunit structurei
Binary interactionsi
P15873
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 32794, 471 interactors |
ComplexPortali | CPX-544, PCNA homotrimer |
DIPi | DIP-2417N |
IntActi | P15873, 36 interactors |
MINTi | P15873 |
STRINGi | 4932.YBR088C |
Miscellaneous databases
RNActi | P15873, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P15873 |
SASBDBi | P15873 |
SMRi | P15873 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P15873 |
Family & Domainsi
Sequence similaritiesi
Belongs to the PCNA family.Curated
Phylogenomic databases
eggNOGi | KOG1636, Eukaryota |
GeneTreei | ENSGT00390000004965 |
HOGENOMi | CLU_043978_3_0_1 |
InParanoidi | P15873 |
OMAi | EMKLINM |
Family and domain databases
HAMAPi | MF_00317, DNApol_clamp_arch, 1 hit |
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 |
PANTHERi | PTHR11352:SF0, PTHR11352:SF0, 1 hit |
Pfami | View protein in Pfam PF02747, PCNA_C, 1 hit PF00705, PCNA_N, 1 hit |
PRINTSi | PR00339, PCNACYCLIN |
TIGRFAMsi | TIGR00590, pcna, 1 hit |
PROSITEi | View protein in PROSITE PS01251, PCNA_1, 1 hit PS00293, PCNA_2, 1 hit |
i Sequence
Sequence statusi: Complete.
P15873-1 [UniParc]FASTAAdd to basket
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
Select the link destinations: EMBLi GenBanki DDBJi 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 |
Genome annotation databases
EnsemblFungii | YBR088C_mRNA; YBR088C; YBR088C |
GeneIDi | 852385 |
KEGGi | sce:YBR088C |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
4L6P | X-ray | 2.68 | A/B/C | 1-258 | [»] | |
4YHR | X-ray | 2.95 | A | 1-258 | [»] | |
5JNE | X-ray | 2.85 | D/H | 1-258 | [»] | |
5T9D | X-ray | 3.27 | A/B/C | 2-258 | [»] | |
5V7K | X-ray | 3.05 | A | 1-258 | [»] | |
5V7L | X-ray | 3.20 | A | 1-258 | [»] | |
5V7M | X-ray | 1.93 | A | 1-258 | [»] | |
5ZUT | X-ray | 2.82 | A | 1-258 | [»] | |
6CX2 | X-ray | 3.10 | A | 1-258 | [»] | |
6CX3 | X-ray | 3.10 | A | 1-258 | [»] | |
6CX4 | X-ray | 3.08 | A | 1-258 | [»] | |
6D0Q | X-ray | 2.80 | A | 1-258 | [»] | |
6D0R | X-ray | 2.86 | A | 1-258 | [»] | |
6E49 | X-ray | 2.90 | A/B/C | 1-258 | [»] | |
6W9W | X-ray | 2.65 | A | 1-254 | [»] | |
6WAC | X-ray | 2.90 | A | 1-253 | [»] | |
7KC0 | electron microscopy | 3.20 | E/F/G | 1-258 | [»] | |
AlphaFoldDBi | P15873 | |||||
SASBDBi | P15873 | |||||
SMRi | P15873 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 32794, 471 interactors |
ComplexPortali | CPX-544, PCNA homotrimer |
DIPi | DIP-2417N |
IntActi | P15873, 36 interactors |
MINTi | P15873 |
STRINGi | 4932.YBR088C |
PTM databases
iPTMneti | P15873 |
Proteomic databases
MaxQBi | P15873 |
PaxDbi | P15873 |
PRIDEi | P15873 |
TopDownProteomicsi | P15873 |
Genome annotation databases
EnsemblFungii | YBR088C_mRNA; YBR088C; YBR088C |
GeneIDi | 852385 |
KEGGi | sce:YBR088C |
Organism-specific databases
SGDi | S000000292, POL30 |
VEuPathDBi | FungiDB:YBR088C |
Phylogenomic databases
eggNOGi | KOG1636, Eukaryota |
GeneTreei | ENSGT00390000004965 |
HOGENOMi | CLU_043978_3_0_1 |
InParanoidi | P15873 |
OMAi | EMKLINM |
Enzyme and pathway databases
Reactomei | R-SCE-110312, Translesion synthesis by REV1 R-SCE-110314, Recognition of DNA damage by PCNA-containing replication complex R-SCE-110320, Translesion Synthesis by POLH R-SCE-4615885, SUMOylation of DNA replication proteins R-SCE-5358565, Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) R-SCE-5655862, Translesion synthesis by POLK R-SCE-5656121, Translesion synthesis by POLI R-SCE-5656169, Termination of translesion DNA synthesis R-SCE-6782135, Dual incision in TC-NER R-SCE-69091, Polymerase switching R-SCE-69166, Removal of the Flap Intermediate R-SCE-69183, Processive synthesis on the lagging strand |
Miscellaneous databases
EvolutionaryTracei | P15873 |
PROi | PR:P15873 |
RNActi | P15873, protein |
Family and domain databases
HAMAPi | MF_00317, DNApol_clamp_arch, 1 hit |
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 |
PANTHERi | PTHR11352:SF0, PTHR11352:SF0, 1 hit |
Pfami | View protein in Pfam PF02747, PCNA_C, 1 hit PF00705, PCNA_N, 1 hit |
PRINTSi | PR00339, PCNACYCLIN |
TIGRFAMsi | TIGR00590, pcna, 1 hit |
PROSITEi | View protein in PROSITE PS01251, PCNA_1, 1 hit PS00293, PCNA_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PCNA_YEAST | |
Accessioni | P15873Primary (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: | May 25, 2022 | |
This is version 204 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome II
Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families