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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: 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

  • DNA binding Source: UniProtKB-KW
  • DNA polymerase processivity factor activity Source: SGD
  • identical protein binding Source: IntAct

GO - Biological processi

  • chromatin silencing at silent mating-type cassette Source: SGD
  • chromatin silencing at telomere Source: SGD
  • 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 exodeoxyribonuclease activity Source: SGD
  • positive regulation of phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands Source: SGD
  • postreplication repair Source: SGD
  • 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.
ReactomeiR-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-113510. E2F mediated regulation of DNA replication.
R-SCE-174411. Polymerase switching on the C-strand of the telomere.
R-SCE-4615885. SUMOylation of DNA replication proteins.
R-SCE-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-SCE-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-SCE-5655862. Translesion synthesis by POLK.
R-SCE-5656121. Translesion synthesis by POLI.
R-SCE-5656169. Termination of translesion DNA synthesis.
R-SCE-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-SCE-5696400. Dual Incision in GG-NER.
R-SCE-6782135. Dual incision in TC-NER.
R-SCE-6782210. Gap-filling DNA repair synthesis and ligation 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.
R-SCE-69205. 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
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR088C.
SGDiS000000292. POL30.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: GOC
  • nucleus Source: SGD
  • PCNA complex Source: SGD
  • 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.
TopDownProteomicsiP15873.

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

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi32794. 227 interactions.
DIPiDIP-2417N.
IntActiP15873. 18 interactions.
MINTiMINT-675752.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4L6PX-ray2.68A/B/C1-258[»]
4YHRX-ray2.95A1-258[»]
ProteinModelPortaliP15873.
SMRiP15873. Positions 1-258.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15873.

Family & Domainsi

Sequence similaritiesi

Belongs to the PCNA family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000004965.
HOGENOMiHOG000211098.
InParanoidiP15873.
KOiK04802.
OMAiCNFNCTE.
OrthoDBiEOG092C4AWZ.

Family and domain databases

HAMAPiMF_00317. DNApol_clamp_arch. 1 hit.
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:
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.
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:
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.
PIRiS22851. WMBYET.
RefSeqiNP_009645.1. NM_001178436.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4L6PX-ray2.68A/B/C1-258[»]
4YHRX-ray2.95A1-258[»]
ProteinModelPortaliP15873.
SMRiP15873. Positions 1-258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32794. 227 interactions.
DIPiDIP-2417N.
IntActiP15873. 18 interactions.
MINTiMINT-675752.

Proteomic databases

MaxQBiP15873.
TopDownProteomicsiP15873.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YBR088C.
SGDiS000000292. POL30.

Phylogenomic databases

GeneTreeiENSGT00390000004965.
HOGENOMiHOG000211098.
InParanoidiP15873.
KOiK04802.
OMAiCNFNCTE.
OrthoDBiEOG092C4AWZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-29055-MONOMER.
ReactomeiR-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-113510. E2F mediated regulation of DNA replication.
R-SCE-174411. Polymerase switching on the C-strand of the telomere.
R-SCE-4615885. SUMOylation of DNA replication proteins.
R-SCE-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-SCE-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-SCE-5655862. Translesion synthesis by POLK.
R-SCE-5656121. Translesion synthesis by POLI.
R-SCE-5656169. Termination of translesion DNA synthesis.
R-SCE-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-SCE-5696400. Dual Incision in GG-NER.
R-SCE-6782135. Dual incision in TC-NER.
R-SCE-6782210. Gap-filling DNA repair synthesis and ligation 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.
R-SCE-69205. G1/S-Specific Transcription.

Miscellaneous databases

EvolutionaryTraceiP15873.
PROiP15873.

Family and domain databases

HAMAPiMF_00317. DNApol_clamp_arch. 1 hit.
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]
ProtoNetiSearch...

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: September 7, 2016
This is version 162 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.