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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: -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)DescriptionActionsGraphical viewLength
DNA bindingi61 – 80Sequence analysisAdd BLAST20

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

Keywordsi

Molecular functionDNA-binding
Biological processDNA damage, DNA repair, DNA replication

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-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-8866654 E3 ubiquitin ligases ubiquitinate target proteins

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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001491761 – 258Proliferating cell nuclear antigenAdd BLAST258

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki127Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate2 Publications
Cross-linki164Glycyl 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 conjugation

Proteomic databases

MaxQBiP15873
PaxDbiP15873
PRIDEiP15873
TopDownProteomicsiP15873

PTM databases

iPTMnetiP15873

Interactioni

Subunit structurei

Homotrimer (PubMed:15201901). Interacts with RAD30 (PubMed:11545742). Interacts with MCM10 (PubMed:16782870). Interacts with UBP10 (PubMed:22829782).4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi32794, 457 interactors
ComplexPortaliCPX-544 PCNA homotrimer
DIPiDIP-2417N
IntActiP15873, 37 interactors
MINTiP15873
STRINGi4932.YBR088C

Structurei

Secondary structure

1258
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Helixi9 – 17Combined sources9
Turni18 – 22Combined sources5
Beta strandi24 – 31Combined sources8
Beta strandi34 – 40Combined sources7
Beta strandi42 – 44Combined sources3
Beta strandi46 – 53Combined sources8
Helixi54 – 56Combined sources3
Beta strandi57 – 64Combined sources8
Beta strandi66 – 71Combined sources6
Helixi72 – 79Combined sources8
Beta strandi80 – 82Combined sources3
Beta strandi84 – 92Combined sources9
Beta strandi97 – 104Combined sources8
Beta strandi106 – 109Combined sources4
Beta strandi111 – 117Combined sources7
Helixi122 – 124Combined sources3
Beta strandi134 – 140Combined sources7
Helixi141 – 152Combined sources12
Beta strandi156 – 163Combined sources8
Beta strandi166 – 173Combined sources8
Beta strandi176 – 182Combined sources7
Beta strandi185 – 187Combined sources3
Beta strandi188 – 190Combined sources3
Helixi191 – 193Combined sources3
Beta strandi195 – 201Combined sources7
Beta strandi203 – 208Combined sources6
Helixi209 – 215Combined sources7
Helixi216 – 220Combined sources5
Beta strandi223 – 229Combined sources7
Beta strandi231 – 233Combined sources3
Beta strandi235 – 241Combined sources7
Beta strandi244 – 250Combined sources7
Beta strandi254 – 256Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5JNEX-ray2.85D/H1-258[»]
5T9DX-ray3.27A/B/C2-258[»]
5V7KX-ray3.05A1-258[»]
5V7LX-ray3.20A1-258[»]
5V7MX-ray1.93A1-258[»]
6B8IX-ray2.90A/B/C1-258[»]
6CX2X-ray3.10A1-258[»]
6CX3X-ray3.10A1-258[»]
6CX4X-ray3.08A1-258[»]
ProteinModelPortaliP15873
SMRiP15873
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15873

Family & Domainsi

Sequence similaritiesi

Belongs to the PCNA family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000004965
HOGENOMiHOG000211098
InParanoidiP15873
KOiK04802
OMAiSDGFDKY
OrthoDBiEOG092C4AWZ

Family and domain databases

HAMAPiMF_00317 DNApol_clamp_arch, 1 hit
InterProiView 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
PANTHERiPTHR11352:SF0 PTHR11352:SF0, 1 hit
PfamiView protein in Pfam
PF02747 PCNA_C, 1 hit
PF00705 PCNA_N, 1 hit
PRINTSiPR00339 PCNACYCLIN
TIGRFAMsiTIGR00590 pcna, 1 hit
PROSITEiView protein in PROSITE
PS01251 PCNA_1, 1 hit
PS00293 PCNA_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiPCNA_YEAST
AccessioniPrimary (citable) accession number: P15873
Secondary accession number(s): D6VQ89
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 20, 2018
This is version 180 of the entry and version 1 of the sequence. See 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

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