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Protein

Proliferating cell nuclear antigen

Gene

pcn1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission 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.

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: PomBase

GO - Biological processi

  • DNA strand elongation involved in DNA replication Source: PomBase
  • error-free translesion synthesis Source: PomBase
  • error-prone translesion synthesis Source: PomBase
  • leading strand elongation Source: GO_Central
  • mismatch repair Source: GO_Central
  • mitotic DNA replication leading strand elongation Source: PomBase
  • positive regulation of cellular protein catabolic process Source: PomBase
  • positive regulation of DNA-directed DNA polymerase activity Source: PomBase
  • postreplication repair Source: PomBase
  • translesion synthesis Source: GO_Central
  • UV-damage excision repair Source: PomBase
Complete GO annotation...

Keywords - Biological processi

DNA replication

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-SPO-110312. Translesion synthesis by REV1.
R-SPO-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-SPO-110320. Translesion Synthesis by POLH.
R-SPO-113510. E2F mediated regulation of DNA replication.
R-SPO-174411. Polymerase switching on the C-strand of the telomere.
R-SPO-174414. Processive synthesis on the C-strand of the telomere.
R-SPO-174417. Telomere C-strand (Lagging Strand) Synthesis.
R-SPO-174437. Removal of the Flap Intermediate from the C-strand.
R-SPO-4615885. SUMOylation of DNA replication proteins.
R-SPO-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-SPO-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-SPO-5655862. Translesion synthesis by POLK.
R-SPO-5656121. Translesion synthesis by POLI.
R-SPO-5656169. Termination of translesion DNA synthesis.
R-SPO-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-SPO-5696400. Dual Incision in GG-NER.
R-SPO-6782135. Dual incision in TC-NER.
R-SPO-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SPO-69091. Polymerase switching.
R-SPO-69109. Leading Strand Synthesis.
R-SPO-69166. Removal of the Flap Intermediate.
R-SPO-69183. Processive synthesis on the lagging strand.
R-SPO-69205. G1/S-Specific Transcription.

Names & Taxonomyi

Protein namesi
Recommended name:
Proliferating cell nuclear antigen
Short name:
PCNA
Gene namesi
Name:pcn1
Synonyms:pcn
ORF Names:SPBC16D10.09
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC16D10.09.
PomBaseiSPBC16D10.09. pcn1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nuclear replication fork Source: PomBase
  • nucleoplasm Source: PomBase
  • nucleus Source: PomBase
  • PCNA complex Source: PomBase
  • replication fork Source: PomBase
  • site of double-strand break Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 260260Proliferating cell nuclear antigenPRO_0000149175Add
BLAST

Proteomic databases

MaxQBiQ03392.

Interactioni

Subunit structurei

Interacts with cdc24, rfc1, and rtf2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
cdc27P302615EBI-768724,EBI-866919

Protein-protein interaction databases

BioGridi276564. 38 interactions.
DIPiDIP-33811N.
IntActiQ03392. 8 interactions.
MINTiMINT-1209782.

Structurei

3D structure databases

ProteinModelPortaliQ03392.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PCNA family.Curated

Phylogenomic databases

HOGENOMiHOG000211098.
InParanoidiQ03392.
KOiK04802.
OMAiSDGFDKY.
OrthoDBiEOG7M3J9S.
PhylomeDBiQ03392.

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.

Q03392-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEARFQQAA LLKKLLDAIK ELVTDANFDC NDNGISLQAM DSSHVALVSM
60 70 80 90 100
LIKSDGFEPY RCDRNIALGI NLNALSKVLR CAQNEDLVTL KAEDTPEVLN
110 120 130 140 150
LVFESEKNDR ISDYDVKLMD IDQEHLGIPD IEYDATITMP AAEFQRITRD
160 170 180 190 200
LLTLSDSVTI NASKEGVRFS CKGDIGNGST TLKQHTDLSD QDQSIEISLT
210 220 230 240 250
QAVTLTFSLK YLAQFTKATP LATRVTLSMS NDVPLLVEYK MESGFLRFYL
260
APKIGEEDEE
Length:260
Mass (Da):28,969
Last modified:October 1, 1993 - v1
Checksum:i1EE5B2A27A899C4E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54857 Genomic DNA. Translation: CAA38636.1.
CU329671 Genomic DNA. Translation: CAB38513.1.
PIRiS28053. WMZPET.
RefSeqiNP_596504.1. NM_001022425.2.

Genome annotation databases

EnsemblFungiiSPBC16D10.09.1; SPBC16D10.09.1:pep; SPBC16D10.09.
GeneIDi2540020.
KEGGispo:SPBC16D10.09.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54857 Genomic DNA. Translation: CAA38636.1.
CU329671 Genomic DNA. Translation: CAB38513.1.
PIRiS28053. WMZPET.
RefSeqiNP_596504.1. NM_001022425.2.

3D structure databases

ProteinModelPortaliQ03392.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276564. 38 interactions.
DIPiDIP-33811N.
IntActiQ03392. 8 interactions.
MINTiMINT-1209782.

Proteomic databases

MaxQBiQ03392.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC16D10.09.1; SPBC16D10.09.1:pep; SPBC16D10.09.
GeneIDi2540020.
KEGGispo:SPBC16D10.09.

Organism-specific databases

EuPathDBiFungiDB:SPBC16D10.09.
PomBaseiSPBC16D10.09. pcn1.

Phylogenomic databases

HOGENOMiHOG000211098.
InParanoidiQ03392.
KOiK04802.
OMAiSDGFDKY.
OrthoDBiEOG7M3J9S.
PhylomeDBiQ03392.

Enzyme and pathway databases

ReactomeiR-SPO-110312. Translesion synthesis by REV1.
R-SPO-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-SPO-110320. Translesion Synthesis by POLH.
R-SPO-113510. E2F mediated regulation of DNA replication.
R-SPO-174411. Polymerase switching on the C-strand of the telomere.
R-SPO-174414. Processive synthesis on the C-strand of the telomere.
R-SPO-174417. Telomere C-strand (Lagging Strand) Synthesis.
R-SPO-174437. Removal of the Flap Intermediate from the C-strand.
R-SPO-4615885. SUMOylation of DNA replication proteins.
R-SPO-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-SPO-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-SPO-5655862. Translesion synthesis by POLK.
R-SPO-5656121. Translesion synthesis by POLI.
R-SPO-5656169. Termination of translesion DNA synthesis.
R-SPO-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-SPO-5696400. Dual Incision in GG-NER.
R-SPO-6782135. Dual incision in TC-NER.
R-SPO-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SPO-69091. Polymerase switching.
R-SPO-69109. Leading Strand Synthesis.
R-SPO-69166. Removal of the Flap Intermediate.
R-SPO-69183. Processive synthesis on the lagging strand.
R-SPO-69205. G1/S-Specific Transcription.

Miscellaneous databases

PROiQ03392.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and analysis of the fission yeast gene encoding polymerase delta accessory protein PCNA."
    Waseem N.H., Labib K., Nurse P., Lane D.P.
    EMBO J. 11:5111-5120(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Fission yeast cdc24 is a replication factor C- and proliferating cell nuclear antigen-interacting factor essential for S-phase completion."
    Tanaka H., Tanaka K., Murakami H., Okayama H.
    Mol. Cell. Biol. 19:1038-1048(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDC24 AND RFC1.
  4. "Schizosaccharomyces pombe Rtf2 mediates site-specific replication termination by inhibiting replication restart."
    Inagawa T., Yamada-Inagawa T., Eydmann T., Mian I.S., Wang T.S., Dalgaard J.Z.
    Proc. Natl. Acad. Sci. U.S.A. 106:7927-7932(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RTF2.

Entry informationi

Entry nameiPCNA_SCHPO
AccessioniPrimary (citable) accession number: Q03392
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 6, 2016
This is version 131 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

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.