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Protein

Proliferating cell nuclear antigen

Gene

pcna

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 4 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.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi61 – 80Sequence analysisAdd BLAST20

GO - Molecular functioni

GO - Biological processi

  • leading strand elongation Source: GO_Central
  • mismatch repair Source: GO_Central
  • regulation of DNA replication Source: InterPro
  • response to activity Source: ZFIN
  • response to bacterium Source: ZFIN
  • translesion synthesis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA replication

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-DRE-110312. Translesion synthesis by REV1.
R-DRE-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-DRE-110320. Translesion Synthesis by POLH.
R-DRE-113510. E2F mediated regulation of DNA replication.
R-DRE-1538133. G0 and Early G1.
R-DRE-174411. Polymerase switching on the C-strand of the telomere.
R-DRE-174414. Processive synthesis on the C-strand of the telomere.
R-DRE-174417. Telomere C-strand (Lagging Strand) Synthesis.
R-DRE-174437. Removal of the Flap Intermediate from the C-strand.
R-DRE-4615885. SUMOylation of DNA replication proteins.
R-DRE-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-DRE-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-DRE-5655862. Translesion synthesis by POLK.
R-DRE-5656121. Translesion synthesis by POLI.
R-DRE-5656169. Termination of translesion DNA synthesis.
R-DRE-5685942. HDR through Homologous Recombination (HRR).
R-DRE-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-DRE-5696400. Dual Incision in GG-NER.
R-DRE-6782135. Dual incision in TC-NER.
R-DRE-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-DRE-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-DRE-69091. Polymerase switching.
R-DRE-69166. Removal of the Flap Intermediate.
R-DRE-69183. Processive synthesis on the lagging strand.
R-DRE-69205. G1/S-Specific Transcription.

Names & Taxonomyi

Protein namesi
Recommended name:
Proliferating cell nuclear antigen
Short name:
PCNA
Gene namesi
Name:pcna
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 10

Organism-specific databases

ZFINiZDB-GENE-000210-8. pcna.

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

  • nucleus Source: ZFIN
  • PCNA complex Source: GO_Central
  • PCNA-p21 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001491651 – 260Proliferating cell nuclear antigenAdd BLAST260

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei259Phosphoserine1 Publication1
Modified residuei260Phosphoserine1 Publication1

Post-translational modificationi

Monoubiquitinated by the ube2b-rad18 complex on Lys-164. Monoubiquitination at Lys-164 also takes place in undamaged proliferating cells, and is mediated by the dcx(dtl) complex, leading to enhance PCNA-dependent translesion DNA synthesis (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9PTP1.
PRIDEiQ9PTP1.

PTM databases

iPTMnetiQ9PTP1.

Expressioni

Gene expression databases

BgeeiENSDARG00000054155.

Interactioni

Subunit structurei

Homotrimer. Forms a complex with activator 1 heteropentamer in the presence of ATP (By similarity).By similarity

Protein-protein interaction databases

STRINGi7955.ENSDARP00000070780.

Structurei

3D structure databases

ProteinModelPortaliQ9PTP1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PCNA family.Curated

Phylogenomic databases

eggNOGiKOG1636. Eukaryota.
COG0592. LUCA.
GeneTreeiENSGT00390000004965.
HOGENOMiHOG000211098.
HOVERGENiHBG000947.
InParanoidiQ9PTP1.
KOiK04802.
OMAiSDGFDKY.
PhylomeDBiQ9PTP1.
TreeFamiTF313441.

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.

Q9PTP1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFEARLVQGS ILKKVLEALK DLITEACWDV SSSGISLQSM DSSHVSLVQL
60 70 80 90 100
TLRSDGFDSY RCDRNLAMGV NLSSMSKILK CAGNEDIITL RAEDNADALA
110 120 130 140 150
LVFETLNQEK VSDYEMKLMD LDVEQLGIPE QEYSCVVKMP SGEFARICRD
160 170 180 190 200
LSQIGDAVMI SCAKDGVKFS ASGELGTGNI KLSQTSNVDK EDEAVTIEMN
210 220 230 240 250
EPVQLIFALN YLNFFTKATP LSKTVTLSMS ADIPLVVEYK IADMGHVKYY
260
LAPKIDEESS
Length:260
Mass (Da):28,611
Last modified:May 24, 2005 - v2
Checksum:i59D27AC8C95B472D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti88I → Q in AAF18324 (Ref. 1) Curated1
Sequence conflicti98A → T in AAF18324 (Ref. 1) Curated1
Sequence conflicti105 – 106TL → AQ in AAF18324 (Ref. 1) Curated2
Sequence conflicti218A → P in AAF18324 (Ref. 1) Curated1
Sequence conflicti223K → R in AAF18324 (Ref. 1) Curated1
Sequence conflicti228S → R in AAF18324 (Ref. 1) Curated1
Sequence conflicti232D → H in AAF18324 (Ref. 1) Curated1
Sequence conflicti239Y → D in AAF18324 (Ref. 1) Curated1
Sequence conflicti244 – 245MG → LE in AAF18324 (Ref. 1) Curated2
Sequence conflicti254 – 255KI → QIE in AAF18324 (Ref. 1) Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF140608 mRNA. Translation: AAF18324.1.
BC049535 mRNA. Translation: AAH49535.1.
BC064299 mRNA. Translation: AAH64299.1.
RefSeqiNP_571479.2. NM_131404.2.
UniGeneiDr.35605.

Genome annotation databases

EnsembliENSDART00000076304; ENSDARP00000070780; ENSDARG00000054155.
GeneIDi30678.
KEGGidre:30678.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF140608 mRNA. Translation: AAF18324.1.
BC049535 mRNA. Translation: AAH49535.1.
BC064299 mRNA. Translation: AAH64299.1.
RefSeqiNP_571479.2. NM_131404.2.
UniGeneiDr.35605.

3D structure databases

ProteinModelPortaliQ9PTP1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000070780.

PTM databases

iPTMnetiQ9PTP1.

Proteomic databases

PaxDbiQ9PTP1.
PRIDEiQ9PTP1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000076304; ENSDARP00000070780; ENSDARG00000054155.
GeneIDi30678.
KEGGidre:30678.

Organism-specific databases

CTDi5111.
ZFINiZDB-GENE-000210-8. pcna.

Phylogenomic databases

eggNOGiKOG1636. Eukaryota.
COG0592. LUCA.
GeneTreeiENSGT00390000004965.
HOGENOMiHOG000211098.
HOVERGENiHBG000947.
InParanoidiQ9PTP1.
KOiK04802.
OMAiSDGFDKY.
PhylomeDBiQ9PTP1.
TreeFamiTF313441.

Enzyme and pathway databases

ReactomeiR-DRE-110312. Translesion synthesis by REV1.
R-DRE-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-DRE-110320. Translesion Synthesis by POLH.
R-DRE-113510. E2F mediated regulation of DNA replication.
R-DRE-1538133. G0 and Early G1.
R-DRE-174411. Polymerase switching on the C-strand of the telomere.
R-DRE-174414. Processive synthesis on the C-strand of the telomere.
R-DRE-174417. Telomere C-strand (Lagging Strand) Synthesis.
R-DRE-174437. Removal of the Flap Intermediate from the C-strand.
R-DRE-4615885. SUMOylation of DNA replication proteins.
R-DRE-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-DRE-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-DRE-5655862. Translesion synthesis by POLK.
R-DRE-5656121. Translesion synthesis by POLI.
R-DRE-5656169. Termination of translesion DNA synthesis.
R-DRE-5685942. HDR through Homologous Recombination (HRR).
R-DRE-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-DRE-5696400. Dual Incision in GG-NER.
R-DRE-6782135. Dual incision in TC-NER.
R-DRE-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-DRE-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-DRE-69091. Polymerase switching.
R-DRE-69166. Removal of the Flap Intermediate.
R-DRE-69183. Processive synthesis on the lagging strand.
R-DRE-69205. G1/S-Specific Transcription.

Miscellaneous databases

PROiQ9PTP1.

Gene expression databases

BgeeiENSDARG00000054155.

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_DANRE
AccessioniPrimary (citable) accession number: Q9PTP1
Secondary accession number(s): Q7ZW84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 24, 2005
Last modified: October 5, 2016
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.