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Protein

Proliferating cell nuclear antigen

Gene

PCNA

Organism
Drosophila melanogaster (Fruit fly)
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.By similarity

Regions

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

GO - Molecular functioni

GO - Biological processi

  • antimicrobial humoral response Source: FlyBase
  • DNA-dependent DNA replication Source: FlyBase
  • DNA replication Source: FlyBase
  • eggshell chorion gene amplification Source: FlyBase
  • leading strand elongation Source: GO_Central
  • mismatch repair Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • neurogenesis Source: FlyBase
  • nucleotide-excision repair Source: FlyBase
  • regulation of DNA replication Source: InterPro
  • translesion synthesis Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

DNA replication

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-DME-110312. Translesion synthesis by REV1.
R-DME-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-DME-110320. Translesion Synthesis by POLH.
R-DME-113510. E2F mediated regulation of DNA replication.
R-DME-1538133. G0 and Early G1.
R-DME-174411. Polymerase switching on the C-strand of the telomere.
R-DME-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-DME-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-DME-5655862. Translesion synthesis by POLK.
R-DME-5656121. Translesion synthesis by POLI.
R-DME-5656169. Termination of translesion DNA synthesis.
R-DME-69091. Polymerase switching.
R-DME-69166. Removal of the Flap Intermediate.
R-DME-69183. Processive synthesis on the lagging strand.
R-DME-69205. G1/S-Specific Transcription.
SignaLinkiP17917.

Names & Taxonomyi

Protein namesi
Recommended name:
Proliferating cell nuclear antigen
Short name:
PCNA
Alternative name(s):
Cyclin
Mutagen-sensitive 209 protein
Gene namesi
Name:PCNA
Synonyms:mus209
ORF Names:CG9193
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0005655. PCNA.

Subcellular locationi

  • Nucleus 1 Publication

  • Note: Colocalizes with crm in polytene nuclei during embryogenesis.

GO - Cellular componenti

  • microtubule associated complex Source: FlyBase
  • nucleus Source: GO_Central
  • PCNA complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Mutant flies show temperature-sensitive lethality, hypersensitivity to DNA-damaging agents such as ionizing radiation and methyl methanesulfonate, suppression of position-effect variegation and female sterility.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001491701 – 260Proliferating cell nuclear antigenAdd BLAST260

Proteomic databases

PaxDbiP17917.
PRIDEiP17917.

Expressioni

Tissue specificityi

Expressed at high levels in adult ovary.1 Publication

Developmental stagei

Expressed maternally and zygotically. Expressed at high levels in unfertilized eggs and during early stages of embryogenesis. Low expression detected during late embryogenesis, in second and third instar larvae and in adult flies.1 Publication

Gene expression databases

BgeeiFBgn0005655.
GenevisibleiP17917. DM.

Interactioni

Subunit structurei

Homotrimer. Forms a complex with activator 1 heteropentamer in the presence of ATP (By similarity). Interacts with E2f.By similarity1 Publication

Protein-protein interaction databases

BioGridi62946. 70 interactors.
DIPiDIP-20560N.
IntActiP17917. 16 interactors.
MINTiMINT-833658.
STRINGi7227.FBpp0085619.

Structurei

Secondary structure

1260
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Helixi9 – 19Combined sources11
Turni20 – 22Combined sources3
Beta strandi24 – 31Combined sources8
Beta strandi34 – 40Combined sources7
Beta strandi44 – 53Combined sources10
Helixi54 – 56Combined sources3
Beta strandi57 – 64Combined sources8
Beta strandi66 – 71Combined sources6
Helixi72 – 79Combined sources8
Beta strandi87 – 92Combined sources6
Beta strandi98 – 104Combined sources7
Beta strandi111 – 117Combined sources7
Beta strandi137 – 140Combined sources4
Helixi141 – 151Combined sources11
Turni152 – 154Combined sources3
Beta strandi156 – 162Combined sources7
Beta strandi167 – 173Combined sources7
Beta strandi176 – 182Combined sources7
Beta strandi203 – 208Combined sources6
Helixi209 – 215Combined sources7
Helixi216 – 221Combined sources6
Beta strandi223 – 228Combined sources6
Beta strandi235 – 241Combined sources7
Turni242 – 244Combined sources3
Beta strandi245 – 251Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HK1X-ray2.00A1-260[»]
ProteinModelPortaliP17917.
SMRiP17917.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PCNA family.Curated

Phylogenomic databases

eggNOGiKOG1636. Eukaryota.
COG0592. LUCA.
GeneTreeiENSGT00390000004965.
InParanoidiP17917.
KOiK04802.
OMAiSDGFDKY.
OrthoDBiEOG091G0GQ7.
PhylomeDBiP17917.

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.

P17917-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFEARLGQAT ILKKILDAIK DLLNEATFDC SDSGIQLQAM DNSHVSLVSL
60 70 80 90 100
TLRSDGFDKF RCDRNLSMGM NLGSMAKILK CANNEDNVTM KAQDNADTVT
110 120 130 140 150
IMFESANQEK VSDYEMKLMN LDQEHLGIPE TDFSCVVRMP AMEFARICRD
160 170 180 190 200
LAQFSESVVI CCTKEGVKFS ASGDVGTANI KLAQTGSVDK EEEAVIIEMQ
210 220 230 240 250
EPVTLTFACR YLNAFTKATP LSTQVQLSMC ADVPLVVEYA IKDLGHIRYY
260
LAPKIEDNET
Length:260
Mass (Da):28,830
Last modified:February 1, 1991 - v2
Checksum:i9A46280EA2C61FC5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33950 Genomic DNA. Translation: AAA28746.1.
AE013599 Genomic DNA. Translation: AAF57493.1.
AE013599 Genomic DNA. Translation: AAS64796.1.
AY122197 mRNA. Translation: AAM52709.1.
PIRiA34752.
RefSeqiNP_476905.1. NM_057557.4.
NP_995904.1. NM_206182.2.
UniGeneiDm.4751.

Genome annotation databases

EnsemblMetazoaiFBtr0086307; FBpp0085619; FBgn0005655.
FBtr0086308; FBpp0089395; FBgn0005655.
GeneIDi37290.
KEGGidme:Dmel_CG9193.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33950 Genomic DNA. Translation: AAA28746.1.
AE013599 Genomic DNA. Translation: AAF57493.1.
AE013599 Genomic DNA. Translation: AAS64796.1.
AY122197 mRNA. Translation: AAM52709.1.
PIRiA34752.
RefSeqiNP_476905.1. NM_057557.4.
NP_995904.1. NM_206182.2.
UniGeneiDm.4751.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HK1X-ray2.00A1-260[»]
ProteinModelPortaliP17917.
SMRiP17917.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62946. 70 interactors.
DIPiDIP-20560N.
IntActiP17917. 16 interactors.
MINTiMINT-833658.
STRINGi7227.FBpp0085619.

Proteomic databases

PaxDbiP17917.
PRIDEiP17917.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086307; FBpp0085619; FBgn0005655.
FBtr0086308; FBpp0089395; FBgn0005655.
GeneIDi37290.
KEGGidme:Dmel_CG9193.

Organism-specific databases

CTDi5111.
FlyBaseiFBgn0005655. PCNA.

Phylogenomic databases

eggNOGiKOG1636. Eukaryota.
COG0592. LUCA.
GeneTreeiENSGT00390000004965.
InParanoidiP17917.
KOiK04802.
OMAiSDGFDKY.
OrthoDBiEOG091G0GQ7.
PhylomeDBiP17917.

Enzyme and pathway databases

ReactomeiR-DME-110312. Translesion synthesis by REV1.
R-DME-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-DME-110320. Translesion Synthesis by POLH.
R-DME-113510. E2F mediated regulation of DNA replication.
R-DME-1538133. G0 and Early G1.
R-DME-174411. Polymerase switching on the C-strand of the telomere.
R-DME-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-DME-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-DME-5655862. Translesion synthesis by POLK.
R-DME-5656121. Translesion synthesis by POLI.
R-DME-5656169. Termination of translesion DNA synthesis.
R-DME-69091. Polymerase switching.
R-DME-69166. Removal of the Flap Intermediate.
R-DME-69183. Processive synthesis on the lagging strand.
R-DME-69205. G1/S-Specific Transcription.
SignaLinkiP17917.

Miscellaneous databases

GenomeRNAii37290.
PROiP17917.

Gene expression databases

BgeeiFBgn0005655.
GenevisibleiP17917. DM.

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_DROME
AccessioniPrimary (citable) accession number: P17917
Secondary accession number(s): Q540V1, Q9V909
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 1, 1991
Last modified: November 30, 2016
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.