UniProtKB - P17917 (PCNA_DROME)
Protein
Proliferating cell nuclear antigen
Gene
PCNA
Organism
Drosophila melanogaster (Fruit fly)
Status
Functioni
Likely to be an auxiliary protein of DNA polymerase delta complex and is probably involved in the control of DNA replication and repair by increasing the polymerase's processibility.1 Publication
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
DNA bindingi | 61 – 80 | Sequence analysisAdd BLAST | 20 |
GO - Molecular functioni
- chromatin binding Source: UniProtKB
- DNA binding Source: UniProtKB-KW
- DNA polymerase processivity factor activity Source: GO_Central
GO - Biological processi
- cellular response to DNA damage stimulus Source: UniProtKB
- 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: GO_Central
- mitotic spindle organization Source: FlyBase
- nucleotide-excision repair Source: FlyBase
- regulation of DNA replication Source: InterPro
- response to hydrogen peroxide Source: UniProtKB
- response to methyl methanesulfonate Source: UniProtKB
- response to UV Source: UniProtKB
- translesion synthesis Source: GO_Central
Keywordsi
Molecular function | DNA-binding |
Biological process | DNA replication |
Enzyme and pathway databases
Reactomei | R-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-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-5696400, Dual Incision in GG-NER R-DME-6782135, Dual incision in TC-NER R-DME-6804114, TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest R-DME-69091, Polymerase switching R-DME-69166, Removal of the Flap Intermediate R-DME-69183, Processive synthesis on the lagging strand |
SignaLinki | P17917 |
Names & Taxonomyi
Protein namesi | Recommended name: Proliferating cell nuclear antigen1 PublicationShort name: PCNA1 Publication Alternative name(s): Cyclin1 Publication Mutagen-sensitive 209 proteinImported |
Gene namesi | ORF Names:CG9193Imported |
Organismi | Drosophila melanogaster (Fruit fly) |
Taxonomic identifieri | 7227 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Holometabola › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora › |
Proteomesi |
|
Organism-specific databases
FlyBasei | FBgn0005655, PCNA |
Subcellular locationi
Nucleus
- Nucleus 2 Publications
Other locations
- Chromosome 1 Publication
- Cytoplasm 1 Publication
Note: Colocalizes with crm in polytene nuclei during embryogenesis (PubMed:9310333). Increased association with chromatin in response to DNA damage caused by methyl methanesulfonate (MMS), hydrogen peroxide (H2O2) and UV (PubMed:17087725).2 Publications
Nucleus
- nucleus Source: FlyBase
Other locations
- chromatin Source: UniProtKB
- cytoplasm Source: UniProtKB
- PCNA complex Source: GO_Central
Keywords - Cellular componenti
Chromosome, Cytoplasm, NucleusPathology & 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000149170 | 1 – 260 | Proliferating cell nuclear antigenAdd BLAST | 260 |
Proteomic databases
PaxDbi | P17917 |
PRIDEi | P17917 |
Expressioni
Tissue specificityi
Expressed at high levels in adult ovary.1 Publication
Developmental stagei
Expressed maternally and zygotically (PubMed:1968224). Expressed at high levels in embryos at 0-2 and 8-12 h of development (PubMed:17087725, PubMed:1968224). Moderate levels detected at later stages of embryogenesis, in unfertilized eggs and adult females, and relatively low levels of expression were detected in larvae and adult males (PubMed:17087725).2 Publications
Gene expression databases
Bgeei | FBgn0005655, Expressed in embryo and 56 other tissues |
Genevisiblei | P17917, DM |
Interactioni
Subunit structurei
Homotrimer (PubMed:17087725).
Forms a complex with activator 1 heteropentamer in the presence of ATP (By similarity).
Interacts with E2f (PubMed:19081076).
Interacts with the catalytic subunits of two DNA polymerase complexes: DNApol-delta/DNApolD1 from the delta complex and DNApol-epsilon255/DNApol-epsilon from the epsilon complex (PubMed:17087725).
By similarity2 PublicationsProtein-protein interaction databases
BioGRIDi | 62946, 79 interactors |
ComplexPortali | CPX-543, PCNA homotrimer |
DIPi | DIP-20560N |
ELMi | P17917 |
IntActi | P17917, 16 interactors |
STRINGi | 7227.FBpp0085619 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P17917 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the PCNA family.Curated
Phylogenomic databases
eggNOGi | KOG1636, Eukaryota |
GeneTreei | ENSGT00390000004965 |
HOGENOMi | CLU_043978_3_0_1 |
InParanoidi | P17917 |
OMAi | EMKLINM |
OrthoDBi | 1012066at2759 |
PhylomeDBi | P17917 |
Family and domain databases
HAMAPi | MF_00317, DNApol_clamp_arch, 1 hit |
InterProi | View 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 |
Pfami | View protein in Pfam PF02747, PCNA_C, 1 hit PF00705, PCNA_N, 1 hit |
PRINTSi | PR00339, PCNACYCLIN |
TIGRFAMsi | TIGR00590, pcna, 1 hit |
PROSITEi | View protein in PROSITE PS01251, PCNA_1, 1 hit PS00293, PCNA_2, 1 hit |
i Sequence
Sequence statusi: Complete.
P17917-1 [UniParc]FASTAAdd to basket
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
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 |
PIRi | A34752 |
RefSeqi | NP_476905.1, NM_057557.4 NP_995904.1, NM_206182.2 |
Genome annotation databases
EnsemblMetazoai | FBtr0086307; FBpp0085619; FBgn0005655 FBtr0086308; FBpp0089395; FBgn0005655 |
GeneIDi | 37290 |
KEGGi | dme:Dmel_CG9193 |
Similar proteinsi
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 |
PIRi | A34752 |
RefSeqi | NP_476905.1, NM_057557.4 NP_995904.1, NM_206182.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4HK1 | X-ray | 2.00 | A | 1-260 | [»] | |
SMRi | P17917 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 62946, 79 interactors |
ComplexPortali | CPX-543, PCNA homotrimer |
DIPi | DIP-20560N |
ELMi | P17917 |
IntActi | P17917, 16 interactors |
STRINGi | 7227.FBpp0085619 |
Proteomic databases
PaxDbi | P17917 |
PRIDEi | P17917 |
Genome annotation databases
EnsemblMetazoai | FBtr0086307; FBpp0085619; FBgn0005655 FBtr0086308; FBpp0089395; FBgn0005655 |
GeneIDi | 37290 |
KEGGi | dme:Dmel_CG9193 |
Organism-specific databases
CTDi | 5111 |
FlyBasei | FBgn0005655, PCNA |
Phylogenomic databases
eggNOGi | KOG1636, Eukaryota |
GeneTreei | ENSGT00390000004965 |
HOGENOMi | CLU_043978_3_0_1 |
InParanoidi | P17917 |
OMAi | EMKLINM |
OrthoDBi | 1012066at2759 |
PhylomeDBi | P17917 |
Enzyme and pathway databases
Reactomei | R-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-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-5696400, Dual Incision in GG-NER R-DME-6782135, Dual incision in TC-NER R-DME-6804114, TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest R-DME-69091, Polymerase switching R-DME-69166, Removal of the Flap Intermediate R-DME-69183, Processive synthesis on the lagging strand |
SignaLinki | P17917 |
Miscellaneous databases
BioGRID-ORCSi | 37290, 0 hits in 1 CRISPR screen |
GenomeRNAii | 37290 |
PROi | PR:P17917 |
Gene expression databases
Bgeei | FBgn0005655, Expressed in embryo and 56 other tissues |
Genevisiblei | P17917, DM |
Family and domain databases
HAMAPi | MF_00317, DNApol_clamp_arch, 1 hit |
InterProi | View 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 |
Pfami | View protein in Pfam PF02747, PCNA_C, 1 hit PF00705, PCNA_N, 1 hit |
PRINTSi | PR00339, PCNACYCLIN |
TIGRFAMsi | TIGR00590, pcna, 1 hit |
PROSITEi | View protein in PROSITE PS01251, PCNA_1, 1 hit PS00293, PCNA_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PCNA_DROME | |
Accessioni | P17917Primary (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: | December 2, 2020 | |
This is version 176 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Drosophila annotation project |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Drosophila
Drosophila: entries, gene names and cross-references to FlyBase - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families