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Protein

Discs overgrown protein kinase

Gene

dco

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in circadian rhythms, viability and molecular oscillations of the clock genes period (per) and timeless (tim). Dbt reduces the stability and thus the accumulation of monomeric per proteins, probably through phosphorylation. No evident circadian oscillation is detected in head.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381ATPPROSITE-ProRule annotation
Active sitei128 – 1281Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 239ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. kinase activity Source: FlyBase
  3. protein kinase activity Source: FlyBase
  4. protein serine/threonine kinase activity Source: GO_Central

GO - Biological processi

  1. behavioral response to cocaine Source: FlyBase
  2. cell communication Source: FlyBase
  3. circadian rhythm Source: FlyBase
  4. eclosion rhythm Source: FlyBase
  5. endocytosis Source: GO_Central
  6. establishment of imaginal disc-derived wing hair orientation Source: FlyBase
  7. establishment of ommatidial planar polarity Source: FlyBase
  8. imaginal disc growth Source: FlyBase
  9. locomotor rhythm Source: FlyBase
  10. negative regulation of apoptotic process Source: FlyBase
  11. peptidyl-serine phosphorylation Source: GO_Central
  12. phosphorylation Source: FlyBase
  13. positive regulation of cell division Source: FlyBase
  14. positive regulation of cell growth Source: FlyBase
  15. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: FlyBase
  16. positive regulation of protein catabolic process Source: FlyBase
  17. protein autophosphorylation Source: FlyBase
  18. protein phosphorylation Source: FlyBase
  19. regulation of cell shape Source: GO_Central
  20. regulation of circadian rhythm Source: FlyBase
  21. regulation of protein import into nucleus Source: FlyBase
  22. rhythmic behavior Source: FlyBase
  23. sleep Source: FlyBase
  24. Wnt signaling pathway Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Biological rhythms

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 1994.
ReactomeiREACT_239233. Circadian Clock.
REACT_251367. WNT mediated activation of DVL.
SignaLinkiO76324.

Names & Taxonomyi

Protein namesi
Recommended name:
Discs overgrown protein kinase (EC:2.7.11.1)
Alternative name(s):
Protein double-time
Gene namesi
Name:dco
Synonyms:dbt
ORF Names:CG2048
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0002413. dco.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
  2. nucleus Source: FlyBase
  3. plasma membrane Source: FlyBase
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471P → S in dbtS; shortens the behavioral period. 1 Publication
Mutagenesisi80 – 801M → I in dbtL; lengthens the behavioral period. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Discs overgrown protein kinasePRO_0000192849Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei333 – 3331Phosphoserine1 Publication
Modified residuei334 – 3341Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO76324.
PRIDEiO76324.

Expressioni

Tissue specificityi

Expressed in photoreceptor cells of the eyes as well as in the region situated between the optic lobe and the central brain.1 Publication

Gene expression databases

BgeeiO76324.

Interactioni

Subunit structurei

Forms a complex with per.

Protein-protein interaction databases

BioGridi68523. 10 interactions.
DIPiDIP-46048N.
IntActiO76324. 3 interactions.
MINTiMINT-774247.

Structurei

3D structure databases

ProteinModelPortaliO76324.
SMRiO76324. Positions 1-296.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 277269Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi319 – 33214Poly-AlaAdd
BLAST
Compositional biasi336 – 3394Poly-Gln
Compositional biasi347 – 3515Poly-Gly
Compositional biasi414 – 42613Poly-GlyAdd
BLAST
Compositional biasi430 – 4378Poly-Gly

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119040.
HOGENOMiHOG000148798.
InParanoidiO76324.
KOiK08960.
OMAiMISRIDY.
OrthoDBiEOG7CZK5W.
PhylomeDBiO76324.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O76324-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELRVGNKYR LGRKIGSGSF GDIYLGTTIN TGEEVAIKLE CIRTKHPQLH
60 70 80 90 100
IESKFYKTMQ GGIGIPRIIW CGSEGDYNVM VMELLGPSLE DLFNFCSRRF
110 120 130 140 150
SLKTVLLLAD QMISRIDYIH SRDFIHRDIK PDNFLMGLGK KGNLVYIIDF
160 170 180 190 200
GLAKKFRDAR SLKHIPYREN KNLTGTARYA SINTHLGIEQ SRRDDLESLG
210 220 230 240 250
YVLMYFNLGA LPWQGLKAAN KRQKYERISE KKLSTSIVVL CKGFPSEFVN
260 270 280 290 300
YLNFCRQMHF DQRPDYCHLR KLFRNLFHRL GFTYDYVFDW NLLKFGGPRN
310 320 330 340 350
PQAIQQAQDG ADGQAGHDAV AAAAAVAAAA AASSHQQQQH KVNAALGGGG
360 370 380 390 400
GSAAQQQLQG GQTLAMLGGN GGGNGSQLIG GNGLNMDDSM AATNSSRPPY
410 420 430 440
DTPERRPSIR MRQGGGGGGG GVGVGGMPSG GGGGGVGNAK
Length:440
Mass (Da):47,958
Last modified:August 16, 2005 - v2
Checksum:i0B67B83E44213902
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti353 – 3531A → R in AAC39134 (PubMed:9674431).Curated
Sequence conflicti428 – 4281P → Q in AAC39134 (PubMed:9674431).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055583 mRNA. Translation: AAC39134.1.
AF192484 Genomic DNA. Translation: AAF27346.1.
AE014297 Genomic DNA. Translation: AAF57109.1.
AE014297 Genomic DNA. Translation: AAF57110.1.
AF132558 mRNA. Translation: AAD27857.1.
RefSeqiNP_001263132.1. NM_001276203.1.
NP_524602.1. NM_079863.3.
NP_733414.1. NM_170535.2.
NP_733415.1. NM_170536.3.
UniGeneiDm.1901.

Genome annotation databases

EnsemblMetazoaiFBtr0085742; FBpp0085104; FBgn0002413.
FBtr0085743; FBpp0085105; FBgn0002413.
FBtr0085744; FBpp0085106; FBgn0002413.
FBtr0334548; FBpp0306615; FBgn0002413.
GeneIDi43673.
KEGGidme:Dmel_CG2048.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055583 mRNA. Translation: AAC39134.1.
AF192484 Genomic DNA. Translation: AAF27346.1.
AE014297 Genomic DNA. Translation: AAF57109.1.
AE014297 Genomic DNA. Translation: AAF57110.1.
AF132558 mRNA. Translation: AAD27857.1.
RefSeqiNP_001263132.1. NM_001276203.1.
NP_524602.1. NM_079863.3.
NP_733414.1. NM_170535.2.
NP_733415.1. NM_170536.3.
UniGeneiDm.1901.

3D structure databases

ProteinModelPortaliO76324.
SMRiO76324. Positions 1-296.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68523. 10 interactions.
DIPiDIP-46048N.
IntActiO76324. 3 interactions.
MINTiMINT-774247.

Proteomic databases

PaxDbiO76324.
PRIDEiO76324.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085742; FBpp0085104; FBgn0002413.
FBtr0085743; FBpp0085105; FBgn0002413.
FBtr0085744; FBpp0085106; FBgn0002413.
FBtr0334548; FBpp0306615; FBgn0002413.
GeneIDi43673.
KEGGidme:Dmel_CG2048.

Organism-specific databases

CTDi43673.
FlyBaseiFBgn0002413. dco.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119040.
HOGENOMiHOG000148798.
InParanoidiO76324.
KOiK08960.
OMAiMISRIDY.
OrthoDBiEOG7CZK5W.
PhylomeDBiO76324.

Enzyme and pathway databases

BRENDAi2.7.11.1. 1994.
ReactomeiREACT_239233. Circadian Clock.
REACT_251367. WNT mediated activation of DVL.
SignaLinkiO76324.

Miscellaneous databases

ChiTaRSidco. fly.
GenomeRNAii43673.
NextBioi835197.

Gene expression databases

BgeeiO76324.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila clock gene double-time encodes a protein closely related to human casein kinase I epsilon."
    Kloss B., Price J.L., Saez L., Blau J., Rothenfluh A., Wesley C.S., Young M.W.
    Cell 94:97-107(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PER.
  2. "Double-time is identical to discs overgrown, which is required for cell survival, proliferation and growth arrest in Drosophila imaginal discs."
    Zilian O., Frei E., Burke R., Brentrup D., Gutjahr T., Bryant P.J., Noll M.
    Development 126:5409-5420(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. "Double-time is a novel Drosophila clock gene that regulates PERIOD protein accumulation."
    Price J.L., Blau J., Rothenfluh A., Abodeely M., Kloss B., Young M.W.
    Cell 94:83-95(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS, FUNCTION.
  7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 AND SER-334, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiDCO_DROME
AccessioniPrimary (citable) accession number: O76324
Secondary accession number(s): A4V3P5, Q0KHY4, Q9V462
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 16, 2005
Last modified: March 4, 2015
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.