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O76324 (DCO_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Discs overgrown protein kinase

EC=2.7.11.1
Alternative name(s):
Protein double-time
Gene names
Name:dco
Synonyms:dbt
ORF Names:CG2048
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.6

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Forms a complex with per.

Tissue specificity

Expressed in photoreceptor cells of the eyes as well as in the region situated between the optic lobe and the central brain. Ref.2

Sequence similarities

Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processBiological rhythms
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from mutant phenotype PubMed 16824922. Source: FlyBase

behavioral response to cocaine

Inferred from mutant phenotype PubMed 10446052. Source: FlyBase

cell communication

Inferred from mutant phenotype PubMed 2373260. Source: FlyBase

circadian rhythm

Inferred from direct assay PubMed 18666831. Source: FlyBase

eclosion rhythm

Traceable author statement PubMed 12111533. Source: FlyBase

establishment of imaginal disc-derived wing hair orientation

Inferred from mutant phenotype PubMed 16824921PubMed 16824922. Source: FlyBase

establishment of ommatidial planar polarity

Inferred from mutant phenotype PubMed 16824921PubMed 16824922. Source: FlyBase

imaginal disc growth

Inferred from mutant phenotype PubMed 2373260. Source: FlyBase

locomotor rhythm

Inferred from mutant phenotype PubMed 17893330PubMed 18957703. Source: FlyBase

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 17134692. Source: FlyBase

phosphorylation

Inferred from direct assay PubMed 18666831. Source: FlyBase

positive regulation of cell division

Inferred from mutant phenotype PubMed 17134692. Source: FlyBase

positive regulation of cell growth

Inferred from mutant phenotype PubMed 17134692. Source: FlyBase

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 19364825. Source: FlyBase

positive regulation of protein catabolic process

Inferred from direct assay PubMed 17893330. Source: FlyBase

protein autophosphorylation

Inferred from direct assay PubMed 18957703. Source: FlyBase

protein phosphorylation

Inferred from direct assay PubMed 16326393PubMed 19574458. Source: FlyBase

regulation of circadian rhythm

Inferred from mutant phenotype PubMed 17893330PubMed 18957703PubMed 19139270. Source: FlyBase

regulation of protein import into nucleus

Traceable author statement PubMed 12486701. Source: FlyBase

rhythmic behavior

Traceable author statement PubMed 12486701. Source: FlyBase

sleep

Non-traceable author statement PubMed 11715043. Source: FlyBase

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 16824921PubMed 16987508PubMed 19223210. Source: FlyBase

nucleus

Inferred from direct assay PubMed 16987508PubMed 19223210. Source: FlyBase

plasma membrane

Inferred from direct assay PubMed 16824921. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

kinase activity

Inferred from mutant phenotype PubMed 16824921. Source: FlyBase

protein kinase activity

Inferred from direct assay PubMed 17893330PubMed 18957703. Source: FlyBase

protein serine/threonine kinase activity

Inferred from sequence or structural similarity Ref.1. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 440440Discs overgrown protein kinase
PRO_0000192849

Regions

Domain9 – 277269Protein kinase
Nucleotide binding15 – 239ATP By similarity
Compositional bias319 – 33214Poly-Ala
Compositional bias336 – 3394Poly-Gln
Compositional bias347 – 3515Poly-Gly
Compositional bias414 – 42613Poly-Gly
Compositional bias430 – 4378Poly-Gly

Sites

Active site1281Proton acceptor By similarity
Binding site381ATP By similarity

Amino acid modifications

Modified residue3331Phosphoserine Ref.7
Modified residue3341Phosphoserine Ref.7

Experimental info

Mutagenesis471P → S in dbtS; shortens the behavioral period.
Mutagenesis801M → I in dbtL; lengthens the behavioral period.
Sequence conflict3531A → R in AAC39134. Ref.1
Sequence conflict4281P → Q in AAC39134. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O76324 [UniParc].

Last modified August 16, 2005. Version 2.
Checksum: 0B67B83E44213902

FASTA44047,958
        10         20         30         40         50         60 
MELRVGNKYR LGRKIGSGSF GDIYLGTTIN TGEEVAIKLE CIRTKHPQLH IESKFYKTMQ 

        70         80         90        100        110        120 
GGIGIPRIIW CGSEGDYNVM VMELLGPSLE DLFNFCSRRF SLKTVLLLAD QMISRIDYIH 

       130        140        150        160        170        180 
SRDFIHRDIK PDNFLMGLGK KGNLVYIIDF GLAKKFRDAR SLKHIPYREN KNLTGTARYA 

       190        200        210        220        230        240 
SINTHLGIEQ SRRDDLESLG YVLMYFNLGA LPWQGLKAAN KRQKYERISE KKLSTSIVVL 

       250        260        270        280        290        300 
CKGFPSEFVN YLNFCRQMHF DQRPDYCHLR KLFRNLFHRL GFTYDYVFDW NLLKFGGPRN 

       310        320        330        340        350        360 
PQAIQQAQDG ADGQAGHDAV AAAAAVAAAA AASSHQQQQH KVNAALGGGG GSAAQQQLQG 

       370        380        390        400        410        420 
GQTLAMLGGN GGGNGSQLIG GNGLNMDDSM AATNSSRPPY DTPERRPSIR MRQGGGGGGG 

       430        440 
GVGVGGMPSG GGGGGVGNAK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"A Drosophila complementary DNA resource."
Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M., Harvey D.A.
Science 287:2222-2224(2000) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001263132.1. NM_001276203.1.
NP_524602.1. NM_079863.3.
NP_733414.1. NM_170535.2.
NP_733415.1. NM_170536.3.
UniGeneDm.1901.

3D structure databases

ProteinModelPortalO76324.
SMRO76324. Positions 1-296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid68523. 10 interactions.
DIPDIP-46048N.
IntActO76324. 3 interactions.
MINTMINT-774247.

Proteomic databases

PaxDbO76324.
PRIDEO76324.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0085742; FBpp0085104; FBgn0002413.
FBtr0085743; FBpp0085105; FBgn0002413.
FBtr0085744; FBpp0085106; FBgn0002413.
GeneID43673.
KEGGdme:Dmel_CG2048.

Organism-specific databases

CTD43673.
FlyBaseFBgn0002413. dco.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000110518.
HOGENOMHOG000148798.
InParanoidO76324.
KOK08960.
OMAQMISRID.
OrthoDBEOG7CZK5W.
PhylomeDBO76324.

Enzyme and pathway databases

BRENDA2.7.11.1. 1994.
SignaLinkO76324.

Gene expression databases

BgeeO76324.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSdco. drosophila.
GenomeRNAi43673.
NextBio835197.

Entry information

Entry nameDCO_DROME
AccessionPrimary (citable) accession number: O76324
Secondary accession number(s): A4V3P5, Q0KHY4, Q9V462
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 16, 2005
Last modified: April 16, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase