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O76324

- DCO_DROME

UniProt

O76324 - DCO_DROME

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Protein

Discs overgrown protein kinase

Gene

dco

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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: FlyBase

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. establishment of imaginal disc-derived wing hair orientation Source: FlyBase
  6. establishment of ommatidial planar polarity Source: FlyBase
  7. imaginal disc growth Source: FlyBase
  8. locomotor rhythm Source: FlyBase
  9. negative regulation of apoptotic process Source: FlyBase
  10. phosphorylation Source: FlyBase
  11. positive regulation of cell division Source: FlyBase
  12. positive regulation of cell growth Source: FlyBase
  13. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: FlyBase
  14. positive regulation of protein catabolic process Source: FlyBase
  15. protein autophosphorylation Source: FlyBase
  16. protein phosphorylation Source: FlyBase
  17. regulation of circadian rhythm Source: FlyBase
  18. regulation of protein import into nucleus Source: FlyBase
  19. rhythmic behavior Source: FlyBase
  20. sleep Source: FlyBase
  21. 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.
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.
OMAiLTARHDQ.
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:
EMBL
GenBank
DDBJ
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.
GeneIDi43673.
KEGGidme:Dmel_CG2048.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
RefSeqi NP_001263132.1. NM_001276203.1.
NP_524602.1. NM_079863.3.
NP_733414.1. NM_170535.2.
NP_733415.1. NM_170536.3.
UniGenei Dm.1901.

3D structure databases

ProteinModelPortali O76324.
SMRi O76324. Positions 1-296.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 68523. 10 interactions.
DIPi DIP-46048N.
IntActi O76324. 3 interactions.
MINTi MINT-774247.

Proteomic databases

PaxDbi O76324.
PRIDEi O76324.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0085742 ; FBpp0085104 ; FBgn0002413 .
FBtr0085743 ; FBpp0085105 ; FBgn0002413 .
FBtr0085744 ; FBpp0085106 ; FBgn0002413 .
GeneIDi 43673.
KEGGi dme:Dmel_CG2048.

Organism-specific databases

CTDi 43673.
FlyBasei FBgn0002413. dco.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119040.
HOGENOMi HOG000148798.
InParanoidi O76324.
KOi K08960.
OMAi LTARHDQ.
OrthoDBi EOG7CZK5W.
PhylomeDBi O76324.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 1994.
SignaLinki O76324.

Miscellaneous databases

ChiTaRSi dco. drosophila.
GenomeRNAii 43673.
NextBioi 835197.

Gene expression databases

Bgeei O76324.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 118 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