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O76324

- DCO_DROME

UniProt

O76324 - DCO_DROME

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
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (16 Aug 2005)
      Previous versions | rss
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    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 binding Source: FlyBase
    4. protein kinase activity Source: FlyBase
    5. 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

    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

    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.
    GeneTreeiENSGT00730000110518.
    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

    MELRVGNKYR LGRKIGSGSF GDIYLGTTIN TGEEVAIKLE CIRTKHPQLH    50
    IESKFYKTMQ GGIGIPRIIW CGSEGDYNVM VMELLGPSLE DLFNFCSRRF 100
    SLKTVLLLAD QMISRIDYIH SRDFIHRDIK PDNFLMGLGK KGNLVYIIDF 150
    GLAKKFRDAR SLKHIPYREN KNLTGTARYA SINTHLGIEQ SRRDDLESLG 200
    YVLMYFNLGA LPWQGLKAAN KRQKYERISE KKLSTSIVVL CKGFPSEFVN 250
    YLNFCRQMHF DQRPDYCHLR KLFRNLFHRL GFTYDYVFDW NLLKFGGPRN 300
    PQAIQQAQDG ADGQAGHDAV AAAAAVAAAA AASSHQQQQH KVNAALGGGG 350
    GSAAQQQLQG GQTLAMLGGN GGGNGSQLIG GNGLNMDDSM AATNSSRPPY 400
    DTPERRPSIR MRQGGGGGGG GVGVGGMPSG GGGGGVGNAK 440
    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 ENSGT00730000110518.
    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

    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 1, 2014
    This is version 117 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