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P23573

- CDC2C_DROME

UniProt

P23573 - CDC2C_DROME

Protein

Cell division control protein 2 cognate

Gene

cdc2c

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 140 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    Like cdc2, could play a key role in the control of the eukaryotic cell cycle.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.
    ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei37 – 371ATPPROSITE-ProRule annotation
    Active sitei130 – 1301Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi14 – 229ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cyclin-dependent protein serine/threonine kinase activity Source: FlyBase
    3. protein binding Source: IntAct
    4. protein serine/threonine kinase activity Source: FlyBase
    5. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular process Source: FlyBase
    2. G1/S transition of mitotic cell cycle Source: FlyBase
    3. G2/M transition of mitotic cell cycle Source: FlyBase
    4. JAK-STAT cascade Source: FlyBase
    5. mitotic nuclear division Source: UniProtKB-KW
    6. protein phosphorylation Source: FlyBase
    7. regulation of cell cycle Source: GOC

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.22. 1994.
    ReactomeiREACT_104865. G2 Phase.
    REACT_180258. Factors involved in megakaryocyte development and platelet production.
    REACT_180658. G0 and Early G1.
    REACT_182058. Senescence-Associated Secretory Phenotype (SASP).
    REACT_209977. Activation of the pre-replicative complex.
    REACT_211248. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_218568. Activation of ATR in response to replication stress.
    REACT_218589. Orc1 removal from chromatin.
    REACT_224351. Regulation of APC/C activators between G1/S and early anaphase.
    SignaLinkiP23573.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cell division control protein 2 cognate (EC:2.7.11.22, EC:2.7.11.23)
    Gene namesi
    Name:cdc2c
    ORF Names:CG10498
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0004107. cdc2c.

    Subcellular locationi

    GO - Cellular componenti

    1. microtubule associated complex Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 314314Cell division control protein 2 cognatePRO_0000085744Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei18 – 181PhosphothreonineBy similarity
    Modified residuei19 – 191PhosphotyrosineBy similarity
    Modified residuei162 – 1621Phosphotyrosine1 Publication
    Modified residuei163 – 1631Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP23573.
    PRIDEiP23573.

    Expressioni

    Gene expression databases

    BgeeiP23573.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CycJQ241595EBI-95916,EBI-455799
    CycKQ961D15EBI-95916,EBI-130995
    dapP916543EBI-95916,EBI-868936

    Protein-protein interaction databases

    BioGridi67428. 50 interactions.
    DIPiDIP-648N.
    IntActiP23573. 73 interactions.
    MINTiMINT-1509625.

    Structurei

    3D structure databases

    ProteinModelPortaliP23573.
    SMRiP23573. Positions 5-290.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 287280Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00720000108415.
    InParanoidiP23573.
    KOiK02206.
    OMAiAHELIMS.
    OrthoDBiEOG7966H8.
    PhylomeDBiP23573.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 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.

    P23573-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTILDNFQR AEKIGEGTYG IVYKARSNST GQDVALKKIR LEGETEGVPS    50
    TAIREISLLK NLKHPNVVQL FDVVISGNNL YMIFEYLNMD LKKLMDKKKD 100
    VFTPQLIKSY MHQILDAVGF CHTNRILHRD LKPQNLLVDT AGKIKLADFG 150
    LARAFNVPMR AYTHEVVTLW YRAPEILLGT KFYSTGVDIW SLGCIFSEMI 200
    MRRSLFPGDS EIDQLYRIFR TLSTPDETNW PGVTQLPDFK TKFPRWEGTN 250
    MPQPITEHEA HELIMSMLCY DPNLRISAKD ALQHAYFRNV QHVDHVALPV 300
    DPNAGSASRL TRLV 314
    Length:314
    Mass (Da):35,888
    Last modified:November 1, 1991 - v1
    Checksum:i576A88767F9D35C0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271S → T(PubMed:1378625)Curated
    Sequence conflicti119 – 1191G → A(PubMed:1378625)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57486 mRNA. Translation: CAA40724.1.
    AE014297 Genomic DNA. Translation: AAN14363.1.
    AY051671 mRNA. Translation: AAK93095.1.
    PIRiE46036.
    RefSeqiNP_001163666.1. NM_001170195.2.
    NP_524420.1. NM_079696.6.
    NP_732544.1. NM_169916.3.
    UniGeneiDm.2392.

    Genome annotation databases

    EnsemblMetazoaiFBtr0083921; FBpp0083329; FBgn0004107.
    FBtr0083922; FBpp0083330; FBgn0004107.
    FBtr0300447; FBpp0289675; FBgn0004107.
    GeneIDi42453.
    KEGGidme:Dmel_CG10498.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57486 mRNA. Translation: CAA40724.1 .
    AE014297 Genomic DNA. Translation: AAN14363.1 .
    AY051671 mRNA. Translation: AAK93095.1 .
    PIRi E46036.
    RefSeqi NP_001163666.1. NM_001170195.2.
    NP_524420.1. NM_079696.6.
    NP_732544.1. NM_169916.3.
    UniGenei Dm.2392.

    3D structure databases

    ProteinModelPortali P23573.
    SMRi P23573. Positions 5-290.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 67428. 50 interactions.
    DIPi DIP-648N.
    IntActi P23573. 73 interactions.
    MINTi MINT-1509625.

    Proteomic databases

    PaxDbi P23573.
    PRIDEi P23573.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0083921 ; FBpp0083329 ; FBgn0004107 .
    FBtr0083922 ; FBpp0083330 ; FBgn0004107 .
    FBtr0300447 ; FBpp0289675 ; FBgn0004107 .
    GeneIDi 42453.
    KEGGi dme:Dmel_CG10498.

    Organism-specific databases

    CTDi 42453.
    FlyBasei FBgn0004107. cdc2c.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00720000108415.
    InParanoidi P23573.
    KOi K02206.
    OMAi AHELIMS.
    OrthoDBi EOG7966H8.
    PhylomeDBi P23573.

    Enzyme and pathway databases

    BRENDAi 2.7.11.22. 1994.
    Reactomei REACT_104865. G2 Phase.
    REACT_180258. Factors involved in megakaryocyte development and platelet production.
    REACT_180658. G0 and Early G1.
    REACT_182058. Senescence-Associated Secretory Phenotype (SASP).
    REACT_209977. Activation of the pre-replicative complex.
    REACT_211248. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_218568. Activation of ATR in response to replication stress.
    REACT_218589. Orc1 removal from chromatin.
    REACT_224351. Regulation of APC/C activators between G1/S and early anaphase.
    SignaLinki P23573.

    Miscellaneous databases

    GenomeRNAii 42453.
    NextBioi 828859.

    Gene expression databases

    Bgeei P23573.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 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. "Drosophila cdc2 homologs: a functional homolog is coexpressed with a cognate variant."
      Lehner C.F., O'Farrell P.H.
      EMBO J. 9:3573-3581(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Oregon-R.
      Tissue: Embryo.
    2. "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.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    5. "Primary structure, expression, and signal-dependent tyrosine phosphorylation of a Drosophila homolog of extracellular signal-regulated kinase."
      Biggs W.H. III, Zipursky S.L.
      Proc. Natl. Acad. Sci. U.S.A. 89:6295-6299(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 21-167.
      Tissue: Imaginal disk.
    6. "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 TYR-162 AND THR-163, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiCDC2C_DROME
    AccessioniPrimary (citable) accession number: P23573
    Secondary accession number(s): Q0KI40, Q9TXB2, Q9VDJ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 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