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Q9C9M7

- CDKD2_ARATH

UniProt

Q9C9M7 - CDKD2_ARATH

Protein

Cyclin-dependent kinase D-2

Gene

CDKD-2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Forms a stable complex with cyclin CYCH1-1 that phosphorylates human CDK2 and the C-terminal domain (CTD) of the large subunit of RNA polymerase II.2 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Activated by phosphorylation by CDKF-1. Down-regulated by phosphorylation by WEE1.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei42 – 421ATPCurated
    Active sitei135 – 1351Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi19 – 279ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW
    3. regulation of cyclin-dependent protein serine/threonine kinase activity Source: TAIR

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciARA:AT1G66750-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-dependent kinase D-2 (EC:2.7.11.22, EC:2.7.11.23)
    Short name:
    CDKD;2
    Alternative name(s):
    CDK-activating kinase 4-At
    Short name:
    CAK4-At
    Gene namesi
    Name:CDKD-2
    Ordered Locus Names:At1g66750
    ORF Names:F4N21.12
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G66750.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: TAIR
    2. nucleus Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi24 – 241Y → F: Abolishes phosphorylation by WEE1. 1 Publication
    Mutagenesisi42 – 421K → R: Prevents autophosphorylation. 1 Publication
    Mutagenesisi162 – 1621S → A: Reduces phosphorylation by CDKF-1 by 30%. 1 Publication
    Mutagenesisi168 – 1681T → A: Almost abolishes phosphorylation by CDKF-1. Loss of CTD-kinase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 348348Cyclin-dependent kinase D-2PRO_0000293120Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei24 – 241Phosphotyrosine1 Publication
    Modified residuei162 – 1621Phosphoserine; by CAK1 Publication
    Modified residuei168 – 1681Phosphothreonine; by CAK1 Publication

    Post-translational modificationi

    Phosphorylated by CDKF-1 at Ser-162 and Thr-168. Phosphorylated by WEE1 at Tyr-24. Autophosphorylated.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9C9M7.
    PRIDEiQ9C9M7.

    Expressioni

    Tissue specificityi

    Expressed in suspension cell culture, but not in plant organs.1 Publication

    Gene expression databases

    GenevestigatoriQ9C9M7.

    Interactioni

    Subunit structurei

    Interacts with CYCH1-1. Binding to CYCH1-1 activates CDK kinase.2 Publications

    Protein-protein interaction databases

    BioGridi28214. 43 interactions.
    IntActiQ9C9M7. 22 interactions.
    STRINGi3702.AT1G66750.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9C9M7.
    SMRiQ9C9M7. Positions 19-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 293281Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233024.
    InParanoidiQ9C9M7.
    KOiK02202.
    OMAiPNRINTH.
    PhylomeDBiQ9C9M7.

    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.

    Q9C9M7-1 [UniParc]FASTAAdd to Basket

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    MSKSGDNQPV DRYLRRQILG EGTYGVVYKA TDTKTGKTVA VKKIRLGNQK    50
    EGVNFTALRE IKLLKELNHP HIVELIDAFP HDGSLHLVFE YMQTDLEAVI 100
    RDRNIFLSPG DIKSYMLMTL KGLAYCHKKW VLHRDMKPNN LLIGENGLLK 150
    LADFGLARLF GSPNRRFTHQ VFATWYRAPE LLFGSRQYGA GVDVWAAGCI 200
    FAELLLRRPF LPGSTEIDQL GKIFQAFGTP VPSQWSDMIY LPDYMEFSYT 250
    PAPPLRTIFP MASDDALDLL AKMFIYDPRQ RITIQQALDH RYFSSSPSPT 300
    EPGKLQIPAS KGDALEPKAS EQNQHGNSPA VLSPPGKMRR VMGPEGFT 348
    Length:348
    Mass (Da):39,201
    Last modified:June 1, 2001 - v1
    Checksum:iA32CA3E98204DDAD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB074116 mRNA. Translation: BAB91558.1.
    AC013288 Genomic DNA. Translation: AAG60076.1.
    CP002684 Genomic DNA. Translation: AEE34551.1.
    AY136355 mRNA. Translation: AAM97021.1.
    BT000198 mRNA. Translation: AAN15517.1.
    RefSeqiNP_176847.1. NM_105345.4.
    UniGeneiAt.35737.

    Genome annotation databases

    EnsemblPlantsiAT1G66750.1; AT1G66750.1; AT1G66750.
    GeneIDi842993.
    KEGGiath:AT1G66750.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB074116 mRNA. Translation: BAB91558.1 .
    AC013288 Genomic DNA. Translation: AAG60076.1 .
    CP002684 Genomic DNA. Translation: AEE34551.1 .
    AY136355 mRNA. Translation: AAM97021.1 .
    BT000198 mRNA. Translation: AAN15517.1 .
    RefSeqi NP_176847.1. NM_105345.4.
    UniGenei At.35737.

    3D structure databases

    ProteinModelPortali Q9C9M7.
    SMRi Q9C9M7. Positions 19-308.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 28214. 43 interactions.
    IntActi Q9C9M7. 22 interactions.
    STRINGi 3702.AT1G66750.1-P.

    Proteomic databases

    PaxDbi Q9C9M7.
    PRIDEi Q9C9M7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G66750.1 ; AT1G66750.1 ; AT1G66750 .
    GeneIDi 842993.
    KEGGi ath:AT1G66750.

    Organism-specific databases

    GeneFarmi 3289. 109.
    TAIRi AT1G66750.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233024.
    InParanoidi Q9C9M7.
    KOi K02202.
    OMAi PNRINTH.
    PhylomeDBi Q9C9M7.

    Enzyme and pathway databases

    BioCyci ARA:AT1G66750-MONOMER.

    Gene expression databases

    Genevestigatori Q9C9M7.

    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. "Differential phosphorylation activities of CDK-activating kinases in Arabidopsis thaliana."
      Shimotohno A., Matsubayashi S., Yamaguchi M., Uchimiya H., Umeda M.
      FEBS Lett. 534:69-74(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Genome-wide analysis of core cell cycle genes in Arabidopsis."
      Vandepoele K., Raes J., de Veylder L., Rouze P., Rombauts S., Inze D.
      Plant Cell 14:903-916(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.
    6. "The plant-specific kinase CDKF;1 is involved in activating phosphorylation of cyclin-dependent kinase-activating kinases in Arabidopsis."
      Shimotohno A., Umeda-Hara C., Bisova K., Uchimiya H., Umeda M.
      Plant Cell 16:2954-2966(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH CYCH1-1, PHOSPHORYLATION AT SER-162 AND THR-168, MUTAGENESIS OF LYS-42; SER-162 AND THR-168.
    7. "Cell cycle regulation in plant development."
      Inze D., de Veylder L.
      Annu. Rev. Genet. 40:77-105(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    8. "Diverse phosphoregulatory mechanisms controlling cyclin-dependent kinase-activating kinases in Arabidopsis."
      Shimotohno A., Ohno R., Bisova K., Sakaguchi N., Huang J., Koncz C., Uchimiya H., Umeda M.
      Plant J. 47:701-710(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT TYR-24, INTERACTION WITH CYCH1-1, MUTAGENESIS OF TYR-24.

    Entry informationi

    Entry nameiCDKD2_ARATH
    AccessioniPrimary (citable) accession number: Q9C9M7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 10, 2007
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3