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Q9LMT0

- CDKD3_ARATH

UniProt

Q9LMT0 - CDKD3_ARATH

Protein

Cyclin-dependent kinase D-3

Gene

CDKD-3

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 106 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    May form 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-1.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei41 – 411ATPCurated
    Active sitei134 – 1341Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi18 – 269ATPPROSITE-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 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 cell cycle 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:AT1G18040-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-dependent kinase D-3 (EC:2.7.11.22, EC:2.7.11.23)
    Short name:
    CDKD;3
    Alternative name(s):
    CDK-activating kinase 2-At
    Short name:
    CAK2-At
    Gene namesi
    Name:CDKD-3
    Ordered Locus Names:At1g18040
    ORF Names:T10F20.5, T10O22.1
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G18040.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: TAIR

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi23 – 231Y → F: Abolishes phosphorylation by WEE1. 1 Publication
    Mutagenesisi41 – 411K → R: Prevents autophosphorylation. 1 Publication
    Mutagenesisi161 – 1611S → A: Reduces phosphorylation by CDKF-1 by 20%. Abolishes phosphorylation by CDKF-1; when associated with A-167. 1 Publication
    Mutagenesisi167 – 1671T → A: Reduces phosphorylation by CDKF-1 by 80%. Abolishes phosphorylation by CDKF-1; when associated with A-161. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 391391Cyclin-dependent kinase D-3PRO_0000293121Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei23 – 231Phosphotyrosine1 Publication
    Modified residuei161 – 1611Phosphoserine; by CAK1 Publication
    Modified residuei167 – 1671Phosphothreonine; by CAK1 Publication

    Post-translational modificationi

    Phosphorylated by CDKF-1 at Ser-161 and Thr-167. Phosphorylated at Tyr-23 by WEE1. Autophosphorylated.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ9LMT0.

    Expressioni

    Tissue specificityi

    Expressed in roots, shoots and suspension cell culture.1 Publication

    Gene expression databases

    GenevestigatoriQ9LMT0.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi23623. 32 interactions.
    IntActiQ9LMT0. 6 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LMT0.
    SMRiQ9LMT0. Positions 12-350.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 292281Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233024.
    InParanoidiQ9LMT0.
    KOiK02202.
    OMAiCHRNWIL.
    PhylomeDBiQ9LMT0.

    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.

    Q9LMT0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPEQPKKVAD RYLKQEVLGQ GTYGVVFKAT DTKTEQTVAI KKIRLGKQRE    50
    GVNITALREI KMLKELKHPH IILLIDAFPH KENLHLVFEF METDLEAVIR 100
    DSNIFLSPAD IKSYLLMTFK GLAYCHDKWV LHRDMKPNNL LIGVDGQLKL 150
    ADFGLARIFG SPNRKFTHQV FARWYRAPEL LFGAKQYGAA VDVWAVACIF 200
    AELLLRRPFL QGNSDIDQLS KIFAAFGTPK ADQWPDLTKL PDYVEYQFVP 250
    APSLRSLFPA VSDDALDLLS KMFTYDPKAR ISIKQALEHR YFTSAPAPTD 300
    PAKLPKPVPK QDGKSSYGKH EAITVQSPPR KLRRVMPERG RVDSLKSHVD 350
    KDQQAPMSLD FTILAERPPN RPTITSADRS HLKRKLDLEF Q 391
    Length:391
    Mass (Da):44,530
    Last modified:October 1, 2000 - v1
    Checksum:i3FD4A2293283B656
    GO

    Sequence cautioni

    The sequence AAF78394.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB047274 mRNA. Translation: BAB62843.1.
    AC034107 Genomic DNA. Translation: AAF97821.1.
    AC069551 Genomic DNA. Translation: AAF78394.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE29667.1.
    AY099677 mRNA. Translation: AAM20528.1.
    AY128857 mRNA. Translation: AAM91257.1.
    PIRiH86315.
    RefSeqiNP_173244.1. NM_101666.2.
    UniGeneiAt.14957.
    At.26247.

    Genome annotation databases

    EnsemblPlantsiAT1G18040.1; AT1G18040.1; AT1G18040.
    GeneIDi838384.
    KEGGiath:AT1G18040.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB047274 mRNA. Translation: BAB62843.1 .
    AC034107 Genomic DNA. Translation: AAF97821.1 .
    AC069551 Genomic DNA. Translation: AAF78394.1 . Sequence problems.
    CP002684 Genomic DNA. Translation: AEE29667.1 .
    AY099677 mRNA. Translation: AAM20528.1 .
    AY128857 mRNA. Translation: AAM91257.1 .
    PIRi H86315.
    RefSeqi NP_173244.1. NM_101666.2.
    UniGenei At.14957.
    At.26247.

    3D structure databases

    ProteinModelPortali Q9LMT0.
    SMRi Q9LMT0. Positions 12-350.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 23623. 32 interactions.
    IntActi Q9LMT0. 6 interactions.

    Proteomic databases

    PRIDEi Q9LMT0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G18040.1 ; AT1G18040.1 ; AT1G18040 .
    GeneIDi 838384.
    KEGGi ath:AT1G18040.

    Organism-specific databases

    GeneFarmi 3292. 109.
    TAIRi AT1G18040.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233024.
    InParanoidi Q9LMT0.
    KOi K02202.
    OMAi CHRNWIL.
    PhylomeDBi Q9LMT0.

    Enzyme and pathway databases

    BioCyci ARA:AT1G18040-MONOMER.

    Gene expression databases

    Genevestigatori Q9LMT0.

    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-161 AND THR-167, MUTAGENESIS OF LYS-41; SER-161 AND THR-167.
    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, PHOSPHORYLATION AT TYR-23, INTERACTION WITH CYCH1-1, MUTAGENESIS OF TYR-23.

    Entry informationi

    Entry nameiCDKD3_ARATH
    AccessioniPrimary (citable) accession number: Q9LMT0
    Secondary accession number(s): Q9LM42
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 10, 2007
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 106 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