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O80345

- CDKF1_ARATH

UniProt

O80345 - CDKF1_ARATH

Protein

Cyclin-dependent kinase F-1

Gene

CDKF-1

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 107 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    CDK-activating kinase that modulates CDKD-2 and CDKD-3 activities by phosphorylation of the T-loop. Activates CDKD-2 C-terminal domain (CTD) kinase activity. Activates CDKA-1 probably by phosphorylation. Posseses a CDK kinase activity independently of association with cyclin CYCH1-1. Phosphorylates the CTD of the large subunit of RNA polymerase II.3 Publications

    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 sitei50 – 501ATPPROSITE-ProRule annotation
    Active sitei146 – 1461Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi27 – 359ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cyclin-dependent protein kinase activating kinase activity Source: TAIR
    3. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
    4. protein binding Source: TAIR
    5. protein serine/threonine kinase activity Source: TAIR
    6. 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. maintenance of root meristem identity Source: TAIR
    4. positive regulation of protein kinase activity Source: GOC
    5. protein phosphorylation Source: TAIR
    6. 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:AT4G28980-MONOMER.
    ARA:GQT-608-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-dependent kinase F-1 (EC:2.7.11.22, EC:2.7.11.23)
    Short name:
    CDKF;1
    Alternative name(s):
    CDK-activating kinase 1-At
    Short name:
    CAK1-At
    Gene namesi
    Name:CDKF-1
    Synonyms:CAK1
    Ordered Locus Names:At4g28980
    ORF Names:F19B15.10
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G28980.

    Subcellular locationi

    GO - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi50 – 501K → A: No effect on CDKA-1 activation. 1 Publication
    Mutagenesisi290 – 2901T → A: Abolishes CDKA-1 activation and kinase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 479479Cyclin-dependent kinase F-1PRO_0000293123Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei32 – 321PhosphotyrosineBy similarity
    Modified residuei179 – 1791Phosphoserine1 Publication
    Modified residuei247 – 2471Phosphoserine1 Publication
    Modified residuei290 – 2901PhosphothreonineCurated

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO80345.
    PRIDEiO80345.

    Expressioni

    Tissue specificityi

    Highly expressed in suspension cell culture. Expressed at low levels in all plant organs.1 Publication

    Gene expression databases

    GenevestigatoriO80345.

    Interactioni

    Protein-protein interaction databases

    BioGridi14306. 28 interactions.
    IntActiO80345. 5 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliO80345.
    SMRiO80345. Positions 14-426.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 418398Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233024.
    InParanoidiO80345.
    OMAiVDACHRN.
    PhylomeDBiO80345.

    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. 2 hits.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O80345-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDKQPATSWS IHTRPEIIAK YEIFERVGSG AYADVYRARR LSDGLIVALK    50
    EIFDYQSAFR EIDALTILNG SPNVVVMHEY FWREEENAVL VLEFLRSDLA 100
    AVIRDGKRKK KVEGGDGFSV GEIKRWMIQI LTGVDACHRN LIVHRDLKPG 150
    NMLISDDGVL KLADFGQARI LMEHDIVASD ENQQAYKLED KDGETSEPPE 200
    VIPDYENSPR QGSDGQEREA MSKDEYFRQV EELKAKQVVR DDTDKDSNVH 250
    DGDISCLATC TVSEMDDDLG RNSFSYDADE AVDDTQGLMT SCVGTRWFRP 300
    PELLYGSTMY GLEVDLWSLG CVFAELLSLE PLFPGISDID QISRVTNVLG 350
    NLNEEVWPGC VDLPDYKSIS FAKVESPLGI EGCLPNHSGD VISLLKKLIC 400
    YDPASRATTM EMLNDKYLSE EPLPVPVSEL YVPPTMSGPD EDSPRKWNDY 450
    REMDSDSDFD GFGPMNVKPT SSGFTIEFP 479
    Length:479
    Mass (Da):53,752
    Last modified:November 1, 1998 - v1
    Checksum:iCA08BF178B7CC831
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB009399 mRNA. Translation: BAA28775.1.
    AL078470 Genomic DNA. Translation: CAB43912.1.
    AL161574 Genomic DNA. Translation: CAB79656.1.
    CP002687 Genomic DNA. Translation: AEE85567.1.
    CP002687 Genomic DNA. Translation: AEE85568.1.
    AY042816 mRNA. Translation: AAK68756.1.
    AY064627 mRNA. Translation: AAL47340.1.
    PIRiT08953.
    RefSeqiNP_194627.1. NM_119042.4.
    NP_849468.1. NM_179137.2.
    UniGeneiAt.19673.

    Genome annotation databases

    EnsemblPlantsiAT4G28980.1; AT4G28980.1; AT4G28980.
    AT4G28980.2; AT4G28980.2; AT4G28980.
    GeneIDi829019.
    KEGGiath:AT4G28980.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB009399 mRNA. Translation: BAA28775.1 .
    AL078470 Genomic DNA. Translation: CAB43912.1 .
    AL161574 Genomic DNA. Translation: CAB79656.1 .
    CP002687 Genomic DNA. Translation: AEE85567.1 .
    CP002687 Genomic DNA. Translation: AEE85568.1 .
    AY042816 mRNA. Translation: AAK68756.1 .
    AY064627 mRNA. Translation: AAL47340.1 .
    PIRi T08953.
    RefSeqi NP_194627.1. NM_119042.4.
    NP_849468.1. NM_179137.2.
    UniGenei At.19673.

    3D structure databases

    ProteinModelPortali O80345.
    SMRi O80345. Positions 14-426.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 14306. 28 interactions.
    IntActi O80345. 5 interactions.

    Proteomic databases

    PaxDbi O80345.
    PRIDEi O80345.

    Protocols and materials databases

    DNASUi 829019.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G28980.1 ; AT4G28980.1 ; AT4G28980 .
    AT4G28980.2 ; AT4G28980.2 ; AT4G28980 .
    GeneIDi 829019.
    KEGGi ath:AT4G28980.

    Organism-specific databases

    GeneFarmi 3296. 111.
    TAIRi AT4G28980.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233024.
    InParanoidi O80345.
    OMAi VDACHRN.
    PhylomeDBi O80345.

    Enzyme and pathway databases

    BioCyci ARA:AT4G28980-MONOMER.
    ARA:GQT-608-MONOMER.

    Gene expression databases

    Genevestigatori O80345.

    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. 2 hits.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    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. "A distinct cyclin-dependent kinase-activating kinase of Arabidopsis thaliana."
      Umeda M., Bhalerao R.P., Schell J., Uchimiya H., Koncz C.
      Proc. Natl. Acad. Sci. U.S.A. 95:5021-5026(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Strain: cv. Columbia.
    2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [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. "Comparison of Cak1p-like cyclin-dependent kinase-activating kinases."
      Tsakraklides V., Solomon M.J.
      J. Biol. Chem. 277:33482-33489(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-50.
    6. "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.
    7. "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.
    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, MUTAGENESIS OF THR-290.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Root.
    10. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
      Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
      Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCDKF1_ARATH
    AccessioniPrimary (citable) accession number: O80345
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 10, 2007
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 107 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