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P24100

- CDKA1_ARATH

UniProt

P24100 - CDKA1_ARATH

Protein

Cyclin-dependent kinase A-1

Gene

CDKA-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 134 (01 Oct 2014)
      Sequence version 1 (01 Mar 1992)
      Previous versions | rss
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    Functioni

    Involved in the control of the cell cycle. Essential for both G1/S and G2/M (mitosis) phase transitions. Functions in cell morphogenesis as well as cell proliferation. Required for cell division (entry into mitosis) of the generative cell in male gametogenesis.3 Publications

    Catalytic activityi

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

    Enzyme regulationi

    CDK kinase activated by CDKF-1. CDK kinase activity inhibited by KRP1/ICK1, KRP2/ICK2, KRP3/ICK6, KRP4/ICK7, KRP5/ICK3, KRP6/ICK4 and KRP7/ICK5. Down-regulated by phosphorylation by WEE1.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei33 – 331ATPPROSITE-ProRule annotation
    Active sitei127 – 1271Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 189ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. asymmetric cell division Source: TAIR
    2. DNA endoreduplication Source: TAIR
    3. embryo development ending in seed dormancy Source: TAIR
    4. gametophyte development Source: TAIR
    5. mitotic nuclear division Source: UniProtKB-KW
    6. pollen development Source: TAIR
    7. positive regulation of cell proliferation Source: TAIR
    8. regulation of meiosis Source: TAIR
    9. response to cold Source: TAIR

    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

    BioCyciARA:AT3G48750-MONOMER.
    BRENDAi2.7.11.22. 399.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-dependent kinase A-1 (EC:2.7.11.22, EC:2.7.11.23)
    Short name:
    CDKA;1
    Alternative name(s):
    Cell division control protein 2 homolog A
    Gene namesi
    Name:CDKA-1
    Synonyms:CDC2, CDC2A
    Ordered Locus Names:At3g48750
    ORF Names:T21J18.20
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G48750.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Mainly cytoplasmic. Nuclear distribution increases after binding to ICK1/KRP1.

    GO - Cellular componenti

    1. cortical microtubule, transverse to long axis Source: TAIR
    2. cytoplasm Source: TAIR
    3. cytosol Source: TAIR
    4. nucleus Source: TAIR
    5. plasma membrane Source: TAIR
    6. preprophase band Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Plants display lethal male gametophyte.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141T → A: Increased kinase activity; when associated with F-15. 1 Publication
    Mutagenesisi15 – 151Y → F: Abolishes phosphorylation by WEE1. Increased kinase activity; when associated with A-14. 2 Publications
    Mutagenesisi146 – 1461D → N: Decreased kinase activity and disturbed cell cycle. Reduced frequency of cell division during embryo development. 2 Publications
    Mutagenesisi156 – 1561P → L: Decreased kinase activity and disturbed cell cycle. 1 Publication
    Mutagenesisi161 – 1611T → D: Strong reduction in kinase activity and ability to bind substrate. Strong reduction in plant growth. Sterile plants. 1 Publication
    Mutagenesisi161 – 1611T → V: Strong reduction in kinase activity and ability to bind substrate. 1 Publication
    Mutagenesisi166 – 1661T → I: Decreased kinase activity and disturbed cell cycle. 1 Publication
    Mutagenesisi234 – 2363Missing: No change in kinase activity, but disturbed cell cycle. Loss of interaction with CKS1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 294294Cyclin-dependent kinase A-1PRO_0000085749Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei15 – 151Phosphotyrosine2 Publications
    Modified residuei161 – 1611Phosphothreonine3 Publications

    Post-translational modificationi

    Phosphorylated at Tyr-15 by WEE1. Phosphorylation at Thr-161 is important for the kinase activity and substrate binding. Binding to the anti-phosphatase PAS2 prevents dephosphorylation.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP24100.
    PRIDEiP24100.

    Expressioni

    Tissue specificityi

    Expressed in roots, stems, flowers and siliques.1 Publication

    Developmental stagei

    Expressed throughout the cell cycle. Expressed in actively dividing cells: root and shoot apical meristems, leaf primordia and emerging lateral root meristem. Expressed in light-grown seedlings from 1 up to 7 days after germination with a peak at 2 and 3 days.2 Publications

    Inductioni

    By nematode infection in roots. Down-regulated by salt stress in root meristem and replication blocking agents (hydroxyurea and aphidicolin).3 Publications

    Gene expression databases

    GenevestigatoriP24100.

    Interactioni

    Subunit structurei

    Interacts with CDT1A, CYCA2-3, CYCD2-1, CYCD3-1, CYCD4-1, CYCD4-2, CYCH1-1, CYCU1-1, CYCU2-1, CYCU2-2, CYCU3-1, CYCU4-1, CYCU4-2, CYCU4-3, CKS1, KRP2/ICK2, KRP3/ICK6, KRP4/ICK7, KRP6/ICK4, KRP7/ICK5, and C-terminal domain of KRP1/ICK1. Interacts with WEE1 and TIF4A-1/EIF4A-1. Interacts with PAS2; when phosphorylated at Tyr-15.24 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CKS1O232499EBI-371713,EBI-1253127
    CYCD2-1P427524EBI-371713,EBI-1253160
    CYCD3-1P427535EBI-371713,EBI-1253610
    CYCD4-1Q8LGA14EBI-371713,EBI-1253202
    CYCU1-1Q9LJ452EBI-371713,EBI-1773749
    CYCU4-1O805132EBI-371713,EBI-1773819
    CYCU4-3Q9FKF62EBI-371713,EBI-1773829
    KRP1Q67Y9310EBI-371713,EBI-1636730
    KRP2Q9SCR26EBI-371713,EBI-1636748
    KRP3Q9FKB54EBI-371713,EBI-1773302
    KRP4Q8GYJ34EBI-371713,EBI-1253225
    KRP5Q9LRY03EBI-371713,EBI-1636764
    KRP6Q0WNX93EBI-371713,EBI-1253171
    KRP7Q94CL93EBI-371713,EBI-1773344
    TIF4A-1P413762EBI-371713,EBI-371706

    Protein-protein interaction databases

    BioGridi9354. 103 interactions.
    IntActiP24100. 73 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP24100.
    SMRiP24100. Positions 13-290.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 287284Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233024.
    InParanoidiP24100.
    KOiK02206.
    OMAiKSAFPRW.
    PhylomeDBiP24100.

    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.

    P24100-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDQYEKVEKI GEGTYGVVYK ARDKVTNETI ALKKIRLEQE DEGVPSTAIR    50
    EISLLKEMQH SNIVKLQDVV HSEKRLYLVF EYLDLDLKKH MDSTPDFSKD 100
    LHMIKTYLYQ ILRGIAYCHS HRVLHRDLKP QNLLIDRRTN SLKLADFGLA 150
    RAFGIPVRTF THEVVTLWYR APEILLGSHH YSTPVDIWSV GCIFAEMISQ 200
    KPLFPGDSEI DQLFKIFRIM GTPYEDTWRG VTSLPDYKSA FPKWKPTDLE 250
    TFVPNLDPDG VDLLSKMLLM DPTKRINARA ALEHEYFKDL GGMP 294
    Length:294
    Mass (Da):34,030
    Last modified:March 1, 1992 - v1
    Checksum:iB5FAE55FA9EC366E
    GO

    Sequence cautioni

    The sequence AAL91258.1 differs from that shown. Reason: Frameshift at position 285.
    The sequence CAB87903.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59198 mRNA. Translation: AAA32831.1.
    S45387 mRNA. Translation: AAB23643.1.
    X57839 mRNA. Translation: CAA40971.1.
    D10850 Genomic DNA. Translation: BAA01623.1.
    AL132963 Genomic DNA. Translation: CAB87903.1. Sequence problems.
    CP002686 Genomic DNA. Translation: AEE78452.1.
    AY090353 mRNA. Translation: AAL91258.1. Frameshift.
    BT024706 mRNA. Translation: ABD59044.1.
    AK226373 mRNA. Translation: BAE98520.1.
    AY085153 mRNA. Translation: AAM61706.1.
    PIRiS23095.
    T49271.
    RefSeqiNP_566911.1. NM_114734.3.
    UniGeneiAt.24166.

    Genome annotation databases

    EnsemblPlantsiAT3G48750.1; AT3G48750.1; AT3G48750.
    GeneIDi824036.
    KEGGiath:AT3G48750.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59198 mRNA. Translation: AAA32831.1 .
    S45387 mRNA. Translation: AAB23643.1 .
    X57839 mRNA. Translation: CAA40971.1 .
    D10850 Genomic DNA. Translation: BAA01623.1 .
    AL132963 Genomic DNA. Translation: CAB87903.1 . Sequence problems.
    CP002686 Genomic DNA. Translation: AEE78452.1 .
    AY090353 mRNA. Translation: AAL91258.1 . Frameshift.
    BT024706 mRNA. Translation: ABD59044.1 .
    AK226373 mRNA. Translation: BAE98520.1 .
    AY085153 mRNA. Translation: AAM61706.1 .
    PIRi S23095.
    T49271.
    RefSeqi NP_566911.1. NM_114734.3.
    UniGenei At.24166.

    3D structure databases

    ProteinModelPortali P24100.
    SMRi P24100. Positions 13-290.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 9354. 103 interactions.
    IntActi P24100. 73 interactions.

    Proteomic databases

    PaxDbi P24100.
    PRIDEi P24100.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G48750.1 ; AT3G48750.1 ; AT3G48750 .
    GeneIDi 824036.
    KEGGi ath:AT3G48750.

    Organism-specific databases

    GeneFarmi 2945. 106.
    TAIRi AT3G48750.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233024.
    InParanoidi P24100.
    KOi K02206.
    OMAi KSAFPRW.
    PhylomeDBi P24100.

    Enzyme and pathway databases

    BioCyci ARA:AT3G48750-MONOMER.
    BRENDAi 2.7.11.22. 399.

    Gene expression databases

    Genevestigatori P24100.

    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. "Identification of two cell-cycle-controlling cdc2 gene homologs in Arabidopsis thaliana."
      Hirayama T., Imajuku Y., Anai T., Matsui M., Oka A.
      Gene 105:159-165(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
    2. "The Arabidopsis functional homolog of the p34cdc2 protein kinase."
      Ferreira P.C.G., Hemerly A.S., Villarroel R., van Montagu M., Inze D.
      Plant Cell 3:531-540(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
    3. "Control of cell division in plants."
      Inze D., Ferreira P.C.G., Hemerly A.S., van Montagu M.
      Biochem. Soc. Trans. 20:80-84(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
    4. "Exon-intron organization of the Arabidopsis thaliana protein kinase genes CDC2a and CDC2b."
      Imajuku Y., Hirayama T., Endoh H., Oka A.
      FEBS Lett. 304:73-77(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Columbia.
    5. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    6. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    7. "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.
    8. "Arabidopsis ORF clones."
      Shinn P., Chen H., Kim C.J., Ecker J.R.
      Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    9. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    10. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    11. "The Arabidopsis cyclin-dependent kinase gene cdc2bAt is preferentially expressed during S and G2 phases of the cell cycle."
      Segers G., Gadisseur I., Bergounioux C., de Almeida Engler J., Jacqmard A., van Montagu M., Inze D.
      Plant J. 10:601-612(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    12. "Induction of cdc2a and cyc1At expression in Arabidopsis thaliana during early phases of nematode-induced feeding cell formation."
      Niebel A., de Almeida Engler J., Hemerly A.S., Ferreira P.C.G., Inze D., van Montagu M., Gheysen G.
      Plant J. 10:1037-1043(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    13. "The Arabidopsis Cks1At protein binds the cyclin-dependent kinases Cdc2aAt and Cdc2bAt."
      de Veylder L., Segers G., Glab N., Casteels P., van Montagu M., Inze D.
      FEBS Lett. 412:446-452(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CKS1.
    14. "A plant cyclin-dependent kinase inhibitor gene."
      Wang H., Fowke L.C., Crosby W.L.
      Nature 386:451-452(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KRP1/ICK1.
    15. "ICK1, a cyclin-dependent protein kinase inhibitor from Arabidopsis thaliana interacts with both Cdc2a and CycD3, and its expression is induced by abscisic acid."
      Wang H., Qi Q., Schorr P., Cutler A.J., Crosby W.L., Fowke L.C.
      Plant J. 15:501-510(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KRP1/ICK1 AND CYCD3-1.
    16. "Mutational analysis of two Arabidopsis thaliana cyclin-dependent kinases in fission yeast."
      Porceddu A., de Veylder L., Hayles J., van Montagu M., Inze D., Mironov V.
      FEBS Lett. 446:182-188(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CKS1 AND CYCD1-1, MUTAGENESIS OF THR-14; TYR-15; ASP-146; PRO-156; THR-166 AND 234-LEU--ASP-236.
    17. "A new D-type cyclin of Arabidopsis thaliana expressed during lateral root primordia formation."
      de Veylder L., de Almeida Engler J., Burssens S., Manevski A., Lescure B., van Montagu M., Engler G., Inze D.
      Planta 208:453-462(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CYCD4-1.
    18. "An Arabidopsis cell cycle-dependent kinase-related gene, CDC2b, plays a role in regulating seedling growth in darkness."
      Yoshizumi T., Nagata N., Shimada H., Matsui M.
      Plant Cell 11:1883-1896(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    19. "Expression of cell cycle regulatory genes and morphological alterations in response to salt stress in Arabidopsis thaliana."
      Burssens S., Himanen K., van de Cotte B., Beeckman T., van Montagu M., Inze D., Verbruggen N.
      Planta 211:632-640(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    20. "The Arabidopsis Cdc2a-interacting protein ICK2 is structurally related to ICK1 and is a potent inhibitor of cyclin-dependent kinase activity in vitro."
      Lui H., Wang H., Delong C., Fowke L.C., Crosby W.L., Fobert P.R.
      Plant J. 21:379-385(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KRP2/ICK2.
    21. "Cell division events are essential for embryo patterning and morphogenesis: studies on dominant-negative cdc2aAt mutants of Arabidopsis."
      Hemerly A.S., Ferreira P.C.G., van Montagu M., Engler G., Inze D.
      Plant J. 23:123-130(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-146.
    22. "The Arabidopsis D-type cyclins CycD2 and CycD3 both interact in vivo with the PSTAIRE cyclin-dependent kinase Cdc2a but are differentially controlled."
      Healy J.M.S., Menges M., Doonan J.H., Murray J.A.H.
      J. Biol. Chem. 276:7041-7047(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CYCD2-1 AND CYCD3-1.
    23. Cited for: INTERACTION WITH KRP1/ICK1; KRP2/ICK2; KRP3/ICK6; KRP4/ICK7; KRP6/ICK4 AND KRP7/ICK5.
    24. "CKS1At overexpression in Arabidopsis thaliana inhibits growth by reducing meristem size and inhibiting cell-cycle progression."
      de Veylder L., Beemster G.T.S., Beeckman T., Inze D.
      Plant J. 25:617-626(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CKS1.
    25. "A cell-cycle-regulated kinase activity phosphorylates plant retinoblastoma protein and contains, in Arabidopsis, a CDKA/cyclin D complex."
      Boniotti M.B., Gutierrez C.
      Plant J. 28:341-350(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CYCD2-1.
    26. "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.
    27. "Misexpression of the cyclin-dependent kinase inhibitor ICK1/KRP1 in single-celled Arabidopsis trichomes reduces endoreduplication and cell size and induces cell death."
      Schnittger A., Weinl C., Bouyer D., Schoebinger U., Huelskamp M.
      Plant Cell 15:303-315(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KRP1/ICK1.
    28. "Arabidopsis D-type cyclin CYCD4;1 is a novel cyclin partner of B2-type cyclin-dependent kinase."
      Kono A., Umeda-Hara C., Lee J., Ito M., Uchimiya H., Umeda M.
      Plant Physiol. 132:1315-1321(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CYCD4-1.
    29. "In vivo interaction between CDKA and eIF4A: a possible mechanism linking translation and cell proliferation."
      Hutchins A.P., Roberts G.R., Lloyd C.W., Doonan J.H.
      FEBS Lett. 556:91-94(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIF4A-1/EIF4A-1.
    30. "Molecular characterization of Arabidopsis PHO80-like proteins, a novel class of CDKA;1-interacting cyclins."
      Torres Acosta J.A., de Almeida Engler J., Raes J., Magyar Z., de Groodt R., Inze D., de Veylder L.
      Cell. Mol. Life Sci. 61:1485-1497(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CYCU1-1; CYCU2-1; CYCU2-2; CYCU3-1; CYCU4-1; CYCU4-2 AND CYCU4-3.
    31. "DNA replication licensing affects cell proliferation or endoreplication in a cell type-specific manner."
      del Mar Castellano M., Boniotti M.B., Caro E., Schnittger A., Gutierrez C.
      Plant Cell 16:2380-2393(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDT1A.
      Strain: cv. Columbia.
    32. "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: INTERACTION WITH CYCH1-1.
    33. "The cyclin-dependent kinase inhibitor KRP2 controls the onset of the endoreduplication cycle during Arabidopsis leaf development through inhibition of mitotic CDKA;1 kinase complexes."
      Verkest A., de Oliveira Manes C.L., Vercruysse S., Maes S., van der Schueren E., Beeckman T., Genschik P., Kuiper M., Inze D., de Veylder L.
      Plant Cell 17:1723-1736(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, INTERACTION WITH KRP2/ICK2.
    34. "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.
    35. "Arabidopsis KRPs have distinct inhibitory activity toward cyclin D2-associated kinases, including plant-specific B-type cyclin-dependent kinase."
      Nakai T., Kato K., Shinmyo A., Sekine M.
      FEBS Lett. 580:336-340(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    36. "The A-type cyclin CYCA2;3 is a key regulator of ploidy levels in Arabidopsis endoreduplication."
      Imai K.K., Ohashi Y., Tsuge T., Yoshizumi T., Matsui M., Oka A., Aoyama T.
      Plant Cell 18:382-396(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CYCA2-3.
    37. "The D-type cyclin CYCD3;1 is limiting for the G1-to-S-phase transition in Arabidopsis."
      Menges M., Samland A.K., Planchais S., Murray J.A.H.
      Plant Cell 18:893-906(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CYCD3-1.
    38. "Arabidopsis PASTICCINO2 is an antiphosphatase involved in regulation of cyclin-dependent kinase A."
      Da Costa M., Bach L., Landrieu I., Bellec Y., Catrice O., Brown S., De Veylder L., Lippens G., Inze D., Faure J.-D.
      Plant Cell 18:1426-1437(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAS2.
    39. "A distinct type of cyclin D, CYCD4;2, involved in the activation of cell division in Arabidopsis."
      Kono A., Ohno R., Umeda-Hara C., Uchimiya H., Umeda M.
      Plant Cell Rep. 25:540-545(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CYCD4-2.
    40. "Arabidopsis CDKA;1, a cdc2 homologue, controls proliferation of generative cells in male gametogenesis."
      Iwakawa H., Shinmyo A., Sekine M.
      Plant J. 45:819-831(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    41. "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: ENZYME REGULATION, PHOSPHORYLATION AT TYR-15, INTERACTION WITH CYCH1-1, MUTAGENESIS OF TYR-15.
    42. "Molecular control of nuclear and subnuclear targeting of the plant CDK inhibitor ICK1 and ICK1-mediated nuclear transport of CDKA."
      Zhou Y., Niu H., Brandizzi F., Fowke L.C., Wang H.
      Plant Mol. Biol. 62:261-278(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH KRP1/ICK1.
    43. "Arabidopsis WEE1 kinase controls cell cycle arrest in response to activation of the DNA integrity checkpoint."
      de Schutter K., Joubes J., Cools T., Verkest A., Corellou F., Babiychuk E., van der Schueren E., Beeckman T., Kushnir S., Inze D., de Veylder L.
      Plant Cell 19:211-225(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, PHOSPHORYLATION, INTERACTION WITH WEE1.
    44. "T-loop phosphorylation of Arabidopsis CDKA;1 is required for its function and can be partially substituted by an aspartate residue."
      Dissmeyer N., Nowack M.K., Pusch S., Stals H., Inze D., Grini P.E., Schnittger A.
      Plant Cell 19:972-985(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-161, MUTAGENESIS OF THR-161.
    45. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Root.
    46. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
      Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
      J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: cv. Columbia.
    47. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCDKA1_ARATH
    AccessioniPrimary (citable) accession number: P24100
    Secondary accession number(s): Q29Q50, Q8RX68, Q9M307
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: March 1, 1992
    Last modified: October 1, 2014
    This is version 134 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