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P24100 (CDKA1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-dependent kinase A-1

Short name=CDKA;1
EC=2.7.11.22
EC=2.7.11.23
Alternative name(s):
Cell division control protein 2 homolog A
Gene names
Name:CDKA-1
Synonyms:CDC2, CDC2A
Ordered Locus Names:At3g48750
ORF Names:T21J18.20
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.21 Ref.40 Ref.44

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

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

Enzyme regulation

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. Ref.33 Ref.35 Ref.41

Subunit structure

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. Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.36 Ref.37 Ref.38 Ref.39 Ref.41 Ref.42 Ref.43

Subcellular location

Cytoplasm. Nucleus. Note: Mainly cytoplasmic. Nuclear distribution increases after binding to ICK1/KRP1. Ref.36 Ref.42

Tissue specificity

Expressed in roots, stems, flowers and siliques. Ref.11

Developmental stage

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. Ref.11 Ref.18

Induction

By nematode infection in roots. Down-regulated by salt stress in root meristem and replication blocking agents (hydroxyurea and aphidicolin). Ref.12 Ref.19 Ref.33 Ref.35 Ref.41 Ref.43

Post-translational modification

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. Ref.41 Ref.43 Ref.44

Disruption phenotype

Plants display lethal male gametophyte. Ref.40

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Sequence caution

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.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA endoreduplication

Inferred from mutant phenotype Ref.33. Source: TAIR

asymmetric cell division

Inferred from genetic interaction PubMed 23104828. Source: TAIR

embryo development ending in seed dormancy

Inferred from mutant phenotype Ref.40. Source: TAIR

gametophyte development

Inferred from mutant phenotype PubMed 17764501. Source: TAIR

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

pollen development

Inferred from mutant phenotype PubMed 16311592. Source: TAIR

positive regulation of cell proliferation

Inferred from mutant phenotype Ref.40. Source: TAIR

regulation of meiosis

Inferred from mutant phenotype Ref.44. Source: TAIR

response to cold

Inferred from expression pattern PubMed 8570631. Source: TAIR

   Cellular_componentcortical microtubule, transverse to long axis

Inferred from direct assay PubMed 9428718. Source: TAIR

cytoplasm

Inferred from direct assay PubMed 20018602. Source: TAIR

cytosol

Inferred from direct assay Ref.45. Source: TAIR

nucleus

Inferred from direct assay Ref.45PubMed 20018602. Source: TAIR

plasma membrane

Inferred from direct assay PubMed 17317660. Source: TAIR

preprophase band

Traceable author statement PubMed 9428718. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

cyclin-dependent protein serine/threonine kinase activity

Inferred from sequence or structural similarity Ref.1. Source: TAIR

kinase activity

Inferred from mutant phenotype Ref.44. Source: TAIR

protein kinase activity

Inferred from direct assay PubMed 16920782. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 294294Cyclin-dependent kinase A-1
PRO_0000085749

Regions

Domain4 – 287284Protein kinase
Nucleotide binding10 – 189ATP By similarity

Sites

Active site1271Proton acceptor By similarity
Binding site331ATP By similarity

Amino acid modifications

Modified residue151Phosphotyrosine Ref.41
Modified residue1611Phosphothreonine Ref.44 Ref.45

Experimental info

Mutagenesis141T → A: Increased kinase activity; when associated with F-15. Ref.16
Mutagenesis151Y → F: Abolishes phosphorylation by WEE1. Increased kinase activity; when associated with A-14. Ref.16 Ref.41
Mutagenesis1461D → N: Decreased kinase activity and disturbed cell cycle. Reduced frequency of cell division during embryo development. Ref.16 Ref.21
Mutagenesis1561P → L: Decreased kinase activity and disturbed cell cycle. Ref.16
Mutagenesis1611T → D: Strong reduction in kinase activity and ability to bind substrate. Strong reduction in plant growth. Sterile plants. Ref.44
Mutagenesis1611T → V: Strong reduction in kinase activity and ability to bind substrate. Ref.44
Mutagenesis1661T → I: Decreased kinase activity and disturbed cell cycle. Ref.16
Mutagenesis234 – 2363Missing: No change in kinase activity, but disturbed cell cycle. Loss of interaction with CKS1. Ref.16

Sequences

Sequence LengthMass (Da)Tools
P24100 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: B5FAE55FA9EC366E

FASTA29434,030
        10         20         30         40         50         60 
MDQYEKVEKI GEGTYGVVYK ARDKVTNETI ALKKIRLEQE DEGVPSTAIR EISLLKEMQH 

        70         80         90        100        110        120 
SNIVKLQDVV HSEKRLYLVF EYLDLDLKKH MDSTPDFSKD LHMIKTYLYQ ILRGIAYCHS 

       130        140        150        160        170        180 
HRVLHRDLKP QNLLIDRRTN SLKLADFGLA RAFGIPVRTF THEVVTLWYR APEILLGSHH 

       190        200        210        220        230        240 
YSTPVDIWSV GCIFAEMISQ KPLFPGDSEI DQLFKIFRIM GTPYEDTWRG VTSLPDYKSA 

       250        260        270        280        290 
FPKWKPTDLE TFVPNLDPDG VDLLSKMLLM DPTKRINARA ALEHEYFKDL GGMP 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"Functional analysis of cyclin-dependent kinase inhibitors of Arabidopsis."
de Veylder L., Beeckman T., Beemster G.T.S., Krols L., Terras F., Landrieu I., van der Schueren E., Maes S., Naudts M., Inze D.
Plant Cell 13:1653-1667(2001) [PubMed] [Europe PMC] [Abstract]
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]"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis."
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.
J. Proteome Res. 7:2458-2470(2008) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS23095.
T49271.
RefSeqNP_566911.1. NM_114734.3.
UniGeneAt.24166.

3D structure databases

ProteinModelPortalP24100.
SMRP24100. Positions 13-290.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid9354. 103 interactions.
IntActP24100. 73 interactions.

Proteomic databases

PaxDbP24100.
PRIDEP24100.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G48750.1; AT3G48750.1; AT3G48750.
GeneID824036.
KEGGath:AT3G48750.

Organism-specific databases

GeneFarm2945. 106.
TAIRAT3G48750.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
InParanoidP24100.
KOK02206.
OMARGIKHCH.
PhylomeDBP24100.
ProtClustDBPLN00009.

Enzyme and pathway databases

BioCycARA:AT3G48750-MONOMER.
BRENDA2.7.11.22. 399.

Gene expression databases

GenevestigatorP24100.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCDKA1_ARATH
AccessionPrimary (citable) accession number: P24100
Secondary accession number(s): Q29Q50, Q8RX68, Q9M307
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: April 16, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names