Cyclin-dependent kinase A-1 - Arabidopsis thaliana (Mouse-ear cress)

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P24100 (CDKA1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 120. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	294 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA endoreduplication Inferred from mutant phenotype Ref.33. Source: TAIR asymmetric cell division Inferred from genetic interaction PubMed 23104828. Source: TAIR cytokinesis Inferred from mutant phenotype PubMed 7664733. Source: TAIR embryo development ending in seed dormancy Inferred from mutant phenotype Ref.40. 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_component	cortical microtubule, transverse to long axis Inferred from direct assay PubMed 9428718. Source: TAIR cytosol Inferred from direct assay Ref.45. Source: TAIR nucleus Inferred from direct assay Ref.45 PubMed 20018602. Source: TAIR plasma membrane Inferred from direct assay PubMed 17317660. Source: TAIR preprophase band Traceable author statement PubMed 9428718. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II carboxy-terminal domain kinase activity Inferred from electronic annotation. Source: EC cyclin-dependent protein serine/threonine kinase activity Inferred from sequence or structural similarity Ref.1. Source: TAIR
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
CKS1	O23249	9	EBI-371713,EBI-1253127
CYCD2-1	P42752	4	EBI-371713,EBI-1253160
CYCD3-1	P42753	5	EBI-371713,EBI-1253610
CYCD4-1	Q8LGA1	4	EBI-371713,EBI-1253202
CYCU1-1	Q9LJ45	2	EBI-371713,EBI-1773749
CYCU4-1	O80513	2	EBI-371713,EBI-1773819
CYCU4-3	Q9FKF6	2	EBI-371713,EBI-1773829
KRP1	Q67Y93	10	EBI-371713,EBI-1636730
KRP2	Q9SCR2	6	EBI-371713,EBI-1636748
KRP3	Q9FKB5	4	EBI-371713,EBI-1773302
KRP4	Q8GYJ3	4	EBI-371713,EBI-1253225
KRP5	Q9LRY0	3	EBI-371713,EBI-1636764
KRP6	Q0WNX9	3	EBI-371713,EBI-1253171
KRP7	Q94CL9	3	EBI-371713,EBI-1773344
TIF4A-1	P41376	2	EBI-371713,EBI-371706

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 294

294

Cyclin-dependent kinase A-1

PRO_0000085749

Regions

Domain

4 – 287

284

Protein kinase

Nucleotide binding

10 – 18

ATP By similarity

Sites

Active site

127

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphotyrosine

Modified residue

161

Phosphothreonine Ref.44 Ref.45

Experimental info

Mutagenesis

T → A: Increased kinase activity; when associated with F-15. Ref.16

Mutagenesis

Y → F: Abolishes phosphorylation by WEE1. Increased kinase activity; when associated with A-14. Ref.16 Ref.41

Mutagenesis

146

D → N: Decreased kinase activity and disturbed cell cycle. Reduced frequency of cell division during embryo development. Ref.16 Ref.21

Mutagenesis

156

P → L: Decreased kinase activity and disturbed cell cycle. Ref.16

Mutagenesis

161

T → D: Strong reduction in kinase activity and ability to bind substrate. Strong reduction in plant growth. Sterile plants. Ref.44

Mutagenesis

161

T → V: Strong reduction in kinase activity and ability to bind substrate. Ref.44

Mutagenesis

166

T → I: Decreased kinase activity and disturbed cell cycle. Ref.16

Mutagenesis

234 – 236

Missing: No change in kinase activity, but disturbed cell cycle. Loss of interaction with CKS1. Ref.16

Sequences

Sequence

Length

Mass (Da)

Tools

P24100 [UniParc].

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

FASTA

294

34,030

        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' referencesShow '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. 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. 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. 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, 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, MASS SPECTROMETRY. Tissue: Root.
+	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.
IPI	IPI00521649.
PIR	S23095. T49271.
RefSeq	NP_566911.1. NM_114734.3.
UniGene	At.24166.
3D structure databases
ProteinModelPortal	P24100.
SMR	P24100. Positions 13-290.
ModBase	Search...
Protein-protein interaction databases
IntAct	P24100. 73 interactions.
Proteomic databases
PaxDb	P24100.
PRIDE	P24100.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G48750.1; AT3G48750.1; AT3G48750.
GeneID	824036.
KEGG	ath:AT3G48750.
Organism-specific databases
GeneFarm	2945. 106.
TAIR	At3g48750.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233024.
InParanoid	P24100.
KO	K02206.
OMA	PYFSSTE.
PhylomeDB	P24100.
ProtClustDB	PLN00009.
Enzyme and pathway databases
BRENDA	2.7.11.22. 399.
Gene expression databases
Genevestigator	P24100.
GermOnline	AT3G48750. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CDKA1_ARATH

Accession

Primary (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:	May 1, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents