[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Columbia; DOI=10.1016/0378-1119(91)90146-3; PubMed=1937013 [NCBI, ExPASy, EBI, Israel, Japan] Hirayama T., Imajuku Y., Anai T., Matsui M., Oka A.; "Identification of two cell-cycle-controlling cdc2 gene homologs in Arabidopsis thaliana."; Gene 105:159-165(1991).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Columbia; DOI=10.1105/tpc.3.5.531; PubMed=1840925 [NCBI, ExPASy, EBI, Israel, Japan] Ferreira P.C.G., Hemerly A.S., Villarroel R., van Montagu M., Inze D.; "The Arabidopsis functional homolog of the p34cdc2 protein kinase."; Plant Cell 3:531-540(1991).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Columbia; PubMed=1634002 [NCBI, ExPASy, EBI, Israel, Japan] Inze D., Ferreira P.C.G., Hemerly A.S., van Montagu M.; "Control of cell division in plants."; Biochem. Soc. Trans. 20:80-84(1992).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. Columbia; DOI=10.1016/0014-5793(92)80592-5; PubMed=1618302 [NCBI, ExPASy, EBI, Israel, Japan] Imajuku Y., Hirayama T., Endoh H., Oka A.; "Exon-intron organization of the Arabidopsis thaliana protein kinase genes CDC2a and CDC2b."; FEBS Lett. 304:73-77(1992).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Columbia; DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."; Nature 408:820-822(2000).
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=cv. Columbia; DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Empirical analysis of transcriptional activity in the Arabidopsis genome."; Science 302:842-846(2003).
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=cv. Columbia; Shinn P., Chen H., Kim C.J., Ecker J.R.; "Arabidopsis ORF clones."; Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=cv. Columbia; 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.; "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[9]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.; "Full-length cDNA from Arabidopsis thaliana."; Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[10]	TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. PubMed=8893539 [NCBI, ExPASy, EBI, Israel, Japan] Segers G., Gadisseur I., Bergounioux C., de Almeida Engler J., Jacqmard A., van Montagu M., Inze D.; "The Arabidopsis cyclin-dependent kinase gene cdc2bAt is preferentially expressed during S and G2 phases of the cell cycle."; Plant J. 10:601-612(1996).
[11]	INDUCTION. PubMed=9011085 [NCBI, ExPASy, EBI, Israel, Japan] Niebel A., de Almeida Engler J., Hemerly A.S., Ferreira P.C.G., Inze D., van Montagu M., Gheysen G.; "Induction of cdc2a and cyc1At expression in Arabidopsis thaliana during early phases of nematode-induced feeding cell formation."; Plant J. 10:1037-1043(1996).
[12]	INTERACTION WITH CKS1. DOI=10.1016/S0014-5793(97)00822-3; PubMed=9276444 [NCBI, ExPASy, EBI, Israel, Japan] de Veylder L., Segers G., Glab N., Casteels P., van Montagu M., Inze D.; "The Arabidopsis Cks1At protein binds the cyclin-dependent kinases Cdc2aAt and Cdc2bAt."; FEBS Lett. 412:446-452(1997).
[13]	INTERACTION WITH KRP1/ICK1. DOI=10.1038/386451a0; PubMed=9087400 [NCBI, ExPASy, EBI, Israel, Japan] Wang H., Fowke L.C., Crosby W.L.; "A plant cyclin-dependent kinase inhibitor gene."; Nature 386:451-452(1997).
[14]	INTERACTION WITH KRP1/ICK1 AND CYCD3-1. PubMed=9753775 [NCBI, ExPASy, EBI, Israel, Japan] Wang H., Qi Q., Schorr P., Cutler A.J., Crosby W.L., Fowke L.C.; "ICK1, a cyclin-dependent protein kinase inhibitor from Arabidopsis thaliana interacts with both Cdc2a and CycD3, and its expression is induced by abscisic acid."; Plant J. 15:501-510(1998).
[15]	INTERACTION WITH CKS1 AND CYCD1-1, AND MUTAGENESIS OF THR-14; TYR-15; ASP-146; PRO-156; THR-166 AND 234-LEU--ASP-236. DOI=10.1016/S0014-5793(99)00211-2; PubMed=10100639 [NCBI, ExPASy, EBI, Israel, Japan] Porceddu A., de Veylder L., Hayles J., van Montagu M., Inze D., Mironov V.; "Mutational analysis of two Arabidopsis thaliana cyclin-dependent kinases in fission yeast."; FEBS Lett. 446:182-188(1999).
[16]	INTERACTION WITH CYCD4-1. DOI=10.1007/s004250050582; PubMed=10420643 [NCBI, ExPASy, EBI, Israel, Japan] de Veylder L., de Almeida Engler J., Burssens S., Manevski A., Lescure B., van Montagu M., Engler G., Inze D.; "A new D-type cyclin of Arabidopsis thaliana expressed during lateral root primordia formation."; Planta 208:453-462(1999).
[17]	DEVELOPMENTAL STAGE. DOI=10.1105/tpc.11.10.1883; PubMed=10521519 [NCBI, ExPASy, EBI, Israel, Japan] Yoshizumi T., Nagata N., Shimada H., Matsui M.; "An Arabidopsis cell cycle-dependent kinase-related gene, CDC2b, plays a role in regulating seedling growth in darkness."; Plant Cell 11:1883-1896(1999).
[18]	INDUCTION. DOI=10.1007/s004250000334; PubMed=11089675 [NCBI, ExPASy, EBI, Israel, Japan] Burssens S., Himanen K., van de Cotte B., Beeckman T., van Montagu M., Inze D., Verbruggen N.; "Expression of cell cycle regulatory genes and morphological alterations in response to salt stress in Arabidopsis thaliana."; Planta 211:632-640(2000).
[19]	INTERACTION WITH KRP2/ICK2. PubMed=10758489 [NCBI, ExPASy, EBI, Israel, Japan] Lui H., Wang H., Delong C., Fowke L.C., Crosby W.L., Fobert P.R.; "The Arabidopsis Cdc2a-interacting protein ICK2 is structurally related to ICK1 and is a potent inhibitor of cyclin-dependent kinase activity in vitro."; Plant J. 21:379-385(2000).
[20]	FUNCTION, AND MUTAGENESIS OF ASP-146. PubMed=10929107 [NCBI, ExPASy, EBI, Israel, Japan] Hemerly A.S., Ferreira P.C.G., van Montagu M., Engler G., Inze D.; "Cell division events are essential for embryo patterning and morphogenesis: studies on dominant-negative cdc2aAt mutants of Arabidopsis."; Plant J. 23:123-130(2000).
[21]	INTERACTION WITH CYCD2-1 AND CYCD3-1. DOI=10.1074/jbc.M009074200; PubMed=11096103 [NCBI, ExPASy, EBI, Israel, Japan] Healy J.M.S., Menges M., Doonan J.H., Murray J.A.H.; "The Arabidopsis D-type cyclins CycD2 and CycD3 both interact in vivo with the PSTAIRE cyclin-dependent kinase Cdc2a but are differentially controlled."; J. Biol. Chem. 276:7041-7047(2001).
[22]	INTERACTION WITH KRP1/ICK1; KRP2/ICK2; KRP3/ICK6; KRP4/ICK7; KRP6/ICK4 AND KRP7/ICK5. DOI=10.1105/tpc.13.7.1653; PubMed=11449057 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Functional analysis of cyclin-dependent kinase inhibitors of Arabidopsis."; Plant Cell 13:1653-1667(2001).
[23]	INTERACTION WITH CKS1. PubMed=11319029 [NCBI, ExPASy, EBI, Israel, Japan] de Veylder L., Beemster G.T.S., Beeckman T., Inze D.; "CKS1At overexpression in Arabidopsis thaliana inhibits growth by reducing meristem size and inhibiting cell-cycle progression."; Plant J. 25:617-626(2001).
[24]	INTERACTION WITH CYCD2-1. PubMed=11722776 [NCBI, ExPASy, EBI, Israel, Japan] Boniotti M.B., Gutierrez C.; "A cell-cycle-regulated kinase activity phosphorylates plant retinoblastoma protein and contains, in Arabidopsis, a CDKA/cyclin D complex."; Plant J. 28:341-350(2001).
[25]	GENE FAMILY, AND NOMENCLATURE. DOI=10.1105/tpc.010445; PubMed=11971144 [NCBI, ExPASy, EBI, Israel, Japan] Vandepoele K., Raes J., de Veylder L., Rouze P., Rombauts S., Inze D.; "Genome-wide analysis of core cell cycle genes in Arabidopsis."; Plant Cell 14:903-916(2002).
[26]	INTERACTION WITH KRP1/ICK1. DOI=10.1105/tpc.008342; PubMed=12566574 [NCBI, ExPASy, EBI, Israel, Japan] Schnittger A., Weinl C., Bouyer D., Schoebinger U., Huelskamp M.; "Misexpression of the cyclin-dependent kinase inhibitor ICK1/KRP1 in single-celled Arabidopsis trichomes reduces endoreduplication and cell size and induces cell death."; Plant Cell 15:303-315(2003).
[27]	INTERACTION WITH CYCD4-1. DOI=10.1104/pp.103.020644; PubMed=12857813 [NCBI, ExPASy, EBI, Israel, Japan] Kono A., Umeda-Hara C., Lee J., Ito M., Uchimiya H., Umeda M.; "Arabidopsis D-type cyclin CYCD4;1 is a novel cyclin partner of B2-type cyclin-dependent kinase."; Plant Physiol. 132:1315-1321(2003).
[28]	INTERACTION WITH TIF4A-1/EIF4A-1. DOI=10.1016/S0014-5793(03)01382-6; PubMed=14706832 [NCBI, ExPASy, EBI, Israel, Japan] Hutchins A.P., Roberts G.R., Lloyd C.W., Doonan J.H.; "In vivo interaction between CDKA and eIF4A: a possible mechanism linking translation and cell proliferation."; FEBS Lett. 556:91-94(2004).
[29]	INTERACTION WITH CYCU1-1; CYCU2-1; CYCU2-2; CYCU3-1; CYCU4-1; CYCU4-2 AND CYCU4-3. DOI=10.1007/s00018-004-4057-4; PubMed=15197472 [NCBI, ExPASy, EBI, Israel, Japan] Torres Acosta J.A., de Almeida Engler J., Raes J., Magyar Z., de Groodt R., Inze D., de Veylder L.; "Molecular characterization of Arabidopsis PHO80-like proteins, a novel class of CDKA;1-interacting cyclins."; Cell. Mol. Life Sci. 61:1485-1497(2004).
[30]	INTERACTION WITH CYCH1-1. DOI=10.1105/tpc.104.025601; PubMed=15486101 [NCBI, ExPASy, EBI, Israel, Japan] Shimotohno A., Umeda-Hara C., Bisova K., Uchimiya H., Umeda M.; "The plant-specific kinase CDKF;1 is involved in activating phosphorylation of cyclin-dependent kinase-activating kinases in Arabidopsis."; Plant Cell 16:2954-2966(2004).
[31]	ENZYME REGULATION, AND INTERACTION WITH KRP2/ICK2. DOI=10.1105/tpc.105.032383; PubMed=15863515 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "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."; Plant Cell 17:1723-1736(2005).
[32]	REVIEW. DOI=10.1146/annurev.genet.40.110405.090431; PubMed=17094738 [NCBI, ExPASy, EBI, Israel, Japan] Inze D., de Veylder L.; "Cell cycle regulation in plant development."; Annu. Rev. Genet. 40:77-105(2006).
[33]	ENZYME REGULATION. DOI=10.1016/j.febslet.2005.12.018; PubMed=16376885 [NCBI, ExPASy, EBI, Israel, Japan] Nakai T., Kato K., Shinmyo A., Sekine M.; "Arabidopsis KRPs have distinct inhibitory activity toward cyclin D2-associated kinases, including plant-specific B-type cyclin-dependent kinase."; FEBS Lett. 580:336-340(2006).
[34]	SUBCELLULAR LOCATION, AND INTERACTION WITH CYCA2-3. DOI=10.1105/tpc.105.037309; PubMed=16415207 [NCBI, ExPASy, EBI, Israel, Japan] Imai K.K., Ohashi Y., Tsuge T., Yoshizumi T., Matsui M., Oka A., Aoyama T.; "The A-type cyclin CYCA2;3 is a key regulator of ploidy levels in Arabidopsis endoreduplication."; Plant Cell 18:382-396(2006).
[35]	INTERACTION WITH CYCD3-1. DOI=10.1105/tpc.105.039636; PubMed=16517759 [NCBI, ExPASy, EBI, Israel, Japan] Menges M., Samland A.K., Planchais S., Murray J.A.H.; "The D-type cyclin CYCD3;1 is limiting for the G1-to-S-phase transition in Arabidopsis."; Plant Cell 18:893-906(2006).
[36]	INTERACTION WITH CYCD4-2. DOI=10.1007/s00299-005-0075-4; PubMed=16408177 [NCBI, ExPASy, EBI, Israel, Japan] Kono A., Ohno R., Umeda-Hara C., Uchimiya H., Umeda M.; "A distinct type of cyclin D, CYCD4;2, involved in the activation of cell division in Arabidopsis."; Plant Cell Rep. 25:540-545(2006).
[37]	FUNCTION. DOI=10.1111/j.1365-313X.2005.02643.x; PubMed=16460514 [NCBI, ExPASy, EBI, Israel, Japan] Iwakawa H., Shinmyo A., Sekine M.; "Arabidopsis CDKA;1, a cdc2 homologue, controls proliferation of generative cells in male gametogenesis."; Plant J. 45:819-831(2006).
[38]	ENZYME REGULATION, PHOSPHORYLATION, INTERACTION WITH CYCH1-1, AND MUTAGENESIS OF TYR-15. DOI=10.1111/j.1365-313X.2006.02820.x; PubMed=16856985 [NCBI, ExPASy, EBI, Israel, Japan] Shimotohno A., Ohno R., Bisova K., Sakaguchi N., Huang J., Koncz C., Uchimiya H., Umeda M.; "Diverse phosphoregulatory mechanisms controlling cyclin-dependent kinase-activating kinases in Arabidopsis."; Plant J. 47:701-710(2006).
[39]	SUBCELLULAR LOCATION, AND INTERACTION WITH KRP1/ICK1. DOI=10.1007/s11103-006-9019-9; PubMed=16845478 [NCBI, ExPASy, EBI, Israel, Japan] Zhou Y., Niu H., Brandizzi F., Fowke L.C., Wang H.; "Molecular control of nuclear and subnuclear targeting of the plant CDK inhibitor ICK1 and ICK1-mediated nuclear transport of CDKA."; Plant Mol. Biol. 62:261-278(2006).
[40]	INDUCTION, PHOSPHORYLATION, AND INTERACTION WITH WEE1. DOI=10.1105/tpc.106.045047; PubMed=17209125 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Arabidopsis WEE1 kinase controls cell cycle arrest in response to activation of the DNA integrity checkpoint."; Plant Cell 19:211-225(2007).
[41]	FUNCTION, PHOSPHORYLATION AT THR-161, AND MUTAGENESIS OF THR-161. DOI=10.1105/tpc.107.050401; PubMed=17369369 [NCBI, ExPASy, EBI, Israel, Japan] Dissmeyer N., Nowack M.K., Pusch S., Stals H., Inze D., Grini P.E., Schnittger A.; "T-loop phosphorylation of Arabidopsis CDKA;1 is required for its function and can be partially substituted by an aspartate residue."; Plant Cell 19:972-985(2007).

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.
CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CATALYTIC ACTIVITY: 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.
SUBUNIT: Interacts with 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.
INTERACTION:
Q8LF80:CDKB2-1; NbExp=2; IntAct=EBI-371713, EBI-1253579;
O23249:CKS1; NbExp=5; IntAct=EBI-371713, EBI-1253127;
P61024:CKS1B (xeno); NbExp=1; IntAct=EBI-371713, EBI-456371;
P42753:CYCD3-1; NbExp=1; IntAct=EBI-371713, EBI-1253610;
Q9LJ45:CYCU1-1; NbExp=1; IntAct=EBI-371713, EBI-1773749;
Q9SHD3:CYCU2-1; NbExp=1; IntAct=EBI-371713, EBI-1773781;
O80513:CYCU4-1; NbExp=1; IntAct=EBI-371713, EBI-1773819;
Q9FKF6:CYCU4-3; NbExp=1; IntAct=EBI-371713, EBI-1773829;
Q67Y93:KRP1; NbExp=7; IntAct=EBI-371713, EBI-1636730;
Q9SCR2:KRP2; NbExp=4; IntAct=EBI-371713, EBI-1636748;
Q9FKB5:KRP3; NbExp=3; IntAct=EBI-371713, EBI-1773302;
Q9LRY0:KRP5; NbExp=2; IntAct=EBI-371713, EBI-1636764;
P08463:suc1 (xeno); NbExp=1; IntAct=EBI-371713, EBI-1104317;
Q9LZ78:T32M21_70; NbExp=1; IntAct=EBI-371713, EBI-1774363;
P41376:TIF4A-1; NbExp=1; IntAct=EBI-371713, EBI-371706;
Q9FQ25:TON1a; NbExp=1; IntAct=EBI-371713, EBI-1266493;
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly cytoplasmic. Nuclear distribution increases after binding to ICK1/KRP1.
TISSUE SPECIFICITY: Expressed in roots, stems, flowers and siliques.
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.
INDUCTION: By nematode infection in roots. Down-regulated by salt stress in root meristem and replication blocking agents (hydroxyurea and aphidicolin).
PTM: Phosphorylated at Tyr-15 by WEE1. Phosphorylation at Thr-161 is important for the kinase activity and substrate binding.
MISCELLANEOUS: Plants lacking CDKA-1 display lethal male gametophyte.
SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.
SIMILARITY: Contains 1 protein kinase domain.
SEQUENCE CAUTION:
- Sequence=AAL91258.1; Type=Frameshift; Positions=285;
- Sequence=CAB87903.1; Type=Erroneous gene model prediction;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M59198; AAA32831.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S45387; AAB23643.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X57839; CAA40971.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D10850; BAA01623.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL132963; CAB87903.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY090353; AAL91258.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT024706; ABD59044.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK226373; BAE98520.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY085153; AAM61706.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S23095; S23095.
T49271; T49271.

RefSeq

NP_566911.1; -.

UniGene

At.24166

3D structure databases

HSSP

P24941; 1P2A. [HSSP ENTRY / PDB]

ModBase

P24100.

Protein-protein interaction databases

IntAct

P24100; -.

Organism-specific databases

GeneFarm

2945; 106.

TAIR

At3g48750; -.

Gene expression databases

ArrayExpress

P24100; -.

GermOnline

AT3G48750; Arabidopsis thaliana.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.

Family and domain databases

InterPro

IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.

Pfam

PF00069; Pkinase; 1.
Pfam graphical view of domain structure.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00220; S_TKc; 1.
SMART graphical view of domain structure.

PROSITE

PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P24100.

Genome annotation databases

GeneID

824036; -.

GenomeReviews

BA000014_GR; AT3G48750.

KEGG

ath:AT3G48750; -.

NMPDR

fig|3702.1.peg.16115; -.

Other

ProtoNet

P24100.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cell cycle; Cell division; Complete proteome; Cytoplasm; Kinase; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Serine/threonine-protein kinase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 294`	`294`	`Cyclin-dependent kinase A-1.`	`PRO_0000085749`
`DOMAIN`	`4 287`	`284`	`Protein kinase.`
`NP_BIND`	`10 18`	`9`	`ATP (By similarity).`
`ACT_SITE`	`127 127`		`Proton acceptor (By similarity).`
`BINDING`	`33 33`		`ATP (By similarity).`
`MOD_RES`	`14 14`		`Phosphothreonine (By similarity).`
`MOD_RES`	`15 15`		`Phosphotyrosine.`
`MOD_RES`	`161 161`		`Phosphothreonine.`
`MUTAGEN`	`14 14`		`T->A: Increased kinase activity; when associated with F-15.`
`MUTAGEN`	`15 15`		`Y->F: Abolishes phosphorylation by WEE1. Increased kinase activity; when associated with A-14.`
`MUTAGEN`	`146 146`		`D->N: Decreased kinase activity and disturbed cell cycle. Reduced frequency of cell division during embryo development.`
`MUTAGEN`	`156 156`		`P->L: Decreased kinase activity and disturbed cell cycle.`
`MUTAGEN`	`161 161`		`T->D: Strong reduction in kinase activity and ability to bind substrate. Strong reduction in plant growth. Sterile plants.`
`MUTAGEN`	`161 161`		`T->V: Strong reduction in kinase activity and ability to bind substrate.`
`MUTAGEN`	`166 166`		`T->I: Decreased kinase activity and disturbed cell cycle.`
`MUTAGEN`	`234 236`		`Missing: No change in kinase activity, but disturbed cell cycle. Loss of intercation with CKS1.`

Sequence information

Length: 294 AA [This is the length of the unprocessed precursor]

Molecular weight: 34030 Da [This is the MW of the unprocessed precursor]

CRC64: B5FAE55FA9EC366E [This is a checksum on the sequence]

        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

P24100 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools