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Cyclin-dependent kinase A-1 (CDKA;1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog A)

 CDKA1_ARATH             Reviewed;         294 AA.
P24100; Q29Q50; Q8RX68; Q9M307;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 1.
22-NOV-2017, entry version 161.
RecName: Full=Cyclin-dependent kinase A-1;
Short=CDKA;1;
EC=2.7.11.22;
EC=2.7.11.23;
AltName: Full=Cell division control protein 2 homolog A;
Name=CDKA-1; Synonyms=CDC2, CDC2A; OrderedLocusNames=At3g48750;
ORFNames=T21J18.20;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
PubMed=1937013; DOI=10.1016/0378-1119(91)90146-3;
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;
PubMed=1840925; DOI=10.1105/tpc.3.5.531;
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; DOI=10.1042/bst0200080;
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;
PubMed=1618302; DOI=10.1016/0014-5793(92)80592-5;
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;
PubMed=11130713; DOI=10.1038/35048706;
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]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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).
[8]
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.
[9]
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.
[10]
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.
[11]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=8893539; DOI=10.1046/j.1365-313X.1996.10040601.x;
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).
[12]
INDUCTION.
PubMed=9011085; DOI=10.1046/j.1365-313X.1996.10061037.x;
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).
[13]
INTERACTION WITH CKS1.
PubMed=9276444; DOI=10.1016/S0014-5793(97)00822-3;
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).
[14]
INTERACTION WITH KRP1/ICK1.
PubMed=9087400; DOI=10.1038/386451a0;
Wang H., Fowke L.C., Crosby W.L.;
"A plant cyclin-dependent kinase inhibitor gene.";
Nature 386:451-452(1997).
[15]
INTERACTION WITH KRP1/ICK1 AND CYCD3-1.
PubMed=9753775; DOI=10.1046/j.1365-313X.1998.00231.x;
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).
[16]
INTERACTION WITH CKS1 AND CYCD1-1, AND MUTAGENESIS OF THR-14; TYR-15;
ASP-146; PRO-156; THR-166 AND 234-LEU--ASP-236.
PubMed=10100639; DOI=10.1016/S0014-5793(99)00211-2;
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).
[17]
INTERACTION WITH CYCD4-1.
PubMed=10420643; DOI=10.1007/s004250050582;
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).
[18]
DEVELOPMENTAL STAGE.
PubMed=10521519; DOI=10.1105/tpc.11.10.1883;
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).
[19]
INDUCTION.
PubMed=11089675; DOI=10.1007/s004250000334;
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).
[20]
INTERACTION WITH KRP2/ICK2.
PubMed=10758489; DOI=10.1046/j.1365-313x.2000.00688.x;
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).
[21]
FUNCTION, AND MUTAGENESIS OF ASP-146.
PubMed=10929107; DOI=10.1046/j.1365-313x.2000.00800.x;
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).
[22]
INTERACTION WITH CYCD2-1 AND CYCD3-1.
PubMed=11096103; DOI=10.1074/jbc.M009074200;
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).
[23]
INTERACTION WITH KRP1/ICK1; KRP2/ICK2; KRP3/ICK6; KRP4/ICK7; KRP6/ICK4
AND KRP7/ICK5.
PubMed=11449057; DOI=10.1105/tpc.13.7.1653;
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).
[24]
INTERACTION WITH CKS1.
PubMed=11319029; DOI=10.1046/j.1365-313x.2001.00996.x;
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).
[25]
INTERACTION WITH CYCD2-1.
PubMed=11722776; DOI=10.1046/j.1365-313X.2001.01160.x;
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).
[26]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11971144; DOI=10.1105/tpc.010445;
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).
[27]
INTERACTION WITH KRP1/ICK1.
PubMed=12566574; DOI=10.1105/tpc.008342;
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).
[28]
INTERACTION WITH CYCD4-1.
PubMed=12857813; DOI=10.1104/pp.103.020644;
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).
[29]
INTERACTION WITH TIF4A-1/EIF4A-1.
PubMed=14706832; DOI=10.1016/S0014-5793(03)01382-6;
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).
[30]
INTERACTION WITH CYCU1-1; CYCU2-1; CYCU2-2; CYCU3-1; CYCU4-1; CYCU4-2
AND CYCU4-3.
PubMed=15197472; DOI=10.1007/s00018-004-4057-4;
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).
[31]
INTERACTION WITH CDT1A.
STRAIN=cv. Columbia;
PubMed=15316110; DOI=10.1105/tpc.104.022400;
del Mar Castellano M., Boniotti M.B., Caro E., Schnittger A.,
Gutierrez C.;
"DNA replication licensing affects cell proliferation or
endoreplication in a cell type-specific manner.";
Plant Cell 16:2380-2393(2004).
[32]
INTERACTION WITH CYCH1-1.
PubMed=15486101; DOI=10.1105/tpc.104.025601;
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).
[33]
ENZYME REGULATION, AND INTERACTION WITH KRP2/ICK2.
PubMed=15863515; DOI=10.1105/tpc.105.032383;
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).
[34]
REVIEW.
PubMed=17094738; DOI=10.1146/annurev.genet.40.110405.090431;
Inze D., de Veylder L.;
"Cell cycle regulation in plant development.";
Annu. Rev. Genet. 40:77-105(2006).
[35]
ENZYME REGULATION.
PubMed=16376885; DOI=10.1016/j.febslet.2005.12.018;
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).
[36]
SUBCELLULAR LOCATION, AND INTERACTION WITH CYCA2-3.
PubMed=16415207; DOI=10.1105/tpc.105.037309;
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).
[37]
INTERACTION WITH CYCD3-1.
PubMed=16517759; DOI=10.1105/tpc.105.039636;
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).
[38]
INTERACTION WITH PAS2.
PubMed=16698944; DOI=10.1105/tpc.105.040485;
Da Costa M., Bach L., Landrieu I., Bellec Y., Catrice O., Brown S.,
De Veylder L., Lippens G., Inze D., Faure J.-D.;
"Arabidopsis PASTICCINO2 is an antiphosphatase involved in regulation
of cyclin-dependent kinase A.";
Plant Cell 18:1426-1437(2006).
[39]
INTERACTION WITH CYCD4-2.
PubMed=16408177; DOI=10.1007/s00299-005-0075-4;
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).
[40]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16460514; DOI=10.1111/j.1365-313X.2005.02643.x;
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).
[41]
ENZYME REGULATION, PHOSPHORYLATION AT TYR-15, INTERACTION WITH
CYCH1-1, AND MUTAGENESIS OF TYR-15.
PubMed=16856985; DOI=10.1111/j.1365-313X.2006.02820.x;
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).
[42]
SUBCELLULAR LOCATION, AND INTERACTION WITH KRP1/ICK1.
PubMed=16845478; DOI=10.1007/s11103-006-9019-9;
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).
[43]
INDUCTION, PHOSPHORYLATION, AND INTERACTION WITH WEE1.
PubMed=17209125; DOI=10.1105/tpc.106.045047;
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).
[44]
FUNCTION, PHOSPHORYLATION AT THR-161, AND MUTAGENESIS OF THR-161.
PubMed=17369369; DOI=10.1105/tpc.107.050401;
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).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Root;
PubMed=18433157; DOI=10.1021/pr8000173;
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.;
"Site-specific phosphorylation profiling of Arabidopsis proteins by
mass spectrometry and peptide chip analysis.";
J. Proteome Res. 7:2458-2470(2008).
[46]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[47]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[48]
INTERACTION WITH SMR3; SMR4; SMR5; SMR6; SMR8 AND AT4G14310.
PubMed=20706207; DOI=10.1038/msb.2010.53;
Van Leene J., Hollunder J., Eeckhout D., Persiau G., Van De Slijke E.,
Stals H., Van Isterdael G., Verkest A., Neirynck S., Buffel Y.,
De Bodt S., Maere S., Laukens K., Pharazyn A., Ferreira P.C.G.,
Eloy N., Renne C., Meyer C., Faure J.-D., Steinbrenner J., Beynon J.,
Larkin J.C., Van de Peer Y., Hilson P., Kuiper M., De Veylder L.,
Van Onckelen H., Inze D., Witters E., De Jaeger G.;
"Targeted interactomics reveals a complex core cell cycle machinery in
Arabidopsis thaliana.";
Mol. Syst. Biol. 6:397-397(2010).
[49]
FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH CYCD3-2.
STRAIN=cv. Columbia;
PubMed=24687979; DOI=10.1093/jxb/eru139;
Yang K., Wang H., Xue S., Qu X., Zou J., Le J.;
"Requirement for A-type cyclin-dependent kinase and cyclins for the
terminal division in the stomatal lineage of Arabidopsis.";
J. Exp. Bot. 65:2449-2461(2014).
[50]
INTERACTION WITH MYB3R3 AND MYB3R4.
STRAIN=cv. Columbia;
PubMed=26069325; DOI=10.15252/embj.201490899;
Kobayashi K., Suzuki T., Iwata E., Nakamichi N., Suzuki T., Chen P.,
Ohtani M., Ishida T., Hosoya H., Mueller S., Leviczky T.,
Pettko-Szandtner A., Darula Z., Iwamoto A., Nomoto M., Tada Y.,
Higashiyama T., Demura T., Doonan J.H., Hauser M.T., Sugimoto K.,
Umeda M., Magyar Z., Boegre L., Ito M.;
"Transcriptional repression by MYB3R proteins regulates plant organ
growth.";
EMBO J. 34:1992-2007(2015).
-!- 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. Required to trigger guard mother cells (GMC)
symmetric divisions at the late stage of stomatal development,
probably via the regulation of G1 to S transition in the cell
cycle. Promotes divisions in the guard cells (GCs) after the guard
mother cells (GMC) symmetric division when in the presence of
CYCD3-2 (PubMed:24687979). {ECO:0000269|PubMed:10929107,
ECO:0000269|PubMed:16460514, ECO:0000269|PubMed:17369369,
ECO:0000269|PubMed:24687979}.
-!- 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. {ECO:0000269|PubMed:15863515,
ECO:0000269|PubMed:16376885, ECO:0000269|PubMed:16856985}.
-!- SUBUNIT: 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. Interacts with SMR3, SMR4, SMR5, SMR6,
SMR8 and At4g14310. Binds to CYCD3-2 (PubMed:24687979). Component
of a DREAM-like complex which modulates a variety of
developmentally regulated genes and of the mitotic genes in
proliferating and differentiated cells. Interacts with MYB3R3 at
later and with MYB3R4 at earlier stages of leaf development
(PubMed:26069325). {ECO:0000269|PubMed:10100639,
ECO:0000269|PubMed:10420643, ECO:0000269|PubMed:10758489,
ECO:0000269|PubMed:11096103, ECO:0000269|PubMed:11319029,
ECO:0000269|PubMed:11449057, ECO:0000269|PubMed:11722776,
ECO:0000269|PubMed:12566574, ECO:0000269|PubMed:12857813,
ECO:0000269|PubMed:14706832, ECO:0000269|PubMed:15197472,
ECO:0000269|PubMed:15316110, ECO:0000269|PubMed:15486101,
ECO:0000269|PubMed:15863515, ECO:0000269|PubMed:16408177,
ECO:0000269|PubMed:16415207, ECO:0000269|PubMed:16517759,
ECO:0000269|PubMed:16698944, ECO:0000269|PubMed:16845478,
ECO:0000269|PubMed:16856985, ECO:0000269|PubMed:17209125,
ECO:0000269|PubMed:20706207, ECO:0000269|PubMed:24687979,
ECO:0000269|PubMed:26069325, ECO:0000269|PubMed:9087400,
ECO:0000269|PubMed:9276444, ECO:0000269|PubMed:9753775}.
-!- INTERACTION:
O23249:CKS1; NbExp=9; IntAct=EBI-371713, EBI-1253127;
P42752:CYCD2-1; NbExp=4; IntAct=EBI-371713, EBI-1253160;
P42753:CYCD3-1; NbExp=5; IntAct=EBI-371713, EBI-1253610;
Q8LGA1:CYCD4-1; NbExp=4; IntAct=EBI-371713, EBI-1253202;
Q9LJ45:CYCU1-1; NbExp=2; IntAct=EBI-371713, EBI-1773749;
O80513:CYCU4-1; NbExp=2; IntAct=EBI-371713, EBI-1773819;
Q9FKF6:CYCU4-3; NbExp=2; IntAct=EBI-371713, EBI-1773829;
Q67Y93:KRP1; NbExp=10; IntAct=EBI-371713, EBI-1636730;
Q9SCR2:KRP2; NbExp=6; IntAct=EBI-371713, EBI-1636748;
Q9FKB5:KRP3; NbExp=4; IntAct=EBI-371713, EBI-1773302;
Q8GYJ3:KRP4; NbExp=4; IntAct=EBI-371713, EBI-1253225;
Q9LRY0:KRP5; NbExp=3; IntAct=EBI-371713, EBI-1636764;
Q0WNX9:KRP6; NbExp=3; IntAct=EBI-371713, EBI-1253171;
Q94CL9:KRP7; NbExp=3; IntAct=EBI-371713, EBI-1773344;
P41376:TIF4A-1; NbExp=2; IntAct=EBI-371713, EBI-371706;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly cytoplasmic.
Nuclear distribution increases after binding to ICK1/KRP1.
-!- TISSUE SPECIFICITY: Expressed in roots, stems, flowers and
siliques. {ECO:0000269|PubMed:8893539}.
-!- 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.
{ECO:0000269|PubMed:10521519, ECO:0000269|PubMed:8893539}.
-!- INDUCTION: By nematode infection in roots. Down-regulated by salt
stress in root meristem and replication blocking agents
(hydroxyurea and aphidicolin). {ECO:0000269|PubMed:11089675,
ECO:0000269|PubMed:17209125, ECO:0000269|PubMed:9011085}.
-!- PTM: 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.
{ECO:0000269|PubMed:16856985, ECO:0000269|PubMed:17209125,
ECO:0000269|PubMed:17369369}.
-!- DISRUPTION PHENOTYPE: Plants display lethal male gametophyte
(PubMed:16460514). Impaired stomata formation with arrested guard
mother cells (GMC) divisions. Impaired last mitotic division in
the male gametophyte, leading to 50 percent of pollen with two
gametes. The double mutant flp-1 myb88 displays an enhanced
stomatal phenotype with more and larger stomatal clusters. Triple
mutants cdka;1 flp-1 myb88 don't have guard cells stacks but
accumulates sGCs (PubMed:24687979). {ECO:0000269|PubMed:16460514,
ECO:0000269|PubMed:24687979}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAL91258.1; Type=Frameshift; Positions=285; Evidence={ECO:0000305};
Sequence=CAB87903.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M59198; AAA32831.1; -; mRNA.
EMBL; S45387; AAB23643.1; -; mRNA.
EMBL; X57839; CAA40971.1; -; mRNA.
EMBL; D10850; BAA01623.1; -; Genomic_DNA.
EMBL; AL132963; CAB87903.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002686; AEE78452.1; -; Genomic_DNA.
EMBL; AY090353; AAL91258.1; ALT_FRAME; mRNA.
EMBL; BT024706; ABD59044.1; -; mRNA.
EMBL; AK226373; BAE98520.1; -; mRNA.
EMBL; AY085153; AAM61706.1; -; mRNA.
PIR; S23095; S23095.
PIR; T49271; T49271.
RefSeq; NP_566911.1; NM_114734.4.
UniGene; At.24166; -.
ProteinModelPortal; P24100; -.
SMR; P24100; -.
BioGrid; 9354; 107.
IntAct; P24100; 73.
STRING; 3702.AT3G48750.1; -.
iPTMnet; P24100; -.
PaxDb; P24100; -.
PRIDE; P24100; -.
EnsemblPlants; AT3G48750.1; AT3G48750.1; AT3G48750.
GeneID; 824036; -.
Gramene; AT3G48750.1; AT3G48750.1; AT3G48750.
KEGG; ath:AT3G48750; -.
Araport; AT3G48750; -.
TAIR; locus:2099478; AT3G48750.
eggNOG; KOG0594; Eukaryota.
eggNOG; ENOG410XPP3; LUCA.
HOGENOM; HOG000233024; -.
InParanoid; P24100; -.
KO; K02206; -.
OMA; EMMLVYD; -.
OrthoDB; EOG09360GJR; -.
PhylomeDB; P24100; -.
BRENDA; 2.7.11.22; 399.
Reactome; R-ATH-110056; MAPK3 (ERK1) activation.
Reactome; R-ATH-1538133; G0 and Early G1.
Reactome; R-ATH-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-ATH-176408; Regulation of APC/C activators between G1/S and early anaphase.
Reactome; R-ATH-2299718; Condensation of Prophase Chromosomes.
Reactome; R-ATH-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-ATH-4419969; Depolymerisation of the Nuclear Lamina.
Reactome; R-ATH-5693607; Processing of DNA double-strand break ends.
Reactome; R-ATH-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-ATH-68911; G2 Phase.
Reactome; R-ATH-68949; Orc1 removal from chromatin.
Reactome; R-ATH-68962; Activation of the pre-replicative complex.
Reactome; R-ATH-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-ATH-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
Reactome; R-ATH-69202; Cyclin E associated events during G1/S transition.
Reactome; R-ATH-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-ATH-69478; G2/M DNA replication checkpoint.
Reactome; R-ATH-69656; Cyclin A:Cdk2-associated events at S phase entry.
Reactome; R-ATH-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
PRO; PR:P24100; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; P24100; baseline and differential.
Genevisible; P24100; AT.
GO; GO:0010005; C:cortical microtubule, transverse to long axis; IDA:TAIR.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009574; C:preprophase band; TAS:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; ISS:TAIR.
GO; GO:0016301; F:kinase activity; IMP:TAIR.
GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
GO; GO:0008353; F:RNA polymerase II carboxy-terminal domain kinase activity; IEA:UniProtKB-EC.
GO; GO:0008356; P:asymmetric cell division; IGI:TAIR.
GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:TAIR.
GO; GO:0042023; P:DNA endoreduplication; IMP:TAIR.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
GO; GO:0048229; P:gametophyte development; IMP:TAIR.
GO; GO:0010235; P:guard mother cell cytokinesis; IMP:UniProtKB.
GO; GO:0010444; P:guard mother cell differentiation; IMP:UniProtKB.
GO; GO:0016572; P:histone phosphorylation; IBA:GO_Central.
GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
GO; GO:0009555; P:pollen development; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:TAIR.
GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; IMP:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0040020; P:regulation of meiotic nuclear division; IMP:TAIR.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0009409; P:response to cold; IEP:TAIR.
GO; GO:0098725; P:symmetric cell division; IMP:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Cell cycle; Cell division; Complete proteome; Cytoplasm;
Kinase; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 294 Cyclin-dependent kinase A-1.
/FTId=PRO_0000085749.
DOMAIN 4 287 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 10 18 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 127 127 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 33 33 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 15 15 Phosphotyrosine.
{ECO:0000269|PubMed:16856985}.
MOD_RES 161 161 Phosphothreonine.
{ECO:0000244|PubMed:18433157,
ECO:0000269|PubMed:17369369}.
MUTAGEN 14 14 T->A: Increased kinase activity; when
associated with F-15.
{ECO:0000269|PubMed:10100639}.
MUTAGEN 15 15 Y->F: Abolishes phosphorylation by WEE1.
Increased kinase activity; when
associated with A-14.
{ECO:0000269|PubMed:10100639,
ECO:0000269|PubMed:16856985}.
MUTAGEN 146 146 D->N: Decreased kinase activity and
disturbed cell cycle. Reduced frequency
of cell division during embryo
development.
{ECO:0000269|PubMed:10100639,
ECO:0000269|PubMed:10929107}.
MUTAGEN 156 156 P->L: Decreased kinase activity and
disturbed cell cycle.
{ECO:0000269|PubMed:10100639}.
MUTAGEN 161 161 T->D: Strong reduction in kinase activity
and ability to bind substrate. Strong
reduction in plant growth. Sterile
plants. {ECO:0000269|PubMed:17369369}.
MUTAGEN 161 161 T->V: Strong reduction in kinase activity
and ability to bind substrate.
{ECO:0000269|PubMed:17369369}.
MUTAGEN 166 166 T->I: Decreased kinase activity and
disturbed cell cycle.
{ECO:0000269|PubMed:10100639}.
MUTAGEN 234 236 Missing: No change in kinase activity,
but disturbed cell cycle. Loss of
interaction with CKS1.
{ECO:0000269|PubMed:10100639}.
SEQUENCE 294 AA; 34030 MW; B5FAE55FA9EC366E CRC64;
MDQYEKVEKI GEGTYGVVYK ARDKVTNETI ALKKIRLEQE DEGVPSTAIR EISLLKEMQH
SNIVKLQDVV HSEKRLYLVF EYLDLDLKKH MDSTPDFSKD LHMIKTYLYQ ILRGIAYCHS
HRVLHRDLKP QNLLIDRRTN SLKLADFGLA RAFGIPVRTF THEVVTLWYR APEILLGSHH
YSTPVDIWSV GCIFAEMISQ KPLFPGDSEI DQLFKIFRIM GTPYEDTWRG VTSLPDYKSA
FPKWKPTDLE TFVPNLDPDG VDLLSKMLLM DPTKRINARA ALEHEYFKDL GGMP


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