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Cyclin-dependent kinase 6 (EC 2.7.11.22) (Cell division protein kinase 6) (Serine/threonine-protein kinase PLSTIRE)

 CDK6_HUMAN              Reviewed;         326 AA.
Q00534; A4D1G0;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
22-NOV-2017, entry version 197.
RecName: Full=Cyclin-dependent kinase 6;
EC=2.7.11.22;
AltName: Full=Cell division protein kinase 6;
AltName: Full=Serine/threonine-protein kinase PLSTIRE;
Name=CDK6; Synonyms=CDKN6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1639063;
Meyerson M., Enders G.H., Wu C.-L., Su L.-K., Gorka C., Nelson C.,
Harlow E., Tsai L.-H.;
"A family of human cdc2-related protein kinases.";
EMBO J. 11:2909-2917(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION AS PRB/RB1 KINASE, TISSUE SPECIFICITY, AND INTERACTION WITH
D-TYPE CYCLINS.
PubMed=8114739; DOI=10.1128/MCB.14.3.2077;
Meyerson M., Harlow E.;
"Identification of G1 kinase activity for cdk6, a novel cyclin D
partner.";
Mol. Cell. Biol. 14:2077-2086(1994).
[9]
SUBCELLULAR LOCATION, AND INTERACTION WITH D-TYPE CYCLINS; CDKN2D;
HSP90AB1 AND CDC37.
PubMed=9482106; DOI=10.1038/sj.onc.1201570;
Mahony D., Parry D.A., Lees E.;
"Active cdk6 complexes are predominantly nuclear and represent only a
minority of the cdk6 in T cells.";
Oncogene 16:603-611(1998).
[10]
FUNCTION IN DIFFERENTIATION, AND ENZYME REGULATION.
PubMed=12833137; DOI=10.1038/sj.onc.1206484;
Matushansky I., Radparvar F., Skoultchi A.I.;
"CDK6 blocks differentiation: coupling cell proliferation to the block
to differentiation in leukemic cells.";
Oncogene 22:4143-4149(2003).
[11]
FUNCTION IN CELL PROLIFERATION.
PubMed=14985467;
Lucas J.J., Domenico J., Gelfand E.W.;
"Cyclin-dependent kinase 6 inhibits proliferation of human mammary
epithelial cells.";
Mol. Cancer Res. 2:105-114(2004).
[12]
FUNCTION IN DIFFERENTIATION.
PubMed=15254224; DOI=10.1128/MCB.24.15.6560-6568.2004;
Ogasawara T., Kawaguchi H., Jinno S., Hoshi K., Itaka K., Takato T.,
Nakamura K., Okayama H.;
"Bone morphogenetic protein 2-induced osteoblast differentiation
requires Smad-mediated down-regulation of Cdk6.";
Mol. Cell. Biol. 24:6560-6568(2004).
[13]
INTERACTION WITH FBXO7, AND SUBCELLULAR LOCATION.
PubMed=16096642; DOI=10.1038/sj.emboj.7600775;
Laman H., Funes J.M., Ye H., Henderson S., Galinanes-Garcia L.,
Hara E., Knowles P., McDonald N., Boshoff C.;
"Transforming activity of Fbxo7 is mediated specifically through
regulation of cyclin D/cdk6.";
EMBO J. 24:3104-3116(2005).
[14]
FUNCTION AS PRB/RB1 KINASE.
PubMed=15809340; DOI=10.1093/jb/mvi050;
Takaki T., Fukasawa K., Suzuki-Takahashi I., Semba K., Kitagawa M.,
Taya Y., Hirai H.;
"Preferences for phosphorylation sites in the retinoblastoma protein
of D-type cyclin-dependent kinases, Cdk4 and Cdk6, in vitro.";
J. Biochem. 137:381-386(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-13 AND TYR-24, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[16]
INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
Leong W.F., Chow V.T.;
"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells
reveal differential cellular gene expression in response to
enterovirus 71 infection.";
Cell. Microbiol. 8:565-580(2006).
[17]
FUNCTION IN MYELOID DIFFERENTIATION, AND INTERACTION WITH RUNX1.
PubMed=17431401; DOI=10.1038/sj.emboj.7601675;
Fujimoto T., Anderson K., Jacobsen S.E., Nishikawa S.I., Nerlov C.;
"Cdk6 blocks myeloid differentiation by interfering with Runx1 DNA
binding and Runx1-C/EBPalpha interaction.";
EMBO J. 26:2361-2370(2007).
[18]
FUNCTION IN SENESCENCE.
PubMed=17420273; DOI=10.1128/MCB.02286-06;
Ruas M., Gregory F., Jones R., Poolman R., Starborg M., Rowe J.,
Brookes S., Peters G.;
"CDK4 and CDK6 delay senescence by kinase-dependent and p16INK4a-
independent mechanisms.";
Mol. Cell. Biol. 27:4273-4282(2007).
[19]
INDUCTION BY NANOG.
PubMed=19139263; DOI=10.1083/jcb.200801009;
Zhang X., Neganova I., Przyborski S., Yang C., Cooke M.,
Atkinson S.P., Anyfantis G., Fenyk S., Keith W.N., Hoare S.F.,
Hughes O., Strachan T., Stojkovic M., Hinds P.W., Armstrong L.,
Lako M.;
"A role for NANOG in G1 to S transition in human embryonic stem cells
through direct binding of CDK6 and CDC25A.";
J. Cell Biol. 184:67-82(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24; THR-49; THR-70 AND
THR-325, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-264, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[23]
FUNCTION IN BETA-CELL PROLIFERATION, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
PubMed=20668294; DOI=10.2337/db09-1776;
Fiaschi-Taesch N.M., Salim F., Kleinberger J., Troxell R.,
Cozar-Castellano I., Selk K., Cherok E., Takane K.K., Scott D.K.,
Stewart A.F.;
"Induction of human beta-cell proliferation and engraftment using a
single G1/S regulatory molecule, cdk6.";
Diabetes 59:1926-1936(2010).
[24]
FUNCTION AS NPM1 KINASE, AND INTERACTION WITH KSHV V-CYCLIN.
PubMed=20333249; DOI=10.1371/journal.ppat.1000818;
Sarek G., Jaerviluoma A., Moore H.M., Tojkander S., Vartia S.,
Biberfeld P., Laiho M., Ojala P.M.;
"Nucleophosmin phosphorylation by v-cyclin-CDK6 controls KSHV
latency.";
PLoS Pathog. 6:E1000818-E1000818(2010).
[25]
REVIEW ON CELL DIFFERENTIATION.
PubMed=16294322; DOI=10.1002/jcb.20712;
Grossel M.J., Hinds P.W.;
"Beyond the cell cycle: a new role for Cdk6 in differentiation.";
J. Cell. Biochem. 97:485-493(2006).
[26]
REVIEW ON CELL CYCLE CONTROL, INHIBITORS, AND GENE FAMILY.
PubMed=19238148; DOI=10.1038/nrc2602;
Malumbres M., Barbacid M.;
"Cell cycle, CDKs and cancer: a changing paradigm.";
Nat. Rev. Cancer 9:153-166(2009).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[29]
FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN MCPH12, AND VARIANT
MCPH12 THR-197.
PubMed=23918663; DOI=10.1093/hmg/ddt374;
Hussain M.S., Baig S.M., Neumann S., Peche V.S., Szczepanski S.,
Nurnberg G., Tariq M., Jameel M., Khan T.N., Fatima A., Malik N.A.,
Ahmad I., Altmuller J., Frommolt P., Thiele H., Hohne W., Yigit G.,
Wollnik B., Neubauer B.A., Nurnberg P., Noegel A.A.;
"CDK6 associates with the centrosome during mitosis and is mutated in
a large Pakistani family with primary microcephaly.";
Hum. Mol. Genet. 22:5199-5214(2013).
[30]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEXES WITH INK4A AND
INK4D.
PubMed=9751050; DOI=10.1038/26155;
Russo A.A., Tong L., Lee J.O., Jeffrey P.D., Pavletich N.P.;
"Structural basis for inhibition of the cyclin-dependent kinase Cdk6
by the tumour suppressor p16INK4a.";
Nature 395:237-243(1998).
[31]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH INHIBITOR
CDKN2C/P18-INK4C.
PubMed=11124804; DOI=10.1101/gad.851100;
Jeffrey P.D., Tong L., Pavletich N.P.;
"Structural basis of inhibition of CDK-cyclin complexes by INK4
inhibitors.";
Genes Dev. 14:3115-3125(2000).
[32]
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-308 IN COMPLEX WITH
HERPESVIRUS SAIMIRI V-CYCLIN/ECLF2, AND PHOSPHORYLATION AT THR-177.
PubMed=11828325; DOI=10.1038/nsb756;
Schulze-Gahmen U., Kim S.-H.;
"Structural basis for CDK6 activation by a virus-encoded cyclin.";
Nat. Struct. Biol. 9:177-181(2002).
[33]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-308 IN COMPLEX WITH
INHIBITOR.
PubMed=15689157; DOI=10.1021/jm049353p;
Lu H., Chang D.J., Baratte B., Meijer L., Schulze-Gahmen U.;
"Crystal structure of a human cyclin-dependent kinase 6 complex with a
flavonol inhibitor, fisetin.";
J. Med. Chem. 48:737-743(2005).
[34]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-308 IN COMPLEX WITH
INHIBITORS AND V-CYCLIN.
PubMed=16789739; DOI=10.1021/jm0600388;
Lu H., Schulze-Gahmen U.;
"Toward understanding the structural basis of cyclin-dependent kinase
6 specific inhibition.";
J. Med. Chem. 49:3826-3831(2006).
[35]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-301 IN COMPLEX WITH
INHIBITORS.
PubMed=21038853; DOI=10.1021/jm100571n;
Cho Y.S., Borland M., Brain C., Chen C.H.-T., Cheng H., Chopra R.,
Chung K., Groarke J., He G., Hou Y., Kim S., Kovats S., Lu Y.,
O'Reilly M., Shen J., Smith T., Trakshel G., Voegtle M., Xu M., Xu M.,
Sung M.J.;
"4-(Pyrazol-4-yl)-pyrimidines as selective inhibitors of cyclin-
dependent kinase 4/6.";
J. Med. Chem. 53:7938-7957(2010).
[36]
VARIANTS [LARGE SCALE ANALYSIS] ASN-110 AND LEU-199.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Serine/threonine-protein kinase involved in the control
of the cell cycle and differentiation; promotes G1/S transition.
Phosphorylates pRB/RB1 and NPM1. Interacts with D-type G1 cyclins
during interphase at G1 to form a pRB/RB1 kinase and controls the
entrance into the cell cycle. Involved in initiation and
maintenance of cell cycle exit during cell differentiation;
prevents cell proliferation and regulates negatively cell
differentiation, but is required for the proliferation of specific
cell types (e.g. erythroid and hematopoietic cells). Essential for
cell proliferation within the dentate gyrus of the hippocampus and
the subventricular zone of the lateral ventricles. Required during
thymocyte development. Promotes the production of newborn neurons,
probably by modulating G1 length. Promotes, at least in
astrocytes, changes in patterns of gene expression, changes in the
actin cytoskeleton including loss of stress fibers, and enhanced
motility during cell differentiation. Prevents myeloid
differentiation by interfering with RUNX1 and reducing its
transcription transactivation activity, but promotes proliferation
of normal myeloid progenitors. Delays senescence. Promotes the
proliferation of beta-cells in pancreatic islets of Langerhans.
May play a role in the centrosome organization during the cell
cycle phases (PubMed:23918663). {ECO:0000269|PubMed:12833137,
ECO:0000269|PubMed:14985467, ECO:0000269|PubMed:15254224,
ECO:0000269|PubMed:15809340, ECO:0000269|PubMed:17420273,
ECO:0000269|PubMed:17431401, ECO:0000269|PubMed:20333249,
ECO:0000269|PubMed:20668294, ECO:0000269|PubMed:23918663,
ECO:0000269|PubMed:8114739}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Inhibited by INK4 proteins (CDKN2C/p18-INK4c),
aminopurvalanol, PD0332991, 4-(Pyrazol-4-yl)-pyrimidines and
fisetin, a flavonol inhibitor. Activated by Thr-177
phosphorylation and Tyr-24 dephosphorylation (By similarity).
Stimulated by cyclin from herpesvirus saimiri (V-cyclin/ECLF2).
Rapidly down-regulated prior to cell differentiation (e.g.
erythroid and osteoblast). {ECO:0000250,
ECO:0000269|PubMed:12833137}.
-!- SUBUNIT: Interaction with D-type G1 cyclins. Cyclin binding
promotes enzyme activation by phosphorylation at Thr-177 (By
similarity). Binds to RUNX1, CDKN2D, FBXO7 and CDKN2C/p18-INK4c.
Forms a cytoplasmic complex with Hsp90/HSP90AB1 and CDC37. FBXO7-
binding promotes D-type cyclin binding. Interacts with Kaposi's
sarcoma herpesvirus (KSHV) V-cyclin and herpesvirus saimiri (V-
cyclin/ECLF2); the CDK6/V-cyclin complex phosphorylates NPM1 and
thus lead to viral reactivation by reducing viral LANA levels.
{ECO:0000250, ECO:0000269|PubMed:11124804,
ECO:0000269|PubMed:11828325, ECO:0000269|PubMed:15689157,
ECO:0000269|PubMed:16096642, ECO:0000269|PubMed:16789739,
ECO:0000269|PubMed:17431401, ECO:0000269|PubMed:20333249,
ECO:0000269|PubMed:21038853, ECO:0000269|PubMed:8114739,
ECO:0000269|PubMed:9482106}.
-!- INTERACTION:
P24385:CCND1; NbExp=4; IntAct=EBI-295663, EBI-375001;
P30281:CCND3; NbExp=13; IntAct=EBI-295663, EBI-375013;
Q16543:CDC37; NbExp=3; IntAct=EBI-295663, EBI-295634;
P42771:CDKN2A; NbExp=14; IntAct=EBI-295663, EBI-375053;
P42772:CDKN2B; NbExp=10; IntAct=EBI-295663, EBI-711280;
P42773:CDKN2C; NbExp=19; IntAct=EBI-295663, EBI-711290;
P55273:CDKN2D; NbExp=14; IntAct=EBI-295663, EBI-745859;
Q08050-1:FOXM1; NbExp=2; IntAct=EBI-295663, EBI-866499;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-295663, EBI-352572;
Q01196:RUNX1; NbExp=5; IntAct=EBI-295663, EBI-925904;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell projection, ruffle.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:23918663}. Note=Localized to the ruffling edge
of spreading fibroblasts. Kinase activity only in nucleus.
Localized to the cytosol of neurons and showed prominent staining
around either side of the nucleus (By similarity). Present in the
cytosol and in the nucleus in interphase cells and at the
centrosome during mitosis from prophase to telophase
(PubMed:23918663). {ECO:0000250|UniProtKB:Q64261,
ECO:0000269|PubMed:23918663}.
-!- TISSUE SPECIFICITY: Expressed ubiquitously. Accumulates in
squamous cell carcinomas, proliferating hematopoietic progenitor
cells, beta-cells of pancreatic islets of Langerhans, and
neuroblastomas. Reduced levels in differentiating cells.
{ECO:0000269|PubMed:20668294, ECO:0000269|PubMed:8114739}.
-!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71)
infection. Induced by NANOG during S-phase entry.
{ECO:0000269|PubMed:16548883, ECO:0000269|PubMed:19139263}.
-!- PTM: Thr-177 phosphorylation and Tyr-24 dephosphorylation promotes
kinase activity. {ECO:0000269|PubMed:11828325}.
-!- POLYMORPHISM: Genetic variations in CDK6 may influence stature as
a quantitative trait, contributing to the stature quantitative
trait locus 11 (STQTL11) [MIM:612223]. Adult height is an easily
observable and highly heritable complex continuous trait. Because
of this, it is a model trait for studying genetic influence on
quantitative traits.
-!- DISEASE: Microcephaly 12, primary, autosomal recessive (MCPH12)
[MIM:616080]: A form of microcephaly, a disease defined as a head
circumference more than 3 standard deviations below the age-
related mean. Brain weight is markedly reduced and the cerebral
cortex is disproportionately small. {ECO:0000269|PubMed:23918663}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: Over-expressed in some leukemias and malignancies
(including sarcoma, glioma, breast tumors, lymphoma and melanoma)
as a consequence of nearby translocations.
-!- MISCELLANEOUS: Enhances beta-cells engraftment in pancreatic
islets of Langerhans of diabetic patients.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdk6/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X66365; CAA47008.1; -; mRNA.
EMBL; AY128534; AAM76970.1; -; Genomic_DNA.
EMBL; AK313491; BAG36273.1; -; mRNA.
EMBL; AC000065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC004128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC004011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236949; EAL24146.1; -; Genomic_DNA.
EMBL; CH471091; EAW76827.1; -; Genomic_DNA.
EMBL; BC052264; AAH52264.1; -; mRNA.
CCDS; CCDS5628.1; -.
PIR; S23387; S23387.
RefSeq; NP_001138778.1; NM_001145306.1.
RefSeq; NP_001250.1; NM_001259.6.
RefSeq; XP_006715898.1; XM_006715835.2.
UniGene; Hs.119882; -.
PDB; 1BI7; X-ray; 3.40 A; A=1-326.
PDB; 1BI8; X-ray; 2.80 A; A/C=1-326.
PDB; 1BLX; X-ray; 1.90 A; A=1-326.
PDB; 1G3N; X-ray; 2.90 A; A/E=1-326.
PDB; 1JOW; X-ray; 3.10 A; B=1-308.
PDB; 1XO2; X-ray; 2.90 A; B=1-308.
PDB; 2EUF; X-ray; 3.00 A; B=1-308.
PDB; 2F2C; X-ray; 2.80 A; B=1-308.
PDB; 3NUP; X-ray; 2.60 A; A=1-301.
PDB; 3NUX; X-ray; 2.70 A; A=1-301.
PDB; 4AUA; X-ray; 2.31 A; A=1-301.
PDB; 4EZ5; X-ray; 2.70 A; A=1-301.
PDB; 4TTH; X-ray; 2.90 A; B=1-326.
PDB; 5L2I; X-ray; 2.75 A; A=1-301.
PDB; 5L2S; X-ray; 2.27 A; A=1-301.
PDB; 5L2T; X-ray; 2.37 A; A=1-301.
PDBsum; 1BI7; -.
PDBsum; 1BI8; -.
PDBsum; 1BLX; -.
PDBsum; 1G3N; -.
PDBsum; 1JOW; -.
PDBsum; 1XO2; -.
PDBsum; 2EUF; -.
PDBsum; 2F2C; -.
PDBsum; 3NUP; -.
PDBsum; 3NUX; -.
PDBsum; 4AUA; -.
PDBsum; 4EZ5; -.
PDBsum; 4TTH; -.
PDBsum; 5L2I; -.
PDBsum; 5L2S; -.
PDBsum; 5L2T; -.
ProteinModelPortal; Q00534; -.
SMR; Q00534; -.
BioGrid; 107456; 124.
CORUM; Q00534; -.
DIP; DIP-687N; -.
IntAct; Q00534; 101.
MINT; MINT-232049; -.
STRING; 9606.ENSP00000265734; -.
BindingDB; Q00534; -.
ChEMBL; CHEMBL2508; -.
DrugBank; DB07379; (2S)-2-({6-[(3-amino-5-chlorophenyl)amino]-9-isopropyl-9H-purin-2-yl}amino)-3-methylbutan-1-ol.
DrugBank; DB03496; Flavopiridol.
DrugBank; DB09073; Palbociclib.
DrugBank; DB11730; Ribociclib.
GuidetoPHARMACOLOGY; 1978; -.
iPTMnet; Q00534; -.
PhosphoSitePlus; Q00534; -.
BioMuta; CDK6; -.
DMDM; 266423; -.
EPD; Q00534; -.
MaxQB; Q00534; -.
PaxDb; Q00534; -.
PeptideAtlas; Q00534; -.
PRIDE; Q00534; -.
DNASU; 1021; -.
Ensembl; ENST00000265734; ENSP00000265734; ENSG00000105810.
Ensembl; ENST00000424848; ENSP00000397087; ENSG00000105810.
GeneID; 1021; -.
KEGG; hsa:1021; -.
UCSC; uc010lez.4; human.
CTD; 1021; -.
DisGeNET; 1021; -.
EuPathDB; HostDB:ENSG00000105810.9; -.
GeneCards; CDK6; -.
GeneReviews; CDK6; -.
HGNC; HGNC:1777; CDK6.
HPA; CAB004363; -.
HPA; HPA002637; -.
MalaCards; CDK6; -.
MIM; 603368; gene.
MIM; 612223; phenotype.
MIM; 616080; phenotype.
neXtProt; NX_Q00534; -.
OpenTargets; ENSG00000105810; -.
Orphanet; 2512; Autosomal recessive primary microcephaly.
PharmGKB; PA103; -.
eggNOG; KOG0594; Eukaryota.
eggNOG; ENOG410XPP3; LUCA.
GeneTree; ENSGT00900000140881; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; Q00534; -.
KO; K02091; -.
OMA; CIIFEMF; -.
OrthoDB; EOG091G0I1Q; -.
PhylomeDB; Q00534; -.
TreeFam; TF101022; -.
BRENDA; 2.7.11.22; 2681.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-2559585; Oncogene Induced Senescence.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-8934593; Regulation of RUNX1 Expression and Activity.
SignaLink; Q00534; -.
SIGNOR; Q00534; -.
ChiTaRS; CDK6; human.
EvolutionaryTrace; Q00534; -.
GeneWiki; Cyclin-dependent_kinase_6; -.
GenomeRNAi; 1021; -.
PRO; PR:Q00534; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000105810; -.
CleanEx; HS_CDK6; -.
Genevisible; Q00534; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0097132; C:cyclin D2-CDK6 complex; IEA:Ensembl.
GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0001726; C:ruffle; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
GO; GO:0030332; F:cyclin binding; IPI:BHF-UCL.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:BHF-UCL.
GO; GO:0098770; F:FBXO family protein binding; IPI:ParkinsonsUK-UCL.
GO; GO:0014002; P:astrocyte development; ISS:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; TAS:UniProtKB.
GO; GO:0043697; P:cell dedifferentiation; IMP:BHF-UCL.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:1904628; P:cellular response to phorbol 13-acetate 12-myristate; IDA:UniProtKB.
GO; GO:0021542; P:dentate gyrus development; ISS:UniProtKB.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:UniProtKB.
GO; GO:0048699; P:generation of neurons; ISS:UniProtKB.
GO; GO:0042063; P:gliogenesis; IMP:BHF-UCL.
GO; GO:0060218; P:hematopoietic stem cell differentiation; IEA:Ensembl.
GO; GO:0021670; P:lateral ventricle development; ISS:UniProtKB.
GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB.
GO; GO:0045596; P:negative regulation of cell differentiation; TAS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:UniProtKB.
GO; GO:2000773; P:negative regulation of cellular senescence; IDA:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:BHF-UCL.
GO; GO:0045656; P:negative regulation of monocyte differentiation; IDA:UniProtKB.
GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:UniProtKB.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IDA:BHF-UCL.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:BHF-UCL.
GO; GO:2000145; P:regulation of cell motility; ISS:UniProtKB.
GO; GO:0045646; P:regulation of erythrocyte differentiation; IMP:BHF-UCL.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
GO; GO:0010468; P:regulation of gene expression; IDA:BHF-UCL.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; IEA:Ensembl.
GO; GO:0009615; P:response to virus; IEP:UniProtKB.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
GO; GO:0003323; P:type B pancreatic cell development; IDA:UniProtKB.
CDD; cd07862; STKc_CDK6; 1.
InterPro; IPR028788; CDK6.
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;
3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
Cell projection; Complete proteome; Cytoplasm; Cytoskeleton;
Differentiation; Disease mutation; Kinase; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Primary microcephaly;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 326 Cyclin-dependent kinase 6.
/FTId=PRO_0000085789.
DOMAIN 13 300 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 19 27 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 145 145 Proton acceptor.
BINDING 43 43 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 13 13 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 24 24 Phosphotyrosine.
{ECO:0000244|PubMed:15592455,
ECO:0000244|PubMed:19369195}.
MOD_RES 49 49 Phosphothreonine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 70 70 Phosphothreonine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 177 177 Phosphothreonine.
{ECO:0000269|PubMed:11828325}.
MOD_RES 264 264 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 325 325 Phosphothreonine.
{ECO:0000244|PubMed:19369195}.
VARIANT 110 110 D -> N (in dbSNP:rs35654944).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041978.
VARIANT 197 197 A -> T (in MCPH12; dbSNP:rs606231255).
{ECO:0000269|PubMed:23918663}.
/FTId=VAR_072638.
VARIANT 199 199 P -> L (in a metastatic melanoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041979.
HELIX 9 11 {ECO:0000244|PDB:1BLX}.
STRAND 13 22 {ECO:0000244|PDB:1BLX}.
STRAND 25 32 {ECO:0000244|PDB:1BLX}.
TURN 33 37 {ECO:0000244|PDB:1BLX}.
STRAND 39 49 {ECO:0000244|PDB:1BLX}.
HELIX 58 70 {ECO:0000244|PDB:1BLX}.
STRAND 79 87 {ECO:0000244|PDB:1BLX}.
STRAND 89 99 {ECO:0000244|PDB:1BLX}.
STRAND 102 104 {ECO:0000244|PDB:5L2S}.
HELIX 105 111 {ECO:0000244|PDB:1BLX}.
TURN 113 115 {ECO:0000244|PDB:4TTH}.
HELIX 119 138 {ECO:0000244|PDB:1BLX}.
HELIX 148 150 {ECO:0000244|PDB:1BLX}.
STRAND 151 153 {ECO:0000244|PDB:1BLX}.
STRAND 159 161 {ECO:0000244|PDB:1BLX}.
HELIX 172 176 {ECO:0000244|PDB:1BLX}.
STRAND 180 182 {ECO:0000244|PDB:1BI8}.
HELIX 183 185 {ECO:0000244|PDB:2F2C}.
HELIX 188 191 {ECO:0000244|PDB:1BLX}.
HELIX 199 214 {ECO:0000244|PDB:1BLX}.
HELIX 224 235 {ECO:0000244|PDB:1BLX}.
HELIX 240 242 {ECO:0000244|PDB:1BLX}.
STRAND 245 249 {ECO:0000244|PDB:1XO2}.
HELIX 251 253 {ECO:0000244|PDB:1BLX}.
HELIX 262 264 {ECO:0000244|PDB:1BLX}.
STRAND 266 268 {ECO:0000244|PDB:1XO2}.
HELIX 271 280 {ECO:0000244|PDB:1BLX}.
TURN 285 287 {ECO:0000244|PDB:1BLX}.
HELIX 291 295 {ECO:0000244|PDB:1BLX}.
HELIX 298 300 {ECO:0000244|PDB:1BLX}.
SEQUENCE 326 AA; 36938 MW; 571733EE6BE7FD4A CRC64;
MEKDGLCRAD QQYECVAEIG EGAYGKVFKA RDLKNGGRFV ALKRVRVQTG EEGMPLSTIR
EVAVLRHLET FEHPNVVRLF DVCTVSRTDR ETKLTLVFEH VDQDLTTYLD KVPEPGVPTE
TIKDMMFQLL RGLDFLHSHR VVHRDLKPQN ILVTSSGQIK LADFGLARIY SFQMALTSVV
VTLWYRAPEV LLQSSYATPV DLWSVGCIFA EMFRRKPLFR GSSDVDQLGK ILDVIGLPGE
EDWPRDVALP RQAFHSKSAQ PIEKFVTDID ELGKDLLLKC LTFNPAKRIS AYSALSHPYF
QDLERCKENL DSHLPPSQNT SELNTA


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