Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Cyclin-dependent kinase 4 (EC 2.7.11.22) (Cell division protein kinase 4) (PSK-J3)

 CDK4_HUMAN              Reviewed;         303 AA.
P11802; B2R9A0; B4DNF9; O00576; Q6FG61;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
22-NOV-2017, entry version 215.
RecName: Full=Cyclin-dependent kinase 4;
EC=2.7.11.22;
AltName: Full=Cell division protein kinase 4;
AltName: Full=PSK-J3;
Name=CDK4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Hanks S.K.;
Submitted (FEB-1987) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9192850; DOI=10.1006/geno.1997.4727;
Elkahloun A.G., Krizman D.B., Wang Z., Hofmann T.A., Roe B.A.,
Meltzer P.S.;
"Transcript mapping in a 46-kb sequenced region at the core of 12q13.3
amplification in human cancers.";
Genomics 42:295-301(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CMM3 CYS-24, AND
CHARACTERIZATION OF VARIANT CYS-24.
PubMed=7652577; DOI=10.1126/science.7652577;
Wolfel T., Hauer M., Schneider J., Serrano M., Wolfel C.,
Klehmann-Hieb E., De Plaen E., Hankeln T.,
Meyer Zum Bueschenfelde K.-H., Beach D.;
"A p16INK4a-insensitive CDK4 mutant targeted by cytolytic T
lymphocytes in a human melanoma.";
Science 269:1281-1284(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CMM3 CYS-24, AND
CHARACTERIZATION OF VARIANT CYS-24.
PubMed=8528263; DOI=10.1038/ng0196-97;
Zuo L., Weger J., Yang Q., Goldstein A.M., Tucker M.A., Walker G.J.,
Hayward N., Dracopoli N.C.;
"Germline mutations in the p16INK4a binding domain of CDK4 in familial
melanoma.";
Nat. Genet. 12:97-99(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-82.
NIEHS SNPs program;
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Embryo;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[9]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
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).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 88-188 (ISOFORM 1).
PubMed=2948189; DOI=10.1073/pnas.84.2.388;
Hanks S.K.;
"Homology probing: identification of cDNA clones encoding members of
the protein-serine kinase family.";
Proc. Natl. Acad. Sci. U.S.A. 84:388-392(1987).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-182.
PubMed=8221695;
Khatib Z.A., Matsushime H., Valentine M., Shapiro D.N., Sherr C.J.,
Look A.T.;
"Coamplification of the CDK4 gene with MDM2 and GLI in human
sarcomas.";
Cancer Res. 53:5535-5541(1993).
[13]
FUNCTION.
PubMed=9003781;
Kitagawa M., Higashi H., Jung H.K., Suzuki-Takahashi I., Ikeda M.,
Tamai K., Kato J., Segawa K., Yoshida E., Nishimura S., Taya Y.;
"The consensus motif for phosphorylation by cyclin D1-Cdk4 is
different from that for phosphorylation by cyclin A/E-Cdk2.";
EMBO J. 15:7060-7069(1996).
[14]
INTERACTION WITH CDKN1A; CCND1 AND CCND3, SUBCELLULAR LOCATION, AND
CATALYTIC ACTIVITY.
PubMed=9106657; DOI=10.1101/gad.11.7.847;
LaBaer J., Garrett M.D., Stevenson L.F., Slingerland J.M., Sandhu C.,
Chou H.S., Fattaey A., Harlow E.;
"New functional activities for the p21 family of CDK inhibitors.";
Genes Dev. 11:847-862(1997).
[15]
INTERACTION WITH SEI1.
PubMed=10580009; DOI=10.1101/gad.13.22.3027;
Sugimoto M., Nakamura T., Ohtani N., Hampson L., Hampson I.N.,
Shimamoto A., Furuichi Y., Okumura K., Niwa S., Taya Y., Hara E.;
"Regulation of CDK4 activity by a novel CDK4-binding protein, p34(SEI-
1).";
Genes Dev. 13:3027-3033(1999).
[16]
INTERACTION WITH CEBPA.
PubMed=15107404; DOI=10.1101/gad.1183304;
Wang G.L., Iakova P., Wilde M., Awad S., Timchenko N.A.;
"Liver tumors escape negative control of proliferation via PI3K/Akt-
mediated block of C/EBP alpha growth inhibitory activity.";
Genes Dev. 18:912-925(2004).
[17]
FUNCTION.
PubMed=15241418; DOI=10.1038/nature02650;
Matsuura I., Denissova N.G., Wang G., He D., Long J., Liu F.;
"Cyclin-dependent kinases regulate the antiproliferative function of
Smads.";
Nature 430:226-231(2004).
[18]
INTERACTION WITH ZNF655.
PubMed=15558030; DOI=10.1038/sj.onc.1208043;
Houlard M., Romero-Portillo F., Germani A., Depaux A.,
Regnier-Ricard F., Gisselbrecht S., Varin-Blank N.;
"Characterization of VIK-1: a new Vav-interacting Kruppel-like
protein.";
Oncogene 24:28-38(2005).
[19]
PHOSPHORYLATION AT THR-172, INTERACTION WITH CCND1; CCND3; CDKN2A AND
CDKN1B, AND MUTAGENESIS OF THR-172.
PubMed=16782892; DOI=10.1128/MCB.02006-05;
Bockstaele L., Kooken H., Libert F., Paternot S., Dumont J.E.,
de Launoit Y., Roger P.P., Coulonval K.;
"Regulated activating Thr172 phosphorylation of cyclin-dependent
kinase 4(CDK4): its relationship with cyclins and CDK 'inhibitors'.";
Mol. Cell. Biol. 26:5070-5085(2006).
[20]
SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH CCND2.
PubMed=18827403; DOI=10.1247/csf.08019;
Wang Z., Xie Y., Zhang L., Zhang H., An X., Wang T., Meng A.;
"Migratory localization of cyclin D2-Cdk4 complex suggests a spatial
regulation of the G1-S transition.";
Cell Struct. Funct. 33:171-183(2008).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[22]
INTERACTION WITH CCND1.
PubMed=19124461; DOI=10.1074/jbc.M808843200;
Zhang T., Liu W.D., Saunee N.A., Breslin M.B., Lan M.S.;
"Zinc finger transcription factor INSM1 interrupts cyclin D1 and CDK4
binding and induces cell cycle arrest.";
J. Biol. Chem. 284:5574-5581(2009).
[23]
INTERACTION WITH CDKN1B, PHOSPHORYLATION, AND CATALYTIC ACTIVITY.
PubMed=19075005; DOI=10.1128/MCB.00898-08;
Ray A., James M.K., Larochelle S., Fisher R.P., Blain S.W.;
"p27Kip1 inhibits cyclin D-cyclin-dependent kinase 4 by two
independent modes.";
Mol. Cell. Biol. 29:986-999(2009).
[24]
PHOSPHORYLATION AT THR-172, ENZYME REGULATION, AND MUTAGENESIS OF
PRO-173.
PubMed=19487459; DOI=10.1128/MCB.01823-08;
Bockstaele L., Bisteau X., Paternot S., Roger P.P.;
"Differential regulation of cyclin-dependent kinase 4 (CDK4) and CDK6,
evidence that CDK4 might not be activated by CDK7, and design of a
CDK6 activating mutation.";
Mol. Cell. Biol. 29:4188-4200(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172, 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).
[26]
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).
[27]
INTERACTION WITH FNIP1 AND FNIP2.
PubMed=27353360; DOI=10.1038/ncomms12037;
Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D.,
Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W.,
Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S.,
Marston Linehan W., Bratslavsky G., Mollapour M.;
"The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and
enhance drug binding.";
Nat. Commun. 7:12037-12037(2016).
[28]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF THR-172-PHOSPHORYLATED WILD
TYPE AND MUTANTS ALA-172; PHE-172 AND ASP-172 IN COMPLEX WITH CCND1,
IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT THR-172, AND
CATALYTIC ACTIVITY.
PubMed=19237565; DOI=10.1073/pnas.0809645106;
Day P.J., Cleasby A., Tickle I.J., O'Reilly M., Coyle J.E.,
Holding F.P., McMenamin R.L., Yon J., Chopra R., Lengauer C.,
Jhoti H.;
"Crystal structure of human CDK4 in complex with a D-type cyclin.";
Proc. Natl. Acad. Sci. U.S.A. 106:4166-4170(2009).
[29]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF NONPHOSPHORYLATED FORM IN
COMPLEX WITH CCND3, PHOSPHORYLATION AT THR-172, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=19237555; DOI=10.1073/pnas.0809674106;
Takaki T., Echalier A., Brown N.R., Hunt T., Endicott J.A.,
Noble M.E.;
"The structure of CDK4/cyclin D3 has implications for models of CDK
activation.";
Proc. Natl. Acad. Sci. U.S.A. 106:4171-4176(2009).
[30]
VARIANT CMM3 SER-41.
PubMed=9311594;
DOI=10.1002/(SICI)1097-0215(19970904)72:5<780::AID-IJC13>3.0.CO;2-D;
Guldberg P., Kirkin A.F., Gronbaek K., thor Straten P., Ahrenkiel V.,
Zeuthen J.;
"Complete scanning of the CDK4 gene by denaturing gradient gel
electrophoresis: a novel missense mutation but low overall frequency
of mutations in sporadic metastatic malignant melanoma.";
Int. J. Cancer 72:780-783(1997).
[31]
VARIANT CMM3 HIS-24.
PubMed=9425228; DOI=10.1093/hmg/7.2.209;
Soufir N., Avril M.-F., Chompret A., Demenais F., Bombled J.,
Spatz A., Stoppa-Lyonnet D., Benard J., Bressac-De Paillerets B.;
"Prevalence of p16 and CDK4 germline mutations in 48 melanoma-prone
families in France.";
Hum. Mol. Genet. 7:209-216(1998).
[32]
ERRATUM.
Soufir N., Avril M.-F., Chompret A., Demenais F., Bombled J.,
Spatz A., Stoppa-Lyonnet D., Benard J., Bressac-De Paillerets B.;
Hum. Mol. Genet. 7:941-941(1998).
[33]
VARIANT [LARGE SCALE ANALYSIS] HIS-122.
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: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes
that phosphorylate and inhibit members of the retinoblastoma (RB)
protein family including RB1 and regulate the cell-cycle during
G(1)/S transition. Phosphorylation of RB1 allows dissociation of
the transcription factor E2F from the RB/E2F complexes and the
subsequent transcription of E2F target genes which are responsible
for the progression through the G(1) phase. Hypophosphorylates RB1
in early G(1) phase. Cyclin D-CDK4 complexes are major integrators
of various mitogenenic and antimitogenic signals. Also
phosphorylates SMAD3 in a cell-cycle-dependent manner and
represses its transcriptional activity. Component of the ternary
complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation
and activity of the cyclin D-CDK4 complex.
{ECO:0000269|PubMed:15241418, ECO:0000269|PubMed:18827403,
ECO:0000269|PubMed:9003781}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:19075005, ECO:0000269|PubMed:19237565,
ECO:0000269|PubMed:9106657}.
-!- ENZYME REGULATION: Both phosphorylation at Thr-172 and binding of
a D-type cyclin are necessary for enzymatic activity. Full
activation of the cyclin-D-CDK4 complex appears to require other
factors such as recruitment of the substrate via a substrate
recruitment motif, and/or formation of the CDKN1B ternary complex.
Inhibited by INK4 family members. In resting cells, the non-
tyrosine-phosphorylated form of CDKN1B prevents phosphorylation at
Thr-172 and inactivation, while, in proliferating cells, tyrosine
phosphorylation of CDKN1B allows phosphorylation of Thr-172 of
CDK4 and subsequennt activation. {ECO:0000269|PubMed:19487459}.
-!- SUBUNIT: Component of the D-CDK4 complex, composed of CDK4 and
some D-type G1 cyclin (CCND1, CCND2 or CCND3). Interacts directly
in the complex with CCND1, CCND2 or CCND3. Interacts with SEI1 and
ZNF655. Forms a ternary complex, cyclin D-CDK4-CDKN1B, involved in
modulating CDK4 enzymatic activity. Interacts directly with CDKN1B
(phosphorylated on 'Tyr-88' and 'Tyr-89'); the interaction allows
assembly of the cyclin D-CDK4 complex, Thr-172 phosphorylation,
nuclear translocation and enhances the cyclin D-CDK4 complex
activity. CDK4 activity is either inhibited or enhanced depending
on stoichiometry of complex. The non-tyrosine-phosphorylated form
of CDKN1B prevents T-loop phosphorylation of CDK4 producing
inactive CDK4. Interacts (unphosphorylated form) with CDK2. Also
forms ternary complexes with CDKN1A or CDKN2A. Interacts directly
with CDKN1A (via its N-terminal); the interaction promotes the
assembly of the cyclin D-CDK4 complex, its nuclear translocation
and promotes the cyclin D-dependent enzyme activity of CDK4.
Interacts with CCND1; the interaction is prevented with the
binding of CCND1 to INSM1 during cell cycle progression. Interacts
with CEBPA (when phosphorylated) (PubMed:15107404). Interacts with
FNIP1 and FNIP2 (PubMed:27353360). {ECO:0000250|UniProtKB:P30285,
ECO:0000269|PubMed:10580009, ECO:0000269|PubMed:15107404,
ECO:0000269|PubMed:15558030, ECO:0000269|PubMed:16782892,
ECO:0000269|PubMed:18827403, ECO:0000269|PubMed:19075005,
ECO:0000269|PubMed:19124461, ECO:0000269|PubMed:19237555,
ECO:0000269|PubMed:19237565, ECO:0000269|PubMed:27353360,
ECO:0000269|PubMed:9106657}.
-!- INTERACTION:
P24385:CCND1; NbExp=29; IntAct=EBI-295644, EBI-375001;
P30279:CCND2; NbExp=12; IntAct=EBI-295644, EBI-748789;
P30281:CCND3; NbExp=27; IntAct=EBI-295644, EBI-375013;
Q16543:CDC37; NbExp=11; IntAct=EBI-295644, EBI-295634;
P50613:CDK7; NbExp=2; IntAct=EBI-295644, EBI-1245958;
P38936:CDKN1A; NbExp=5; IntAct=EBI-295644, EBI-375077;
P46527:CDKN1B; NbExp=6; IntAct=EBI-295644, EBI-519280;
P42771:CDKN2A; NbExp=13; IntAct=EBI-295644, EBI-375053;
P42772:CDKN2B; NbExp=15; IntAct=EBI-295644, EBI-711280;
P42773:CDKN2C; NbExp=17; IntAct=EBI-295644, EBI-711290;
P55273:CDKN2D; NbExp=18; IntAct=EBI-295644, EBI-745859;
Q9UJC3:HOOK1; NbExp=9; IntAct=EBI-295644, EBI-746704;
P08238:HSP90AB1; NbExp=3; IntAct=EBI-295644, EBI-352572;
Q9UKT9:IKZF3; NbExp=4; IntAct=EBI-295644, EBI-747204;
P01106:MYC; NbExp=2; IntAct=EBI-295644, EBI-447544;
P28749:RBL1; NbExp=2; IntAct=EBI-295644, EBI-971402;
Q8N720:ZNF655; NbExp=3; IntAct=EBI-295644, EBI-625509;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane.
Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex
in the cytoplasm as cells progress through G(1) phase. The complex
accumulates on the nuclear membrane and enters the nucleus on
transition from G(1) to S phase. Also present in nucleoli and
heterochromatin lumps. Colocalizes with RB1 after release into the
nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P11802-1; Sequence=Displayed;
Name=2;
IsoId=P11802-2; Sequence=VSP_056487;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylation at Thr-172 is required for enzymatic
activity. Phosphorylated, in vitro, at this site by CCNH-CDK7,
but, in vivo, appears to be phosphorylated by a proline-directed
kinase. In the cyclin D-CDK4-CDKN1B complex, this phosphorylation
and consequent CDK4 enzyme activity, is dependent on the tyrosine
phosphorylation state of CDKN1B. Thus, in proliferating cells,
CDK4 within the complex is phosphorylated on Thr-172 in the T-
loop. In resting cells, phosphorylation on Thr-172 is prevented by
the non-tyrosine-phosphorylated form of CDKN1B.
{ECO:0000269|PubMed:16782892, ECO:0000269|PubMed:19075005,
ECO:0000269|PubMed:19237555, ECO:0000269|PubMed:19237565,
ECO:0000269|PubMed:19487459}.
-!- DISEASE: Melanoma, cutaneous malignant 3 (CMM3) [MIM:609048]: A
malignant neoplasm of melanocytes, arising de novo or from a pre-
existing benign nevus, which occurs most often in the skin but
also may involve other sites. {ECO:0000269|PubMed:7652577,
ECO:0000269|PubMed:8528263, ECO:0000269|PubMed:9311594,
ECO:0000269|PubMed:9425228}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CDK4ID238ch12q14.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdk4/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M14505; AAA35673.1; -; mRNA.
EMBL; U81031; AAC39521.2; -; Genomic_DNA.
EMBL; Z48970; CAA88834.1; -; mRNA.
EMBL; U37022; AAC50506.1; -; Genomic_DNA.
EMBL; AF507942; AAM23014.1; -; Genomic_DNA.
EMBL; AK297901; BAG60221.1; -; mRNA.
EMBL; AK313701; BAG36447.1; -; mRNA.
EMBL; CR407668; CAG28596.1; -; mRNA.
EMBL; CR542247; CAG47043.1; -; mRNA.
EMBL; AC025165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW97058.1; -; Genomic_DNA.
EMBL; BC003644; AAH03644.1; -; mRNA.
EMBL; BC005864; AAH05864.1; -; mRNA.
EMBL; BC010153; AAH10153.1; -; mRNA.
EMBL; S67448; AAD13991.1; -; Genomic_DNA.
CCDS; CCDS8953.1; -. [P11802-1]
PIR; I52695; I52695.
PIR; S52841; S52841.
RefSeq; NP_000066.1; NM_000075.3. [P11802-1]
UniGene; Hs.95577; -.
PDB; 1LD2; Model; -; A=1-303.
PDB; 2W96; X-ray; 2.30 A; B=1-303.
PDB; 2W99; X-ray; 2.80 A; B=1-303.
PDB; 2W9F; X-ray; 2.85 A; B=1-303.
PDB; 2W9Z; X-ray; 2.45 A; B=1-303.
PDB; 3G33; X-ray; 3.00 A; A/C=1-303.
PDB; 5FWK; EM; 3.90 A; K=1-303.
PDB; 5FWL; EM; 9.00 A; K=1-303.
PDB; 5FWM; EM; 8.00 A; K=1-303.
PDB; 5FWP; EM; 7.20 A; K=1-303.
PDBsum; 1LD2; -.
PDBsum; 2W96; -.
PDBsum; 2W99; -.
PDBsum; 2W9F; -.
PDBsum; 2W9Z; -.
PDBsum; 3G33; -.
PDBsum; 5FWK; -.
PDBsum; 5FWL; -.
PDBsum; 5FWM; -.
PDBsum; 5FWP; -.
ProteinModelPortal; P11802; -.
SMR; P11802; -.
BioGrid; 107454; 165.
CORUM; P11802; -.
DIP; DIP-875N; -.
ELM; P11802; -.
IntAct; P11802; 96.
MINT; MINT-1201237; -.
STRING; 9606.ENSP00000257904; -.
BindingDB; P11802; -.
ChEMBL; CHEMBL331; -.
DrugBank; DB03496; Flavopiridol.
DrugBank; DB09073; Palbociclib.
DrugBank; DB02733; Purvalanol.
DrugBank; DB11730; Ribociclib.
GuidetoPHARMACOLOGY; 1976; -.
iPTMnet; P11802; -.
PhosphoSitePlus; P11802; -.
BioMuta; CDK4; -.
DMDM; 1168867; -.
EPD; P11802; -.
MaxQB; P11802; -.
PaxDb; P11802; -.
PeptideAtlas; P11802; -.
PRIDE; P11802; -.
DNASU; 1019; -.
Ensembl; ENST00000257904; ENSP00000257904; ENSG00000135446. [P11802-1]
GeneID; 1019; -.
KEGG; hsa:1019; -.
UCSC; uc001spv.4; human. [P11802-1]
CTD; 1019; -.
DisGeNET; 1019; -.
EuPathDB; HostDB:ENSG00000135446.16; -.
GeneCards; CDK4; -.
HGNC; HGNC:1773; CDK4.
HPA; CAB069405; -.
HPA; HPA006024; -.
MalaCards; CDK4; -.
MIM; 123829; gene.
MIM; 609048; phenotype.
neXtProt; NX_P11802; -.
OpenTargets; ENSG00000135446; -.
Orphanet; 99970; Dedifferentiated liposarcoma.
Orphanet; 618; Familial melanoma.
Orphanet; 99971; Well-differentiated liposarcoma.
PharmGKB; PA102; -.
eggNOG; KOG0594; Eukaryota.
eggNOG; ENOG410XPP3; LUCA.
GeneTree; ENSGT00900000140881; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P11802; -.
KO; K02089; -.
OMA; ARIYSCH; -.
OrthoDB; EOG091G0I1Q; -.
PhylomeDB; P11802; -.
TreeFam; TF101022; -.
BRENDA; 2.7.11.22; 2681.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
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-3214858; RMTs methylate histone arginines.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-8849470; PTK6 Regulates Cell Cycle.
Reactome; R-HSA-8878166; Transcriptional regulation by RUNX2.
Reactome; R-HSA-912446; Meiotic recombination.
SignaLink; P11802; -.
SIGNOR; P11802; -.
ChiTaRS; CDK4; human.
EvolutionaryTrace; P11802; -.
GeneWiki; Cyclin-dependent_kinase_4; -.
GenomeRNAi; 1019; -.
PRO; PR:P11802; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000135446; -.
CleanEx; HS_CDK4; -.
ExpressionAtlas; P11802; baseline and differential.
Genevisible; P11802; HS.
GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
GO; GO:0000785; C:chromatin; IDA:UniProtKB.
GO; GO:0097129; C:cyclin D2-CDK4 complex; IEA:Ensembl.
GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:BHF-UCL.
GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; TAS:Reactome.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
GO; GO:1904637; P:cellular response to ionomycin; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:1904628; P:cellular response to phorbol 13-acetate 12-myristate; IEA:Ensembl.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:BHF-UCL.
GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0071157; P:negative regulation of cell cycle arrest; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0045787; P:positive regulation of cell cycle; TAS:Reactome.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:0045793; P:positive regulation of cell size; IEA:Ensembl.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:BHF-UCL.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IDA:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:BHF-UCL.
GO; GO:0010468; P:regulation of gene expression; IMP:BHF-UCL.
GO; GO:0046626; P:regulation of insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:0046890; P:regulation of lipid biosynthetic process; IEA:Ensembl.
GO; GO:0050994; P:regulation of lipid catabolic process; IEA:Ensembl.
GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEP:UniProtKB.
GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
GO; GO:0010288; P:response to lead ion; IEA:Ensembl.
GO; GO:0010033; P:response to organic substance; IBA:GO_Central.
GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; Alternative splicing; ATP-binding;
Cell cycle; Cell division; Complete proteome; Cytoplasm;
Disease mutation; Kinase; Membrane; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 303 Cyclin-dependent kinase 4.
/FTId=PRO_0000085778.
DOMAIN 6 295 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 12 20 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 50 56 Required for binding D-type cyclins.
COMPBIAS 42 48 Poly-Gly.
ACT_SITE 140 140 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 35 35 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 172 172 Phosphothreonine.
{ECO:0000244|PubMed:19369195,
ECO:0000269|PubMed:16782892,
ECO:0000269|PubMed:19237555,
ECO:0000269|PubMed:19237565,
ECO:0000269|PubMed:19487459}.
VAR_SEQ 1 120 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056487.
VARIANT 24 24 R -> C (in CMM3; somatic and familial;
generates a dominant oncogene resistant
to inhibition by p16(INK4a);
dbSNP:rs11547328).
{ECO:0000269|PubMed:7652577,
ECO:0000269|PubMed:8528263}.
/FTId=VAR_006200.
VARIANT 24 24 R -> H (in CMM3; dbSNP:rs104894340).
{ECO:0000269|PubMed:9425228}.
/FTId=VAR_006201.
VARIANT 41 41 N -> S (in CMM3; sporadic;
dbSNP:rs144890720).
{ECO:0000269|PubMed:9311594}.
/FTId=VAR_021152.
VARIANT 82 82 R -> Q (in dbSNP:rs3211612).
{ECO:0000269|Ref.5}.
/FTId=VAR_029153.
VARIANT 122 122 R -> H (in dbSNP:rs34386532).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041976.
MUTAGEN 172 172 T->A: Weak enzyme activity towards RB1,
but no effect on binding of CCDN1 nor
CCDN3. {ECO:0000269|PubMed:16782892}.
MUTAGEN 172 172 T->E: Retains moderate enzyme activity.
{ECO:0000269|PubMed:16782892}.
MUTAGEN 173 173 P->S: No effect on in vitro
phosphorylation by CDK7. Greatly reduced
T-172 phosphorylation and enzyme
activity. {ECO:0000269|PubMed:19487459}.
CONFLICT 117 117 I -> L (in Ref. 6; BAG36447).
{ECO:0000305}.
STRAND 7 13 {ECO:0000244|PDB:2W96}.
STRAND 15 17 {ECO:0000244|PDB:3G33}.
STRAND 20 24 {ECO:0000244|PDB:2W96}.
TURN 26 28 {ECO:0000244|PDB:2W96}.
STRAND 31 40 {ECO:0000244|PDB:2W96}.
HELIX 51 63 {ECO:0000244|PDB:2W96}.
HELIX 64 66 {ECO:0000244|PDB:2W96}.
STRAND 74 82 {ECO:0000244|PDB:2W96}.
STRAND 84 94 {ECO:0000244|PDB:2W96}.
STRAND 97 99 {ECO:0000244|PDB:2W9Z}.
HELIX 100 105 {ECO:0000244|PDB:2W96}.
TURN 109 111 {ECO:0000244|PDB:2W9F}.
HELIX 114 133 {ECO:0000244|PDB:2W96}.
TURN 143 145 {ECO:0000244|PDB:2W96}.
STRAND 146 148 {ECO:0000244|PDB:2W96}.
TURN 150 152 {ECO:0000244|PDB:2W9Z}.
STRAND 154 156 {ECO:0000244|PDB:2W96}.
HELIX 162 169 {ECO:0000244|PDB:2W96}.
HELIX 172 175 {ECO:0000244|PDB:3G33}.
TURN 183 185 {ECO:0000244|PDB:2W96}.
STRAND 186 189 {ECO:0000244|PDB:2W96}.
HELIX 195 208 {ECO:0000244|PDB:2W96}.
STRAND 209 211 {ECO:0000244|PDB:2W96}.
HELIX 219 230 {ECO:0000244|PDB:2W96}.
TURN 235 237 {ECO:0000244|PDB:3G33}.
STRAND 242 244 {ECO:0000244|PDB:2W99}.
HELIX 246 248 {ECO:0000244|PDB:3G33}.
HELIX 257 260 {ECO:0000244|PDB:2W99}.
HELIX 266 275 {ECO:0000244|PDB:2W96}.
HELIX 280 282 {ECO:0000244|PDB:2W96}.
HELIX 286 290 {ECO:0000244|PDB:2W96}.
SEQUENCE 303 AA; 33730 MW; 0916A0C07403A33A CRC64;
MATSRYEPVA EIGVGAYGTV YKARDPHSGH FVALKSVRVP NGGGGGGGLP ISTVREVALL
RRLEAFEHPN VVRLMDVCAT SRTDREIKVT LVFEHVDQDL RTYLDKAPPP GLPAETIKDL
MRQFLRGLDF LHANCIVHRD LKPENILVTS GGTVKLADFG LARIYSYQMA LTPVVVTLWY
RAPEVLLQST YATPVDMWSV GCIFAEMFRR KPLFCGNSEA DQLGKIFDLI GLPPEDDWPR
DVSLPRGAFP PRGPRPVQSV VPEMEESGAQ LLLEMLTFNP HKRISAFRAL QHSYLHKDEG
NPE


Related products :

Catalog number Product name Quantity
EIAAB06522 CDC2L6,CDC2-related protein kinase 6,CDK11,CDK19,Cell division cycle 2-like protein kinase 6,Cell division protein kinase 19,Cyclin-dependent kinase 11,Cyclin-dependent kinase 19,Death-preventing kina
EIAAB06524 CAK-kinase p42,CCRK,CDCH,CDK20,CDK-activating kinase p42,Cell cycle-related kinase,Cell division protein kinase 20,Cyclin-dependent kinase 20,Cyclin-dependent protein kinase H,Cyclin-kinase-activating
EIAAB06523 CAK-kinase p42,Ccrk,Cdch,Cdk20,CDK-activating kinase p42,CDK-related protein kinase PNQLARE,Cell cycle-related kinase,Cell division protein kinase 20,Cyclin-dependent kinase 20,Cyclin-dependent protei
EIAAB06263 CDC2L2,CDC2L3,CDK11A,Cell division cycle 2-like protein kinase 2,Cell division protein kinase 11A,Cyclin-dependent kinase 11A,Galactosyltransferase-associated protein kinase p58_GTA,Homo sapiens,Human
EIAAB06533 C-2K,CDC2L4,CDK9,Cell division cycle 2-like protein kinase 4,Cell division protein kinase 9,Cyclin-dependent kinase 9,Homo sapiens,Human,Serine_threonine-protein kinase PITALRE,TAK,Tat-associated kina
EIAAB06506 Bos taurus,Bovine,CDC2L,CDC2L5,CDC2-related protein kinase 5,CDK13,Cell division cycle 2-like protein kinase 5,Cell division protein kinase 13,Cyclin-dependent kinase 13
EIAAB06505 Cdc2l5,CDC2-related protein kinase 5,Cdk13,Cell division cycle 2-like protein kinase 5,Cell division protein kinase 13,Cyclin-dependent kinase 13,Kiaa1791,Mouse,Mus musculus
EIAAB06521 Cdc2l6,CDC2-related protein kinase 6,Cdk19,Cell division cycle 2-like protein kinase 6,Cell division protein kinase 19,Cyclin-dependent kinase 19,Kiaa1028,Mouse,Mus musculus
EIAAB06500 Cdc2l1,Cdk11,Cell division cycle 2-like protein kinase 1,Cell division protein kinase 11,Cyclin-dependent kinase 11,Galactosyltransferase-associated protein kinase p58_GTA,Mouse,Mus musculus,PITSLRE s
EIAAB06264 CDC2L1,CDK11,CDK11B,Cell division cycle 2-like protein kinase 1,Cell division protein kinase 11B,CLK-1,Cyclin-dependent kinase 11B,Galactosyltransferase-associated protein kinase p58_GTA,Homo sapiens,
EIAAB06499 Cdc2l1,Cdk11,Cell division cycle 2-like protein kinase 1,Cell division protein kinase 11,Cyclin-dependent kinase 11,Galactosyltransferase-associated protein kinase p58_GTA,PITSLRE serine_threonine-pro
EIAAB06507 CDC2L,CDC2L5,CDC2-related protein kinase 5,CDK13,Cell division cycle 2-like protein kinase 5,Cell division protein kinase 13,CHED,Cholinesterase-related cell division controller,Cyclin-dependent kinas
18-003-44328 Cell division protein kinase 9 - EC 2.7.11.22; EC 2.7.11.23; Cyclin-dependent kinase 9; Serine_threonine-protein kinase PITALRE; C-2K; Cell division cycle 2-like protein kinase 4 Polyclonal 0.1 mg Protein A
U1888h CLIA kit CDC2,CDC28A,CDK1,CDK1,CDKN1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Homo sapiens,Human,p34 protein kinase,P34CDC2 96T
U1888h CLIA CDC2,CDC28A,CDK1,CDK1,CDKN1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Homo sapiens,Human,p34 protein kinase,P34CDC2 96T
E1888h ELISA CDC2,CDC28A,CDK1,CDK1,CDKN1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Homo sapiens,Human,p34 protein kinase,P34CDC2 96T
E1888h ELISA kit CDC2,CDC28A,CDK1,CDK1,CDKN1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Homo sapiens,Human,p34 protein kinase,P34CDC2 96T
U1888m CLIA kit Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Mouse,Mus musculus,p34 protein kinase 96T
E1888m ELISA Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Mouse,Mus musculus,p34 protein kinase 96T
U1888m CLIA Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Mouse,Mus musculus,p34 protein kinase 96T
E1888r ELISA Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,p34 protein kinase,Rat,Rattus norvegicus 96T
U1888r CLIA Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,p34 protein kinase,Rat,Rattus norvegicus 96T
E1888r ELISA kit Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,p34 protein kinase,Rat,Rattus norvegicus 96T
U1888r CLIA kit Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,p34 protein kinase,Rat,Rattus norvegicus 96T
E1888m ELISA kit Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Mouse,Mus musculus,p34 protein kinase 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur