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 9 (EC 2.7.11.22) (EC 2.7.11.23) (C-2K) (Cell division cycle 2-like protein kinase 4) (Cell division protein kinase 9) (Serine/threonine-protein kinase PITALRE) (Tat-associated kinase complex catalytic subunit)

 CDK9_HUMAN              Reviewed;         372 AA.
P50750; Q5JU24; Q5JU25; Q5U006; Q96TF1;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 3.
22-NOV-2017, entry version 201.
RecName: Full=Cyclin-dependent kinase 9;
EC=2.7.11.22;
EC=2.7.11.23;
AltName: Full=C-2K;
AltName: Full=Cell division cycle 2-like protein kinase 4;
AltName: Full=Cell division protein kinase 9;
AltName: Full=Serine/threonine-protein kinase PITALRE;
AltName: Full=Tat-associated kinase complex catalytic subunit;
Name=CDK9; Synonyms=CDC2L4, TAK;
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).
PubMed=8170997; DOI=10.1073/pnas.91.9.3834;
Grana X., de Luca A., Sang N., Fu Y., Claudio P.P., Rosenblatt J.,
Morgan D.O., Giordano A.;
"PITALRE, a nuclear CDC2-related protein kinase that phosphorylates
the retinoblastoma protein in vitro.";
Proc. Natl. Acad. Sci. U.S.A. 91:3834-3838(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-231.
PubMed=7695608; DOI=10.1006/bbrc.1995.1375;
Best J.L., Presky D.H., Swerlick R.A., Burns D.K., Chu W.;
"Cloning of a full-length cDNA sequence encoding a cdc2-related
protein kinase from human endothelial cells.";
Biochem. Biophys. Res. Commun. 208:562-568(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-231.
PubMed=10903437; DOI=10.1016/S0378-1119(00)00215-8;
Liu H., Rice A.P.;
"Genomic organization and characterization of promoter function of the
human CDK9 gene.";
Gene 252:51-59(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix;
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]
INTERACTION WITH HIV TAT.
PubMed=9491887; DOI=10.1016/S0092-8674(00)80939-3;
Wei P., Garber M.E., Fang S.-M., Fischer W.H., Jones K.A.;
"A novel CDK9-associated C-type cyclin interacts directly with HIV-1
Tat and mediates its high-affinity, loop-specific binding to TAR
RNA.";
Cell 92:451-462(1998).
[9]
FUNCTION.
PubMed=9857195; DOI=10.1093/emboj/17.24.7395;
Wada T., Takagi T., Yamaguchi Y., Watanabe D., Handa H.;
"Evidence that P-TEFb alleviates the negative effect of DSIF on RNA
polymerase II-dependent transcription in vitro.";
EMBO J. 17:7395-7403(1998).
[10]
IDENTIFICATION IN A COMPLEX WITH CCNT1 AND CCNT2.
PubMed=9499409; DOI=10.1101/gad.12.5.755;
Peng J.-M., Zhu Y., Milton J.T., Price D.H.;
"Identification of multiple cyclin subunits of human P-TEFb.";
Genes Dev. 12:755-762(1998).
[11]
FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH HTATSF1; CCNT1; RNA POL
II; SUPT5H AND NCL.
PubMed=10393184; DOI=10.1093/emboj/18.13.3688;
Parada C.A., Roeder R.G.;
"A novel RNA polymerase II-containing complex potentiates Tat-enhanced
HIV-1 transcription.";
EMBO J. 18:3688-3701(1999).
[12]
FUNCTION, AND INTERACTION WITH CCNK.
PubMed=10574912; DOI=10.1074/jbc.274.49.34527;
Fu T.J., Peng J., Lee G., Price D.H., Flores O.;
"Cyclin K functions as a CDK9 regulatory subunit and participates in
RNA polymerase II transcription.";
J. Biol. Chem. 274:34527-34530(1999).
[13]
FUNCTION.
PubMed=10912001; DOI=10.1016/S1097-2765(00)80272-5;
Wada T., Orphanides G., Hasegawa J., Kim D.-K., Shima D.,
Yamaguchi Y., Fukuda A., Hisatake K., Oh S., Reinberg D., Handa H.;
"FACT relieves DSIF/NELF-mediated inhibition of transcriptional
elongation and reveals functional differences between P-TEFb and
TFIIH.";
Mol. Cell 5:1067-1072(2000).
[14]
FUNCTION.
PubMed=10757782; DOI=10.1128/MCB.20.9.2970-2983.2000;
Ivanov D., Kwak Y.T., Guo J., Gaynor R.B.;
"Domains in the SPT5 protein that modulate its transcriptional
regulatory properties.";
Mol. Cell. Biol. 20:2970-2983(2000).
[15]
PHOSPHORYLATION BY PKA, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT
SER-347; THR-350; SER-353; THR-354 AND SER-357, INTERACTION WITH HIV
TAT, AND MUTAGENESIS OF 347-SER--SER-357 AND ASP-167.
PubMed=10958691; DOI=10.1128/MCB.20.18.6958-6969.2000;
Garber M.E., Mayall T.P., Suess E.M., Meisenhelder J., Thompson N.E.,
Jones K.A.;
"CDK9 autophosphorylation regulates high-affinity binding of the human
immunodeficiency virus type 1 tat-P-TEFb complex to TAR RNA.";
Mol. Cell. Biol. 20:6958-6969(2000).
[16]
FUNCTION, AND MUTAGENESIS OF ASP-167 AND THR-186.
PubMed=11145967; DOI=10.1074/jbc.M010908200;
Kim J.B., Sharp P.A.;
"Positive transcription elongation factor B phosphorylates hSPT5 and
RNA polymerase II carboxyl-terminal domain independently of cyclin-
dependent kinase-activating kinase.";
J. Biol. Chem. 276:12317-12323(2001).
[17]
FUNCTION.
PubMed=11112772; DOI=10.1074/jbc.M006130200;
Ping Y.-H., Rana T.M.;
"DSIF and NELF interact with RNA polymerase II elongation complex and
HIV-1 Tat stimulates P-TEFb-mediated phosphorylation of RNA polymerase
II and DSIF during transcription elongation.";
J. Biol. Chem. 276:12951-12958(2001).
[18]
FUNCTION.
PubMed=11575923; DOI=10.1006/jmbi.2001.4991;
Lavoie S.B., Albert A.L., Handa H., Vincent M., Bensaude O.;
"The peptidyl-prolyl isomerase Pin1 interacts with hSpt5
phosphorylated by Cdk9.";
J. Mol. Biol. 312:675-685(2001).
[19]
FUNCTION, AND INTERACTION WITH CCNK/CYCLIN K.
PubMed=11884399; DOI=10.1074/jbc.M200117200;
Lin X., Taube R., Fujinaga K., Peterlin B.M.;
"P-TEFb containing cyclin K and Cdk9 can activate transcription via
RNA.";
J. Biol. Chem. 277:16873-16878(2002).
[20]
INTERACTION WITH AFF4.
PubMed=12065898; DOI=10.1007/BF02256070;
Estable M.C., Naghavi M.H., Kato H., Xiao H., Qin J., Vahlne A.,
Roeder R.G.;
"MCEF, the newest member of the AF4 family of transcription factors
involved in leukemia, is a positive transcription elongation factor-b-
associated protein.";
J. Biomed. Sci. 9:234-245(2002).
[21]
SUBCELLULAR LOCATION.
PubMed=12115727; DOI=10.1002/jcp.10130;
Napolitano G., Licciardo P., Carbone R., Majello B., Lania L.;
"CDK9 has the intrinsic property to shuttle between nucleus and
cytoplasm, and enhanced expression of cyclin T1 promotes its nuclear
localization.";
J. Cell. Physiol. 192:209-215(2002).
[22]
FUNCTION.
PubMed=11809800; DOI=10.1128/MCB.22.4.1079-1093.2002;
Bourgeois C.F., Kim Y.K., Churcher M.J., West M.J., Karn J.;
"Spt5 cooperates with human immunodeficiency virus type 1 Tat by
preventing premature RNA release at terminator sequences.";
Mol. Cell. Biol. 22:1079-1093(2002).
[23]
FUNCTION AS MYOD1 KINASE, AND INTERACTION WITH MYOD1 AND CCNT2.
PubMed=12037670; DOI=10.1038/sj.onc.1205493;
Simone C., Stiegler P., Bagella L., Pucci B., Bellan C., De Falco G.,
De Luca A., Guanti G., Puri P.L., Giordano A.;
"Activation of MyoD-dependent transcription by cdk9/cyclin T2.";
Oncogene 21:4137-4148(2002).
[24]
INTERACTION WITH SUPT5H.
PubMed=12718890; DOI=10.1016/S1097-2765(03)00101-1;
Kwak Y.T., Guo J., Prajapati S., Park K.-J., Surabhi R.M., Miller B.,
Gehrig P., Gaynor R.B.;
"Methylation of SPT5 regulates its interaction with RNA polymerase II
and transcriptional elongation properties.";
Mol. Cell 11:1055-1066(2003).
[25]
FUNCTION.
PubMed=15564463; DOI=10.1128/JVI.78.24.13522-13533.2004;
Zhou M., Deng L., Lacoste V., Park H.U., Pumfery A., Kashanchi F.,
Brady J.N., Kumar A.;
"Coordination of transcription factor phosphorylation and histone
methylation by the P-TEFb kinase during human immunodeficiency virus
type 1 transcription.";
J. Virol. 78:13522-13533(2004).
[26]
FUNCTION.
PubMed=14701750; DOI=10.1128/MCB.24.2.787-795.2004;
Fujinaga K., Irwin D., Huang Y., Taube R., Kurosu T., Peterlin B.M.;
"Dynamics of human immunodeficiency virus transcription: P-TEFb
phosphorylates RD and dissociates negative effectors from the
transactivation response element.";
Mol. Cell. Biol. 24:787-795(2004).
[27]
IDENTIFICATION IN INACTIVE 7SK SNRNP COMPLEX, AND PHOSPHORYLATION AT
THR-186.
PubMed=15965233; DOI=10.1074/jbc.M502712200;
Li Q., Price J.P., Byers S.A., Cheng D., Peng J., Price D.H.;
"Analysis of the large inactive P-TEFb complex indicates that it
contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two P-TEFb
molecules containing Cdk9 phosphorylated at threonine 186.";
J. Biol. Chem. 280:28819-28826(2005).
[28]
FUNCTION, AND INTERACTION WITH BRD4.
PubMed=16109376; DOI=10.1016/j.molcel.2005.06.027;
Jang M.K., Mochizuki K., Zhou M., Jeong H.S., Brady J.N., Ozato K.;
"The bromodomain protein Brd4 is a positive regulatory component of P-
TEFb and stimulates RNA polymerase II-dependent transcription.";
Mol. Cell 19:523-534(2005).
[29]
FUNCTION, AND INTERACTION WITH BRD4.
PubMed=16109377; DOI=10.1016/j.molcel.2005.06.029;
Yang Z., Yik J.H., Chen R., He N., Jang M.K., Ozato K., Zhou Q.;
"Recruitment of P-TEFb for stimulation of transcriptional elongation
by the bromodomain protein Brd4.";
Mol. Cell 19:535-545(2005).
[30]
FUNCTION IN CYTOKINE SIGNALING, AND INTERACTION WITH STAT3.
PubMed=17956865; DOI=10.1074/jbc.M706458200;
Hou T., Ray S., Brasier A.R.;
"The functional role of an interleukin 6-inducible CDK9.STAT3 complex
in human gamma-fibrinogen gene expression.";
J. Biol. Chem. 282:37091-37102(2007).
[31]
IDENTIFICATION IN THE 7SK SNRNP COMPLEX.
PubMed=17643375; DOI=10.1016/j.molcel.2007.06.027;
Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C.,
Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B.,
Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B.;
"Systematic analysis of the protein interaction network for the human
transcription machinery reveals the identity of the 7SK capping
enzyme.";
Mol. Cell 27:262-274(2007).
[32]
ACETYLATION AT LYS-44 BY P300/CBP, IDENTIFICATION IN COMPLEX WITH
NCOR1; HEXIM1 AND HDAC3, AND MUTAGENESIS OF LYS-44.
PubMed=17452463; DOI=10.1128/MCB.00857-06;
Fu J., Yoon H.-G., Qin J., Wong J.;
"Regulation of P-TEFb elongation complex activity by CDK9
acetylation.";
Mol. Cell. Biol. 27:4641-4651(2007).
[33]
PHOSPHORYLATION AT THR-186, DEPHOSPHORYLATION BY PPP1CA, P-TEFB/7SK
SNRNP COMPLEX, SUBUNIT, INTERACTION WITH BRD4, AND ENZYME REGULATION.
PubMed=18483222; DOI=10.1101/gad.1636008;
Chen R., Liu M., Li H., Xue Y., Ramey W.N., He N., Ai N., Luo H.,
Zhu Y., Zhou N., Zhou Q.;
"PP2B and PP1alpha cooperatively disrupt 7SK snRNP to release P-TEFb
for transcription in response to Ca2+ signaling.";
Genes Dev. 22:1356-1368(2008).
[34]
PHOSPHORYLATION AT THR-186, AND DEPHOSPHORYLATION BY PPM1A AND PPM1B.
PubMed=18829461; DOI=10.1074/jbc.M807495200;
Wang Y., Dow E.C., Liang Y.Y., Ramakrishnan R., Liu H., Sung T.L.,
Lin X., Rice A.P.;
"Phosphatase PPM1A regulates phosphorylation of Thr-186 in the Cdk9 T-
loop.";
J. Biol. Chem. 283:33578-33584(2008).
[35]
IDENTIFICATION IN COMPLEX WITH LARP7 IN 7SK SNRNP COMPLEX.
PubMed=18249148; DOI=10.1016/j.molcel.2008.01.003;
He N., Jahchan N.S., Hong E., Li Q., Bayfield M.A., Maraia R.J.,
Luo K., Zhou Q.;
"A La-related protein modulates 7SK snRNP integrity to suppress P-
TEFb-dependent transcriptional elongation and tumorigenesis.";
Mol. Cell 29:588-599(2008).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT SER-35 (ISOFORM 2), AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[37]
ACETYLATION AT LYS-44 AND LYS-48 BY PCAF/KAT2B AND GCN5/KAT2A, ENZYME
REGULATION BY ACETYLATION, AND SUBCELLULAR LOCATION.
PubMed=18250157; DOI=10.1128/MCB.01557-07;
Sabo A., Lusic M., Cereseto A., Giacca M.;
"Acetylation of conserved lysines in the catalytic core of cyclin-
dependent kinase 9 inhibits kinase activity and regulates
transcription.";
Mol. Cell. Biol. 28:2201-2212(2008).
[38]
FUNCTION IN CYTOKINE SIGNALING, AND INTERACTION WITH RELA/P65.
PubMed=18362169; DOI=10.1128/MCB.01152-07;
Nowak D.E., Tian B., Jamaluddin M., Boldogh I., Vergara L.A.,
Choudhary S., Brasier A.R.;
"RelA Ser276 phosphorylation is required for activation of a subset of
NF-kappaB-dependent genes by recruiting cyclin-dependent kinase
9/cyclin T1 complexes.";
Mol. Cell. Biol. 28:3623-3638(2008).
[39]
FUNCTION IN HISTONE REGULATION.
PubMed=19844166; DOI=10.4161/cc.8.22.9890;
Pirngruber J., Shchebet A., Johnsen S.A.;
"Insights into the function of the human P-TEFb component CDK9 in the
regulation of chromatin modifications and co-transcriptional mRNA
processing.";
Cell Cycle 8:3636-3642(2009).
[40]
FUNCTION IN HISTONE H2B UBIQUITINATION.
PubMed=19575011; DOI=10.1038/embor.2009.108;
Pirngruber J., Shchebet A., Schreiber L., Shema E., Minsky N.,
Chapman R.D., Eick D., Aylon Y., Oren M., Johnsen S.A.;
"CDK9 directs H2B monoubiquitination and controls replication-
dependent histone mRNA 3'-end processing.";
EMBO Rep. 10:894-900(2009).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347 AND THR-350,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 (ISOFORM 2), 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).
[42]
FUNCTION IN DNA REPAIR, AND INTERACTION WITH KU70/XRCC6.
PubMed=20493174; DOI=10.1016/j.bbrc.2010.05.092;
Liu H., Herrmann C.H., Chiang K., Sung T.L., Moon S.H.,
Donehower L.A., Rice A.P.;
"55K isoform of CDK9 associates with Ku70 and is involved in DNA
repair.";
Biochem. Biophys. Res. Commun. 397:245-250(2010).
[43]
FUNCTION IN CDK9/CYCLIN K COMPLEX DURING REPLICATION STRESS.
PubMed=20930849; DOI=10.1038/embor.2010.153;
Yu D.S., Zhao R., Hsu E.L., Cayer J., Ye F., Guo Y., Shyr Y.,
Cortez D.;
"Cyclin-dependent kinase 9-cyclin K functions in the replication
stress response.";
EMBO Rep. 11:876-882(2010).
[44]
FUNCTION IN CARDIAC HYPERTROPHY, AND IDENTIFICATION IN COMPLEX WITH
CCNT1/CYCLIN-T1; EP300 AND GATA4.
PubMed=20081228; DOI=10.1074/jbc.M109.070458;
Sunagawa Y., Morimoto T., Takaya T., Kaichi S., Wada H., Kawamura T.,
Fujita M., Shimatsu A., Kita T., Hasegawa K.;
"Cyclin-dependent kinase-9 is a component of the p300/GATA4 complex
required for phenylephrine-induced hypertrophy in cardiomyocytes.";
J. Biol. Chem. 285:9556-9568(2010).
[45]
IDENTIFICATION IN THE SEC COMPLEX.
PubMed=20471948; DOI=10.1016/j.molcel.2010.04.013;
He N., Liu M., Hsu J., Xue Y., Chou S., Burlingame A., Krogan N.J.,
Alber T., Zhou Q.;
"HIV-1 Tat and host AFF4 recruit two transcription elongation factors
into a bifunctional complex for coordinated activation of HIV-1
transcription.";
Mol. Cell 38:428-438(2010).
[46]
IDENTIFICATION IN THE SEC COMPLEX.
PubMed=20159561; DOI=10.1016/j.molcel.2010.01.026;
Lin C., Smith E.R., Takahashi H., Lai K.C., Martin-Brown S.,
Florens L., Washburn M.P., Conaway J.W., Conaway R.C., Shilatifard A.;
"AFF4, a component of the ELL/P-TEFb elongation complex and a shared
subunit of MLL chimeras, can link transcription elongation to
leukemia.";
Mol. Cell 37:429-437(2010).
[47]
FUNCTION IN AR KINASE, AND INTERACTION WITH AR.
PubMed=20980437; DOI=10.1210/me.2010-0238;
Gordon V., Bhadel S., Wunderlich W., Zhang J., Ficarro S.B.,
Mollah S.A., Shabanowitz J., Hunt D.F., Xenarios I., Hahn W.C.,
Conaway M., Carey M.F., Gioeli D.;
"CDK9 regulates AR promoter selectivity and cell growth through serine
81 phosphorylation.";
Mol. Endocrinol. 24:2267-2280(2010).
[48]
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).
[49]
IDENTIFICATION IN THE SEC COMPLEX.
PubMed=22195968; DOI=10.1016/j.molcel.2011.12.008;
Smith E.R., Lin C., Garrett A.S., Thornton J., Mohaghegh N., Hu D.,
Jackson J., Saraf A., Swanson S.K., Seidel C., Florens L.,
Washburn M.P., Eissenberg J.C., Shilatifard A.;
"The little elongation complex regulates small nuclear RNA
transcription.";
Mol. Cell 44:954-965(2011).
[50]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-186, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[51]
ENZYME REGULATION BY CDKI-71.
PubMed=21484792; DOI=10.1002/ijc.26127;
Liu X., Shi S., Lam F., Pepper C., Fischer P.M., Wang S.;
"CDKI-71, a novel CDK9 inhibitor, is preferentially cytotoxic to
cancer cells compared to flavopiridol.";
Int. J. Cancer 130:1216-1226(2012).
[52]
FUNCTION AS RPB1/POLR2A CTD KINASE, POLYUBIQUITINATION BY UBR5, AND
INTERACTION WITH UBR5 AND TFIIS/TCEA1.
PubMed=21127351; DOI=10.1074/jbc.M110.176628;
Cojocaru M., Bouchard A., Cloutier P., Cooper J.J., Varzavand K.,
Price D.H., Coulombe B.;
"Transcription factor IIS cooperates with the E3 ligase UBR5 to
ubiquitinate the CDK9 subunit of the positive transcription elongation
factor B.";
J. Biol. Chem. 286:5012-5022(2011).
[53]
PHOSPHORYLATION AT THR-186, ENZYME REGULATION, DEGRADATION BY THE
PROTEASOME, AND MUTAGENESIS OF THR-186.
PubMed=21448926; DOI=10.1002/jcp.22760;
Ramakrishnan R., Rice A.P.;
"Cdk9 T-loop phosphorylation is regulated by the calcium signaling
pathway.";
J. Cell. Physiol. 227:609-617(2012).
[54]
PHOSPHORYLATION AT SER-175, DEPHOSPHORYLATION AT SER-175 BY PP1, AND
MUTAGENESIS OF SER-175.
PubMed=21533037; DOI=10.1371/journal.pone.0018985;
Ammosova T., Obukhov Y., Kotelkin A., Breuer D., Beullens M.,
Gordeuk V.R., Bollen M., Nekhai S.;
"Protein phosphatase-1 activates CDK9 by dephosphorylating Ser175.";
PLoS ONE 6:E18985-E18985(2011).
[55]
REVIEW ON NELF AND DSIF KINASE ACTIVITY.
PubMed=16885020; DOI=10.1016/j.molcel.2006.06.014;
Peterlin B.M., Price D.H.;
"Controlling the elongation phase of transcription with P-TEFb.";
Mol. Cell 23:297-305(2006).
[56]
REVIEW ON CYTOKINE SIGNALING.
PubMed=18728388; DOI=10.4161/cc.7.17.6594;
Brasier A.R.;
"Expanding role of cyclin dependent kinases in cytokine inducible gene
expression.";
Cell Cycle 7:2661-2666(2008).
[57]
REVIEW ON TRANSCRIPTION REGULATION, AND INHIBITORS.
PubMed=19029809; DOI=10.4161/cc.7.23.7122;
Romano G., Giordano A.;
"Role of the cyclin-dependent kinase 9-related pathway in mammalian
gene expression and human diseases.";
Cell Cycle 7:3664-3668(2008).
[58]
REVIEW ON TRANSCRIPTION REGULATION, AND INHIBITORS.
PubMed=18423896; DOI=10.1016/j.tips.2008.03.003;
Wang S., Fischer P.M.;
"Cyclin-dependent kinase 9: a key transcriptional regulator and
potential drug target in oncology, virology and cardiology.";
Trends Pharmacol. Sci. 29:302-313(2008).
[59]
ENZYME REGULATION, 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).
[60]
REVIEW ON CARDIAC HYPERTROPHY, AND INHIBITORS.
PubMed=19757441; DOI=10.1002/med.20172;
Krystof V., Chamrad I., Jorda R., Kohoutek J.;
"Pharmacological targeting of CDK9 in cardiac hypertrophy.";
Med. Res. Rev. 30:646-666(2010).
[61]
REVIEW ON GENOME INTEGRITY MAINTENANCE.
PubMed=21200140; DOI=10.4161/cc.10.1.14364;
Yu D.S., Cortez D.;
"A role for cdk9-cyclin k in maintaining genome integrity.";
Cell Cycle 10:28-32(2011).
[62]
INTERACTION WITH HERPES SIMPLEX VIRUS 1 PROTEIN ICP22.
PubMed=23029222; DOI=10.1371/journal.pone.0045749;
Guo L., Wu W.J., Liu L.D., Wang L.C., Zhang Y., Wu L.Q., Guan Y.,
Li Q.H.;
"Herpes simplex virus 1 ICP22 inhibits the transcription of viral gene
promoters by binding to and blocking the recruitment of P-TEFb.";
PLoS ONE 7:E45749-E45749(2012).
[63]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT THR-54 (ISOFORM 2), AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[64]
INTERACTION WITH HSF1.
PubMed=27189267; DOI=10.1038/srep26294;
Pan X.Y., Zhao W., Zeng X.Y., Lin J., Li M.M., Shen X.T., Liu S.W.;
"Heat shock factor 1 mediates latent HIV reactivation.";
Sci. Rep. 6:26294-26294(2016).
[65]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-345 IN COMPLEX WITH HIV-1
TAT AND CCNT1, AND PHOSPHORYLATION AT THR-186.
PubMed=20535204; DOI=10.1038/nature09131;
Tahirov T.H., Babayeva N.D., Varzavand K., Cooper J.J., Sedore S.C.,
Price D.H.;
"Crystal structure of HIV-1 Tat complexed with human P-TEFb.";
Nature 465:747-751(2010).
[66]
X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 2-330 IN COMPLEX WITH
INHIBITOR FLAVOPIRIDOL; ATP AND CCNT1, PHOSPHORYLATION AT THR-186
SER-347; THR-362 AND THR-363, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF
THR-186.
PubMed=18566585; DOI=10.1038/emboj.2008.121;
Baumli S., Lolli G., Lowe E.D., Troiani S., Rusconi L., Bullock A.N.,
Debreczeni J.E., Knapp S., Johnson L.N.;
"The structure of P-TEFb (CDK9/cyclin T1), its complex with
flavopiridol and regulation by phosphorylation.";
EMBO J. 27:1907-1918(2008).
[67]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-330 IN COMPLEX WITH
INHIBITOR DRB, AND PHOSPHORYLATION AT THR-186.
PubMed=20851342; DOI=10.1016/j.chembiol.2010.07.012;
Baumli S., Endicott J.A., Johnson L.N.;
"Halogen bonds form the basis for selective P-TEFb inhibition by
DRB.";
Chem. Biol. 17:931-936(2010).
[68]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-330 IN COMPLEX WITH CCNT1;
INHIBITORS ROSCOVITINE AND CR8, PHOSPHORYLATION AT THR-186, AND ENZYME
REGULATION.
PubMed=21779453; DOI=10.1177/1947601910369817;
Bettayeb K., Baunbaek D., Delehouze C., Loaec N., Hole A.J.,
Baumli S., Endicott J.A., Douc-Rasy S., Benard J., Oumata N.,
Galons H., Meijer L.;
"CDK inhibitors roscovitine and CR8 trigger Mcl-1 down-regulation and
apoptotic cell death in neuroblastoma cells.";
Genes Cancer 1:369-380(2010).
[69]
VARIANT [LARGE SCALE ANALYSIS] LEU-59.
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: Protein kinase involved in the regulation of
transcription. Member of the cyclin-dependent kinase pair
(CDK9/cyclin-T) complex, also called positive transcription
elongation factor b (P-TEFb), which facilitates the transition
from abortive to productive elongation by phosphorylating the CTD
(C-terminal domain) of the large subunit of RNA polymerase II
(RNAP II) POLR2A, SUPT5H and RDBP. This complex is inactive when
in the 7SK snRNP complex form. Phosphorylates EP300, MYOD1,
RPB1/POLR2A and AR, and the negative elongation factors DSIF and
NELF. Regulates cytokine inducible transcription networks by
facilitating promoter recognition of target transcription factors
(e.g. TNF-inducible RELA/p65 activation and IL-6-inducible STAT3
signaling). Promotes RNA synthesis in genetic programs for cell
growth, differentiation and viral pathogenesis. P-TEFb is also
involved in cotranscriptional histone modification, mRNA
processing and mRNA export. Modulates a complex network of
chromatin modifications including histone H2B monoubiquitination
(H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3;
integrates phosphorylation during transcription with chromatin
modifications to control co-transcriptional histone mRNA
processing. The CDK9/cyclin-K complex has also a kinase activity
towards CTD of RNAP II and can substitute for CDK9/cyclin-T P-TEFb
in vitro. Replication stress response protein; the CDK9/cyclin-K
complex is required for genome integrity maintenance, by promoting
cell cycle recovery from replication arrest and limiting single-
stranded DNA amount in response to replication stress, thus
reducing the breakdown of stalled replication forks and avoiding
DNA damage. In addition, probable function in DNA repair of
isoform 2 via interaction with KU70/XRCC6. Promotes cardiac
myocyte enlargement. RPB1/POLR2A phosphorylation on 'Ser-2' in CTD
activates transcription. AR phosphorylation modulates AR
transcription factor promoter selectivity and cell growth. DSIF
and NELF phosphorylation promotes transcription by inhibiting
their negative effect. The phosphorylation of MYOD1 enhances its
transcriptional activity and thus promotes muscle differentiation.
{ECO:0000269|PubMed:10393184, ECO:0000269|PubMed:10574912,
ECO:0000269|PubMed:10757782, ECO:0000269|PubMed:10912001,
ECO:0000269|PubMed:11112772, ECO:0000269|PubMed:11145967,
ECO:0000269|PubMed:11575923, ECO:0000269|PubMed:11809800,
ECO:0000269|PubMed:11884399, ECO:0000269|PubMed:12037670,
ECO:0000269|PubMed:14701750, ECO:0000269|PubMed:15564463,
ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:16109377,
ECO:0000269|PubMed:17956865, ECO:0000269|PubMed:18362169,
ECO:0000269|PubMed:19575011, ECO:0000269|PubMed:19844166,
ECO:0000269|PubMed:20081228, ECO:0000269|PubMed:20493174,
ECO:0000269|PubMed:20930849, ECO:0000269|PubMed:20980437,
ECO:0000269|PubMed:21127351, ECO:0000269|PubMed:9857195}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP +
[DNA-directed RNA polymerase] phosphate.
-!- ENZYME REGULATION: Inhibited by CDKI-71, CR8, GPC-286199, AG-
024322, flavopiridol (alvocidib), RBG-286147, anilinopyrimidine
32, arylazopyrazole 31b, indirubin 3'-monoxime, meriolin 3,P276-
00, olomoucine II, pyrazolotriazine, meriolin, variolin,
thiazolyl-pyrimidine, thiazolyl-pyrimidine, indirubin-30-monoxime,
ZK 304709, AG-012986, AT7519, R547, RGB-286638, imidazole
pyrimidine, EXEL-3700, EXEL-8647, 5,6-dichloro-1-b-ribofur-anosyl-
benzimidazole (DRB), P276-00, roscovitine (seliciclib, CYC202) and
SNS-032 (BMS-387032). Activation by Thr-186 phosphorylation is
calcium Ca(2+) signaling pathway-dependent; actively inactivated
by dephosphorylation mediated by PPP1CA, PPM1A and PPM1B.
Reversibly repressed by acetylation at Lys-44 and Lys-48.
{ECO:0000269|PubMed:18250157, ECO:0000269|PubMed:18483222,
ECO:0000269|PubMed:19238148, ECO:0000269|PubMed:21448926,
ECO:0000269|PubMed:21484792, ECO:0000269|PubMed:21779453}.
-!- SUBUNIT: Component of the super elongation complex (SEC), at least
composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the
P-TEFb complex and ELL (ELL, ELL2 or ELL3). Associates with
CCNT1/cyclin-T1, CCNT2/cyclin-T2 (isoform A and isoform B) or
CCNK/cyclin-K to form active P-TEFb. P-TEFb forms a complex with
AFF4/AF5Q31 and is part of the super elongation complex (SEC).
Component of a complex which is composed of at least 5 members:
HTATSF1/Tat-SF1, P-TEFb complex, RNA pol II, SUPT5H, and
NCL/nucleolin. Associates with UBR5 and forms a transcription
regulatory complex composed of CDK9, RNAP II, UBR5 and TFIIS/TCEA1
that can stimulate target gene transcription (e.g. gamma
fibrinogen/FGG) by recruiting their promoters. Component of the
7SK snRNP inactive complex which is composed of at least 8
members: P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1,
HEXIM2, LARP7, BCDIN3, SART3 proteins and 7SK and U6 snRNAs. This
inactive 7SK snRNP complex can also interact with NCOR1 and HDAC3,
probably to regulate CDK9 acetylation. Release of P-TEFb from P-
TEFb/7SK snRNP complex requires both PP2B to transduce calcium
Ca(2+) signaling in response to stimuli (e.g. UV or hexamethylene
bisacetamide (HMBA)), and PPP1CA to dephosphorylate Thr-186. This
released P-TEFb remains inactive in the pre-initiation complex
with BRD4 until new Thr-186 phosphorylation occurs after the
synthesis of a short RNA. Interacts with BRD4, probably to target
chromatin binding. Interacts with the acidic/proline-rich region
of HIV-1 and HIV-2 Tat via T-loop region, and is thus required for
HIV to hijack host transcription machinery during its replication
through cooperative binding to viral TAR RNA. Interacts with
activated nuclear STAT3 and RELA/p65. Binds to AR and MYOD1. Forms
a complex composed of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that
stimulates hypertrophy in cardiomyocytes. The large PER complex
involved in the repression of transcriptional termination is
composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A.
Isoform 3 binds to KU70/XRCC6. Interacts with herpes simplex virus
1 protein ICP22; this interaction inhibits the positive
transcription elongation factor b (P-TEFb). Interacts with HSF1
(PubMed:27189267). Interacts with TBX21 (By similarity).
{ECO:0000250|UniProtKB:Q99J95, ECO:0000269|PubMed:10393184,
ECO:0000269|PubMed:10574912, ECO:0000269|PubMed:10958691,
ECO:0000269|PubMed:11884399, ECO:0000269|PubMed:12037670,
ECO:0000269|PubMed:12065898, ECO:0000269|PubMed:12718890,
ECO:0000269|PubMed:15965233, ECO:0000269|PubMed:16109376,
ECO:0000269|PubMed:16109377, ECO:0000269|PubMed:17452463,
ECO:0000269|PubMed:17643375, ECO:0000269|PubMed:17956865,
ECO:0000269|PubMed:18249148, ECO:0000269|PubMed:18362169,
ECO:0000269|PubMed:18483222, ECO:0000269|PubMed:18566585,
ECO:0000269|PubMed:20081228, ECO:0000269|PubMed:20159561,
ECO:0000269|PubMed:20471948, ECO:0000269|PubMed:20493174,
ECO:0000269|PubMed:20535204, ECO:0000269|PubMed:20851342,
ECO:0000269|PubMed:20980437, ECO:0000269|PubMed:21127351,
ECO:0000269|PubMed:21779453, ECO:0000269|PubMed:22195968,
ECO:0000269|PubMed:23029222, ECO:0000269|PubMed:27189267,
ECO:0000269|PubMed:9491887, ECO:0000269|PubMed:9499409}.
-!- INTERACTION:
Q13535:ATR; NbExp=3; IntAct=EBI-1383449, EBI-968983;
Q8WXE1:ATRIP; NbExp=3; IntAct=EBI-1383449, EBI-747353;
O60885-1:BRD4; NbExp=9; IntAct=EBI-1383449, EBI-9345088;
O60563:CCNT1; NbExp=20; IntAct=EBI-1383449, EBI-2479671;
Q16543:CDC37; NbExp=3; IntAct=EBI-1383449, EBI-295634;
Q9HAW4:CLSPN; NbExp=3; IntAct=EBI-1383449, EBI-1369377;
Q7L2E3:DHX30; NbExp=5; IntAct=EBI-1383449, EBI-1211456;
Q13451:FKBP5; NbExp=4; IntAct=EBI-1383449, EBI-306914;
O94992:HEXIM1; NbExp=9; IntAct=EBI-1383449, EBI-2832510;
P07900:HSP90AA1; NbExp=2; IntAct=EBI-1383449, EBI-296047;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-1383449, EBI-352572;
Q6NYC1:JMJD6; NbExp=5; IntAct=EBI-1383449, EBI-8464037;
Q4G0J3:LARP7; NbExp=9; IntAct=EBI-1383449, EBI-2371923;
Q6XYB7-2:LBX2; NbExp=4; IntAct=EBI-12029902, EBI-12029900;
Q9Y5X4:NR2E3; NbExp=4; IntAct=EBI-1383449, EBI-7216962;
P53041:PPP5C; NbExp=3; IntAct=EBI-1383449, EBI-716663;
P04608:tat (xeno); NbExp=8; IntAct=EBI-1383449, EBI-6164389;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Nucleus, PML body.
Note=Accumulates on chromatin in response to replication stress.
Complexed with CCNT1 in nuclear speckles, but uncomplexed form in
the cytoplasm. The translocation from nucleus to cytoplasm is
XPO1/CRM1-dependent. Associates with PML body when acetylated.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P50750-1; Sequence=Displayed;
Name=2;
IsoId=P50750-2; Sequence=VSP_016288;
Note=Contains a phosphoserine at position 35. Contains a
phosphothreonine at position 54. {ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195, ECO:0000244|PubMed:24275569};
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- INDUCTION: By replication stress, in chromatin. Probably degraded
by the proteasome upon Thr-186 dephosphorylation.
-!- PTM: Autophosphorylation at Thr-186, Ser-347, Thr-350, Ser-353,
Thr-354 and Ser-357 triggers kinase activity by promoting cyclin
and substrate binding (e.g. HIV TAT) upon conformational changes.
Thr-186 phosphorylation requires the calcium Ca(2+) signaling
pathway, including CaMK1D and calmodulin. This inhibition is
relieved by Thr-29 dephosphorylation. However, phosphorylation at
Thr-29 is inhibitory within the HIV transcription initiation
complex. Phosphorylation at Ser-175 inhibits kinase activity. Can
be phosphorylated on either Thr-362 or Thr-363 but not on both
simultaneously (PubMed:18566585). {ECO:0000269|PubMed:10958691,
ECO:0000269|PubMed:15965233, ECO:0000269|PubMed:18483222,
ECO:0000269|PubMed:18566585, ECO:0000269|PubMed:18829461,
ECO:0000269|PubMed:20535204, ECO:0000269|PubMed:20851342,
ECO:0000269|PubMed:21448926, ECO:0000269|PubMed:21533037,
ECO:0000269|PubMed:21779453}.
-!- PTM: Dephosphorylation of Thr-186 by PPM1A and PPM1B blocks CDK9
activity and may lead to CDK9 proteasomal degradation. However,
PPP1CA-mediated Thr-186 dephosphorylation is required to release
P-TEFb from its inactive P-TEFb/7SK snRNP complex.
Dephosphorylation of C-terminus Thr and Ser residues by protein
phosphatase-1 (PP1) triggers CDK9 activity, contributing to the
activation of HIV-1 transcription.
-!- PTM: N6-acetylation of Lys-44 by CBP/p300 promotes kinase
activity, whereas acetylation of both Lys-44 and Lys-48 mediated
by PCAF/KAT2B and GCN5/KAT2A reduces kinase activity. The
acetylated form associates with PML bodies in the nuclear matrix
and with the transcriptionally silent HIV-1 genome; deacetylated
upon transcription stimulation. {ECO:0000269|PubMed:17452463,
ECO:0000269|PubMed:18250157}.
-!- PTM: Polyubiquitinated and thus activated by UBR5. This
ubiquitination is promoted by TFIIS/TCEA1 and favors 'Ser-2'
phosphorylation of RPB1/POLR2A CTD. {ECO:0000269|PubMed:21127351}.
-!- DISEASE: Note=Chronic activation of CDK9 causes cardiac myocyte
enlargement leading to cardiac hypertrophy, and confers
predisposition to heart failure.
-!- MISCELLANEOUS: CDK9 inhibition contributes to the anticancer
activity of most CDK inhibitors under clinical investigation
(PubMed:18423896 and PubMed:21779453). As a retroviruses target
during the hijack of host transcription (e.g. HIV), CDK9
inhibitors might become specific antiretroviral agents
(PubMed:18423896). May be a target for cardiac hypertrophy future
treatments (PubMed:19757441 and PubMed:18423896). May also be a
target in anti-inflammatory therapy in innate immunity and
systemic inflammation (PubMed:18728388).
{ECO:0000305|PubMed:18423896, ECO:0000305|PubMed:18728388}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAI39767.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdk9/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L25676; AAA35668.1; -; mRNA.
EMBL; X80230; CAA56516.1; -; mRNA.
EMBL; AF255306; AAF72183.1; -; Genomic_DNA.
EMBL; BT019903; AAV38706.1; -; mRNA.
EMBL; AF517840; AAM54039.1; -; Genomic_DNA.
EMBL; AL162586; CAI39767.1; ALT_SEQ; Genomic_DNA.
EMBL; AL162586; CAI39768.1; -; Genomic_DNA.
EMBL; BC001968; AAH01968.1; -; mRNA.
CCDS; CCDS6879.1; -. [P50750-1]
PIR; A55262; A55262.
RefSeq; NP_001252.1; NM_001261.3. [P50750-1]
UniGene; Hs.150423; -.
UniGene; Hs.706809; -.
PDB; 1PF6; Model; -; A=1-372.
PDB; 3BLH; X-ray; 2.48 A; A=2-330.
PDB; 3BLQ; X-ray; 2.90 A; A=2-330.
PDB; 3BLR; X-ray; 2.80 A; A=2-330.
PDB; 3LQ5; X-ray; 3.00 A; A=2-330.
PDB; 3MI9; X-ray; 2.10 A; A=1-345.
PDB; 3MIA; X-ray; 3.00 A; A=1-345.
PDB; 3MY1; X-ray; 2.80 A; A=2-330.
PDB; 3TN8; X-ray; 2.95 A; A=2-330.
PDB; 3TNH; X-ray; 3.20 A; A=2-330.
PDB; 3TNI; X-ray; 3.23 A; A=2-330.
PDB; 4BCF; X-ray; 3.01 A; A=2-330.
PDB; 4BCG; X-ray; 3.08 A; A=2-330.
PDB; 4BCH; X-ray; 2.96 A; A=2-330.
PDB; 4BCI; X-ray; 3.10 A; A=2-330.
PDB; 4BCJ; X-ray; 3.16 A; A=2-330.
PDB; 4EC8; X-ray; 3.60 A; A=2-372.
PDB; 4EC9; X-ray; 3.21 A; A=2-372.
PDB; 4IMY; X-ray; 2.94 A; A/C/E=1-330.
PDB; 4OGR; X-ray; 3.00 A; A/E/I=1-330.
PDB; 4OR5; X-ray; 2.90 A; A/F=7-332.
PDB; 5L1Z; X-ray; 5.90 A; A=1-330.
PDBsum; 1PF6; -.
PDBsum; 3BLH; -.
PDBsum; 3BLQ; -.
PDBsum; 3BLR; -.
PDBsum; 3LQ5; -.
PDBsum; 3MI9; -.
PDBsum; 3MIA; -.
PDBsum; 3MY1; -.
PDBsum; 3TN8; -.
PDBsum; 3TNH; -.
PDBsum; 3TNI; -.
PDBsum; 4BCF; -.
PDBsum; 4BCG; -.
PDBsum; 4BCH; -.
PDBsum; 4BCI; -.
PDBsum; 4BCJ; -.
PDBsum; 4EC8; -.
PDBsum; 4EC9; -.
PDBsum; 4IMY; -.
PDBsum; 4OGR; -.
PDBsum; 4OR5; -.
PDBsum; 5L1Z; -.
ProteinModelPortal; P50750; -.
SMR; P50750; -.
BioGrid; 107459; 203.
CORUM; P50750; -.
DIP; DIP-29016N; -.
ELM; P50750; -.
IntAct; P50750; 77.
MINT; MINT-1532814; -.
STRING; 9606.ENSP00000362361; -.
BindingDB; P50750; -.
ChEMBL; CHEMBL3116; -.
DrugBank; DB03496; Flavopiridol.
GuidetoPHARMACOLOGY; 1981; -.
iPTMnet; P50750; -.
PhosphoSitePlus; P50750; -.
BioMuta; CDK9; -.
DMDM; 68067660; -.
EPD; P50750; -.
MaxQB; P50750; -.
PaxDb; P50750; -.
PeptideAtlas; P50750; -.
PRIDE; P50750; -.
DNASU; 1025; -.
Ensembl; ENST00000373264; ENSP00000362361; ENSG00000136807. [P50750-1]
GeneID; 1025; -.
KEGG; hsa:1025; -.
UCSC; uc004bse.3; human. [P50750-1]
CTD; 1025; -.
DisGeNET; 1025; -.
EuPathDB; HostDB:ENSG00000136807.11; -.
GeneCards; CDK9; -.
HGNC; HGNC:1780; CDK9.
HPA; CAB004216; -.
HPA; HPA006738; -.
MIM; 603251; gene.
neXtProt; NX_P50750; -.
OpenTargets; ENSG00000136807; -.
PharmGKB; PA26316; -.
eggNOG; KOG0600; Eukaryota.
eggNOG; ENOG410XPIR; LUCA.
GeneTree; ENSGT00890000139396; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P50750; -.
KO; K02211; -.
OMA; KDPTGCD; -.
OrthoDB; EOG091G08Z8; -.
PhylomeDB; P50750; -.
TreeFam; TF101039; -.
BRENDA; 2.7.11.22; 2681.
BRENDA; 2.7.11.23; 2681.
Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
Reactome; R-HSA-167287; HIV elongation arrest and recovery.
Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
Reactome; R-HSA-176034; Interactions of Tat with host cellular proteins.
Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
SignaLink; P50750; -.
SIGNOR; P50750; -.
ChiTaRS; CDK9; human.
EvolutionaryTrace; P50750; -.
GeneWiki; CDK9; -.
GeneWiki; Cyclin-dependent_kinase_9; -.
GenomeRNAi; 1025; -.
PRO; PR:P50750; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000136807; -.
CleanEx; HS_CDK9; -.
ExpressionAtlas; P50750; baseline and differential.
Genevisible; P50750; HS.
GO; GO:0005694; C:chromosome; IBA:GO_Central.
GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IDA:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0016605; C:PML body; IDA:UniProtKB.
GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
GO; GO:0097322; F:7SK snRNA binding; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0016301; F:kinase activity; TAS:Reactome.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0008353; F:RNA polymerase II carboxy-terminal domain kinase activity; IDA:UniProtKB.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0071157; P:negative regulation of cell cycle arrest; IDA:UniProtKB.
GO; GO:1900364; P:negative regulation of mRNA polyadenylation; IMP:UniProtKB.
GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IEA:Ensembl.
GO; GO:2001168; P:positive regulation of histone H2B ubiquitination; IMP:UniProtKB.
GO; GO:0033129; P:positive regulation of histone phosphorylation; IMP:UniProtKB.
GO; GO:1903839; P:positive regulation of mRNA 3'-UTR binding; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0006282; P:regulation of DNA repair; IDA:UniProtKB.
GO; GO:0031056; P:regulation of histone modification; IDA:UniProtKB.
GO; GO:0051147; P:regulation of muscle cell differentiation; IMP:UniProtKB.
GO; GO:0031297; P:replication fork processing; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0042795; P:snRNA transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:ProtInc.
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;
Complete proteome; Cytoplasm; DNA damage; DNA repair; Kinase;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transcription;
Transcription regulation; Transferase; Ubl conjugation.
CHAIN 1 372 Cyclin-dependent kinase 9.
/FTId=PRO_0000085800.
DOMAIN 19 315 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 25 33 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 104 106 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:18566585}.
REGION 166 191 T-loop.
ACT_SITE 149 149 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 48 48 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:18566585}.
BINDING 167 167 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:18566585}.
MOD_RES 29 29 Phosphothreonine.
{ECO:0000269|PubMed:10958691}.
MOD_RES 44 44 N6-acetyllysine; by P300/CBP, PCAF/KAT2B
and GCN5/KAT2A.
{ECO:0000269|PubMed:17452463,
ECO:0000269|PubMed:18250157}.
MOD_RES 48 48 N6-acetyllysine; by PCAF/KAT2B and
GCN5/KAT2A.
{ECO:0000269|PubMed:18250157}.
MOD_RES 175 175 Phosphoserine.
{ECO:0000269|PubMed:21533037}.
MOD_RES 186 186 Phosphothreonine; by CaMK1D.
{ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:15965233,
ECO:0000269|PubMed:18483222,
ECO:0000269|PubMed:18566585,
ECO:0000269|PubMed:18829461,
ECO:0000269|PubMed:20535204,
ECO:0000269|PubMed:20851342,
ECO:0000269|PubMed:21448926,
ECO:0000269|PubMed:21779453}.
MOD_RES 347 347 Phosphoserine; by CDK9 and PKA.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:10958691,
ECO:0000269|PubMed:18566585}.
MOD_RES 350 350 Phosphothreonine; by CDK9.
{ECO:0000244|PubMed:19369195,
ECO:0000269|PubMed:10958691}.
MOD_RES 353 353 Phosphoserine; by CDK9.
{ECO:0000269|PubMed:10958691}.
MOD_RES 354 354 Phosphothreonine; by CDK9.
{ECO:0000269|PubMed:10958691}.
MOD_RES 357 357 Phosphoserine; by CDK9.
{ECO:0000269|PubMed:10958691}.
MOD_RES 362 362 Phosphothreonine; by CDK9.
{ECO:0000269|PubMed:18566585}.
MOD_RES 363 363 Phosphothreonine; by CDK9.
{ECO:0000269|PubMed:18566585}.
VAR_SEQ 1 1 M -> MQRDAPPRAPAPAPRLPAPPIGAAASSGGGGGGGSG
GGGGGASAAPAPPGLSGTTSPRGPGGGRRAEEAGSAPRGRK
WPWRRKWRGRGGAWSAAAAGPGAGAAAAATGGGGGALEAAM
(in isoform 2). {ECO:0000305}.
/FTId=VSP_016288.
VARIANT 59 59 F -> L (in dbSNP:rs55640715).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041982.
VARIANT 231 231 G -> A. {ECO:0000269|PubMed:10903437,
ECO:0000269|PubMed:7695608}.
/FTId=VAR_013456.
MUTAGEN 44 44 K->R: Impaired kinase and transcriptional
elongation activities, but normal cyclin
T1 and HEXIM1 binding.
{ECO:0000269|PubMed:17452463}.
MUTAGEN 167 167 D->N: Abrogates kinase activity.
{ECO:0000269|PubMed:10958691,
ECO:0000269|PubMed:11145967}.
MUTAGEN 175 175 S->A: Constitutive kinase activity.
{ECO:0000269|PubMed:21533037}.
MUTAGEN 175 175 S->D: Mimics phosphorylation,
constitutive loss of kinase activity.
{ECO:0000269|PubMed:21533037}.
MUTAGEN 186 186 T->A: Abrogates autophosphorylation; no
effect on kinase activity, but impaired
CTD phosphorylation.
{ECO:0000269|PubMed:11145967,
ECO:0000269|PubMed:18566585,
ECO:0000269|PubMed:21448926}.
MUTAGEN 186 186 T->D: Mimics autophosphorylation;
constitutive kinase activity,
independently of calcium signaling.
{ECO:0000269|PubMed:11145967,
ECO:0000269|PubMed:18566585,
ECO:0000269|PubMed:21448926}.
MUTAGEN 347 357 SQITQQSTNQS->AQIAQQAANQA: Loss of
autophosphorylation and impaired
interaction with HIV TAT.
{ECO:0000269|PubMed:10958691}.
MUTAGEN 347 357 SQITQQSTNQS->EQIEQQEENQE: Mimics
autophosphorylation and promotes
interaction with HIV TAT.
{ECO:0000269|PubMed:10958691}.
CONFLICT 163 163 L -> P (in Ref. 4; AAV38706).
{ECO:0000305}.
STRAND 13 15 {ECO:0000244|PDB:4EC9}.
HELIX 16 18 {ECO:0000244|PDB:3MI9}.
STRAND 19 24 {ECO:0000244|PDB:3MI9}.
STRAND 28 30 {ECO:0000244|PDB:3BLR}.
STRAND 32 38 {ECO:0000244|PDB:3MI9}.
TURN 39 41 {ECO:0000244|PDB:3MI9}.
STRAND 44 49 {ECO:0000244|PDB:3MI9}.
STRAND 56 59 {ECO:0000244|PDB:3MI9}.
HELIX 61 72 {ECO:0000244|PDB:3MI9}.
STRAND 81 87 {ECO:0000244|PDB:3MI9}.
STRAND 98 104 {ECO:0000244|PDB:3MI9}.
STRAND 107 109 {ECO:0000244|PDB:3MI9}.
HELIX 110 115 {ECO:0000244|PDB:3MI9}.
STRAND 116 118 {ECO:0000244|PDB:3LQ5}.
HELIX 123 142 {ECO:0000244|PDB:3MI9}.
HELIX 152 154 {ECO:0000244|PDB:3MI9}.
STRAND 155 157 {ECO:0000244|PDB:3MI9}.
STRAND 163 165 {ECO:0000244|PDB:3MI9}.
HELIX 168 170 {ECO:0000244|PDB:4OGR}.
STRAND 178 181 {ECO:0000244|PDB:3MI9}.
HELIX 192 194 {ECO:0000244|PDB:3MI9}.
HELIX 197 200 {ECO:0000244|PDB:3MI9}.
HELIX 209 224 {ECO:0000244|PDB:3MI9}.
HELIX 234 245 {ECO:0000244|PDB:3MI9}.
TURN 250 252 {ECO:0000244|PDB:3MI9}.
HELIX 256 258 {ECO:0000244|PDB:3MI9}.
HELIX 260 262 {ECO:0000244|PDB:3MI9}.
HELIX 263 265 {ECO:0000244|PDB:3MY1}.
HELIX 275 283 {ECO:0000244|PDB:3MI9}.
HELIX 286 295 {ECO:0000244|PDB:3MI9}.
HELIX 300 302 {ECO:0000244|PDB:3MI9}.
HELIX 306 310 {ECO:0000244|PDB:3MI9}.
HELIX 313 316 {ECO:0000244|PDB:3MI9}.
STRAND 317 319 {ECO:0000244|PDB:3MI9}.
HELIX 325 329 {ECO:0000244|PDB:3MI9}.
HELIX 335 339 {ECO:0000244|PDB:3MI9}.
SEQUENCE 372 AA; 42778 MW; 69E851CC6F7A0388 CRC64;
MAKQYDSVEC PFCDEVSKYE KLAKIGQGTF GEVFKARHRK TGQKVALKKV LMENEKEGFP
ITALREIKIL QLLKHENVVN LIEICRTKAS PYNRCKGSIY LVFDFCEHDL AGLLSNVLVK
FTLSEIKRVM QMLLNGLYYI HRNKILHRDM KAANVLITRD GVLKLADFGL ARAFSLAKNS
QPNRYTNRVV TLWYRPPELL LGERDYGPPI DLWGAGCIMA EMWTRSPIMQ GNTEQHQLAL
ISQLCGSITP EVWPNVDNYE LYEKLELVKG QKRKVKDRLK AYVRDPYALD LIDKLLVLDP
AQRIDSDDAL NHDFFWSDPM PSDLKGMLST HLTSMFEYLA PPRRKGSQIT QQSTNQSRNP
ATTNQTEFER VF


Related products :

Catalog number Product name Quantity
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
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
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
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
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,
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
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
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
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
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
E0739r ELISA kit Cdk5,Cdkn5,Cell division protein kinase 5,Cyclin-dependent kinase 5,Rat,Rattus norvegicus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit,TPKII catalytic sub 96T
E0739h ELISA kit CDK5,CDKN5,Cell division protein kinase 5,Cyclin-dependent kinase 5,Homo sapiens,Human,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit,TPKII catalytic subuni 96T
E0739h ELISA CDK5,CDKN5,Cell division protein kinase 5,Cyclin-dependent kinase 5,Homo sapiens,Human,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit,TPKII catalytic subunit 96T
U0739h CLIA CDK5,CDKN5,Cell division protein kinase 5,Cyclin-dependent kinase 5,Homo sapiens,Human,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit,TPKII catalytic subunit 96T
E0739r ELISA Cdk5,Cdkn5,Cell division protein kinase 5,Cyclin-dependent kinase 5,Rat,Rattus norvegicus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit,TPKII catalytic subunit 96T
U0739r CLIA Cdk5,Cdkn5,Cell division protein kinase 5,Cyclin-dependent kinase 5,Rat,Rattus norvegicus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit,TPKII catalytic subunit 96T
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
U0739m CLIA Cdk5,Cdkn5,Cell division protein kinase 5,CR6 protein kinase,CRK6,Crk6,Cyclin-dependent kinase 5,Mouse,Mus musculus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit 96T
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
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
E0739m ELISA Cdk5,Cdkn5,Cell division protein kinase 5,CR6 protein kinase,CRK6,Crk6,Cyclin-dependent kinase 5,Mouse,Mus musculus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subuni 96T
E0739m ELISA kit Cdk5,Cdkn5,Cell division protein kinase 5,CR6 protein kinase,CRK6,Crk6,Cyclin-dependent kinase 5,Mouse,Mus musculus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic s 96T
18-272-195263 Cdk9 - Rabbit polyclonal to Cdk9; 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 0.05 ml
E0739b ELISA kit Bos taurus,Bovine,CDK5,CDKN5,Cell division protein kinase 5,Cyclin-dependent kinase 5,PDPK,Proline-directed protein kinase 33 kDa subunit,Serine_threonine-protein kinase PSSALRE,Tau protein 96T
E0739b ELISA Bos taurus,Bovine,CDK5,CDKN5,Cell division protein kinase 5,Cyclin-dependent kinase 5,PDPK,Proline-directed protein kinase 33 kDa subunit,Serine_threonine-protein kinase PSSALRE,Tau protein kina 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