P50750 (CDK9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclin-dependent kinase 9
EC=2.7.11.22
EC=2.7.11.23

Alternative name(s):
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

Gene names

Name:	CDK9
Synonyms:	CDC2L4, TAK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.22 Ref.23 Ref.25 Ref.26 Ref.28 Ref.36 Ref.37 Ref.38 Ref.40 Ref.41 Ref.42 Ref.45 Ref.49
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. 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 Ca2+ signaling pathway-dependent; actively inactivated by dephosphorylation mediated by PPP1CA, PPM1A and PPM1B. Reversibly repressed by acetylation at Lys-44 and Lys-48. Ref.31 Ref.35 Ref.48 Ref.50 Ref.56 Ref.62
Subunit structure	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 Ca2+ 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 preinitiation complex with BRD4 until new Thr-186 phosphorylation occurs after the synthesis of a short RNA. Binds to 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. Isoform 3 binds to KU70/XRCC6. Ref.8 Ref.10 Ref.11 Ref.12 Ref.15 Ref.19 Ref.20 Ref.23 Ref.24 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.33 Ref.36 Ref.40 Ref.42 Ref.43 Ref.44 Ref.45 Ref.49
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. Ref.21 Ref.35
Tissue specificity	Ubiquitous.
Induction	By replication stress, in chromatin. Probably degraded by the proteasome upon Thr-186 dephosphorylation. Ref.31 Ref.35 Ref.48 Ref.50 Ref.56 Ref.62
Post-translational modification	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 Ca2+ 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 (Ref.60). Ref.15 Ref.27 Ref.31 Ref.32 Ref.50 Ref.51 Ref.59 Ref.60 Ref.61 Ref.62 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. 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. Polyubiquitinated and thus activated by UBR5. This ubiquitination is promoted by TFIIS/TCEA1 and favors 'Ser-2' phosphorylation of RPB1/POLR2A CTD.
Involvement in disease	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 (Ref.55 and Ref.62). As a retroviruses target during the hijack of host transcription (e.g. HIV), CDK9 inhibitors might become specific antiretroviral agents (Ref.55). May be a target for cardiac hypertrophy future treatments (Ref.57 and Ref.55). May also be a target in anti-inflammatory therapy in innate immunity and systemic inflammation (Ref.53).
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence CAI39767.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	DNA damage DNA repair Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Traceable author statement Ref.1. Source: ProtInc cellular response to cytokine stimulus Inferred from direct assay Ref.28. Source: UniProtKB negative regulation of cell cycle arrest Inferred from direct assay Ref.41. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: Reactome positive regulation of viral transcription Traceable author statement. Source: Reactome regulation of DNA repair Inferred from direct assay Ref.40. Source: UniProtKB regulation of histone modification Inferred from direct assay Ref.37. Source: UniProtKB replication fork arrest Inferred from direct assay Ref.41. Source: UniProtKB transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome viral reproductive process Traceable author statement. Source: Reactome
Cellular_component	PML body Inferred from direct assay Ref.35. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell positive transcription elongation factor complex b Inferred from direct assay PubMed 15905409. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from direct assay PubMed 16109376. Source: MGI RNA polymerase II carboxy-terminal domain kinase activity Inferred from direct assay PubMed 12721286. Source: UniProtKB cyclin-dependent protein serine/threonine kinase activity Traceable author statement PubMed 10866664. Source: ProtInc snRNA binding Inferred from electronic annotation. Source: Compara transcription regulatory region DNA binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSP90AB1	P08238	2	EBI-1383449,EBI-352572
tat	P04608	5	EBI-1383449,EBI-6164389	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P50750-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P50750-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MQRDAPPRAP...GGGGALEAAM

Note: Phosphorylated on Ser-27, Ser-35, Ser-52, Thr-54, Thr55 and Ser-56. Contains a phosphoserine at position 35.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 372

372

Cyclin-dependent kinase 9

PRO_0000085800

Regions

Domain

19 – 315

297

Protein kinase

Nucleotide binding

25 – 33

9

ATP By similarity

Nucleotide binding

104 – 106

3

ATP

Region

166 – 191

26

T-loop

Sites

Active site

149

1

Proton acceptor By similarity

Binding site

48

1

ATP

Binding site

167

1

ATP

Amino acid modifications

Modified residue

29

1

Phosphothreonine

Modified residue

44

1

N6-acetyllysine; by P300/CBP, PCAF/KAT2B and GCN5/KAT2A Ref.30 Ref.35

Modified residue

48

1

N6-acetyllysine; by PCAF/KAT2B and GCN5/KAT2A Ref.35

Modified residue

175

1

Phosphoserine Ref.51

Modified residue

186

1

Phosphothreonine; by CaMK1D Ref.27 Ref.31 Ref.32 Ref.47 Ref.50 Ref.59 Ref.60 Ref.61 Ref.62

Modified residue

347

1

Phosphoserine; by CDK9 and PKA Ref.15 Ref.34 Ref.39

Modified residue

350

1

Phosphothreonine; by CDK9 Ref.15 Ref.39

Modified residue

353

1

Phosphoserine; by CDK9 Ref.15

Modified residue

354

1

Phosphothreonine; by CDK9 Ref.15

Modified residue

357

1

Phosphoserine; by CDK9 Ref.15

Modified residue

362

1

Phosphothreonine; by CDK9

Modified residue

363

1

Phosphothreonine; by CDK9

Natural variations

Alternative sequence

1

1

M → MQRDAPPRAPAPAPRLPAPP IGAAASSGGGGGGGSGGGGG GASAAPAPPGLSGTTSPRGP GGGRRAEEAGSAPRGRKWPW RRKWRGRGGAWSAAAAGPGA GAAAAATGGGGGALEAAM in isoform 2.

VSP_016288

Natural variant

59

1

F → L. Ref.63
Corresponds to variant rs55640715 [ dbSNP | Ensembl ].

VAR_041982

Natural variant

231

1

G → A. Ref.2 Ref.3

VAR_013456

Experimental info

Mutagenesis

44

1

K → R: Impaired kinase and transcriptional elongation activities, but normal cyclin T1 and HEXIM1 binding. Ref.30

Mutagenesis

167

1

D → N: Abrogates kinase activity. Ref.15 Ref.16

Mutagenesis

175

1

S → A: Constitutive kinase activity. Ref.51

Mutagenesis

175

1

S → D: Mimics phosphorylation, constitutive loss of kinase activity. Ref.51

Mutagenesis

186

1

T → A: Abrogates autophosphorylation; no effect on kinase activity, but impaired CTD phosphorylation. Ref.16 Ref.50 Ref.60

Mutagenesis

186

1

T → D: Mimics autophosphorylation; constitutive kinase activity, independently of calcium signaling. Ref.16 Ref.50 Ref.60

Mutagenesis

347 – 357

11

SQITQQSTNQS → AQIAQQAANQA: Loss of autophosphorylation and impaired interaction with HIV TAT. Ref.15

Mutagenesis

347 – 357

11

SQITQQSTNQS → EQIEQQEENQE: Mimics autophosphorylation and promotes interaction with HIV TAT. Ref.15

Sequence conflict

163

1

L → P in AAV38706. Ref.4

Secondary structure

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372

Helix Strand Turn

Details...

Beta strand

13 – 15

3

Helix

16 – 18

3

Beta strand

19 – 24

6

Beta strand

28 – 30

3

Beta strand

32 – 38

7

Turn

39 – 41

3

Beta strand

44 – 49

6

Beta strand

56 – 59

4

Helix

61 – 72

12

Beta strand

81 – 87

7

Beta strand

98 – 104

7

Beta strand

107 – 109

3

Helix

110 – 115

6

Beta strand

116 – 118

3

Helix

123 – 142

20

Helix

152 – 154

3

Beta strand

155 – 157

3

Beta strand

163 – 165

3

Beta strand

178 – 181

4

Helix

192 – 194

3

Helix

197 – 200

4

Helix

209 – 224

16

Helix

234 – 245

12

Turn

250 – 252

3

Helix

256 – 258

3

Helix

260 – 262

3

Helix

263 – 265

3

Helix

275 – 283

9

Helix

286 – 295

10

Helix

300 – 302

3

Helix

306 – 310

5

Helix

313 – 316

4

Beta strand

317 – 319

3

Helix

325 – 329

5

Helix

335 – 339

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 21, 2005. Version 3. Checksum: 69E851CC6F7A0388	FASTA	372	42,778
	10 20 30 40 50 60 MAKQYDSVEC PFCDEVSKYE KLAKIGQGTF GEVFKARHRK TGQKVALKKV LMENEKEGFP 70 80 90 100 110 120 ITALREIKIL QLLKHENVVN LIEICRTKAS PYNRCKGSIY LVFDFCEHDL AGLLSNVLVK 130 140 150 160 170 180 FTLSEIKRVM QMLLNGLYYI HRNKILHRDM KAANVLITRD GVLKLADFGL ARAFSLAKNS 190 200 210 220 230 240 QPNRYTNRVV TLWYRPPELL LGERDYGPPI DLWGAGCIMA EMWTRSPIMQ GNTEQHQLAL 250 260 270 280 290 300 ISQLCGSITP EVWPNVDNYE LYEKLELVKG QKRKVKDRLK AYVRDPYALD LIDKLLVLDP 310 320 330 340 350 360 AQRIDSDDAL NHDFFWSDPM PSDLKGMLST HLTSMFEYLA PPRRKGSQIT QQSTNQSRNP 370 ATTNQTEFER VF
	Isoform 2 [UniParc]. Checksum: A0437DC909235A20	FASTA	489	53,365
	10 20 30 40 50 60 MQRDAPPRAP APAPRLPAPP IGAAASSGGG GGGGSGGGGG GASAAPAPPG LSGTTSPRGP 70 80 90 100 110 120 GGGRRAEEAG SAPRGRKWPW RRKWRGRGGA WSAAAAGPGA GAAAAATGGG GGALEAAMAK 130 140 150 160 170 180 QYDSVECPFC DEVSKYEKLA KIGQGTFGEV FKARHRKTGQ KVALKKVLME NEKEGFPITA 190 200 210 220 230 240 LREIKILQLL KHENVVNLIE ICRTKASPYN RCKGSIYLVF DFCEHDLAGL LSNVLVKFTL 250 260 270 280 290 300 SEIKRVMQML LNGLYYIHRN KILHRDMKAA NVLITRDGVL KLADFGLARA FSLAKNSQPN 310 320 330 340 350 360 RYTNRVVTLW YRPPELLLGE RDYGPPIDLW GAGCIMAEMW TRSPIMQGNT EQHQLALISQ 370 380 390 400 410 420 LCGSITPEVW PNVDNYELYE KLELVKGQKR KVKDRLKAYV RDPYALDLID KLLVLDPAQR 430 440 450 460 470 480 IDSDDALNHD FFWSDPMPSD LKGMLSTHLT SMFEYLAPPR RKGSQITQQS TNQSRNPATT NQTEFERVF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"PITALRE, a nuclear CDC2-related protein kinase that phosphorylates the retinoblastoma protein in vitro." Grana X., de Luca A., Sang N., Fu Y., Claudio P.P., Rosenblatt J., Morgan D.O., Giordano A. Proc. Natl. Acad. Sci. U.S.A. 91:3834-3838(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Cloning of a full-length cDNA sequence encoding a cdc2-related protein kinase from human endothelial cells." Best J.L., Presky D.H., Swerlick R.A., Burns D.K., Chu W. Biochem. Biophys. Res. Commun. 208:562-568(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-231.
[3]	"Genomic organization and characterization of promoter function of the human CDK9 gene." Liu H., Rice A.P. Gene 252:51-59(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-231.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	NIEHS SNPs program Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"DNA sequence and analysis of human chromosome 9." 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. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Cervix.
[8]	"A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA." Wei P., Garber M.E., Fang S.-M., Fischer W.H., Jones K.A. Cell 92:451-462(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV TAT.
[9]	"Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro." Wada T., Takagi T., Yamaguchi Y., Watanabe D., Handa H. EMBO J. 17:7395-7403(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Identification of multiple cyclin subunits of human P-TEFb." Peng J.-M., Zhu Y., Milton J.T., Price D.H. Genes Dev. 12:755-762(1998) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH CCNT1 AND CCNT2.
[11]	"A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription." Parada C.A., Roeder R.G. EMBO J. 18:3688-3701(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH HTATSF1; CCNT1; RNA POL II; SUPT5H AND NCL.
[12]	"Cyclin K functions as a CDK9 regulatory subunit and participates in RNA polymerase II transcription." Fu T.J., Peng J., Lee G., Price D.H., Flores O. J. Biol. Chem. 274:34527-34530(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CCNK.
[13]	"FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH." Wada T., Orphanides G., Hasegawa J., Kim D.-K., Shima D., Yamaguchi Y., Fukuda A., Hisatake K., Oh S., Reinberg D., Handa H. Mol. Cell 5:1067-1072(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"Domains in the SPT5 protein that modulate its transcriptional regulatory properties." Ivanov D., Kwak Y.T., Guo J., Gaynor R.B. Mol. Cell. Biol. 20:2970-2983(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"CDK9 autophosphorylation regulates high-affinity binding of the human immunodeficiency virus type 1 tat-P-TEFb complex to TAR RNA." Garber M.E., Mayall T.P., Suess E.M., Meisenhelder J., Thompson N.E., Jones K.A. Mol. Cell. Biol. 20:6958-6969(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY PKA, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-347; THR-350; SER-353; THR-354 AND SER-357, INTERACTION WITH HIV TAT, MUTAGENESIS OF 347-SER--SER-357 AND ASP-167.
[16]	"Positive transcription elongation factor B phosphorylates hSPT5 and RNA polymerase II carboxyl-terminal domain independently of cyclin-dependent kinase-activating kinase." Kim J.B., Sharp P.A. J. Biol. Chem. 276:12317-12323(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-167 AND THR-186.
[17]	"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." Ping Y.-H., Rana T.M. J. Biol. Chem. 276:12951-12958(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[18]	"The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by Cdk9." Lavoie S.B., Albert A.L., Handa H., Vincent M., Bensaude O. J. Mol. Biol. 312:675-685(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"P-TEFb containing cyclin K and Cdk9 can activate transcription via RNA." Lin X., Taube R., Fujinaga K., Peterlin B.M. J. Biol. Chem. 277:16873-16878(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CCNK/CYCLIN K.
[20]	"MCEF, the newest member of the AF4 family of transcription factors involved in leukemia, is a positive transcription elongation factor-b-associated protein." Estable M.C., Naghavi M.H., Kato H., Xiao H., Qin J., Vahlne A., Roeder R.G. J. Biomed. Sci. 9:234-245(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AFF4.
[21]	"CDK9 has the intrinsic property to shuttle between nucleus and cytoplasm, and enhanced expression of cyclin T1 promotes its nuclear localization." Napolitano G., Licciardo P., Carbone R., Majello B., Lania L. J. Cell. Physiol. 192:209-215(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[22]	"Spt5 cooperates with human immunodeficiency virus type 1 Tat by preventing premature RNA release at terminator sequences." Bourgeois C.F., Kim Y.K., Churcher M.J., West M.J., Karn J. Mol. Cell. Biol. 22:1079-1093(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[23]	"Activation of MyoD-dependent transcription by cdk9/cyclin T2." Simone C., Stiegler P., Bagella L., Pucci B., Bellan C., De Falco G., De Luca A., Guanti G., Puri P.L., Giordano A. Oncogene 21:4137-4148(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS MYOD1 KINASE, INTERACTION WITH MYOD1 AND CCNT2.
[24]	"Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties." Kwak Y.T., Guo J., Prajapati S., Park K.-J., Surabhi R.M., Miller B., Gehrig P., Gaynor R.B. Mol. Cell 11:1055-1066(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SUPT5H.
[25]	"Coordination of transcription factor phosphorylation and histone methylation by the P-TEFb kinase during human immunodeficiency virus type 1 transcription." Zhou M., Deng L., Lacoste V., Park H.U., Pumfery A., Kashanchi F., Brady J.N., Kumar A. J. Virol. 78:13522-13533(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[26]	"Dynamics of human immunodeficiency virus transcription: P-TEFb phosphorylates RD and dissociates negative effectors from the transactivation response element." Fujinaga K., Irwin D., Huang Y., Taube R., Kurosu T., Peterlin B.M. Mol. Cell. Biol. 24:787-795(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[27]	"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." Li Q., Price J.P., Byers S.A., Cheng D., Peng J., Price D.H. J. Biol. Chem. 280:28819-28826(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN INACTIVE 7SK SNRNP COMPLEX, PHOSPHORYLATION AT THR-186.
[28]	"The functional role of an interleukin 6-inducible CDK9.STAT3 complex in human gamma-fibrinogen gene expression." Hou T., Ray S., Brasier A.R. J. Biol. Chem. 282:37091-37102(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CYTOKINE SIGNALING, INTERACTION WITH STAT3.
[29]	"Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme." 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. Mol. Cell 27:262-274(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE 7SK SNRNP COMPLEX.
[30]	"Regulation of P-TEFb elongation complex activity by CDK9 acetylation." Fu J., Yoon H.-G., Qin J., Wong J. Mol. Cell. Biol. 27:4641-4651(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-44 BY P300/CBP, IDENTIFICATION IN COMPLEX WITH NCOR1; HEXIM1 AND HDAC3, MUTAGENESIS OF LYS-44.
[31]	"PP2B and PP1alpha cooperatively disrupt 7SK snRNP to release P-TEFb for transcription in response to Ca2+ signaling." Chen R., Liu M., Li H., Xue Y., Ramey W.N., He N., Ai N., Luo H., Zhu Y., Zhou N., Zhou Q. Genes Dev. 22:1356-1368(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-186, DEPHOSPHORYLATION BY PPP1CA, P-TEFB/7SK SNRNP COMPLEX, SUBUNIT, INTERACTION WITH BRD4, ENZYME REGULATION.
[32]	"Phosphatase PPM1A regulates phosphorylation of Thr-186 in the Cdk9 T-loop." Wang Y., Dow E.C., Liang Y.Y., Ramakrishnan R., Liu H., Sung T.L., Lin X., Rice A.P. J. Biol. Chem. 283:33578-33584(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-186, DEPHOSPHORYLATION BY PPM1A AND PPM1B.
[33]	"A La-related protein modulates 7SK snRNP integrity to suppress P-TEFb-dependent transcriptional elongation and tumorigenesis." He N., Jahchan N.S., Hong E., Li Q., Bayfield M.A., Maraia R.J., Luo K., Zhou Q. Mol. Cell 29:588-599(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN COMPLEX WITH LARP7 IN 7SK SNRNP COMPLEX.
[34]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[35]	"Acetylation of conserved lysines in the catalytic core of cyclin-dependent kinase 9 inhibits kinase activity and regulates transcription." Sabo A., Lusic M., Cereseto A., Giacca M. Mol. Cell. Biol. 28:2201-2212(2008) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-44 AND LYS-48 BY PCAF/KAT2B AND GCN5/KAT2A, ENZYME REGULATION BY ACETYLATION, SUBCELLULAR LOCATION.
[36]	"RelA Ser276 phosphorylation is required for activation of a subset of NF-kappaB-dependent genes by recruiting cyclin-dependent kinase 9/cyclin T1 complexes." Nowak D.E., Tian B., Jamaluddin M., Boldogh I., Vergara L.A., Choudhary S., Brasier A.R. Mol. Cell. Biol. 28:3623-3638(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CYTOKINE SIGNALING, INTERACTION WITH RELA/P65.
[37]	"Insights into the function of the human P-TEFb component CDK9 in the regulation of chromatin modifications and co-transcriptional mRNA processing." Pirngruber J., Shchebet A., Johnsen S.A. Cell Cycle 8:3636-3642(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HISTONE REGULATION.
[38]	"CDK9 directs H2B monoubiquitination and controls replication-dependent histone mRNA 3'-end processing." Pirngruber J., Shchebet A., Schreiber L., Shema E., Minsky N., Chapman R.D., Eick D., Aylon Y., Oren M., Johnsen S.A. EMBO Rep. 10:894-900(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HISTONE H2B UBIQUITINATION.
[39]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347 AND THR-350, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 (ISOFORM 2), MASS SPECTROMETRY.
[40]	"55K isoform of CDK9 associates with Ku70 and is involved in DNA repair." Liu H., Herrmann C.H., Chiang K., Sung T.L., Moon S.H., Donehower L.A., Rice A.P. Biochem. Biophys. Res. Commun. 397:245-250(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DNA REPAIR, INTERACTION WITH KU70/XRCC6.
[41]	"Cyclin-dependent kinase 9-cyclin K functions in the replication stress response." Yu D.S., Zhao R., Hsu E.L., Cayer J., Ye F., Guo Y., Shyr Y., Cortez D. EMBO Rep. 11:876-882(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CDK9/CYCLIN K COMPLEX DURING REPLICATION STRESS.
[42]	"Cyclin-dependent kinase-9 is a component of the p300/GATA4 complex required for phenylephrine-induced hypertrophy in cardiomyocytes." Sunagawa Y., Morimoto T., Takaya T., Kaichi S., Wada H., Kawamura T., Fujita M., Shimatsu A., Kita T., Hasegawa K. J. Biol. Chem. 285:9556-9568(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CARDIAC HYPERTROPHY, IDENTIFICATION IN COMPLEX WITH CCNT1/CYCLIN-T1; EP300 AND GATA4.
[43]	"HIV-1 Tat and host AFF4 recruit two transcription elongation factors into a bifunctional complex for coordinated activation of HIV-1 transcription." He N., Liu M., Hsu J., Xue Y., Chou S., Burlingame A., Krogan N.J., Alber T., Zhou Q. Mol. Cell 38:428-438(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE SEC COMPLEX.
[44]	"AFF4, a component of the ELL/P-TEFb elongation complex and a shared subunit of MLL chimeras, can link transcription elongation to leukemia." 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. Mol. Cell 37:429-437(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE SEC COMPLEX.
[45]	"CDK9 regulates AR promoter selectivity and cell growth through serine 81 phosphorylation." 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. Mol. Endocrinol. 24:2267-2280(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN AR KINASE, INTERACTION WITH AR.
[46]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[47]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-186, MASS SPECTROMETRY.
[48]	"CDKI-71, a novel CDK9 inhibitor, is preferentially cytotoxic to cancer cells compared to flavopiridol." Liu X., Shi S., Lam F., Pepper C., Fischer P.M., Wang S. Int. J. Cancer 130:1216-1226(2012) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION BY CDKI-71.
[49]	"Transcription factor IIS cooperates with the E3 ligase UBR5 to ubiquitinate the CDK9 subunit of the positive transcription elongation factor B." Cojocaru M., Bouchard A., Cloutier P., Cooper J.J., Varzavand K., Price D.H., Coulombe B. J. Biol. Chem. 286:5012-5022(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS RPB1/POLR2A CTD KINASE, POLYUBIQUITINATION BY UBR5, INTERACTION WITH UBR5 AND TFIIS/TCEA1.
[50]	"Cdk9 T-loop phosphorylation is regulated by the calcium signaling pathway." Ramakrishnan R., Rice A.P. J. Cell. Physiol. 227:609-617(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-186, ENZYME REGULATION, DEGRADATION BY PROTEASOME, MUTAGENESIS OF THR-186.
[51]	"Protein phosphatase-1 activates CDK9 by dephosphorylating Ser175." Ammosova T., Obukhov Y., Kotelkin A., Breuer D., Beullens M., Gordeuk V.R., Bollen M., Nekhai S. PLoS ONE 6:E18985-E18985(2011) [PubMed] [Europe PMC] [Abstract] Cited for: DEPHOSPHORYLATION AT SER-175 BY PP1, MUTAGENESIS OF SER-175.
[52]	"Controlling the elongation phase of transcription with P-TEFb." Peterlin B.M., Price D.H. Mol. Cell 23:297-305(2006) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON NELF AND DSIF KINASE ACTIVITY.
[53]	"Expanding role of cyclin dependent kinases in cytokine inducible gene expression." Brasier A.R. Cell Cycle 7:2661-2666(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON CYTOKINE SIGNALING.
[54]	"Role of the cyclin-dependent kinase 9-related pathway in mammalian gene expression and human diseases." Romano G., Giordano A. Cell Cycle 7:3664-3668(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON TRANSCRIPTION REGULATION, INHIBITORS.
[55]	"Cyclin-dependent kinase 9: a key transcriptional regulator and potential drug target in oncology, virology and cardiology." Wang S., Fischer P.M. Trends Pharmacol. Sci. 29:302-313(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON TRANSCRIPTION REGULATION, INHIBITORS.
[56]	"Cell cycle, CDKs and cancer: a changing paradigm." Malumbres M., Barbacid M. Nat. Rev. Cancer 9:153-166(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, GENE FAMILY.
[57]	"Pharmacological targeting of CDK9 in cardiac hypertrophy." Krystof V., Chamrad I., Jorda R., Kohoutek J. Med. Res. Rev. 30:646-666(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON CARDIAC HYPERTROPHY, INHIBITORS.
[58]	"A role for cdk9-cyclin k in maintaining genome integrity." Yu D.S., Cortez D. Cell Cycle 10:28-32(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON GENOME INTEGRITY MAINTENANCE.
[59]	"Crystal structure of HIV-1 Tat complexed with human P-TEFb." Tahirov T.H., Babayeva N.D., Varzavand K., Cooper J.J., Sedore S.C., Price D.H. Nature 465:747-751(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-345 IN COMPLEX WITH HIV-1 TAT AND CCNT1, PHOSPHORYLATION AT THR-186.
[60]	"The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation." Baumli S., Lolli G., Lowe E.D., Troiani S., Rusconi L., Bullock A.N., Debreczeni J.E., Knapp S., Johnson L.N. EMBO J. 27:1907-1918(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 2-330 IN COMPLEX WITH INHIBITOR FLAVOPIRIDOL; ATP AND CCNT1, PHOSPHORYLATION AT THR-186 SER347; THR362 AND THR363, AUTOPHOSPHORYLATION, MUTAGENESIS OF THR-186.
[61]	"Halogen bonds form the basis for selective P-TEFb inhibition by DRB." Baumli S., Endicott J.A., Johnson L.N. Chem. Biol. 17:931-936(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-330 IN COMPLEX WITH INHIBITOR DRB, PHOSPHORYLATION AT THR-186.
[62]	"CDK inhibitors roscovitine and CR8 trigger Mcl-1 down-regulation and apoptotic cell death in neuroblastoma cells." 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. Genes Cancer 1:369-380(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-330 IN COMPLEX WITH CCNT1; INHIBITORS ROSCOVITINE AND CR8, PHOSPHORYLATION AT THR-186, ENZYME REGULATION.
[63]	"Patterns of somatic mutation in human cancer genomes." 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. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-59.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L25676 mRNA. Translation: AAA35668.1.
X80230 mRNA. Translation: CAA56516.1.
AF255306 Genomic DNA. Translation: AAF72183.1.
BT019903 mRNA. Translation: AAV38706.1.
AF517840 Genomic DNA. Translation: AAM54039.1.
AL162586 Genomic DNA. Translation: CAI39767.1. Sequence problems.
AL162586 Genomic DNA. Translation: CAI39768.1.
BC001968 mRNA. Translation: AAH01968.1.

IPI

IPI00301923.
IPI00552413.

PIR

A55262.

RefSeq

NP_001252.1. NM_001261.3.

UniGene

Hs.150423.
Hs.706809.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PF6	model	-	A	1-372	[»]
3BLH	X-ray	2.48	A	2-330	[»]
3BLQ	X-ray	2.90	A	2-330	[»]
3BLR	X-ray	2.80	A	2-330	[»]
3LQ5	X-ray	3.00	A	2-330	[»]
3MI9	X-ray	2.10	A	1-345	[»]
3MIA	X-ray	3.00	A	1-345	[»]
3MY1	X-ray	2.80	A	2-330	[»]
3TN8	X-ray	2.95	A	2-330	[»]
3TNH	X-ray	3.20	A	2-330	[»]
3TNI	X-ray	3.23	A	2-330	[»]
4BCF	X-ray	3.01	A	2-330	[»]
4BCH	X-ray	2.96	A	2-330	[»]
4BCI	X-ray	3.10	A	2-330	[»]
4BCJ	X-ray	3.16	A	2-330	[»]
4EC8	X-ray	3.60	A	2-372	[»]
4EC9	X-ray	3.21	A	2-372	[»]
4IMY	X-ray	2.94	A/C/E	1-330	[»]

ProteinModelPortal

P50750.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29016N.

IntAct

P50750. 36 interactions.

MINT

MINT-1532814.

STRING

9606.ENSP00000362361.

PTM databases

PhosphoSite

P50750.

Polymorphism databases

DMDM

68067660.

Proteomic databases

PaxDb

P50750.

PRIDE

P50750.

Protocols and materials databases

DNASU

1025.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000373264; ENSP00000362361; ENSG00000136807.
ENST00000373265; ENSP00000362362; ENSG00000136807.
ENST00000421939; ENSP00000395872; ENSG00000136807.

GeneID

1025.

KEGG

hsa:1025.

UCSC

uc004bse.2. human.

Organism-specific databases

CTD

1025.

GeneCards

GC09P130547.

HGNC

HGNC:1780. CDK9.

HPA

CAB004216.
HPA006738.

MIM

603251. gene.

neXtProt

NX_P50750.

PharmGKB

PA26316.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233024.

HOVERGEN

HBG014652.

InParanoid

P50750.

KO

K02211.

OMA

LMDNEKE.

PhylomeDB

P50750.

Enzyme and pathway databases

BRENDA

2.7.11.22. 2681.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_71. Gene Expression.

SignaLink

P50750.

Gene expression databases

Bgee

P50750.

CleanEx

HS_CDK9.

Genevestigator

P50750.

GermOnline

ENSG00000136807. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P50750.

ChEMBL

CHEMBL3116.

ChiTaRS

CDK9. human.

EvolutionaryTrace

P50750.

GenomeRNAi

1025.

NextBio

4305.

SOURCE

Search...

Entry information

Entry name

CDK9_HUMAN

Accession

Primary (citable) accession number: P50750
Secondary accession number(s): Q5JU24 , Q5JU25, Q5U006, Q96TF1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	June 21, 2005
Last modified:	May 29, 2013
This is version 151 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.