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P50750

- CDK9_HUMAN

UniProt

P50750 - CDK9_HUMAN

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Protein

Cyclin-dependent kinase 9

Gene

CDK9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.24 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.
ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.

Enzyme regulationi

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-48.6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei48 – 481ATP1 PublicationPROSITE-ProRule annotation
Active sitei149 – 1491Proton acceptorPROSITE-ProRule annotation
Binding sitei167 – 1671ATP1 PublicationPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi25 – 339ATPPROSITE-ProRule annotation
Nucleotide bindingi104 – 1063ATP1 PublicationPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. chromatin binding Source: Ensembl
  3. cyclin-dependent protein serine/threonine kinase activity Source: ProtInc
  4. DNA binding Source: MGI
  5. protein kinase activity Source: ProtInc
  6. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB
  7. snRNA binding Source: Ensembl
  8. transcription regulatory region DNA binding Source: Ensembl

GO - Biological processi

  1. cell proliferation Source: ProtInc
  2. cellular response to cytokine stimulus Source: UniProtKB
  3. DNA repair Source: UniProtKB-KW
  4. gene expression Source: Reactome
  5. negative regulation of cell cycle arrest Source: UniProtKB
  6. positive regulation of transcription from RNA polymerase II promoter Source: Reactome
  7. positive regulation of viral transcription Source: Reactome
  8. protein phosphorylation Source: MGI
  9. regulation of DNA repair Source: UniProtKB
  10. regulation of histone modification Source: UniProtKB
  11. replication fork arrest Source: UniProtKB
  12. transcription, DNA-templated Source: Reactome
  13. transcription elongation from RNA polymerase II promoter Source: Reactome
  14. transcription from RNA polymerase II promoter Source: Reactome
  15. transcription initiation from RNA polymerase II promoter Source: Reactome
  16. transforming growth factor beta receptor signaling pathway Source: Reactome
  17. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.22. 2681.
ReactomeiREACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6259. HIV elongation arrest and recovery.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_6905. Interactions of Tat with host cellular proteins.
REACT_833. RNA Polymerase II Transcription Elongation.
SignaLinkiP50750.

Names & Taxonomyi

Protein namesi
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 namesi
Name:CDK9
Synonyms:CDC2L4, TAK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:1780. CDK9.

Subcellular locationi

Nucleus. Cytoplasm. NucleusPML 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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. intracellular membrane-bounded organelle Source: HPA
  3. membrane Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. nucleus Source: HPA
  6. PML body Source: UniProtKB
  7. positive transcription elongation factor complex b Source: UniProtKB
  8. transcription elongation factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Chronic activation of CDK9 causes cardiac myocyte enlargement leading to cardiac hypertrophy, and confers predisposition to heart failure.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 441K → R: Impaired kinase and transcriptional elongation activities, but normal cyclin T1 and HEXIM1 binding. 1 Publication
Mutagenesisi167 – 1671D → N: Abrogates kinase activity. 2 Publications
Mutagenesisi175 – 1751S → A: Constitutive kinase activity. 1 Publication
Mutagenesisi175 – 1751S → D: Mimics phosphorylation, constitutive loss of kinase activity. 1 Publication
Mutagenesisi186 – 1861T → A: Abrogates autophosphorylation; no effect on kinase activity, but impaired CTD phosphorylation. 3 Publications
Mutagenesisi186 – 1861T → D: Mimics autophosphorylation; constitutive kinase activity, independently of calcium signaling. 3 Publications
Mutagenesisi347 – 35711SQITQQSTNQS → AQIAQQAANQA: Loss of autophosphorylation and impaired interaction with HIV TAT. 1 PublicationAdd
BLAST
Mutagenesisi347 – 35711SQITQQSTNQS → EQIEQQEENQE: Mimics autophosphorylation and promotes interaction with HIV TAT. 1 PublicationAdd
BLAST

Organism-specific databases

PharmGKBiPA26316.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 372372Cyclin-dependent kinase 9PRO_0000085800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei29 – 291Phosphothreonine1 Publication
Modified residuei44 – 441N6-acetyllysine; by P300/CBP, PCAF/KAT2B and GCN5/KAT2A2 Publications
Modified residuei48 – 481N6-acetyllysine; by PCAF/KAT2B and GCN5/KAT2A1 Publication
Modified residuei175 – 1751Phosphoserine1 Publication
Modified residuei186 – 1861Phosphothreonine; by CaMK1D9 Publications
Modified residuei347 – 3471Phosphoserine; by CDK9 and PKA4 Publications
Modified residuei350 – 3501Phosphothreonine; by CDK92 Publications
Modified residuei353 – 3531Phosphoserine; by CDK91 Publication
Modified residuei354 – 3541Phosphothreonine; by CDK91 Publication
Modified residuei357 – 3571Phosphoserine; by CDK91 Publication
Modified residuei362 – 3621Phosphothreonine; by CDK91 Publication
Modified residuei363 – 3631Phosphothreonine; by CDK91 Publication

Post-translational modificationi

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 (PubMed:18566585).13 Publications
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.2 Publications
Polyubiquitinated and thus activated by UBR5. This ubiquitination is promoted by TFIIS/TCEA1 and favors 'Ser-2' phosphorylation of RPB1/POLR2A CTD.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP50750.
PaxDbiP50750.
PRIDEiP50750.

PTM databases

PhosphoSiteiP50750.

Expressioni

Tissue specificityi

Ubiquitous.

Inductioni

By replication stress, in chromatin. Probably degraded by the proteasome upon Thr-186 dephosphorylation.

Gene expression databases

BgeeiP50750.
CleanExiHS_CDK9.
ExpressionAtlasiP50750. baseline and differential.
GenevestigatoriP50750.

Organism-specific databases

HPAiCAB004216.
HPA006738.

Interactioni

Subunit structurei

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 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 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/XRCC6.29 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATRQ135353EBI-1383449,EBI-968983
ATRIPQ8WXE13EBI-1383449,EBI-747353
CCNT1O6056313EBI-1383449,EBI-2479671
CDC37Q165433EBI-1383449,EBI-295634
CLSPNQ9HAW43EBI-1383449,EBI-1369377
DHX30Q7L2E35EBI-1383449,EBI-1211456
FKBP5Q134514EBI-1383449,EBI-306914
HEXIM1O949927EBI-1383449,EBI-2832510
HSP90AA1P079002EBI-1383449,EBI-296047
HSP90AB1P082382EBI-1383449,EBI-352572
JMJD6Q6NYC15EBI-1383449,EBI-8464037
LARP7Q4G0J37EBI-1383449,EBI-2371923
NR2E3Q9Y5X44EBI-1383449,EBI-7216962
tatP046085EBI-1383449,EBI-6164389From a different organism.

Protein-protein interaction databases

BioGridi107459. 184 interactions.
DIPiDIP-29016N.
IntActiP50750. 61 interactions.
MINTiMINT-1532814.
STRINGi9606.ENSP00000362361.

Structurei

Secondary structure

1
372
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 153Combined sources
Helixi16 – 183Combined sources
Beta strandi19 – 246Combined sources
Beta strandi28 – 303Combined sources
Beta strandi32 – 387Combined sources
Turni39 – 413Combined sources
Beta strandi44 – 496Combined sources
Beta strandi56 – 594Combined sources
Helixi61 – 7212Combined sources
Beta strandi81 – 877Combined sources
Beta strandi98 – 1047Combined sources
Beta strandi107 – 1093Combined sources
Helixi110 – 1156Combined sources
Beta strandi116 – 1183Combined sources
Helixi123 – 14220Combined sources
Helixi152 – 1543Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi163 – 1653Combined sources
Helixi168 – 1703Combined sources
Beta strandi178 – 1814Combined sources
Helixi192 – 1943Combined sources
Helixi197 – 2004Combined sources
Helixi209 – 22416Combined sources
Helixi234 – 24512Combined sources
Turni250 – 2523Combined sources
Helixi256 – 2583Combined sources
Helixi260 – 2623Combined sources
Helixi263 – 2653Combined sources
Helixi275 – 2839Combined sources
Helixi286 – 29510Combined sources
Helixi300 – 3023Combined sources
Helixi306 – 3105Combined sources
Helixi313 – 3164Combined sources
Beta strandi317 – 3193Combined sources
Helixi325 – 3295Combined sources
Helixi335 – 3395Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PF6model-A1-372[»]
3BLHX-ray2.48A2-330[»]
3BLQX-ray2.90A2-330[»]
3BLRX-ray2.80A2-330[»]
3LQ5X-ray3.00A2-330[»]
3MI9X-ray2.10A1-345[»]
3MIAX-ray3.00A1-345[»]
3MY1X-ray2.80A2-330[»]
3TN8X-ray2.95A2-330[»]
3TNHX-ray3.20A2-330[»]
3TNIX-ray3.23A2-330[»]
4BCFX-ray3.01A2-330[»]
4BCGX-ray3.08A2-330[»]
4BCHX-ray2.96A2-330[»]
4BCIX-ray3.10A2-330[»]
4BCJX-ray3.16A2-330[»]
4EC8X-ray3.60A2-372[»]
4EC9X-ray3.21A2-372[»]
4IMYX-ray2.94A/C/E1-330[»]
4OGRX-ray3.00A/E/I1-330[»]
4OR5X-ray2.90A/F7-332[»]
ProteinModelPortaliP50750.
SMRiP50750. Positions 8-332.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50750.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 315297Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni166 – 19126T-loopAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120511.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP50750.
KOiK02211.
OMAiMELPKGQ.
OrthoDBiEOG76DTSM.
PhylomeDBiP50750.
TreeFamiTF101039.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P50750-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAKQYDSVEC PFCDEVSKYE KLAKIGQGTF GEVFKARHRK TGQKVALKKV
60 70 80 90 100
LMENEKEGFP ITALREIKIL QLLKHENVVN LIEICRTKAS PYNRCKGSIY
110 120 130 140 150
LVFDFCEHDL AGLLSNVLVK FTLSEIKRVM QMLLNGLYYI HRNKILHRDM
160 170 180 190 200
KAANVLITRD GVLKLADFGL ARAFSLAKNS QPNRYTNRVV TLWYRPPELL
210 220 230 240 250
LGERDYGPPI DLWGAGCIMA EMWTRSPIMQ GNTEQHQLAL ISQLCGSITP
260 270 280 290 300
EVWPNVDNYE LYEKLELVKG QKRKVKDRLK AYVRDPYALD LIDKLLVLDP
310 320 330 340 350
AQRIDSDDAL NHDFFWSDPM PSDLKGMLST HLTSMFEYLA PPRRKGSQIT
360 370
QQSTNQSRNP ATTNQTEFER VF
Length:372
Mass (Da):42,778
Last modified:June 21, 2005 - v3
Checksum:i69E851CC6F7A0388
GO
Isoform 2 (identifier: P50750-2) [UniParc]FASTAAdd to Basket

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

Note: Contains a phosphoserine at position 35.

Show »
Length:489
Mass (Da):53,365
Checksum:iA0437DC909235A20
GO

Sequence cautioni

The sequence CAI39767.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631L → P in AAV38706. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591F → L.1 Publication
Corresponds to variant rs55640715 [ dbSNP | Ensembl ].
VAR_041982
Natural varianti231 – 2311G → A.2 Publications
VAR_013456

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MQRDAPPRAPAPAPRLPAPP IGAAASSGGGGGGGSGGGGG GASAAPAPPGLSGTTSPRGP GGGRRAEEAGSAPRGRKWPW RRKWRGRGGAWSAAAAGPGA GAAAAATGGGGGALEAAM in isoform 2. CuratedVSP_016288

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6879.1. [P50750-1]
PIRiA55262.
RefSeqiNP_001252.1. NM_001261.3. [P50750-1]
UniGeneiHs.150423.
Hs.706809.

Genome annotation databases

EnsembliENST00000373264; ENSP00000362361; ENSG00000136807. [P50750-1]
GeneIDi1025.
KEGGihsa:1025.
UCSCiuc004bse.2. human. [P50750-1]

Polymorphism databases

DMDMi68067660.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS6879.1. [P50750-1 ]
PIRi A55262.
RefSeqi NP_001252.1. NM_001261.3. [P50750-1 ]
UniGenei Hs.150423.
Hs.706809.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
4BCG X-ray 3.08 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 [» ]
4OGR X-ray 3.00 A/E/I 1-330 [» ]
4OR5 X-ray 2.90 A/F 7-332 [» ]
ProteinModelPortali P50750.
SMRi P50750. Positions 8-332.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107459. 184 interactions.
DIPi DIP-29016N.
IntActi P50750. 61 interactions.
MINTi MINT-1532814.
STRINGi 9606.ENSP00000362361.

Chemistry

BindingDBi P50750.
ChEMBLi CHEMBL2111389.
GuidetoPHARMACOLOGYi 1981.

PTM databases

PhosphoSitei P50750.

Polymorphism databases

DMDMi 68067660.

Proteomic databases

MaxQBi P50750.
PaxDbi P50750.
PRIDEi P50750.

Protocols and materials databases

DNASUi 1025.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373264 ; ENSP00000362361 ; ENSG00000136807 . [P50750-1 ]
GeneIDi 1025.
KEGGi hsa:1025.
UCSCi uc004bse.2. human. [P50750-1 ]

Organism-specific databases

CTDi 1025.
GeneCardsi GC09P130547.
HGNCi HGNC:1780. CDK9.
HPAi CAB004216.
HPA006738.
MIMi 603251. gene.
neXtProti NX_P50750.
PharmGKBi PA26316.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120511.
HOGENOMi HOG000233024.
HOVERGENi HBG014652.
InParanoidi P50750.
KOi K02211.
OMAi MELPKGQ.
OrthoDBi EOG76DTSM.
PhylomeDBi P50750.
TreeFami TF101039.

Enzyme and pathway databases

BRENDAi 2.7.11.22. 2681.
Reactomei REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6259. HIV elongation arrest and recovery.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_6905. Interactions of Tat with host cellular proteins.
REACT_833. RNA Polymerase II Transcription Elongation.
SignaLinki P50750.

Miscellaneous databases

ChiTaRSi CDK9. human.
EvolutionaryTracei P50750.
GeneWikii CDK9.
Cyclin-dependent_kinase_9.
GenomeRNAii 1025.
NextBioi 4305.
PROi P50750.
SOURCEi Search...

Gene expression databases

Bgeei P50750.
CleanExi HS_CDK9.
ExpressionAtlasi P50750. baseline and differential.
Genevestigatori P50750.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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 bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription."
    Jang M.K., Mochizuki K., Zhou M., Jeong H.S., Brady J.N., Ozato K.
    Mol. Cell 19:523-534(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BRD4.
  29. "Recruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4."
    Yang Z., Yik J.H., Chen R., He N., Jang M.K., Ozato K., Zhou Q.
    Mol. Cell 19:535-545(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BRD4.
  30. "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.
  31. "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.
  32. "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.
  33. "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.
  34. "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.
  35. "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.
  36. "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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  37. "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.
  38. "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.
  39. "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.
  40. "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.
  41. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347 AND THR-350, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  42. "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.
  43. "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.
  44. "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.
  45. "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.
  46. "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.
  47. Cited for: FUNCTION IN AR KINASE, INTERACTION WITH AR.
  48. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  49. Cited for: IDENTIFICATION IN THE SEC COMPLEX.
  50. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  51. "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.
  52. "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.
  53. "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 THE PROTEASOME, MUTAGENESIS OF THR-186.
  54. Cited for: PHOSPHORYLATION AT SER-175, DEPHOSPHORYLATION AT SER-175 BY PP1, MUTAGENESIS OF SER-175.
  55. "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.
  56. "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.
  57. "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.
  58. "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.
  59. "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.
  60. "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.
  61. "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.
  62. "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.
  63. "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 SER-347; THR-362 AND THR-363, AUTOPHOSPHORYLATION, MUTAGENESIS OF THR-186.
  64. "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.
  65. "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.
  66. "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.

Entry informationi

Entry nameiCDK9_HUMAN
AccessioniPrimary (citable) accession number: P50750
Secondary accession number(s): Q5JU24
, Q5JU25, Q5U006, Q96TF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 21, 2005
Last modified: November 26, 2014
This is version 168 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

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).2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3