CDK9 cyclin dependent kinase 9 [Homo sapiens (human)] - Gene

Summary

Official Symbol: CDK9provided by HGNC
Official Full Name: cyclin dependent kinase 9provided by HGNC
Primary source: HGNC:HGNC:1780
See related: Ensembl:ENSG00000136807 MIM:603251; AllianceGenome:HGNC:1780
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: TAK; C-2k; CTK1; CDC2L4; PITALRE
Summary: The protein encoded by this gene is a member of the cyclin-dependent protein kinase (CDK) family. CDK family members are highly similar to the gene products of S. cerevisiae cdc28, and S. pombe cdc2, and known as important cell cycle regulators. This kinase was found to be a component of the multiprotein complex TAK/P-TEFb, which is an elongation factor for RNA polymerase II-directed transcription and functions by phosphorylating the C-terminal domain of the largest subunit of RNA polymerase II. This protein forms a complex with and is regulated by its regulatory subunit cyclin T or cyclin K. HIV-1 Tat protein was found to interact with this protein and cyclin T, which suggested a possible involvement of this protein in AIDS. [provided by RefSeq, Jul 2008]
Expression: Ubiquitous expression in ovary (RPKM 32.0), spleen (RPKM 23.0) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 9q34.11

Exon count:: 7

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	9	NC_000009.12 (127786034..127790792)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	9	NC_060933.1 (139993485..139998243)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	9	NC_000009.11 (130548313..130553071)

Chromosome 9 - NC_000009.12 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

CDK9 phosphorylates RUNX1 to promote megakaryocytic fate in megakaryocytic-erythroid progenitors.
Title: CDK9 phosphorylates RUNX1 to promote megakaryocytic fate in megakaryocytic-erythroid progenitors.
Human promoter directionality is determined by transcriptional initiation and the opposing activities of INTS11 and CDK9.
Title: Human promoter directionality is determined by transcriptional initiation and the opposing activities of INTS11 and CDK9.
Transcriptional regulation and therapeutic potential of cyclin-dependent kinase 9 (CDK9) in sarcoma.
Title: Transcriptional regulation and therapeutic potential of cyclin-dependent kinase 9 (CDK9) in sarcoma.
CDK9 inhibition activates innate immune response through viral mimicry.
Title: CDK9 inhibition activates innate immune response through viral mimicry.
Actin associates with actively elongating genes and binds directly to the Cdk9 subunit of P-TEFb.
Title: Actin associates with actively elongating genes and binds directly to the Cdk9 subunit of P-TEFb.
RNF20 contributes to epigenetic immunosuppression through CDK9-dependent LSD1 stabilization.
Title: RNF20 contributes to epigenetic immunosuppression through CDK9-dependent LSD1 stabilization.
CDK7 and CDK9 inhibition interferes with transcription, translation, and stemness, and induces cytotoxicity in GBM irrespective of temozolomide sensitivity.
Title: CDK7 and CDK9 inhibition interferes with transcription, translation, and stemness, and induces cytotoxicity in GBM irrespective of temozolomide sensitivity.
Histone-lysine N-methyltransferase EHMT2 (G9a) inhibition mitigates tumorigenicity in Myc-driven liver cancer.
Title: Histone-lysine N-methyltransferase EHMT2 (G9a) inhibition mitigates tumorigenicity in Myc-driven liver cancer.
Degradation of CDK9 by Ubiquitin E3 Ligase STUB1 Regulates P-TEFb Level and Its Functions for Global Target Gene Expression within Mammalian Cells.
Title: Degradation of CDK9 by Ubiquitin E3 Ligase STUB1 Regulates P-TEFb Level and Its Functions for Global Target Gene Expression within Mammalian Cells.
Selective CDK9 knockdown sensitizes TRAIL response by suppression of antiapoptotic factors and NF-kappaB pathway.
Title: Selective CDK9 knockdown sensitizes TRAIL response by suppression of antiapoptotic factors and NF-kappaB pathway.

Submit: New GeneRIF Correction See all GeneRIFs (167)

Phenotypes

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Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Replication interactions

Interaction	Pubs
HIV transcription is restricted by the dissociation of a functional P-TEFb complex (CCNT1-CDK9) caused by PPP1R10 (PNUTS)	PubMed
HIV-1 NL4-3 replication requires CDK9 as replication is inhibited when CDK9 is deleted through CRISPR/Cas9 genome editing	PubMed

Protein interactions

Protein	Gene	Interaction	Pubs
Nef	nef	HIV-1 Nef induces cyclin K interaction with CDK9, which contributes to the inhibition of CDK9 nuclear translocation	PubMed
	nef	CDK9 mRNA and kinase activity are upregulated in HIV-1 Nef-expressing human T cell lines	PubMed
	nef	HIV-1 Nef interacts with Hsp40, leading to increased Hsp40 translocation to the nucleus of infected cells and facilitation of viral gene expression by complex formation of Hsp40 with the cdk9-associated transcription complex	PubMed
Tat	tat	HIV-1 Tat binds to CDK9 and CCNT1 (CycT1) in an additive manner as shown through Fluoppi (fluorescent-based technology detecting protein-protein interactions)	PubMed
	tat	The N-terminus (amino acids 1-48, including activation domain) of HIV-1 Tat binds to P-TEFb through a direct interaction with the N-terminus (amino acids 1-290) of cyclin T1 during Tat-mediated transactivation of the HIV-1 LTR promoter	PubMed
	tat	Binding of HIV-1 Tat to CDK9 stabilizes hydrogen bonds between ATP and residues Lys48, Asp104, and Cys106 and facilitates the salt bridge network pertaining to the phosphorylated Thr186 at the activation loop	PubMed
	tat	HIV-1 Tat competes with HEXIM1 for binding to 7SK RNA and inhibits the formation of the P-TEFb-HEXIM1-7SK complex. Tat binds to nucleotides 10-48 of 7SK RNA	PubMed
	tat	A La-related protein, LARP7, is associated with P-TEFb, HEXIM1/2, MEPCE, and 7SK RNA in a large stable complex form. Knockdown of LARP7 decreases the steady-state level of 7SK, but increases free P-TEFb and enhances Tat-mediated transcription	PubMed
	tat	HIV-1 Tat forms at least two distinct P-TEFb-containing complexes. Tatcom1 is composed of P-TEFb, AF9, ENL, ELL, AFF1, AFF4, and PAF1, presenting strong CTD-kinase activity, while Tatcom2 consists of 7SK, LARP7, and MEPCE with two molecules of Tat/P-TEFb	PubMed
	tat	HIV-1 Tat recruits P-TEFb to the HIV-1 Transcription Activation Response (TAR) RNA during Tat-mediated transactivation of the HIV-1 LTR promoter	PubMed
	tat	P-TEFb interacts with HIV-1 Tat as part of both the HIV-1 transcription preinitiation and elongation complexes	PubMed
	tat	Cyclin-dependent kinase 9 (CDK9, CDC2-related kinase) is identified to interact with HIV-1 Tat mutant Nullbasic in HeLa cells by LC MS/MS	PubMed
	tat	A homogeneous assay in AlphaLISA indicates that the affinity between HIV-1 Tat and pTEFb is determined to be approximately 20pM, and only 7% of purified Tat is found to be active in forming tertiary complex with pTEFb	PubMed
	tat	AFF1 enhances the affinity of HIV-1 Tat for CycT1, which competitively dissociates HEXIM1 and is responsible for AFF1's promotion of Tat's extraction of CDK9/CycT1 from 7SK snRNP	PubMed
	tat	HIV-1 Tat increases the amount of ELL2 bound to P-TEFb without affecting the AFF4-P-TEFb binding. CDK9 is required for the Tat-induced ELL2 accumulation and Tat interaction with ELL2	PubMed
	tat	The interaction of HIV-1 Tat with HIV-1 Transcription Activation Response (TAR) RNA is enhanced by the interaction of Tat with P-TEFb, and TAR RNA also enhances the interaction between Tat and cyclin T1	PubMed
	tat	P-TEFb is required for HIV-1 Tat-mediated transcriptional activation	PubMed
	tat	During HIV-1 Tat mediated transactivation of the HIV-1 LTR promoter, Tat stimulates the phosphorylation of the C-terminal domain (CTD) of RNA polymerase II by P-TEFb, leading to transcription elongation	PubMed
	tat	ZASC1, a cellular transcription factor, interacts with HIV-1 Tat and cellular proteins CDK9/Cyclin T1 (P-TEFb) in a TAR-independent manner, suggesting that the Tat/P-TEFb complex in the transcriptional elongation site is promoted by ZASC1	PubMed
	tat	Small molecule ligands disrupt the CDK9/Cyclin T1/Tat complex and dissociate CDK9 away from the HIV-1 transcription complex	PubMed
	tat	The Tat-AFF4-P-TEFb complex containing HIV-1 Tat (residues 1-48), human Cyclin T1 (residues 1-266), human Cdk9 (residues 7-332), and human AFF4 (residues 27-69) is determined by the crystal structure analysis	PubMed
	tat	HIV-1 Tat recruits PPM1G phosphatase protein to dephosphorylate the T loop of CDK9 and release P-TEFb from the 7SK snRNP complex	PubMed
	tat	Binding of isolated AFF1(1-308) CBS to CDK9/CycT1 prevents HIV-1 Tat from activating HIV transcription and assembling complete SECs (AFF1, AFF4, ELL2, and ENL). The AFF1(1-308) M60A/L61A mutant shows no suppression of Tat transactivation	PubMed
	tat	The interaction of HIV-1 Tat with cellular transcription factors CDK9 and Sp1 is required for Tat activation of MAP2K3-, MAP2K6-, and IRF7-mediated luciferase transcription	PubMed
	tat	The interaction of Tip110 with HIV-1 Tat and the RNAPII C-terminal domain leads to the recruitment of increased CDK9/CycT1 to the transcription complex	PubMed
	tat	CDK9-CycT1-AFF1 is stimulated by HIV-1 Tat and transferred as a single complex unit to BRD4 upon stress-induced disruption of AFF1-containing 7SK snRNP (HEXIM1, MEPCE, LARP7, 7SK RNA, CDK9, CycT1, and AFF1)	PubMed
	tat	Phosphorylation of CDK9 at position Ser175 regulates the competition between HIV-1 Tat and BRD4 for P-TEFb binding	PubMed
	tat	JQ1, a small molecule inhibitor of Brd4, increases CDK9 T-loop phosphorylation in Tat-dependent manner and partially dissociates P-TEFb from 7SK snRNP in Jurkat cells	PubMed
	tat	Brd4 inhibits HIV-1 Tat-human super elongation complex (components AFF4, ELL2, CycT1, and CDK9) by competing with HIV-1 Tat for binding to P-TEFb on HIV-1 promoter	PubMed
	tat	CDK2 regulates HIV-1 Tat-mediated transcription by phosphorylation of CDK9 at position Ser90 and decreases 7SK RNA levels	PubMed
	tat	HIV-1 Tat mutations at positions Y26 and K28 show the most defect in the Tat:TAR:P-TEFb complex formation, but Tat:P-TEFb assembly is not abolished	PubMed
	tat	HIV-1 Tat mutations at positions P3, P6, W11, K12, T20, T23, V36, I39, T40, and Y47 show decreased Tat activity and P-TEFb assembly/Cdk9 activation, with three residues P3, P6, and W11 possibly involved in Cdk9 interactions	PubMed
	tat	Coexpression of RNA-binding domain deficient Tat (T-RS) and two fusion proteins CycT1N-Rev and Cdk9-Rev synergistically stimulates transcription when P-TEFb is tethered to RNA through Rev, and thus T-RS is no longer as an inhibitor	PubMed
	tat	An RNA-binding domain deficient Tat excludes wild-type Tat from the promoter by preferentially assembling with P-TEFb through the Tat activation domain, but can not facilitate transfer of P-TEFb to TAR, thus blocking transition to elongation	PubMed
	tat	HIV-1 Tat-mediated release of P-TEFb from the 7SK sn RNP results in a conformational change in 7SK RNA and release of HEXIM1 from the complex	PubMed
	tat	TAR binds Tat and P-TEFb as it emerges on the nascent transcript, competitively displacing the inhibitory 7SK snRNP (HEXIM1 and LARP7) and activating the P-TEFb kinase	PubMed
	tat	HIV-1 Tat stimulates the phosphorylation of SPT5 by P-TEFb during transactivation of the HIV-1 LTR promoter	PubMed
	tat	HIV-1 Tat-mediated stimulation of RNA polymerase II C-terminal domain phosphorylation by P-TEFb leads to stimulation of co-transcriptional capping of HIV-1 mRNA	PubMed
	tat	Inhibition of Ca(2+) signaling leads to dephosphorylation of Thr186 on CDK9, which results in the decreased transactivation of the HIV-1 LTR by HIV-1 Tat	PubMed
	tat	ATP analogs are effective inhibitors of HIV-1 Tat-mediated activated transcription with a decreased loading of CDK9 onto the HIV-1 DNA	PubMed
	tat	HIV-1 Q35L mutant fails to efficiently bind either CDK9 or CycT1 resulting in the defective gene expression. However, the I39Q mutation rescues the Q35L mutant's loss of function	PubMed
	tat	SKIP is required for Tat transactivation in vivo and stimulates HIV-1 transcription elongation by associating with CycT1:CDK9 (P-TEFb) and Tat:P-TEFb complexes both in nuclear extracts and in recombinant Tat:P-TEFb:TAR RNA complexes in vitro	PubMed
	tat	HIV-1 Tat and P-TEFb undergo constant association and dissociation cycles with TAR and the elongating polymerase in living cells	PubMed
	tat	Tat-C/EBPbeta association is mediated through cdk9, which phosphorylates C/EBPbeta. C/EBPbeta-cyclin T1 association requires the presence of cdk9	PubMed
	tat	HIV-1 infection leads to activation of P-TEFb due to HIV-1 Tat-mediated release of P-TEFb from the large form	PubMed
	tat	The P-TEFb binding region (amino acids 1209-1362) of BRD4 is required for HIV-1 Tat-mediated release of P-TEFb from the 7SK snRNP	PubMed
	tat	CDK11 depletion reduces protein expression of CDK9 and HEXIM1 and Tat transactivation of HIV-1 provirus	PubMed
	tat	Acetylation of HIV-1 Tat by cellular histone acetyltransferases regulates the binding of Tat to P-TEFb	PubMed
	tat	Mutant CycT1 protein containing triple T-to-A mutations in the N-terminal region (amino acids T143, T149, and T155) associates with CDK9 and HIV-1 Tat as a kinase-negative complex and blocks HIV transactivation	PubMed
	tat	The human I-mfa domain-containing protein (HIC) interacts with both P-TEFb and HIV-1 Tat, and modulates Tat transactivation of the HIV-1 LTR promoter	PubMed
	tat	Cyclin T1 is capable of recruiting CDK9 and HIV-1 Tat to splicing factor-rich nuclear speckle regions, suggesting nuclear speckles are a site of P-TEFb and Tat function	PubMed
	tat	The up and downregulation of expression of CDK9 and cyclin T1 or sequestration of cyclin T1 in infected cells may regulate HIV-1 latency by up or downregulating HIV-1 Tat transcriptional activation	PubMed
	tat	Amino acids 260-263 of cyclin T1 are critical for HIV-1 Tat-mediated transcriptional activation, and mediate the species specificity of cyclin T1 and P-TEFb binding to Tat	PubMed
	tat	P-TEFb regulates HIV-1 Tat-mediated activation of transcription through two built-in auto inhibitory mechanisms, autophosphorylation of CDK9 and cyclin T1 binding to the transcription elongation factor Tat-SF1	PubMed
	tat	Undetectable CycT1 protein and un-phosphorylation of CDK9 in undifferentiated monocytes result in the lack of Tat transactivation of the LTR promoter in early viral life cycle	PubMed
	tat	Interaction of P-TEFb with histone H1 results in its phosphorylation at position Ser-183 in a Tat-dependent manner, which is necessary for transcription from the HIV-1 LTR	PubMed
	tat	CDK9 is involved in Tat-induced MCP-1/CCL2 gene expression in human astrocytes	PubMed
	tat	PARP1 negatively regulates HIV-1 transcription by directly competing with Tat-P-TEFb complex for binding to TAR RNA	PubMed
	tat	HIV-1 Tat-induced kinase activity of P-TEFb is highly sensitive to flavopiridol, a CDK inhibitor. P-TEFb-mediated phosphorylation of RNAP II CTD, SPT5, and Tat-SF1 during HIV-1 transcription elongation is also highly sensitive to flavopiridol	PubMed
	tat	The p160 nuclear receptor co-activator GRIP1 binds to the N-terminal region of HIV-1 Tat, bridging HIV-1 LTR promoter-bound factors to the Tat-P-TEFb complex and enhancing the transactivating activity of Tat	PubMed
	tat	Cdk9, the catalytic subunit of P-TEFb, is ubiquitinated by Skp1/Cul1/F-box protein E3 ubiquitin ligase Skp2, which facilitates the formation of the RNA-protein complex between P-TEFb, Tat, and TAR, thereby enhancing Tat transactivation	PubMed
	tat	The growth factor granulin and the promyelocytic leukemia (PML) protein regulate HIV-1 Tat-mediated transcriptional activation by competing with the Tat interaction with cyclin T1/P-TEFb	PubMed
	tat	TFIIH inhibits the phosphorylation of CDK9 in the HIV-1 transcription preinitiation complex, while HIV-1 Tat stimulates CDK9 autophosphorylation to activate transcription elongation	PubMed
	tat	Overexpression of CDK9 or CDK9 mutants inhibits HIV-1 Tat transcriptional activation	PubMed
	tat	Tat-SF1 is a required cofactor for HIV-1 Tat activity that complexes with P-TEFb and Tat, and stimulates Tat-mediated activation of the HIV-1 LTR promoter	PubMed
	tat	P-TEFb, Puralpha and HIV-1 Tat cooperate to activate the TNFalpha promoter	PubMed
	tat	Hsp70 and Hsp90/Cdc37 stabilize CDK9 as well as the assembly of an active P-TEFb complex which is stimulated by HIV-1 Tat during HIV-1 transcriptional activation	PubMed
	tat	HIV-1 Tat competes with CIITA for the binding to P-TEFb, leading to the downregulation of MHC class II gene expression	PubMed
	tat	MAQ1 and 7SK RNA interact with P-TEFb and compete with the binding of HIV-1 Tat to cyclin T1, suggesting the TAR RNA/Tat lentivirus system evolved to subvert the cellular 7SK RNA/MAQ1 system	PubMed
Vif	vif	HIV-1 Vif interacts with CDK9 to regulate Vif-mediated G1-to-S transition and siRNA against CDK9 counteracts the transition	PubMed
Vpr	vpr	HIV-1 Vpr interacts with CDK9 through binding to HIV-1 Tat and cyclin T1 in a ternary complex, Tat-Vpr-Cyclin T1-CDK9, and enhances Tat transactivation of the viral LTR promoter	PubMed

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

WI-15190 (e-PCR)
- UniSTS:42267

D9S2040 (e-PCR)
- UniSTS:1146

WI-19919 (e-PCR)
- UniSTS:1147

RH16566 (e-PCR)
- UniSTS:3451

SHGC-33502 (e-PCR)
- UniSTS:80767

STS-L25676 (e-PCR)
- UniSTS:63402

CDK9_3250.2 (e-PCR)
- UniSTS:466118

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables 7SK snRNA binding	IDA Inferred from Direct Assay more info	PubMed
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables DNA binding	IDA Inferred from Direct Assay more info	PubMed
enables RNA polymerase II CTD heptapeptide repeat S2 kinase activity	IEA Inferred from Electronic Annotation more info
enables RNA polymerase II CTD heptapeptide repeat S5 kinase activity	IEA Inferred from Electronic Annotation more info
enables RNA polymerase II CTD heptapeptide repeat S7 kinase activity	IEA Inferred from Electronic Annotation more info
enables RNA polymerase II CTD heptapeptide repeat T4 kinase activity	IEA Inferred from Electronic Annotation more info
enables RNA polymerase II CTD heptapeptide repeat Y1 kinase activity	IEA Inferred from Electronic Annotation more info
enables RNA polymerase II CTD heptapeptide repeat kinase activity	IBA Inferred from Biological aspect of Ancestor more info
enables RNA polymerase II CTD heptapeptide repeat kinase activity	IDA Inferred from Direct Assay more info	PubMed
enables RNA polymerase II cis-regulatory region sequence-specific DNA binding	IEA Inferred from Electronic Annotation more info
enables chromatin binding	ISS Inferred from Sequence or Structural Similarity more info
enables cyclin-dependent protein serine/threonine kinase activity	IBA Inferred from Biological aspect of Ancestor more info
enables cyclin-dependent protein serine/threonine kinase activity	IDA Inferred from Direct Assay more info	PubMed
enables kinase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein kinase activity	TAS Traceable Author Statement more info	PubMed
enables protein kinase binding	IEA Inferred from Electronic Annotation more info
enables protein serine kinase activity	IEA Inferred from Electronic Annotation more info
enables protein serine/threonine kinase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein serine/threonine kinase activity	TAS Traceable Author Statement more info
enables transcription coactivator binding	IPI Inferred from Physical Interaction more info	PubMed
enables transcription elongation factor activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in DNA repair	IEA Inferred from Electronic Annotation more info
involved_in cell population proliferation	TAS Traceable Author Statement more info	PubMed
involved_in cellular response to cytokine stimulus	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of protein localization to chromatin	IDA Inferred from Direct Assay more info	PubMed
involved_in nucleus localization	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation by host of viral transcription	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation by host of viral transcription	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of protein localization to chromatin	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of transcription by RNA polymerase II	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of transcription elongation by RNA polymerase II	IBA Inferred from Biological aspect of Ancestor more info
involved_in positive regulation of transcription elongation by RNA polymerase II	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within protein phosphorylation	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of DNA repair	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of cell cycle	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of mRNA 3'-end processing	IMP Inferred from Mutant Phenotype more info	PubMed
NOT involved_in regulation of mitotic cell cycle	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of muscle cell differentiation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in replication fork processing	IDA Inferred from Direct Assay more info	PubMed
involved_in transcription by RNA polymerase II	IDA Inferred from Direct Assay more info	PubMed
involved_in transcription elongation by RNA polymerase II	IDA Inferred from Direct Assay more info	PubMed
involved_in transcription elongation by RNA polymerase II	TAS Traceable Author Statement more info
involved_in transcription elongation-coupled chromatin remodeling	IDA Inferred from Direct Assay more info	PubMed
involved_in transcription initiation at RNA polymerase II promoter	TAS Traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
part_of P-TEFb complex	IDA Inferred from Direct Assay more info	PubMed
located_in PML body	IDA Inferred from Direct Assay more info	PubMed
part_of cyclin/CDK positive transcription elongation factor complex	IDA Inferred from Direct Assay more info	PubMed
part_of cyclin/CDK positive transcription elongation factor complex	IPI Inferred from Physical Interaction more info	PubMed
located_in cytoplasmic ribonucleoprotein granule	IDA Inferred from Direct Assay more info
located_in membrane	HDA more info	PubMed
located_in nucleoplasm	IDA Inferred from Direct Assay more info
located_in nucleoplasm	TAS Traceable Author Statement more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
is_active_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
part_of transcription elongation factor complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: cyclin-dependent kinase 9

Names: CDC2-related kinase; cell division cycle 2-like protein kinase 4; cell division protein kinase 9; serine/threonine protein kinase PITALRE; tat-associated kinase complex catalytic subunit

NP_001252.1

EC 2.7.11.22

EC 2.7.11.23

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.