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CDK9 (human)

Overview CDK9 a protein kinase of the CDK family. Forms a complex with and is regulated by its regulatory subunit cyclin T or cyclin K. 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. Transcriptional elongation factor and cofactor for HIV Tat protein; RNAi blocks HIV replication, and inhibitors also block varicella zoster replication. Mediates signals leading to cardiac hypertrophy. Inhibitor: Flavopiridol. Note: This description may include information from UniProtKB. Protein type: EC 2.7.11.22; Kinase, protein; Nuclear receptor co-regulator; Protein kinase, CMGC; Protein kinase, Ser/Thr (non-receptor); EC 2.7.11.23; CMGC group; CDK family; CDK9 subfamily; CDK/CDK9 subfamily Cellular Component: nucleoplasm; transcription elongation factor complex; PML body; intracellular membrane-bound organelle; cytoplasm; nucleolus; nucleus Molecular Function: RNA polymerase subunit kinase activity; identical protein binding; protein binding; snRNA binding; DNA binding; cyclin-dependent protein kinase activity; ATP binding; protein kinase activity Biological Process: transcription from RNA polymerase II promoter; regulation of histone modification; transcription initiation from RNA polymerase II promoter; transcription, DNA-dependent; viral reproduction; positive regulation of viral transcription; cell cycle; DNA repair; protein amino acid phosphorylation; regulation of DNA repair; cell proliferation; transforming growth factor beta receptor signaling pathway; RNA elongation from RNA polymerase II promoter; gene expression; replication fork arrest; positive regulation of transcription from RNA polymerase II promoter Reference #:  P50750 (UniProtKB) Alt. Names/Synonyms: C-2K; CDC2-related kinase; CDC2L4; CDK9; Cell division cycle 2-like protein kinase 4; Cell division protein kinase 9; CTK1; Cyclin-dependent kinase 9; PITALRE; PTEFB; serine/threonine protein kinase PITALRE; Serine/threonine-protein kinase PITALRE; TAK Gene Symbols: CDK9 Molecular weight: 42,778 Da Basal Isoelectric point: 8.97  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below CDK9 1PF6 - A=1-372 (human) 3BLH - A=2-330 (human) 3BLQ - A=2-330 (human) 3BLR - A=2-330 (human) 3LQ5 - A=2-330 (human) 3MI9 - A=1-345 (human) 3MIA - A=1-345 (human) 3MY1 - A=2-330 (human) 3TN8 - A=2-330 (human) 3TNH - A=2-330 (human) 3TNI - A=2-330 (human) 4BCF - B=2-259 (human) 4BCG - B=2-259 (human) 4BCH - B=2-259 (human) 4BCI - B=2-259 (human) 4BCJ - B=2-259 (human) 4EC8 - B=2-259 (human) 4EC9 - B=2-259 (human) 4IMY - H/I/G=2-73 (human) Substrate Sequence Logo

STRING  |  Scansite  |  KinBase  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1PF6 3BLH 3BLQ 3BLR 3LQ5 3MI9 3MIA 3MY1 3TN8 3TNH 3TNI 4BCF 4BCG 4BCH 4BCI 4BCJ 4EC8 4EC9 4IMY  |  ENZYME 2.7.11.22 2.7.11.23  |  Phospho3D  |  DISEASE  |  Source  |  NURSA  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Sites Implicated In
transcription, altered: S175‑p, T186‑p enzymatic activity, induced: S175‑p, T186‑p enzymatic activity, inhibited: S175‑p molecular association, regulation: S175‑p, T186‑p, S347‑p protein stabilization: T186‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human ► Hide Isoforms
0	1		-	gap
0	2		-	gap
0	1		-	gap
0	1		-	gap
0	2		-	gap
0	1		K24-u	SKYEKLAkIGQGTFG
0	7		K35-u	GTFGEVFkARHRKTG
2	0		K44-a	RHRKTGQkVALKkVL
1	0		K49-a	GQkVALKkVLMENEk
0	1		K56-u	kVLMENEkEGFPITA
0	3		K68-u	ITALREIkILQLLKH
0	2		K88-u	LIEICRTkASPYNRC
0	1		R148	HRNKILHRDMkAANV
0	1		K151-u	KILHRDMkAANVLIT
0	7		K164-u	ITRDGVLkLADFGLA
2	1		S175-p	FGLARAFsLAkNSQP
0	5		K178-u	ARAFsLAkNSQPNRy
0	1		Y185-p	kNSQPNRytNRVVTL
10	18		T186-p	NSQPNRytNRVVTLW
0	1		Y194-p	NRVVTLWyRPPELLL
0	1		K264	DNYELYEKLELVkGQ
0	1		K269-u	YEKLELVkGQKRkVk
0	3		K274-a	LVkGQKRkVkDRLKA
0	3		K276-a	kGQKRkVkDRLKAYV
0	1		Y287-p	KAYVRDPyALDLIDk
0	8		K294-u	yALDLIDkLLVLDPA
0	4		Y338-p	HLTSMFEyLAPPRRk
0	3		K345-u	yLAPPRRkGsQItQQ
2	75		S347-p	APPRRkGsQItQQst
0	3		T350-p	RRkGsQItQQstNQs
1	2		S353-p	GsQItQQstNQsRNP
1	0		T354-p	sQItQQstNQsRNPA
0	2		S357-p	tQQstNQsRNPAttN
1	0		T362-p	NQsRNPAttNQtEFE
1	0		T363-p	QsRNPAttNQtEFER
0	1		T366-p	NPAttNQtEFERVF_

	CDK9 iso2
S27-p	PIGAAASsGGGGGGG
S35-p	GGGGGGGsGGGGGGA
S52-p	APAPPGLsGtTsPRG
T54-p	APPGLsGtTsPRGPG
S56-p	PGLsGtTsPRGPGGG
K141	SKYEKLAKIGQGTFG
K152	GTFGEVFKARHRKTG
K161	RHRKTGQKVALKKVL
K166	GQKVALKKVLMENEK
K173	KVLMENEKEGFPITA
K185	ITALREIKILQLLKH
K205	LIEICRTKASPYNRC
R265	HRNKILHRDMKAANV
K268	KILHRDMKAANVLIT
K281	ITRDGVLKLADFGLA
S292	FGLARAFSLAKNSQP
K295	ARAFSLAKNSQPNRY
Y302	KNSQPNRYTNRVVTL
T303	NSQPNRYTNRVVTLW
Y311	NRVVTLWYRPPELLL
K381	DNYELYEKLELVKGQ
K386	YEKLELVKGQKRkVk
K391-a	LVKGQKRkVkDRLKA
K393-a	KGQKRkVkDRLKAYV
Y404	KAYVRDPYALDLIDK
K411	YALDLIDKLLVLDPA
Y455	HLTSMFEYLAPPRRK
K462	YLAPPRRKGSQITQQ
S464	APPRRKGSQITQQST
T467	RRKGSQITQQSTNQS
S470	GSQITQQSTNQSRNP
T471	SQITQQSTNQSRNPA
S474	TQQSTNQSRNPATTN
T479	NQSRNPATTNQTEFE
T480	QSRNPATTNQTEFER
T483	NPATTNQTEFERVF_

	mouse
-	gap
-	gap
-	gap
-	gap
-	gap
K24	TKYEKLAKIGQGTFG
K35	GTFGEVFKAKHRQTG
K44	KHRQTGQKVALKKVL
K49	GQKVALKKVLMENEK
K56	KVLMENEKEGFPITA
K68-u	ITALREIkILQLLKH
K88	LIEICRTKASPYNRC
R148-m2	HRNKILHrDMKAANV
K151	KILHrDMKAANVLIT
K164-u	ITRDGVLkLADFGLA
S175	FGLARAFSLAkNSQP
K178-u	ARAFSLAkNSQPNRY
Y185	kNSQPNRYtNRVVTL
T186-p	NSQPNRYtNRVVTLW
Y194	NRVVTLWYRPPELLL
K264-u	DKYELFEkLELVKGQ
K269	FEkLELVKGQKRKVK
K274	LVKGQKRKVKDRLKA
K276	KGQKRKVKDRLKAYV
Y287-p	KAYVRDPyALDLIDK
K294	yALDLIDKLLVLDPA
Y338	HLTSMFEYLAPPRRK
K345	YLAPPRRKGsQITQQ
S347-p	APPRRKGsQITQQST
T350	RRKGsQITQQSTNQS
S353	GsQITQQSTNQSRNP
T354	sQITQQSTNQSRNPA
S357	TQQSTNQSRNPATTN
T362	NQSRNPATTNQTEFE
T363	QSRNPATTNQTEFER
T366	NPATTNQTEFERVF_

	rat
-	gap
-	gap
-	gap
-	gap
-	gap
K24	TKYEKLAKIGQGTFG
K35	GTFGEVFKAKHRQTG
K44	KHRQTGQKVALKKVL
K49	GQKVALKKVLMENEK
K56	KVLMENEKEGFPITA
K68	ITALREIKILQLLKH
K88	LIEICRTKASPYNRC
R148	HRNKILHRDMKAANV
K151	KILHRDMKAANVLIT
K164	ITRDGVLKLADFGLA
S175	FGLARAFSLAKNSQP
K178	ARAFSLAKNSQPNRY
Y185	KNSQPNRYTNRVVTL
T186	NSQPNRYTNRVVTLW
Y194	NRVVTLWYRPPELLL
K264	DKYELFEKLELVKGQ
K269	FEKLELVKGQKRKVK
K274	LVKGQKRKVKDRLKA
K276	KGQKRKVKDRLKAYV
Y287	KAYVRDPYALDLIDK
K294	YALDLIDKLLVLDPA
Y338	HLTSMFEYLAPPRRK
K345	YLAPPRRKGsQITQQ
S347-p	APPRRKGsQITQQST
T350	RRKGsQITQQSTNQS
S353	GsQITQQSTNQSRNP
T354	sQITQQSTNQSRNPA
S357	TQQSTNQSRNPATTN
T362	NQSRNPATTNQTEFE
T363	QSRNPATTNQTEFER
T366	NPATTNQTEFERVF_

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