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Protein

Cyclin-dependent kinase 9

Gene

CDK9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei48ATPPROSITE-ProRule annotation1 Publication1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei149Proton acceptorPROSITE-ProRule annotation1
Binding sitei167ATPPROSITE-ProRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi25 – 33ATPPROSITE-ProRule annotation9
Nucleotide bindingi104 – 106ATPPROSITE-ProRule annotation1 Publication3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processDNA damage, DNA repair, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.11.22 2681
2.7.11.23 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-112382 Formation of RNA Pol II elongation complex
R-HSA-167152 Formation of HIV elongation complex in the absence of HIV Tat
R-HSA-167200 Formation of HIV-1 elongation complex containing HIV-1 Tat
R-HSA-167238 Pausing and recovery of Tat-mediated HIV elongation
R-HSA-167243 Tat-mediated HIV elongation arrest and recovery
R-HSA-167246 Tat-mediated elongation of the HIV-1 transcript
R-HSA-167287 HIV elongation arrest and recovery
R-HSA-167290 Pausing and recovery of HIV elongation
R-HSA-176034 Interactions of Tat with host cellular proteins
R-HSA-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-HSA-674695 RNA Polymerase II Pre-transcription Events
R-HSA-6796648 TP53 Regulates Transcription of DNA Repair Genes
R-HSA-6807505 RNA polymerase II transcribes snRNA genes
R-HSA-75955 RNA Polymerase II Transcription Elongation
R-HSA-9018519 Estrogen-dependent gene expression

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P50750

SIGNOR Signaling Network Open Resource

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SIGNORi
P50750

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CDK9
Synonyms:CDC2L4, TAK
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000136807.11

Human Gene Nomenclature Database

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HGNCi
HGNC:1780 CDK9

Online Mendelian Inheritance in Man (OMIM)

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MIMi
603251 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P50750

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi44K → R: Impaired kinase and transcriptional elongation activities, but normal cyclin T1 and HEXIM1 binding. 1 Publication1
Mutagenesisi167D → N: Abrogates kinase activity. 2 Publications1
Mutagenesisi175S → A: Constitutive kinase activity. 1 Publication1
Mutagenesisi175S → D: Mimics phosphorylation, constitutive loss of kinase activity. 1 Publication1
Mutagenesisi186T → A: Abrogates autophosphorylation; no effect on kinase activity, but impaired CTD phosphorylation. 3 Publications1
Mutagenesisi186T → D: Mimics autophosphorylation; constitutive kinase activity, independently of calcium signaling. 3 Publications1
Mutagenesisi347 – 357SQITQQSTNQS → AQIAQQAANQA: Loss of autophosphorylation and impaired interaction with HIV TAT. 1 PublicationAdd BLAST11
Mutagenesisi347 – 357SQITQQSTNQS → EQIEQQEENQE: Mimics autophosphorylation and promotes interaction with HIV TAT. 1 PublicationAdd BLAST11

Organism-specific databases

DisGeNET

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DisGeNETi
1025

Open Targets

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OpenTargetsi
ENSG00000136807

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA26316

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3116

Drug and drug target database

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DrugBanki
DB03496 Flavopiridol

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1981

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
CDK9

Domain mapping of disease mutations (DMDM)

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DMDMi
68067660

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000858001 – 372Cyclin-dependent kinase 9Add BLAST372

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei44N6-acetyllysine; by P300/CBP, PCAF/KAT2B and GCN5/KAT2A2 Publications1
Modified residuei48N6-acetyllysine; by PCAF/KAT2B and GCN5/KAT2A1 Publication1
Modified residuei175Phosphoserine1 Publication1
Modified residuei186Phosphothreonine; by CaMK1DCombined sources8 Publications1
Modified residuei347Phosphoserine; by CDK9 and PKACombined sources2 Publications1
Modified residuei350Phosphothreonine; by CDK9Combined sources1 Publication1
Modified residuei353Phosphoserine; by CDK91 Publication1
Modified residuei354Phosphothreonine; by CDK91 Publication1
Modified residuei357Phosphoserine; by CDK91 Publication1
Modified residuei362Phosphothreonine; by CDK91 Publication1
Modified residuei363Phosphothreonine; by CDK91 Publication1
Isoform 2 (identifier: P50750-2)
Modified residuei35PhosphoserineCombined sources1
Modified residuei54PhosphothreonineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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).10 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

Encyclopedia of Proteome Dynamics

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EPDi
P50750

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P50750

MaxQB - The MaxQuant DataBase

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MaxQBi
P50750

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P50750

PeptideAtlas

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PeptideAtlasi
P50750

PRoteomics IDEntifications database

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PRIDEi
P50750

ProteomicsDB human proteome resource

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ProteomicsDBi
56263
56264 [P50750-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P50750

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P50750

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitous.

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000136807 Expressed in 184 organ(s), highest expression level in right ovary

CleanEx database of gene expression profiles

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CleanExi
HS_CDK9

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P50750 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P50750 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004216
HPA006738

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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. Interacts with herpes simplex virus 1 protein ICP22; this interaction inhibits the positive transcription elongation factor b (P-TEFb). Interacts with HSF1 (PubMed:27189267). Interacts with TBX21 (By similarity).By similarity31 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
107459, 291 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-222 Positive transcription elongation factor B, CDK9-cyclinT1 complex
CPX-321 Positive transcription elongation factor B, CDK9-cyclinT2a complex
CPX-322 Positive transcription elongation factor B, CDK9-cyclinT2b complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P50750

Database of interacting proteins

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DIPi
DIP-29016N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P50750

Protein interaction database and analysis system

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IntActi
P50750, 75 interactors

Molecular INTeraction database

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MINTi
P50750

STRING: functional protein association networks

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STRINGi
9606.ENSP00000362361

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P50750

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1372
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB 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[»]
5L1ZX-ray5.90A1-330[»]
6GZHX-ray3.17A1-326[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P50750

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P50750

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P50750

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini19 – 315Protein kinasePROSITE-ProRule annotationAdd BLAST297

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni166 – 191T-loopAdd BLAST26

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0600 Eukaryota
ENOG410XPIR LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155373

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233024

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG014652

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P50750

KEGG Orthology (KO)

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KOi
K02211

Identification of Orthologs from Complete Genome Data

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OMAi
KDPTGCD

Database of Orthologous Groups

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OrthoDBi
594395at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P50750

TreeFam database of animal gene trees

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TreeFami
TF101039

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

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Pfami
View protein in Pfam
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
X6RE90X6RE90_HUMAN
Cyclin-dependent kinase 9
CDK9
194Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti163L → P in AAV38706 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_04198259F → L1 PublicationCorresponds to variant dbSNP:rs55640715Ensembl.1
Natural variantiVAR_013456231G → A2 Publications1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0162881M → MQRDAPPRAPAPAPRLPAPP IGAAASSGGGGGGGSGGGGG GASAAPAPPGLSGTTSPRGP GGGRRAEEAGSAPRGRKWPW RRKWRGRGGAWSAAAAGPGA GAAAAATGGGGGALEAAM in isoform 2. Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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 No translation available.
BC001968 mRNA Translation: AAH01968.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS6879.1 [P50750-1]

Protein sequence database of the Protein Information Resource

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PIRi
A55262

NCBI Reference Sequences

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RefSeqi
NP_001252.1, NM_001261.3 [P50750-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.150423
Hs.706809

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000373264; ENSP00000362361; ENSG00000136807 [P50750-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
1025

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:1025

UCSC genome browser

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UCSCi
uc004bse.3 human [P50750-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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 No translation available.
BC001968 mRNA Translation: AAH01968.1
CCDSiCCDS6879.1 [P50750-1]
PIRiA55262
RefSeqiNP_001252.1, NM_001261.3 [P50750-1]
UniGeneiHs.150423
Hs.706809

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5L1ZX-ray5.90A1-330[»]
6GZHX-ray3.17A1-326[»]
ProteinModelPortaliP50750
SMRiP50750
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107459, 291 interactors
ComplexPortaliCPX-222 Positive transcription elongation factor B, CDK9-cyclinT1 complex
CPX-321 Positive transcription elongation factor B, CDK9-cyclinT2a complex
CPX-322 Positive transcription elongation factor B, CDK9-cyclinT2b complex
CORUMiP50750
DIPiDIP-29016N
ELMiP50750
IntActiP50750, 75 interactors
MINTiP50750
STRINGi9606.ENSP00000362361

Chemistry databases

BindingDBiP50750
ChEMBLiCHEMBL3116
DrugBankiDB03496 Flavopiridol
GuidetoPHARMACOLOGYi1981

PTM databases

iPTMnetiP50750
PhosphoSitePlusiP50750

Polymorphism and mutation databases

BioMutaiCDK9
DMDMi68067660

Proteomic databases

EPDiP50750
jPOSTiP50750
MaxQBiP50750
PaxDbiP50750
PeptideAtlasiP50750
PRIDEiP50750
ProteomicsDBi56263
56264 [P50750-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1025
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373264; ENSP00000362361; ENSG00000136807 [P50750-1]
GeneIDi1025
KEGGihsa:1025
UCSCiuc004bse.3 human [P50750-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1025
DisGeNETi1025
EuPathDBiHostDB:ENSG00000136807.11

GeneCards: human genes, protein and diseases

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GeneCardsi
CDK9
HGNCiHGNC:1780 CDK9
HPAiCAB004216
HPA006738
MIMi603251 gene
neXtProtiNX_P50750
OpenTargetsiENSG00000136807
PharmGKBiPA26316

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0600 Eukaryota
ENOG410XPIR LUCA
GeneTreeiENSGT00940000155373
HOGENOMiHOG000233024
HOVERGENiHBG014652
InParanoidiP50750
KOiK02211
OMAiKDPTGCD
OrthoDBi594395at2759
PhylomeDBiP50750
TreeFamiTF101039

Enzyme and pathway databases

BRENDAi2.7.11.22 2681
2.7.11.23 2681
ReactomeiR-HSA-112382 Formation of RNA Pol II elongation complex
R-HSA-167152 Formation of HIV elongation complex in the absence of HIV Tat
R-HSA-167200 Formation of HIV-1 elongation complex containing HIV-1 Tat
R-HSA-167238 Pausing and recovery of Tat-mediated HIV elongation
R-HSA-167243 Tat-mediated HIV elongation arrest and recovery
R-HSA-167246 Tat-mediated elongation of the HIV-1 transcript
R-HSA-167287 HIV elongation arrest and recovery
R-HSA-167290 Pausing and recovery of HIV elongation
R-HSA-176034 Interactions of Tat with host cellular proteins
R-HSA-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-HSA-674695 RNA Polymerase II Pre-transcription Events
R-HSA-6796648 TP53 Regulates Transcription of DNA Repair Genes
R-HSA-6807505 RNA polymerase II transcribes snRNA genes
R-HSA-75955 RNA Polymerase II Transcription Elongation
R-HSA-9018519 Estrogen-dependent gene expression
SignaLinkiP50750
SIGNORiP50750

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
CDK9 human
EvolutionaryTraceiP50750

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
CDK9
Cyclin-dependent_kinase_9

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
1025

Protein Ontology

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PROi
PR:P50750

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000136807 Expressed in 184 organ(s), highest expression level in right ovary
CleanExiHS_CDK9
ExpressionAtlasiP50750 baseline and differential
GenevisibleiP50750 HS

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCDK9_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P50750
Secondary accession number(s): Q5JU24
, Q5JU25, Q5U006, Q96TF1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 21, 2005
Last modified: January 16, 2019
This is version 213 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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