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Protein

Cyclin-dependent kinase 7

Gene

CDK7

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

Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. Cyclin-dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between 2 subsequent phases in the cell cycle. Required for both activation and complex formation of CDK1/cyclin-B during G2-M transition, and for activation of CDK2/cyclins during G1-S transition (but not complex formation). CDK7 is the catalytic subunit of the CDK-activating kinase (CAK) complex. Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation, thus regulating cell cycle progression. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Phosphorylation of POLR2A in complex with DNA promotes transcription initiation by triggering dissociation from DNA. Its expression and activity are constant throughout the cell cycle. Upon DNA damage, triggers p53/TP53 activation by phosphorylation, but is inactivated in turn by p53/TP53; this feedback loop may lead to an arrest of the cell cycle and of the transcription, helping in cell recovery, or to apoptosis. Required for DNA-bound peptides-mediated transcription and cellular growth inhibition.14 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

Inactivated by phosphorylation. Repressed by roscovitine (seliciclib, CYC202), R547 (Ro-4584820) and SNS-032 (BMS-387032). The association of p53/TP53 to the CAK complex in response to DNA damage reduces kinase activity toward CDK2 and RNA polymerase II repetitive C-terminal domain (CTD), thus stopping cell cycle progression. The inactivation by roscovitine promotes caspase-mediated apoptosis in leukemic cells.2 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 sitei41ATPPROSITE-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 sitei137Proton acceptorPROSITE-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 bindingi18 – 26ATPPROSITE-ProRule annotation1 Publication9

<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

  • androgen receptor binding Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • cyclin-dependent protein serine/threonine kinase activity Source: GO_Central
  • DNA-dependent ATPase activity Source: UniProtKB
  • kinase activity Source: Reactome
  • protein C-terminus binding Source: UniProtKB
  • protein kinase activity Source: ProtInc
  • protein serine/threonine kinase activity Source: Reactome
  • RNA polymerase II CTD heptapeptide repeat kinase activity Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB

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 processCell cycle, Cell division, DNA 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-113418 Formation of the Early Elongation Complex
R-HSA-167152 Formation of HIV elongation complex in the absence of HIV Tat
R-HSA-167158 Formation of the HIV-1 Early Elongation Complex
R-HSA-167160 RNA Pol II CTD phosphorylation and interaction with CE during HIV infection
R-HSA-167161 HIV Transcription Initiation
R-HSA-167162 RNA Polymerase II HIV Promoter Escape
R-HSA-167172 Transcription of the HIV genome
R-HSA-167200 Formation of HIV-1 elongation complex containing HIV-1 Tat
R-HSA-167246 Tat-mediated elongation of the HIV-1 transcript
R-HSA-427413 NoRC negatively regulates rRNA expression
R-HSA-5696395 Formation of Incision Complex in GG-NER
R-HSA-674695 RNA Polymerase II Pre-transcription Events
R-HSA-6781823 Formation of TC-NER Pre-Incision Complex
R-HSA-6781827 Transcription-Coupled Nucleotide Excision Repair (TC-NER)
R-HSA-6782135 Dual incision in TC-NER
R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-6796648 TP53 Regulates Transcription of DNA Repair Genes
R-HSA-6807505 RNA polymerase II transcribes snRNA genes
R-HSA-69202 Cyclin E associated events during G1/S transition
R-HSA-69231 Cyclin D associated events in G1
R-HSA-69273 Cyclin A/B1/B2 associated events during G2/M transition
R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry
R-HSA-72086 mRNA Capping
R-HSA-73762 RNA Polymerase I Transcription Initiation
R-HSA-73772 RNA Polymerase I Promoter Escape
R-HSA-73776 RNA Polymerase II Promoter Escape
R-HSA-73777 RNA Polymerase I Chain Elongation
R-HSA-73779 RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
R-HSA-73863 RNA Polymerase I Transcription Termination
R-HSA-75953 RNA Polymerase II Transcription Initiation
R-HSA-75955 RNA Polymerase II Transcription Elongation
R-HSA-76042 RNA Polymerase II Transcription Initiation And Promoter Clearance
R-HSA-77075 RNA Pol II CTD phosphorylation and interaction with CE
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs

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

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SignaLinki
P50613

SIGNOR Signaling Network Open Resource

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SIGNORi
P50613

<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 7 (EC:2.7.11.22, EC:2.7.11.23)
Alternative name(s):
39 kDa protein kinase
Short name:
p39 Mo15
CDK-activating kinase 1
Cell division protein kinase 7
Serine/threonine-protein kinase 1
TFIIH basal transcription factor complex kinase 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:CDK7
Synonyms:CAK, CAK1, CDKN7, MO15, STK1
<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 5

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000134058.10

Human Gene Nomenclature Database

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HGNCi
HGNC:1778 CDK7

Online Mendelian Inheritance in Man (OMIM)

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MIMi
601955 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P50613

<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

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>Mutagenesisi41K → A: Total loss of activity. 1
Mutagenesisi91F → G: Enhanced capacity to bind ATP analogs. 1 Publication1
Mutagenesisi164S → A: No mitotic repression of transcriptional activity of the reconstituted TFIIH complex. 1 Publication1
Mutagenesisi170T → A: Total loss of activity. Total loss of transcriptional activity of the reconstituted TFIIH complex. 2 Publications1

Organism-specific databases

DisGeNET

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DisGeNETi
1022

Open Targets

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OpenTargetsi
ENSG00000134058

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA26314

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3055

Drug and drug target database

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DrugBanki
DB03496 Flavopiridol
DB02482 Phosphonothreonine

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1979

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
CDK7

Domain mapping of disease mutations (DMDM)

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DMDMi
1705722

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00000857912 – 346Cyclin-dependent kinase 7Add BLAST345

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 residuei2N-acetylalanineCombined sources1
Modified residuei7PhosphoserineCombined sources1
Modified residuei164Phosphoserine; by CDK1 and CDK2Combined sources2 Publications1
Modified residuei170Phosphothreonine; by CDK2Combined sources3 Publications1
Modified residuei321PhosphoserineCombined 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

Phosphorylation of Ser-164 during mitosis inactivates the enzyme. Phosphorylation of Thr-170 is required for activity. Phosphorylated at Ser-164 and Thr-170 by CDK2.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P50613

MaxQB - The MaxQuant DataBase

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MaxQBi
P50613

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

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PaxDbi
P50613

PeptideAtlas

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PeptideAtlasi
P50613

PRoteomics IDEntifications database

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PRIDEi
P50613

ProteomicsDB human proteome resource

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ProteomicsDBi
56258

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P50613

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

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PhosphoSitePlusi
P50613

<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

Repressed by DNA-bound peptides.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000134058 Expressed in 91 organ(s), highest expression level in testis

CleanEx database of gene expression profiles

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CleanExi
HS_CDK7

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P50613 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P50613 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004364
HPA007932

<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

Associates primarily with cyclin-H (CCNH) and MAT1 to form the CAK complex. CAK can further associate with the core-TFIIH to form the TFIIH basal transcription factor; this complex is sensitive to UV light. The CAK complex binds to p53/TP53 in response to DNA damage. Interacts with CDK2, SF1/NR5A1, PUF60 and PRKCI.8 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
107457, 86 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-578 Cyclin-dependent protein kinase-activating kinase complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P50613

Database of interacting proteins

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DIPi
DIP-5995N

Protein interaction database and analysis system

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IntActi
P50613, 100 interactors

Molecular INTeraction database

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MINTi
P50613

STRING: functional protein association networks

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STRINGi
9606.ENSP00000256443

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P50613

<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

1346
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P50613

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

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SMRi
P50613

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
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P50613

<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>Domaini12 – 295Protein kinasePROSITE-ProRule annotationAdd BLAST284

<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
KOG0659 Eukaryota
ENOG410XQDH LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155179

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
P50613

KEGG Orthology (KO)

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KOi
K02202

Identification of Orthologs from Complete Genome Data

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OMAi
YGAADIK

Database of Orthologous Groups

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OrthoDBi
EOG091G0CI9

Database for complete collections of gene phylogenies

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PhylomeDBi
P50613

TreeFam database of animal gene trees

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TreeFami
TF101024

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR037770 CDK7
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

The PANTHER Classification System

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PANTHERi
PTHR24056:SF0 PTHR24056:SF0, 1 hit

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>Sequence (1+)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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 9 potential isoforms that are computationally mapped.Show allAlign All

P50613-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MALDVKSRAK RYEKLDFLGE GQFATVYKAR DKNTNQIVAI KKIKLGHRSE
60 70 80 90 100
AKDGINRTAL REIKLLQELS HPNIIGLLDA FGHKSNISLV FDFMETDLEV
110 120 130 140 150
IIKDNSLVLT PSHIKAYMLM TLQGLEYLHQ HWILHRDLKP NNLLLDENGV
160 170 180 190 200
LKLADFGLAK SFGSPNRAYT HQVVTRWYRA PELLFGARMY GVGVDMWAVG
210 220 230 240 250
CILAELLLRV PFLPGDSDLD QLTRIFETLG TPTEEQWPDM CSLPDYVTFK
260 270 280 290 300
SFPGIPLHHI FSAAGDDLLD LIQGLFLFNP CARITATQAL KMKYFSNRPG
310 320 330 340
PTPGCQLPRP NCPVETLKEQ SNPALAIKRK RTEALEQGGL PKKLIF
Length:346
Mass (Da):39,038
Last modified:October 1, 1996 - v1
<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:i0A94BFA7DD416CEB
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 are 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D6R9G1D6R9G1_HUMAN
Cyclin-dependent kinase 7
CDK7
253Annotation 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>
D6REC6D6REC6_HUMAN
Cyclin-dependent kinase 7
CDK7
149Annotation 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>
D6RAD4D6RAD4_HUMAN
Cyclin-dependent kinase 7
CDK7
309Annotation 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>
D6RI01D6RI01_HUMAN
Cyclin-dependent kinase 7
CDK7
58Annotation 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>
D6RF14D6RF14_HUMAN
Cyclin-dependent kinase 7
CDK7
69Annotation 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>
D6RGG9D6RGG9_HUMAN
Cyclin-dependent kinase 7
CDK7
55Annotation 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>
D6RIG9D6RIG9_HUMAN
Cyclin-dependent kinase 7
CDK7
77Annotation 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>
D6RFL0D6RFL0_HUMAN
Cyclin-dependent kinase 7 isoform 3
CDK7
43Annotation 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>
D6R9Z2D6R9Z2_HUMAN
Cyclin-dependent kinase 7
CDK7
58Annotation 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 conflicti130Q → R in AAH05298 (PubMed:15489334).Curated1
Sequence conflicti249F → C in CAA73587 (Ref. 5) Curated1
Sequence conflicti321S → A in CAA73587 (Ref. 5) 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_023118163G → A1 Publication1
Natural variantiVAR_023119285T → M2 PublicationsCorresponds to variant dbSNP:rs34584424Ensembl.1

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
X79193 mRNA Translation: CAA55785.1
L20320 mRNA Translation: AAA36657.1
X77743 mRNA Translation: CAA54793.1
X77303 mRNA Translation: CAA54508.1
Y13120 mRNA Translation: CAA73587.1
AY130859 Genomic DNA Translation: AAM77799.1
BC000834 mRNA Translation: AAH00834.1
BC005298 mRNA Translation: AAH05298.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS3999.1

Protein sequence database of the Protein Information Resource

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PIRi
A54820
I37215

NCBI Reference Sequences

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RefSeqi
NP_001310998.1, NM_001324069.1
NP_001310999.1, NM_001324070.1
NP_001311000.1, NM_001324071.1
NP_001311006.1, NM_001324077.1
NP_001790.1, NM_001799.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.184298

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000256443; ENSP00000256443; ENSG00000134058
ENST00000615305; ENSP00000479116; ENSG00000277273

Database of genes from NCBI RefSeq genomes

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GeneIDi
1022

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:1022

UCSC genome browser

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UCSCi
uc003jvs.5 human

Keywords - Coding sequence diversityi

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
X79193 mRNA Translation: CAA55785.1
L20320 mRNA Translation: AAA36657.1
X77743 mRNA Translation: CAA54793.1
X77303 mRNA Translation: CAA54508.1
Y13120 mRNA Translation: CAA73587.1
AY130859 Genomic DNA Translation: AAM77799.1
BC000834 mRNA Translation: AAH00834.1
BC005298 mRNA Translation: AAH05298.1
CCDSiCCDS3999.1
PIRiA54820
I37215
RefSeqiNP_001310998.1, NM_001324069.1
NP_001310999.1, NM_001324070.1
NP_001311000.1, NM_001324071.1
NP_001311006.1, NM_001324077.1
NP_001790.1, NM_001799.3
UniGeneiHs.184298

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
1LG3model-A1-307[»]
1PA8model-A181-346[»]
1UA2X-ray3.02A/B/C/D1-346[»]
2HICmodel-B13-311[»]
ProteinModelPortaliP50613
SMRiP50613
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107457, 86 interactors
ComplexPortaliCPX-578 Cyclin-dependent protein kinase-activating kinase complex
CORUMiP50613
DIPiDIP-5995N
IntActiP50613, 100 interactors
MINTiP50613
STRINGi9606.ENSP00000256443

Chemistry databases

BindingDBiP50613
ChEMBLiCHEMBL3055
DrugBankiDB03496 Flavopiridol
DB02482 Phosphonothreonine
GuidetoPHARMACOLOGYi1979

PTM databases

iPTMnetiP50613
PhosphoSitePlusiP50613

Polymorphism and mutation databases

BioMutaiCDK7
DMDMi1705722

Proteomic databases

EPDiP50613
MaxQBiP50613
PaxDbiP50613
PeptideAtlasiP50613
PRIDEiP50613
ProteomicsDBi56258

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1022
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000256443; ENSP00000256443; ENSG00000134058
ENST00000615305; ENSP00000479116; ENSG00000277273
GeneIDi1022
KEGGihsa:1022
UCSCiuc003jvs.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1022
DisGeNETi1022
EuPathDBiHostDB:ENSG00000134058.10

GeneCards: human genes, protein and diseases

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GeneCardsi
CDK7
HGNCiHGNC:1778 CDK7
HPAiCAB004364
HPA007932
MIMi601955 gene
neXtProtiNX_P50613
OpenTargetsiENSG00000134058
PharmGKBiPA26314

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0659 Eukaryota
ENOG410XQDH LUCA
GeneTreeiENSGT00940000155179
HOGENOMiHOG000233024
HOVERGENiHBG014652
InParanoidiP50613
KOiK02202
OMAiYGAADIK
OrthoDBiEOG091G0CI9
PhylomeDBiP50613
TreeFamiTF101024

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-113418 Formation of the Early Elongation Complex
R-HSA-167152 Formation of HIV elongation complex in the absence of HIV Tat
R-HSA-167158 Formation of the HIV-1 Early Elongation Complex
R-HSA-167160 RNA Pol II CTD phosphorylation and interaction with CE during HIV infection
R-HSA-167161 HIV Transcription Initiation
R-HSA-167162 RNA Polymerase II HIV Promoter Escape
R-HSA-167172 Transcription of the HIV genome
R-HSA-167200 Formation of HIV-1 elongation complex containing HIV-1 Tat
R-HSA-167246 Tat-mediated elongation of the HIV-1 transcript
R-HSA-427413 NoRC negatively regulates rRNA expression
R-HSA-5696395 Formation of Incision Complex in GG-NER
R-HSA-674695 RNA Polymerase II Pre-transcription Events
R-HSA-6781823 Formation of TC-NER Pre-Incision Complex
R-HSA-6781827 Transcription-Coupled Nucleotide Excision Repair (TC-NER)
R-HSA-6782135 Dual incision in TC-NER
R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-6796648 TP53 Regulates Transcription of DNA Repair Genes
R-HSA-6807505 RNA polymerase II transcribes snRNA genes
R-HSA-69202 Cyclin E associated events during G1/S transition
R-HSA-69231 Cyclin D associated events in G1
R-HSA-69273 Cyclin A/B1/B2 associated events during G2/M transition
R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry
R-HSA-72086 mRNA Capping
R-HSA-73762 RNA Polymerase I Transcription Initiation
R-HSA-73772 RNA Polymerase I Promoter Escape
R-HSA-73776 RNA Polymerase II Promoter Escape
R-HSA-73777 RNA Polymerase I Chain Elongation
R-HSA-73779 RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
R-HSA-73863 RNA Polymerase I Transcription Termination
R-HSA-75953 RNA Polymerase II Transcription Initiation
R-HSA-75955 RNA Polymerase II Transcription Elongation
R-HSA-76042 RNA Polymerase II Transcription Initiation And Promoter Clearance
R-HSA-77075 RNA Pol II CTD phosphorylation and interaction with CE
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
SignaLinkiP50613
SIGNORiP50613

Miscellaneous databases

EvolutionaryTraceiP50613

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Cyclin-dependent_kinase_7

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

More...
GenomeRNAii
1022

Protein Ontology

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PROi
PR:P50613

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000134058 Expressed in 91 organ(s), highest expression level in testis
CleanExiHS_CDK7
ExpressionAtlasiP50613 baseline and differential
GenevisibleiP50613 HS

Family and domain databases

InterProiView protein in InterPro
IPR037770 CDK7
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR24056:SF0 PTHR24056:SF0, 1 hit
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 nameiCDK7_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: P50613
Secondary accession number(s): Q9BS60, Q9UE19
<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: October 1, 1996
Last modified: December 5, 2018
This is version 207 of the entry and version 1 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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