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P51952 (CDK7_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-dependent kinase 7

EC=2.7.11.22
EC=2.7.11.23
Alternative name(s):
39 protein kinase
Short name=P39 Mo15
CDK-activating kinase 1
Cell division protein kinase 7
TFIIH basal transcription factor complex kinase subunit
Gene names
Name:Cdk7
Synonyms:Cak, Cak1, Mo15
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length329 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

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

Enzyme regulation

Phosphorylation at Thr-162 is required for enzymatic activity. 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 By similarity.

Subunit structure

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 By similarity.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Note: Colocalizes with PRKCI in the cytoplasm and nucleus. Translocates from the nucleus to cytoplasm and perinuclear region in response to DNA-bound peptides By similarity.

Post-translational modification

Phosphorylation of Ser-156 during mitosis inactivates the enzyme. Phosphorylation of Thr-162 is required for activity. Phosphorylated at Ser-156 and Thr-162 by CDK2 By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Sequence caution

The sequence CAA58562.1 differs from that shown. Reason: Erroneous termination at position 313. Translated as Ser.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
DNA repair
Meiosis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from sequence or structural similarity. Source: GOC

DNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

meiotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

protein phosphorylation

Inferred from direct assay PubMed 8906616. Source: RGD

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcyclin-dependent protein kinase holoenzyme complex

Traceable author statement PubMed 8906616. Source: RGD

cytoskeleton

Inferred from direct assay PubMed 15886195. Source: RGD

cytosol

Inferred from direct assay PubMed 15886195. Source: RGD

holo TFIIH complex

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from direct assay PubMed 15886195. Source: RGD

nucleus

Inferred from direct assay PubMed 15886195. Source: RGD

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-dependent ATPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay PubMed 8906616. Source: RGD

protein complex binding

Inferred from direct assay PubMed 7885450PubMed 9891058. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›329›329Cyclin-dependent kinase 7
PRO_0000085793

Regions

Domain4 – 287284Protein kinase
Nucleotide binding10 – 189ATP By similarity

Sites

Active site1291Proton acceptor By similarity
Binding site331ATP By similarity

Amino acid modifications

Modified residue1561Phosphoserine; by CDK1 and CDK2 By similarity
Modified residue1621Phosphothreonine; by CDK2 By similarity
Modified residue3131Phosphoserine By similarity

Experimental info

Non-terminal residue11
Non-terminal residue3291

Sequences

Sequence LengthMass (Da)Tools
P51952 [UniParc].

Last modified May 10, 2005. Version 2.
Checksum: B7159FD074881B0F

FASTA32937,141
        10         20         30         40         50         60 
ANRNEKLDFL GEGQFATVYK ARDKNTNQIV AIKKIKLGHR SEAKDGINRT ALREIKLLQE 

        70         80         90        100        110        120 
LSHPNIIGLL DAFGHKSNIS LVFDFMETDL EVIIKDNSLV LTPSHIKAYM LMTLQGLEYL 

       130        140        150        160        170        180 
HQHWILHRDL KPNNLLLDEN GVLKLADFGL AKSFGSPNWA YTHQVVTRWY RAPELLFGAR 

       190        200        210        220        230        240 
MYGVGVDMWA VGCILAELLL RVPFLPGDSD LDQLTRIFET LGTPTEEQWP DMCSLPDYVT 

       250        260        270        280        290        300 
FKSFPGIPLQ HIFIAAGDDL LELIQGLFLF NPCTRITASQ ALRTKYFSNR PGPTPGCQLP 

       310        320 
RPNCPVEALK EQSNPAMATK RKRAEALEQ 

« Hide

References

[1]Wu L., Hall F.
Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83579 mRNA. Translation: CAA58562.1. Sequence problems.
PIRS51085.
UniGeneRn.98896.

3D structure databases

ProteinModelPortalP51952.
SMRP51952. Positions 5-303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000025026.

PTM databases

PhosphoSiteP51952.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:621124. rat.

Organism-specific databases

RGD621124. Cdk7.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
HOVERGENHBG014652.
InParanoidP51952.
PhylomeDBP51952.

Gene expression databases

GenevestigatorP51952.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP51952.

Entry information

Entry nameCDK7_RAT
AccessionPrimary (citable) accession number: P51952
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 10, 2005
Last modified: May 14, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families