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P51952

- CDK7_RAT

UniProt

P51952 - CDK7_RAT

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Protein

Cyclin-dependent kinase 7

Gene
Cdk7, Cak, Cak1, Mo15
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

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 By similarity.

Catalytic activityi

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

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331ATP By similarity
Active sitei129 – 1291Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 189ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein serine/threonine kinase activity Source: RGD
  3. DNA-dependent ATPase activity Source: UniProtKB
  4. protein complex binding Source: RGD
  5. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. DNA repair Source: UniProtKB-KW
  3. meiotic nuclear division Source: UniProtKB-KW
  4. protein phosphorylation Source: RGD
  5. regulation of transcription, DNA-templated Source: UniProtKB-KW
  6. transcription from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA repair, Meiosis, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Cdk7
Synonyms:Cak, Cak1, Mo15
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621124. Cdk7.

Subcellular locationi

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.

GO - Cellular componenti

  1. cyclin-dependent protein kinase holoenzyme complex Source: RGD
  2. cytoskeleton Source: RGD
  3. cytosol Source: RGD
  4. holo TFIIH complex Source: UniProtKB
  5. membrane Source: RGD
  6. nucleus Source: RGD
  7. perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›329›329Cyclin-dependent kinase 7PRO_0000085793Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei156 – 1561Phosphoserine; by CDK1 and CDK2 By similarity
Modified residuei162 – 1621Phosphothreonine; by CDK2 By similarity
Modified residuei313 – 3131Phosphoserine By similarity

Post-translational modificationi

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.

Keywords - PTMi

Phosphoprotein

PTM databases

PhosphoSiteiP51952.

Expressioni

Gene expression databases

GenevestigatoriP51952.

Interactioni

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 By similarity.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025026.

Structurei

3D structure databases

ProteinModelPortaliP51952.
SMRiP51952. Positions 5-303.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 287284Protein kinaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP51952.
PhylomeDBiP51952.

Family and domain databases

InterProiIPR011009. 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]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P51952-1 [UniParc]FASTAAdd to Basket

« Hide

ANRNEKLDFL GEGQFATVYK ARDKNTNQIV AIKKIKLGHR SEAKDGINRT    50
ALREIKLLQE LSHPNIIGLL DAFGHKSNIS LVFDFMETDL EVIIKDNSLV 100
LTPSHIKAYM LMTLQGLEYL HQHWILHRDL KPNNLLLDEN GVLKLADFGL 150
AKSFGSPNWA YTHQVVTRWY RAPELLFGAR MYGVGVDMWA VGCILAELLL 200
RVPFLPGDSD LDQLTRIFET LGTPTEEQWP DMCSLPDYVT FKSFPGIPLQ 250
HIFIAAGDDL LELIQGLFLF NPCTRITASQ ALRTKYFSNR PGPTPGCQLP 300
RPNCPVEALK EQSNPAMATK RKRAEALEQ 329
Length:329
Mass (Da):37,141
Last modified:May 10, 2005 - v2
Checksum:iB7159FD074881B0F
GO

Sequence cautioni

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

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei329 – 3291

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83579 mRNA. Translation: CAA58562.1. Sequence problems.
PIRiS51085.
UniGeneiRn.98896.

Genome annotation databases

UCSCiRGD:621124. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83579 mRNA. Translation: CAA58562.1 . Sequence problems.
PIRi S51085.
UniGenei Rn.98896.

3D structure databases

ProteinModelPortali P51952.
SMRi P51952. Positions 5-303.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000025026.

PTM databases

PhosphoSitei P51952.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:621124. rat.

Organism-specific databases

RGDi 621124. Cdk7.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233024.
HOVERGENi HBG014652.
InParanoidi P51952.
PhylomeDBi P51952.

Miscellaneous databases

PROi P51952.

Gene expression databases

Genevestigatori P51952.

Family and domain databases

InterProi IPR011009. 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 ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

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

Entry informationi

Entry nameiCDK7_RAT
AccessioniPrimary (citable) accession number: P51952
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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