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P20911

- CDK7_XENLA

UniProt

P20911 - CDK7_XENLA

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Protein

Cyclin-dependent kinase 7

Gene

cdk7

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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. 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 (By similarity). Involved in negative regulation of the meiotic maturation of Xenopus oocytes.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-176 is required for enzymatic activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei47 – 471ATPPROSITE-ProRule annotation
Active sitei143 – 1431Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi24 – 329ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
  3. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. meiotic nuclear division Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Meiosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.22. 6726.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 7 (EC:2.7.11.22, EC:2.7.11.23)
Alternative name(s):
40 kDa protein kinase
CDC2/CDK2,4-activating kinase
Cell division protein kinase 7
P40 MO15
Gene namesi
Name:cdk7
Synonyms:mo15
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-485511. cdk7.

Subcellular locationi

Nucleus
Note: In the prominent nucleus of oocytes.

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352Cyclin-dependent kinase 7PRO_0000085795Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei170 – 1701Phosphoserine; by CDK1 and CDK21 Publication
Modified residuei176 – 1761Phosphothreonine; by CDK21 Publication

Post-translational modificationi

Phosphorylation of Ser-170 during mitosis inactivates the enzyme. Phosphorylation of Thr-176 is required for activity. Phosphorylated at Ser-170 and Thr-176 by CDK2 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Expressioni

Developmental stagei

Expressed only in non-mature oocytes.

Interactioni

Subunit structurei

Probably associates with cyclin-H (ccnh) and mat1 to form a multimeric active enzyme.

Protein-protein interaction databases

BioGridi100785. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliP20911.
SMRiP20911. Positions 19-317.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 301284Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG014652.
KOiK02202.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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: Complete.

P20911-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEGIAARGVD VRSRAKQYEK LDFLGEGQFA TVYKARDKNT DRIVAIKKIK
60 70 80 90 100
LGHRAEANDG INRTALREIK LLQELSHPNI IGLLDAFGHK SNISLVFDFM
110 120 130 140 150
ETDLEVIIKD TSLVLTPAHI KSYMLMTLQG LEYLHHLWIL HRDLKPNNLL
160 170 180 190 200
LDENGVLKLA DFGLAKSFGS PNRIYTHQVV TRWYRSPELL FGARMYGVGV
210 220 230 240 250
DMWAVGCILA ELLLRVPFLP GDSDLDQLTR IFETLGTPTE EQWPGMSSLP
260 270 280 290 300
DYVAFKSFPG TPLHLIFIAA GDDLLELLQG LFTFNPCARC TASQALRKRY
310 320 330 340 350
FSNRPAPTPG NLLPRPNCSI EALKEQQNLN LGIKRKRTEG MDQKDIAKKL

SF
Length:352
Mass (Da):39,691
Last modified:February 1, 1991 - v1
Checksum:iC4E21D21509317C4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53962 mRNA. Translation: CAA37915.1.
BC130134 mRNA. Translation: AAI30135.1.
PIRiS12091.
RefSeqiNP_001084361.1. NM_001090892.1.
UniGeneiXl.15107.

Genome annotation databases

GeneIDi399461.
KEGGixla:399461.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53962 mRNA. Translation: CAA37915.1 .
BC130134 mRNA. Translation: AAI30135.1 .
PIRi S12091.
RefSeqi NP_001084361.1. NM_001090892.1.
UniGenei Xl.15107.

3D structure databases

ProteinModelPortali P20911.
SMRi P20911. Positions 19-317.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 100785. 3 interactions.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 399461.
KEGGi xla:399461.

Organism-specific databases

CTDi 1022.
Xenbasei XB-GENE-485511. cdk7.

Phylogenomic databases

HOVERGENi HBG014652.
KOi K02202.

Enzyme and pathway databases

BRENDAi 2.7.11.22. 6726.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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

« Hide 'large scale' publications
  1. "p40MO15, a cdc2-related protein kinase involved in negative regulation of meiotic maturation of Xenopus oocytes."
    Shuttleworth J., Godfrey R., Colman A.
    EMBO J. 9:3233-3240(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Oocyte.
  2. NIH - Xenopus Gene Collection (XGC) project
    Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.
  3. "p40MO15 associates with a p36 subunit and requires both nuclear translocation and Thr176 phosphorylation to generate cdk-activating kinase activity in Xenopus oocytes."
    Labbe J.-C., Martinez A.-M., Fesquet D., Capony J.-P., Darbon J.-M., Derancourt J., Devault A., Morin N., Cavadore J.-C., Doree M.
    EMBO J. 13:5155-5164(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-170 AND THR-176, INTERACTION WITH CCNH.
    Tissue: Oocyte.

Entry informationi

Entry nameiCDK7_XENLA
AccessioniPrimary (citable) accession number: P20911
Secondary accession number(s): A2BDA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: October 29, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3