Cyclin-dependent kinase 7 - Xenopus laevis (African clawed frog)

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P20911 (CDK7_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	cdk7
Synonyms:	mo15

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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. 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-terminus 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.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
Enzyme regulation	Phosphorylation at Thr-176 is required for enzymatic activity.
Subunit structure	Probably associates with cyclin-H (ccnh) and mat1 to form a multimeric active enzyme.
Subcellular location	Nucleus. Note: In the prominent nucleus of oocytes.
Developmental stage	Expressed only in non-mature oocytes.
Post-translational modification	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. Ref.3
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Meiosis
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW meiosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II carboxy-terminal domain kinase activity Inferred from electronic annotation. Source: EC cyclin-dependent protein serine/threonine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 352

352

Cyclin-dependent kinase 7

PRO_0000085795

Regions

Domain

18 – 301

284

Protein kinase

Nucleotide binding

24 – 32

ATP By similarity

Sites

Active site

143

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

170

Phosphoserine; by CDK1 and CDK2 Ref.3

Modified residue

176

Phosphothreonine; by CDK2 Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P20911 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: C4E21D21509317C4
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FASTA

352

39,691

        10         20         30         40         50         60 
MEGIAARGVD VRSRAKQYEK LDFLGEGQFA TVYKARDKNT DRIVAIKKIK LGHRAEANDG 

        70         80         90        100        110        120 
INRTALREIK LLQELSHPNI IGLLDAFGHK SNISLVFDFM ETDLEVIIKD TSLVLTPAHI 

       130        140        150        160        170        180 
KSYMLMTLQG LEYLHHLWIL HRDLKPNNLL LDENGVLKLA DFGLAKSFGS PNRIYTHQVV 

       190        200        210        220        230        240 
TRWYRSPELL FGARMYGVGV DMWAVGCILA ELLLRVPFLP GDSDLDQLTR IFETLGTPTE 

       250        260        270        280        290        300 
EQWPGMSSLP DYVAFKSFPG TPLHLIFIAA GDDLLELLQG LFTFNPCARC TASQALRKRY 

       310        320        330        340        350 
FSNRPAPTPG NLLPRPNCSI EALKEQQNLN LGIKRKRTEG MDQKDIAKKL SF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X53962 mRNA. Translation: CAA37915.1. BC130134 mRNA. Translation: AAI30135.1.
PIR	S12091.
RefSeq	NP_001084361.1. NM_001090892.1.
UniGene	Xl.15107.
3D structure databases
ProteinModelPortal	P20911.
SMR	P20911. Positions 19-317.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	399461.
KEGG	xla:399461.
Organism-specific databases
CTD	1022.
Xenbase	XB-GENE-485511. cdk7.
Phylogenomic databases
HOVERGEN	HBG014652.
KO	K02202.
Enzyme and pathway databases
BRENDA	2.7.11.22. 6726.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CDK7_XENLA

Accession

Primary (citable) accession number: P20911
Secondary accession number(s): A2BDA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents