CDK7_XENLA
ID CDK7_XENLA Reviewed; 352 AA.
AC P20911; A2BDA1;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Cyclin-dependent kinase 7;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
DE AltName: Full=40 kDa protein kinase;
DE AltName: Full=CDC2/CDK2,4-activating kinase;
DE AltName: Full=Cell division protein kinase 7;
DE AltName: Full=P40 MO15;
GN Name=cdk7; Synonyms=mo15;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RX PubMed=2209545; DOI=10.1002/j.1460-2075.1990.tb07522.x;
RA Shuttleworth J., Godfrey R., Colman A.;
RT "p40MO15, a cdc2-related protein kinase involved in negative regulation of
RT meiotic maturation of Xenopus oocytes.";
RL EMBO J. 9:3233-3240(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION AT SER-170 AND THR-176, AND INTERACTION WITH CCNH.
RC TISSUE=Oocyte;
RX PubMed=7957080; DOI=10.1002/j.1460-2075.1994.tb06845.x;
RA Labbe J.-C., Martinez A.-M., Fesquet D., Capony J.-P., Darbon J.-M.,
RA Derancourt J., Devault A., Morin N., Cavadore J.-C., Doree M.;
RT "p40MO15 associates with a p36 subunit and requires both nuclear
RT translocation and Thr176 phosphorylation to generate cdk-activating kinase
RT activity in Xenopus oocytes.";
RL EMBO J. 13:5155-5164(1994).
CC -!- FUNCTION: Serine/threonine kinase involved in cell cycle control and in
CC RNA polymerase II-mediated RNA transcription. Cyclin-dependent kinases
CC (CDKs) are activated by the binding to a cyclin and mediate the
CC progression through the cell cycle. Each different complex controls a
CC specific transition between 2 subsequent phases in the cell cycle.
CC Required for both activation and complex formation of cdk1/cyclin-B
CC during G2-M transition, and for activation of cdk2/cyclins during G1-S
CC transition (but not complex formation). cdk7 is the catalytic subunit
CC of the CDK-activating kinase (CAK) complex. CAK activates the cyclin-
CC associated kinases cdk1, cdk2, cdk4 and cdk6 by threonine
CC phosphorylation, thus regulating cell cycle progression. CAK complexed
CC to the core-TFIIH basal transcription factor activates RNA polymerase
CC II by serine phosphorylation of the repetitive C-terminal domain (CTD)
CC of its large subunit (polr2a), allowing its escape from the promoter
CC and elongation of the transcripts (By similarity). Involved in negative
CC regulation of the meiotic maturation of Xenopus oocytes. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.22;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC ChEBI:CHEBI:456216; EC=2.7.11.23;
CC -!- ACTIVITY REGULATION: Phosphorylation at Thr-176 is required for
CC enzymatic activity.
CC -!- SUBUNIT: Probably associates with cyclin-H (ccnh) and mat1 to form a
CC multimeric active enzyme.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=In the prominent nucleus of
CC oocytes.
CC -!- DEVELOPMENTAL STAGE: Expressed only in non-mature oocytes.
CC -!- PTM: Phosphorylation of Ser-170 during mitosis inactivates the enzyme.
CC Phosphorylation of Thr-176 is required for activity. Phosphorylated at
CC Ser-170 and Thr-176 by CDK2 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; X53962; CAA37915.1; -; mRNA.
DR EMBL; BC130134; AAI30135.1; -; mRNA.
DR PIR; S12091; S12091.
DR RefSeq; NP_001084361.1; NM_001090892.1.
DR AlphaFoldDB; P20911; -.
DR SMR; P20911; -.
DR BioGRID; 100785; 3.
DR iPTMnet; P20911; -.
DR DNASU; 399461; -.
DR GeneID; 399461; -.
DR KEGG; xla:399461; -.
DR CTD; 399461; -.
DR Xenbase; XB-GENE-485511; cdk7.L.
DR OrthoDB; 1367115at2759; -.
DR BRENDA; 2.7.11.22; 6725.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 399461; Expressed in oocyte and 19 other tissues.
DR GO; GO:0070985; C:transcription factor TFIIK complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd07841; STKc_CDK7; 1.
DR InterPro; IPR037770; CDK7.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24056:SF375; PTHR24056:SF375; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Kinase; Meiosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..352
FT /note="Cyclin-dependent kinase 7"
FT /id="PRO_0000085795"
FT DOMAIN 18..301
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 24..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 170
FT /note="Phosphoserine; by CDK1 and CDK2"
FT /evidence="ECO:0000269|PubMed:7957080"
FT MOD_RES 176
FT /note="Phosphothreonine; by CDK2"
FT /evidence="ECO:0000269|PubMed:7957080"
SQ SEQUENCE 352 AA; 39691 MW; C4E21D21509317C4 CRC64;
MEGIAARGVD VRSRAKQYEK LDFLGEGQFA TVYKARDKNT DRIVAIKKIK LGHRAEANDG
INRTALREIK LLQELSHPNI IGLLDAFGHK SNISLVFDFM ETDLEVIIKD TSLVLTPAHI
KSYMLMTLQG LEYLHHLWIL HRDLKPNNLL LDENGVLKLA DFGLAKSFGS PNRIYTHQVV
TRWYRSPELL FGARMYGVGV DMWAVGCILA ELLLRVPFLP GDSDLDQLTR IFETLGTPTE
EQWPGMSSLP DYVAFKSFPG TPLHLIFIAA GDDLLELLQG LFTFNPCARC TASQALRKRY
FSNRPAPTPG NLLPRPNCSI EALKEQQNLN LGIKRKRTEG MDQKDIAKKL SF
