CDK9_XENTR
ID CDK9_XENTR Reviewed; 376 AA.
AC Q6GLD8; Q28F30;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Cyclin-dependent kinase 9;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
DE AltName: Full=Cell division protein kinase 9;
GN Name=cdk9; ORFNames=TGas123e01.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Member of the cyclin-dependent kinase pair (CDK9/cyclin-T)
CC complex, also called positive transcription elongation factor B (P-
CC TEFb), which is proposed to facilitate the transition from abortive to
CC production elongation by phosphorylating the CTD (C-terminal domain) of
CC the large subunit of RNA polymerase II (RNAP II) and SUPT5H.
CC {ECO:0000250|UniProtKB:P50750}.
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 Evidence={ECO:0000250|UniProtKB:P50750};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000250|UniProtKB:P50750};
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; Evidence={ECO:0000250|UniProtKB:P50750};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000250|UniProtKB:P50750};
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 Evidence={ECO:0000250|UniProtKB:P50750};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10217;
CC Evidence={ECO:0000250|UniProtKB:P50750};
CC -!- SUBUNIT: Associates with cyclin-T to form P-TEFb. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {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; CR762201; CAJ82512.1; -; mRNA.
DR EMBL; BC074560; AAH74560.1; -; mRNA.
DR RefSeq; NP_001005448.1; NM_001005448.1.
DR AlphaFoldDB; Q6GLD8; -.
DR SMR; Q6GLD8; -.
DR STRING; 8364.ENSXETP00000031527; -.
DR PaxDb; Q6GLD8; -.
DR DNASU; 448039; -.
DR GeneID; 448039; -.
DR KEGG; xtr:448039; -.
DR CTD; 1025; -.
DR Xenbase; XB-GENE-483721; cdk9.
DR eggNOG; KOG0669; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q6GLD8; -.
DR OMA; KARCKST; -.
DR OrthoDB; 925637at2759; -.
DR TreeFam; TF101039; -.
DR Reactome; R-XTR-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-XTR-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-XTR-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-XTR-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-XTR-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-XTR-9018519; Estrogen-dependent gene expression.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000024742; Expressed in gastrula and 15 other tissues.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; ISS:UniProtKB.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; ISS:UniProtKB.
DR GO; GO:0120187; P:positive regulation of protein localization to chromatin; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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 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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..376
FT /note="Cyclin-dependent kinase 9"
FT /id="PRO_0000085806"
FT DOMAIN 19..319
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 345..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 25..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 376 AA; 43273 MW; 7C2E6045CDBEF5E4 CRC64;
MAKNYDSVEF PYCDEVSKYE RLAKIGQGTF GEVFKAKHRQ TGKKVALKKV LMENEKEGFP
ITALREIKIL QLLKHENVVN LIEICRTKIS PTANQYNRCK GTIFLVFDFC EHDLAGLLSN
AHVKFTLSEI KKVMQMLLNG LYYIHRNKIL HRDMKAANVL ITRDGVLKLA DFGLARAFSL
AKNSQPNKYT NRVVTLWYRP PELLLGERDY GPPIDLWGAG CIMAEMWTRS PIMQGNTEQH
QLTLISQLCG SITPEVWPNV DKYELYQKLE LPKGQKRKVK ERLKAYVKDL YALDLIDKLL
VLDPAQRIDS DDALNHDFFW SDPMPSDLKN MLSTHNQSMF EYLAPPRRRG GHMPQQPANQ
ARNPAATNQS EFDRVF
