CDK9_CAEEL
ID CDK9_CAEEL Reviewed; 478 AA.
AC Q9TVL3; Q9XTH5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Probable 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=cdk-9; ORFNames=H25P06.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12183367; DOI=10.1101/gad.999002;
RA Shim E.Y., Walker A.K., Shi Y., Blackwell T.K.;
RT "CDK-9/cyclin T (P-TEFb) is required in two postinitiation pathways for
RT transcription in the C. elegans embryo.";
RL Genes Dev. 16:2135-2146(2002).
CC -!- FUNCTION: Essential member of the cyclin-dependent kinase pair
CC (CDK9/cyclin-T) complex, also called positive transcription elongation
CC factor B (P-TEFb), which is proposed to facilitate the transition from
CC abortive to production elongation by phosphorylating the CTD (C-
CC terminal domain) of the large subunit of RNA polymerase II (RNAP II)
CC and spt-5. {ECO:0000269|PubMed:12183367}.
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 -!- SUBUNIT: Associates with cyclin-T (cit-1.1 or cit-1.2) to form P-TEFb.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12183367}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=Q9TVL3-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q9TVL3-2; Sequence=VSP_016291, VSP_016292;
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; Z92797; CAB07237.2; -; Genomic_DNA.
DR EMBL; Z83118; CAB07237.2; JOINED; Genomic_DNA.
DR EMBL; Z92797; CAB07238.3; -; Genomic_DNA.
DR EMBL; Z83118; CAB07238.3; JOINED; Genomic_DNA.
DR PIR; F87920; F87920.
DR PIR; T23123; T23123.
DR PIR; T23124; T23124.
DR RefSeq; NP_492906.2; NM_060505.3. [Q9TVL3-1]
DR RefSeq; NP_492907.2; NM_060506.3. [Q9TVL3-2]
DR AlphaFoldDB; Q9TVL3; -.
DR SMR; Q9TVL3; -.
DR BioGRID; 38431; 3.
DR IntAct; Q9TVL3; 2.
DR STRING; 6239.H25P06.2b; -.
DR iPTMnet; Q9TVL3; -.
DR EPD; Q9TVL3; -.
DR PaxDb; Q9TVL3; -.
DR PeptideAtlas; Q9TVL3; -.
DR EnsemblMetazoa; H25P06.2a.1; H25P06.2a.1; WBGene00000410. [Q9TVL3-2]
DR EnsemblMetazoa; H25P06.2b.1; H25P06.2b.1; WBGene00000410. [Q9TVL3-1]
DR GeneID; 173023; -.
DR KEGG; cel:CELE_H25P06.2; -.
DR UCSC; H25P06.2b; c. elegans. [Q9TVL3-1]
DR CTD; 173023; -.
DR WormBase; H25P06.2a; CE37838; WBGene00000410; cdk-9. [Q9TVL3-2]
DR WormBase; H25P06.2b; CE37839; WBGene00000410; cdk-9. [Q9TVL3-1]
DR eggNOG; KOG0669; Eukaryota.
DR GeneTree; ENSGT00940000155373; -.
DR InParanoid; Q9TVL3; -.
DR OMA; VTKMPWF; -.
DR OrthoDB; 925637at2759; -.
DR PhylomeDB; Q9TVL3; -.
DR Reactome; R-CEL-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-CEL-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-CEL-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-CEL-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-CEL-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-CEL-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-CEL-9018519; Estrogen-dependent gene expression.
DR PRO; PR:Q9TVL3; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000410; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000791; C:euchromatin; IDA:WormBase.
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:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0007281; P:germ cell development; IMP:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:2001253; P:regulation of histone H3-K36 trimethylation; IMP:UniProtKB.
DR GO; GO:1901407; P:regulation of phosphorylation of RNA polymerase II C-terminal domain; IMP:UniProtKB.
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 3: Inferred from homology;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..478
FT /note="Probable cyclin-dependent kinase 9"
FT /id="PRO_0000085807"
FT DOMAIN 85..413
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 91..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 432..445
FT /note="NSQFEYTVGKGAHA -> VRKFEAKWLKKREK (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_016291"
FT VAR_SEQ 446..478
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_016292"
SQ SEQUENCE 478 AA; 53593 MW; C8E307EA3465E36B CRC64;
MSAQNYHAGL HQSSTQRPPK RPNTEHAQEP PKRALIGGQT TPSSSGGGQT PNGTNYELEV
KQQLSNYQKL FDQATYPFIR DVSTYEKLNK IGQGTFGEVF KARCKNTGRM VALKKILMEN
EKEGFPITAL REVKMLEQLK HPNITDLIEV CSAKSTGTTG SKDRATFYLV MALCAHDLAG
LLSNPKIRMS LVHIKTMMKH LMSGLNKLHR SKILHRDMKA ANVLISKDGI LKLADFGLAR
PFVQRENGAG PRPLYTNRVV TLWYRPPELL LGDRQYGTKI DVWGAGCIMA EMWTRQPIMQ
GDTEQKQLQL ISGLCGSINK DVWPNCVNMP LWSAMSSEPN SALPQGKYRI LPNKMKNLMK
FDAPDSKTDP FGKNVKQHDS ATDDDALHLL EILLAIDPDK RPTSDEAEDD IWFFKDPVPM
ANVQDLMDTI PNSQFEYTVG KGAHANRGRH QNAQQRPNQQ QARPSNAIPA GQYRDTIF
