ID CDK8_XENLA Reviewed; 416 AA. AC Q66KH9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 105. DE RecName: Full=Cyclin-dependent kinase 8; DE EC=2.7.11.22; DE EC=2.7.11.23; DE AltName: Full=Cell division protein kinase 8; DE AltName: Full=Mediator complex subunit cdk8; DE AltName: Full=Mediator of RNA polymerase II transcription subunit cdk8; GN Name=cdk8; 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 [LARGE SCALE MRNA]. RC TISSUE=Kidney; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in CC regulated gene transcription of nearly all RNA polymerase II-dependent CC genes. Mediator functions as a bridge to convey information from gene- CC specific regulatory proteins to the basal RNA polymerase II CC transcription machinery. Mediator is recruited to promoters by direct CC interactions with regulatory proteins and serves as a scaffold for the CC assembly of a functional pre-initiation complex with RNA polymerase II CC and the general transcription factors. Phosphorylates the CTD (C- CC terminal domain) of the large subunit of RNA polymerase II (RNAp II), CC which may inhibit the formation of a transcription initiation complex CC (By similarity). {ECO:0000250|UniProtKB:P49336}. 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SUBUNIT: Component of the Mediator complex. Interacts with ccnc. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC080386; AAH80386.1; -; mRNA. DR RefSeq; NP_001087585.1; NM_001094116.1. DR AlphaFoldDB; Q66KH9; -. DR SMR; Q66KH9; -. DR BioGRID; 104269; 1. DR IntAct; Q66KH9; 1. DR DNASU; 447409; -. DR GeneID; 447409; -. DR KEGG; xla:447409; -. DR AGR; Xenbase:XB-GENE-962272; -. DR CTD; 447409; -. DR Xenbase; XB-GENE-962272; cdk8.S. DR OrthoDB; 46620at2759; -. DR Proteomes; UP000186698; Chromosome 2S. DR Bgee; 447409; Expressed in egg cell and 19 other cell types or tissues. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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:0004672; F:protein kinase activity; ISS:UniProtKB. 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2. 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; CELL DIVISION PROTEIN KINASE; 1. DR PANTHER; PTHR24056:SF243; CYCLIN-DEPENDENT KINASE 8; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 Activator; ATP-binding; Kinase; Nucleotide-binding; Nucleus; KW Reference proteome; Repressor; Serine/threonine-protein kinase; KW Transcription; Transcription regulation; Transferase. FT CHAIN 1..416 FT /note="Cyclin-dependent kinase 8" FT /id="PRO_0000312927" FT DOMAIN 21..287 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..15 FT /note="Interaction with CCNC" FT /evidence="ECO:0000250" FT REGION 313..416 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 325..349 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 364..416 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 151 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 27..35 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 52 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 416 AA; 47763 MW; F5524A35EF0A0BF3 CRC64; MDYDFKVKLT GERERVEDLF EYEGCKVGRG TYGHVYKAKR KDGKDDRDYA LKQIEGTGIS MSACREIALL RELKHPNVIS LQKVFLSHAD RKVWLLFDFA EHDLWHIIKF HRASKANKKP VQLPRGMVKS LLYQILDGIH YLHANWVLHR DLKPANILVM GEGPERGRVK IADMGFARLF NSPLKPLADL DPVVVTFWYR APELLLGARH YTKAIDKDWE DIKKMPEHST LIKDFRRNTY TNCSLIKYME KHKVKPDSKT FHLLQKLLTM DPIKRISSEQ AMQDPYFLED PLPTSDVFAG CQIPYPKREF LTEEEPDDKG DKKNQQQQQG NNHTNGTGHP GNQDNSHAQG PPLKKVRVVP PTTTSGGLIM TSDYQRSNPH AAYQNPGPST SQPQSSMGYT STSQQPPQYS HQTHRY //