CDK8_CAEEL
ID CDK8_CAEEL Reviewed; 588 AA.
AC P90866;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 4.
DT 03-AUG-2022, entry version 161.
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 cdk-8;
DE AltName: Full=Mediator of RNA polymerase II transcription subunit cdk-8;
GN Name=cdk-8; ORFNames=F39H11.3;
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].
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).
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:Q9VT57}.
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. {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}.
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DR EMBL; BX284601; CAB03083.2; -; Genomic_DNA.
DR PIR; T22001; T22001.
DR RefSeq; NP_492357.2; NM_059956.6.
DR AlphaFoldDB; P90866; -.
DR SMR; P90866; -.
DR BioGRID; 38110; 4.
DR IntAct; P90866; 1.
DR STRING; 6239.F39H11.3; -.
DR EPD; P90866; -.
DR PaxDb; P90866; -.
DR PeptideAtlas; P90866; -.
DR PRIDE; P90866; -.
DR EnsemblMetazoa; F39H11.3.1; F39H11.3.1; WBGene00000409.
DR GeneID; 172677; -.
DR KEGG; cel:CELE_F39H11.3; -.
DR UCSC; F39H11.3; c. elegans.
DR CTD; 172677; -.
DR WormBase; F39H11.3; CE32409; WBGene00000409; cdk-8.
DR eggNOG; KOG0666; Eukaryota.
DR GeneTree; ENSGT00940000175924; -.
DR HOGENOM; CLU_000288_181_6_1; -.
DR InParanoid; P90866; -.
DR OMA; VYLHRNW; -.
DR OrthoDB; 642369at2759; -.
DR PhylomeDB; P90866; -.
DR Reactome; R-CEL-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR PRO; PR:P90866; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000409; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS: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 Activator; ATP-binding; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..588
FT /note="Cyclin-dependent kinase 8"
FT /id="PRO_0000312931"
FT DOMAIN 26..348
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 376..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 32..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 588 AA; 67785 MW; 7409832B107F6563 CRC64;
MTLMIDENFK KQLAQRRERV EDLFYFENSK EIGRGTYGLV YKAVPKKQNG QFPNKEYALK
MIEGQGFSMS ACREIALFRE LRHPNLICLQ RVFLTNEKKV WLLLDYAEHD LWHVIKHHRT
AKSKKVPIMV PRNMVKNILF QILSGMHYLH SNWVLHRDLK PANILLMGDG PPDMRGRVKI
ADLGFSRIYA NPLKPMAELD PVVVTFWYRA PELLLGAKHY TKAIDVWAIG CIFAELLTAE
PLFFCKEEDI KAQNPYHYDQ VKRIFHLLGY PSDADWPDMK KMPDHQRLLS DARNEGTPIQ
TFPNSLHRYF DKWKINSQSS PYRLLVKLLT VDPTKRVSCE EAMNDIYFRK MERPPRETDD
VFNKYPIPYA KKEQQMTVAP DQAQQQHQQQ QVQMQQQPQM GQQQMMGQPQ MVQPQMGQPP
MGGAHPGVVA PDGHPHQMMQ QQQHPQQHHM QYQGMHDPMQ GGMDEGPQAK MMRMGNVPVG
RYAPMPPPYG APQDYHPQQG PPMVQMMQQP GPSGYYPQRP GQPTGAVPGP GPQGYMNPQM
GMQMGMRAPG VPPQGYMPGR GMAPPQMGQQ QPGPNQQQQQ QWQQQYHR
