CDKE1_ARATH
ID CDKE1_ARATH Reviewed; 470 AA.
AC Q84TI6; Q70Z09; Q9FFQ3;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cyclin-dependent kinase E-1;
DE Short=CDKE;1;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
DE AltName: Full=Cyclin-dependent kinase 8;
DE AltName: Full=Protein HUA ENHANCER 3 {ECO:0000312|EMBL:AAT36644.1};
GN Name=CDKE-1;
GN Synonyms=CDK8, HEN3 {ECO:0000312|EMBL:AAT36644.1},
GN RAO1 {ECO:0000303|PubMed:23229550};
GN OrderedLocusNames=At5g63610 {ECO:0000312|Araport:AT5G63610};
GN ORFNames=MBK5.8 {ECO:0000312|EMBL:BAB10454.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15175247; DOI=10.1242/dev.01187;
RA Wang W., Chen X.;
RT "HUA ENHANCER3 reveals a role for a cyclin-dependent protein kinase in the
RT specification of floral organ identity in Arabidopsis.";
RL Development 131:3147-3156(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 170-470.
RA Pu S.Y., Huang H.J.;
RT "The identification of Arabidopsis cyclin-dependent kinase 8.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11971144; DOI=10.1105/tpc.010445;
RA Vandepoele K., Raes J., de Veylder L., Rouze P., Rombauts S., Inze D.;
RT "Genome-wide analysis of core cell cycle genes in Arabidopsis.";
RL Plant Cell 14:903-916(2002).
RN [9]
RP REVIEW.
RX PubMed=17094738; DOI=10.1146/annurev.genet.40.110405.090431;
RA Inze D., de Veylder L.;
RT "Cell cycle regulation in plant development.";
RL Annu. Rev. Genet. 40:77-105(2006).
RN [10]
RP INTERACTION WITH MED14; LUG AND HDA19.
RX PubMed=17526732; DOI=10.1128/mcb.01912-06;
RA Gonzalez D., Bowen A.J., Carroll T.S., Conlan R.S.;
RT "The transcription corepressor LEUNIG interacts with the histone
RT deacetylase HDA19 and mediator components MED14 (SWP) and CDK8 (HEN3) to
RT repress transcription.";
RL Mol. Cell. Biol. 27:5306-5315(2007).
RN [11]
RP INTERACTION WITH KIN10, AND SUBCELLULAR LOCATION.
RX PubMed=23229550; DOI=10.1074/jbc.m112.416727;
RA Ng S., Giraud E., Duncan O., Law S.R., Wang Y., Xu L., Narsai R.,
RA Carrie C., Walker H., Day D.A., Blanco N.E., Strand A., Whelan J.,
RA Ivanova A.;
RT "Cyclin-dependent kinase E1 (CDKE1) provides a cellular switch in plants
RT between growth and stress responses.";
RL J. Biol. Chem. 288:3449-3459(2013).
CC -!- FUNCTION: Involved in cell differentiation. Required for the
CC specification of stamen and carpel identities and for the proper
CC termination of stem cells in the floral meristem.
CC {ECO:0000269|PubMed:15175247}.
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: Interacts with MED14, HDA19 and LUG. Interacts with KIN10
CC (PubMed:23229550). {ECO:0000269|PubMed:17526732,
CC ECO:0000269|PubMed:23229550}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23229550}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and stems. Expressed in
CC young dividing tissue, such as shoot and root tips, lateral root
CC primordia, young leaves and flowers. Expressed in the inflorescence
CC meristem, inflorescence stem and young flowers.
CC {ECO:0000269|PubMed:15175247}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD29165.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY600243; AAT36644.1; -; mRNA.
DR EMBL; AB005234; BAB10454.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97776.1; -; Genomic_DNA.
DR EMBL; BT005753; AAO64158.1; -; mRNA.
DR EMBL; BT020376; AAV85731.1; -; mRNA.
DR EMBL; AK228654; BAF00561.1; -; mRNA.
DR EMBL; AJ439879; CAD29165.1; ALT_FRAME; mRNA.
DR RefSeq; NP_201166.1; NM_125756.5.
DR AlphaFoldDB; Q84TI6; -.
DR SMR; Q84TI6; -.
DR BioGRID; 21723; 26.
DR IntAct; Q84TI6; 4.
DR STRING; 3702.AT5G63610.1; -.
DR PaxDb; Q84TI6; -.
DR PRIDE; Q84TI6; -.
DR ProteomicsDB; 223976; -.
DR EnsemblPlants; AT5G63610.1; AT5G63610.1; AT5G63610.
DR GeneID; 836481; -.
DR Gramene; AT5G63610.1; AT5G63610.1; AT5G63610.
DR KEGG; ath:AT5G63610; -.
DR Araport; AT5G63610; -.
DR TAIR; locus:2160609; AT5G63610.
DR eggNOG; KOG0666; Eukaryota.
DR HOGENOM; CLU_000288_181_6_1; -.
DR InParanoid; Q84TI6; -.
DR OMA; VYLHRNW; -.
DR OrthoDB; 642369at2759; -.
DR PhylomeDB; Q84TI6; -.
DR PRO; PR:Q84TI6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84TI6; baseline and differential.
DR Genevisible; Q84TI6; AT.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA: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:0019900; F:kinase binding; IPI: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; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..470
FT /note="Cyclin-dependent kinase E-1"
FT /id="PRO_0000293122"
FT DOMAIN 25..333
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 428..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 31..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 36
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24100"
FT CONFLICT 452
FT /note="K -> E (in Ref. 4; AAO64158 and 6; BAF00561)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 52797 MW; 85A92D0000FD5E46 CRC64;
MGDGSSSRSN SSNSTSEKPE WLQQYNLVGK IGEGTYGLVF LARTKTPPKR PIAIKKFKQS
KDGDGVSPTA IREIMLLREI SHENVVKLVN VHINFADMSL YLAFDYAEYD LYEIIRHHRD
KVGHSLNTYT VKSLLWQLLN GLNYLHSNWI IHRDLKPSNI LVMGDAEEHG IVKIADFGLA
RIYQAPLKPL SDNGVVVTIW YRAPELLLGS KHYTSAVDMW AVGCIFAELL TLKPLFQGAE
AKSSQNPFQL DQLDKIFKIL GHPTMDKWPT LVNLPHWQND VQHIQAHKYD SVGLHNVVHL
NQKSPAYDLL SKMLEYDPLK RITASQALEH EYFRMDPLPG RNAFVASQPM EKNVNYPTRP
VDTNTDFEGT TSINPPQAVA AGNVAGNMAG AHGMGSRSMP RPMVAHNMQR MQQSQGMMAY
NFPAQAGLNP SVPLQQQRGM AQPHQQQQLR RKDPGMGMSG YAPPNKSRRL
