CDKF1_ARATH
ID CDKF1_ARATH Reviewed; 479 AA.
AC O80345;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Cyclin-dependent kinase F-1;
DE Short=CDKF;1;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
DE AltName: Full=CDK-activating kinase 1-At;
DE Short=CAK1-At;
GN Name=CDKF-1; Synonyms=CAK1; OrderedLocusNames=At4g28980;
GN ORFNames=F19B15.10;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9560221; DOI=10.1073/pnas.95.9.5021;
RA Umeda M., Bhalerao R.P., Schell J., Uchimiya H., Koncz C.;
RT "A distinct cyclin-dependent kinase-activating kinase of Arabidopsis
RT thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:5021-5026(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 FUNCTION, AND MUTAGENESIS OF LYS-50.
RX PubMed=12084729; DOI=10.1074/jbc.m205537200;
RA Tsakraklides V., Solomon M.J.;
RT "Comparison of Cak1p-like cyclin-dependent kinase-activating kinases.";
RL J. Biol. Chem. 277:33482-33489(2002).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=15486101; DOI=10.1105/tpc.104.025601;
RA Shimotohno A., Umeda-Hara C., Bisova K., Uchimiya H., Umeda M.;
RT "The plant-specific kinase CDKF;1 is involved in activating phosphorylation
RT of cyclin-dependent kinase-activating kinases in Arabidopsis.";
RL Plant Cell 16:2954-2966(2004).
RN [8]
RP FUNCTION, PHOSPHORYLATION AT THR-290, AND MUTAGENESIS OF THR-290.
RX PubMed=16856985; DOI=10.1111/j.1365-313x.2006.02820.x;
RA Shimotohno A., Ohno R., Bisova K., Sakaguchi N., Huang J., Koncz C.,
RA Uchimiya H., Umeda M.;
RT "Diverse phosphoregulatory mechanisms controlling cyclin-dependent kinase-
RT activating kinases in Arabidopsis.";
RL Plant J. 47:701-710(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: CDK-activating kinase that modulates CDKD-2 and CDKD-3
CC activities by phosphorylation of the T-loop. Activates CDKD-2 C-
CC terminal domain (CTD) kinase activity. Activates CDKA-1 probably by
CC phosphorylation. Posseses a CDK kinase activity independently of
CC association with cyclin CYCH1-1. Phosphorylates the CTD of the large
CC subunit of RNA polymerase II. {ECO:0000269|PubMed:12084729,
CC ECO:0000269|PubMed:15486101, ECO:0000269|PubMed:16856985}.
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 -!- TISSUE SPECIFICITY: Highly expressed in suspension cell culture.
CC Expressed at low levels in all plant organs.
CC {ECO:0000269|PubMed:9560221}.
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; AB009399; BAA28775.1; -; mRNA.
DR EMBL; AL078470; CAB43912.1; -; Genomic_DNA.
DR EMBL; AL161574; CAB79656.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85567.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85568.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67753.1; -; Genomic_DNA.
DR EMBL; AY042816; AAK68756.1; -; mRNA.
DR EMBL; AY064627; AAL47340.1; -; mRNA.
DR PIR; T08953; T08953.
DR RefSeq; NP_001329562.1; NM_001341955.1.
DR RefSeq; NP_194627.1; NM_119042.5.
DR RefSeq; NP_849468.1; NM_179137.3.
DR AlphaFoldDB; O80345; -.
DR SMR; O80345; -.
DR BioGRID; 14306; 30.
DR IntAct; O80345; 7.
DR STRING; 3702.AT4G28980.2; -.
DR iPTMnet; O80345; -.
DR PaxDb; O80345; -.
DR PRIDE; O80345; -.
DR ProteomicsDB; 223978; -.
DR DNASU; 829019; -.
DR EnsemblPlants; AT4G28980.1; AT4G28980.1; AT4G28980.
DR EnsemblPlants; AT4G28980.2; AT4G28980.2; AT4G28980.
DR EnsemblPlants; AT4G28980.3; AT4G28980.3; AT4G28980.
DR GeneID; 829019; -.
DR Gramene; AT4G28980.1; AT4G28980.1; AT4G28980.
DR Gramene; AT4G28980.2; AT4G28980.2; AT4G28980.
DR Gramene; AT4G28980.3; AT4G28980.3; AT4G28980.
DR KEGG; ath:AT4G28980; -.
DR Araport; AT4G28980; -.
DR TAIR; locus:2119961; AT4G28980.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; O80345; -.
DR OMA; RWMIQIL; -.
DR OrthoDB; 683664at2759; -.
DR PhylomeDB; O80345; -.
DR PRO; PR:O80345; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O80345; baseline and differential.
DR Genevisible; O80345; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019912; F:cyclin-dependent protein kinase activating kinase activity; IBA:GO_Central.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:TAIR.
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:0010078; P:maintenance of root meristem identity; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:TAIR.
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; 2.
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 Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..479
FT /note="Cyclin-dependent kinase F-1"
FT /id="PRO_0000293123"
FT DOMAIN 21..418
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 187..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
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 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 32
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24100"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C9M7"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 290
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:16856985"
FT MUTAGEN 50
FT /note="K->A: No effect on CDKA-1 activation."
FT /evidence="ECO:0000269|PubMed:12084729"
FT MUTAGEN 290
FT /note="T->A: Abolishes CDKA-1 activation and kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:16856985"
SQ SEQUENCE 479 AA; 53752 MW; CA08BF178B7CC831 CRC64;
MDKQPATSWS IHTRPEIIAK YEIFERVGSG AYADVYRARR LSDGLIVALK EIFDYQSAFR
EIDALTILNG SPNVVVMHEY FWREEENAVL VLEFLRSDLA AVIRDGKRKK KVEGGDGFSV
GEIKRWMIQI LTGVDACHRN LIVHRDLKPG NMLISDDGVL KLADFGQARI LMEHDIVASD
ENQQAYKLED KDGETSEPPE VIPDYENSPR QGSDGQEREA MSKDEYFRQV EELKAKQVVR
DDTDKDSNVH DGDISCLATC TVSEMDDDLG RNSFSYDADE AVDDTQGLMT SCVGTRWFRP
PELLYGSTMY GLEVDLWSLG CVFAELLSLE PLFPGISDID QISRVTNVLG NLNEEVWPGC
VDLPDYKSIS FAKVESPLGI EGCLPNHSGD VISLLKKLIC YDPASRATTM EMLNDKYLSE
EPLPVPVSEL YVPPTMSGPD EDSPRKWNDY REMDSDSDFD GFGPMNVKPT SSGFTIEFP
