O80345 (CDKF1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclin-dependent kinase F-1
Short name=CDKF;1
EC=2.7.11.22
EC=2.7.11.23

Alternative name(s):
CDK-activating kinase 1-At
Short name=CAK1-At

Gene names

Name:	CDKF-1
Synonyms:	CAK1
Ordered Locus Names:	At4g28980
ORF Names:	F19B15.10

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	479 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	CDK-activating kinase that modulates CDKD-2 and CDKD-3 activities by phosphorylation of the T-loop. Activates CDKD-2 C-terminal domain (CTD) kinase activity. Activates CDKA-1 probably by phosphorylation. Posseses a CDK kinase activity independently of association with cyclin CYCH1-1. Phosphorylates the CTD of the large subunit of RNA polymerase II. Ref.5 Ref.7 Ref.8
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
Tissue specificity	Highly expressed in suspension cell culture. Expressed at low levels in all plant organs. Ref.1
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW maintenance of root meristem identity Inferred from mutant phenotype PubMed 11069305. Source: TAIR regulation of cyclin-dependent protein serine/threonine kinase activity Traceable author statement PubMed 16024551. Source: TAIR
Cellular_component	cytosol Inferred from direct assay Ref.9. Source: TAIR nucleus Inferred from direct assay PubMed 15610358. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II carboxy-terminal domain kinase activity Inferred from electronic annotation. Source: EC cyclin-dependent protein kinase activating kinase activity Inferred from genetic interaction Ref.1. Source: TAIR cyclin-dependent protein serine/threonine kinase activity Inferred from electronic annotation. Source: EC protein serine/threonine kinase activity Traceable author statement PubMed 16024551. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 479	479	Cyclin-dependent kinase F-1		PRO_0000293123
Regions
	Domain	21 – 418	398	Protein kinase
	Nucleotide binding	27 – 35	9	ATP By similarity
Sites
	Active site	146	1	Proton acceptor By similarity
	Binding site	50	1	ATP By similarity
Amino acid modifications
	Modified residue	179	1	Phosphoserine Ref.9 Ref.11
	Modified residue	208	1	Phosphoserine Ref.10 Ref.11
	Modified residue	247	1	Phosphoserine Ref.11
	Modified residue	290	1	Phosphothreonine Probable
	Modified residue	443	1	Phosphoserine Ref.9
Experimental info
	Mutagenesis	50	1	K → A: No effect on CDKA-1 activation. Ref.5
	Mutagenesis	290	1	T → A: Abolishes CDKA-1 activation and kinase activity. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	O80345 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: CA08BF178B7CC831	FASTA	479	53,752
	10 20 30 40 50 60 MDKQPATSWS IHTRPEIIAK YEIFERVGSG AYADVYRARR LSDGLIVALK EIFDYQSAFR 70 80 90 100 110 120 EIDALTILNG SPNVVVMHEY FWREEENAVL VLEFLRSDLA AVIRDGKRKK KVEGGDGFSV 130 140 150 160 170 180 GEIKRWMIQI LTGVDACHRN LIVHRDLKPG NMLISDDGVL KLADFGQARI LMEHDIVASD 190 200 210 220 230 240 ENQQAYKLED KDGETSEPPE VIPDYENSPR QGSDGQEREA MSKDEYFRQV EELKAKQVVR 250 260 270 280 290 300 DDTDKDSNVH DGDISCLATC TVSEMDDDLG RNSFSYDADE AVDDTQGLMT SCVGTRWFRP 310 320 330 340 350 360 PELLYGSTMY GLEVDLWSLG CVFAELLSLE PLFPGISDID QISRVTNVLG NLNEEVWPGC 370 380 390 400 410 420 VDLPDYKSIS FAKVESPLGI EGCLPNHSGD VISLLKKLIC YDPASRATTM EMLNDKYLSE 430 440 450 460 470 EPLPVPVSEL YVPPTMSGPD EDSPRKWNDY REMDSDSDFD GFGPMNVKPT SSGFTIEFP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A distinct cyclin-dependent kinase-activating kinase of Arabidopsis thaliana." Umeda M., Bhalerao R.P., Schell J., Uchimiya H., Koncz C. Proc. Natl. Acad. Sci. U.S.A. 95:5021-5026(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Comparison of Cak1p-like cyclin-dependent kinase-activating kinases." Tsakraklides V., Solomon M.J. J. Biol. Chem. 277:33482-33489(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LYS-50.
[6]	"Genome-wide analysis of core cell cycle genes in Arabidopsis." Vandepoele K., Raes J., de Veylder L., Rouze P., Rombauts S., Inze D. Plant Cell 14:903-916(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[7]	"The plant-specific kinase CDKF;1 is involved in activating phosphorylation of cyclin-dependent kinase-activating kinases in Arabidopsis." Shimotohno A., Umeda-Hara C., Bisova K., Uchimiya H., Umeda M. Plant Cell 16:2954-2966(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Diverse phosphoregulatory mechanisms controlling cyclin-dependent kinase-activating kinases in Arabidopsis." Shimotohno A., Ohno R., Bisova K., Sakaguchi N., Huang J., Koncz C., Uchimiya H., Umeda M. Plant J. 47:701-710(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF THR-290.
[9]	"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis." de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H. J. Proteome Res. 7:2458-2470(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179 AND SER-443, MASS SPECTROMETRY. Tissue: Root.
[10]	"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana." Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C. J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, MASS SPECTROMETRY. Strain: cv. Columbia.
[11]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179; SER-208 AND SER-247, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB009399 mRNA. Translation: BAA28775.1. AL078470 Genomic DNA. Translation: CAB43912.1. AL161574 Genomic DNA. Translation: CAB79656.1. CP002687 Genomic DNA. Translation: AEE85567.1. CP002687 Genomic DNA. Translation: AEE85568.1. AY042816 mRNA. Translation: AAK68756.1. AY064627 mRNA. Translation: AAL47340.1.
IPI	IPI00527792.
PIR	T08953.
RefSeq	NP_194627.1. NM_119042.4. NP_849468.1. NM_179137.2.
UniGene	At.19673.
3D structure databases
ProteinModelPortal	O80345.
SMR	O80345. Positions 17-426.
ModBase	Search...
Protein-protein interaction databases
IntAct	O80345. 5 interactions.
Proteomic databases
PaxDb	O80345.
PRIDE	O80345.
Protocols and materials databases
DNASU	829019.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G28980.1; AT4G28980.1; AT4G28980. AT4G28980.2; AT4G28980.2; AT4G28980.
GeneID	829019.
KEGG	ath:AT4G28980.
Organism-specific databases
GeneFarm	3296. 111.
TAIR	At4g28980.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233024.
InParanoid	O80345.
OMA	TSCVGTR.
PhylomeDB	O80345.
ProtClustDB	CLSN2685783.
Gene expression databases
ArrayExpress	O80345.
Genevestigator	O80345.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 2 hits. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CDKF1_ARATH

Accession

Primary (citable) accession number: O80345

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program