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O80345 (CDKF1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processCell cycle
Cell division
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell division

Inferred from electronic annotation. Source: UniProtKB-KW

maintenance of root meristem identity

Inferred from mutant phenotype PubMed 11069305. Source: TAIR

positive regulation of protein kinase activity

Inferred from genetic interaction Ref.1. Source: GOC

protein phosphorylation

Inferred from direct assay Ref.1. Source: TAIR

regulation of cyclin-dependent protein serine/threonine kinase activity

Traceable author statement PubMed 16024551. Source: TAIR

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15610358. Source: TAIR

cytosol

Inferred from direct assay Ref.9. Source: TAIR

nucleus

Inferred from direct assay PubMed 15610358. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from electronic annotation. Source: UniProtKB-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: UniProtKB-EC

protein serine/threonine kinase activity

Traceable author statement PubMed 16024551. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479Cyclin-dependent kinase F-1
PRO_0000293123

Regions

Domain21 – 418398Protein kinase
Nucleotide binding27 – 359ATP By similarity

Sites

Active site1461Proton acceptor By similarity
Binding site501ATP By similarity

Amino acid modifications

Modified residue321Phosphotyrosine By similarity
Modified residue1791Phosphoserine Ref.9
Modified residue2471Phosphoserine Ref.10
Modified residue2901Phosphothreonine Probable

Experimental info

Mutagenesis501K → A: No effect on CDKA-1 activation. Ref.5
Mutagenesis2901T → A: Abolishes CDKA-1 activation and kinase activity. Ref.8

Sequences

Sequence LengthMass (Da)Tools
O80345 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: CA08BF178B7CC831

FASTA47953,752
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Root.
[10]"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-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRT08953.
RefSeqNP_194627.1. NM_119042.4.
NP_849468.1. NM_179137.2.
UniGeneAt.19673.

3D structure databases

ProteinModelPortalO80345.
SMRO80345. Positions 17-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid14306. 28 interactions.
IntActO80345. 5 interactions.

Proteomic databases

PaxDbO80345.
PRIDEO80345.

Protocols and materials databases

DNASU829019.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G28980.1; AT4G28980.1; AT4G28980.
AT4G28980.2; AT4G28980.2; AT4G28980.
GeneID829019.
KEGGath:AT4G28980.

Organism-specific databases

GeneFarm3296. 111.
TAIRAT4G28980.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
InParanoidO80345.
OMAVDACHRN.
PhylomeDBO80345.
ProtClustDBCLSN2685783.

Enzyme and pathway databases

BioCycARA:AT4G28980-MONOMER.
ARA:GQT-608-MONOMER.

Gene expression databases

GenevestigatorO80345.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 2 hits.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCDKF1_ARATH
AccessionPrimary (citable) accession number: O80345
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names