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O80345

- CDKF1_ARATH

UniProt

O80345 - CDKF1_ARATH

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Protein

Cyclin-dependent kinase F-1

Gene

CDKF-1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.
ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501ATPPROSITE-ProRule annotation
Active sitei146 – 1461Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi27 – 359ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein kinase activating kinase activity Source: TAIR
  3. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
  4. protein serine/threonine kinase activity Source: TAIR
  5. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. maintenance of root meristem identity Source: TAIR
  4. positive regulation of protein kinase activity Source: GOC
  5. protein phosphorylation Source: TAIR
  6. regulation of cyclin-dependent protein serine/threonine kinase activity Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase F-1 (EC:2.7.11.22, EC:2.7.11.23)
Short name:
CDKF;1
Alternative name(s):
CDK-activating kinase 1-At
Short name:
CAK1-At
Gene namesi
Name:CDKF-1
Synonyms:CAK1
Ordered Locus Names:At4g28980
ORF Names:F19B15.10
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G28980.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: TAIR
  2. cytosol Source: TAIR
  3. nucleus Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi50 – 501K → A: No effect on CDKA-1 activation. 1 Publication
Mutagenesisi290 – 2901T → A: Abolishes CDKA-1 activation and kinase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 479479Cyclin-dependent kinase F-1PRO_0000293123Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321PhosphotyrosineBy similarity
Modified residuei179 – 1791Phosphoserine1 Publication
Modified residuei247 – 2471Phosphoserine1 Publication
Modified residuei290 – 2901PhosphothreonineCurated

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO80345.
PRIDEiO80345.

Expressioni

Tissue specificityi

Highly expressed in suspension cell culture. Expressed at low levels in all plant organs.1 Publication

Gene expression databases

ExpressionAtlasiO80345. baseline and differential.
GenevestigatoriO80345.

Interactioni

Protein-protein interaction databases

BioGridi14306. 28 interactions.
IntActiO80345. 5 interactions.

Structurei

3D structure databases

ProteinModelPortaliO80345.
SMRiO80345. Positions 14-426.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 418398Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233024.
InParanoidiO80345.
OMAiVDACHRN.
PhylomeDBiO80345.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O80345-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDKQPATSWS IHTRPEIIAK YEIFERVGSG AYADVYRARR LSDGLIVALK
60 70 80 90 100
EIFDYQSAFR EIDALTILNG SPNVVVMHEY FWREEENAVL VLEFLRSDLA
110 120 130 140 150
AVIRDGKRKK KVEGGDGFSV GEIKRWMIQI LTGVDACHRN LIVHRDLKPG
160 170 180 190 200
NMLISDDGVL KLADFGQARI LMEHDIVASD ENQQAYKLED KDGETSEPPE
210 220 230 240 250
VIPDYENSPR QGSDGQEREA MSKDEYFRQV EELKAKQVVR DDTDKDSNVH
260 270 280 290 300
DGDISCLATC TVSEMDDDLG RNSFSYDADE AVDDTQGLMT SCVGTRWFRP
310 320 330 340 350
PELLYGSTMY GLEVDLWSLG CVFAELLSLE PLFPGISDID QISRVTNVLG
360 370 380 390 400
NLNEEVWPGC VDLPDYKSIS FAKVESPLGI EGCLPNHSGD VISLLKKLIC
410 420 430 440 450
YDPASRATTM EMLNDKYLSE EPLPVPVSEL YVPPTMSGPD EDSPRKWNDY
460 470
REMDSDSDFD GFGPMNVKPT SSGFTIEFP
Length:479
Mass (Da):53,752
Last modified:November 1, 1998 - v1
Checksum:iCA08BF178B7CC831
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiT08953.
RefSeqiNP_194627.1. NM_119042.4.
NP_849468.1. NM_179137.2.
UniGeneiAt.19673.

Genome annotation databases

EnsemblPlantsiAT4G28980.1; AT4G28980.1; AT4G28980.
AT4G28980.2; AT4G28980.2; AT4G28980.
GeneIDi829019.
KEGGiath:AT4G28980.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi T08953.
RefSeqi NP_194627.1. NM_119042.4.
NP_849468.1. NM_179137.2.
UniGenei At.19673.

3D structure databases

ProteinModelPortali O80345.
SMRi O80345. Positions 14-426.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 14306. 28 interactions.
IntActi O80345. 5 interactions.

Proteomic databases

PaxDbi O80345.
PRIDEi O80345.

Protocols and materials databases

DNASUi 829019.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G28980.1 ; AT4G28980.1 ; AT4G28980 .
AT4G28980.2 ; AT4G28980.2 ; AT4G28980 .
GeneIDi 829019.
KEGGi ath:AT4G28980.

Organism-specific databases

GeneFarmi 3296. 111.
TAIRi AT4G28980.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233024.
InParanoidi O80345.
OMAi VDACHRN.
PhylomeDBi O80345.

Enzyme and pathway databases

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

Gene expression databases

ExpressionAtlasi O80345. baseline and differential.
Genevestigatori O80345.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 2 hits.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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].

Entry informationi

Entry nameiCDKF1_ARATH
AccessioniPrimary (citable) accession number: O80345
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: November 1, 1998
Last modified: October 29, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3