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Q9LMT0

- CDKD3_ARATH

UniProt

Q9LMT0 - CDKD3_ARATH

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Protein

Cyclin-dependent kinase D-3

Gene

CDKD-3

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

Functioni

May form a stable complex with cyclin CYCH1-1 that phosphorylates human CDK2 and the C-terminal domain (CTD) of the large subunit of RNA polymerase II.2 Publications

Catalytic activityi

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

Enzyme regulationi

Activated by phosphorylation by CDKF-1.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei41 – 411ATPCurated
Active sitei134 – 1341Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 269ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
  3. protein kinase activity Source: TAIR
  4. 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. regulation of cell cycle 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:AT1G18040-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase D-3 (EC:2.7.11.22, EC:2.7.11.23)
Short name:
CDKD;3
Alternative name(s):
CDK-activating kinase 2-At
Short name:
CAK2-At
Gene namesi
Name:CDKD-3
Ordered Locus Names:At1g18040
ORF Names:T10F20.5, T10O22.1
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G18040.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231Y → F: Abolishes phosphorylation by WEE1. 1 Publication
Mutagenesisi41 – 411K → R: Prevents autophosphorylation. 1 Publication
Mutagenesisi161 – 1611S → A: Reduces phosphorylation by CDKF-1 by 20%. Abolishes phosphorylation by CDKF-1; when associated with A-167. 1 Publication
Mutagenesisi167 – 1671T → A: Reduces phosphorylation by CDKF-1 by 80%. Abolishes phosphorylation by CDKF-1; when associated with A-161. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391Cyclin-dependent kinase D-3PRO_0000293121Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Phosphotyrosine1 Publication
Modified residuei161 – 1611Phosphoserine; by CAK1 Publication
Modified residuei167 – 1671Phosphothreonine; by CAK1 Publication

Post-translational modificationi

Phosphorylated by CDKF-1 at Ser-161 and Thr-167. Phosphorylated at Tyr-23 by WEE1. Autophosphorylated.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ9LMT0.

Expressioni

Tissue specificityi

Expressed in roots, shoots and suspension cell culture.1 Publication

Gene expression databases

GenevestigatoriQ9LMT0.

Interactioni

Subunit structurei

Interacts with CYCH1-1. Binding to CYCH1-1 activates CDK kinase.2 Publications

Protein-protein interaction databases

BioGridi23623. 32 interactions.
IntActiQ9LMT0. 6 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9LMT0.
SMRiQ9LMT0. Positions 8-329.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 292281Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233024.
InParanoidiQ9LMT0.
KOiK02202.
OMAiCHRNWIL.
PhylomeDBiQ9LMT0.

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. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9LMT0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPEQPKKVAD RYLKQEVLGQ GTYGVVFKAT DTKTEQTVAI KKIRLGKQRE
60 70 80 90 100
GVNITALREI KMLKELKHPH IILLIDAFPH KENLHLVFEF METDLEAVIR
110 120 130 140 150
DSNIFLSPAD IKSYLLMTFK GLAYCHDKWV LHRDMKPNNL LIGVDGQLKL
160 170 180 190 200
ADFGLARIFG SPNRKFTHQV FARWYRAPEL LFGAKQYGAA VDVWAVACIF
210 220 230 240 250
AELLLRRPFL QGNSDIDQLS KIFAAFGTPK ADQWPDLTKL PDYVEYQFVP
260 270 280 290 300
APSLRSLFPA VSDDALDLLS KMFTYDPKAR ISIKQALEHR YFTSAPAPTD
310 320 330 340 350
PAKLPKPVPK QDGKSSYGKH EAITVQSPPR KLRRVMPERG RVDSLKSHVD
360 370 380 390
KDQQAPMSLD FTILAERPPN RPTITSADRS HLKRKLDLEF Q
Length:391
Mass (Da):44,530
Last modified:October 1, 2000 - v1
Checksum:i3FD4A2293283B656
GO

Sequence cautioni

The sequence AAF78394.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB047274 mRNA. Translation: BAB62843.1.
AC034107 Genomic DNA. Translation: AAF97821.1.
AC069551 Genomic DNA. Translation: AAF78394.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE29667.1.
AY099677 mRNA. Translation: AAM20528.1.
AY128857 mRNA. Translation: AAM91257.1.
PIRiH86315.
RefSeqiNP_173244.1. NM_101666.2.
UniGeneiAt.14957.
At.26247.

Genome annotation databases

EnsemblPlantsiAT1G18040.1; AT1G18040.1; AT1G18040.
GeneIDi838384.
KEGGiath:AT1G18040.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB047274 mRNA. Translation: BAB62843.1 .
AC034107 Genomic DNA. Translation: AAF97821.1 .
AC069551 Genomic DNA. Translation: AAF78394.1 . Sequence problems.
CP002684 Genomic DNA. Translation: AEE29667.1 .
AY099677 mRNA. Translation: AAM20528.1 .
AY128857 mRNA. Translation: AAM91257.1 .
PIRi H86315.
RefSeqi NP_173244.1. NM_101666.2.
UniGenei At.14957.
At.26247.

3D structure databases

ProteinModelPortali Q9LMT0.
SMRi Q9LMT0. Positions 8-329.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 23623. 32 interactions.
IntActi Q9LMT0. 6 interactions.

Proteomic databases

PRIDEi Q9LMT0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G18040.1 ; AT1G18040.1 ; AT1G18040 .
GeneIDi 838384.
KEGGi ath:AT1G18040.

Organism-specific databases

GeneFarmi 3292. 109.
TAIRi AT1G18040.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233024.
InParanoidi Q9LMT0.
KOi K02202.
OMAi CHRNWIL.
PhylomeDBi Q9LMT0.

Enzyme and pathway databases

BioCyci ARA:AT1G18040-MONOMER.

Gene expression databases

Genevestigatori Q9LMT0.

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. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
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. "Differential phosphorylation activities of CDK-activating kinases in Arabidopsis thaliana."
    Shimotohno A., Matsubayashi S., Yamaguchi M., Uchimiya H., Umeda M.
    FEBS Lett. 534:69-74(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [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. "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.
  6. "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, ENZYME REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH CYCH1-1, PHOSPHORYLATION AT SER-161 AND THR-167, MUTAGENESIS OF LYS-41; SER-161 AND THR-167.
  7. "Cell cycle regulation in plant development."
    Inze D., de Veylder L.
    Annu. Rev. Genet. 40:77-105(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  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, PHOSPHORYLATION AT TYR-23, INTERACTION WITH CYCH1-1, MUTAGENESIS OF TYR-23.

Entry informationi

Entry nameiCDKD3_ARATH
AccessioniPrimary (citable) accession number: Q9LMT0
Secondary accession number(s): Q9LM42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 107 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