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Q9LMT0 (CDKD3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 D-3
Short name=CDKD;3
EC=2.7.11.22
EC=2.7.11.23
Alternative name(s):
CDK-activating kinase 2-At
Short name=CAK2-At
Gene names
Name:CDKD-3
Ordered Locus Names:At1g18040
ORF Names:T10F20.5, T10O22.1
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.8

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

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

Enzyme regulation

Activated by phosphorylation by CDKF-1. Ref.6

Subunit structure

Interacts with CYCH1-1. Binding to CYCH1-1 activates CDK kinase. Ref.6 Ref.8

Subcellular location

Nucleus Ref.6.

Tissue specificity

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

Post-translational modification

Phosphorylated by CDKF-1 at Ser-161 and Thr-167. Phosphorylated at Tyr-23 by WEE1. Autophosphorylated. Ref.6 Ref.8

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 391391Cyclin-dependent kinase D-3
PRO_0000293121

Regions

Domain12 – 292281Protein kinase
Nucleotide binding18 – 269ATP By similarity

Sites

Active site1341Proton acceptor By similarity
Binding site411ATP Probable

Amino acid modifications

Modified residue221Phosphothreonine By similarity
Modified residue231Phosphotyrosine
Modified residue1611Phosphoserine; by CAK Ref.6
Modified residue1671Phosphothreonine; by CAK Ref.6

Experimental info

Mutagenesis231Y → F: Abolishes phosphorylation by WEE1. Ref.8
Mutagenesis411K → R: Prevents autophosphorylation. Ref.6
Mutagenesis1611S → A: Reduces phosphorylation by CDKF-1 by 20%. Abolishes phosphorylation by CDKF-1; when associated with A-167. Ref.6
Mutagenesis1671T → A: Reduces phosphorylation by CDKF-1 by 80%. Abolishes phosphorylation by CDKF-1; when associated with A-161. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9LMT0 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3FD4A2293283B656

FASTA39144,530
        10         20         30         40         50         60 
MPEQPKKVAD RYLKQEVLGQ GTYGVVFKAT DTKTEQTVAI KKIRLGKQRE GVNITALREI 

        70         80         90        100        110        120 
KMLKELKHPH IILLIDAFPH KENLHLVFEF METDLEAVIR DSNIFLSPAD IKSYLLMTFK 

       130        140        150        160        170        180 
GLAYCHDKWV LHRDMKPNNL LIGVDGQLKL ADFGLARIFG SPNRKFTHQV FARWYRAPEL 

       190        200        210        220        230        240 
LFGAKQYGAA VDVWAVACIF AELLLRRPFL QGNSDIDQLS KIFAAFGTPK ADQWPDLTKL 

       250        260        270        280        290        300 
PDYVEYQFVP APSLRSLFPA VSDDALDLLS KMFTYDPKAR ISIKQALEHR YFTSAPAPTD 

       310        320        330        340        350        360 
PAKLPKPVPK QDGKSSYGKH EAITVQSPPR KLRRVMPERG RVDSLKSHVD KDQQAPMSLD 

       370        380        390 
FTILAERPPN RPTITSADRS HLKRKLDLEF Q

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. 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]"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, INTERACTION WITH CYCH1-1, MUTAGENESIS OF TYR-23.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00531977.
PIRH86315.
RefSeqNP_173244.1. NM_101666.2.
UniGeneAt.14957.
At.26247.

3D structure databases

HSSPHSSP built from PDB template 1UA2 based on UniProtKB P50613.
ProteinModelPortalQ9LMT0.
SMRQ9LMT0. Positions 12-350.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9LMT0. 6 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G18040.1; AT1G18040.1; AT1G18040.
GeneID838384.
KEGGath:AT1G18040.

Organism-specific databases

GeneFarm3292. 109.
TAIRAt1g18040.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
InParanoidQ9LMT0.
KOK02202.
OMAPRPNCPA.
PhylomeDBQ9LMT0.
ProtClustDBCLSN2679882.

Gene expression databases

GenevestigatorQ9LMT0.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCDKD3_ARATH
AccessionPrimary (citable) accession number: Q9LMT0
Secondary accession number(s): Q9LM42
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: October 1, 2000
Last modified: May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents