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Q9C9M7 (CDKD2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 97. 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 D-2

Short name=CDKD;2
EC=2.7.11.22
EC=2.7.11.23
Alternative name(s):
CDK-activating kinase 4-At
Short name=CAK4-At
Gene names
Name:CDKD-2
Ordered Locus Names:At1g66750
ORF Names:F4N21.12
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Forms 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. Down-regulated by phosphorylation by WEE1. Ref.6 Ref.8

Subunit structure

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

Subcellular location

Cytoplasm. Nucleus Ref.6.

Tissue specificity

Expressed in suspension cell culture, but not in plant organs. Ref.1

Post-translational modification

Phosphorylated by CDKF-1 at Ser-162 and Thr-168. Phosphorylated by WEE1 at Tyr-24. 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 348348Cyclin-dependent kinase D-2
PRO_0000293120

Regions

Domain13 – 293281Protein kinase
Nucleotide binding19 – 279ATP By similarity

Sites

Active site1351Proton acceptor By similarity
Binding site421ATP Probable

Amino acid modifications

Modified residue241Phosphotyrosine
Modified residue1621Phosphoserine; by CAK Ref.6
Modified residue1681Phosphothreonine; by CAK Ref.6

Experimental info

Mutagenesis241Y → F: Abolishes phosphorylation by WEE1. Ref.8
Mutagenesis421K → R: Prevents autophosphorylation. Ref.6
Mutagenesis1621S → A: Reduces phosphorylation by CDKF-1 by 30%. Ref.6
Mutagenesis1681T → A: Almost abolishes phosphorylation by CDKF-1. Loss of CTD-kinase activity. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9C9M7 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: A32CA3E98204DDAD

FASTA34839,201
        10         20         30         40         50         60 
MSKSGDNQPV DRYLRRQILG EGTYGVVYKA TDTKTGKTVA VKKIRLGNQK EGVNFTALRE 

        70         80         90        100        110        120 
IKLLKELNHP HIVELIDAFP HDGSLHLVFE YMQTDLEAVI RDRNIFLSPG DIKSYMLMTL 

       130        140        150        160        170        180 
KGLAYCHKKW VLHRDMKPNN LLIGENGLLK LADFGLARLF GSPNRRFTHQ VFATWYRAPE 

       190        200        210        220        230        240 
LLFGSRQYGA GVDVWAAGCI FAELLLRRPF LPGSTEIDQL GKIFQAFGTP VPSQWSDMIY 

       250        260        270        280        290        300 
LPDYMEFSYT PAPPLRTIFP MASDDALDLL AKMFIYDPRQ RITIQQALDH RYFSSSPSPT 

       310        320        330        340 
EPGKLQIPAS KGDALEPKAS EQNQHGNSPA VLSPPGKMRR VMGPEGFT 

« 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-162 AND THR-168, MUTAGENESIS OF LYS-42; SER-162 AND THR-168.
[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, ENZYME REGULATION, PHOSPHORYLATION, INTERACTION WITH CYCH1-1, MUTAGENESIS OF TYR-24.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB074116 mRNA. Translation: BAB91558.1.
AC013288 Genomic DNA. Translation: AAG60076.1.
CP002684 Genomic DNA. Translation: AEE34551.1.
AY136355 mRNA. Translation: AAM97021.1.
BT000198 mRNA. Translation: AAN15517.1.
RefSeqNP_176847.1. NM_105345.4.
UniGeneAt.35737.

3D structure databases

ProteinModelPortalQ9C9M7.
SMRQ9C9M7. Positions 19-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid28214. 43 interactions.
IntActQ9C9M7. 22 interactions.
STRING3702.AT1G66750.1-P.

Proteomic databases

PaxDbQ9C9M7.
PRIDEQ9C9M7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G66750.1; AT1G66750.1; AT1G66750.
GeneID842993.
KEGGath:AT1G66750.

Organism-specific databases

GeneFarm3289. 109.
TAIRAT1G66750.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
InParanoidQ9C9M7.
KOK02202.
OMAQRITIQQ.
PhylomeDBQ9C9M7.
ProtClustDBCLSN2681793.

Enzyme and pathway databases

BioCycARA:AT1G66750-MONOMER.

Gene expression databases

GenevestigatorQ9C9M7.

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. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 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 nameCDKD2_ARATH
AccessionPrimary (citable) accession number: Q9C9M7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: June 1, 2001
Last modified: March 19, 2014
This is version 97 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