Q9C9M7 (CDKD2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW regulation of cyclin-dependent protein serine/threonine kinase activity Traceable author statement PubMed 16024551. Source: TAIR
Cellular_component	cytoplasm Inferred from direct assay PubMed 15610358. Source: TAIR nucleus Inferred from direct assay PubMed 15610358. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II carboxy-terminal domain kinase activity Inferred from electronic annotation. Source: EC cyclin-dependent protein serine/threonine kinase activity Inferred from electronic annotation. Source: EC protein serine/threonine kinase activity Traceable author statement PubMed 16024551. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 348	348	Cyclin-dependent kinase D-2		PRO_0000293120
Regions
	Domain	13 – 293	281	Protein kinase
	Nucleotide binding	19 – 27	9	ATP By similarity
Sites
	Active site	135	1	Proton acceptor By similarity
	Binding site	42	1	ATP Probable
Amino acid modifications
	Modified residue	23	1	Phosphothreonine By similarity
	Modified residue	24	1	Phosphotyrosine
	Modified residue	162	1	Phosphoserine; by CAK Ref.6
	Modified residue	168	1	Phosphothreonine; by CAK Ref.6
Experimental info
	Mutagenesis	24	1	Y → F: Abolishes phosphorylation by WEE1. Ref.8
	Mutagenesis	42	1	K → R: Prevents autophosphorylation. Ref.6
	Mutagenesis	162	1	S → A: Reduces phosphorylation by CDKF-1 by 30%. Ref.6
	Mutagenesis	168	1	T → A: Almost abolishes phosphorylation by CDKF-1. Loss of CTD-kinase activity. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q9C9M7 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: A32CA3E98204DDAD	FASTA	348	39,201
	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

References

	« Hide 'large scale' referencesShow '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. , 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-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.
+	Additional computationally mapped references.

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.
IPI	IPI00519212.
RefSeq	NP_176847.1. NM_105345.4.
UniGene	At.35737.
3D structure databases
HSSP	HSSP built from PDB template 1P2A based on UniProtKB P24941.
ProteinModelPortal	Q9C9M7.
SMR	Q9C9M7. Positions 19-332.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9C9M7. 22 interactions.
STRING	3702.AT1G66750.1-P.
Proteomic databases
PaxDb	Q9C9M7.
PRIDE	Q9C9M7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G66750.1; AT1G66750.1; AT1G66750.
GeneID	842993.
KEGG	ath:AT1G66750.
Organism-specific databases
GeneFarm	3289. 109.
TAIR	At1g66750.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233024.
InParanoid	Q9C9M7.
KO	K02202.
OMA	NVITRWY.
PhylomeDB	Q9C9M7.
ProtClustDB	CLSN2681793.
Gene expression databases
Genevestigator	Q9C9M7.
Family and domain databases
InterPro	IPR011009. 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]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CDKD2_ARATH

Accession

Primary (citable) accession number: Q9C9M7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program