dbPTM

CDKD2_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CDKD2_ARATH
UniProt AC	Q9C9M7
Protein Name	Cyclin-dependent kinase D-2
Gene Name	CDKD-2
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	348
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	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..
Protein Sequence	MSKSGDNQPVDRYLRRQILGEGTYGVVYKATDTKTGKTVAVKKIRLGNQKEGVNFTALREIKLLKELNHPHIVELIDAFPHDGSLHLVFEYMQTDLEAVIRDRNIFLSPGDIKSYMLMTLKGLAYCHKKWVLHRDMKPNNLLIGENGLLKLADFGLARLFGSPNRRFTHQVFATWYRAPELLFGSRQYGAGVDVWAAGCIFAELLLRRPFLPGSTEIDQLGKIFQAFGTPVPSQWSDMIYLPDYMEFSYTPAPPLRTIFPMASDDALDLLAKMFIYDPRQRITIQQALDHRYFSSSPSPTEPGKLQIPASKGDALEPKASEQNQHGNSPAVLSPPGKMRRVMGPEGFT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
24	Phosphorylation	QILGEGTYGVVYKAT HHHCCCCEEEEEEEE	20.84	16856985
162	Phosphorylation	GLARLFGSPNRRFTH HHHHHHCCCCCCHHC	16.21	23776212
168	Phosphorylation	GSPNRRFTHQVFATW CCCCCCHHCHHHHHH	15.02	16856985
320	Phosphorylation	DALEPKASEQNQHGN CCCCCCHHHCCCCCC	45.93	23776212
328	Phosphorylation	EQNQHGNSPAVLSPP HCCCCCCCCCCCCCC	20.87	30291188
333	Phosphorylation	GNSPAVLSPPGKMRR CCCCCCCCCCCCCCC	23.58	30291188

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
162	S	Phosphorylation	Kinase	CDK7	-	GPS
162	S	Phosphorylation	Kinase	CAK	-	Uniprot
168	T	Phosphorylation	Kinase	CDK7	-	GPS
168	T	Phosphorylation	Kinase	CAK	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
162	S	Phosphorylation	15486101
Phosphorylated by CDKF-1 at Ser-162 and Thr-168.
168	T	Phosphorylation	15486101
Phosphorylated by CDKF-1 at Ser-162 and Thr-168.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of CDKD2_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CCH11_ARATH	CYCH;1	physical	17426018
ATPBN_ARATH	AT5G08690	physical	17426018
CDKF1_ARATH	CAK1AT	physical	20407024
CCH11_ARATH	CYCH;1	physical	20407024
CDKE1_ARATH	CDKE;1	physical	20407024
CKS1_ARATH	CKS1	physical	20407024
CKS2_ARATH	CKS2	physical	20407024
CCD41_ARATH	CYCD4;1	physical	20407024
CCD42_ARATH	CYCD4;2	physical	20407024
CCD51_ARATH	CYCD5;1	physical	20407024
CCD61_ARATH	CYCD6;1	physical	20407024
E2FA_ARATH	E2F3	physical	20407024
KRP1_ARATH	ICK1	physical	20407024
KRP2_ARATH	KRP2	physical	20407024
KRP3_ARATH	ICK6	physical	20407024
KRP4_ARATH	KRP4	physical	20407024
KRP5_ARATH	ICK3	physical	20407024
KRP6_ARATH	KRP6	physical	20407024
KRP7_ARATH	ICK5	physical	20407024
CCH11_ARATH	CYCH;1	physical	20706207
ERCC2_ARATH	UVH6	physical	20706207
KPRS1_ARATH	AT2G35390	physical	20706207
KPRS2_ARATH	PRS2	physical	20706207
KPRS5_ARATH	AT2G44530	physical	20706207
TFB1A_ARATH	AT1G55750	physical	20706207
ATP5E_ARATH	AT1G51650	physical	20706207
ETR1_ARATH	ETR1	physical	20706207
IF2B_ARATH	EIF2 BETA	physical	20706207
PABP8_ARATH	PAB8	physical	20706207
SFH12_ARATH	SFH12	physical	20706207

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CDKD2_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The plant-specific kinase CDKF;1 is involved in activatingphosphorylation of cyclin-dependent kinase-activating kinases inArabidopsis."; Shimotohno A., Umeda-Hara C., Bisova K., Uchimiya H., Umeda M.; Plant Cell 16:2954-2966(2004). Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, INTERACTION WITHCYCH1-1, PHOSPHORYLATION AT SER-162 AND THR-168, AND MUTAGENESIS OFLYS-42; SER-162 AND THR-168.	15486101 [Abstract]