CDKF1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CDKF1_ARATH
• UniProt AC: O80345
• Protein Name: Cyclin-dependent kinase F-1
• Gene Name: CDKF-1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 479
• Protein Description: CDK-activating kinase that modulates CDKD-2 and CDKD-3 activities by phosphorylation of the T-loop. Activates CDKD-2 C-terminal domain (CTD) kinase activity. Activates CDKA-1 probably by phosphorylation. Posseses a CDK kinase activity independently of association with cyclin CYCH1-1. Phosphorylates the CTD of the large subunit of RNA polymerase II..
• Protein Sequence: MDKQPATSWSIHTRPEIIAKYEIFERVGSGAYADVYRARRLSDGLIVALKEIFDYQSAFREIDALTILNGSPNVVVMHEYFWREEENAVLVLEFLRSDLAAVIRDGKRKKKVEGGDGFSVGEIKRWMIQILTGVDACHRNLIVHRDLKPGNMLISDDGVLKLADFGQARILMEHDIVASDENQQAYKLEDKDGETSEPPEVIPDYENSPRQGSDGQEREAMSKDEYFRQVEELKAKQVVRDDTDKDSNVHDGDISCLATCTVSEMDDDLGRNSFSYDADEAVDDTQGLMTSCVGTRWFRPPELLYGSTMYGLEVDLWSLGCVFAELLSLEPLFPGISDIDQISRVTNVLGNLNEEVWPGCVDLPDYKSISFAKVESPLGIEGCLPNHSGDVISLLKKLICYDPASRATTMEMLNDKYLSEEPLPVPVSELYVPPTMSGPDEDSPRKWNDYREMDSDSDFDGFGPMNVKPTSSGFTIEFP

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
32	Phosphorylation	ERVGSGAYADVYRAR HCCCCCCHHCHHHHH	13.58	-
179	Phosphorylation	MEHDIVASDENQQAY EECCEECCCCCCCEE	34.27	30291188
195	Phosphorylation	LEDKDGETSEPPEVI EECCCCCCCCCCCCC	43.87	23776212
196	Phosphorylation	EDKDGETSEPPEVIP ECCCCCCCCCCCCCC	43.75	23776212
205	Phosphorylation	PPEVIPDYENSPRQG CCCCCCCCCCCCCCC	16.20	23776212
208	Phosphorylation	VIPDYENSPRQGSDG CCCCCCCCCCCCCCH	14.98	27532006
213	Phosphorylation	ENSPRQGSDGQEREA CCCCCCCCCHHHHHH	30.17	30407730
247	Phosphorylation	RDDTDKDSNVHDGDI CCCCCCCCCCCCCCE	46.63	19376835
290	Phosphorylation	DDTQGLMTSCVGTRW CCCCCCCHHHCCCCC	24.82	23776212
291	Phosphorylation	DTQGLMTSCVGTRWF CCCCCCHHHCCCCCC	7.89	23776212
295	Phosphorylation	LMTSCVGTRWFRPPE CCHHHCCCCCCCCHH	12.34	23776212
417	Phosphorylation	MEMLNDKYLSEEPLP HHHHCCCCCCCCCCC	20.51	23776212
419	Phosphorylation	MLNDKYLSEEPLPVP HHCCCCCCCCCCCCC	36.50	23776212
428	Phosphorylation	EPLPVPVSELYVPPT CCCCCCHHHEECCCC	18.80	23776212
431	Phosphorylation	PVPVSELYVPPTMSG CCCHHHEECCCCCCC	13.58	23776212
435	Phosphorylation	SELYVPPTMSGPDED HHEECCCCCCCCCCC	20.21	23776212
437	Phosphorylation	LYVPPTMSGPDEDSP EECCCCCCCCCCCCC	50.05	23776212
443	Phosphorylation	MSGPDEDSPRKWNDY CCCCCCCCCCCCCCC	25.26	23776212

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

Oops, there are no upstream regulatory protein records of CDKF1_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CDKF1_ARATH !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CDKF1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
Y3627_ARATH	AT3G16270	physical	17426018
CDKD2_ARATH	CAK4	physical	17426018
CDKD3_ARATH	CDKD1;3	physical	15486101
CDKD2_ARATH	CAK4	physical	15486101
CKS1_ARATH	CKS1	physical	20407024
CKS2_ARATH	CKS2	physical	20407024
CCA34_ARATH	CYCA3;4	physical	20407024
CCD41_ARATH	CYCD4;1	physical	20407024
CCD42_ARATH	CYCD4;2	physical	20407024
CCH11_ARATH	CYCH;1	physical	20407024
KRP7_ARATH	ICK5	physical	20407024
RBR1_ARATH	RBR1	physical	20407024
CDKA1_ARATH	CDC2	physical	20407024
CDKF1_ARATH	CAK1AT	physical	20407024
CDKD2_ARATH	CAK4	physical	20706207
CDKF1_ARATH	CAK1AT	physical	25969537

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179; SER-208 ANDSER-247, AND MASS SPECTROMETRY.
PubMed: 19376835

"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana.";
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.;
J. Proteomics 72:439-451(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND MASSSPECTROMETRY.
PubMed: 19245862

"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis.";
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.;
J. Proteome Res. 7:2458-2470(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179 AND SER-443, ANDMASS SPECTROMETRY.
PubMed: 18433157