dbPTM

CDPK1_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CDPK1_ARATH
UniProt AC	Q06850
Protein Name	Calcium-dependent protein kinase 1
Gene Name	CPK1
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	610
Subcellular Localization	Peroxisome membrane Lipid-anchor .
Protein Description	May play a role in signal transduction pathways that involve calcium as a second messenger. Phosphorylates the Ca(2+)-ATPase ACA2 resulting in the inhibition of its calcium activation..
Protein Sequence	MGNTCVGPSRNGFLQSVSAAMWRPRDGDDSASMSNGDIASEAVSGELRSRLSDEVQNKPPEQVTMPKPGTDVETKDREIRTESKPETLEEISLESKPETKQETKSETKPESKPDPPAKPKKPKHMKRVSSAGLRTESVLQRKTENFKEFYSLGRKLGQGQFGTTFLCVEKTTGKEFACKSIAKRKLLTDEDVEDVRREIQIMHHLAGHPNVISIKGAYEDVVAVHLVMECCAGGELFDRIIQRGHYTERKAAELTRTIVGVVEACHSLGVMHRDLKPENFLFVSKHEDSLLKTIDFGLSMFFKPDDVFTDVVGSPYYVAPEVLRKRYGPEADVWSAGVIVYILLSGVPPFWAETEQGIFEQVLHGDLDFSSDPWPSISESAKDLVRKMLVRDPKKRLTAHQVLCHPWVQVDGVAPDKPLDSAVLSRMKQFSAMNKFKKMALRVIAESLSEEEIAGLKEMFNMIDADKSGQITFEELKAGLKRVGANLKESEILDLMQAADVDNSGTIDYKEFIAATLHLNKIEREDHLFAAFTYFDKDGSGYITPDELQQACEEFGVEDVRIEELMRDVDQDNDGRIDYNEFVAMMQKGSITGGPVKMGLEKSFSIALKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Myristoylation	------MGNTCVGPS ------CCCCCCCCC	37.85	12913141
5	S-palmitoylation	---MGNTCVGPSRNG ---CCCCCCCCCCCC	3.75	12913141
30	Phosphorylation	RPRDGDDSASMSNGD CCCCCCCCCCCCCCC	27.30	25561503
32	Phosphorylation	RDGDDSASMSNGDIA CCCCCCCCCCCCCHH	27.05	19880383
34	Phosphorylation	GDDSASMSNGDIASE CCCCCCCCCCCHHHH	34.86	29654922
40	Phosphorylation	MSNGDIASEAVSGEL CCCCCHHHHHHCHHH	26.82	30407730
44	Phosphorylation	DIASEAVSGELRSRL CHHHHHHCHHHHHHC	33.33	19880383
49	Phosphorylation	AVSGELRSRLSDEVQ HHCHHHHHHCCHHHH	50.64	23776212
52	Phosphorylation	GELRSRLSDEVQNKP HHHHHHCCHHHHCCC	30.52	23776212
64	Phosphorylation	NKPPEQVTMPKPGTD CCCHHHCCCCCCCCC	27.70	23776212
70	Phosphorylation	VTMPKPGTDVETKDR CCCCCCCCCCCCCCC	45.45	27545962
74	Phosphorylation	KPGTDVETKDREIRT CCCCCCCCCCCCCCC	37.79	27545962
83	Phosphorylation	DREIRTESKPETLEE CCCCCCCCCCCCHHH	53.55	-
107	Phosphorylation	KQETKSETKPESKPD CCCCCCCCCCCCCCC	60.02	-
129	Phosphorylation	PKHMKRVSSAGLRTE CHHHHHHHHHCCCCH	20.64	23776212
130	Phosphorylation	KHMKRVSSAGLRTES HHHHHHHHHCCCCHH	24.41	23776212
137	Phosphorylation	SAGLRTESVLQRKTE HHCCCCHHHHHHHCC	27.75	-
151	Phosphorylation	ENFKEFYSLGRKLGQ CCHHHHHHHHHHHCC	29.66	-
314	Phosphorylation	VFTDVVGSPYYVAPE CCCCCCCCCCCCCHH	9.71	-
603	Phosphorylation	VKMGLEKSFSIALKL CCCCCEEEEEEEECC	18.17	23776212
605	Phosphorylation	MGLEKSFSIALKL-- CCCEEEEEEEECC--	17.65	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
Oops, there are no upstream regulatory protein records of CDPK1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CDPK1_ARATH !!

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 CDPK1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CDPK1_ARATH	CPK1	physical	16430916

Drug and Disease Associations

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

Regulatory Network of CDPK1_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-605, AND MASSSPECTROMETRY.	19376835 [Abstract]
"A phyloproteomic characterization of in vitro autophosphorylation incalcium-dependent protein kinases."; Hegeman A.D., Rodriguez M., Han B.W., Uno Y., Phillips G.N. Jr.,Hrabak E.M., Cushman J.C., Harper J.F., Harmon A.C., Sussman M.R.; Proteomics 6:3649-3664(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-64; SER-83; THR-107;SER-137 AND SER-151, AND MASS SPECTROMETRY.	16758442 [Abstract]