PPDK1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PPDK1_ARATH
• UniProt AC: O23404
• Protein Name: Pyruvate, phosphate dikinase 1, chloroplastic
• Gene Name: PPDK
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 963
• Subcellular Localization: Plastid, chloroplast . Cytoplasm . Isoform 1 is targeted to the chloroplast while isoform 2 is found in the cytoplasm.
• Protein Description: Formation of phosphoenolpyruvate. May be involved in regulating the flux of carbon into starch and fatty acids of seeds and in the remobilization of nitrogen reserves in senescing leaves..
• Protein Sequence: MLYIRKKMTSMIVKTTPELFKGNGVFRTDHLGENRMVSRSNRLGDGSNRFPRTGTIHCQRLSIAKTGLHRETKARAILSPVSDPAASIAQKRVFTFGKGRSEGNKGMKSLLGGKGANLAEMASIGLSVPPGLTISTEACQQYQIAGKKLPEGLWEEILEGLSFIERDIGASLADPSKPLLLSVRSGAAISMPGMMDTVLNLGLNDQVVVGLAAKSGERFAYDSFRRFLDMFGDVVMGIPHAKFEEKLERMKERKGVKNDTDLSAADLKELVEQYKSVYLEAKGQEFPSDPKKQLELAIEAVFDSWDSPRANKYRSINQITGLKGTAVNIQCMVFGNMGDTSGTGVLFTRNPSTGEKKLYGEFLVNAQGEDVVAGIRTPEDLDTMKRFMPEAYAELVENCNILERHYKDMMDIEFTVQEERLWMLQCRAGKRTGKGAVKIAVDMVGEGLVEKSSAIKMVEPQHLDQLLHPQFHDPSGYREKVVAKGLPASPGAAVGQVVFTAEEAEAWHSQGKTVILVRTETSPDDVGGMHAAEGILTARGGMTSHAAVVARGWGKCCIAGCSEIRVDENHKVLLIGDLTINEGEWISMNGSTGEVILGKQALAPPALSPDLETFMSWADAIRRLKVMANADTPEDAIAARKNGAQGIGLCRTEHMFFGADRIKAVRKMIMAVTTEQRKASLDILLPYQRSDFEGIFRAMDGLPVTIRLLDPPLHEFLPEGDLDNIVHELAEETGVKEDEVLSRIEKLSEVNPMLGFRGCRLGISYPELTEMQARAIFEAAASMQDQGVTVIPEIMVPLVGTPQELGHQVDVIRKVAKKVFAEKGHTVSYKVGTMIEIPRAALIADEIAKEAEFFSFGTNDLTQMTFGYSRDDVGKFLPIYLAKGILQHDPFEVLDQQGVGQLIKMATEKGRAARPSLKVGICGEHGGDPSSVGFFAEAGLDYVSCSPFRVPIARLAAAQVVVA

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
66	Phosphorylation	QRLSIAKTGLHRETK EEEEECCCCCCHHHH	35.63	19880383
98	Ubiquitination	KRVFTFGKGRSEGNK HHEEEECCCCCCCCH	47.13	17272265
105	Ubiquitination	KGRSEGNKGMKSLLG CCCCCCCHHHHHHHC	71.84	-
263	Phosphorylation	VKNDTDLSAADLKEL CCCCCCCCHHHHHHH	24.99	19880383
543	Phosphorylation	LTARGGMTSHAAVVA EEECCCCCCCHHHHH	22.19	30291188
544	Phosphorylation	TARGGMTSHAAVVAR EECCCCCCCHHHHHC	11.39	19880383

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
543	T	Phosphorylation	Kinase	PDRP1	O49562	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
543	T	Phosphorylation	Phosphorylation of Thr-543 in the dark inactivates the enzyme.	18433157

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PPDK1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference

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 THR-543 AND SER-544, ANDMASS SPECTROMETRY.
PubMed: 19376835

Ubiquitylation

"Multidimensional protein identification technology (MudPIT) analysisof ubiquitinated proteins in plants.";
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
Mol. Cell. Proteomics 6:601-610(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-105, AND MASSSPECTROMETRY.
PubMed: 17272265