Phosphoproteomic analysis reveals major default phosphorylation sites outside long intrinsically disordered regions of Arabidopsis plasma membrane proteins

Proteome Science

Volumn 10, Issue 1, 2012, Pages

  Nespoulous, Claude ^a   Rofidal, Valérie ^a   Sommerer, Nicolas ^b   Hem, Sonia ^a   Rossignol, Michel ^a  

^a CEMAGREF   (France)

^b SPO   (France)

Author keywords

Arabidopsis; Intrinsically disordered regions; Phosphoproteome; Plasma membrane

Indexed keywords

ARABIDOPSIS PROTEIN; MEMBRANE PROTEIN; PHOSPHATASE; PHOSPHOPROTEIN; PROTEOME;

ANION EXCHANGE CHROMATOGRAPHY; ARABIDOPSIS; ARTICLE; BIOINFORMATICS; ENZYME ACTIVITY; NONHUMAN; PREDICTIVE VALUE; PROTEIN ANALYSIS; PROTEIN DEPHOSPHORYLATION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN PURIFICATION; PROTEIN TRANSPORT; PROTEOMICS; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION; TANDEM MASS SPECTROMETRY;

ARABIDOPSIS; EUKARYOTA;

EID: 84867896145     PISSN: None     EISSN: 14775956     Source Type: Journal    
DOI: 10.1186/1477-5956-10-62     Document Type: Article

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