Large-scale phosphoproteome profiling reveals kinase substrates and phosphorylation motif use in Arabidopsis thaliana chloroplasts
Ontology highlight
ABSTRACT:
INSTRUMENT(S): instrument model, LTQ
ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)
TISSUE(S): Rosette, Shoot
SUBMITTER: 
Katja Baerenfaller
PROVIDER: PRD000096 | Pride | 2009-07-28
REPOSITORIES: Pride
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Publications
Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks.
Reiland Sonja S Messerli Gaëlle G Baerenfaller Katja K Gerrits Bertran B Endler Anne A Grossmann Jonas J Gruissem Wilhelm W Baginsky Sacha S
Plant physiology 20090417 2
We have characterized the phosphoproteome of Arabidopsis (Arabidopsis thaliana) seedlings using high-accuracy mass spectrometry and report the identification of 1,429 phosphoproteins and 3,029 unique phosphopeptides. Among these, 174 proteins were chloroplast phosphoproteins. Motif-X (motif extractor) analysis of the phosphorylation sites in chloroplast proteins identified four significantly enriched kinase motifs, which include casein kinase II (CKII) and proline-directed kinase motifs, as well ...[more]
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