Proteomics

Dataset Information

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Large-scale phosphoproteome profiling reveals kinase substrates and phosphorylation motif use in Arabidopsis thaliana chloroplasts


ABSTRACT: Not available

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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