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Protein phosphorylation is a complex network of signaling and regulatory events that affects virtually every cellular process. Our understanding of the nature of this network as a whole remains limited, largely because of an array of technical challenges in the isolation and high-throughput sequencing of phosphorylated species. In the present work, we demonstrate that a combination of tandem phosphopeptide enrichment methods, high performance MS, and optimized database search/data filtering strategies is a powerful tool for surveying the phosphoproteome. Using our integrated analytical platform, we report the identification of 5,635 nonredundant phosphorylation sites from 2,328 proteins from mouse liver. From this list of sites, we extracted both novel and known motifs for specific Ser/Thr kinases including a "dipolar" motif. We also found that C-terminal phosphorylation was more frequent than at any other location and that the distribution of potential kinases for these sites was unique. Finally, we identified double phosphorylation motifs that may be involved in ordered phosphorylation.
Authors : Villén Judit , Beausoleil Sean A , Gerber Scott A , Gygi Steven P ,
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WP1110: Oxidative phosphorylation
WP1248: Oxidative phosphorylation
WP1283: Oxidative phosphorylation
WP1335: Oxidative phosphorylation
WP1403: AMPK signaling
WP1671: Methane metabolism
WP1680: Oxidative phosphorylation
WP1711: Trinitrotoluene degradation
WP623: Oxidative phosphorylation
WP766: Oxidative phosphorylation
WP876: Oxidative phosphorylation
WP994: Oxidative phosphorylation
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