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Cell, Volume 143, Issue 7, 1174-1189, 23 December 2010

Here we report the most thorough characterization of tissue specific
protein abundance and phosphorylation to date, including
12,000 proteins and 36,000 phosphorylation sites from nine
mouse tissues. These data revealed distinctive and complementary
protein and phosphoprotein expression profiles that support
each tissue&#8217;s unique physiology. Moreover, by combining
protein abundance measurements with phosphorylation observations,
we could distinguish tissue-specific phosphorylation
of ubiquitous proteins from phosphorylation of tissue-specific
proteins. Furthermore, most phosphoproteins integrate input
from multiple kinases spanning diverse signaling pathways.
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yet is variably phosphorylated to tune protein function to the
needs of each tissue. We now present these protein abundance
and phosphorylation data as a web-based resource (http://gygi.
med.harvard.edu/phosphomouse/index.php) to aid analysis
of existing biological data and inspire future biological
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