Phosphoproteomics

<p>Phosphoproteomics is a branch of <a href="/facts/Proteomics/3aqQ1tFh">proteomics</a> that identifies, catalogs, and characterizes <a href="/facts/Protein/Jxmagu3E">proteins</a> containing a <a href="/facts/Phosphate_group/FDGVCxUG">phosphate group</a> as a <a href="/facts/Posttranslational_modification/KMUayTIc">posttranslational modification</a>.  <a href="/facts/Phosphorylation/LXUEEeIL">Phosphorylation</a> is a key reversible modification that regulates protein function, subcellular localization, complex formation, degradation of proteins and therefore <a href="/facts/Cell_signaling/6oYAVP9I">cell signaling</a> networks.  With all of these modification results, it is estimated that between 30–65% of all proteins may be phosphorylated, some multiple times. Based on statistical estimates from many datasets, 230,000, 156,000 and 40,000 phosphorylation sites should exist in human, mouse, and yeast, respectively.
</p><p>Compared to expression analysis, phosphoproteomics provides two additional layers of information.  First, it provides clues on what protein or pathway might be activated because a change in phosphorylation status almost always reflects a change in protein activity. Second, it indicates what proteins might be potential drug targets as exemplified by the kinase inhibitor Gleevec. While phosphoproteomics will greatly expand knowledge about the numbers and types of phosphoproteins, its greatest promise is the rapid analysis of entire phosphorylation based signalling networks.
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Phosphoproteomics open-in-new

Phosphoproteomics