{"rating_data": {"avg_stars": 0, "total": 0, "avg": 0}, "name": "mouse tissue phosphorylation database", "created": "2010-12-23 19:36:18", "url": "https://gygi.med.harvard.edu/phosphomouse/search_results.php?search_phrase={{Symbol}}", "lastmodified": "2011-05-03 22:50:50", "usage_data": {"layouts": 4.0, "users": 4}, "popularity": 4.0, "owner": {"username": "nsalathi", "url": "/profile/80/nsalathi", "name": "Neeraj Salathia"}, "species": ["mouse"], "shortUrl": "gygi.med.harvard.edu", "id": 851, "short_description": "From E.L. Huttlin et al Cell, Volume 143, Issue 7, 1174-1189, 23 December 2010  Here we report the most thorough characterization of...", "role_permission": ["biogpsusers"], "permission_style": "public", "type": "iframe", "options": {"allowedSpecies": ["mouse"]}, "tags": ["phosphorylation", "tissue"], "description": "From E.L. Huttlin et al\nCell, Volume 143, Issue 7, 1174-1189, 23 December 2010\n\nHere we report the most thorough characterization of tissue specific\nprotein abundance and phosphorylation to date, including\n12,000 proteins and 36,000 phosphorylation sites from nine\nmouse tissues. These data revealed distinctive and complementary\nprotein and phosphoprotein expression profiles that support\neach tissue\u2019s unique physiology. Moreover, by combining\nprotein abundance measurements with phosphorylation observations,\nwe could distinguish tissue-specific phosphorylation\nof ubiquitous proteins from phosphorylation of tissue-specific\nproteins. Furthermore, most phosphoproteins integrate input\nfrom multiple kinases spanning diverse signaling pathways.\nOverall, the \u2018\u2018typical\u2019\u2019 phosphoprotein is broadly expressed\nyet is variably phosphorylated to tune protein function to the\nneeds of each tissue. We now present these protein abundance\nand phosphorylation data as a web-based resource (http://gygi.\nmed.harvard.edu/phosphomouse/index.php) to aid analysis\nof existing biological data and inspire future biological\ninvestigations."}