A tissue-specific atlas of mouse protein phosphorylation and expression.
Article Details
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Huttlin EL, Jedrychowski MP, Elias JE, Goswami T, Rad R, Beausoleil SA, Villen J, Haas W, Sowa ME, Gygi SP
A tissue-specific atlas of mouse protein phosphorylation and expression.
Cell. 2010 Dec 23;143(7):1174-89. doi: 10.1016/j.cell.2010.12.001.
- PubMed ID
- 21183079 [ View in PubMed]
- Abstract
Although most tissues in an organism are genetically identical, the biochemistry of each is optimized to fulfill its unique physiological roles, with important consequences for human health and disease. Each tissue's unique physiology requires tightly regulated gene and protein expression coordinated by specialized, phosphorylation-dependent intracellular signaling. To better understand the role of phosphorylation in maintenance of physiological differences among tissues, we performed proteomic and phosphoproteomic characterizations of nine mouse tissues. We identified 12,039 proteins, including 6296 phosphoproteins harboring nearly 36,000 phosphorylation sites. Comparing protein abundances and phosphorylation levels revealed specialized, interconnected phosphorylation networks within each tissue while suggesting that many proteins are regulated by phosphorylation independently of their expression. Our data suggest that the "typical" phosphoprotein is widely expressed yet displays variable, often tissue-specific phosphorylation that tunes protein activity to the specific needs of each tissue. We offer this dataset as an online resource for the biological research community.
DrugBank Data that Cites this Article
- Polypeptides
Name UniProt ID Cytochrome P450 2B9 P12790 Details Calcium-activated potassium channel subunit alpha-1 Q08460 Details Cell growth-regulating nucleolar protein Q08288 Details Histamine H1 receptor P70174 Details Solute carrier family 12 member 5 Q91V14 Details Protein unc-13 homolog B Q9Z1N9 Details Thioredoxin reductase 3 Q99MD6 Details Thioredoxin reductase 2, mitochondrial Q9JLT4 Details Thioredoxin reductase 1, cytoplasmic Q9JMH6 Details Serine/threonine-protein kinase 38 Q91VJ4 Details E3 ubiquitin-protein ligase Mdm2 P23804 Details