A tissue-specific atlas of mouse protein phosphorylation and expression.

Article Details

Citation

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
NameUniProt ID
Cytochrome P450 2B9P12790Details
Calcium-activated potassium channel subunit alpha-1Q08460Details
Cell growth-regulating nucleolar proteinQ08288Details
Histamine H1 receptorP70174Details
Solute carrier family 12 member 5Q91V14Details
Protein unc-13 homolog BQ9Z1N9Details
Thioredoxin reductase 3Q99MD6Details
Thioredoxin reductase 2, mitochondrialQ9JLT4Details
Thioredoxin reductase 1, cytoplasmicQ9JMH6Details
Serine/threonine-protein kinase 38Q91VJ4Details
E3 ubiquitin-protein ligase Mdm2P23804Details