MassIVE MSV000081226

Complete Public PXD006902

Quantitative chemical proteomic profiling of phosphoprotein phosphatases

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Description

We have developed a chemical proteomic strategy for the systematic interrogation of endogenous phosphoprotein phosphatases (PPP) and their interacting proteins, including regulatory and scaffolding subunits, and substrates (the 'PPPome'). PPPs are captured using an immobilized non-selective PPP inhibitor, followed by identification and quantification by mass spectrometry. Using this approach, we map the PPPome in human cancer cell lines, mouse tissues, and yeast species, identify cell and tissue type specific PPP expression patterns, and discover new PPP interacting proteins. [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: PPP ; phosphoprotein phosphatases ; PPPome ; quantitative ; proteomics ; human cancer cell lines ; A172 ; T47D ; MCF7 ; SKBR3 ; expression ; interaction

Contact

Principal Investigators:
(in alphabetical order) 		Arminja Kettenbach, The Geisel School of Medicine at Dartmouth, United States
Submitting User: madamo

Publications

Lyons SP, Jenkins NP, Nasa I, Choy MS, Adamo ME, Page R, Peti W, Moorhead GB, Kettenbach AN.
A Quantitative Chemical Proteomic Strategy for Profiling Phosphoprotein Phosphatases from Yeast to Humans.
Mol. Cell Proteomics. Epub 2018 Sep 18.

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Number of distinct proteins found to be differentially abundant in at least one comparison across all analyses (original submission and reanalyses) associated with this dataset.

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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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