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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 inhi...
ORGANISM(S): Neurospora Crassa (ncbitaxon:5141) Candida Albicans (ncbitaxon:5476) Saccharomyces Cerevisiae (ncbitaxon:4932) Homo Sapiens (ncbitaxon:9606) Mus Musculus (ncbitaxon:10090) Schizosaccharomyces Pombe (ncbitaxon:4896) 
2017-07-07 | MSV000081226 | MassIVE
Phosphorylation of the aquaporin-2 (AQP2) water channel at four COOH-terminal serines plays a central role in the regulation of water permeability of the renal collecting duct. The level of phosphorylation at these sites is determined by a balance between phosphorylation by protein kinases and depho...
ORGANISM(S): Rattus norvegicus (Rat) 
2018-10-26 | PXD005488 | Pride
To investigate the influence of STP and STK on protein expression in S. suis, we performed a comparative proteomics analysis with the WT, Δstp, and Δstk strains using liquid chromatography mass spectrometry/mass spectrometry (LC-MS/MS).STK and STP are serine/threonine kinases and phosphatases, respe...
ORGANISM(S): Streptococcus suis SC84 
2021-11-30 | PXD029994 | Pride
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