Yu T, et al. (2019) Modulation of M2 macrophage polarization by the crosstalk between Stat6 and Trim24. Nat Commun 10, 4353 31554795

This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.

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K383-ac - STAT6 (mouse) ▲

Modsite: TESVTEEkCAVLFST SwissProt Entrez-Gene Orthologous residues STAT6 (human): K383‑ac, STAT6 iso2 (human): K209‑ac, STAT6 (mouse): K383‑ac, STAT6 (rat): K383‑ac Characterization Methods used to characterize site in vivo:  flow cytometry, immunoprecipitation, mass spectrometry, modification-specific antibody, mutation of modification site, western blotting Relevant cell lines - cell types - tissues:  macrophage-bone marrow Cellular systems studied:  primary cells Species studied:  human, mouse Upstream Regulation Potential in vivo enzymes for site:  Type Enzyme Evidence Notes ACETYLTRANSFERASE CBP (mouse) siRNA inhibition of enzyme, transfection of wild-type enzyme Treatments, proteins and their effect on site modification:  Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes nicotinamide, trichostatin_A increase Downstream Regulation Effect of modification (process):  transcription, inhibited Modification regulates interactions with:  Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays Disrupts co-immunoprecipitation Comments:  Trim24-mediated Stat6 K383 acetylation disrupts Stat6–DNA association and inhibits M2 macrophage M2 polarization.