Curated Information
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Home > Curated Information Page > PubMed Id: 31554795
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.