Curated Information
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Curated Information Page
PubMed Id: 18818105 
This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
Zhong B, et al. (2008) The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation. Immunity 29, 538-50 18818105
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S358-p - TMEM173 (human)
Orthologous residues
TMEM173 (human): S358‑p, TMEM173 (mouse): S357‑p, TMEM173 iso2 (mouse): S406‑p
Characterization
 Methods used to characterize site in vivo mass spectrometry, mutation of modification site, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  293 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE TBK1 (human) transfection of wild-type enzyme, genetic knockout/knockin of upstream enzyme, co-immunoprecipitation, transfection of inactive enzyme, mutation in upstream enzyme recognition motif
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
virus infection increase
Downstream Regulation
 Effect of modification (function):  activity, induced, molecular association, regulation
 Comments:  activates IRF-E and enhances interaction between TBK1 and IRF3.


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