Curated Information
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Curated Information Page
PubMed Id: 22020126 
Yuan H, et al. (2012) MYST protein acetyltransferase activity requires active site lysine autoacetylation. EMBO J 31, 58-70 22020126
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, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
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K274-ac - MYST1 (human)
Orthologous residues
MYST1 (human): K274‑ac, MYST1 (mouse): K274‑ac, MYST1 (rat): K274‑ac
 Methods used to characterize site in vivo mass spectrometry, mutation of modification site
 Disease tissue studied:  lung cancer, non-small cell lung cancer
 Relevant cell lines - cell types - tissues:  E.coli (bacterial), NCI-H1299 (pulmonary)
 Cellular systems studied:  cell lines
 Species studied:  bacteria, human
 Enzymes shown to modify site in vitro
Type Enzyme
 Comments:  autoacetylation
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
ACETYLTRANSFERASE MYST1 (human) autoacetylation
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced, protein conformation

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