Curated Information
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Curated Information Page
PubMed Id: 11877457 
Ricotta D, et al. (2002) Phosphorylation of the AP2 mu subunit by AAK1 mediates high affinity binding to membrane protein sorting signals. J Cell Biol 156, 791-5 11877457
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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T156-p - AP2M1 (human)
Orthologous residues
AP2M1 (human): T156‑p, AP2M1 iso2 (human): T154‑p, AP2M1 (mouse): T156‑p, AP2M1 iso3 (mouse): T154‑p, AP2M1 (rat): T156‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Cellular systems studied:  primary cultured cells
 Species studied:  pig
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE AAK1 (human)
Downstream Regulation
 Effect of modification (function):  intracellular localization, molecular association, regulation
 Comments:  phosphorylation mediates high-affinity binding of AP-2 to membrane protein sorting signals.


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