Curated Information
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Curated Information Page
PubMed Id: 11516654 
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.
Olusanya O, Andrews PD, Swedlow JR, Smythe E (2001) Phosphorylation of threonine 156 of the mu2 subunit of the AP2 complex is essential for endocytosis in vitro and in vivo. Curr Biol 11, 896-900 11516654
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T156-p - AP2M1 (rat)
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 mutation of modification site
 Relevant cell lines - cell types - tissues:  HeLa (cervical) [AP2M1 (rat)]
 Cellular systems studied:  cell lines
 Species studied:  human
 Comments:  The authors state that they identified the in vitro phosphorylation site as T156, data not shown.
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Comments:  T156A mutants are defective in the endocytosis of labelled transferrin. Although the paper demonstrates a functional correlation between T156 and endocytosis, it does not directly prove that this effect is due to phosphorylation.


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