Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Curated Information Page
PubMed Id: 11516654 
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
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.
Download Sites

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
 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.

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.