Curated Information

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PubMed Id: 11877457

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.

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

T156-p - AP2M1 (human)

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Orthologous residues

AP2M1 (human): T156‑p, AP2M1 iso2 (human): T154‑p, AP2M1 (mouse): T156‑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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