Curated Information
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Curated Information Page
PubMed Id: 11076974 
Kamsteeg EJ, Heijnen I, van Os CH, Deen PM (2000) The subcellular localization of an aquaporin-2 tetramer depends on the stoichiometry of phosphorylated and nonphosphorylated monomers. J Cell Biol 151, 919-30 11076974
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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S256-p - AQP2 (human)
Orthologous residues
AQP2 (human): S256‑p, AQP2 (mouse): S256‑p, AQP2 (rat): S256‑p
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, immunoprecipitation, mutation of modification site, western blotting
 Relevant cell lines - cell types - tissues:  oocyte [CPEB (mouse)]
 Cellular systems studied:  primary cells
 Species studied:  frog
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
cAMP analog no change compared to control
H-89 no change compared to control
Downstream Regulation
 Effect of modification (function):  intracellular localization, molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
AQP2 (human) Induces molecular association, regulation electrophoretic visualization
 Comments:  S256-p is found in the plasma membrane in a tetramer, in which 3 out of 4 monomers must be phosphorylated for localization.

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