Curated Information
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Home > Curated Information Page > PubMed Id: 9516477
Venema RC, et al. (1998) Angiotensin II-induced association of phospholipase Cgamma1 with the G-protein-coupled AT1 receptor. J Biol Chem 273, 7703-8 9516477
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, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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Y319-p - AT1 (human)
Modsite: YFLQLLKyIPPKAKS SwissProt Entrez-Gene
Orthologous residues
AT1 (human): Y319‑p, AT1 (mouse): Y319‑p, AT1 (rat): Y319‑p
Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
Relevant cell lines - cell types - tissues:  VSMC-aorta
Cellular systems studied:  primary cultured cells
Species studied:  rat
Enzymes shown to modify site in vitro
Type Enzyme
KINASE Src (human)
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
angiotensin increase
vanadate, angiotensin angiotensin augment treatment-induced increase
PP1, angiotensin angiotensin inhibit treatment-induced increase
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
PLCG1 (human) SH2 Induces in vitro, co-immunoprecipitation