Curated Information
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Home > Curated Information Page > PubMed Id: 10657242
Liu J, et al. (2000) Mutations of the serine phosphorylated in the protein phosphatase-1-binding motif in the skeletal muscle glycogen-targeting subunit. Biochem J 346 Pt 1, 77-82 10657242
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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S67-p - PPP1R3A (rabbit)
Modsite: SSGGRRVsFADNFGF SwissProt Entrez-Gene
Orthologous residues
PPP1R3A (human): S65‑p, PPP1R3A iso100 (human): S65‑p, PPP1R3A (mouse): S67‑p, PPP1R3A (rat): S67‑p, PPP1R3A (rabbit): S67‑p
Characterization
Methods used to characterize site in vivo mutation of modification site
Relevant cell lines - cell types - tissues:  COS (fibroblast)
Cellular systems studied:  cell lines
Species studied:  green monkey
Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKACA (human)
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
PPP1CA (human) Disrupts pull-down assay, co-immunoprecipitation