Curated Information
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Home > Curated Information Page > PubMed Id: 16421094
Klenk C, Humrich J, Quitterer U, Lohse MJ (2006) SUMO-1 controls the protein stability and the biological function of phosducin. J Biol Chem 281, 8357-64 16421094
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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K33-sm - phosducin (cow)
Modsite: INDWRKFkLESEDSD SwissProt Entrez-Gene
Orthologous residues
phosducin (human): K33‑sm, phosducin (mouse): K33‑sm, phosducin (rat): K33‑sm, phosducin (cow): K33‑sm
Methods used to characterize site in vivo electrophoretic mobility shift, modification-specific antibody, mutation of modification site, western blotting
Relevant cell lines - cell types - tissues:  293 (epithelial), COS7 (fibroblast), E.coli (bacterial), myocyte-heart, retina
Cellular systems studied:  cell lines, primary cultured cells, tissue
Species studied:  bacteria, cow, green monkey, human, rat
Enzymes shown to modify site in vitro
Type Enzyme
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
SUMO LIGASE UBC9 (human) transfection of wild-type enzyme
Downstream Regulation
Effect of modification (function):  molecular association, regulation, protein stabilization, ubiquitination
Effect of modification (process):  signaling pathway regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
G-beta 4 (human) Disrupts in vitro
Comments:  inhibits ubiquitination, regulates binding of G-beta-gamma to phosducin and G-protein-mediated signal transduction