Curated Information
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Curated Information Page
PubMed Id: 15228588 
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.
Grossman SD, et al. (2004) Spinophilin is phosphorylated by Ca2+/calmodulin-dependent protein kinase II resulting in regulation of its binding to F-actin. J Neurochem 90, 317-24 15228588
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S100-p - Spinophilin (rat)
Orthologous residues
Spinophilin (human): S100‑p, Spinophilin (mouse): S100‑p, Spinophilin (rat): S100‑p
Characterization
 Methods used to characterize site in vivo phospho-antibody
 Relevant cell lines - cell types - tissues:  'brain, neostriatum'
 Cellular systems studied:  tissue
 Species studied:  rat
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CAMK2A (rat)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CAMK2A (rat) inhibition of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
low Ca(2+) decrease
KN-93 decrease


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