Curated Information
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Home > Curated Information Page > PubMed Id: 16300646
Uematsu K, et al. (2005) Regulation of spinophilin Ser94 phosphorylation in neostriatal neurons involves both DARPP-32-dependent and independent pathways. J Neurochem 95, 1642-52 16300646
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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S94-p - Spinophilin (mouse)
Modsite: SDRGVRLsLPRAssL SwissProt Entrez-Gene
Orthologous residues
Spinophilin (human): S94‑p, Spinophilin (mouse): S94‑p, Spinophilin (rat): S94‑p
Methods used to characterize site in vivo phospho-antibody
Relevant cell lines - cell types - tissues:  'brain, neostriatum'
Cellular systems studied:  tissue
Species studied:  mouse
Enzymes shown to modify site in vitro
Type Enzyme
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
PHOSPHATASE PPP1CA (human) pharmacological inhibitor of upstream enzyme
PHOSPHATASE PPP2CA (human) pharmacological inhibitor of upstream enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
SKF81297 increase
quinpirole SKF81297 no effect upon treatment-induced increase
NMDA SKF81297 inhibit treatment-induced increase
CGS_21680 increase
quinpirole CGS_21680 inhibit treatment-induced increase
NMDA CGS_21680 inhibit treatment-induced increase
quinpirole decrease
okadaic_acid increase
NMDA decrease
okadaic_acid NMDA inhibit treatment-induced decrease
ciclosporin NMDA no effect upon treatment-induced decrease
AMPA decrease