Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Curated Information Page
PubMed Id: 12417592 
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.
Hsieh-Wilson LC, et al. (2003) Phosphorylation of spinophilin modulates its interaction with actin filaments. J Biol Chem 278, 1186-94 12417592
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
Download Sites

S94-p - Spinophilin (rat) ▲
Orthologous residues
Spinophilin (human): S94‑p, Spinophilin (mouse): S94‑p, Spinophilin (rat): S94‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mass spectrometry, peptide sequencing, phospho-antibody, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  'neuron, neostriatal'-brain, 293 (epithelial) [Spinophilin (rat)]
 Cellular systems studied:  cell lines, primary cultured cells
 Species studied:  rat
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE PKACa (human)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
forskolin increase
SKF81297 increase
quinpirole no change compared to control
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Comments:  Phospho-S94 is enriched in membrane fractions and PSDs.

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:  [32P] bio-synthetic labeling, mass spectrometry, peptide sequencing, phospho-antibody, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  'neuron, neostriatal'-brain, 293 (epithelial) [Spinophilin (rat)]
 Cellular systems studied:  cell lines, primary cultured cells
 Species studied:  rat
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE PKACa (human)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
forskolin no change compared to control

S177-p - Spinophilin (rat) ▲
Orthologous residues
Spinophilin (human): G175‑p, Spinophilin (mouse): G177‑p, Spinophilin (rat): S177‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mass spectrometry, peptide sequencing, phospho-antibody, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  'neuron, neostriatal'-brain, 293 (epithelial) [Spinophilin (rat)]
 Cellular systems studied:  cell lines, primary cultured cells
 Species studied:  rat
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE PKACa (human)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
forskolin increase
SKF81297 increase
quinpirole no change compared to control
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Comments:  Phospho S177 is enriched in the cytosol and absent in PSDs.


Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.