Curated Information
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Curated Information Page
PubMed Id: 22727668 
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.
Zhou Z, et al. (2012) The Akt-SRPK-SR Axis Constitutes a Major Pathway in Transducing EGF Signaling to Regulate Alternative Splicing in the Nucleus. Mol Cell 47, 422-33 22727668
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.
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S33-p - SRPK1 (human)
Orthologous residues
SRPK1 (human): S33‑p, SRPK1 (mouse): S33‑p, SRPK1 (rat): S33‑p
Characterization
 Methods used to characterize site in vivo mass spectrometry, mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE SRPK1 (human)
 Comments:  autophosphorylation-T326 and S587 are only autophosphorylated in the presence of activated Akt.
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE SRPK1 (human) phosphopeptide analysis

S309-p - SRPK1 (human)
Orthologous residues
SRPK1 (human): S309‑p, SRPK1 (mouse): S309‑p, SRPK1 (rat): S309‑p
Characterization
 Methods used to characterize site in vivo mass spectrometry, mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE SRPK1 (human)
 Comments:  autophosphorylation-T326 and S587 are only autophosphorylated in the presence of activated Akt.
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE SRPK1 (human) phosphopeptide analysis

T326-p - SRPK1 (human)
Orthologous residues
SRPK1 (human): T326‑p, SRPK1 (mouse): T326‑p, SRPK1 (rat): T326‑p
Characterization
 Methods used to characterize site in vivo mass spectrometry, mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE SRPK1 (human)
 Comments:  autophosphorylation-T326 and S587 are only autophosphorylated in the presence of activated Akt.
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE SRPK1 (human) phosphopeptide analysis
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Effect of modification (process):  RNA splicing, induced
 Comments:  translocation to the nucleus-regulation of E1A splicing

S587-p - SRPK1 (human)
Orthologous residues
SRPK1 (human): S587‑p, SRPK1 (mouse): S580‑p, SRPK1 (rat): S587‑p
Characterization
 Methods used to characterize site in vivo mass spectrometry, mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE SRPK1 (human)
 Comments:  autophosphorylation-T326 and S587 are only autophosphorylated in the presence of activated Akt.
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Effect of modification (process):  RNA splicing, induced
 Comments:  translocation to the nucleus-regulation of E1A splicing


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