Curated Information
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Curated Information Page
PubMed Id: 12478298 
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.
Matter N, Herrlich P, König H (2002) Signal-dependent regulation of splicing via phosphorylation of Sam68. Nature 420, 691-5 12478298
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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S58-p - Sam68 (mouse) ▲
Orthologous residues
Sam68 (human): S58‑p, Sam68 (mouse): S58‑p, Sam68 (rat): S58‑p
Characterization
 Methods used to characterize site in vivo:  mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  lymphoma, T cell lymphoma
 Relevant cell lines - cell types - tissues:  EL-4 (T lymphocyte)
 Cellular systems studied:  cell lines
 Species studied:  mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE ERK2 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK2 (mouse) modification site within consensus motif, pharmacological activator of upstream enzyme, phospho-motif antibody, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
phorbol ester increase
U0126 phorbol ester inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  activation
 Effect of modification (process):  translation, altered
 Comments:  regulates splicing

T71-p - Sam68 (mouse) ▲
Orthologous residues
Sam68 (human): A71‑p, Sam68 (mouse): T71‑p, Sam68 (rat): N71‑p
Characterization
 Methods used to characterize site in vivo:  mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  lymphoma, T cell lymphoma
 Relevant cell lines - cell types - tissues:  EL-4 (T lymphocyte)
 Cellular systems studied:  cell lines
 Species studied:  mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE ERK2 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK2 (mouse) modification site within consensus motif, pharmacological activator of upstream enzyme, phospho-motif antibody, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
phorbol ester increase
U0126 phorbol ester inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  activation
 Effect of modification (process):  translation, altered
 Comments:  regulates splicing

T84-p - Sam68 (mouse) ▲
Orthologous residues
Sam68 (human): T84‑p, Sam68 (mouse): T84‑p, Sam68 (rat): T84‑p
Characterization
 Methods used to characterize site in vivo:  mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  lymphoma, T cell lymphoma
 Relevant cell lines - cell types - tissues:  EL-4 (T lymphocyte)
 Cellular systems studied:  cell lines
 Species studied:  mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE ERK2 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK2 (mouse) modification site within consensus motif, pharmacological activator of upstream enzyme, phospho-motif antibody, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
phorbol ester increase
U0126 phorbol ester inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  activation
 Effect of modification (process):  translation, altered
 Comments:  regulates splicing


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