Curated Information
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Curated Information Page
PubMed Id: 9858547 
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.
Cacace AM, et al. (1999) Identification of constitutive and ras-inducible phosphorylation sites of KSR: implications for 14-3-3 binding, mitogen-activated protein kinase binding, and KSR overexpression. Mol Cell Biol 19, 229-40 9858547
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

T260-p - KSR (mouse) ▲
Orthologous residues
KSR (human): T272‑p, KSR (mouse): T260‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site, peptide sequencing, phosphoamino acid analysis
 Relevant cell lines - cell types - tissues:  293 (epithelial), 3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout], oocyte [CPEB (mouse)]
 Cellular systems studied:  cell lines, primary cells
 Species studied:  frog, human, mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE ERK2 (mouse)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK2 (mouse) co-immunoprecipitation, activation of upstream enzyme, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
PDGF increase
PD98059 PDGF inhibit treatment-induced increase

T274-p - KSR (mouse) ▲
Orthologous residues
KSR (human): T286‑p, KSR (mouse): T274‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site, peptide sequencing, phosphoamino acid analysis
 Relevant cell lines - cell types - tissues:  293 (epithelial), 3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout], oocyte [CPEB (mouse)]
 Cellular systems studied:  cell lines, primary cells
 Species studied:  frog, human, mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE ERK2 (mouse)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK2 (mouse) co-immunoprecipitation, activation of upstream enzyme, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
PDGF increase
PD98059 PDGF inhibit treatment-induced increase

S297-p - KSR (mouse) ▲
Orthologous residues
KSR (human): S309‑p, KSR (mouse): S297‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site, peptide sequencing, phosphoamino acid analysis
 Relevant cell lines - cell types - tissues:  293 (epithelial), 3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout], oocyte [CPEB (mouse)]
 Cellular systems studied:  cell lines, primary cells
 Species studied:  frog, human, mouse
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
PDGF no change compared to control
PD98059 PDGF no change compared to control
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
14-3-3 beta (human) Induces not reported co-immunoprecipitation

S392-p - KSR (mouse) ▲
Orthologous residues
KSR (human): S404‑p, KSR (mouse): S392‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site, peptide sequencing, phosphoamino acid analysis
 Relevant cell lines - cell types - tissues:  293 (epithelial), 3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout], oocyte [CPEB (mouse)]
 Cellular systems studied:  cell lines, primary cells
 Species studied:  frog, human, mouse
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
PDGF no change compared to control
PD98059 PDGF no change compared to control
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
14-3-3 beta (human) Induces not reported co-immunoprecipitation

S443-p - KSR (mouse) ▲
Orthologous residues
KSR (human): S456‑p, KSR (mouse): S443‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site, peptide sequencing, phosphoamino acid analysis
 Relevant cell lines - cell types - tissues:  293 (epithelial), 3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout], oocyte [CPEB (mouse)]
 Cellular systems studied:  cell lines, primary cells
 Species studied:  frog, human, mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE ERK2 (mouse)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK2 (mouse) co-immunoprecipitation, activation of upstream enzyme, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
PDGF increase
PD98059 PDGF inhibit treatment-induced increase


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