Curated Information
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Home > Curated Information Page > PubMed Id: 1312697
Saksela K, et al. (1992) Activation of protein kinase C increases phosphorylation of the L-myc trans-activator domain at a GSK-3 target site. Oncogene 7, 347-53 1312697
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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S38-p - L-Myc (human)
Modsite: KKFELVPsPPtsPPW SwissProt Entrez-Gene
Orthologous residues
L‑Myc (human): S38‑p, L‑Myc (mouse): S38‑p
Characterization
Methods used to characterize site in vivo [32P] bio-synthetic labeling, immunoprecipitation, mutation of modification site
Relevant cell lines - cell types - tissues:  COS (fibroblast)
Cellular systems studied:  cell lines
Species studied:  green monkey
Enzymes shown to modify site in vitro
Type Enzyme
KINASE GSK3B (human)
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
okadaic_acid increase
phorbol_ester increase

S42-p - L-Myc (human)
Modsite: LVPsPPtsPPWGLGP SwissProt Entrez-Gene
Orthologous residues
L‑Myc (human): S42‑p, L‑Myc (mouse): S42‑p
Characterization
Methods used to characterize site in vivo [32P] bio-synthetic labeling, immunoprecipitation, mutation of modification site
Relevant cell lines - cell types - tissues:  COS (fibroblast)
Cellular systems studied:  cell lines
Species studied:  green monkey
Enzymes shown to modify site in vitro
Type Enzyme
KINASE GSK3B (human)
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
okadaic_acid increase
phorbol_ester increase