Curated Information
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Curated Information Page
PubMed Id: 17594292 
Giamas G, et al. (2007) Phosphorylation of CK1delta: identification of Ser370 as the major phosphorylation site targeted by PKA in vitro and in vivo. Biochem J 406, 389-98 17594292
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, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
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S370-p - CK1D (rat)
Orthologous residues
CK1D (human): S370‑p, CK1D iso2 (human): S370‑p, CK1D (mouse): S370‑p, CK1D iso2 (mouse): S370‑p, CK1D (rat): S370‑p
 Methods used to characterize site in vivo 2D analysis, phospho-antibody, western blotting
 Disease tissue studied:  pancreatic cancer, pancreatic carcinoma
 Relevant cell lines - cell types - tissues:  MIA PaCa (pancreatic)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
KINASE CLK2 (human)
 Comments:  weakly phosphorylatd by PKCA and CLK2
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKACA (human) phosphopeptide analysis, pharmacological inhibitor of upstream enzyme, 2D analysis
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
forskolin increase
H-89 decrease
Downstream Regulation
 Effect of modification (function):  enzymatic activity, inhibited, intracellular localization

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