Choi EK, et al. (2003) Phosphorylation of calsenilin at Ser63 regulates its cleavage by caspase-3. Mol Cell Neurosci 23, 495-506 12837631

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.

Click on the protein name to open the protein page, and on the RSD number to open the site page.

Download

S63-p - calsenilin (human) ▲

Modsite: APQGSDSsDSELELS SwissProt Entrez-Gene Orthologous residues calsenilin (human): S63‑p, calsenilin (mouse): S63‑p, calsenilin (rat): S63‑p Characterization Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, electrophoretic mobility shift, mutation of modification site, phospho-antibody Relevant cell lines - cell types - tissues:  H4 (glial), SH-SY5Y (neural crest) Cellular systems studied:  cell lines Species studied:  human Enzymes shown to modify site in vitro:  Type Enzyme KINASE CK1A (human) Upstream Regulation Treatments, proteins and their effect on site modification:  Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes calyculin_A increase thapsigargin increase okadaic_acid increase phorbol_ester no change compared to control staurosporine no change compared to control colforsin no change compared to control FK506 no change compared to control ciclosporin no change compared to control Downstream Regulation Effect of modification (function):  protein processing Comments:  Phosphorylation of calsenilin at Ser-63 inhibits cleavage of the molecule by caspase-3.

S63-p - calsenilin (mouse) ▲
Modsite: APQGsDssDsELELS SwissProt Entrez-Gene Orthologous residues calsenilin (human): S63‑p, calsenilin (mouse): S63‑p, calsenilin (rat): S63‑p