Curated Information
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Curated Information Page
PubMed Id: 11723108 
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.
Lu PJ, et al. (2002) Critical role of WW domain phosphorylation in regulating phosphoserine binding activity and Pin1 function. J Biol Chem 277, 2381-4 11723108
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S16-p - Pin1 (human)
Orthologous residues
Pin1 (human): S16‑p, Pin1 (mouse): S16‑p, Pin1 (rat): S16‑p
Characterization
 Methods used to characterize site in vivo 2D analysis, [32P] bio-synthetic labeling, mutation of modification site, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  HeLa (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKACA (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKACA (human) mutation in upstream enzyme recognition motif, pharmacological activator of upstream enzyme, phosphoaminoacid analysis
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
forskolin increase
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Effect of modification (process):  cell cycle regulation


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