Curated Information
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Curated Information Page
PubMed Id: 16488886 
Marcinkiewicz A, Gauthier D, Garcia A, Brasaemle DL (2006) The phosphorylation of serine 492 of perilipin a directs lipid droplet fragmentation and dispersion. J Biol Chem 281, 11901-9 16488886
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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S492-p - perilipin (mouse)
Orthologous residues
perilipin (human): S497‑p, perilipin (mouse): S492‑p, perilipin (rat): S492‑p, perilipin iso2 (rat):
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout]
 Cellular systems studied:  cell lines
 Species studied:  mouse
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKACA (human) phospho-motif antibody
Downstream Regulation
 Effect of modification (function):  activity, induced
 Comments:  phosphorylation of site facilitates lipolysis of lipid droplets.


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