Curated Information
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Curated Information Page
PubMed Id: 10022832 
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.
Hoffmann R, et al. (1999) The MAP kinase ERK2 inhibits the cyclic AMP-specific phosphodiesterase HSPDE4D3 by phosphorylating it at Ser579. EMBO J 18, 893-903 10022832
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S578-p - PDE4D iso2 (human)
Orthologous residues
PDE4D (human): S715‑p, PDE4D iso2 (human): S578‑p, PDE4D iso4 (human): S490‑p, PDE4D iso5 (human): S413‑p, PDE4D iso6 (human): S651‑p, PDE4D iso7 (human): , PDE4D (mouse): S654‑p, PDE4D iso3 (mouse): S491‑p, PDE4D iso4 (mouse): , PDE4D iso9 (mouse): , PDE4D (rat): S710‑p, PDE4D iso8 (rat): S652‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, immunoprecipitation, mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial), COS (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  monkey
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK2 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK2 (human) activation of upstream enzyme, pharmacological inhibitor of upstream enzyme
Downstream Regulation
 Effect of modification (function):  enzymatic activity, inhibited
 Comments:  regulates levels of intracellular cAMP


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