Curated Information
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Curated Information Page
PubMed Id: 16230355 
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.
Luo M, et al. (2005) Phosphorylation by protein kinase a inhibits nuclear import of 5-lipoxygenase. J Biol Chem 280, 40609-16 16230355
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S524-p - 5-LO (human)
Orthologous residues
5‑LO (human): S524‑p, 5‑LO (mouse): S524‑p, 5‑LO (rat): S523‑p
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) transfection of wild-type enzyme, pharmacological activator of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
forskolin increase
IBMX forskolin augment treatment-induced increase
cAMP analog increase
H-89 cAMP analog inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  enzymatic activity, inhibited, intracellular localization
 Comments:  phosphorylation inhibits nuclear import of 5-LO, resulting in its accumulation in the cytoplasm.


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