Curated Information
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Curated Information Page
PubMed Id: 11844797 
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.
Werz O, Szellas D, Steinhilber D, R├ądmark O (2002) Arachidonic acid promotes phosphorylation of 5-lipoxygenase at Ser-271 by MAPK-activated protein kinase 2 (MK2). J Biol Chem 277, 14793-800 11844797
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S272-p - 5-LO (human)
Orthologous residues
5‑LO (human): S272‑p, 5‑LO (mouse): S272‑p, 5‑LO (rat): S271‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial), HeLa (cervical), Mono Mac 6 (myeloid), neutrophil-blood
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE MAPKAPK2 (human)
KINASE CAMK2A (human)
KINASE PKACA (human)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
A23187 increase
fMLP increase
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced, intracellular localization


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