Curated Information

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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, Rådmark 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

S272-p - 5-LO (human)

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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	PKACa (human)
KINASE	CaMK2-alpha (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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