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Article

Aromatase is phosphorylated in situ at serine-118.

The Journal of steroid biochemistry and molecular biology - 1 Nov 2008

Miller Todd W, Shin Incheol, Kagawa Norio, Evans Dean B, Waterman Michael R, Arteaga Carlos L

Abstract excerpt

Phosphorylation of the cytochrome P450 aromatase has been proposed as a switch to rapidly modulate enzymatic activity and estrogen biosynthesis. Herein, we demonstrate that aromatase serine-118 is a potential phosphorylation site in mammalian cells. The amino acid context surrounding S118 is highly conserved among diverse animal species and suggests that an AGC-like kinase may phosphorylate aromatase. Mutation of...

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Identifiers

PMID: 18822378
DOI: 10.1016/j.jsbmb.2008.09.001
PMCID: PMC2856845

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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