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Background:Acetyl‑Histone H3 (Lys37), abbreviated as H3K37ac, corresponds to lysine acetylation at lysine‑37 near the boundary between the flexible N‑terminal tail and globular core domain of histone H3. This modification is detectable across plants, yeast and human cells by high‑depth mass‑spectrometry. Functional evidence is well‑established in plant stress response, while mammalian mechanistic data remain limited. Dedicated writer and reader proteins are not fully characterized; site‑specific knock‑in/knock‑out mammalian models are absent.
