LSD1

Lysine (K)-specific demethylase 1A (LSD1) is a is_associated_with::protein in humans that is encoded by the KDM1A is_associated_with::gene. LSD1 is a flavin-dependent is_associated_with::monoamine oxidase, which can is_associated_with::demethylate mono- and di-methylated is_associated_with::lysines, specifically is_associated_with::histone 3, lysines 4 and 9 (H3K4 and H3K9).

Structure
This gene encodes a nuclear protein containing a SWIRM domain, a is_associated_with::FAD-binding motif, and an is_associated_with::amine oxidase domain. This protein is a component of several is_associated_with::histone deacetylase complexes, though it silences genes by functioning as a histone demethylase.

Function
LSD1 (lysine-specific demethylase 1), also known as KDM1, is the first of several protein is_associated_with::lysine demethylases discovered. Through a FAD-dependent oxidative reaction, LSD1 speficially removes histone H3K4me2 to H3K4me1 or H3K4me0. When forming a complex with is_associated_with::androgen receptor (and possibly other is_associated_with::nuclear hormone receptors), LSD1 changes its substrates to H3K9me2. It's now known LSD1 complex mediates a coordinated is_associated_with::histone modification switch through enzymatic activities as well as histone modification readers in the complex.