LSD1 is a histone demethylase that specifically demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. LSD1 contains a SWIRM domain, a FAD-binding motif, and an amine oxidase domain. This protein is a component of several histone deacetylase complexes, though it silences genes by functioning as a histone demethylase. It acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. LSD1 demethylates both mono- and tri-methylted 'Lys-4' of histone H3. This protein may play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3 'Lys-4' on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. It may also demethylate 'Lys-9' of histone H3, a specific tag for epigenetic transcriptional repression, thereby leading to derepression of androgen receptor target genes. Mutations affecting this gene can result in cleft palate, psychomotor retardation, and distintive facial features.
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Protein Aliases: [histone H3]-dimethyl-L-lysine(4) FAD-dependent demethylase 1A; amine oxidase (flavin containing) domain 2; BRAF35-HDAC complex protein BHC110; FAD-binding protein BRAF35-HDAC complex, 110 kDa subunit; Flavin-containing amine oxidase domain-containing protein 2; lysine (K)-specific demethylase 1; lysine (K)-specific demethylase 1A; lysine-specific histone demethylase 1; Lysine-specific histone demethylase 1A; RP1-184J9.1
Gene Aliases: 1810043O07Rik; AA408884; AOF2; BHC110; CPRF; D4Ertd478e; KDM1; KDM1A; KIAA0601; LSD1; mKIAA0601
Molecular Function: oxidase