KDM1A
| amine oxidase (flavin containing) domain 2 | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | AOF2 | ||||||
| Alt. symbols | LSD1 | ||||||
| NCBI gene | 23028 | ||||||
| HGNC | 29079 | ||||||
| OMIM | 609132 | ||||||
| RefSeq | NM_015013 | ||||||
| UniProt | O60341 | ||||||
| Other data | |||||||
| Locus | Chr. 1 p36.12 | ||||||
| |||||||
LSD1 is a gene which codes a flavin-dependent monoamine oxidase, which can demethylate mono- and di-methylated lysines, specifically histone 3, lysines 4 and 9 (H3K4 and H3K9).
See also
LSD1, discovered by Yang Shi's laboratory at Harvard Medical School and reported in Cell in December 2004, is the first of several protein lysine demethylases discovered. Through a FAD-dependent oxidative reaction, LSD1 speficially removes histone H3K4me2 to H3K4me1 or H3K4me0. When forming a complex with androgen receptor (and possibly other nuclear hormone receptors), LSD1 changes its substrates to H3K9me2. Functions of other components in LSD1 complex, such as CoREST and BHC80, have been further studied by Yang Shi's lab, as well as Ramin Shiekhattar's lab. It's now known LSD1 complex mediates a coordinated histone modification switch through enzymatic activities as well as histone modification readers in the complex.
External links
- lysine+specific+demethylase+1,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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