Lysine Specific Demethylase 1B (KDM1B)

Flavin-dependent histone demethylases, such as KDM1B, regulate histone lysine methylation, an epigenetic mark that regulates gene expression and chromatin function.

The deduced mouse and human proteins contain 826 and 820 amino acids, respectively, and share 92% identity. LSD2 has a short disordered region at its N terminus, followed by several possible zinc-binding residues, a putative CW-type zinc finger domain, a central SWIRM domain, and a C-terminal catalytic amine oxidase domain. LSD2 shares significant homology with LSD1 in the catalytic domain, including conservation of residues involved in FAD and substrate binding, but LSD2 lacks the COREST (RCOR)-binding domain found in LSD1.