EC Number   |
Natural Substrates |
|---|
   1.14.99.66 | a [histone H3]-N6,N6-dimethyl-L-lysine4 + O2 + 2 H2O |
- |
| 1.14.99.66 | histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2 |
- |
| 1.14.99.66 | histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2 |
- |
| 1.14.99.66 | more |
functional interplay between histone demethylase and histone deacetylase |
| 1.14.99.66 | more |
amine oxidase flavin-containing domain 1, AOF1, also called lysine demethylase 1B , KDM1B, is a protein related to the lysine demethylase KDM1or LSD1, it functions as a H3K4 demethylase and is required for de novo DNA methylation of some imprinted genes in oocytes |
| 1.14.99.66 | more |
LSD1 forms a complex with CoREST and histone deacetylase 1. LSD1 mediates the transrepressive function of TLX, an orphan nuclear receptor, also called NR2E1, that regulates the expression of target genes by functioning as a constitutive transrepressor, through direct interaction via its SWIRM and amine oxidase domains. Physiological significance of TLX in the cytodifferentiation of neural cells in the brain |
| 1.14.99.66 | more |
LSD1 forms a stable complex with Rb, but with E2F1, cell cycle regulatory proteins. LSD1 binds to Epstein-Barr virus C promoter Cp in a cell cycle-dependent manner, as do the the cell cycle regulatory proteins E2F1 and Rb. Rb and LSD1 binding to Cp increase after the S phase, corresponding to a decrease in histone H3 K4 methylation and Cp transcription, overview |
| 1.14.99.66 | more |
LSD1 interacts with CoREST, a co-repressor protein that binds REST and recruits other histone-modifying enzymes such as histone deacetylases 1 ? 2. The function of the LSD1CoRESThistone deacetylase subcomplex in transcriptional repression events is not limited to REST-regulated neuronal genes, but can be extended to other contexts such as hematopoietic differentiation and the telomerase reverse transcriptase genes |
| 1.14.99.66 | more |
LSD1 interacts with several interaction partners and transcription factors for performing its role in gene regulation, overview |
| 1.14.99.66 | more |
LSD1 interacts with several interaction partners and transcription factors for performing its role in gene regulation, overview. LSD1 forms a complex with CoREST, structure with bound histone H3 peptide substrate, overview. LSD1 tightly associates with the CoREST C-terminal SANT domain. This intermolecular association is mediated by the LSD1 tower domain, whose alpha-helices are embraced by a helical segment of CoREST, generating an intermolecular helical coil. The histone H3 N-terminal peptide binds deeply in the LSD1 amine oxidase domain in proximity to the flavin cofactor |
