KDM2A
Description
The KDM2A (lysine demethylase 2A) is a protein-coding gene located on chromosome 11.
KDM2A, also known as FBXL11, is an enzyme that removes methyl groups from histone H3, specifically at lysine 36. It belongs to the family of alpha-ketoglutarate-dependent hydroxylases and contains an F-box motif, which is characteristic of proteins involved in protein ubiquitination. KDM2A is part of a protein complex called SCF (SKP1-cullin-F-box) that regulates protein degradation. KDM2A has a JmjC domain that is required for its demethylase activity. It also has a ZF-CxxC DNA binding domain that targets KDM2A to CpG islands, regions of the genome that are often involved in gene regulation. By removing methyl groups from histone H3 at CpG islands, KDM2A helps to create a chromatin environment that makes these regions more accessible to transcription factors. This helps to ensure that genes located near CpG islands are appropriately regulated.
KDM2A is a histone demethylase that specifically removes the methyl group from lysine 36 of histone H3 (H3K36me). It prefers to demethylate dimethylated H3K36 (H3K36me2) over mono- or trimethylated forms. In addition to its demethylase activity, KDM2A can recognize and bind to phosphorylated proteins, promoting their ubiquitination and degradation. KDM2A plays a crucial role in maintaining heterochromatin, a densely packed form of chromatin that is generally transcriptionally inactive. It associates with centromeres, the constricted region of a chromosome that plays a vital role in cell division, and represses the transcription of small non-coding RNAs encoded by satellite repeats located at the centromere. KDM2A is essential for centromeric integrity and genomic stability, particularly during mitosis. It also regulates circadian gene expression by suppressing the activity of CLOCK-BMAL1 heterodimer and RORA, two transcriptional activators, in a manner that does not require its demethylase activity.
KDM2A is also known as CXXC8, FBL11, FBL7, FBXL11, JHDM1A, LILINA.
