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PHD finger found in Lysine-specific demethylase 2A (KDM2A) KDM2A, also termed CXXC-type zinc finger protein 8, or F-box and leucine-rich repeat protein 11 (FBXL11), or F-box protein FBL7, or F-box protein Lilina, or F-box/LRR-repeat protein 11, or JmjC domain-containing histone demethylation protein 1A (Jhdm1a), or [Histone-H3]-lysine-36 demethylase 1A, is a ubiquitously expressed histone H3 lysine 36 (H3K36) demethylase that has been implicated in gene silencing, cell cycle, cell growth, and cancer development. It acts as a key negative regulator of gluconeogenic gene expression and plays a critical role in the invasiveness, proliferation, and anchorage-independent growth of non-small cell lung cancer (NSCLC) cells, as well as in the osteo/dentinogenic differentiation of Mesenchymal stem cells (MSCs). It regulates rRNA transcription in response to starvation. Meanwhile, it is a negative regulator of NFkappaB. Moreover, KDM2A is a heterochromatin-associated and HP1-interacting protein that promotes HP1 localization to chromatin. It is specifically recruited to CpG islands to define a unique chromatin architecture, which requires direct and specific interaction with linker DNA. It also functions as a H3K4 demethylase that regulates cell proliferation through p15 (INK4B) and p27 (Kip1) in stem cells from apical papilla (SCAPs). KDM2A belongs to the JmjC-domain-containing histone demethylase family. KDM2A consists of two Jumonji C (JmjC) domains, and FBXHA and FBXHB domains. A CXXC zinc-finger domain, followed by a plant homeodomain (PHD) finger, is located within the FBXHA domain, and an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain, is located within the FBXHB domain. |
Jiyao W et al.(2023). "The conserved domain database in 2023.",