Ribosomal oxygenase 2 (RIOX2)

Ribosomal oxygenase 2 (RIOX2), also known as MINA53, is a Jumonji domain-containing oxygenase that acts as a bifunctional enzyme with both histone lysine demethylase and ribosomal histidine hydroxylase activities[3]. RIOX2 demethylates trimethylated lysine-9 on histone H3 (H3K9me3), leading to increased ribosomal RNA expression, and hydroxylates histidine-39 of the 60S ribosomal protein L27a, implicating it in ribosome biogenesis[3]. RIOX2 is a downstream target of the oncogene MYC and is strongly overexpressed in several cancers, especially prostate cancer, where upregulation correlates with poor prognosis, high Gleason scores, TP53 mutations, and advanced disease stage[1]. Its protein levels can serve as biomarker for cancer prognosis. RIOX2 is not directly regulated by androgen receptor signaling but is strongly associated with AR activity in castration-resistant prostate cancer, and its expression is modulated by epigenetic factors including promoter hypomethylation[1]. There are no currently approved drugs specifically targeting RIOX2.

Other names

MINA53MINAMDIGNO52JMJD10Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINAHistone lysine demethylase MINA60S ribosomal protein L27a histidine hydroxylaseMYC-induced nuclear antigenMineral dust-induced gene proteinNucleolar protein 52Ribosomal oxygenase MINAFLJ14393