Ring finger protein, transmembrane 2 (RNFT2)

Ring finger protein, transmembrane 2 (RNFT2) is a membrane-associated E3 ubiquitin-protein ligase characterized by a RING finger domain, mediating the covalent attachment of ubiquitin to target substrate proteins[1][3][4][5][6]. RNFT2 is predicted to play a role in the positive regulation of the endoplasmic-reticulum-associated degradation (ERAD) pathway and is involved in the negative regulation of cytokine signaling, including IL3-dependent cellular responses, likely through ubiquitination and degradation of IL3RA (interleukin-3 receptor alpha chain), thereby exerting anti-inflammatory effects[3][8]. RING finger proteins such as RNFT2 are widely implicated in cellular processes, including protein homeostasis, signal transduction, and immune modulation, and their dysregulation is associated with diverse disease states such as cancer, inflammation, and neurodegeneration[2][4]. Expression of RNFT2 is observed in several tissues, most abundantly in the central nervous system[7]. While E3 ligases as a family are considered therapeutic targets and have attracted interest for drug discovery, no specific drugs or biomarkers are currently documented for RNFT2 itself.

Other names

E3 ubiquitin-protein ligase RNFT2TMEM118FLJ14627RING finger and transmembrane domain-containing protein 2Transmembrane protein 118

Modulation of ubiquitination and proteasomal degradation of target proteins; Negative regulation of cytokine receptor-mediated signaling; Regulation of protein stability at the membrane.