E3 ubiquitin-protein ligase RNF38 (RNF38)

E3 ubiquitin-protein ligase RNF38 (RNF38) is a member of the RING finger protein family, characterized by a RING-H2 zinc-binding domain and a coiled-coil motif[4][7]. RNF38 functions as a nuclear E3 ubiquitin ligase; it interacts with the tumor suppressor p53, promoting its ubiquitination both in vitro and in vivo, and potentially altering its localization and function[1][2][7]. RNF38 also mediates ubiquitination of the transcription factor RUNX1, thereby stabilizing RUNX1 and enhancing its ability to repress erythroid differentiation[5]. RNF38 is implicated in the regulation of key cellular processes such as the cell cycle, apoptosis, and transcriptional modulation. Its gene is broadly expressed in human tissues, with known localization to chromosome 9p13—a region frequently deleted or altered in various cancers—indicating potential involvement in oncogenesis or tumor suppression[1][3][4]. RNF38 is not currently known to interact with any approved drugs, and no clinically validated biomarkers or therapeutic agents targeting this molecule have been reported.

Other names

RING finger protein 38RING-type E3 ubiquitin transferase RNF38

Ubiquitination of substrate proteins (e.g., p53, RUNX1) modulating their stability or activity