Ring finger protein 1 (RING1)

Ring finger protein 1 (RING1), also known as E3 ubiquitin-protein ligase RING1, is an enzyme in humans encoded by the RING1 gene. It is a member of the RING finger family, characterized by a RING domain—a zinc-coordinating motif—critical for its function as an E3 ubiquitin ligase. RING1 is a core enzymatic component of the Polycomb repressive complex 1 (PRC1), mediating monoubiquitination of histone H2A at lysine 119, thereby contributing to transcriptional repression and chromatin compaction. Through its association with PRC1, RING1 plays key roles in epigenetic regulation during development, stem cell maintenance, and cell fate determination. Mutations or dysregulation of RING1 have been implicated in developmental disorders and cancers, highlighting its central role in gene silencing and epigenetic control[2][3][4][5].

Other names

E3 ubiquitin-protein ligase RING1RING1ARNF1Polycomb complex protein RING1RING-type E3 ubiquitin transferase RING1Really interesting new gene 1 protein

Inhibition of E3 ubiquitin ligase activity (theoretical/experimental, targeted for modulating chromatin state); Disruption of PRC1 complex function (theoretical target for epigenetic therapies)