E3 ubiquitin-protein ligase RING2 (RNF2)

E3 ubiquitin-protein ligase RING2 (RNF2) is a core component of the Polycomb Repressive Complex 1 (PRC1), functioning primarily as an epigenetic transcriptional repressor[3][5]. It catalyzes the ubiquitination of histone H2A at lysine 119, facilitating chromatin compaction and gene silencing—a process central to the regulation of developmental genes, maintenance of stem cell identity, and cell proliferation[1][3]. RNF2 exhibits E3 ubiquitin ligase activity and is involved in the targeted degradation of specific substrates, notably acting as an E3 ligase for p53 in certain cancer cell types, promoting p53 ubiquitination and proteasomal degradation[4]. RNF2 is highly expressed in various human malignancies, where its overexpression correlates with tumor growth, metastasis, and poor patient prognosis, making it both a functional contributor to oncogenesis and a potential prognostic biomarker[1]. RNF2 also interacts with a variety of partners, including transcription factors (e.g., TFCP2) and other ubiquitin system proteins (e.g., HIP2), and is essential for many normal developmental and epigenetic processes[3][5].

Other names

RING finger protein 2RING1BRING finger protein 1BHuntingtin-interacting protein 2-interacting protein 3HIPI3BAP-1protein DinGHIP2-interacting protein 3RING-type E3 ubiquitin transferase RING2

E3 ubiquitin ligase activity (adds ubiquitin to histone H2A and target proteins such as p53, promoting their degradation) Suppresses gene expression through chromatin compaction and transcriptional repression