The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.
E3 ubiquitin ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their ubiquitination. Plays a role in the regulation of antiviral responses by promoting the degradation of TRAF3, TLR4 and TLR9. In turn, down-regulates NF-kappa-B and IRF3 activation as well as beta interferon production. Participates also in the regulation of autophagy by ubiquitinating BECN1 leading to its degradation and autophagy inhibition. Plays a role in ARC-dependent synaptic plasticity by mediating ARC ubiquitination resulting in its rapid proteasomal degradation (By similarity). Plays aso an essential role in spermatogenesis and male fertility (PubMed:30649198). Mechanistically, regulates meiosis by promoting the degradation of PRKACB through the ubiquitin-mediated lysosome pathway (PubMed:33724554). Modulates the gonadotropin-releasing hormone signal pathway by affecting the stability of STAU2 that is required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite (PubMed:37439148).
Protein modification; protein ubiquitination.
Auto-ubiquitinated.
Phosphorylation at Ser-719 enhances acceptor ubiquitin binding and chain-type specificity towards 'Lys-63' di-ubiquitin but not di-ubiquitin with other linkage types.
Triad3, Ubce7ip1, Uip83, Zin, E3 ubiquitin-protein ligase RNF216, RING finger protein 216, RING-type E3 ubiquitin transferase RNF216, Triad domain-containing protein 3, UbcM4-interacting protein 83, Ubiquitin-conjugating enzyme 7-interacting protein 1
Proteins
Epigenetics
104210Da
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