RNF185
Domain
The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity.
Function
E3 ubiquitin-protein ligase that regulates selective mitochondrial autophagy by mediating 'Lys-63'-linked polyubiquitination of BNIP1 (PubMed:21931693). Acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and subsequent proteasome-mediated degradation (PubMed:27485036). Protects cells from ER stress-induced apoptosis (PubMed:27485036). Responsible for the cotranslational ubiquitination and degradation of CFTR in the ERAD pathway (PubMed:24019521). Also acts as a regulator of the innate antiviral response by catalyzing 'Lys-27'-linked polyubiquitination of CGAS at 'Lys-173' and 'Lys-384', thereby promoting CGAS cyclic GMP-AMP synthase activity (PubMed:28273161). Preferentially associates with the E2 enzymes UBE2J1 and UBE2J2 (PubMed:24019521).
Pathway
Protein modification; protein ubiquitination.
Tissue Specificity
Ubiquitously expressed.
Cellular localization
- Mitochondrion outer membrane
- Multi-pass membrane protein
- Endoplasmic reticulum membrane
- Multi-pass membrane protein
Alternative names
E3 ubiquitin-protein ligase RNF185, RING finger protein 185, RNF185