UniProt ID: Q6PC78 |
FUNCTION: E3 ubiquitin-protein ligase that regulates selective mitochondrial autophagy by mediating 'Lys-63'-linked polyubiquitination. 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. Protects cells from ER stress-induced apoptosis. Responsible for the cotranslational ubiquitination and degradation of CFTR in the ERAD pathway. Also acts as a regulator of the innate antiviral response by catalyzing 'Lys-27'- linked polyubiquitination of CGAS, thereby promoting CGAS cyclic GMP- AMP synthase activity. Preferentially associates with the E2 enzymes UBE2J1 and UBE2J2 (By similarity). {ECO:0000250|UniProtKB:Q96GF1}. CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q96GF1}; PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q96GF1}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q96GF1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96GF1}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96GF1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96GF1}. DOMAIN: The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity. {ECO:0000250|UniProtKB:Q96GF1}. |
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