UniProt ID: Q803I8 |
FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system also called ER- associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins. Protects cells from ER stress-induced apoptosis. Sequesters p53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis (By similarity). {ECO:0000250|UniProtKB:Q86TM6}. 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:Q86TM6}; PATHWAY: Protein modification; protein ubiquitination. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q86TM6}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86TM6}. DOMAIN: The RING-type zinc finger is required for E3 ligase activity. {ECO:0000250}. SIMILARITY: Belongs to the HRD1 family. {ECO:0000305}. SEQUENCE CAUTION: Sequence=AAH44465.1; Type=Frameshift; Evidence={ECO:0000305}; |
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