E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation (PubMed:
12459480, PubMed:
12646171, PubMed:
12975321, PubMed:
14593114, PubMed:
16289116, PubMed:
16847254, PubMed:
17059562, PubMed:
17141218, PubMed:
17170702, PubMed:
22607976, PubMed:
26471130, PubMed:
28827405). 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 (PubMed:
12459480, PubMed:
12646171, PubMed:
12975321, PubMed:
14593114, PubMed:
16289116, PubMed:
16847254, PubMed:
17059562, PubMed:
17141218, PubMed:
17170702, PubMed:
22607976, PubMed:
26471130, PubMed:
28842558). Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation (PubMed:
17141218). Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis (PubMed:
17170702). Mediates the ubiquitination and subsequent degradation of cytoplasmic NFE2L1 (By similarity). During the early stage of B cell development, required for degradation of the pre-B cell receptor (pre-BCR) complex, hence supporting further differentiation into mature B cells (By similarity).
