Anti-SYVN1/HRD1 antibody

Target data

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).