UBAC2

Acts as an ER-phagy receptor required for the selective autophagic degradation of endoplasmic reticulum (ER) fragments to maintain ER homeostasis and restrain ER stress-induced inflammatory responses. Its function depends on phosphorylation-induced dimerization, which enhances interaction with GABARAP and facilitates recruitment of ER fragments to autophagosomes. Restricts trafficking of FAF2 from the endoplasmic reticulum to lipid droplets. In association with LMBR1L and E3 ubiquitin-protein ligase AMFR, negatively regulates the canonical Wnt signaling pathway in the lymphocytes by promoting the ubiquitin-mediated degradation of CTNNB1 and Wnt receptors FZD6 and LRP6..

Function from UniProtKB (Q8NBM4), read 2026-09-23. CC BY 4.0.