UBX domain-containing protein 4 (UBXN4)

UBX domain-containing protein 4 (UBXN4) is an integral membrane protein predominantly located in the endoplasmic reticulum and nuclear envelope, with both N- and C- termini oriented toward the cytoplasm or nucleoplasm[1]. UBXN4 is a highly conserved member of the UBX family of proteins, defined by the presence of the UBX (ubiquitin regulatory X) domain, a ubiquitin-like fold that mediates protein-protein interactions. Its primary molecular function is as a cofactor for the AAA-ATPase valosin-containing protein (VCP/p97), a key chaperone in ER-associated protein degradation (ERAD)[1][6][3][7]. UBXN4 binds both UBQLN1 and VCP, thereby acting as an adaptor or platform for assembly of the ERAD machinery and facilitating the targeted degradation of misfolded or damaged proteins in the ER[6]. Its expression is widely detected in many tissues and is induced by ER stress. UBXN4 has been implicated in processes such as autophagy and the cellular stress response, and is being investigated as a potential target in cancer therapy due to its regulatory role in protein quality control and emerging association with cancer cell biology[1][3]. There is no evidence of direct small-molecule drugs targeting UBXN4, and no clear mechanism-of-action or safety issues specific to this protein have been reported in the literature.

Other names

ErasinUBXD2UBXDC1KIAA0242