FunctionE3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se.
Tissue specificityBroadly expressed, with lowest levels in brain and thymus, and highest levels detectable in heart, ovary and testis.
PathwayProtein modification; protein ubiquitination.
Sequence similaritiesBelongs to the RBR family. RNF144 subfamily. Contains 1 IBR-type zinc finger. Contains 2 RING-type zinc fingers.
DomainThe RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme (By similarity). The transmembrane domain is essential for translocation to the mitochondria upon induction of apoptosis.