HACE 1 (HECT domain and ankyrin repeat containing E3 ubiquitin protein ligase 1) is an ubiquitin ligase with six N-terminal ankyrin and a C-terminal HECT domain. HACE 1 is ubiquitously expressed in normal tissues and is frequently downregulated in human tumors. HACE 1 has been reported to act as a tumor suppressor through a phosphorylation-dependent degradation of cyclin D1. HACE1 has also been shown to bind GTP-bound Rac1 (Ras-related C3 botulinum toxin substrate 1) and to catalyze its polyubiquitination. HACE1 expression increases the ubiquitination of Rac1 when the GTPase is activated. HACE1 is required for cytotoxic necrosis factor 1 (CNSF1)-mediated depletion of Rac1 and efficient invasion of endothelial cell monolayer by bacteria, which suggests a role for HACE1 in host defense against pathogens. More recently, HACE1 was reported to target the Golgi membrane through interactions with Rab proteins. During mitotic Golgi disassembly, the ubiquitin ligase activity of HACE1 is required for subsequent post-mitotic Golgi membrane fusion.