The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM72 (tripartite motif containing 72), also known as MG53, is a 477 amino acid cytoplasmic vesicle membrane protein that belongs to the TRIM/RBCC family. Existing as a homooligomer, TRIM72 contains one B box-type zinc finger, one B30.2/SPRY domain and a RING-type zinc finger. TRIM72 is considered a muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. TRIM72 is required for transport of dysferlin to sites of cell injury during repair patch formation. TRIM72 also regulates membrane budding and exocytosis and may be involved in the regulation of the mobility of KV2.1-containing endocytic vesicles. TRIM72 exists as two alternatively spliced isoforms and is encoded by a gene located on human chromosome 16p11.2.