[8] Its name derives from the fact that it is highly expressed in units of tubular myofibrils known as sarcomeres and is a large protein, at 2,324 amino acids.

[9] Myomegalin is mostly composed of alpha-helix and coiled-coil structures and has domains shared with microtubule-associated proteins.

The CM-MMG isoform binds at the centrosome with γ-tubulin in an AKAP9-dependent manner and on the near side of the Golgi apparatus, while the EB-MMG isoform binds with MAPRE1 at the Golgi apparatus and increases MAPRE1's effects on microtubule growth.

[8] Orthologues of myomegalin are seen in vertebrates as far back as bony fish, around 450 million years ago.

In mammals, around 200 million years ago, myomegalin gained an Olduvai domain.