Microtubule-associated Protein 2 (MAP2) is an 1827 amino acid (aa) cytoskeletal-associated protein that contains C-terminal microtubule-binding repeats and a conserved N-terminal domain, which has been shown to interact with the RII regulatory subunit of Protein Kinase A. Human MAP2 shares 84% and 79% aa identity with the mouse and rat orthologs, respectively.
Multiple splice forms exist, resulting in four distinct isoforms with differing N-terminal domains. Mammalian MAP2 is mainly expressed in neurons, but can also be weakly detected in some non-neuronal cells including oligodendrocytes. MAP2 functions in microtubule polymerization and stabilization in both normal and malignant cell types. It has been demonstrated to play a critical role in neurite outgrowth and loss of MAP2 function in neurons may lead to neural degeneration.