Ankyrin repeat and MYND domain containing 1 (ANKMY1)

Ankyrin repeat and MYND domain containing 1 (ANKMY1) is a large, conserved protein encoded by the ANKMY1 gene in humans, comprising 941 amino acids. The protein's structure features seven ankyrin repeats, three MORN (Membrane Occupation and Recognition Nexus) domains, and a C-terminal MYND-type zinc finger domain, reflecting its prominent role in protein-protein interactions and regulatory assembly. ANKMY1 is broadly expressed in human tissues and localizes primarily in the cytosol with shuttling capacity to the nucleus, suggesting roles in cytoplasmic signaling and potentially transcriptional control. Functionally, the protein interacts with various partners involved in cytoskeletal reorganization, transcriptional regulation, cell adhesion, and stress responses. Clinically, alterations in the ANKMY1 gene, especially hyper- or hypomethylation and missense mutations, have been implicated in cancer pathogenesis, with specific links to osteosarcoma prognosis and metabolic regulation in adipose tissue. While ANKMY1 has notable research interest due to its interaction network and disease associations, it is not currently recognized as a direct therapeutic drug target [1][2][3].

Other names

ZMYND13Ankyrin repeat and MYND domain protein 1Zinc finger myeloid, nervy and DEAF-1 domain containing protein 1