BM88, also known as CEND1 (cell cycle exit and neuronal differentiation protein 1), is a 149 amino acid protein that belongs to the CEND1 familly. Involved in neuroblastoma cell differentiation, BM88 is a single-pass type IV membrane protein that is neuron specific. It is suggested that BM88 forms a dimer of two identical polypeptides linked by disulfide bridges. BM88 has a central proline-rich region containing four PxxP motifs, which typically bind SRC homology-3 (SH3) domains, as well as a putative C-terminal transmembrane region, and several potential sites for N-glycosylation, myristoylation and phosphorylation. It is also suggested that a novel signaling mechanism exists by which BM88 interferes with calcium release from inositol 1,4,5-trisphosphate-sensitive stores and exerts anti-proliferative and anti-apoptotic functions. BM88 is an important molecular target for HDAC inhibition, and transcription of BM88 is induced by trichostatin-A.