HEATR5B is a component of clathrin-coated vesicles (Hirst et al. 2005.  More specifically, it is a omponent of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes. It promotes association of Adaptor Protein 1 (AP1) with endosomal membranes independently of dynein. Thus, HEATR5B co-ordinates multiple events in AP1-based trafficking (Madan et al. 2023). Its hydropathy plot reveals many peaks of hydrophobicity (> 10) that could be transmembrane helices although these were not predicted using the WHAT program.