Component of clathrin-coated vesicles (PubMed:15758025). Component 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 (PubMed:15758025). Self-associates (PubMed:15758025). Interacts with GGA1 (via GAE domain) (PubMed:14665628, PubMed:15758025). Interacts with GGA3 (via GAE domain), AP1G1 (via GAE domain) and AP1G2 (via GAE domain) (PubMed:14665628). Component of the aftiphilin/p200/gamma-synergin complex, at least composed of AFTPH/aftiphilin, HEATR5B/p200a and SYNRG/gamma-synergin, which plays a role in the AP1G1/AP-1-mediated protein trafficking from early to recycling endosomes (PubMed:15758025). Within the complex interacts with HEATR5B/p200a and SYNRG/gamma-synergin; the interactions are direct (PubMed:15758025). Interacts with AP1G1/AP-1; the interaction is required to recruit AFTPH/aftiphilin to the perinuclear region of the cell (PubMed:15758025). Interacts with CLTCL1/Clathrin (PubMed:15758025). Co-localizes with AP1G1/AP-1 in the cytoplasm (PubMed:14665628, PubMed:15758025). Recruited to the perinuclear region by AP1G1/AP-1 (PubMed:15758025). The WXXF motifs mediate binding of accessory proteins to the ear-domain of AP-1, GGAs and AP-2 through hydrophobic interactions. Selective binding to the GAE domains of AP-1 or to the alpha-ear domain of AP-2 is tuned by the acidic context surrounding the motif and the properties of the second residue of the motif itself (By similarity). May be due to intron retention. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus.