Sorting nexin 9 (SNX9) has been suggested to be involved in the endocytic process as an accessory factor. SNX9 has binding sites for both clathrin and adaptor protein AP-2 in a low complexity region, and binds dynamin-2 (Dyn2) by its SH3 domain. SNX9 has its own membrane-binding activity, mediated by a carboxyl-terminal region containing the PX domain and the BAR domain. Endogenous SNX9 partially co-localizes with AP-2 and Dyn2 at the plasma membrane, and over expression in K562 and HeLa cells of truncated versions of SNX9 inhibits the uptake of transferrin. Moreover, SNX9 is required for efficient clathrin-mediated endocytosis, which suggests that it functions to regulate dynamin activity.SNXs are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNX9 also contains a BAR and a SH3 domain. This entry represents the SH3 domain of SNX9.