ArfGAP with SH3 domain, ankyrin repeat and PH domain 2 (ASAP2)

ArfGAP with SH3 domain, ankyrin repeat and PH domain 2 (ASAP2) is a multidomain enzyme that contains an N-terminal coiled-coil region, a pleckstrin homology (PH) domain, an Arf-GAP domain, ankyrin repeats, a proline-rich region, and a C-terminal Src homology 3 (SH3) domain[1][3][8]. It is primarily localized in the Golgi apparatus and plasma membrane, where it plays a key role in activating small GTPases (ARF1, ARF5, ARF6), thereby regulating membrane trafficking, vesicle budding, and constitutive cellular secretion[1][2][6][9]. ASAP2 also modulates phagocytosis and cell migration by interacting with cytoskeletal proteins like paxillin and tyrosine kinases such as PYK2 and SRC[1][3]. Its enzyme activity and protein-protein interactions position it as a potential signaling regulator with relevance to cancer cell biology and possibly other pathological processes[1][2][5][6].

Other names

DDEF2KIAA0400PAG3PAPSHAG1CENTB3AMAP2Pap-alphaPaxillin-associated protein with ARF GAP activity 3Pyk2 C-terminus-associated proteinCentaurin beta 3