Arf-GAP with SH3 domain, ankyrin repeat and PH domain-containing protein 3 (ASAP3)

Arf-GAP with SH3 domain, ankyrin repeat and PH domain-containing protein 3 (ASAP3) is a multidomain enzyme that functions as an ADP-ribosylation factor (Arf) GTPase-activating protein. Its domain architecture includes an Arf GAP, SH3, ankyrin repeat, and pleckstrin homology domains, which enable it to regulate hydrolysis of GTP bound to Arf proteins—especially ARF6, but also ARF1 and ARF5—thus inactivating them[1][2][3]. ASAP3 has critical roles in cell migration, invasion, and cytoskeletal remodeling, primarily via its impact on actin stress fibers and focal adhesion structures[1][2]. Notably, it is strongly upregulated in multiple cancers, including liver (where it was originally identified as UPLC1), breast, and colorectal carcinoma, and its increased expression is associated with enhanced migration, invasion, and metastatic potential of tumor cells[3][5]. Loss of ASAP3 impairs cytoskeletal stability and reduces cancer cell motility. While ASAP3 shows biochemical similarity to ASAP1, its cellular localization and functional roles are distinct[1][2]. There is currently no evidence of approved drugs directly targeting ASAP3 or documented safety concerns specific to its modulation. Upregulation of ASAP3 in tumors serves as a potential biomarker for poor prognosis and may indicate invasive disease progression[3].

Other names

ASAP3DDEFL1ACAP4UPLC1CENTB6Development and differentiation-enhancing factor-like 1Protein up-regulated in liver cancer 1centaurin beta 6

GTPase activation and hydrolysis of Arf proteins (ARF1, ARF5, ARF6) via acceleration of GTP hydrolysis, control of cell migration and invasion through regulation of actin stress fibers and focal adhesion dynamics[1][2][3][5]