| ASAP2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Aliases | ASAP2, AMAP2, CENTB3, DDEF2, PAG3, PAP, Pap-alpha, SHAG1, ArfGAP with SH3 domain, ankyrin repeat and PH domain 2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 603817; MGI: 2685438; GeneCards: ASAP2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
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Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 is a protein that in humans is encoded by the ASAP2 gene.
This gene encodes a multidomain protein containing an N-terminal alpha-helical region with a coiled-coil motif, followed by a pleckstrin homology (PH) domain, an Arf-GAP domain, an ankyrin homology region, a proline-rich region, and a C-terminal Src homology 3 (SH3) domain. The protein localizes in the Golgi apparatus and at the plasma membrane, where it colocalizes with protein tyrosine kinase 2-beta (PTK2B). The encoded protein forms a stable complex with PTK2B in vivo. This interaction appears to be mediated by binding of its SH3 domain to the C-terminal proline-rich domain of PTK2B. The encoded protein is tyrosine phosphorylated by activated PTK2B. In vitro it shows strong GTPase-activating protein (GAP) activity towards the small GTPases ADP-ribosylation factor (ARF) 1 and ARF5 and weak activity towards ARF6. The encoded protein is believed to function as an ARF GAP that controls ARF-mediated vesicle budding when recruited to Golgi membranes. In addition, it functions as a substrate and downstream target for PTK2B and SRC, a pathway that may be involved in the regulation of vesicular transport.