VCP/p97 is a member of the large family of ATP-hydrolyzing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. It belongs to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily and contains two ATPase domains (D1-2). It can convert the energy of ATP hydrolysis to structurally remodel or unfold client proteins. ATP hydrolysis in D2 seems to generate the main driving force. A globular N-domain that resides at the periphery of D1 is essential for substrate binding. It can stabilize unfolded proteins, may regulate ATP hydrolysis and even couple substrate and adaptor binding to ATP hydrolysis. Although VCP/p97 associates with a large number of interaction partners and protein cofactors, the largest family of cofactors are proteins containing a ubiquitin-X (UBX) domain or UBX-like domain1, and that its key function is to unfold proteins and disassemble protein complexes,.
ATPases listed: ATPase (cardiac specific myosin), ATPase (p97), ATPase (H+/K+), ATPase (Na+/K+)
 H. Meyer, M. Bug, S. Bremer. Emerging functions of theVCP/p97 AAA-ATPase in the ubiquitin system. Nat. Cell Biol. 2012, 14, 117-123.
 K. Yamanaka, Y. Sasagawa, T. Ogura. Recent advances in p97/VCP/Cdc48 cellular functions. Biochim. Biophys. Act. Mol. Cell Res. 2012, 1823, 130-137.