3.6.4.6 A505L lethal mutation 654648 3.6.4.6 D100A mutant to study the Ca2+ sensitivity of the interaction between NSF and the glutamate receptor subunit 2 of AMPAR 688499 3.6.4.6 D142A mutant to study the Ca2+ sensitivity of the interaction between NSF and the glutamate receptor subunit 2 of AMPAR 688499 3.6.4.6 E153A mutant to study the Ca2+ sensitivity of the interaction between NSF and the glutamate receptor subunit 2 of AMPAR 688499 3.6.4.6 E209K site-directed mutagenesis 733702 3.6.4.6 E219K naturally occurring mutation, constitutes variations in surface-exposed locations 756637 3.6.4.6 E219K naturally occurring mutation, the E219K mutation leads to an almost complete loss of activity 756637 3.6.4.6 E232Q ATPase-deficient mutant 689461 3.6.4.6 E233Q a mutant protein with very low ATPase activity. In the presence of ADP recombinant mutant enzyme forms dimers. In contrast, the addition of ATP results in the formation of a large complex with at least ten subunits 724447 3.6.4.6 E233Q inactive 758466 3.6.4.6 E233Q no ATP hydrolysis, enhanced binding to Vps20p and Vta1p in vitro 656345 3.6.4.6 E233Q site-directed mutagenesis, an ATPase inactive mutant 734303 3.6.4.6 E235Q no ATPase activity, mutation leads to perturbation of various membrane transports via endosomes 656346 3.6.4.6 E243A site-directed mutagenesis, a pore loop mutant, displays essentially unchanged oligomerization, introducing E243A point mutation increases the affinity of peptide C binding by 3fold, shows reduced ATPase activity compared to the wild-type 734303 3.6.4.6 E243A/E247A site-directed mutagenesis, pore loop mutant, displays essentially unchanged oligomerization, the double mutant binds peptides 4fold (peptide C) or 10fold (peptide B) more tightly than wild-type Vps4p, shows reduced ATPase activity compared to the wild-type 734303 3.6.4.6 E247A site-directed mutagenesis, a pore loop mutant, displays essentially unchanged oligomerization, introducing E247A point mutation increases the affinity of peptide C binding by 4fold, shows reduced ATPase activity compared to the wild-type 734303 3.6.4.6 E305Q mutant assembles into oligomer like wild-type, similar ATPase activity as wild-type 656763 3.6.4.6 E305Q/E578Q no ATPase activity 656763 3.6.4.6 E329Q hydrolysis mutant 686724 3.6.4.6 E329Q in contrast to wild-type NFS E329Q mutant is enriched on various structures throughout the cell and is only minimally released by saponin permeabilization 656763 3.6.4.6 E329Q no ATPase activity 656661 3.6.4.6 E350Q hydrolysis mutant 686724 3.6.4.6 E350Q lethal mutation 654648 3.6.4.6 E578Q mutant assembles into oligomer like wild-type, severely impaired ATPase activity 656763 3.6.4.6 G282E mutant protein has no ATPase activity 686724 3.6.4.6 G89D higher intrinsic ATPase activity than wild-type, no stimulation by Sec17 654648 3.6.4.6 K179A no ATP binding, enhanced binding to Vps20p and Vta1p in vitro 656345 3.6.4.6 K251A the p97 mutant carrying mutations in the D2 domain shows little ATPase activity when compared with wild type enzyme 698750 3.6.4.6 K251A the Walker A mutation to the D1 domain alone shows a moderate decrease in ATPase activity, has reduced affinity for nucleotide in the D1 domain and so contains little prebound ADP 698750 3.6.4.6 K266A ATP-binding mutant 686724 3.6.4.6 K266A no nucleotide binding 656661 3.6.4.6 K524A the p97 mutant carrying mutations in the D2 domain shows little ATPase activity when compared with wild type enzyme 698750 3.6.4.6 K549A decrease in NSF vesicular transport activity 656661 3.6.4.6 additional information construction of a Vps4p deletion mutant -, 735147 3.6.4.6 additional information construction of Vps4 knockout mutants, loss of Vps4 affects multiple signaling pathways, phenotypes, detailed overview 733702 3.6.4.6 additional information NSF DELTA-N mutant fails to bind to SNAP-SNARE complex 656661 3.6.4.6 Q216A monomeric mutant form 699526 3.6.4.6 R154C naturally occurring mutation, constitutes variations in surface-exposed locations, but does not alter the ATPase activity 756637 3.6.4.6 R154C/E219K naturally occurring mutation, constitutes variations in surface-exposed locations. The E219K mutation leads to an almost complete loss of activity, which is partially recuperated in the R154C/E219K double-mutant indicating p97 inter-domain communication 756637 3.6.4.6 R155C naturally occurring mutation, constitutes variations in surface-exposed locations and leads to increased ATPase activity, and a twofold decreased kd for human protein UBXD9 756637 3.6.4.6 R155H naturally occurring mutation, constitutes variations in surface-exposed locations and leads to increased ATPase activity, no change in the kd value for human protein UBXD9 756637 3.6.4.6 R241A site-directed mutagenesis, a pore loop 2 mutant, does not bind peptides with appreciable affinity 734303 3.6.4.6 R251A site-directed mutagenesis, a pore loop 2 adjacent mutant, does not bind peptides with appreciable affinity 734303 3.6.4.6 R359A the p97 mutant carrying mutations in the D2 domain shows little ATPase activity when compared with wild type enzyme 698750 3.6.4.6 R635A the p97 mutant carrying mutations in the D2 domain shows little ATPase activity when compared with wild type enzyme 698750 3.6.4.6 R93C naturally occurring mutation, constitutes variations in surface-exposed locations and leads to increased ATPase activity and a twofold increased kd for human protein UBXD9 756637 3.6.4.6 S569A mutation of serine 569 to alanine abolishs the phosphorylation of D2 domain by active Pctaire1 687536 3.6.4.6 T240A site-directed mutagenesis, a pore loop mutant, displays essentially unchanged oligomerization 734303 3.6.4.6 T240F site-directed mutagenesis, a pore loop 2 mutant 734303 3.6.4.6 T240K site-directed mutagenesis, a pore loop 2 mutant 734303 3.6.4.6 T240V site-directed mutagenesis, a pore loop 2 mutant 734303 3.6.4.6 W206A site-directed mutagenesis, a pore loop 1 mutant, does not bind peptides with appreciable affinity 734303