|
P02829
|
ATP-dependent molecular chaperone HSP82 |
Molecular chaperone that promotes the maturation, structuralmaintenance and proper regulation of specific target proteins involvedin cell cycle control and signal transduction. Undergoes a functionalcycle that is linked to its ATPase activity. The nucleotide-free formof the dimer is found in an open conformation in which the N-terminiare not dimerized and the complex is ready for client protein binding.Binding of ATP induces large conformational changes, resulting in theformation of a ring-like closed structure in which the N-terminaldomains associate intramolecularly with the middle domain and alsodimerize with each other, stimulating their intrinsic ATPase activityand acting as a clamp on the substrate. Finally, ATP hydrolysis resultsin the release of the substrate. This cycle probably inducesconformational changes in the client proteins, thereby causing theiractivation. Interacts dynamically with various co-chaperones thatmodulate its substrate recognition, ATPase cycle and chaperonefunction. Required for growth at high temperatures |
YPL240C |
Saccharomyces cerevisiae |
RSY113 |
20559436
|
|
P02829
|
ATP-dependent molecular chaperone HSP82 |
Molecular chaperone that promotes the maturation, structuralmaintenance and proper regulation of specific target proteins involvedin cell cycle control and signal transduction. Undergoes a functionalcycle that is linked to its ATPase activity. The nucleotide-free formof the dimer is found in an open conformation in which the N-terminiare not dimerized and the complex is ready for client protein binding.Binding of ATP induces large conformational changes, resulting in theformation of a ring-like closed structure in which the N-terminaldomains associate intramolecularly with the middle domain and alsodimerize with each other, stimulating their intrinsic ATPase activityand acting as a clamp on the substrate. Finally, ATP hydrolysis resultsin the release of the substrate. This cycle probably inducesconformational changes in the client proteins, thereby causing theiractivation. Interacts dynamically with various co-chaperones thatmodulate its substrate recognition, ATPase cycle and chaperonefunction. Required for growth at high temperatures |
YPL240C |
Saccharomyces cerevisiae |
RSY255 |
20559436
|
|
P02829
|
ATP-dependent molecular chaperone HSP82 |
Molecular chaperone that promotes the maturation, structuralmaintenance and proper regulation of specific target proteins involvedin cell cycle control and signal transduction. Undergoes a functionalcycle that is linked to its ATPase activity. The nucleotide-free formof the dimer is found in an open conformation in which the N-terminiare not dimerized and the complex is ready for client protein binding.Binding of ATP induces large conformational changes, resulting in theformation of a ring-like closed structure in which the N-terminaldomains associate intramolecularly with the middle domain and alsodimerize with each other, stimulating their intrinsic ATPase activityand acting as a clamp on the substrate. Finally, ATP hydrolysis resultsin the release of the substrate. This cycle probably inducesconformational changes in the client proteins, thereby causing theiractivation. Interacts dynamically with various co-chaperones thatmodulate its substrate recognition, ATPase cycle and chaperonefunction. Required for growth at high temperatures |
YPL240C |
Saccharomyces cerevisiae |
RSY782 |
20559436
|
|
P02829
|
ATP-dependent molecular chaperone HSP82 |
Molecular chaperone that promotes the maturation, structuralmaintenance and proper regulation of specific target proteins involvedin cell cycle control and signal transduction. Undergoes a functionalcycle that is linked to its ATPase activity. The nucleotide-free formof the dimer is found in an open conformation in which the N-terminiare not dimerized and the complex is ready for client protein binding.Binding of ATP induces large conformational changes, resulting in theformation of a ring-like closed structure in which the N-terminaldomains associate intramolecularly with the middle domain and alsodimerize with each other, stimulating their intrinsic ATPase activityand acting as a clamp on the substrate. Finally, ATP hydrolysis resultsin the release of the substrate. This cycle probably inducesconformational changes in the client proteins, thereby causing theiractivation. Interacts dynamically with various co-chaperones thatmodulate its substrate recognition, ATPase cycle and chaperonefunction. Required for growth at high temperatures |
YPL240C |
Saccharomyces cerevisiae |
RSY954 |
20559436
|
|
P02829
|
ATP-dependent molecular chaperone HSP82 |
Molecular chaperone that promotes the maturation, structuralmaintenance and proper regulation of specific target proteins involvedin cell cycle control and signal transduction. Undergoes a functionalcycle that is linked to its ATPase activity. The nucleotide-free formof the dimer is found in an open conformation in which the N-terminiare not dimerized and the complex is ready for client protein binding.Binding of ATP induces large conformational changes, resulting in theformation of a ring-like closed structure in which the N-terminaldomains associate intramolecularly with the middle domain and alsodimerize with each other, stimulating their intrinsic ATPase activityand acting as a clamp on the substrate. Finally, ATP hydrolysis resultsin the release of the substrate. This cycle probably inducesconformational changes in the client proteins, thereby causing theiractivation. Interacts dynamically with various co-chaperones thatmodulate its substrate recognition, ATPase cycle and chaperonefunction. Required for growth at high temperatures |
YPL240C |
Saccharomyces cerevisiae |
SEY6210 |
20559436
|
|
P02829
|
ATP-dependent molecular chaperone HSP82 |
Molecular chaperone that promotes the maturation, structuralmaintenance and proper regulation of specific target proteins involvedin cell cycle control and signal transduction. Undergoes a functionalcycle that is linked to its ATPase activity. The nucleotide-free formof the dimer is found in an open conformation in which the N-terminiare not dimerized and the complex is ready for client protein binding.Binding of ATP induces large conformational changes, resulting in theformation of a ring-like closed structure in which the N-terminaldomains associate intramolecularly with the middle domain and alsodimerize with each other, stimulating their intrinsic ATPase activityand acting as a clamp on the substrate. Finally, ATP hydrolysis resultsin the release of the substrate. This cycle probably inducesconformational changes in the client proteins, thereby causing theiractivation. Interacts dynamically with various co-chaperones thatmodulate its substrate recognition, ATPase cycle and chaperonefunction. Required for growth at high temperatures |
YPL240C |
Saccharomyces cerevisiae |
SF264-1D |
20559436
|
|
P02829
|
ATP-dependent molecular chaperone HSP82 |
Molecular chaperone that promotes the maturation, structuralmaintenance and proper regulation of specific target proteins involvedin cell cycle control and signal transduction. Undergoes a functionalcycle that is linked to its ATPase activity. The nucleotide-free formof the dimer is found in an open conformation in which the N-terminiare not dimerized and the complex is ready for client protein binding.Binding of ATP induces large conformational changes, resulting in theformation of a ring-like closed structure in which the N-terminaldomains associate intramolecularly with the middle domain and alsodimerize with each other, stimulating their intrinsic ATPase activityand acting as a clamp on the substrate. Finally, ATP hydrolysis resultsin the release of the substrate. This cycle probably inducesconformational changes in the client proteins, thereby causing theiractivation. Interacts dynamically with various co-chaperones thatmodulate its substrate recognition, ATPase cycle and chaperonefunction. Required for growth at high temperatures |
YPL240C |
Saccharomyces cerevisiae |
Snf7 |
20559436
|
|
P02829
|
ATP-dependent molecular chaperone HSP82 |
Molecular chaperone that promotes the maturation, structuralmaintenance and proper regulation of specific target proteins involvedin cell cycle control and signal transduction. Undergoes a functionalcycle that is linked to its ATPase activity. The nucleotide-free formof the dimer is found in an open conformation in which the N-terminiare not dimerized and the complex is ready for client protein binding.Binding of ATP induces large conformational changes, resulting in theformation of a ring-like closed structure in which the N-terminaldomains associate intramolecularly with the middle domain and alsodimerize with each other, stimulating their intrinsic ATPase activityand acting as a clamp on the substrate. Finally, ATP hydrolysis resultsin the release of the substrate. This cycle probably inducesconformational changes in the client proteins, thereby causing theiractivation. Interacts dynamically with various co-chaperones thatmodulate its substrate recognition, ATPase cycle and chaperonefunction. Required for growth at high temperatures |
YPL240C |
Saccharomyces cerevisiae |
VPS23 |
20559436
|