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ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
Drosophila sp. (in: flies)
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
210594, 210596, 210597, 210598, 210599, 210600, 210601, 210602, 210603, 210604, 210605
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome
-
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide
-
-
-
-
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ATP + H2O
ADP + phosphate
ATP + H2O + gene-3-protein
ADP + phosphate + unfolded gene-3-protein
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
ATP + H2O + polypeptide GFPssrA
ADP + phosphate + unfolded polypeptide GFPssrA
ATP + H2O + polypeptide Myc-Pup-FabD-his
ADP + phosphate + unfolded polypeptide Myc-Pup-FabD-his
-
-
-
-
?
ATP + H2O + polyubiquitinated Sic60PY-Spectrin12-16-SNAP-His6 protein
?
ATP + H2O + polyubiquitylated Sic1PY
ADP + phosphate + unfolded polyubiquitylated Sic1PY
-
-
-
-
?
ATP + H2O + suc-L-Leu-L-Leu-L-Val-L-Tyr-7-amido-4-methylcoumarin
?
-
-
-
?
CTP + H2O
CDP + phosphate
CTP + H2O + polypeptide
CDP + phosphate + unfolded polypeptide
GTP + H2O
GDP + phosphate
GTP + H2O + polypeptide
GDP + phosphate + unfolded polypeptide
ITP + H2O + polypeptide
IDP + phosphate + unfolded polypeptide
-
-
-
-
?
TTP + H2O + polypeptide
TDP + phosphate + unfolded polypeptide
-
-
-
-
?
UTP + H2O + polypeptide
UDP + phosphate + unfolded polypeptide
additional information
?
-
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
highly preferred substrate
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
highly preferred substrate
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
highly preferred substrate
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
highly preferred substrate
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
highly preferred substrate
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
highly preferred substrate
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
ATPase subunit S6' recognizes the polyubiquitin degradation signal
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
other folded as well as unstructured polyubiquitylated proteins require ATP hydrolysis for proteolysis and deubiquitylation
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
PA700 has multiple activities, including ATPase activity, polyubiquitin-chain binding activity, deubiquitination activity, chaperone-like activity, and substrate remodelling activity
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
the 26S proteasome is a 2400000 Da protease complex that selectively degrades proteins modified by polyubiquitin chains. The 26S proteasome is composed of two 700000 Da multisubunit complexes: the 20S proteasome, which serves as the proteolytic core of the complex, and PA700, an ATPase regulatory complex responsible for the binding, modification, and delivery of substrates to the proteolytic chamber
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
ir
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
Pros26.4 negatively regulates Hairless at the genetic and molecular level. Depletion of Pros26.4 results in a specific stabilization of the Hairless protein, but not in stabilization of the intracellular domain of Notch or the effector protein Suppressor of Hairless. Thus, the Hairless-Pros26.4 interaction provides a novel mechanism of positive regulation of Notch signalling
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
Drosophila sp. (in: flies)
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
210594, 210596, 210599, 210600, 210601, 210603, 210604, 655185, 697635, 734207, 749804, 751667, 752040, 752260 -
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
26S proteasome stimulation requires ATP hydrolysis
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
ATP hydrolysis promotes 3 processes in the 20S proteasome, substrate unfolding, gate opening and protein translocation
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
C-terminal ATPase domain of Rpt5, residues 173-442
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
ir
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
ir
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
210594, 210596, 210597, 210598, 210599, 210600, 210601, 210602, 210603, 210604, 210605, 654902, 655201, 655585, 656773, 749585, 751521, 751554 -
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
ir
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
Rpt2 controls the gating of the adjacent core particle channnel of the proteasome
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
ATP hydrolysis is required for degradation of polyubiquitinated proteins by the 26S proteasome. ATP hydrolysis triggers rapid dissociation of the 19S regulatory particles from immunopurified 26S complexes in a manner coincident with release of the bulk of proteasome-interacting proteins. A controlled dissociation of the 19S regulatory particles from the 26S proteasome is part of the mechanism of protein degradation
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
-
-
-
-
?
ATP + H2O + polypeptide GFPssrA
ADP + phosphate + unfolded polypeptide GFPssrA
-
-
-
-
?
ATP + H2O + polypeptide GFPssrA
ADP + phosphate + unfolded polypeptide GFPssrA
-
-
-
?
ATP + H2O + polypeptide GFPssrA
ADP + phosphate + unfolded polypeptide GFPssrA
-
-
-
?
ATP + H2O + polyubiquitinated Sic60PY-Spectrin12-16-SNAP-His6 protein
?
-
-
-
-
?
ATP + H2O + polyubiquitinated Sic60PY-Spectrin12-16-SNAP-His6 protein
?
-
-
-
-
?
CTP + H2O
CDP + phosphate
-
-
-
?
CTP + H2O
CDP + phosphate
-
-
-
?
CTP + H2O
CDP + phosphate
-
-
-
?
CTP + H2O
CDP + phosphate
-
-
-
?
CTP + H2O
CDP + phosphate
-
-
-
?
CTP + H2O
CDP + phosphate
-
-
-
?
CTP + H2O + polypeptide
CDP + phosphate + unfolded polypeptide
-
-
-
-
?
CTP + H2O + polypeptide
CDP + phosphate + unfolded polypeptide
-
-
-
?
CTP + H2O + polypeptide
CDP + phosphate + unfolded polypeptide
-
-
-
?
CTP + H2O + polypeptide
CDP + phosphate + unfolded polypeptide
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O + polypeptide
GDP + phosphate + unfolded polypeptide
-
-
-
-
?
GTP + H2O + polypeptide
GDP + phosphate + unfolded polypeptide
-
-
-
-
?
UTP + H2O + polypeptide
UDP + phosphate + unfolded polypeptide
-
-
-
-
?
UTP + H2O + polypeptide
UDP + phosphate + unfolded polypeptide
-
-
-
-
?
additional information
?
-
RPT5a and RPT5b are essential for male gametophyte development, display accession-dependent redundancy and are crucial in cell cycle progression
-
-
?
additional information
?
-
-
RPT5a and RPT5b are essential for male gametophyte development, display accession-dependent redundancy and are crucial in cell cycle progression
-
-
?
additional information
?
-
-
UNI/uni-1D interacts with the regulatory particle triple-ATPase (RPT) subunits 2a and 2b, base components of the 19S regulatory particle in the 26S proteasome
-
-
?
additional information
?
-
Bl-ARC has a preference for ATP as substrate (100%) when compared against GTP (28%), CTP (31%), and UTP (1.5%)
-
-
-
additional information
?
-
Bl-ARC has a preference for ATP as substrate (100%) when compared against GTP (28%), CTP (31%), and UTP (1.5%)
-
-
-
additional information
?
-
Bl-ARC has a preference for ATP as substrate (100%) when compared against GTP (28%), CTP (31%), and UTP (1.5%)
-
-
-
additional information
?
-
Bl-ARC has a preference for ATP as substrate (100%) when compared against GTP (28%), CTP (31%), and UTP (1.5%)
-
-
-
additional information
?
-
Bl-ARC has a preference for ATP as substrate (100%) when compared against GTP (28%), CTP (31%), and UTP (1.5%)
-
-
-
additional information
?
-
Bl-ARC has a preference for ATP as substrate (100%) when compared against GTP (28%), CTP (31%), and UTP (1.5%)
-
-
-
additional information
?
-
-
PA700 prevents fibril formation of both wild-type and A53T alpha-synuclein. It is hypothesized that PA700 sequesters alpha-synuclein oligomeric species that are the precursors of the fibrillar form of the protein, thus preventing its assembly into fibrils
-
-
?
additional information
?
-
the Pan proteins are part of the 5-member proteasome isoforms, the five proteins are differentially regulated by a posttranscriptional mechanism, e.g. PanA remains relatively constant, a coiled-coil structure at the N-terminus of Pan is involved in substrate recognition
-
-
?
additional information
?
-
the Pan proteins are part of the 5-member proteasome isoforms, the five proteins are differentially regulated by a posttranscriptional mechanism, e.g. PanA remains relatively constant, a coiled-coil structure at the N-terminus of Pan is involved in substrate recognition
-
-
?
additional information
?
-
-
the Pan proteins are part of the 5-member proteasome isoforms, the five proteins are differentially regulated by a posttranscriptional mechanism, e.g. PanA remains relatively constant, a coiled-coil structure at the N-terminus of Pan is involved in substrate recognition
-
-
?
additional information
?
-
the Pan proteins are part of the 5-member proteasome isoforms, the five proteins are differentially regulated by a posttranscriptional mechanism, e.g. PanB increases 7fold in the stationary phase, a coiled-coil structure at the N-terminus of Pan is involved in substrate recognition
-
-
?
additional information
?
-
the Pan proteins are part of the 5-member proteasome isoforms, the five proteins are differentially regulated by a posttranscriptional mechanism, e.g. PanB increases 7fold in the stationary phase, a coiled-coil structure at the N-terminus of Pan is involved in substrate recognition
-
-
?
additional information
?
-
-
the Pan proteins are part of the 5-member proteasome isoforms, the five proteins are differentially regulated by a posttranscriptional mechanism, e.g. PanB increases 7fold in the stationary phase, a coiled-coil structure at the N-terminus of Pan is involved in substrate recognition
-
-
?
additional information
?
-
the Pan proteins are part of the 5-member proteasome isoforms, the five proteins are differentially regulated by a posttranscriptional mechanism, e.g. PanA remains relatively constant, a coiled-coil structure at the N-terminus of Pan is involved in substrate recognition
-
-
?
additional information
?
-
the Pan proteins are part of the 5-member proteasome isoforms, the five proteins are differentially regulated by a posttranscriptional mechanism, e.g. PanA remains relatively constant, a coiled-coil structure at the N-terminus of Pan is involved in substrate recognition
-
-
?
additional information
?
-
the Pan proteins are part of the 5-member proteasome isoforms, the five proteins are differentially regulated by a posttranscriptional mechanism, e.g. PanB increases 7fold in the stationary phase, a coiled-coil structure at the N-terminus of Pan is involved in substrate recognition
-
-
?
additional information
?
-
the Pan proteins are part of the 5-member proteasome isoforms, the five proteins are differentially regulated by a posttranscriptional mechanism, e.g. PanB increases 7fold in the stationary phase, a coiled-coil structure at the N-terminus of Pan is involved in substrate recognition
-
-
?
additional information
?
-
-
TBP-1 functions as a coactivator of AR with TBP-1-interacting protein, TBP-1 interacts with TBP-1-interacting protein in vitro via its N-terminal leucine zipper structure
-
-
?
additional information
?
-
-
a specific interaction between Rpt1 and Hsm3 is required for the proper assembly of the 19 S RP
-
-
?
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Arabidopsis sp., Homo sapiens, Oryza sativa, Rattus norvegicus, Saccharomyces cerevisiae, Solanum lycopersicum, Spinacia oleracea, Thermoplasma sp., Xenopus laevis
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Bos taurus
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Saccharomyces cerevisiae
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Drosophila melanogaster
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Oryctolagus cuniculus
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Rattus norvegicus
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Tat-binding protein-1 (TBP-1), an ATPase of 19S regulatory particles of the 26S proteasome, enhances androgen receptor function in cooperation with Tat-binding protein-1-interacting protein/Hop2
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Homo sapiens
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Gillette, T.G.; Kumar, B.; Thompson, D.; Slaughter, C.A.; DeMartino, G.N.
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Bos taurus
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Homo sapiens
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Nature
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Saccharomyces cerevisiae
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Gallois, J.L.; Guyon-Debast, A.; Lecureuil, A.; Vezon, D.; Carpentier, V.; Bonhomme, S.; Guerche, P.
The Arabidopsis proteasome RPT5 subunits are essential for gametophyte development and show accession-dependent redundancy
Plant Cell
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2009
Arabidopsis thaliana (Q04019), Arabidopsis thaliana
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Brenner, E.D.; Feinberg, P.; Runko, S.; Coruzzi, G.M.
A mutation in the Proteosomal Regulatory Particle AAA-ATPase-3 in Arabidopsis impairs the light-specific hypocotyl elongation response elicited by a glutamate receptor agonist, BMAA
Plant Mol. Biol.
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Arabidopsis thaliana (Q9SEI4)
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Kurepa, J.; Wang, S.; Li, Y.; Zaitlin, D.; Pierce, A.J.; Smalle, J.A.
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Arabidopsis thaliana
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Sutter, M.; Striebel, F.; Damberger, F.F.; Allain, F.H.; Weber-Ban, E.
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Mycobacterium tuberculosis (P9WQN5), Mycobacterium tuberculosis H37Rv (P9WQN5)
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Association of the 19S proteasomal ATPases with the ATPase-binding domain of CIITA is essential for CIITA stability and MHC class II expression
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Homo sapiens
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Djuranovic, S.; Hartmann, M.D.; Habeck, M.; Ursinus, A.; Zwickl, P.; Martin, J.; Lupas, A.N.; Zeth, K.
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Mol. Cell
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Archaeoglobus fulgidus (O28303), Archaeoglobus fulgidus, Rhodococcus erythropolis (O50202), Rhodococcus erythropolis
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Mol. Cell
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Saccharomyces cerevisiae S288c
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Structural insights on the Mycobacterium tuberculosis proteasomal ATPase Mpa
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Mycobacterium tuberculosis (P9WQN5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WQN5)
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Methanocaldococcus jannaschii
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Homo sapiens
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Saccharomyces cerevisiae
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Oryctolagus cuniculus
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RPT2a, a 26S proteasome AAA-ATPase, is directly involved in Arabidopsis CC-NBS-LRR protein uni-1D-induced signaling pathways
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Arabidopsis thaliana
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Mus musculus
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Homo sapiens
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Sequential actions of the AAA-ATPase valosin-containing protein (VCP)/p97 and the proteasome 19 S regulatory particle in sterol-accelerated, endoplasmic reticulum (ER)-associated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
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Mus musculus (O88685), Mus musculus (P54775), Mus musculus (P62192), Mus musculus (P62196), Mus musculus (P62334), Mus musculus (Q8BVQ9)
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Saccharomyces cerevisiae (Q01939), Saccharomyces cerevisiae
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Saccharomyces cerevisiae
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2016
Homo sapiens
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Raynes, R.; Pomatto, L.C.; Davies, K.J.
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Saccharomyces cerevisiae
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An AAA motor-driven mechanical switch in Rpn11 controls deubiquitination at the 26S proteasome
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2017
Saccharomyces cerevisiae
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Wu, Y.; Hu, K.; Li, D.; Bai, L.; Yang, S.; Jastrab, J.B.; Xiao, S.; Hu, Y.; Zhang, S.; Darwin, K.H.; Wang, T.; Li, H.
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Bos taurus
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Homo sapiens
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Methanocaldococcus jannaschii (Q58576), Methanocaldococcus jannaschii ATCC 43067 (Q58576)
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Escherichia coli
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Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome
Nature
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Homo sapiens
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Ohnishi, Y.H.; Ohnishi, Y.N.; Nakamura, T.; Ohno, M.; Kennedy, P.J.; Ohkawa, Y.; Yasuyuki, O.; Nishi, A.; Neve, R.; Tsuzuki, T.; Nestler, E.J.
PSMC5, a 19S proteasomal ATPase, regulates cocaine action in the nucleus accumbens
PLoS ONE
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Mus musculus
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Aufderheide, A.; Beck, F.; Stengel, F.; Hartwig, M.; Schweitzer, A.; Pfeifer, G.; Goldberg, A.L.; Sakata, E.; Baumeister, W.; Foerster, F.
Structural characterization of the interaction of Ubp6 with the 26S proteasome
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Saccharomyces cerevisiae (P33299)
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Chen, S.; Wu, J.; Lu, Y.; Ma, Y.B.; Lee, B.H.; Yu, Z.; Ouyang, Q.; Finley, D.J.; Kirschner, M.W.; Mao, Y.
Structural basis for dynamic regulation of the human 26S proteasome
Proc. Natl. Acad. Sci. USA
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Homo sapiens
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Luan, B.; Huang, X.; Wu, J.; Mei, Z.; Wang, Y.; Xue, X.; Yan, C.; Wang, J.; Finley, D.J.; Shi, Y.; Wang, F.
Structure of an endogenous yeast 26S proteasome reveals two major conformational states
Proc. Natl. Acad. Sci. USA
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Saccharomyces cerevisiae (P33297), Saccharomyces cerevisiae (P33298), Saccharomyces cerevisiae (P33299), Saccharomyces cerevisiae (P40327), Saccharomyces cerevisiae (P53549), Saccharomyces cerevisiae (Q01939)
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Schweitzer, A.; Aufderheide, A.; Rudack, T.; Beck, F.; Pfeifer, G.; Plitzko, J.M.; Sakata, E.; Schulten, K.; Foerster, F.; Baumeister, W.
Structure of the human 26S proteasome at a resolution of 3.9 A
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Homo sapiens (Q99460)
brenda
Majumder, P.; Rudack, T.; Beck, F.; Danev, R.; Pfeifer, G.; Nagy, I.; Baumeister, W.
Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle
Proc. Natl. Acad. Sci. USA
116
534-539
2019
Archaeoglobus fulgidus (O28303), Archaeoglobus fulgidus ATCC 49558 (O28303)
brenda
Sahu, P.P.; Sharma, N.; Puranik, S.; Chakraborty, S.; Prasad, M.
Tomato 26S proteasome subunit RPT4a regulates ToLCNDV transcription and activates hypersensitive response in tomato
Sci. Rep.
6
27078
2016
Solanum lycopersicum
brenda
de la Pena, A.H.; Goodall, E.A.; Gates, S.N.; Lander, G.C.; Martin, A.
Substrate-engaged 26S proteasome structures reveal mechanisms for ATP-hydrolysis-driven translocation
Science
362
eaav0725
2018
Homo sapiens
brenda
Guzman-Rodriguez, M.; de la Rosa, A.P.; Santos, L.
Characterization of ATPase activity of the AAA ARC from Bifidobacterium longum subsp. infantis
Acta Biochim. Pol.
62
221-227
2015
Bifidobacterium longum subsp. infantis (B7GUP3), Bifidobacterium longum subsp. infantis S12 (B7GUP3), Bifidobacterium longum subsp. infantis JCM 1222 (B7GUP3), Bifidobacterium longum subsp. infantis NCTC 11817 (B7GUP3), Bifidobacterium longum subsp. infantis DSM 20088 (B7GUP3), Bifidobacterium longum subsp. infantis ATCC 15697 (B7GUP3)
brenda