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Synonyms
valosin-containing protein, p97/vcp, peroxin, aaa protein, atpase associated with various cellular activities, atpase associated with diverse cellular activities, paf-2, pas1p, lonp2, pex1/pex6,
more
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AAA protein
Q9FNP1; Q8RY16
-
ATP-dependent lon protease
ATPase associated with diverse cellular activities
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ATPase associated with various cellular activities
peroxin ATPase complex
Q9FNP1; Q8RY16
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peroxisomal AAA ATPase complex
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peroxisomal AAA complex
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peroxisomal Pex1/Pex6 ATPase complex
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peroxisomal protease LON2
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peroxisomal receptor export complex
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peroxisome assembly factor-2
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peroxisome-assembly ATPase
peroxisome-associated ATPase
Q9FNP1; Q8RY16
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Pex1/6 type II AAA+ complex
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REM
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the receptor export module (REM) comprises two members of the ATPases associated with diverse cellular activities (AAA+) family, PEX1 and PEX6, and a membrane protein that anchors the ATPases to the organelle membrane
TBP1
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tat-binding protein
valosin-containing protein
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VCP
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valosin-containing protein
ATP-dependent lon protease

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ATP-dependent lon protease
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ATPase associated with various cellular activities

Q9FNP1; Q8RY16
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ATPase associated with various cellular activities
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HpPln

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lon

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lon protease

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LONP2

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PAF-2

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PAS1

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PAS1p

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PAS1p
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peroxisome assembly
peroxisomal Lon protease

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peroxisomal Lon protease
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peroxisomal Lon protease
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peroxisomal Lon protease
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peroxisomal Lon protease
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peroxisomal Lon protease
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peroxisomal Lon-protease

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peroxisomal Lon-protease
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peroxisomal Lon-protease
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peroxisomal Lon-protease
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peroxisome-assembly ATPase

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peroxisome-assembly ATPase
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Pex1

Q9FNP1; Q8RY16
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Pex1/Pex6 complex

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Pex1p

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Pex1p/Pex6p

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PEX6

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PEX6
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peroxisome assembly factor-2
Pex6p

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Pln

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ATP + H2O = ADP + phosphate
ATP + H2O = ADP + phosphate

an extremely diversified group of enzymes that use the energy of ATP hydrolysis to import and assemble peroxisome components into the organelle. Their molecular masses range from 25 to 600 kDa
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ATP + H2O = ADP + phosphate
an extremely diversified group of enzymes that use the energy of ATP hydrolysis to import and assemble peroxisome components into the organelle. Their molecular masses range from 25 to 600 kDa
-
ATP + H2O = ADP + phosphate
an extremely diversified group of enzymes that use the energy of ATP hydrolysis to import and assemble peroxisome components into the organelle. Their molecular masses range from 25 to 600 kDa
-
ATP + H2O = ADP + phosphate
an extremely diversified group of enzymes that use the energy of ATP hydrolysis to import and assemble peroxisome components into the organelle. Their molecular masses range from 25 to 600 kDa
-
ATP + H2O = ADP + phosphate
an extremely diversified group of enzymes that use the energy of ATP hydrolysis to import and assemble peroxisome components into the organelle. Their molecular masses range from 25 to 600 kDa
-
ATP + H2O = ADP + phosphate
an extremely diversified group of enzymes that use the energy of ATP hydrolysis to import and assemble peroxisome components into the organelle. Their molecular masses range from 25 to 600 kDa
-
ATP + H2O = ADP + phosphate
an extremely diversified group of enzymes that use the energy of ATP hydrolysis to import and assemble peroxisome components into the organelle. Their molecular masses range from 25 to 600 kDa
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ATP + H2O = ADP + phosphate
ATP hydrolysis occurs in a unidirectional manner around the ring, with one subunit primarily affecting ATP hydrolysis of only one of the neighboring subunits. ATP binding is initiated on one side of the ring at the nucleotide-free sites where the subunits are most widely spaced
ATP + H2O = ADP + phosphate
an extremely diversified group of enzymes that use the energy of ATP hydrolysis to import and assemble peroxisome components into the organelle. Their molecular masses range from 25 to 600 kDa
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-
ATP + H2O = ADP + phosphate
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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ATP + H2O
ADP + phosphate
additional information
?
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alpha-casein + H2O

?
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ATP-driven proteolytic activity against unfolded model protein
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?
alpha-casein + H2O
?
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ATP-driven proteolytic activity against unfolded model protein
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?
ATP + H2O

ADP + phosphate
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-
?
ATP + H2O
ADP + phosphate
Q9FNP1; Q8RY16
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?
ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
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-
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?
ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
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-
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ir
ATP + H2O
ADP + phosphate
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-
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?
ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
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ir
ATP + H2O
ADP + phosphate
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-
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?
ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
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210587, 210588, 210591, 210592, 756130, 756224, 756699, 756799, 757000, 757203, 757772, 758358 -
-
?
ATP + H2O
ADP + phosphate
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-
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-
ir
ATP + H2O
ADP + phosphate
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-
-
?
ATP + H2O
ADP + phosphate
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-
-
?
ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
the recombinant Pex1-FLAG/His-Pex6 complex is an active ATPase
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?
ATP + H2O
ADP + phosphate
nucleotide hydrolysis by the ATPase domain of Pex1
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?
ATP + H2O
ADP + phosphate
nucleotide hydrolysis by the ATPase domain of Pex6
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?
ATP + H2O
ADP + phosphate
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-
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?
ATP + H2O
ADP + phosphate
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-
-
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?
beta-casein + H2O

?
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ATP-driven proteolytic activity against unfolded model protein
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-
?
beta-casein + H2O
?
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ATP-driven proteolytic activity against unfolded model protein
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-
?
additional information

?
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AWP1 interacts with Pex6 AAA ATPase, but not with Pex1-Pex6 complexes. The ATPase activity of Pex6 modulates its interaction with AWP1
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?
additional information
?
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in vitro binding assays with GST-fused Pex26p show that Pex1p and Pex6p bind to Pex26p in a manner dependent on ATP binding but not ATP hydrolysis
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?
additional information
?
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the bona fide substrate membrane docking/translocation module-embedded monoubiquitinated PEX5 interacts directly with both enzyme forms PEX1 and PEX6 through its ubiquitin moiety. The PEX5 polypeptide chain is globally unfolded during the ATP-dependent extraction event
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additional information
?
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the enzyme degrades soluble unfolded and non-assembled peroxiÂsomal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein
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?
additional information
?
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the enzyme degrades soluble unfolded and non-assembled peroxiÂsomal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein
-
-
?
additional information
?
-
the enzyme degrades soluble unfolded and non-assembled peroxiÂsomal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein
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?
additional information
?
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Pln is a bifunctional protein with chaperone and protease activities, it acts as an ATP-fueled protease and chaperone. Oxidatively damaged, but not the native protein, is a substrate of the Pln protease
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?
additional information
?
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Pln has chaperone activity in vitro
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?
additional information
?
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Pln is a bifunctional protein with chaperone and protease activities, it acts as an ATP-fueled protease and chaperone. Oxidatively damaged, but not the native protein, is a substrate of the Pln protease
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?
additional information
?
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Pln has chaperone activity in vitro
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?
additional information
?
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identification of a peroxisome-specific isoform of Lon protease, an ATP-dependent protease with chaperone-like activity
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?
additional information
?
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model of Pex5p export by threading through the central Pex1p-Pex6p pore, overview
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?
additional information
?
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model of Pex5p export by threading through the central Pex1p-Pex6p pore, overview
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?
additional information
?
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Pex1 and Pex6 interact in vivo in an ATP-dependent manner. In the absence of nucleotide, the association of Pex1 with Pex6-FLAG is substantially diminished
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?
additional information
?
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Pex1 and Pex6 interact in vivo in an ATP-dependent manner. In the absence of nucleotide, the association of Pex1 with Pex6-FLAG is substantially diminished
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?
additional information
?
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Pex1 and Pex6 interact in vivo in an ATP-dependent manner. In the absence of nucleotide, the association of Pex1 with Pex6-FLAG is substantially diminished
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?
additional information
?
-
The recombinant AAA-complex exhibits an ATPase activity
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?
additional information
?
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The recombinant AAA-complex exhibits an ATPase activity
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?
additional information
?
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The recombinant AAA-complex exhibits an ATPase activity
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?
additional information
?
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a set of proteins, PEX1, PEX6 and a poorly conserved tail-anchored membrane protein, is required to extract monoubiquitinated PEX5 from the docking/translocation module. The PEX15 fragment is acting as a substrate for PEX1/PEX6
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additional information
?
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the natural substrate for the Pex1p-Pex6p-dependent release is monoubiquitinated Pex5p
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additional information
?
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the Pex1/Pex6 complex acts on ubiquitinated Pex5
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additional information
?
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the Pex1p/Pex6p enzyme complex is able to bind efficiently to Pex15p in vivo. Pex6p mediates binding to the cytosolic part of Pex15p via a direct interaction
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additional information
?
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the protein translocase unfolds Pex15 in a pore-loop-dependent and ATP-hydrolysis-dependent manner. Pex15 binds the N-terminal domains of enzyme Pex6, before its C-terminal disordered region engages with the pore loops of the motor, which then processively threads Pex15 through the central pore. Furthermore, Pex15 directly binds the cargo receptor Pex5, linking Pex1/Pex6 to other components of the peroxisomal import machinery
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O
ADP + phosphate
additional information
?
-
ATP + H2O

ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
Q9FNP1; Q8RY16
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
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?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
210587, 210588, 210591, 210592, 756130, 756224, 756699, 756799, 757000, 757203, 757772, 758358 -
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
the recombinant Pex1-FLAG/His-Pex6 complex is an active ATPase
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
additional information

?
-
-
AWP1 interacts with Pex6 AAA ATPase, but not with Pex1-Pex6 complexes. The ATPase activity of Pex6 modulates its interaction with AWP1
-
-
?
additional information
?
-
-
in vitro binding assays with GST-fused Pex26p show that Pex1p and Pex6p bind to Pex26p in a manner dependent on ATP binding but not ATP hydrolysis
-
-
?
additional information
?
-
the enzyme degrades soluble unfolded and non-assembled peroxiÂsomal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein
-
-
?
additional information
?
-
-
the enzyme degrades soluble unfolded and non-assembled peroxiÂsomal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein
-
-
?
additional information
?
-
the enzyme degrades soluble unfolded and non-assembled peroxiÂsomal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein
-
-
?
additional information
?
-
-
Pln is a bifunctional protein with chaperone and protease activities, it acts as an ATP-fueled protease and chaperone. Oxidatively damaged, but not the native protein, is a substrate of the Pln protease
-
-
?
additional information
?
-
-
Pln is a bifunctional protein with chaperone and protease activities, it acts as an ATP-fueled protease and chaperone. Oxidatively damaged, but not the native protein, is a substrate of the Pln protease
-
-
?
additional information
?
-
identification of a peroxisome-specific isoform of Lon protease, an ATP-dependent protease with chaperone-like activity
-
-
?
additional information
?
-
model of Pex5p export by threading through the central Pex1p-Pex6p pore, overview
-
-
?
additional information
?
-
model of Pex5p export by threading through the central Pex1p-Pex6p pore, overview
-
-
?
additional information
?
-
Pex1 and Pex6 interact in vivo in an ATP-dependent manner. In the absence of nucleotide, the association of Pex1 with Pex6-FLAG is substantially diminished
-
-
?
additional information
?
-
Pex1 and Pex6 interact in vivo in an ATP-dependent manner. In the absence of nucleotide, the association of Pex1 with Pex6-FLAG is substantially diminished
-
-
?
additional information
?
-
-
Pex1 and Pex6 interact in vivo in an ATP-dependent manner. In the absence of nucleotide, the association of Pex1 with Pex6-FLAG is substantially diminished
-
-
?
additional information
?
-
The recombinant AAA-complex exhibits an ATPase activity
-
-
?
additional information
?
-
The recombinant AAA-complex exhibits an ATPase activity
-
-
?
additional information
?
-
-
The recombinant AAA-complex exhibits an ATPase activity
-
-
?
additional information
?
-
-
a set of proteins, PEX1, PEX6 and a poorly conserved tail-anchored membrane protein, is required to extract monoubiquitinated PEX5 from the docking/translocation module. The PEX15 fragment is acting as a substrate for PEX1/PEX6
-
-
-
additional information
?
-
-
the natural substrate for the Pex1p-Pex6p-dependent release is monoubiquitinated Pex5p
-
-
-
additional information
?
-
-
the Pex1/Pex6 complex acts on ubiquitinated Pex5
-
-
-
additional information
?
-
-
the Pex1p/Pex6p enzyme complex is able to bind efficiently to Pex15p in vivo. Pex6p mediates binding to the cytosolic part of Pex15p via a direct interaction
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.