3.4.21.108: HtrA2 peptidase
This is an abbreviated version!
For detailed information about HtrA2 peptidase, go to the full flat file.
Word Map on EC 3.4.21.108
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3.4.21.108
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xiap
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bcl-2
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parkinson
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proapoptotic
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caspases
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caspase-independent
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aif
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x-linked
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medicine
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apoptosis-inducing
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intermembrane
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htras
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pink1
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apoptogenic
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iap-binding
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apoptosome
- 3.4.21.108
- xiap
- bcl-2
- parkinson
-
proapoptotic
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caspases
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caspase-independent
- aif
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x-linked
- medicine
-
apoptosis-inducing
-
intermembrane
-
htras
- pink1
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apoptogenic
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iap-binding
- apoptosome
Reaction
cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues =
Synonyms
DegP, dOmi/HtrA2, high temperature requirement A serine protease, high temperature requirement A2, high temperature requirement A2 protease, high temperature requirement A2 serine protease, high temperature requirement protein A2, high-temperature requirement factor A2, HtrA protease, HtrA/DegP, HtrA2, HtrA2 protease, HtrA2 serine protease, HtrA2(Omi), HtrA2/Omi, HtrA2/Omi serine protease, Nma11p, Omi, Omi protease, Omi/HtrA2, Omi/HtrA2 protease, Omi/HtrA2 serine protease, pro-apoptotic serine protease, S01.278, serine protease, serine protease HtrA2, serine protease HtrA2/Omi, serine protease Omi/HtrA2
ECTree
3.4.21.108 HtrA2 peptidaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.21.108 - HtrA2 peptidase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
thanatos-associated protein 5 (THAP5) + H2O
?
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in a yeast two-hybrid assay it is shown that Omi/HtrA2 protease interacts with thanatos-associated protein 5. Degradation assays show that thanatos-associated protein 5 is cleaved by Omi/HtrA2
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?
ubiquitin carboxyl-terminal hydrolase L1 + H2O
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natural substrate for HtrA2 in the apoptotic pathway. HtrA2 directly cleaves UCH-L1 and inhibits its hydrolase activity
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?
parkin + H2O
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using cleavage and binding assays, it is demonstrated that HtrA2 specifically binds to and directly cleaves the E3 ubiquitin ligase Parkin
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?
Wilms' tumor suppressor 1 + H2O
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bona fide substrate for HtrA2-mediated proteolysis, cleavage sites are in the C terminus at Val286 and Leu320, resulting in fragments of 20000 and 35000 Da, respectively, while another cleavage site is in the N terminus at Leu91 adjacent to suppression domain
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?
Wilms' tumor suppressor 1 + H2O
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HtrA2 cleaves at, at least, two specific sites. Wilms' tumor suppressor 1 degradation by HtrA2 reveals two major proteolytic products of 20000 Da and 15000 Da, but the same samples immunoblotted with N-Ter antibody reveals major fragment sizes of 35000 Da and 30000 Da. The potential cleavage site that produces the 20000 Da fragment is at Val286, and the potential cleavage site producing the 15000 Da fragment is at Leu320
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?
Wilms' tumor suppressor protein WT1 + H2O
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using a yeat two-hybrid assay WT1 is identified as a binding partner of HtrA2/Omi. HtrA2/Omi cleaves WT1 at multiple binding sites following the treatment of cells with cytotoxic drugs
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?
additional information
?
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cleavage of DIAP1 between the BIR1 and BIR2 domain and further degradation of BIR1
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?
additional information
?
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can promote caspase activation and cell death apoptosis
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?
additional information
?
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induces atypical cell death. Inhibits the caspase-inhibitory activity of XIAP by direct binding to it. Only mature form but not its precursor binds to IAPs
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?
additional information
?
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role in apoptosis, amino-terminal IAP interaction motif displaces IAPs from caspases, leading to enhanced caspase activity
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?
additional information
?
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role in apoptosis, binds to XIAP-binding protein
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?
additional information
?
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role in apoptosis, degradation of aberrantly folded proteins during conditions of cellular stress
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?
additional information
?
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role in apoptosis, degradation of aberrantly folded proteins during conditions of cellular stress
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?
additional information
?
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role in apoptosis, enzyme can induce apoptosis in a caspase-independent manner through its protease activity and in a caspase-dependent manner via its ability to disrupt caspase-IAP interaction
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?
additional information
?
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degradation of inhibitor of apoptosis proteins, IAPs
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?
additional information
?
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HtrA2 cleaves p73alpha in the C-terminal portion
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?
additional information
?
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co-immunoprecipitation show direct interaction of Omi/HtrA2 with optic atrophy protein 1 (OPA1)
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?
additional information
?
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HtrA2 fails to cleave the Wilms' tumor suppressor 1 cofactors Par-4 and BASP1
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?
additional information
?
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induces cell death in a caspase-dependent manner
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?
additional information
?
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role in apoptosis, mice with mutant HtrA2/Omi suffer from neurodegenerative disease due to progressive mitochondrial damage, mutant enzyme is proteolytically inactive but can bind to IAPs
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?
additional information
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loss of enzyme activity causes neuromuscular disorder
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?
additional information
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loss of enzyme activity causes neuromuscular disorder
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?
additional information
?
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role in apoptosis, mice with mutant HtrA2/Omi suffer from neurodegenerative disease due to progressive mitochondrial damage, mutant enzyme is proteolytically inactive but can bind to IAPs
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?
