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
-
caspases
-
caspase-independent
- aif
-
x-linked
- medicine
-
apoptosis-inducing
-
intermembrane
-
htras
- pink1
-
apoptogenic
-
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 (Activating Compound
Activating Compound on EC 3.4.21.108 - HtrA2 peptidase
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
DKVLVVWAGQQ
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full-length denatured alpha-amylase, as well as alpha-amylase fragments and the C-terminus of alpha-amylase, amplify DegP proteolysis
GRIM-19
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direct enhancement of HtrA2 activity in vitro. HtrA2-driven destruction of the antiapoptotic X-linked inhibitor of apoptosis protein is augmented
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heat shock
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pre-incubation of Omi at 42°C for 30 min results in increased proteolytic activity
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IFN/all-trans retinoic acid
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enhances interaction of GRIM-19 with HtrA2. Causes a concurrent release of HtrA2 and GRIM-19 from mitochondria
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inhibitor of apoptosis protein
in presence of inhibitor of apoptosis protein, catalytic efficiency increases up to 3fold. In presence of its BIR2 and/or BIR3 domains, catalytic efficiency increases up to 2fold. Interaction allosterically modulates HtrA2 activity, the activation occurs through a series of coordinated structural reorganizations at distal regulatory loops, leading to a population shift towards the relaxed conformer
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L-phenylalanine
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essential for the formation of a homotrimer and for the HtrA2 serine protease activity
PDZ domain G230A
mutation in recognition sequence of the PDZ domain, shows a significant decrease in the catalytic efficiency
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siRNA
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siRNA-mediated knockdown of HtrA2/Omi combined with the pan-caspase inhibitor zVAD-fmk almost completely protects HeLa cells from undergoing staurosporine-induced cell death, whereas caspase inhibition alone is significantly less effective
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X-linked inhibitor of apoptosis protein
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i.e. XIAP, binding of XIAP to the Reaper motif of the enzyme results in a marked increase in proteolytic activity
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staurosporine
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apoptotic stimulus to release 36-kDa protein fragment of HtrA2 and cytochrome c from the mitochondria to the cytosol
staurosporine
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activates protease activity of Omi leading to cell death. Induces cell death in wild-type MEFs but not in caspase-9-deficient MEFs
additional information
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UV irradiation leads to an almost complete disappearance of mitochondrial Omi/HtrA2 and a parallel appearance of Omi/HtrA2 in the cytoplasm, induction of Omi/HtrA2 binding to ped/pea-15
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additional information
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HtrA2/Omi protein levels are upregulated several fold when the unfolded protein response is triggered by heat shock. Transient exposure to elevated temperatures augments the protease activity of human HtrA2/Omi
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additional information
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phosphorylation of HtrA2 increases its proteolytic activtiy. PINK1 modulates the levels of phosphorylated HtrA2. Activation of MEKK3 induces efficient phosphorylation of both full-length and processed HtrA2 on Ser142. In vitro, p38 is also able to phosphorylate around Ser142
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additional information
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serine/threonine kinases Akt1 and Akt2 phosphorylate mitochondria-released HtrA2/Omi on serine 212 in vivo and in vitro, which results in attenuation of its serine protease activity and pro-apoptotic function. Akt phosphorylation of HtrA2/Omi at serine 212 is a critical event for attenuation of HtrA2/Omi cleaving X-linked inhibitor of apoptosis protein, although it does not affect HtrA2/Omi-X-linked inhibitor of apoptosis protein complex formation
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additional information
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HtrA2 protein level is gradually and significantly increased by up to 10fold in the mitochondria under tunicamycin-induced ER stress
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additional information
HtrA2/Omi levels rise dramatically within mitochondria at late times during infection with cytomegalovirus
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additional information
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apoptotic stimuli induce the activation of Omi and the consequent digestion of WTS by a caspase-independent mechanism
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additional information
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focal cerebral ischemia/reperfusion induces a mitochondrial up-regulation of Omi/HtrA2 and significantly increases cytosolic accumulation of Omi/HtrA2
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