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Information on EC 3.4.21.108 - HtrA2 peptidase and Organism(s) Mus musculus and UniProt Accession Q9JIY5
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EC Tree
3.4.21.108 HtrA2 peptidaseSpecify your search results
Word Map
- 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
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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
omi/htra2, htra2/omi, serine protease omi/htra2, serine protease htra2/omi, serine protease htra2, high temperature requirement a2, htra2 protease, omi/htra2 protease, omi protease, high temperature requirement protein a2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HtrA2 protease
-
-
-
-
HtrA2 serine protease
Omi
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
cleavage of C-N-linkage
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY
204655-80-1
-
SUBSTRATE
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
HS1-associated protein X-1 + H2O
?
-
HtrA2/Omi-mediated degradation of HS1-associated protein X-1 correlates with extensive cell death in response to etoposide, cisplatin and H2O2
-
-
?
receptor-interacting protein 1 + H2O
?
-
the HtrA2/Omi cleavage site receptor-interacting protein 1 is mapped to the intermediate domain and the corresponding N- and C-terminal fragments are impaired in their ability to activate nuclear factor-kappaB, c-Jun N-terminal kinase and p38 mitogen-activated protein kinase
-
-
?
ubiquitin carboxyl-terminal hydrolase L1 + H2O
?
-
natural substrate for HtrA2 in the apoptotic pathway. HtrA2 directly cleaves UCH-L1 and inhibits its hydrolase activity
-
-
?
X-linked inhibitor of apoptosis protein
?
-
HtrA2 promotes degradation of the X-linked inhibitor of apoptosis protein followed by subsequent caspase activation
-
-
?
beta-casein + H2O
?
-
cleaved to approximately 50% by GST-HtrA2 after a cleavage reaction for 1 h
-
-
?
additional information
?
-
loss of enzyme activity causes neuromuscular disorder
-
?
additional information
?
-
-
loss of enzyme activity causes neuromuscular disorder
-
?
additional information
?
-
-
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
-
?
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
ubiquitin carboxyl-terminal hydrolase L1 + H2O
?
-
natural substrate for HtrA2 in the apoptotic pathway. HtrA2 directly cleaves UCH-L1 and inhibits its hydrolase activity
-
-
?
additional information
?
-
loss of enzyme activity causes neuromuscular disorder
-
?
additional information
?
-
-
loss of enzyme activity causes neuromuscular disorder
-
?
additional information
?
-
-
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
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ucf-101
-
blocks protease activity of Omi, protects renal cells from cisplatin-induced cell death, mice treated with cisplatin and ucf-101 were more resistant to nephrotoxicy than animals treated with ciplatin alone
ucf-101
-
treatment of retinal epithelial cells with UCF-101 reduces the cytosolic translocation of HtrA2/Omi, attenuates caspase-3 activation, and decreases apoptosis
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
staurosporine
-
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
-
apoptotic stimuli induce the activation of Omi and the consequent digestion of WTS by a caspase-independent mechanism
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
myocardial ischemia/reperfusion results in Omi/HtrA2 translocation from the mitochondria to the cytosol along with cytochrome c
-
H2O2-induced oxidative damage of retinal pigment epithelial cells results in HtrA2/Omi translocation from mitochondria to cytosol, leading to RPE cell apoptosis via a caspase-mediated pathway
-
HtrA2 in the intermembrane space of healthy cells, density of mitochondria decreased and showed abnormal forms in knockout mice
-
intermembrane space, HtrA2/Omi is required for mitochondrial homeostasis
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
physiological function
physiological function
pharmacological inhibition or genetic deletion of enzyme HtrA2/Omi protects from TNF-induced necroptosis. HtrA2/Omi does not cleave ubiquitin C-terminal hydrolase UCH-L1 during TNF-induced necroptosis, but rather induces monoubiquitination indicative for UCH-L1 activation. Correspondingly, pharmacologic or RNA interference-mediated inhibition of UCH-L1 protects from TNF-induced necroptosis
physiological function
protease HtrA2 restricts the activation of apoptosis-associated speck-like protein containing a caspase-recruitment domain, i.e. ASC, dependent NLRP3 and AIM2 inflammasomes, in a protease activity-dependent manner. Disruption of the protease activity of HtrA2 results in exacerbated NLRP3 and AIM2 inflammasome responses in macrophages ex vivo and systemically in vivo. HtrA2 protease activity regulates autophagy and controls the magnitude and duration of inflammasome signaling by preventing prolonged accumulation of the inflammasome adaptor ASC
malfunction
-
endogenous levels of Parkin are significantly decreased in wild-type (HtrA2+/+) mouse embryonic fibroblasts compared with those in HtrA2-knockout (HtrA2-/-) mouse embryonic fibroblasts under the same stress conditions
malfunction
-
fewer and abnormal mitochondria are found in HtrA2/Omi knockout mice photoreceptors and pigment epithelial cells
malfunction
-
in mouse embryonic HtrA2/omi knockout fibroblast cells the apoptosis-dependent cleavage of Wilms'tumor suppressor protein WT1 is prevented and expression of WT1 is upregulated
malfunction
-
in Omi/HtrA2 knockout mouse embryonic fibroblasts elongated mitochondria are found by live cell imaging. Electron microscopy confirm the mitochondrial morphology alterations and show abnormal cristae structure. Examining the levels of proteins involved in mitochondrial fusion, a selective up-regulation of optic atrophy protein 1 is shown. Complementation of knockout cells with human wild-type Omi/HtrA2 reverses the mitochondrial elongation phenotype and optic atrophy protein 1 alterations
malfunction
-
knockdown of Omi decreases the basal level of autophagy and increases the level of neurodegenerative proteins such as pathogenic A53T alpha-synuclein and truncated polyglutamine-expanded huntingtin, as well as the endogenous autophagy substrate p62
malfunction
-
Omi/HtrA2 knockout mice show significant increase in intramitochondrial reactive oxygen species and decreased mitochondrial membrane potential in MEF cells
malfunction
-
knockdown of HtrA2/Omi affords protection against interleukin-3 withdrawal-induced death in the presence of carbobenzoxy-valyl-analylaspartyl-[O-methyl]-fluoromethylketone
physiological function
-
Omi activates autophagy in a dose-dependent manner through digestion of Hax-1, Omi-induced autophagy facilitates the degradation of neurodegenerative proteins such as pathogenic A53T alpha-synuclein and truncated polyglutamine-expanded huntingtin, as well as the endogenous autophagy substrate p62. Omi is important in the cellular quality control of proteins involved in neurodegenerative diseases
physiological function
-
Omi/HtrA2 functionally and physically interacts with the mitochondrial fusion protein OPA1. Mitochondrial morphology relies on Omi/HtrA2 protease function
physiological function
-
cytosolic HtrA2 decreases ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1) protein level and its hydrolase activity through HtrA2-mediated cleavage of UCH-L1 under apoptotic conditions. HtrA2-mediated cleavage of UCH-L1 plays important roles in regulating the fine balance between cell growth and cell death
physiological function
-
HtrA2/Omi plays a role in caspase-independent cell death during growth factor withdrawal by cleaving receptor-interacting protein 1
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HTRA2_MOUSE
458
1
49348
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
61790
-
GST-HtrA2, calculated by the Compute pI/Mw method at the ExPASy proteomics server of the Swiss Institute of Bioinformatics
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S276C
loss of protease activity, maturation and IAP-binding activity are not affected
HtrA2DELTA134-349
-
mutant, deletion of protease domain, no interaction with Hax1
HtrA2DELTAMTS
-
mutant, deletion of MTS domain, weaker interaction with Hax1 detected
HtrA2DELTAMTS-PDZ
-
mutant, deletion of MTS and PDZ domain, weaker interaction with Hax1 detected
HtrA2DELTAPDZ
-
mutant, deletion of PDZ domain, strong interaction with Hax1 detected
S276C
S306A
additional information
S276C
-
HtrA2/Omi appears to be correctly processed in cells derived from Mnd2 mice (motor neuron degeneration 2), which are homozygous for a naturally occurring Ser276Cys mutation in the HtrA2/Omi protease domain that greatly reduces its catalytic activity. Mnd2 mice display Parkinsonian phenotype, fail to gain weight, and organs such as the heart, thymus and spleen are dramatically smaller when compared to wild-type littermates. Reduced body weight and progressive loss of neurons in the striatum of the basal ganglia are also evident in mice with a targeted deletion of the HtrA2/Omi gene. HtrA2/Omi-/- mice display a lack of coordination, decreased mobility and tremor
S276C
-
motor neuron degeneration (mnd2) mice. Level of cleavage product C161 is remarkably decreased in mnd2 mice in which the serine protease activity of HtrA2 is greatly reduced
additional information
-
HtrA2 knockout mice with general decrease in organ size and neurological abnormalities, deletion of HtrA2 results in a mitochondrial dysfunction, death of these mice ca. 30 days after birth
additional information
-
HtrA2 knockout MEFs, no endogenous PINK1. Show decreased mitochondrial membrane potential
additional information
-
mutations in the genes encoding HtrA proteins correlate with perinatal lethality in mice
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
rapid purification of GST-HtrA2/Omi fusion proteins under non-denaturing conditions by selective binding to glutathione-Sepharose 4B beads
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into plasmid pEGFPN3 and plasmid pGEX-4T1-FLAG. Expression of GST-HtrA2 fusion protein in BL21 cells and in HEK-293 cells
-
successful expression of full-length HtrA2/Omi as a GST fusion protein in Escherichia coli BL21 as compared to human HtrA2/Omi
-
ubiquitin carboxyl-terminal hydrolase L1 and HtrA2 are expressed as GST-fusion proteins in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after specific HtrA2 downregulation using RNAi, increased cell viability is measured in H2O2-treated ARPE-19 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
additional information
medicine
-
HtrA2 knockout mice display features characteristic of a Parkinson syndrome, deletion of HtrA2 results in increased susceptibility to cell death stimuli, Smac/DIABOLO can compensate for the removal of HtrA2 in terms of neutralizing inhibitor of apoptosis proteins
medicine
-
myocardial ischemia/reperfusion significantly increases cytosolic Omi/HtrA2 content and markedly increases apoptosis, ucf-101 can inhibit apoptosis
medicine
-
way to limit renal injury by specifically inhibiting its proteolytic activity
medicine
loss of HtrA2 function might contribute to the activation of a stress response of mitochondrial origin in the brain that promotes neurodegeneration
medicine
-
the function of Omi/HtrA2 is linked to selective vulnerability of striatal neurons in Huntingtons disease
medicine
-
therapeutic interventions that inhibit HtrA2/Omi expression, translocation, or protease activity may represent novel therapeutic strategies for retinal pigment epithelial cells and retinal pigment epithelial cells-related diseases
additional information
-
a role for Omi-mediated processing of WTS in negative regulation of cell cycle progression at interphase. Omi protease is not necessarily required for cell death
additional information
-
simple and rapid strategy for molecular cloning using a gel-free and antibiotic selection method, which allows for the complete elimination of DNA extraction by gel electrophoresis, and thus has several advantages over gel-based cloning methods, including a cloning efficiency that is approximately 10times higher due to the prevention of ethidium bromide ultraviolet-induced DNA damage and contamination with ligase inhibitors, the amount of plasmid DNA required is approximately five times less, and cloning time is several hours less
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vaux, D.L.; Silke, J.
Mammalian mitochondrial IAP binding proteins
Biochem. Biophys. Res. Commun.
304
499-504
2003
Mus musculus
Gray, C.W.; Ward, R.V.; Karran, E.; Turconi, S.; Rowles, A.; Viglienghi, D.; Southan, C.; Barton, A.; Fantom, K.G.; West, A.; Savopoulos, J.; Hassan, N.J.; Clinkenbeard, H.; Hanning, C.; Amegadzie, B.; Davis, J.B.; Dingwall, C.; Livi, G.P.; Creasy, C.L.
Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response
Eur. J. Biochem.
267
5699-5710
2000
Homo sapiens (O43464), Mus musculus (Q9JIY5)
Jones, J.M.; Datta, P.; Srinivasula, S.M.; Ji, W.; Gupta, S.; Zhang, Z.; Davies, E.; Hajnoczky, G.; Saunders, T.L.; Van Keuren, M.L.; Fernandes-Alnemri, T.; Meisler, M.H.; Alnemri, E.S.
Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice
Nature
425
721-727
2003
Mus musculus (Q9JIY5), Mus musculus
Cilenti, L.; Kyrizis, G.A.; Soundarapandian, M.M.; Stratico, V.; Yerkes, A.; Park, K.M.; Sheridan, A.M.; Alnemri, E.S.; Bonventre, J.V.; Zervos, A.S.
Omi/HtrA2 protease mediates cisplatin-induced cell death in renal cells
Am. J. Physiol. Renal Physiol.
288
F371-F379
2005
Homo sapiens, Mus musculus, Mus musculus C57BL6
Liu, H.R.; Gao, E.; Hu, A.; Tao, L.; Qu, Y.; Most, P.; Koch, W.J.; Christopher, T.A.; Lopez, B.L.; Alnemri, E.S.; Zervos, A.S.; Ma, X.L.
Role of Omi/HtrA2 in apoptotic cell death after myocardial ischemia and reperfusion
Circulation
111
90-96
2005
Mus musculus, Rattus norvegicus
Seong, Y.M.; Choi, J.Y.; Park, H.J.; Kim, K.J.; Ahn, S.G.; Seong, G.H.; Kim, I.K.; Kang, S.; Rhim, H.
Autocatalytic processing of HtrA2/Omi is essential for induction of caspase-dependent cell death through antagonizing XIAP
J. Biol. Chem.
279
37588-37596
2004
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Martins, L.M.; Morrison, A.; Klupsch, K.; Fedele, V.; Moisoi, N.; Teismann, P.; Abuin, A.; Grau, E.; Geppert, M.; Livi, G.P.; Creasy, C.L.; Martin, A.; Hargreaves, I.; Heales, S.J.; Okada, H.; Brandner, S.; Schulz, J.B.; Mak, T.; Downward, J.
Neuroprotective role of the Reaper-related serine protease HtrA2/Omi revealed by targeted deletion in mice
Mol. Cell. Biol.
24
9848-9862
2004
Mus musculus
Seong, Y.M.; Park, H.J.; Seong, G.H.; Choi, J.Y.; Yoon, S.J.; Min, B.R.; Kang, S.; Rhim, H.
N-terminal truncation circumvents proteolytic degradation of the human HtrA2/Omi serine protease in Escherichia coli: rapid purification of a proteolytically active HtrA2/Omi
Protein Expr. Purif.
33
200-208
2004
Homo sapiens (O43464), Homo sapiens, Mus musculus
Kim, G.Y.; Nam, M.K.; Kim, S.S.; Kim, H.Y.; Lee, S.K.; Rhim, H.
A simple and rapid strategy for the molecular cloning and monitoring of mouse HtrA2 serine protease
Biotechnol. Lett.
30
397-403
2008
Mus musculus
Vande Walle, L.; Lamkanfi, M.; Vandenabeele, P.
The mitochondrial serine protease HtrA2/Omi: an overview
Cell Death Differ.
15
453-460
2008
Bacillus sp. (in: Bacteria), Bos taurus, Canis lupus familiaris, Clostridium sp., Drosophila melanogaster, Escherichia coli, Homo sapiens, Macaca mulatta, Mesorhizobium loti, Mus musculus, no activity in Caenorhabditis elegans, no activity in Mycoplasma genitalium, no activity in Mycoplasma pneumoniae, Rattus norvegicus
Park, H.J.; Kim, S.S.; Seong, Y.M.; Kim, K.H.; Goo, H.G.; Yoon, E.J.; Min, d.o..S.; Kang, S.; Rhim, H.
Beta-amyloid precursor protein is a direct cleavage target of HtrA2 serine protease. Implications for the physiological function of HtrA2 in the mitochondria
J. Biol. Chem.
281
34277-34287
2006
Homo sapiens, Mus musculus
Plun-Favreau, H.; Klupsch, K.; Moisoi, N.; Gandhi, S.; Kjaer, S.; Frith, D.; Harvey, K.; Deas, E.; Harvey, R.J.; McDonald, N.; Wood, N.W.; Martins, L.M.; Downward, J.
The mitochondrial protease HtrA2 is regulated by Parkinsons disease-associated kinase PINK1
Nat. Cell Biol.
9
1243-1252
2007
Homo sapiens, Mus musculus
Kuninaka, S.; Iida, S.I.; Hara, T.; Nomura, M.; Naoe, H.; Morisaki, T.; Nitta, M.; Arima, Y.; Mimori, T.; Yonehara, S.; Saya, H.
Serine protease Omi/HtrA2 targets WARTS kinase to control cell proliferation
Oncogene
26
2395-2406
2007
Homo sapiens, Mus musculus, synthetic construct
Moisoi, N.; Klupsch, K.; Fedele, V.; East, P.; Sharma, S.; Renton, A.; Plun-Favreau, H.; Edwards, R.E.; Teismann, P.; Esposti, M.D.; Morrison, A.D.; Wood, N.W.; Downward, J.; Martins, L.M.
Mitochondrial dysfunction triggered by loss of HtrA2 results in the activation of a brain-specific transcriptional stress response
Cell Death Differ.
16
449-464
2009
Mus musculus (Q8BHC7)
Inagaki, R.; Tagawa, K.; Qi, M.L.; Enokido, Y.; Ito, H.; Tamura, T.; Shimizu, S.; Oyanagi, K.; Arai, N.; Kanazawa, I.; Wanker, E.E.; Okazawa, H.
Omi /HtrA2 is relevant to the selective vulnerability of striatal neurons in Huntingtons disease
Eur. J. Neurosci.
28
30-40
2008
Homo sapiens, Mus musculus, Rattus norvegicus
Chao, J.R.; Parganas, E.; Boyd, K.; Hong, C.Y.; Opferman, J.T.; Ihle, J.N.
Hax1-mediated processing of HtrA2 by Parl allows survival of lymphocytes and neurons
Nature
452
98-102
2008
Mus musculus
Krick, S.; Shi, S.; Ju, W.; Faul, C.; Tsai, S.Y.; Mundel, P.; Boettinger, E.P.
Mpv17l protects against mitochondrial oxidative stress and apoptosis by activation of Omi/HtrA2 protease
Proc. Natl. Acad. Sci. USA
105
14106-14111
2008
Chlorocebus aethiops, Homo sapiens, Mus musculus
Park, H.M.; Kim, G.Y.; Nam, M.K.; Seong, G.H.; Han, C.; Chung, K.C.; Kang, S.; Rhim, H.
The serine protease HtrA2/Omi cleaves Parkin and irreversibly inactivates its E3 ubiquitin ligase activity
Biochem. Biophys. Res. Commun.
387
537-542
2009
Homo sapiens, Mus musculus
Kieper, N.; Holmstroem, K.M.; Ciceri, D.; Fiesel, F.C.; Wolburg, H.; Ziviani, E.; Whitworth, A.J.; Martins, L.M.; Kahle, P.J.; Krueger, R.
Modulation of mitochondrial function and morphology by interaction of Omi/HtrA2 with the mitochondrial fusion factor OPA1
Exp. Cell Res.
316
1213-1224
2010
Drosophila melanogaster, Homo sapiens, Mus musculus
Ding, X.; Patel, M.; Shen, D.; Herzlich, A.A.; Cao, X.; Villasmil, R.; Klupsch, K.; Tuo, J.; Downward, J.; Chan, C.C.
Enhanced HtrA2/Omi expression in oxidative injury to retinal pigment epithelial cells and murine models of neurodegeneration
Invest. Ophthalmol. Vis. Sci.
50
4957-4966
2009
Mus musculus
Hartkamp, J.; Carpenter, B.; Roberts, S.G.
The Wilms tumor suppressor protein WT1 is processed by the serine protease HtrA2/Omi
Mol. Cell
37
159-171
2010
Homo sapiens, Mus musculus
Li, B.; Hu, Q.; Wang, H.; Man, N.; Ren, H.; Wen, L.; Nukina, N.; Fei, E.; Wang, G.
Omi/HtrA2 is a positive regulator of autophagy that facilitates the degradation of mutant proteins involved in neurodegenerative diseases
Cell Death Differ.
17
1773-1784
2010
Mus musculus
Park, D.W.; Nam, M.K.; Rhim, H.
The serine protease HtrA2 cleaves UCH-L1 and inhibits its hydrolase activity: Implication in the UCH-L1-mediated cell death
Biochem. Biophys. Res. Commun.
415
24-29
2011
Mus musculus
Vande Walle, L.; Wirawan, E.; Lamkanfi, M.; Festjens, N.; Verspurten, J.; Saelens, X.; Vanden Berghe, T.; Vandenabeele, P.
The mitochondrial serine protease HtrA2/Omi cleaves RIP1 during apoptosis of Ba/F3 cells induced by growth factor withdrawal
Cell Res.
20
421-433
2010
Mus musculus
Sosna, J.; Voigt, S.; Mathieu, S.; Kabelitz, D.; Trad, A.; Janssen, O.; Meyer-Schwesinger, C.; Schuetze, S.; Adam, D.
The proteases HtrA2/Omi and UCH-L1 regulate TNF-induced necroptosis
Cell Commun. Signal.
11
76
2013
Mus musculus (Q9JIY5)
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