3.4.22.63: caspase-10
This is an abbreviated version!
For detailed information about caspase-10, go to the full flat file.
Word Map on EC 3.4.22.63
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3.4.22.63
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caspase-8
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necrosis
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fadd
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trail
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apoptosis-inducing
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bid
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lymphoproliferative
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factor-related
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death-inducing
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fas-associated
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casp11
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fas-mediated
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trail-induced
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c-flips
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tnf-related
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lymphadenopathy
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faslg
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caspase-8-deficient
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trail-mediated
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cflar
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apaf-1
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z-ietd-fmk
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tnf-r1
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trail-resistant
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template-based
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medicine
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pharmacology
- 3.4.22.63
- caspase-8
- necrosis
- fadd
-
trail
-
apoptosis-inducing
- bid
-
lymphoproliferative
-
factor-related
-
death-inducing
-
fas-associated
-
casp11
-
fas-mediated
-
trail-induced
- c-flips
-
tnf-related
- lymphadenopathy
-
faslg
-
caspase-8-deficient
-
trail-mediated
-
cflar
- apaf-1
-
z-ietd-fmk
-
tnf-r1
-
trail-resistant
-
template-based
- medicine
- pharmacology
Reaction
strict requirement for Asp at position P1 and has a preferred cleavage sequence of Leu-Gln-Thr-Asp-/-Gly =
Synonyms
apoptotic protease Mch-4, C14.011, CASP10, caspase 10, caspase-10, caspase-10/b, caspase-10beta, FAS-associated death domain protein interleukin-1B-converting enzyme 2, FLICE2, ICE-like apoptotic protease 4, Mch4
ECTree
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Engineering
Engineering on EC 3.4.22.63 - caspase-10
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D219A
involved in proteolytic activation, essential for CASP10-induced cell death
D297A
site-directed mutagenesis, the single mutation D297A completely abrogates autocleavage between the subunits, the purified mutant is a single chain of 35 kDa. The cleavage site mutant has restricted specificity and highly reduced activity on protein substrates, overview
D416A
involved in proteolytic activation, essential for CASP10-induced cell death
I406L
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impairs apoptosis when transfected alone and dominantly inhibits apoptosis mediated by wild-type caspase-10 in a co-transfection assay
L285F
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impairs apoptosis when transfected alone and dominantly inhibits apoptosis mediated by wild-type caspase-10 in a co-transfection assay
L285P
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the mutation may contribute to the pathogenesis of factions of T-acute lymphoblastic leukemia and multiple myeloma
R21C
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the mutation may contribute to the pathogenesis of factions of T-acute lymphoblastic leukemia and multiple myeloma
V410I
Y446C
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no dominant negative effect in co-transfection assay into H9 lymphocytic cell line
additional information
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no dominant negative effect in co-transfection assay into H9 lymphocytic cell line. Protection from severe disease by caspase-10 V410I in 63 families with autoimmune lymphoproliferative syndrome Ia due to dominant Fas mutation
V410I
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the mutation in caspase-10, that is associated with autoimmune lymphoproliferative syndrome, ALPS, is a common polymorphism in the healthy Danish population
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somatic mutation of caspase-10 is rare in colon, breast, lung, and hepatocellular carcinomas, caspase-10 mutation may contribute to the pathogenesis of some colon carcinomas
additional information
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caspase-10 isoforms are transiently downregulated using siRNAs targeting all caspase-10 isoforms, or siRNAs specific for individual caspase-10 isoforms. Downregulation of individual or all caspase-10 isoforms in SH-EP cells does not affect TRAIL sensitivity
additional information
construction of a truncated mutant lacking the first 202 residues, and of the truncation mutant with a substitution D297A in the catalytic site, cloning into a vector with chimeric protein with an N-terminal His-tag followed by the Fv-domain. Chemically inducible dimerization fusions activate the wild-type but not the cleavage site mutant caspase-10
additional information
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construction of a truncated mutant lacking the first 202 residues, and of the truncation mutant with a substitution D297A in the catalytic site, cloning into a vector with chimeric protein with an N-terminal His-tag followed by the Fv-domain. Chemically inducible dimerization fusions activate the wild-type but not the cleavage site mutant caspase-10