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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Posttranslational Modification
Posttranslational Modification on EC 3.4.22.63 - caspase-10
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proteolytic modification
Mch4 is derived from a single chain proenzym, granzyme B cleaves proMch4 at a IXXD-A processing sequence to produce mature Mch4
proteolytic modification
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proMch4 can autoprocess after Asp-219 and Asp-372 to generate the two subunits of the mature enzyme : P17, the large subunit and p12, the small subunit
proteolytic modification
autoprocessing, the wild-type 55000 Da GST fusion protein is cleaved to the 43000 Da active form
proteolytic modification
caspase-10/c and caspase-10/d are splice isoforms. Caspase-10/c is a truncated protein that is essentially a prodomain-only form of the caspase. Caspase-10/d is a hybrid of caspase-10/a (Mch4) and caspase-10/b (FLICE2), as it is identical to FLICE2 except for the small p12 catalytic subunit, which is identical to Mch4
proteolytic modification
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caspase-10 is activated at the DISC, downstream of death-receptor signaling. Caspases-8 and -10 are recruited to the DISC as intact monomers and recruitment of the caspases to the DISC subsequently leads to their dimerization and activation through induced proximity, mechanism, overview
proteolytic modification
procaspase-10 is activated to caspase-10, mechanism of activation and the role of the inter-subunit cleavage, overview. Caspase-10 follows the proximity-induced dimerization model for apical caspases
proteolytic modification
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procaspase-10 is activated to caspase-10. Activation of caspase-10 is induced in apoptosis