3.4.22.60: caspase-7
This is an abbreviated version!
For detailed information about caspase-7, go to the full flat file.
Word Map on EC 3.4.22.60
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3.4.22.60
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caspase-3
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bcl-2
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parp
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anti-apoptotic
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pro-apoptotic
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executioner
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necrosis
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polyadp-ribose
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caspase-dependent
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annexin
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tunel
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survivin
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cyclin
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apoptosis-inducing
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adp-ribose
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apoptosis-related
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bid
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xiap
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calpains
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pan-caspase
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jnk
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cdk2
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hoechst
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caspase-mediated
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antiproliferative
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apaf-1
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z-vad-fmk
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caspase-3-like
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pyroptosis
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ac-devd-cho
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apoptosome
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template-based
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puma
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trail-induced
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devd
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caspase-3-deficient
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mitochondria-dependent
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procaspase
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apoptosis-associated
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molecular biology
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casp10
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spinocerebellar
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sub-g1
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medicine
- 3.4.22.60
- caspase-3
- bcl-2
- parp
-
anti-apoptotic
-
pro-apoptotic
-
executioner
- necrosis
-
polyadp-ribose
-
caspase-dependent
-
annexin
-
tunel
- survivin
- cyclin
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apoptosis-inducing
- adp-ribose
-
apoptosis-related
- bid
- xiap
- calpains
-
pan-caspase
- jnk
- cdk2
-
hoechst
-
caspase-mediated
-
antiproliferative
- apaf-1
- z-vad-fmk
-
caspase-3-like
-
pyroptosis
- ac-devd-cho
- apoptosome
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template-based
- puma
-
trail-induced
- devd
-
caspase-3-deficient
-
mitochondria-dependent
-
procaspase
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apoptosis-associated
- molecular biology
- casp10
-
spinocerebellar
-
sub-g1
- medicine
Reaction
strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-/- =
Synonyms
apoptotic protease Mch-3, C14.004, Casp-7, Casp7, caspase 7, caspase-7, CMH-1, cystein aspartic-specific protease-7, DEVDase, ICE-LAP3, ICE-like apoptotic protease 3, LICE2 cysteine protease, More, SCA-2, SREBP cleavage activity 2
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 3.4.22.60 - caspase-7
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proteolytic modification
proteolytic modification
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viral nucleocapsid protein of transmissible gastroenteritis coronavirus triggers the processing of procaspase 6 in human rectal tumor cell line HRT18jap1
proteolytic modification
Mch3alpha is made of two subunits derived from a precursor ProMch3alpha. Asp23 and Asp198 are the most likely processing sites. Bacterially expressed Mch3 has intrinsic autocatalytic and autoactivation activity
proteolytic modification
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the N-peptide of caspase-7 must be removed, probably be caspase-3, before efficient activation of the zymogen can occur in vivo. The N-peptide serves to physically sequester the caspase-7 zymogen in a cytosolic location that prevents access by upstream activators, caspase-8, caspase-9 and caspase-10
proteolytic modification
both Mch4 and the serine protease granzyme B cleave proMch3 at a conserved IXXD-S sequence to produce the large and small subunits of the active protease. Mch3 is a target of mature protease in apoptotic cells
proteolytic modification
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the 12000 Da and the 11000 Da polypeptides are generated by processing of the CMH-1 protein at Asp198-Ser199 and to a lesser extent at Asp206-Ala207
proteolytic modification
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caspase-7 possesses two cleavage sites after Asp23 and Asp198
proteolytic modification
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procaspase-7 is activated by processing to the mature caspase-7
proteolytic modification
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procaspase-7 is cleaved at Asp198 and Asp206 and activated by caspase-2
proteolytic modification
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the procaspase-7 is cleaved to active enzyme by eliminating the prodomain, blocked by inhibitor carbobenzyloxy-DEVD-fluoromethyl ketone
proteolytic modification
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cleavage of procaspase-7 of 35 kDa to the active forms of 31 and 20 kDa, TNF-induced caspase-7 activation takes place exclusively within TNF receptosomes
proteolytic modification
enzyme is synthesized as an inactive 30000-35000 Da precursor and is thought to be cleaved during apoptosis to generate active fragments of 20000 Da and 10000 Da
proteolytic modification
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procaspase-7 is activated by caspase-1 cleavage to caspase-7
proteolytic modification
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procaspase-7 is activated by caspase-1 cleavage to caspase-7
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