3.4.22.62: caspase-9
This is an abbreviated version!
For detailed information about caspase-9, go to the full flat file.
Word Map on EC 3.4.22.62
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3.4.22.62
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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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tunel
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necrosis
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apoptosis-related
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caspase-dependent
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apoptosis-inducing
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jnk
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apaf-1
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annexin
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extrinsic
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cyclin
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leukemia
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bid
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neuroprotective
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depolarization
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polyadp-ribose
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survivin
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hoechst
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z-vad-fmk
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antiproliferative
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adp-ribose
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xiap
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iodide
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deoxynucleotidyl
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mitochondria-dependent
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mitochondria-mediated
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cisplatin
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dutp
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fadd
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procaspase-3
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caspase-mediated
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pan-caspase
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fas-mediated
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trail
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fas-associated
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trail-induced
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bcl-2-associated
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apoptogenic
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pharmacology
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cdc25c
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puma
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transferase-mediated
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executioner
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factor-related
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deltapsim
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medicine
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tunel-positive
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sub-g1
- 3.4.22.62
- caspase-3
- bcl-2
- parp
-
anti-apoptotic
-
pro-apoptotic
-
tunel
- necrosis
-
apoptosis-related
-
caspase-dependent
-
apoptosis-inducing
- jnk
- apaf-1
-
annexin
-
extrinsic
- cyclin
- leukemia
- bid
-
neuroprotective
-
depolarization
-
polyadp-ribose
- survivin
-
hoechst
- z-vad-fmk
-
antiproliferative
- adp-ribose
- xiap
- iodide
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deoxynucleotidyl
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mitochondria-dependent
-
mitochondria-mediated
- cisplatin
- dutp
- fadd
- procaspase-3
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caspase-mediated
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pan-caspase
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fas-mediated
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trail
-
fas-associated
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trail-induced
-
bcl-2-associated
-
apoptogenic
- pharmacology
- cdc25c
- puma
-
transferase-mediated
-
executioner
-
factor-related
-
deltapsim
- medicine
-
tunel-positive
-
sub-g1
Reaction
strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp-/-Xaa =
Synonyms
APAF, Apaf-3, apoptotic protease activating factor 3, apoptotic protease Mch-6, C14.010, CASP-9, casp9, casp9-gamma, caspase 9, caspase-9, ICE-LAP6, ICE-like apoptotic protease 6, Mch6
ECTree
3.4.22.62 caspase-9Advanced search results
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results (Posttranslational Modification
Posttranslational Modification on EC 3.4.22.62 - caspase-9
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POSTTRANSLATIONAL MODIFICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
nitrosylation
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nitrosylation of caspase-9 at C163 is dependent, at least in part, on subcellular localization. 68% of the procaspase-9 in mitochondria is nitrosylated and 11% of the procaspase-9 in the cytoplasm in unstimulated 10C9 human B cells
phosphoprotein
proteolytic modification
phosphoprotein
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kinase Akt and p21-Ras, an Akt activator, induce phosphorylation of pro-caspase-9 in cells. Akt phosphorylates recombinant caspase-9 in vitro on Ser196 and inhibits its protease activity. Mutant pro-caspase9(Ser196Ala) is resistant to Akt-mediated phosphorylation
phosphoprotein
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caspase-9 is phosphorylated on Thr125 in a MEK172-dependent manner in vivo, efficiently phosphorylated on Thr125 by ERK in vitro. Phosphorylation of Thr125 on caspase-9 may be an important mechanism through which growth factor and survival signals that activate the ERK MAPK pathway can inhibit apoptosis
phosphoprotein
the enzyme is proteolytically processed into an active cysteine protease
phosphoprotein
CPP32 processes pro-Mch6 preferentially at Asp330 to generate two subunits of molecular masses 37000 Da and 10000 Da. Granzyme B can also process pro-Mch6 but at a site N-terminal to that cleaved by CPP32 and generates two cleavage products, a large 35000 Da product and a small 12000 Da product
phosphoprotein
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the kinases PKB-Akt and ERK2 are involved in the phosphorylation of human caspase-9 at Ser196 and Thr125, respectively
phosphoprotein
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caspase-9 is phosphorylated at Thr125 in cells by ERK1/2 but not by c-Jun N-terminal kinases or p38 MAPKs
phosphoprotein
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caspase-9 is regulated during cell cycle through periodic phosphorylation at an inhibitory site, Thr125. This site is phosphorylated by CDK1/cyclin B1 during mitosis and in response to microtubule poisons that arrest cells at this stage of the cell cyclce. Phosphorylation of caspase-9 at Thr125 protects mitoctic cells against apoptosis
phosphoprotein
phophorylation of caspase-9 at the inhibitory threonine residue 125 catalyzed by the protein kinase DYRK1A
phosphoprotein
phophorylation of the inhibitory threonine residue 125, catalyzed by the protein kinase DYRK1A
phosphoprotein
phosphorylation of caspase-9 by casein kinase 2 (CK2) on a serine near the site of caspase-8 cleavage, TNF receptor cross-linking promotes dephosphorylation of caspase-9, phosphorylation of caspase-9 by casein kinase 2 (CK2) decreases its susceptibility to cleavage by active caspase-8
proteolytic modification
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Apaf-1-mediated processing of procaspase-9 occurs at Asp315 by an intrinsic autocatalytic activity of procaspase-9 itself. Apaf-1 can form oligomers and may facilitate procaspase-9 autoactivation by oligomerizing its precursor molecules
proteolytic modification
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proteolytic processing is associated with the removal of a leader sequence, processing by caspase-3 at amino acid 130 and 330. Autolytic processing at amino acid 307 and 315
proteolytic modification
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proteolytic processing is associiated with the removal of a leader sequence, processing by caspase-3 at amino acid 130 and 330. Autolytic processing at amino acid 307 and 315
proteolytic modification
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initiator pro-caspases exist as monomers and possess long pro-domains. These pro-domains contain specific protein-protein interaction sites that are crucial for initiator caspase activation. The pro-domain of caspases-9 contain a caspase activation recruitment domain (CARD) motif. Release of cytochrome-c and other proapoptotic proteins into the cytosol results in the formation of the apoptosome, the activation platform for initiator caspase-9. Flexible linkers connect the caspase activation recruitment domain (CARD) with the large subunit and the large subunit with the small subunit. The linker between the large and small subunits contains the caspase-9 auto-cleavage site (D315). Cleavage at this site generates the p35/p12 form of caspase-9. The p35/p12 form can be further processed by caspase-3 by cleavage at site D330, generating caspase-9
proteolytic modification
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the uncleaved monomeric zymogen of caspase-9 has very low activity, which is increased upon dimerization. In dimeric caspase-9 cleavage at a specific aspartate residue in the intersubuint linker between the large and small subunits is required for caspase-9 to attain increased activity
proteolytic modification
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when bound to the apoptosome, caspase-9 is processed at Asp315, resulting in a CARD-large subunit portion of the enzyme and a small subunit beginning with the N-terminal sequence of ATPF. Proteolytic removal of the CARD domain from the large subunit, which results in decreased activity, is also observed. Processed caspase-9 can be displaced from the apoptosome by additional molecules of procaspase-9, resulting in release of cleaved caspase-9, which can form active dimers
proteolytic modification
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incubation of cytosol from rat kidney proximal tubule cells with cytochrome c and dATP results in rapid autocatalytic processing of procaspase-9 from 50000 Da to 38000 Da size fragment. Cytochrome c concentration influences the production of alternatively processed forms of caspase-9. At lower cytochrome c concentration, two fragments of caspase-9 of the size 38000 Da and 40000 Da are produced. At higher concentrations of cytochrome c only 38000 Da fragment is detected
