3.4.22.55 Ac-DEVD-7-amino-4-trifluoromethyl coumarin + H2O 37°C, pH 7.0, 10 mM dithiothreitol Homo sapiens 7-amino-4-trifluoromethyl coumarin + Ac-DEVD - ? 381307 3.4.22.55 Ac-VDVAD-7-amido-4-trifluoromethylcoumarin + H2O - Homo sapiens Ac-VDVAD + 7-amido-4-trifluoromethylcoumarin - ? 418436 3.4.22.55 acetyl-DEHD-7-amido-4-methylcoumarin + H2O DEHD is the optimal tetrapeptide recognition motif Homo sapiens acetyl-DEHD + 7-amino-4-methylcoumarin - ? 362413 3.4.22.55 acetyl-Val-Asp-Val-Ala-Asp-4-nitroanilide + H2O - Homo sapiens acetyl-Val-Asp-Val-Ala-Asp + 4-nitroaniline - ? 414234 3.4.22.55 acetyl-VDQQD-4-nitroanilide + H2O - Homo sapiens acetyl-VDQQD + 4-nitroaniline - ? 361998 3.4.22.55 acetyl-VDVAD-4-nitroanilide + H2O - Homo sapiens acetyl-VDVAD + 4-nitroaniline - ? 362416 3.4.22.55 acetyl-VDVADGW-amide + H2O preferred peptide substrate Homo sapiens ? - ? 362414 3.4.22.55 all-spectrin + H2O - Homo sapiens ? - ? 430871 3.4.22.55 alpha-all-spectrin + H2O - Mus musculus ? - ? 430872 3.4.22.55 alpha-II-spectrin + H2O - Homo sapiens ? - ? 381395 3.4.22.55 BID + H2O - Mus musculus ? - ? 361973 3.4.22.55 BID + H2O - Homo sapiens ? - ? 361973 3.4.22.55 BID + H2O - Mus musculus ? Bid is cleaved at D59 ? 361973 3.4.22.55 BID + H2O - Xenopus laevis ? Bid is cleaved at D59 ? 361973 3.4.22.55 BID + H2O 37°C, pH 7.0, 10 mM dithiothreitol Homo sapiens ? - ? 361973 3.4.22.55 BID + H2O caspase-2 cleaves BID in response 16 to endoplasmic reticulum stress. Resistance to endoplasmic reticulum stress-induced apoptosis can be conferred by inhibiting caspase-2 activity Mus musculus ? - ? 361973 3.4.22.55 Bid + H2O active caspase-2 cleaves Bid to form tBid, which induces mitochondrial outer membrane permeabilization Mus musculus tBid + ? - ? 417899 3.4.22.55 Bid + H2O active caspase-2 cleaves Bid to form tBid, which induces mitochondrial outer membrane permeabilization Homo sapiens tBid + ? - ? 417899 3.4.22.55 caspase-2 + H2O self-cleavage Mus musculus ? - ? 430922 3.4.22.55 caspase-2 + H2O self-cleavage for activation Mus musculus ? - ? 430922 3.4.22.55 catalytically inactive pro-caspase-2 + H2O 37°C, pH 7.0, 10 mM dithiothreitol Homo sapiens caspase-2 - ? 381625 3.4.22.55 CERT + H2O - Mus musculus ? - ? 430926 3.4.22.55 Cip1/p21 Bid + H2O - Homo sapiens ? - ? 381682 3.4.22.55 CUX1 + H2O - Mus musculus ? - ? 417928 3.4.22.55 CUX1 + H2O - Homo sapiens ? - ? 417928 3.4.22.55 CUX1 + H2O - Rattus norvegicus ? - ? 417928 3.4.22.55 cyclophilin A + H2O - Homo sapiens ? - ? 430950 3.4.22.55 DELTANp63 + H2O - Mus musculus ? - ? 430957 3.4.22.55 desmoplakin + H2O - Homo sapiens ? - ? 430960 3.4.22.55 DEVD-AFC + H2O - Homo sapiens DEVD + AFC - ? 381788 3.4.22.55 DNp63a + H2O - Homo sapiens ? - ? 430965 3.4.22.55 elF4B + H2O - Mus musculus ? - ? 430969 3.4.22.55 eukaryotic translation initiation factor 4B + H2O Asp563 in eukaryotic translation initiation factor 4B is a caspase-2-preferred cleavage site Homo sapiens ? - ? 430982 3.4.22.55 fatty acid binding protein 5 + H2O - Homo sapiens ? - ? 430991 3.4.22.55 golgin-160 + H2O cleavage site is ESPD59G Homo sapiens p163 fragment + ? - ? 362412 3.4.22.55 golgin-160 + H2O - Mus musculus ? - ? 382009 3.4.22.55 golgin-160 + H2O - Homo sapiens ? - ? 382009 3.4.22.55 golgin-160 + H2O caspase-2-specific substrate Homo sapiens ? - ? 382009 3.4.22.55 HDAC4 + H2O - Homo sapiens ? - ? 431005 3.4.22.55 HDAC4 + H2O - Mus musculus ? - ? 431005 3.4.22.55 huntingtin + H2O - Homo sapiens ? - ? 362235 3.4.22.55 huntingtin + H2O - Mus musculus ? - ? 362235 3.4.22.55 ICAD + H2O - Mus musculus ? - ? 392245 3.4.22.55 ICAD + H2O - Homo sapiens ? - ? 392245 3.4.22.55 liposomes + H2O 22°C Homo sapiens permealized liposomes - ? 381792 3.4.22.55 MDM-2 + H2O - Homo sapiens ? - ? 431064 3.4.22.55 MDM2 + H2O active caspase-2 cleaves MDM2 to form MDM2 p60, which binds to and stabilizes p53 Mus musculus MDM2 p60 + ? - ? 418000 3.4.22.55 MDM2 + H2O active caspase-2 cleaves MDM2 to form MDM2 p60, which binds to and stabilizes p53 Homo sapiens MDM2 p60 + ? - ? 418000 3.4.22.55 Mdm2 + H2O Mdm2 is a key negative regulator of p53 Homo sapiens processed Mdm2 + p60 - ? 418001 3.4.22.55 Mdm2 + H2O Mdm2 contains a well-conserved caspase cleavage site, Asp-Val-Pro-Asp or DVPD, at which cleavage generates an 60 kDa N-terminal product. No activity with Mdm2 mutants D367A and D367E Homo sapiens processed Mdm2 + p60 - ? 418001 3.4.22.55 MDM2 + H2O - Mus musculus ? - ? 431065 3.4.22.55 Mdm2 protein + H2O - Homo sapiens ? - ? 448763 3.4.22.55 Mdm2 protein + H2O caspase-2 cleaves and inhibits Mdm2 and thereby promotes the stability of the tumor-suppressor p53 Homo sapiens ? - ? 448763 3.4.22.55 additional information the preferred cleavage sequence is DEHD-/- Homo sapiens ? - ? 89 3.4.22.55 additional information no cleavage of acetyl-YVAD-4-nitroanilide, acetyl-DEVD-4-nitroanilide, acetyl-VEID-4-nitroanilide and acetyl-VQVD-4-nitroanilide Homo sapiens ? - ? 89 3.4.22.55 additional information phenotype of animals deficient in caspase-2: increased number of oocytes at birth, and oocytes are less susceptible to doxorubicin-induced apoptosis. B cells are partially resistant to death induction by granzyme B, accelerated apoptosis of facial motor neurons Mus musculus ? - ? 89 3.4.22.55 additional information the enzyme is an apoptosis initiator Homo sapiens ? - ? 89 3.4.22.55 additional information PARP is not cleaved Homo sapiens ? - ? 89 3.4.22.55 additional information caspase 2 is involved in ischemia-reperfusion-induced germ-cell-specific apoptosis Mus musculus ? - ? 89 3.4.22.55 additional information caspase-2 activation regulates PS-341-induced mitochondrial depolarization and apoptosis, suggesting that caspase-2 can serve as a link between lysosomal and mitochondrial permeabilization Homo sapiens ? - ? 89 3.4.22.55 additional information caspase-2 initiates caspase cascade after trichostatin A treatment and involves the formation of the PIDDosome (a complex of caspase-2-CRADD/RAIDD-PIDD) Homo sapiens ? - ? 89 3.4.22.55 additional information caspase-2 protein substrate recognition and catalysis, structural basis for the essential P5 recognition of caspase-2, molecular replacement and modeling using the structure with PDB ID 1PYO, overview. The key residues involved in catalysis, including the catalytic dyad, formed by Thr380 and Tyr420, and the invariant Arg378, superpose with each other regardless of the peptide inhibitor binding. Caspase-2 uniquely prefers a pentapeptide, such as VDVAD, rather than a tetrapeptide, as required for efficient cleavage by other caspases. The P3 Val is only involved in main chain hydrogen bonds with Arg378, and its side chain makes no contacts with the enzyme. The nitrogen atom of P4 Asp forms a hydrogen bond with the carbonyl oxygen of Tyr420, and its side chain extensively interacts with the enzyme through hydrogen bonds with the backbone of Tyr420 and the side chains of Trp385, Asn379, Arg417, and Glu418 Homo sapiens ? - ? 89 3.4.22.55 additional information caspase-2 is a substrate for caspase-8 and caspase-3 Mus musculus ? - ? 89 3.4.22.55 additional information no activity with N-acetyl-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin Homo sapiens ? - ? 89 3.4.22.55 mouse double minute 2 homolog + H2O - Mus musculus ? - ? 431071 3.4.22.55 myotrophin + H2O - Homo sapiens ? - ? 431073 3.4.22.55 N-acetyl-DEVD-4-nitroanilide + H2O - Xenopus laevis N-acetyl-DEVD + 4-nitroaniline - ? 432170 3.4.22.55 N-acetyl-Val-Asp-Val-Ala-Asp-7-amido-4-methylcoumarin + H2O - Homo sapiens N-acetyl-Val-Asp-Val-Ala-Asp + 7-amino-4-methylcoumarin - ? 432185 3.4.22.55 N-acetyl-VDVAD-7-amido-4-methylcoumarin + H2O - Homo sapiens N-acetyl-VDVAD + 7-amino-4-methylcoumarin - ? 432186 3.4.22.55 NF kappaB activator + H2O RIP1 Homo sapiens ? proteolytic fragments of approximate 56 kDa and 20 kDa ? 415037 3.4.22.55 pakin + H2O - Mus musculus ? - ? 431106 3.4.22.55 PARP + H2O - Homo sapiens ? - ? 370669 3.4.22.55 PARP + H2O - Mus musculus ? - ? 370669 3.4.22.55 PKC-delta + H2O in JURKAT cells Homo sapiens ? - ? 382585 3.4.22.55 plakin + H2O - Homo sapiens ? - ? 431107 3.4.22.55 poly(ADP-ribose) polymerase + H2O - Homo sapiens ? - ? 361965 3.4.22.55 pro-caspase-7 + H2O 37°C, pH 7.0, 10 mM dithiothreitol Homo sapiens caspase-7 - ? 382662 3.4.22.55 procaspase-7 + H2O activation Homo sapiens caspase-7 + ? - ? 402873 3.4.22.55 procaspase-7 + H2O activation by cleavage at Asp198 and Asp206 Homo sapiens caspase-7 + ? - ? 402873 3.4.22.55 procaspase-8 + H2O processing occurs between the large and small subunits Homo sapiens processed procaspase-8 p43/41 form ? 382670 3.4.22.55 profilin 1 + H2O - Homo sapiens ? - ? 431147 3.4.22.55 protein kinase Cdelta + H2O - Homo sapiens ? - ? 390299 3.4.22.55 protein kinase Cdelta + H2O - Mus musculus ? - ? 390299 3.4.22.55 PRP31 pre-mRNA processing factor 31 homolog + H2O - Homo sapiens ? - ? 431181 3.4.22.55 Rho kinase-2 + H2O - Homo sapiens ? - ? 431184 3.4.22.55 ROCK1 + H2O - Mus musculus ? - ? 431185 3.4.22.55 ROCK2 + H2O - Mus musculus ? - ? 431186 3.4.22.55 soluble superoxide dismutase 1 + H2O - Homo sapiens ? - ? 431197 3.4.22.55 stathmin 1 + H2O - Homo sapiens ? - ? 431201 3.4.22.55 tau protein + H2O - Homo sapiens ? - ? 393638 3.4.22.55 tau protein + H2O - Mus musculus ? - ? 393638 3.4.22.55 tau protein + H2O caspase-2 cleavage of tau at Asp314 impairs cognitive and synaptic function in animal and cellular models of tauopathies by promoting the missorting of tau to dendritic spines. The truncation product, DELTAtau314, resists fibrillation and is present at higher levels in brains from cognitively impaired mice and humans with Alzheimer's disease Homo sapiens ? - ? 393638 3.4.22.55 tau protein + H2O caspase-2 cleavage of tau at Asp314 impairs cognitive and synaptic function in animal and cellular models of tauopathies by promoting the missorting of tau to dendritic spines. The truncation product, DELTAtau314, resists fibrillation and is present at higher levels in brains from cognitively impaired mice and humans with Alzheimer's disease Mus musculus ? - ? 393638 3.4.22.55 thioredoxin + H2O - Homo sapiens ? - ? 393662 3.4.22.55 tropomyosin 2beta + H2O - Homo sapiens ? - ? 431224 3.4.22.55 tropomyosin 3 + H2O - Homo sapiens ? - ? 431225 3.4.22.55 Val-Asp-Val-Ala-Asp-7-amido-4-methylcoumarin + H2O - Homo sapiens Val-Asp-Val-Ala-Asp + 7-amino-4-methylcoumarin - ? 413652 3.4.22.55 Val-Asp-Val-Ala-Asp-7-amido-4-trifluoromethylcoumarin + H2O - Homo sapiens Val-Asp-Val-Ala-Asp + 7-amino-4-trifluoromethylcoumarin - ? 415428 3.4.22.55 VDVAD + H2O - Homo sapiens ? - ? 382953 3.4.22.55 VDVAD-4-nitroanilide + H2O 37°C, pH 8.0, 1 mM DTT Homo sapiens ? - ? 382954 3.4.22.55 VDVAD-7-amido-4-methylcoumarin + H2O - Homo sapiens VDVAD + 7-amino-4-methylcoumarin - ? 406869 3.4.22.55 VDVADAFC + H2O - Mus musculus VDVAD + AFC - ? 382955 3.4.22.55 VDVADAFC + H2O - Xenopus laevis VDVAD + AFC - ? 382955 3.4.22.55 Z-VDVAD-7-amino-4-trifluoromethyl coumarin + H2O 37°C, pH 7.0, 10 mM dithiothreitol Homo sapiens 7-amino-4-trifluoromethyl coumarin + Z-VDVAD - ? 382984