3.4.22.52 (4-(4-dimethylaminophenylazo)benzoyl)-TPLKSPPPSPR-(5[(2-aminoethyl)amino]naphthalene-1-sulfonic acid) + H2O - Homo sapiens (4-(4-dimethylaminophenylazo)benzoyl)-TPLK + SPPPSPR-(5[(2-aminoethyl)amino]naphthalene-1-sulfonic acid) - ? 411086 3.4.22.52 (5(6)-carboxyfluorescin)-GGGQLYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-RRK-(5- and 6-carboxytetramethylrhodamine)-OH + H2O - Homo sapiens (5(6)-carboxyfluorescin)-GGGQLY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-RRK-(5- and 6-carboxytetramethylrhodamine)-OH - ? 411087 3.4.22.52 (EDANS)-EALFAERK-(DABCYL) + H2O about 30% cleavage preference Homo sapiens (EDANS)-EA + LFAERK-(DABCYL) - ? 411104 3.4.22.52 (EDANS)-EPLFAARK-(DABCYL) + H2O the sequence PLFAAR is an even better substrate for the calpain 1 protease core than PLFAER, 100% cleavage preference Homo sapiens (EDANS)-EPLFA + ARK-(DABCYL) - ? 411105 3.4.22.52 (EDANS)-EPLFAERK-(DABCYL) + H2O about 40% cleavage preference Homo sapiens (EDANS)-EPLFA + ERK-(DABCYL) - ? 411106 3.4.22.52 (EDANS)-EPLFGERK-(DABCYL) + H2O less than 20% cleavage preference Homo sapiens (EDANS)-EPLF + GERK-(DABCYL) - ? 411107 3.4.22.52 (EDANS)-EPLFMERK-(DABCYL) + H2O the peptide sequence PLFMER is rapidly cleaved by the calpain 1 core at the F-M bond with about 45% cleavage preference Homo sapiens (EDANS)-EPLF + MERK-(DABCYL) - ? 411108 3.4.22.52 2',3'-cyclic nucleotide 3'-phosphodiesterase + H2O - Macaca mulatta ? - ? 358974 3.4.22.52 2-aminobenzoyl-EVYGMMY(3-NO2)-OH + H2O - Homo sapiens 2-aminobenzoyl-EVY + GMMY(3-NO2)-OH - ? 411204 3.4.22.52 4,4-difluoro-5,7-dimethyl-4-bora-31,4a-diaza-s-indacene-3-propioyl-labeled casein + H2O - Homo sapiens ? - ? 411295 3.4.22.52 5-([4,6-dichlorotriazin-2-yl]amino)fluorescin-labeled microtubule-associated protein 2 + H2O - Homo sapiens ? - ? 411396 3.4.22.52 7-methoxycoumarin-4-acetyl-GGGNIFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O - Homo sapiens 7-methoxycoumarin-4-acetyl-GGGNIF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH - ? 411421 3.4.22.52 7-methoxycoumarin-4-acetyl-GGGNIYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O - Homo sapiens 7-methoxycoumarin-4-acetyl-GGGNIY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH - ? 411422 3.4.22.52 7-methoxycoumarin-4-acetyl-GGGNLFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O - Homo sapiens 7-methoxycoumarin-4-acetyl-GGGNLF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH - ? 411423 3.4.22.52 7-methoxycoumarin-4-acetyl-GGGNLYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O - Homo sapiens 7-methoxycoumarin-4-acetyl-GGGNLY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH - ? 411424 3.4.22.52 7-methoxycoumarin-4-acetyl-GGGQIFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O - Homo sapiens 7-methoxycoumarin-4-acetyl-GGGQIF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH - ? 411425 3.4.22.52 7-methoxycoumarin-4-acetyl-GGGQLFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O - Homo sapiens 7-methoxycoumarin-4-acetyl-GGGQLF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH - ? 411426 3.4.22.52 7-methoxycoumarin-4-acetyl-GGGQLYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O - Homo sapiens 7-methoxycoumarin-4-acetyl-GGGQLY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH - ? 411427 3.4.22.52 acetyl-Leu-Leu-Tyr-7-amido-4-trifluoromethyl coumarin + H2O - Homo sapiens ? - ? 391160 3.4.22.52 acetyl-LLY-7-amido-4-fluoromethylcoumarin + H2O - Homo sapiens acetyl-LLY + 7-amino-4-fluoromethylcoumarin - ? 411554 3.4.22.52 AIF + H2O - Rattus norvegicus ? - ? 404250 3.4.22.52 alpha-actinin + H2O - Homo sapiens ? - ? 410711 3.4.22.52 alpha-actinin + H2O - Rattus norvegicus ? - ? 410711 3.4.22.52 alpha-fodrin + H2O - Mus musculus ? - ? 410714 3.4.22.52 alpha-fodrin + H2O - Homo sapiens ? - ? 410714 3.4.22.52 alpha-II-spectrin + H2O - Mus musculus ? - ? 381395 3.4.22.52 alpha-II-spectrin + H2O - Rattus norvegicus ? calpain-specific spectrin cleaved products ? 381395 3.4.22.52 alpha-spectrin - Rattus norvegicus ? - ? 358975 3.4.22.52 alpha-spectrin + H2O - Mus musculus ? - ? 370551 3.4.22.52 alpha-spectrin + H2O - Homo sapiens ? - ? 370551 3.4.22.52 alpha-spectrin + H2O - Rattus norvegicus ? - ? 370551 3.4.22.52 alpha-spectrin + H2O mu-calpain is neuroprotective in the early stage of excitotoxic injury. Activation and proteolysis of alpha-spectrin by mu-calpain preceds neuronal damage in the developing cerebral cortex induced by chronic treatament of methylmercury Rattus norvegicus ? - ? 370551 3.4.22.52 alpha-spectrin II + H2O - Mus musculus ? - ? 411618 3.4.22.52 alpha-subunit of fodrin + H2O - Homo sapiens 150000 Da fragment + ? - ? 358971 3.4.22.52 alpha-synuclein + H2O - Homo sapiens 145000 DA fragment + 150 Da fragment + ? - ? 411619 3.4.22.52 alphaII-spectrin + H2O Fanconi anemia proteins play an important role in maintaining the stability of alphaII-spectrin in the cell by regulating its cleavage by mu-calpain Homo sapiens ? - ? 410719 3.4.22.52 apoptosis inducing factor + H2O - Mus musculus truncated apoptosis inducing factor + ? - ? 417887 3.4.22.52 apoptosis inducing factor + H2O - Homo sapiens ? - ? 448453 3.4.22.52 apoptosis inducing factor + H2O activated mitochondrial calpain 1 within intermembrane space cleaves apoptosis inducing factor (AIF), whereas the activated mitochondrial calpain 1 within the matrix cleaves complex I subunits and metabolic enzymes Homo sapiens ? - ? 448453 3.4.22.52 apoptosis-inducing factor + H2O although calpain I cleaves recombinant apoptosis-inducing factor in a cell free system, in intact cells under conditions where endogenous calpain is activated by either N-methyl-D-aspartate or N-methyl-N'-nitro-N-nitrosoguanidine administration, apoptosis-inducing factor is not cleaved Homo sapiens ? - ? 410728 3.4.22.52 apoptosis-inducing factor + H2O calpain-mediated truncation of apoptosis-inducing factor is contingent upon poly(ADP-ribose) polymerase-1 activity Rattus norvegicus ? - ? 410728 3.4.22.52 apoptosis-inducing factor + H2O micro-calpain mediates the truncation and release of apoptosis-inducing factor from mitochondria following cisplatin treatment Homo sapiens ? - ? 410728 3.4.22.52 apoptosis-inducing factor + H2O - Rattus norvegicus truncated apoptosis-inducing factor + ? - ? 410729 3.4.22.52 apoptosis-inducing factor + H2O mitochondrial micro-calpain is the protease responsible for processing apoptosis-inducing factor prior to its release Rattus norvegicus truncated apoptosis-inducing factor + ? - ? 410729 3.4.22.52 ATP synthase-alpha (ATP5A1) + H2O - Mus musculus ? - ? 448476 3.4.22.52 ATP synthase-alpha (ATP5A1) + H2O calpain-1 accumulation in mitochondria disrupts ATP synthase and induces ROS generation, which promotes diabetic cardiomyopathy Mus musculus ? - ? 448476 3.4.22.52 Bax protein + H2O - Sus scrofa ? - ? 431647 3.4.22.52 beta-integrin + H2O - Homo sapiens ? - ? 411786 3.4.22.52 Bfl-1 protein + H2O mu-calpain cleaves Bfl-1 at two major sites in its N-terminus releasing three fragments of 28000 Da, 12000 Da and 17500 Da Sus scrofa ? - ? 431696 3.4.22.52 BH3-only Bcl2 interacting domain + H2O BH3-only Bcl2 interacting domain is a direct target of a soluble active calpain 1 present in cells expressing hepatitis C virus proteins Homo sapiens ? - ? 411796 3.4.22.52 Boc-Leu-Met-7-amido-4-chloromethylcoumarin + H2O 10 microM, 20 min, 37 °C, with or without magnetic bead stimulation Mus musculus Boc-Leu-Met + 7-amino-4-chloromethylcoumarin - ? 404544 3.4.22.52 casein + H2O - Homo sapiens ? - ? 15445 3.4.22.52 casein + H2O - Rattus norvegicus ? - ? 15445 3.4.22.52 casein + H2O - Sus scrofa ? - ? 15445 3.4.22.52 casein + H2O - Bos taurus ? - ? 15445 3.4.22.52 casein + H2O - Ovis aries ? - ? 15445 3.4.22.52 caspase-7 + H2O recombinant caspase-7 is directly cleaved and activated by calpain-1 within the large subunit of caspase-7 to produce the large subunit p18 and p17 Homo sapiens ? - ? 410770 3.4.22.52 collapsin response mediator protein 1 + H2O - Rattus norvegicus ? - ? 404693 3.4.22.52 collapsin response mediator protein 2 + H2O - Rattus norvegicus ? - ? 404694 3.4.22.52 collapsin response mediator protein 3 + H2O - Rattus norvegicus ? - ? 404695 3.4.22.52 collapsin response mediator protein 4 + H2O - Rattus norvegicus ? - ? 404696 3.4.22.52 complex I subunits + H2O - Homo sapiens ? - ? 448518 3.4.22.52 complex I subunits + H2O activated mitochondrial calpain 1 within intermembrane space cleaves apoptosis inducing factor (AIF), whereas the activated mitochondrial calpain 1 within the matrix cleaves complex I subunits and metabolic enzymes Homo sapiens ? - ? 448518 3.4.22.52 COX-2 + H2O - Sus scrofa ? - ? 411900 3.4.22.52 cyclin dependent kinase-5 + H2O - Rattus norvegicus p25-CDK5 - ? 404734 3.4.22.52 desmin + H2O - Homo sapiens ? - ? 410798 3.4.22.52 desmin + H2O - Rattus norvegicus ? - ? 410798 3.4.22.52 dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala + H2O - Homo sapiens dye-Gln-Gln-Gln-Glu-Val-Tyr + Gly-Met-Met-Pro-Arg-Asp-pSer-Ala - ? 412018 3.4.22.52 dynamin-like protein 1 + H2O dynamin-like protein 1 (DLP1) is the key mitochondrial fission GTPase. It is a substrate of calpain which produced specific N-terminal DLP1 cleavage fragments. DLP1 is a physiological and Alzheimer's disease-relevant pathophysiological substrate of calpain in cells and in the brain. Calpain activation could contribute to reduced DLP1 levels and mitochondrial dynamics abnormalities and mitochondrial dysfunction in Alzheimer's disease Homo sapiens ? - ? 448563 3.4.22.52 dynamin-like protein 1 + H2O dynamin-like protein 1 (DLP1) is the key mitochondrial fission GTPase. It is a substrate of calpain which produced specific N-terminal DLP1 cleavage fragments Homo sapiens ? - ? 448563 3.4.22.52 E-(EDANS)-PLFAERK-(Dabcyl) + H2O - Rattus norvegicus ? - ? 412021 3.4.22.52 E-(EDANS-)PLF-AERK-(Dabcyl) + H2O - Homo sapiens ? - ? 412022 3.4.22.52 filamin A + H2O - Homo sapiens ? - ? 410822 3.4.22.52 filamin-1 + H2O - Cavia porcellus ? - ? 417949 3.4.22.52 fluorescin thiocarbamoyl-labeled casein + H2O - Homo sapiens ? - ? 412061 3.4.22.52 fodrin + H2O - Homo sapiens ? - ? 405166 3.4.22.52 fodrin + H2O - Rattus norvegicus ? - ? 405166 3.4.22.52 Frizzled-7 + H2O - Bos taurus ? - ? 390216 3.4.22.52 Frizzled-7 + H2O calpain-1 is a regulator of Frizzled-7 turnover at the plasma membrane Bos taurus ? - ? 390216 3.4.22.52 full-length glutamic acid decraboxylase67 + H2O - Mus musculus truncated glutamic acid decarboxylase67 + ? - ? 390217 3.4.22.52 full-length glutamic acid decraboxylase67 + H2O in mu-calpain knockout mice, the level of truncated glutamic acid decarboxylase67 in the brain is greatly reduced compared with the wild-type. mu-Calpain is activated by neuronal stimulation and Ca2+-influx Mus musculus truncated glutamic acid decarboxylase67 + ? - ? 390217 3.4.22.52 gamma-filamin + H2O - Mus musculus ? - ? 392023 3.4.22.52 gamma-filamin + H2O phosphorylation of the filamin C-terminus domain by PKCalpha protects gamma-filamin against proteolysis by calpain 1 in COS cells Chlorocebus aethiops ? - ? 392023 3.4.22.52 H-Lys(FAM)-Glu-Val-Tyr-Gly-Met-Met-Lys(Dabcyl)-OH + H2O - Homo sapiens ? - ? 450023 3.4.22.52 Hsp70.1 + H2O Hsp70.1 in the CA-1 tissue is an in-vivo substrate of activated mu-calpain, carbonylated Hsp70.1 in the CA-1 tissue by artificial oxidative stressors such as hydroxynonenal or hydrogen peroxide is much more vulnerable to the calpain cleavage Macaca fuscata ? - ? 412167 3.4.22.52 human epithelial growth factor receptor 2 + H2O overexpression of calpain1 or activation of endogenous calpain during adhesion or trastuzumab treatment of trastuzumab-sensitive cells induces cleavage of cytoplasmic domains of human epithelial growth factor receptor 2/phospho-human epithelial growth factor receptor 2 protein Homo sapiens 75000 Da fragment + 42000 Da fragment - ? 412174 3.4.22.52 I-kappaBalpha polymer + H2O - Homo sapiens ? - ? 417971 3.4.22.52 insulin-like growth factor binding protein-2 + H2O the primary cleavage site in insulin-like growth factor binding protein-2 is localized to the non-conserved central linker regions Homo sapiens ? - ? 392270 3.4.22.52 insulin-like growth factor binding protein-3 + H2O the primary cleavage site in insulin-like growth factor binding protein-3 is localized to the non-conserved central linker regions. In vitro binding of mu-calpain to insulin-like growth factor binding protein-3 is a Ca2+-dependent reaction with a rapid on/off rate Homo sapiens ? - ? 367539 3.4.22.52 integrin + H2O - Homo sapiens ? - ? 410871 3.4.22.52 integrin beta3 + H2O - Homo sapiens ? - ? 392276 3.4.22.52 K-(5(6)-carboxyfluorescein)-EVYGMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH + H2O - Homo sapiens K-(5(6)-carboxyfluorescein)-EVY + GMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH - ? 412201 3.4.22.52 L-plastin + H2O L-plastin interaction with integrin is regulated through cleavage of beta-integrin by micro-calpain Homo sapiens ? - ? 412320 3.4.22.52 leucine-rich repeat protein phosphatase 1 + H2O - Mus musculus ? - ? 450218 3.4.22.52 LIS1 protein + H2O - Mus musculus ? - ? 412380 3.4.22.52 lysosomal associated membrane protein 2 + H2O calpain 1 is responsible for lysosomal permeabilization by cleavage of the lysosomal associated membrane protein 2 Mus musculus ? - ? 431058 3.4.22.52 lysosomal associated membrane protein 2 + H2O calpain 1 is responsible for lysosomal permeabilization by cleavage of the lysosomal associated membrane protein 2 Rattus norvegicus ? - ? 431058 3.4.22.52 MAP2 + H2O - Homo sapiens ? - ? 410895 3.4.22.52 MAP2 + H2O - Rattus norvegicus ? - ? 410895 3.4.22.52 mature apoptosis-inducing factor (62 kDa) + H2O cleaved by the mitochondrial mu-calpain near its N-terminus Rattus norvegicus cleaved apoptosis-inducing factor (57 kDa) + ? - ? 410896 3.4.22.52 microtubule-associated protein 1 - Sus scrofa ? - ? 358965 3.4.22.52 microtubule-associated protein 2 - Homo sapiens ? - ? 358966 3.4.22.52 microtubule-associated protein 2 + H2O calpain translates high-frequency Ca2+ transients into decomposition of its sensitive substrate microtubule-associated protein 2 Homo sapiens ? - ? 370550 3.4.22.52 mitochondrial major Ca2+ extruding pathway Na+/Ca2+ exchanger + H2O cleaved by the mitochondrial mu-calpain Rattus norvegicus ? - ? 410901 3.4.22.52 additional information primary role of calpain 1 and calpain 3 in meat tenderization Bos taurus ? - ? 89 3.4.22.52 additional information enzyme is involved in myofibrillar protein degradation Sus scrofa ? - ? 89 3.4.22.52 additional information prednisolone suppresses ischemia-reperfusion injury of the rat liver. Its cytoprotective effect is partial, but is closely associated with inhibition of activation of mu-calpain and suppression of IL-beta and TNF-alpha transcription as well as with improved survival rate Rattus norvegicus ? - ? 89 3.4.22.52 additional information because the calcium concentration in postmortem muscle is high enough to activate mu-calpain, but not m-calpain, it seems reasonable to conclude that mu-calpain is responsible for postmortem degradation of calpastatin. Degradation of calpastatin by mu-calpain reduces calpain-inhibitory activity and is probably an important event in regulation of postmortem proteolysis, and, thus, meat tenderness Bos taurus ? - ? 89 3.4.22.52 additional information age-dependent myelin degeneration and proteolysis of oligodendrocyte proteins is associated with the activation of calpain-1 Macaca mulatta ? - ? 89 3.4.22.52 additional information the enzyme mediates tissue injury following post-ischemic and post-traumatic stress Rattus norvegicus ? - ? 89 3.4.22.52 additional information mu-calpain, m-calpain, 20S proteasome, dipeptidyl peptidase II and III and soluble alanyl aminopeptidase are thought to induce lens opacification kinetically during cataract formation in Shumiya cataract rats through the intracellular turnover of lens proteins Rattus norvegicus ? - ? 89 3.4.22.52 additional information translational expression of mu-calpain is up-regulated by 462.5% in MW white matter compared with controls. mu-Calpain activity and translational expression are not increased significantly in white matter from patients with Parkinson‘s or Alzheimer diseases compared with that of normal controls. Because calpain degrades all major myelin proteins, the increased activity and expression of this proteinase may play a critical role in myelinolysis in MS Homo sapiens ? - ? 89 3.4.22.52 additional information calpain mediates calcium-induced activation of the Erk1,2 MAPK pathway and cytoskeletal phosphorylation in neurons Homo sapiens ? - ? 89 3.4.22.52 additional information calpain-1 regulates Bax and subsequent Smac-dependent caspase-3 activation in neutrophil apoptosis Homo sapiens ? - ? 89 3.4.22.52 additional information mu-Calpain regulates receptor activator of NF-kappaB ligand (RANKL)-supported osteoclastogenesis via NF-kappaB activation in RAW 264.7 cells Mus musculus ? - ? 89 3.4.22.52 additional information pathological conditions associated with the gene of calpain 1: muscular dystrophy, stroke, traumatic brain injury, spinal cord injury, Alzheimer's diseases, neurodegenerative disorders, cataracts, cancer Homo sapiens ? - ? 89 3.4.22.52 additional information calpain 1 and 2 are required for RNA replication of echovirus 1 Homo sapiens ? - ? 89 3.4.22.52 additional information calpastatin could play an important role in preventing uncontrolled activity of l-calpain which otherwise may facilitate pulmonary hypertension, smooth muscle proliferation and apoptosis Bos taurus ? - ? 89 3.4.22.52 additional information in the ischemic condition such as endometriosis, myoma of uterus and microscopic thrombosis, increasing of intracellular calcium ion concentration leads to the activation of l-calpain. Cleavage of integrin beta3 by over activated l-calpain may lead to an adverse effect on early pregnancy and to causing recurrent miscarriage Homo sapiens ? - ? 89 3.4.22.52 additional information mu-calpain but not m-calpain can restore the cell migration rate. Knockdown of mu-calpain alters cell morphology with increased filopodial projections and a highly elongated tail that seems to prevent cell spreading and migration with reduced rear detachment ability. Knockdown of mu-calpain decreases the proteolytic products of filamin and talin, which are specifically rescued by overexpression of mucalpain but not m-calpain, suggesting that their proteolysis could be one of the key mechanisms by which mu-calpain regulates cell migration Homo sapiens ? - ? 89 3.4.22.52 additional information role for mu-calpain isoform in the hypermeability of the diabetic endothelium Rattus norvegicus ? - ? 89 3.4.22.52 additional information mu-calpain prefers Leu, Val or Ile at the P2 position and Lys, Tyr, Arg, or Met at the P1 position Homo sapiens ? - ? 89 3.4.22.52 additional information (EDANS)-EPAFAERK-(DABCYL), (EDANS)-EPLAAERK-(DABCYL), and (EDANS)-EPLFAEAK-(DABCYL) are very weak substrates for calpain 1 core Homo sapiens ? - ? 89 3.4.22.52 additional information mitochondrial mu-calpain associates with ERp57, whereas, cytosolic mu-calpain does not associate with ERp57 Rattus norvegicus ? - ? 89 3.4.22.52 myelin-associated glycoprotein + H2O - Rattus norvegicus ? - ? 358977 3.4.22.52 myelin-associated glycoprotein + H2O calpain overexpression due to *OH stress, IFN-gamma stimulation, or Ca2+ influx is involved in C6 cell death Rattus norvegicus ? - ? 358977 3.4.22.52 myofibril + H2O - Bos taurus ? - ? 432158 3.4.22.52 myofibrillar protein + H2O - Sus scrofa ? - ? 392680 3.4.22.52 N-acetyl-LLY-7-amido-4-fluoromethylcoumarin + H2O - Homo sapiens N-acetyl-LLY + 7-amino-4-fluoromethylcoumarin - ? 412493 3.4.22.52 N-benzyloxycarbonyl-L-Leu-L-Arg-4-methoxy-2-naphthylamide + H2O - Homo sapiens N-benzyloxycarbonyl-L-Leu-L-Arg + 4-methoxy-2-naphthylamine - ? 411841 3.4.22.52 N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O - Homo sapiens N-benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin - ? 411842 3.4.22.52 N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-trifluoromethylcoumarin + H2O - Homo sapiens N-benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-trifluoromethylcoumarin - ? 411843 3.4.22.52 N-succinyl-L-leucyl-L-valyl-L-tyrosinyl-7-amido-4-methylcoumarin + H2O - Rattus norvegicus ? - ? 392821 3.4.22.52 N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O - Mus musculus N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin - ? 362351 3.4.22.52 N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O - Mus musculus N-succinyl-LLVY + 7-amino-4-methylcoumarin - ? 412572 3.4.22.52 N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O - Homo sapiens N-succinyl-LLVY + 7-amino-4-methylcoumarin - ? 412572 3.4.22.52 N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O - Rattus norvegicus N-succinyl-LLVY + 7-amino-4-methylcoumarin - ? 412572 3.4.22.52 Na+/Ca2+ exchanger isoform 3 + H2O - Rattus norvegicus ? - ? 410915 3.4.22.52 neuronal calcium sensor-1 + H2O mu-calpain cleavage of neuronal calcium sensor-1 occurs within an N-terminal pseudoEF-hand domain (at Lys36), which is unable to bind Ca2+ Homo sapiens ? - ? 412594 3.4.22.52 neuronal nitric oxide synthase + H2O - Mus musculus ? - ? 410920 3.4.22.52 neuronal nitric oxide synthase + H2O the mechanism of neuronal nitric oxide synthase activation is promoted by a calpain-mediated limited proteolysis through conversion of native 160 kDa nNOS into a fully active 130 kDa Homo sapiens ? - ? 410920 3.4.22.52 nNOS + H2O - Mus musculus ? - ? 412600 3.4.22.52 NR2 subunit of NMDA subtype of glutamate receptor + H2O all three subtypes of NR2 subunits can be proteolyzed, cleavage of NR2A, NR2B and NR2C subunits is limited to their C-terminal region. Two cleavage sites at amino acids 1279 and 1330. Cleavage of NR2A-containing receptors does not alter basic NMDA receptor properties including calcium uptake, MK801 binding or electrophysiological measurement Sus scrofa ? - ? 358978 3.4.22.52 NR2B subunit of NMDA receptor + H2O - Mus musculus ? - ? 431082 3.4.22.52 p12 subunit of human DNA polymerase delta + H2O the proteolysis of p12 by mu-calpain may be through a DNA polymerase delta4/PCNA complex. The p12/DNA polymerase delta is a target as a nuclear substrate of mu-calpain in calcium-triggered apoptosis Homo sapiens ? - ? 431096 3.4.22.52 p35 + H2O - Mus musculus p25 + ? - ? 410927 3.4.22.52 PH domain + H2O - Mus musculus ? - ? 450454 3.4.22.52 plasma membrane Ca2+-ATPase isoform 1 + H2O readily and completely degraded by m-calpain Homo sapiens ? - ? 385557 3.4.22.52 plasma membrane Ca2+-ATPase isoform 2 + H2O slow hydrolysis only to large fragments Homo sapiens ? - ? 385558 3.4.22.52 plasma membrane Ca2+-ATPase isoform 4 + H2O slow hydrolysis only to large fragments Homo sapiens ? - ? 385559 3.4.22.52 podoplanin + H2O podoplanin stability is post-translationally regulated by calpain-1 Homo sapiens ? - ? 412725 3.4.22.52 pro-interleukin-33 + H2O - Homo sapiens interleukin-33 + ? - ? 402870 3.4.22.52 prostacyclin synthase + H2O calpain 1 cleaves and inactivates prostacyclin synthase in mesenteric arteries from diabetic mice. It cleaves the C-terminal domain of PGI2 synthase close to the catalytic site of the enzyme Mus musculus ? - ? 448880 3.4.22.52 Rad21 + H2O calpain-1 cleaves Rad21 at Leu192 Homo sapiens ? - ? 418055 3.4.22.52 recombinant procaspase-3 + H2O - Homo sapiens ? - ? 358973 3.4.22.52 recombinant procaspase-3 + H2O - Sus scrofa ? - ? 358973 3.4.22.52 recombinant procaspase-3 + H2O calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation Homo sapiens ? - ? 358973 3.4.22.52 recombinant procaspase-9 + H2O - Homo sapiens ? - ? 358972 3.4.22.52 recombinant procaspase-9 + H2O - Sus scrofa ? - ? 358972 3.4.22.52 recombinant procaspase-9 + H2O calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation Homo sapiens ? - ? 358972 3.4.22.52 RecTat101 + H2O - Rattus norvegicus ? - ? 406557 3.4.22.52 RhoA + H2O - Bos taurus ? - ? 358976 3.4.22.52 RhoA + H2O calpain cleaves RhoA and generates a form that inhibits integrin-induced stress fiber assembly and cell spreading Bos taurus ? - ? 358976 3.4.22.52 spectrin + H2O - Cavia porcellus ? - ? 362513 3.4.22.52 spectrin + H2O - Homo sapiens ? - ? 362513 3.4.22.52 spectrin + H2O - Rattus norvegicus ? - ? 362513 3.4.22.52 striatal-enriched protein tyrosine phosphatase + H2O calpain-cleavage of striatal-enriched protein tyrosine phosphatase 61 is NMDAR-dependent, Cdk5 enhances calpain-mediated cleavage of striatal-enriched protein tyrosine phosphatase 61, calpain cleaves recombinant striatal-enriched protein tyrosine phosphatase 46 in a dose-dependent manner Homo sapiens ? - ? 411023 3.4.22.52 succinyl-bovine serum albumin + H2O - Homo sapiens ? - ? 412916 3.4.22.52 succinyl-bovine serum albumin + H2O - Oryctolagus cuniculus ? - ? 412916 3.4.22.52 succinyl-bovine-serum-albumin + H2O - Oryctolagus cuniculus ? - ? 358968 3.4.22.52 succinyl-casein + H2O - Homo sapiens ? - ? 358967 3.4.22.52 succinyl-casein + H2O - Oryctolagus cuniculus ? - ? 358967 3.4.22.52 succinyl-insulin B + H2O - Homo sapiens ? - ? 358969 3.4.22.52 succinyl-insulin B + H2O - Oryctolagus cuniculus ? - ? 358969 3.4.22.52 succinyl-L-Leu-L-Leu-L-Val-7-amido-4-methylcoumarin + H2O - Homo sapiens succinyl-L-Leu-L-Leu-L-Val + 7-amino-4-methylcoumarin - ? 412923 3.4.22.52 succinyl-L-Leu-L-Leu-L-Val-L-Tyr-7-amido-4-methylcoumarin + H2O - Homo sapiens succinyl-L-Leu-L-Leu-L-Val-L-Tyr + 7-amino-4-methylcoumarin - ? 412924 3.4.22.52 succinyl-L-Leu-L-Met-7-amido-4-methylcoumarin + H2O - Homo sapiens succinyl-L-Leu-L-Met + 7-amino-4-methylcoumarin - ? 412926 3.4.22.52 succinyl-L-Leu-L-Tyr-4-methoxy-2-naphthylamide + H2O - Homo sapiens succinyl-L-Leu-L-Tyr + 4-methoxy-2-naphthylamine - ? 412927 3.4.22.52 succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O - Mus musculus succinyl-L-Leu-L-Tyr + 7-amino-4-methylcoumarin - ? 412928 3.4.22.52 succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O - Homo sapiens succinyl-L-Leu-L-Tyr + 7-amino-4-methylcoumarin - ? 412928 3.4.22.52 succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O - Sus scrofa ? - ? 95053 3.4.22.52 succinyl-Leu-Tyr-4-methylcoumaryl-7-amide + H2O - Homo sapiens ? - ? 393571 3.4.22.52 succinyl-LLVY-7-amido-4-methylcoumarin + H2O - Homo sapiens succinyl-LLVY + 7-amino-4-methylcoumarin - ? 362706 3.4.22.52 succinyl-protamine + H2O - Homo sapiens ? - ? 358970 3.4.22.52 succinyl-protamine + H2O - Oryctolagus cuniculus ? - ? 358970 3.4.22.52 talin + H2O - Mus musculus ? - ? 358996 3.4.22.52 talin + H2O - Homo sapiens ? - ? 358996 3.4.22.52 tau protein + H2O - Homo sapiens ? - ? 393638 3.4.22.52 tert-butyloxycarbonyl-L-Leu-L-Met-7-amido-4-chloromethylcoumarin + H2O - Homo sapiens tert-butyloxycarbonyl-L-Leu-L-Met + 7-amino-4-chloromethylcoumarin - ? 412955 3.4.22.52 tert-butyloxycarbonyl-L-Leu-L-Met-7-amido-4-methylcoumarin + H2O - Homo sapiens tert-butyloxycarbonyl-L-Leu-L-Met + 7-amino-4-methylcoumarin - ? 412956 3.4.22.52 tert-butyloxycarbonyl-L-leucyl-L-methionine-7-amido-4-chloromethylcoumarin + H2O - Homo sapiens tert-butyloxycarbonyl-L-leucyl-L-methionine + 7-amino-4-chloromethylcoumarin - ? 412957 3.4.22.52 tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O - Homo sapiens tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin - ? 412958 3.4.22.52 tert-butyloxycarbonyl-Leu-Met-7-amido-4-chloromethylcoumarin + H2O - Homo sapiens tert-butyloxycarbonyl-Leu-Met + 7-amino-4-chloromethylcoumarin - ? 412959 3.4.22.52 titin + H2O - Homo sapiens ? - ? 380771 3.4.22.52 titin + H2O - Rattus norvegicus ? - ? 380771 3.4.22.52 titin + H2O pH 7.5, absence or presence of 12 microM calcium Sus scrofa ? - ? 380771 3.4.22.52 titin + H2O pH 7.5, absence or presence of 12 microM calcium Bos taurus ? - ? 380771 3.4.22.52 troponin + H2O - Sus scrofa ? - ? 413015 3.4.22.52 troponin complex + H2O - Homo sapiens ? - ? 411041 3.4.22.52 troponin complex + H2O - Rattus norvegicus ? - ? 411041 3.4.22.52 utrophin + H2O - Cavia porcellus ? - ? 418117 3.4.22.52 vimentin + H2O - Homo sapiens ? - ? 393820 3.4.22.52 [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 + H2O - Homo sapiens [2-Abz]-Ser-Thr-Phe + Ala-Gln-Pro-[3-nitrotyrosine]-NH2 - ? 413116 3.4.22.52 [4-((4-(dimethylamino)phenyl)azo)benzoic acid, succinimidyl ester]-Thr-Pro-Leu-Lys-Ser-Pro-Pro-Pro-Ser-Pro-Arg-[5-((2-aminoethyl)amino)naphthalene-1-sulfonic acid] + H2O - Sus scrofa ? - ? 413117