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Information on EC 3.4.22.52 - calpain-1 and Organism(s) Homo sapiens and UniProt Accession P07384
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3.4.22.52 calpain-1Specify your search results
Word Map
- 3.4.22.52
- calpains
- calpastatin
-
ca2+-dependent
-
tender
-
calcium-dependent
-
meat
- cytoskeletal
- beef
- ischemia
- myofibrillar
- hippocampal
- calpeptin
-
autolysis
-
caspase
- proteinase
- spectrin
- longissimus
-
calpain-mediated
-
postmortem
- cathepsins
-
calpain-specific
- leupeptin
- lumborum
- medicine
-
sarcomere
-
non-lysosomal
-
nebulin
-
calpain-dependent
-
slaughter
-
calpain-like
- semimembranosus
- fodrin
- food industry
-
carcass
-
angus
-
autoproteolysis
-
warner-bratzler
-
autolyzed
-
ca2+-activated
-
steak
- caspase-12
- myofibril
- talin
-
troponin-t
-
brahman
-
calmodulin-like
- thoracis
-
proteolyzed
- aif
-
canps
- alpha-spectrin
- desmin
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
mu-calpain, calpain-1, calpain i, calpain 1, capn1, capn2, micro-calpain, capns1, calpain1, calpain-i, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
calcium-activated neutral protease I
-
-
-
-
calpain 1
calpain I
CAPN1 g.p. (Homo sapiens)
-
-
-
-
micro-calpain
mu-calpain
muCANP
-
-
-
-
calpain 1
-
-
-
-
calpain 1
-
-
calpain I
-
-
-
-
micro-calpain
-
-
-
-
mu-calpain
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
689772-75-6
-
78990-62-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(4-(4-dimethylaminophenylazo)benzoyl)-TPLKSPPPSPR-(5[(2-aminoethyl)amino]naphthalene-1-sulfonic acid) + H2O
(4-(4-dimethylaminophenylazo)benzoyl)-TPLK + SPPPSPR-(5[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)
-
-
-
-
?
(5(6)-carboxyfluorescin)-GGGQLYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-RRK-(5- and 6-carboxytetramethylrhodamine)-OH + H2O
(5(6)-carboxyfluorescin)-GGGQLY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-RRK-(5- and 6-carboxytetramethylrhodamine)-OH
-
-
-
-
?
(EDANS)-EALFAERK-(DABCYL) + H2O
(EDANS)-EA + LFAERK-(DABCYL)
-
about 30% cleavage preference
-
-
?
(EDANS)-EPLFAARK-(DABCYL) + H2O
(EDANS)-EPLFA + ARK-(DABCYL)
-
the sequence PLFAAR is an even better substrate for the calpain 1 protease core than PLFAER, 100% cleavage preference
-
-
?
(EDANS)-EPLFAERK-(DABCYL) + H2O
(EDANS)-EPLFA + ERK-(DABCYL)
-
about 40% cleavage preference
-
-
?
(EDANS)-EPLFGERK-(DABCYL) + H2O
(EDANS)-EPLF + GERK-(DABCYL)
-
less than 20% cleavage preference
-
-
?
(EDANS)-EPLFMERK-(DABCYL) + H2O
(EDANS)-EPLF + MERK-(DABCYL)
-
the peptide sequence PLFMER is rapidly cleaved by the calpain 1 core at the F-M bond with about 45% cleavage preference
-
-
?
2-aminobenzoyl-EVYGMMY(3-NO2)-OH + H2O
2-aminobenzoyl-EVY + GMMY(3-NO2)-OH
-
-
-
-
?
4,4-difluoro-5,7-dimethyl-4-bora-31,4a-diaza-s-indacene-3-propioyl-labeled casein + H2O
?
-
-
-
-
?
5-([4,6-dichlorotriazin-2-yl]amino)fluorescin-labeled microtubule-associated protein 2 + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGNIFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGNIF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGNIYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGNIY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGNLFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGNLF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGNLYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGNLY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGQIFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGQIF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGQLFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGQLF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGQLYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGQLY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
acetyl-LLY-7-amido-4-fluoromethylcoumarin + H2O
acetyl-LLY + 7-amino-4-fluoromethylcoumarin
-
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala + H2O
dye-Gln-Gln-Gln-Glu-Val-Tyr + Gly-Met-Met-Pro-Arg-Asp-pSer-Ala
-
-
-
-
?
human epithelial growth factor receptor 2 + H2O
75000 Da fragment + 42000 Da fragment
-
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
-
-
?
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
-
-
?
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
-
-
?
K-(5(6)-carboxyfluorescein)-EVYGMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH + H2O
K-(5(6)-carboxyfluorescein)-EVY + GMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH
-
-
-
-
?
L-plastin + H2O
?
-
L-plastin interaction with integrin is regulated through cleavage of beta-integrin by micro-calpain
-
-
?
microtubule-associated protein 2 + H2O
?
-
calpain translates high-frequency Ca2+ transients into decomposition of its sensitive substrate microtubule-associated protein 2
-
-
?
N-acetyl-LLY-7-amido-4-fluoromethylcoumarin + H2O
N-acetyl-LLY + 7-amino-4-fluoromethylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methoxy-2-naphthylamide + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 4-methoxy-2-naphthylamine
-
-
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-trifluoromethylcoumarin + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
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+
-
-
?
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
-
-
?
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
-
-
?
plasma membrane Ca2+-ATPase isoform 1 + H2O
?
-
readily and completely degraded by m-calpain
-
-
?
plasma membrane Ca2+-ATPase isoform 2 + H2O
?
-
slow hydrolysis only to large fragments
-
-
?
plasma membrane Ca2+-ATPase isoform 4 + H2O
?
-
slow hydrolysis only to large fragments
-
-
?
podoplanin + H2O
?
-
podoplanin stability is post-translationally regulated by calpain-1
-
-
?
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
-
-
?
succinyl-L-Leu-L-Leu-L-Val-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Leu-L-Val + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-L-Leu-L-Leu-L-Val-L-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Leu-L-Val-L-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-L-Leu-L-Met-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Met + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-L-Leu-L-Tyr-4-methoxy-2-naphthylamide + H2O
succinyl-L-Leu-L-Tyr + 4-methoxy-2-naphthylamine
-
-
-
-
?
succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-LLVY-7-amido-4-methylcoumarin + H2O
succinyl-LLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Leu-L-Met-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-L-Leu-L-Met + 7-amino-4-chloromethylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Leu-L-Met-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Leu-L-Met + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-leucyl-L-methionine-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-L-leucyl-L-methionine + 7-amino-4-chloromethylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-Leu-Met-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-Leu-Met + 7-amino-4-chloromethylcoumarin
-
-
-
-
?
[2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 + H2O
[2-Abz]-Ser-Thr-Phe + Ala-Gln-Pro-[3-nitrotyrosine]-NH2
-
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
apoptosis-inducing factor + H2O
?
-
micro-calpain mediates the truncation and release of apoptosis-inducing factor from mitochondria following cisplatin treatment
-
-
?
recombinant procaspase-3 + H2O
?
-
calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
-
-
?
recombinant procaspase-9 + H2O
?
-
calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
-
-
?
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
-
-
?
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 Parkinsons 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
-
-
?
additional information
?
-
-
calpain mediates calcium-induced activation of the Erk1,2 MAPK pathway and cytoskeletal phosphorylation in neurons
-
-
?
additional information
?
-
-
calpain-1 regulates Bax and subsequent Smac-dependent caspase-3 activation in neutrophil apoptosis
-
-
?
additional information
?
-
-
calpain 1 and 2 are required for RNA replication of echovirus 1
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
mu-calpain prefers Leu, Val or Ile at the P2 position and Lys, Tyr, Arg, or Met at the P1 position
-
-
?
additional information
?
-
-
(EDANS)-EPAFAERK-(DABCYL), (EDANS)-EPLAAERK-(DABCYL), and (EDANS)-EPLFAEAK-(DABCYL) are very weak substrates for calpain 1 core
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
microtubule-associated protein 2 + H2O
?
-
calpain translates high-frequency Ca2+ transients into decomposition of its sensitive substrate microtubule-associated protein 2
-
-
?
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
-
-
?
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
-
-
?
recombinant procaspase-3 + H2O
?
-
calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
-
-
?
recombinant procaspase-9 + H2O
?
-
calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
-
-
?
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
-
-
?
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
-
-
?
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 Parkinsons 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
-
-
?
additional information
?
-
-
calpain mediates calcium-induced activation of the Erk1,2 MAPK pathway and cytoskeletal phosphorylation in neurons
-
-
?
additional information
?
-
-
calpain-1 regulates Bax and subsequent Smac-dependent caspase-3 activation in neutrophil apoptosis
-
-
?
additional information
?
-
-
calpain 1 and 2 are required for RNA replication of echovirus 1
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
mu-calpain prefers Leu, Val or Ile at the P2 position and Lys, Tyr, Arg, or Met at the P1 position
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
requires 0.053 mM Ca2+ for half-maximal activity. Activation by Ca2+ promotes the separation of the two subunits of the expressed recombinant protein
Ca2+
-
the primary event in Ca2+-activation corresponds to the binding of Ca2+ to eight interacting sites, of which are four in each of the two calpain subunits. Progressive binding of the metal iuon is linearly correlated with the dissociation of the proteinase, which reaches completion when all eight binding sites are occupied. The affinity for Ca2+ in the native heterodimeric calpain is increased 2fold in the isolated 80000 Da catalytic subunit, but it reaches a Kd-value consistent with the physiological concentration of Ca2+ only in the active autoproteolytically derived 75000 Da form. Binding of the Ca2+ in physiological conditions, and thus the formation of the 75000 Da subunit, can occur only in the presence of positive modulators, the natural activator protein or highly digestible substrates. As a result, both dissociation into the constituent subunits and the autoproteolytic conversion of the native 80000 Da subunit into the active 75000 Da subunit form can occur within the physiological fluctuations in Ca2+ concentrations
Ca2+
-
dependent on (0.002-0.02 mM). At resting [Ca2+], mu-calpain is present predominantly in its full-length, unautolysed/unactivated forms. Once activated, mu-calpain appears in its autolysed form. Endogenously expressed mu-calpain is activated within a physiological [Ca2+] range in a Ca2+- and time-dependent manner. Autolysed mu-calpain isoforms have a greater Ca2+ sensitivity than the full-length 80000 Da isoform
Ca2+
-
dependent on, dysfunctional mitochondria increase cytosolic calcium, thereby inducing calpain activation
Ca2+
-
mu-calpain is autolytically activated at micromolar Ca2+, mice muscle fibers that are partially excitation-contraction uncoupled by exposure to 0.005 mM Ca2+ for 3 min (no ATP) show the presence of autolytic activation of a proportion of the human mu-calpain present
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R)-N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-benzyl-6-oxopiperidine-2-carboxamide
-
(4R)-N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-benzyl-1-methyl-2-oxoimidazolidine-4-carboxamide
-
(4S)-N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-benzyl-4-methyl-5-oxo-D-prolinamide
-
1-(2-chlorobenzyl)-N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
-
1-benzyl-N-[3,4-dioxo-1-phenyl-4-(phenylamino)butan-2-yl]-5-oxo-D-prolinamide
-
1-benzyl-N-[4-(cyclobutylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
-
1-benzyl-N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
-
1-benzyl-N-[4-(ethylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
-
1-benzyl-N-[4-(methoxyamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
-
1-benzyl-N-[4-[(4-fluorophenyl)amino]-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-(2,2-dimethylpropyl)-5-oxo-D-prolinamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-(cyclohexylmethyl)-5-oxo-D-prolinamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-benzyl-6-oxo-1,6-dihydropyridine-2-carboxamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-[(4-methylphenyl)sulfonyl]-D-prolinamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-[2-methoxy-6-(trifluoromethyl)benzyl]-5-oxo-D-prolinamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-2-benzyl-1,2-thiazolidine-3-carboxamide 1,1-dioxide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-(pyridin-4-ylmethyl)-D-prolinamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-[2-(trifluoromethoxy)benzyl]-D-prolinamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-[2-(trifluoromethyl)benzyl]-D-prolinamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-[3-(trifluoromethoxy)benzyl]-D-prolinamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-[3-(trifluoromethyl)benzyl]-D-prolinamide
-
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-1-(1-methyl-1H-pyrazol-4-yl)-5-oxo-D-prolinamide
-
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-1-(2,3-dihydro-1H-inden-2-yl)-5-oxo-D-prolinamide
-
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-1-[2-(trifluoromethoxy)-6-(trifluoromethyl)benzyl]-D-prolinamide
-
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-1-[2-(trifluoromethoxy)benzyl]-D-prolinamide
-
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-1-[2-(trifluoromethyl)benzyl]-D-prolinamide
-
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
-
(2S)-2-[[(4-fluorophenyl)sulfonyl]amino]-N-[(3S)-2-hydroxytetrahydrofuran-3-yl]-3-methylbutanamide
-
-
(3S)-2-hydroxytetrahydrofuran-3-yl N-[(10H-phenothiazin-2-yloxy)acetyl]-L-threonyl-L-leucinate
-
-
(3S)-2-hydroxytetrahydrofuran-3-yl N-[(2S)-2-[[(10H-phenothiazin-2-yloxy)acetyl]amino]butanoyl]-L-leucinate
-
-
(3S)-3-[[N-(10H-phenothiazin-2-ylcarbonyl)-L-norvalyl]amino]tetrahydrofuran-2-yl acetate
-
BN-82270
(4S)-3-[(4-methylphenyl)sulfonyl]-N-(1-oxo-3-phenylpropan-2-yl)-1,3-thiazolidine-4-carboxamide
-
-
(7S,10S,13S,26S)-13,26-dibenzyl-7-methyl-10-(propan-2-yl)-5,7,8,10,11,13,14,25,26,28-decahydrotetrabenzo[k,m,t,v][1,4,7,10,15,18]hexaazacyclotetracosine-6,9,12,15,24,27-hexone
-
-
1-(2-chloro-4-hydroxyphenyl)-4-oxo-7-(pyridin-4-yl)-1,4-dihydroquinoline-3-carboxamide
-
-
2-methyl-N-[(2S)-1-oxo-3-phenylpropan-2-yl]-7,8-dihydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
-
3,4-dichlorophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 56 nM
3,4-dichlorophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
-
IC50: 56 nM
3-([4-[2-(methoxymethoxy)phenyl]-4-oxobutanoyl]amino)-2-oxo-4-phenylbutanamide
-
reversible inhibitor
3-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-2-oxo-4-phenylbutanoic acid
-
reversible inhibitor
3-acetyl-2-[(2,4-dichlorophenyl)amino]-8-(trifluoromethyl)quinolin-4(1H)-one
-
-
3-acetyl-2-[[3,5-bis(trifluoromethyl)phenyl]amino]-5,8-difluoroquinolin-4(1H)-one
-
-
3-acetyl-6-chloro-2-[(2-chloro-4-methylphenyl)amino]-8-nitroquinolin-4(1H)-one
-
-
3-acetyl-6-chloro-8-(trifluoromethyl)-2-[[4-(trifluoromethyl)phenyl]amino]quinolin-4(1H)-one
-
-
3-acetyl-7,8-dichloro-2-[[3-(trifluoromethyl)phenyl]amino]quinolin-4(1H)-one
-
-
3-acetyl-8-chloro-2-[(2,4-dibromophenyl)amino]-5-methylquinolin-4(1H)-one
-
-
3-acetyl-8-chloro-2-[(2-fluoro-5-methylphenyl)amino]-5-(trifluoromethyl)quinolin-4(1H)-one
-
-
3-acetyl-8-chloro-2-[(4-chloro-2-fluorophenyl)amino]-5-methylquinolin-4(1H)-one
-
-
3-acetyl-8-chloro-5-methyl-2-[(2,3,4-trifluorophenyl)amino]quinolin-4(1H)-one
-
-
3-acetyl-8-chloro-5-methyl-2-[(2,4,5-trifluorophenyl)amino]quinolin-4(1H)-one
-
-
4-(4-bromophenyl)-3-([N-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucyl]amino)-2-oxobutanoic acid
-
reversible inhibitor
4-fluorophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 29 nM
4-fluorophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
-
IC50: 50 nM
4-nitrophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 47 nM
4-nitrophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
-
IC50: 50 nM
4-[([(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]oxy)methyl]benzyl (2Z)-[(3R)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]ethanoate
-
-
5-azanylidyne-N-[[(2S,3S)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]-L-norvalyl-L-arginyl-L-tryptophanamide
-
irreversible inhibitor
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]-1H-pyrrole-2-carboxamide
-
CAT0059
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]furan-2-carboxamide
-
-
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]thiophene-2-carboxamide
-
-
benzyl [(6S,9S,12S)-6-formyl-9-(2-methylpropyl)-8,11-dioxo-2-oxa-7,10-diazabicyclo[12.2.2]octadeca-1(16),14,17-trien-12-yl]carbamate
-
-
benzyl [(7S,10S,13S)-7-formyl-10-(2-methylpropyl)-9,12-dioxo-2-oxa-8,11-diazabicyclo[13.2.2]nonadeca-1(17),15,18-trien-13-yl]carbamate
-
CAT811
benzyl [(8S,11S,14S)-8-formyl-11-(2-methylpropyl)-10,13-dioxo-2-oxa-9,12-diazabicyclo[14.2.2]icosa-1(18),16,19-trien-14-yl]carbamate
-
-
butyl (2Z)-[(3S)-3-(butan-2-yl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]ethanoate
-
-
CP1B peptide
-
a 20-mer peptide truncated from region B of calpastatin inhibitory domain 1, 1000fold more selective for mu-calpain than cathepsin L
-
cystatin
-
engineered cystatins. Recombinant hybrids of human stefin B with KS2 and DELTAL110 deletion mutants of chicken cystatin-KD2 hybrids. Substitution of the N-terminal contact region of stefin B by ther corresponding KD2 sequence results in a calpain inhibitor with a Ki-value of 188 nM. Deletion of L110 improves inhibition 4 to 8fold. All engineered cystatins are temporary inhibitors
-
dimethyl (2S,2'S)-2,2'-[biphenyl-2,2'-diylbis(carbonylimino)]bis(3-phenylpropanoate)
-
-
ethyl 3-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-2-oxo-4-phenylbutanoate
-
reversible inhibitor
ethyl 4-(4-bromophenyl)-3-([N-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucyl]amino)-2-oxobutanoate
-
reversible inhibitor
heat shock protein 90
-
incubation of calpain-1 at a molar ratio of 1:1 with heat shock protein 90, at increasing Ca2+ concentrations, results in a significant decrease of calpain proteolytic activity at [Ca2+] up to 0.04 mM. At higher Ca2+ concentrations, the inhibiting effect of heat shock protein 90 is no more detectable
-
methyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 89 nM
methyl (3S)-4-cyclohexyl-3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxobutanoate
-
IC50: 1000 nM
methyl (S,S,Z)-(3-sec-butyl-1-oxo-2,3-dihydro-1H-isoquinolin-4-ylidene)acetate
-
strong inhibitor
methyl N-[[2'-([(2S)-1-[(2'-aminobiphenyl-2-yl)amino]-1-oxo-3-phenylpropan-2-yl]carbamoyl)biphenyl-2-yl]carbonyl]-L-phenylalanyl-L-valinate
-
-
N'-((1S,2R)-1-benzyl-3-[(3,5-dimethoxybenzyl)amino]-2-hydroxypropyl)-N,N-dipropylbenzene-1,3-dicarboxamide
-
IC50: 20 nM
N-((1S)-1-benzyl-2,3-dioxo-3-[(2-phenylethyl)amino]propyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 63 nM
N-((1S)-1-benzyl-3-[(1-methylethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 205 nM
N-((1S)-1-benzyl-3-[(2-methoxyethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 200 nM
N-((1S)-1-benzyl-3-[(cyclopropylmethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 286 nM
N-((1S)-1-[(butylamino)(oxo)acetyl]-3-methylbutyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-(1-benzothiophen-2-ylcarbonyl)piperidine-4-carboxamide
-
reversible inhibitor
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-2-[(E)-2-[4-[(diethylamino)methyl]phenyl]ethenyl]benzamide
-
reversible inhibitor
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-methyl-4-oxo-1,4-dihydroquinoline-2-carboxamide
-
reversible inhibitor
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-methyl-4-oxo-4H-chromene-2-carboxamide
-
reversible inhibitor
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-4-methyl-6-methylidene-1,6-dihydropyridine-3-carboxamide
-
reversible inhibitor
N-[(1S)-1-benzyl-2,3-dioxo-3-(pentylamino)propyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 150 nM
N-[(1S)-1-benzyl-2,3-dioxo-3-(prop-2-en-1-ylamino)propyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 200 nM
N-[(1S)-1-benzyl-3-(benzylamino)-2,3-dioxopropyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 81 nM
N-[(1S)-1-benzyl-3-(butylamino)-2,3-dioxopropyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
-
N-[(1S)-1-benzyl-3-(ethylamino)-2,3-dioxopropyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 340 nM
N-[(2S)-1-oxo-3-phenylpropan-2-yl]-7,8-dihydro-2H-[1,4]dioxino[2,3-g][1,2,4]benzothiadiazine-3-carboxamide 1,1-dioxide
-
-
N-[(2S)-1-[[(3S)-2-hydroxytetrahydrofuran-3-yl]amino]-1-oxopentan-2-yl]-10H-phenothiazine-2-carboxamide
-
BN-82204
N-[(2S)-3,4-dioxo-1-phenyl-4-([3-[(phenylsulfonyl)amino]propyl]amino)butan-2-yl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
reversible inhibitor
N-[(2S)-4-(2-benzylhydrazinyl)-3,4-dioxo-1-phenylbutan-2-yl]-N2-[(benzyloxy)carbonyl]-L-leucinamide
-
reversible inhibitor
N-[(2S)-4-(butylamino)-3,4-dioxo-1-phenylbutan-2-yl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
reversible inhibitor
N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-4-fluoro-1-(4-hydroxyphenyl)-3-oxobutan-2-yl]-L-leucinamide
-
irreversible inhibitor
N-[1-(4-bromophenyl)-4-(ethylamino)-3,4-dioxobutan-2-yl]-N2-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucinamide
-
reversible inhibitor
N-[[(2R,3R)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]-L-histidyl-L-arginyl-L-tryptophanamide
-
irreversible inhibitor
N2-[(2S)-2-([[(2R,3R)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]amino)pent-4-enoyl]-L-arginyl-L-tryptophanamide
-
irreversible inhibitor
N2-[(benzyloxy)carbonyl]-N-[4-(ethylamino)-3,4-dioxo-1-phenylbutan-2-yl]-L-leucinamide
-
reversible inhibitor
phenyl (2-[(3-([(1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 76 nM
phenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 40 nM
phenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
-
IC50: 35 nM
additional information
-
FANCA and FANCG proteins bind directly to mu-calpain, this binding may lead to inhibition of mu-calpain activity in normal cells
-
calpastatin
-
the occurrence of a complex between heat shock protein 90 and calpain-1, in which the protease is still activable, can prevent the complete inhibition of the protease even in the presence of high calpastatin levels
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
required for activation of mu-calpain. Membrane-binding of mu-calpain is Ca2+-dependent. Membrane binding of mu-calpain is due to the exposed hydrophobic surface of the active site conformation and does not reduce the Ca2+ requirement for activation
NS5A protein
-
the nonstructural hepatitis C virus protein NS5Ais sufficient to activate a calpain 1
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.043
2-aminobenzoyl-EVYGMMY(3-NO2)-OH
-
pH and temperature not specified in the publication
0.00074
4,4-difluoro-5,7-dimethyl-4-bora-31,4a-diaza-s-indacene-3-propioyl-labeled casein
-
pH and temperature not specified in the publication
-
0.0131
fluorescin thiocarbamoyl-labeled casein
-
pH and temperature not specified in the publication
-
0.0046
K-(5(6)-carboxyfluorescein)-EVYGMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH
-
pH and temperature not specified in the publication
0.37
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methoxy-2-naphthylamide
-
pH and temperature not specified in the publication
0.19
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.46
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-trifluoromethylcoumarin
-
pH and temperature not specified in the publication
0.002
succinyl-bovine serum albumin
-
pH and temperature not specified in the publication
-
0.284
succinyl-insulin B
-
pH and temperature not specified in the publication
-
0.2
succinyl-L-Leu-L-Leu-L-Val-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.2
succinyl-L-Leu-L-Leu-L-Val-L-Tyr-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
1.2
succinyl-L-Leu-L-Met-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.43
succinyl-L-Leu-L-Tyr-4-methoxy-2-naphthylamide
-
pH and temperature not specified in the publication
4.7
succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.063
succinyl-protamine
-
pH and temperature not specified in the publication
-
5.9
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
2-aminobenzoyl-EVYGMMY(3-NO2)-OH
-
pH and temperature not specified in the publication
0.11
K-(5(6)-carboxyfluorescein)-EVYGMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH
-
pH and temperature not specified in the publication
0.52
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methoxy-2-naphthylamide
-
pH and temperature not specified in the publication
0.02
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.07
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-trifluoromethylcoumarin
-
pH and temperature not specified in the publication
0.29
succinyl-L-Leu-L-Leu-L-Val-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.029
succinyl-L-Leu-L-Leu-L-Val-L-Tyr-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.062
succinyl-L-Leu-L-Met-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.12
succinyl-L-Leu-L-Tyr-4-methoxy-2-naphthylamide
-
pH and temperature not specified in the publication
0.37
succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.49
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000064
(2R)-N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-benzyl-6-oxopiperidine-2-carboxamide
pH and temperature not specified in the publication
0.000101
(4R)-N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-benzyl-1-methyl-2-oxoimidazolidine-4-carboxamide
pH and temperature not specified in the publication
0.00005
(4S)-N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-benzyl-4-methyl-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000073
1-(2-chlorobenzyl)-N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.00007
1-benzyl-N-[3,4-dioxo-1-phenyl-4-(phenylamino)butan-2-yl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.00011
1-benzyl-N-[4-(cyclobutylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.00013
1-benzyl-N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000165
1-benzyl-N-[4-(ethylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.00436
1-benzyl-N-[4-(methoxyamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000048
1-benzyl-N-[4-[(4-fluorophenyl)amino]-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000046
N-(1-amino-1,2-dioxoheptan-3-yl)-1-benzyl-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.00135
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-(2,2-dimethylpropyl)-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000268
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-(cyclohexylmethyl)-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000039
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-benzyl-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000528
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-benzyl-5-oxo-L-prolinamide
pH and temperature not specified in the publication
0.000082
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-benzyl-6-oxo-1,6-dihydropyridine-2-carboxamide
pH and temperature not specified in the publication
0.000129
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-[(4-methylphenyl)sulfonyl]-D-prolinamide
pH and temperature not specified in the publication
0.000036
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-[2-methoxy-6-(trifluoromethyl)benzyl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000268
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-2-benzyl-1,2-thiazolidine-3-carboxamide 1,1-dioxide
pH and temperature not specified in the publication
0.00018
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-(pyridin-4-ylmethyl)-D-prolinamide
pH and temperature not specified in the publication
0.000057
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-[2-(trifluoromethoxy)benzyl]-D-prolinamide
pH and temperature not specified in the publication
0.000059
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-[2-(trifluoromethyl)benzyl]-D-prolinamide
pH and temperature not specified in the publication
0.000125
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-[3-(trifluoromethoxy)benzyl]-D-prolinamide
pH and temperature not specified in the publication
0.000026
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-[3-(trifluoromethyl)benzyl]-D-prolinamide
pH and temperature not specified in the publication
0.00053
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-1-(1-methyl-1H-pyrazol-4-yl)-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000545
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-1-(2,3-dihydro-1H-inden-2-yl)-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.00024
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-1-[2-(trifluoromethoxy)-6-(trifluoromethyl)benzyl]-D-prolinamide
pH and temperature not specified in the publication
0.00005
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-1-[2-(trifluoromethoxy)benzyl]-D-prolinamide
pH and temperature not specified in the publication
0.00009
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-1-[2-(trifluoromethyl)benzyl]-D-prolinamide
pH and temperature not specified in the publication
0.00097
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000081
1-[(4-methylphenyl)sulfonyl]-N-(1-oxo-3-phenylpropan-2-yl)-D-prolinamide
-
pH and temperature not specified in the publication
0.0000085
3-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-2-oxo-4-phenylbutanoic acid
-
pH and temperature not specified in the publication
0.00005
4-(4-bromophenyl)-3-([N-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucyl]amino)-2-oxobutanoic acid
-
pH and temperature not specified in the publication
0.017
acetyl-DPMSSTYIEE-betaAla-GKREVTIPPKYRELLA-NH2
-
pH and temperature not specified in the publication
0.0024
acetyl-DPMSSTYIEELGKREVT-betaAla-PPKYRELLA-NH2
-
pH and temperature not specified in the publication
0.0000002
acetyl-DPMSSTYIEELGKREVTIPPKYRELLA-NH2
-
pH and temperature not specified in the publication
0.00000019
acetyl-RRMKWKKDPMSSTYIEELGKREVTIPPKYRELLA-NH2
-
pH and temperature not specified in the publication
0.000026
acetyl-SSTTYIEELGKREVTIPPKYR-NH2
-
pH and temperature not specified in the publication
0.0018
ethyl 3-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-2-oxo-4-phenylbutanoate
-
pH and temperature not specified in the publication
0.01
ethyl 4-(4-bromophenyl)-3-([N-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucyl]amino)-2-oxobutanoate
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.000009
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-(1-benzothiophen-2-ylcarbonyl)piperidine-4-carboxamide
-
pH and temperature not specified in the publication
0.000027
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-2-[(E)-2-[4-[(diethylamino)methyl]phenyl]ethenyl]benzamide
-
pH and temperature not specified in the publication
0.0000047
N-[(2S)-4-(2-benzylhydrazinyl)-3,4-dioxo-1-phenylbutan-2-yl]-N2-[(benzyloxy)carbonyl]-L-leucinamide
-
pH and temperature not specified in the publication
0.00002
N-[1-(4-bromophenyl)-4-(ethylamino)-3,4-dioxobutan-2-yl]-N2-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucinamide
-
pH and temperature not specified in the publication
0.0002
N2-[(benzyloxy)carbonyl]-N-[4-(ethylamino)-3,4-dioxo-1-phenylbutan-2-yl]-L-leucinamide
-
pH and temperature not specified in the publication
0.000093
acetyl-TYIEELGKREVTIPPKYR-NH2
-
pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00088
(2S)-2-[[(4-fluorophenyl)sulfonyl]amino]-N-[(3S)-2-hydroxytetrahydrofuran-3-yl]-3-methylbutanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0007
(2S,5S)-5-benzyl-6-hydroxy-2-(2-methylpropyl)morpholin-3-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000038
(3S)-2-hydroxytetrahydrofuran-3-yl N-[(10H-phenothiazin-2-yloxy)acetyl]-L-threonyl-L-leucinate
Homo sapiens
-
pH and temperature not specified in the publication
0.000089
(3S)-2-hydroxytetrahydrofuran-3-yl N-[(2S)-2-[[(10H-phenothiazin-2-yloxy)acetyl]amino]butanoyl]-L-leucinate
Homo sapiens
-
pH and temperature not specified in the publication
0.001
(3S)-3-[[N-(10H-phenothiazin-2-ylcarbonyl)-L-norvalyl]amino]tetrahydrofuran-2-yl acetate
Homo sapiens
-
IC50 above 0.001 mM, pH and temperature not specified in the publication
0.029
(7S,10S,13S,26S)-13,26-dibenzyl-7-methyl-10-(propan-2-yl)-5,7,8,10,11,13,14,25,26,28-decahydrotetrabenzo[k,m,t,v][1,4,7,10,15,18]hexaazacyclotetracosine-6,9,12,15,24,27-hexone
Homo sapiens
-
pH and temperature not specified in the publication
0.0005
1-(2-chloro-4-hydroxyphenyl)-4-oxo-7-(pyridin-4-yl)-1,4-dihydroquinoline-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000006
2-methyl-N-[(2S)-1-oxo-3-phenylpropan-2-yl]-7,8-dihydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.000056
3,4-dichlorophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 56 nM
0.000056
3,4-dichlorophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
Homo sapiens
-
IC50: 56 nM
0.00034
3-([4-[2-(methoxymethoxy)phenyl]-4-oxobutanoyl]amino)-2-oxo-4-phenylbutanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0192
3-acetyl-2-[(2,4-dichlorophenyl)amino]-8-(trifluoromethyl)quinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-2-[(3-fluorophenyl)amino]-8-phenylquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-2-[(4-chlorophenyl)amino]-5,8-difluoroquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-2-[(4-tert-butylphenyl)amino]-5,8-difluoroquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00369 - 0.00743
3-acetyl-2-[(4-tert-butylphenyl)amino]-8-chloro-6-nitroquinolin-4(1H)-one
0.03
3-acetyl-2-[[3,5-bis(trifluoromethyl)phenyl]amino]-5,8-difluoroquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-6,8-difluoro-2-[(2,4,5-trifluorophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00316 - 0.00464
3-acetyl-6-chloro-2-[(2,4-dichlorophenyl)amino]-8-nitroquinolin-4(1H)-one
0.00239 - 0.00373
3-acetyl-6-chloro-2-[(2-chloro-4-methylphenyl)amino]-8-nitroquinolin-4(1H)-one
0.03
3-acetyl-6-chloro-8-(trifluoromethyl)-2-[[4-(trifluoromethyl)phenyl]amino]quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-7,8-dichloro-2-[[3-(trifluoromethyl)phenyl]amino]quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.000277 - 0.00306
3-acetyl-8-chloro-2-[(2,4-dibromophenyl)amino]-5-methylquinolin-4(1H)-one
0.03
3-acetyl-8-chloro-2-[(2-fluoro-5-methylphenyl)amino]-5-(trifluoromethyl)quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-8-chloro-2-[(3-methylphenyl)amino]-5-nitroquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-8-chloro-2-[(4-chloro-2-fluorophenyl)amino]-5-methylquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-8-chloro-5-fluoro-2-(phenylamino)quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-8-chloro-5-methyl-2-[(2,3,4-trifluorophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-8-chloro-5-methyl-2-[(2,4,5-trifluorophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.000029
4-fluorophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 29 nM
0.00005
4-fluorophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
Homo sapiens
-
IC50: 50 nM
0.000047
4-nitrophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 47 nM
0.00005
4-nitrophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
Homo sapiens
-
IC50: 50 nM
5
4-[([(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]oxy)methyl]benzyl (2Z)-[(3R)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]ethanoate
Homo sapiens
-
-
0.00033
5-azanylidyne-N-[[(2S,3S)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]-L-norvalyl-L-arginyl-L-tryptophanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00029
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]-1H-pyrrole-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00096
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]furan-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00044
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]thiophene-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0004
benzyl [(6S,9S,12S)-6-formyl-9-(2-methylpropyl)-8,11-dioxo-2-oxa-7,10-diazabicyclo[12.2.2]octadeca-1(16),14,17-trien-12-yl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.00022
benzyl [(7S,10S,13S)-7-formyl-10-(2-methylpropyl)-9,12-dioxo-2-oxa-8,11-diazabicyclo[13.2.2]nonadeca-1(17),15,18-trien-13-yl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.00017
benzyl [(8S,11S,14S)-8-formyl-11-(2-methylpropyl)-10,13-dioxo-2-oxa-9,12-diazabicyclo[14.2.2]icosa-1(18),16,19-trien-14-yl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.000064
dimethyl (2S,2'S)-2,2'-[biphenyl-2,2'-diylbis(carbonylimino)]bis(3-phenylpropanoate)
Homo sapiens
-
pH and temperature not specified in the publication
0.000089
methyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 89 nM
0.001
methyl (3S)-4-cyclohexyl-3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxobutanoate
Homo sapiens
-
IC50: 1000 nM
0.000025
methyl (S,S,Z)-(3-sec-butyl-1-oxo-2,3-dihydro-1H-isoquinolin-4-ylidene)acetate
Homo sapiens
-
pH and temperature not specified in the publication
0.000000087
methyl N-[[2'-([(2S)-1-[(2'-aminobiphenyl-2-yl)amino]-1-oxo-3-phenylpropan-2-yl]carbamoyl)biphenyl-2-yl]carbonyl]-L-phenylalanyl-L-valinate
Homo sapiens
-
pH and temperature not specified in the publication
0.00002
N'-((1S,2R)-1-benzyl-3-[(3,5-dimethoxybenzyl)amino]-2-hydroxypropyl)-N,N-dipropylbenzene-1,3-dicarboxamide
Homo sapiens
-
IC50: 20 nM
0.000063
N-((1S)-1-benzyl-2,3-dioxo-3-[(2-phenylethyl)amino]propyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 63 nM
0.000205
N-((1S)-1-benzyl-3-[(1-methylethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 205 nM
0.0002
N-((1S)-1-benzyl-3-[(2-methoxyethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 200 nM
0.000286
N-((1S)-1-benzyl-3-[(cyclopropylmethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 286 nM
0.00071
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-methyl-4-oxo-1,4-dihydroquinoline-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00004
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-methyl-4-oxo-4H-chromene-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0028
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-4-methyl-6-methylidene-1,6-dihydropyridine-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00015
N-[(1S)-1-benzyl-2,3-dioxo-3-(pentylamino)propyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 150 nM
0.0002
N-[(1S)-1-benzyl-2,3-dioxo-3-(prop-2-en-1-ylamino)propyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 200 nM
0.000081
N-[(1S)-1-benzyl-3-(benzylamino)-2,3-dioxopropyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 81 nM
0.00034
N-[(1S)-1-benzyl-3-(ethylamino)-2,3-dioxopropyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 340 nM
0.000028
N-[(2S)-1-oxo-3-phenylpropan-2-yl]-7,8-dihydro-2H-[1,4]dioxino[2,3-g][1,2,4]benzothiadiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.000023
N-[(2S)-1-[[(3S)-2-hydroxytetrahydrofuran-3-yl]amino]-1-oxopentan-2-yl]-10H-phenothiazine-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000035
N-[(2S)-3,4-dioxo-1-phenyl-4-([3-[(phenylsulfonyl)amino]propyl]amino)butan-2-yl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.00005
N-[(2S)-4-(butylamino)-3,4-dioxo-1-phenylbutan-2-yl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.00078
N2-[(2S)-2-([[(2R,3R)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]amino)pent-4-enoyl]-L-arginyl-L-tryptophanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000076
phenyl (2-[(3-([(1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 76 nM
0.00004
phenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 40 nM
0.000035
phenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
Homo sapiens
-
IC50: 35 nM
0.00369
3-acetyl-2-[(4-tert-butylphenyl)amino]-8-chloro-6-nitroquinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00743
3-acetyl-2-[(4-tert-butylphenyl)amino]-8-chloro-6-nitroquinolin-4(1H)-one
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.00169
3-acetyl-5,8-dibromo-2-[(4-bromophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.00359
3-acetyl-5,8-dibromo-2-[(4-bromophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00317
3-acetyl-5,8-dichloro-2-[(2,4-dichlorophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.00399
3-acetyl-5,8-dichloro-2-[(2,4-dichlorophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00316
3-acetyl-6-chloro-2-[(2,4-dichlorophenyl)amino]-8-nitroquinolin-4(1H)-one
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.00464
3-acetyl-6-chloro-2-[(2,4-dichlorophenyl)amino]-8-nitroquinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00239
3-acetyl-6-chloro-2-[(2-chloro-4-methylphenyl)amino]-8-nitroquinolin-4(1H)-one
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.00373
3-acetyl-6-chloro-2-[(2-chloro-4-methylphenyl)amino]-8-nitroquinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00353
3-acetyl-8-bromo-5-chloro-2-[(4-chlorophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00994
3-acetyl-8-bromo-5-chloro-2-[(4-chlorophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.000277
3-acetyl-8-chloro-2-[(2,4-dibromophenyl)amino]-5-methylquinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00028
3-acetyl-8-chloro-2-[(2,4-dibromophenyl)amino]-5-methylquinolin-4(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00306
3-acetyl-8-chloro-2-[(2,4-dibromophenyl)amino]-5-methylquinolin-4(1H)-one
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.00456
3-acetyl-8-chloro-2-[(4-chlorophenyl)amino]-6-nitroquinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00808
3-acetyl-8-chloro-2-[(4-chlorophenyl)amino]-6-nitroquinolin-4(1H)-one
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.000199
MDL28170
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.0002
MDL28170
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activation of mu-calpain in platelets from patients with type 2 diabetes mellitus
-
from patients with recurrent miscarriage and healthy women with informed consent
-
-
-
rheumatic synovial cell line. mu-calpain, regulates MMP-3 release by rheumatic synovial cells, in addition to exerting its own degradative action on cartilage
-
NO-induced motility in osteoclasts requires regulated Ca2+ release, which activates mu-calpain. This occurs via the inositol (1,4,5)-trisphosphate receptor 1
-
elevated levels of calpain-1 in glaucomatous trabecular meshwork. However, calpain activity in glaucomatous trabecular meshwork is only about 50% of that in controls. Modification by iso-levuglandins renders calpain-1 inactive
-
protein phosphatase 2A functions as a physiological calpain phosphatase to directly dephosphorylate mu-calpain, which leads to decreased calpain activity and suppression of migration and invasion of human lung cancer cells
-
white matter from patients with MS and Parkinsons and Alzheimers diseases and white matter from normal control
-
small interfering RNAs-mediate knockdown of mu-calpain expression in MCF-7 cells that do not express m-calpain leads to a reduction of cell migration
-
autolysis of both mu-calpain and calpain-3 is tightly regulated by Ca2+ concentration in skeletal muscle across a range close to but evidently above that reached during normal activity
-
excentric exercise produces little autolytic activation of mu-calapin
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
mitochondrial calpain 1 is located within the intermembrane space and mitochondrial matrix
-
membrane-binding of mu-calpain is Ca2+-dependent. Membrane binding of mu-calpain is due to the exposed hydrophobic surface of the active site conformation and does not reduce the Ca2+ requirement for activation
-
both calpain 1 and calpain small subunit 1, which together form mu-calpain, are present in the mitochondrial intermembrane space. The N-terminus of calpain 1 is not processed following mitochondrial import, but is removed by autolysis following calpain activation. Calpain small subunit 1 is not directly imported into mitochondria, but is imported in the presence of calpain 1. The presence of a mitochondrial targeting sequence in the N-terminal region of calpain 1 is consistent with the localization of mu-calpain to the mitochondrial intermembrane space
-
calpain-1 normally localizes to the interphase nuclei and chromatin
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
metabolism
-
calpain 1 is involved in the degradation of endothelial nitric oxide synthase and heat shock protein 90 and the phosphorylation of endothelial nitric oxide synthase
physiological function
physiological function
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
physiological function
calpain 1 activity within neutrophils is necessary for them to undergo efficient phagocytosis
physiological function
calpain-1 and calpain-2 play opposite functions in both synaptic plasticity/learning and memory and neuroprotection/neurodegeneration. Calpain-1 activation is necessary for certain forms of synaptic plasticity and learning and memory, while calpain-2 activation during a brief consolidation period limits the extent of plasticity/learning. Calpain-1 is neuroprotective, while calpain-2 is neurodegenerative
physiological function
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
malfunction
-
calpain inhibition does not protect endothelial cells during cold storage
malfunction
-
calpain-1 overactivation in mitochondrial-deficient cells promotes caspase-3 activation, calpain inhibition decreases alpha-synuclein oligomerization
malfunction
-
immunodepletion or inhibition of calpain-1 in hypotonically lysed and resealed erythrocytes prevents the escape of Plasmodium falciparum parasites. Similarly, efficient egress of Tooplasma gondii from mammalian fibroblasts is blocked by either small interfering RNA-mediated suppression or genetic deletion of calpain activity
malfunction
-
inhibition of micro-calpain not only significantly reduces caspase-9/-3 activities but also completely blocks apoptosis-inducing factor redistribution
malfunction
-
knocking down mu-calpain by siRNA in FA-A cells restores levels of alphaII-spectrin to normal and reverses a number of the cellular deficiencies in these cells. siRNA knockdown of mu-Calpain in FA-A cells leads to increased cell viability and formation of nuclear foci after damage with a DNA interstrand cross-linking agent
malfunction
-
engineered cleavage of Rad21 at the calpain-cleavable site without activation of calpain-1 can lead to a loss of sister chromatid cohesion
malfunction
-
the knockdown of calpain 1 increases cell adhesion (by 36% after 30 min), enhances migration (by 46% after 12 h), and stabilizes late-stage cord formation on Matrigel by increasing cord length compared to the control human lymphatic microvascular dermal-derived endothelial cells
physiological function
-
activation of micro-calpain plays an essential role in regulating both caspase-dependent and apoptosis-inducing factor-mediated caspase-independent apoptotic pathways in cisplatin-induced apoptosis
physiological function
-
calcium-dependent plasma membrane repair requires mu-calpain
physiological function
-
calpain activation precedes caspase-12 activation in the Ca2+-mediated apoptotic cascade and, thus, may be necessary for caspase-12 activation
physiological function
-
calpain I is not required for mitochondrial apoptosis-inducing factor release in poly(ADP-ribose) polymerase-1-dependent cell death
physiological function
-
calpain regulates trastuzumab sensitivity and survival, and the deregulation of the activation of calpain promotes trastuzumab resistance, trastuzumab-resistant cells require calpain activity for survival and activation of AKT1
physiological function
-
calpain-I activity colocalizes with apoptotic cell death
physiological function
-
mu-calpain is responsible for Ca2+-induced disruption of excitation-contraction coupling
physiological function
-
mu-calpain is specifically recruited into the NMDA receptor-neuronal nitric oxide synthase-heat shock protein 90 complex following calcium loading
physiological function
-
mu-calpain plays a role in membrane repair and a protective role in skeletal muscle
physiological function
-
mu-calpain up-regulates alpha- and beta-actin in alveolar rhabdomyosarcoma cells
physiological function
-
mu-calpain proteasome-dependent I-kappaBalpha polymer degradation may contribute to cancer progression through constitutive nulear factor-kappaB activation
physiological function
-
Rad21 cleavage by calpain-1 promotes separation of sister chromatid arms
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CAN1_HUMAN
714
0
81890
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
74000
80000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
-
EC 3.4.22.52 is not derived by the autolysis of EC 3.4.22.53, but it is an independent species
additional information
-
Ca2+ causes autoproteolytic conversion of the native 80000 Da subunit into the active 75000 Da subunit
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
proteolytic modification
-
autolysis of both mu-calpain and calpain-3 is tightly regulated by Ca2+ concentration in skeletal muscle across a range close to but evidently above that reached during normal activity
phosphoprotein
-
protein phosphatase 2A functions as a physiological calpain phosphatase to directly dephosphorylate mu-calpain, which leads to decreased calpain activity and suppression of migration and invasion of human lung cancer cells
phosphoprotein
-
brain-derived neurotrophic factor does not stimulate mu-calpain serine phosphorylation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the mutant enzyme L-muyCANPDELTA3 requires 0.4-0.53 mM of Ca2+ compared to 0.06 mM for the native enzyme, bacterially expressed mutant enzyme L-muyCANPDELTA3. A chimeric form composed of domains I-III of muCANP and domain IV of calpain II is also expressed in Sf9 cells. This mutant requires less Ca2+, 0.05 mM, than the native erythrocyte enzyme and has the highest specific activity of all calpains tested. All recombinant proteins are active as monomers in polyethylene glycol-containing buffers. The in vitro association with the regulatory subunit enhances only slightly the maximal velocity and the Ca2+ dependence of the expressed proteins
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography, calmodulin-like domain of the catalytic subunit expressed in E. coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
complete amino acid sequence of the large subunit is deduced from its cDNA sequence
cloning of the 21000 Da small subunit and expression in Escherichia coli BL384
-
large catalytic subunit and two of its mutants are expressed in Escherichia coli using the baculovirus Sf9 system, the L-muCANPDELTA3 mutant lacks domain III, mutant L-muCANPDELTA4 lacks the calmodulin-like domain IV. In Sf9 cells co-expression of the inhibitor calpastatin is necessary to prevent autolysis of the L-muCANP subunit, whereas coexpression of the regulatory subunit enhances it. Only very low levels of mRNA of the truncated form L-muCANPDELTA4 are found in bacmid-transfectred Sf9 cells, and it proves impossible to isolate this mutant using the baculovirus expression system
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
although the levels of the calpain I isoform are higher in the soluble and insoluble fractions of tir- and wild type enteropathogenic Escherichia coli (E2348/69 O127:H6)-infected cells, their levels are not significantly different to the TTSS-negative control
-
calpain 1 activity is increased 2.5fold in FA-A, FA-D2, and FA-F cells as compared to normal cells and 3.5fold in FA-C and FA-G cells compared to normal cells
-
cold storage (at 4°C) induces a time dependent up-regulation of calpain 1, reflected by an increase in the autoproteolytic cleavage of calpain 1, which can be prevented by addition of EDTA or dopamine (0.025 mM) pretreatment
-
compared to control cybrids, Parkonsins disease cybrids reveal a significant increase in calpain activity
-
mu-calpain is not activated immediately following sprint, endurance or eccentric exercise. mu-Calpain is not activated 24 h after a single bout of eccentric exercise
-
there are no significant differences on the expressions of calpain-1 at the levels of mRNA and protein in patients with and without stress urinary incontinence
-
there is no age-related change in calpain 1 protein expression in human female or male kidney samples. In the human kidney, there is no age-related change in calpain 1 mRNA expression
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
inhibition of the mitochondrial calpain 1 could be a potential strategy to decrease cardiac injury during ischemia-reperfusion
medicine
medicine
-
protein phosphatase 2A functions as a physiological calpain phosphatase to directly dephosphorylate mu-calpain, which leads to decreased calpain activity and suppression of migration and invasion of human lung cancer cells. Therapeutic activation of protein phosphatase 2A to dephosphorylate calpain by enhancing ceramide production may have clinical relevance for the treatment of cancer metastasis
medicine
-
calpain and calpain inhibition is a therapeutic tool in Parkinsons disease
medicine
-
manipulating calpain activity by calpain inhibitor SNJ-1945 is a therapy for management of pathological angiogenesis, such as that occurring in proliferative retinopathy and age-related macular degeneration with neovascularization
medicine
-
mu-calpain is a marker of tumor aggressiveness and is apotential target for limiting development of rhabdomyosarcoma tumor as well as their metastatic behavior
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shastri, R.; Anandaraj, M.P.J.S.
A low-calcium-requiring calcium-activated neutral proteinase from human placenta
Biochim. Biophys. Acta
873
260-266
1986
Homo sapiens
Aoki, K.; Imajoh, S.; Ohno, S.; Emori, Y.; Koike, M.; Kosaki, G.; Suzuki K.
Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence
FEBS Lett.
205
313-317
1986
Homo sapiens (P07384), Homo sapiens
Michetti, M.; Salamino, F.; Minafra, R.; Melloni, E.; Pontremoli, S.
Calcium-binding properties of human erythrocyte calpain
Biochem. J.
325
721-726
1997
Homo sapiens
-
Vilei, E.M.; Calderara, S.; Anagli, J
Berardi, S.; Hitomi, K.; Maki, M: Carafoli, E.: Functional properties of recombinant calpain I and of mutants lacking domains III and IV of the catalytic subunits
J. Biol. Chem.
727
25802-25808
1997
Homo sapiens
-
Hitomi, K.; Uchiyama, Y.; Ohkubo, I.; Kunimatsu, M.; Sasaki, M.; Maki, M.
Purification and characterization of the active-site-mutated recombinant human mikro-calpain expressed in baculovirus-infected insect cells
Biochem. Biophys. Res. Commun.
246
681-685
1998
Homo sapiens
Shastri, R.; Jagadeesh, G.; Anandaraj, M.P.J.S.
Human placental calcium activated neutral proteinase: Separation and functional characterization of subunits
J. Biosci.
15
427-434
1990
Homo sapiens
-
Yoshimura, N.; Kikuchi, T.; Sasaki, T.; Kithara, A.; Hatanaka, M.; Murachi, T.
Two distinct Ca2+ proteases (calpain I and calpain II) purified concurrently by the same method from rat kidney
J. Biol. Chem.
258
8883-8889
1983
Homo sapiens, Rattus norvegicus
Molinari, M.; maki, M.; Carafoli, E.
Purification of mu-calpain by a novel affinity chromatography approach. New insight into the mechanism of the interaction of the protease with targets
J. Biol. Chem.
270
14576-14581
1995
Homo sapiens
Diaz, B.G.; Gross, S.; Assfalg-Machleidt, I.; Pfeiler, D.; Gollmitzer, N.; Gabrijelcic-Geiger, D.; Stubbs, M.T.; Fritz, H.; Auerswald, E.A.; Machleidt, W.
Cystatins as calpain inhibitors: engineered chicken cystatin- and stefin B-kininogen domain 2 hybrids support a cystatin-like mode of interaction with the catalytic subunit of m-calpain
Biol. Chem.
382
97-107
2001
Homo sapiens
Shields, D.C.; Schaecher, K.E.; Saido, T.C.; Banik, N.L.
A putative mechanism of demyelination in multiple sclerosis by a proteolytic enzyme, calpain
Proc. Natl. Acad. Sci. USA
96
11486-11491
1999
Homo sapiens
Wolf, B.B.; Goldstein, J.C.; Stennicke, H.R.; Beere, H.; Amarante-Mendes, G.P.; Salvesen, G.S.; Green, D.R.
Calpain functions in a caspase-independent manner to promote apoptosis-like events during platelet activation
Blood
94
1683-1692
1999
Homo sapiens, Sus scrofa
Tompa, P.; Toth-Boconadi, R.; Friedrich, P.
Frequency decoding of fast calcium oscillations by calpain
Cell Calcium
29
161-170
2001
Homo sapiens
Rojas, F.J.; Brush, M.; Moretti-Rojas, I.
Calpain-calpastatin: a novel, complete calcium-dependent protease system in human spermatozoa
Mol. Hum. Reprod.
5
520-526
1999
Homo sapiens
Murphy, R.M.; Snow, R.J.; Lamb, G.D.
m-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans
Am. J. Physiol.
290
C116-C122
2006
Homo sapiens
Veerann, V.; Kaji, T.; Boland, B.; Odrljin, T.; Mohan, P.; Basavarajappa, B.S.; Peterhoff, C.; Cataldo, A.; Rudnicki, A.; Amin, N.; Li, B.S.; Pant, H.C.; Hungund, B.L.; Arancio, O.; Nixon, R.A.
Calpain mediates calcium-induced activation of the Erk1,2 MAPK pathway and cytoskeletal phosphorylation in neurons: Relevance to Alzheimers disease
Am. J. Pathol.
165
795-805
2004
Homo sapiens
Fernandez-Montalvan, A.; Assfalg-Machleidt, I.; Pfeiler, D.; Fritz, H.; Jochum, M.; Machleidt, W.
mu-Calpain binds to lipid bilayers via the exposed hydrophobic surface of its Ca2+-activated conformation
Biol. Chem.
387
617-627
2006
Homo sapiens
Bihovsky, R.; Tao, M.; Mallamo, J.P.; Wells, G.J.
1,2-Benzothiazine 1,1-dioxide alpha-ketoamide analogues as potent calpain I inhibitors
Bioorg. Med. Chem. Lett.
14
1035-1038
2004
Homo sapiens
Carragher, N.O.
Calpain inhibition: a therapeutic strategy targeting multiple disease states
Curr. Pharm. Des.
12
615-638
2006
Homo sapiens (P07384)
Guerini, D.; Pan, B.; Carafoli, E.
Expression, purification, and characterization of isoform 1 of the plasma membrane Ca2+ pump: focus on calpain sensitivity
J. Biol. Chem.
278
38141-38148
2003
Homo sapiens
Altznauer, F.; Conus, S.; Cavalli, A.; Folkers, G.; Simon, H.U.
Calpain-1 regulates Bax and subsequent Smac-dependent caspase-3 activation in neutrophil apoptosis
J. Biol. Chem.
279
5947-5957
2004
Homo sapiens
Kumagai, K.; Ozaki, Y.; Nakanishi, T.; Inomata, M.; Furuno, T.; Nakanishi, M.; Ogasawara, M.S.
Role of mu-calpain in human decidua for recurrent miscarriage
Am. J. Reprod. Immunol.
59
339-346
2008
Homo sapiens
Morita, M.; Banno, Y.; Dohjima, T.; Nozawa, S.; Fushimi, K.; Fan, D.G.; Ohno, T.; Miyazawa, K.; Liu, N.; Shimizu, K.
mu-Calpain is involved in the regulation of TNF-alpha-induced matrix metalloproteinase-3 release in a rheumatoid synovial cell line
Biochem. Biophys. Res. Commun.
343
937-942
2006
Homo sapiens
Govindarajan, B.; Laird, J.; Salomon, R.G.; Bhattacharya, S.K.
Isolevuglandin-modified proteins, including elevated levels of inactive calpain-1, accumulate in glaucomatous trabecular meshwork
Biochemistry
47
817-825
2008
Homo sapiens
Berg, U.; Bang, P.; Carlsson-Skwirut, C.
Calpain proteolysis of insulin-like growth factor binding protein (IGFBP) -2 and -3, but not of IGFBP-1
Biol. Chem.
388
859-863
2007
Homo sapiens
Pfizer, J.; Assfalg-Machleidt, I.; Machleidt, W.; Schaschke, N.
Inhibition of human mu-calpain by conformationally constrained calpastatin peptides
Biol. Chem.
389
83-90
2008
Homo sapiens
Chicharro, R.; Alonso, M.; Mazo, M.T.; Aran, V.J.; Herradon, B.
Derivatives of 3-sec-butyl-1-oxo-2,3-dihydroisoquinoline as inhibitors of micro mu-calpain
ChemMedChem
1
710-714
2006
Homo sapiens, Sus scrofa
Randriamboavonjy, V.; Pistrosch, F.; Boelck, B.; Schwinger, R.H.; Dixit, M.; Badenhoop, K.; Cohen, R.A.; Busse, R.; Fleming, I.
Platelet sarcoplasmic endoplasmic reticulum Ca2+-ATPase and mu-calpain activity are altered in type 2 diabetes mellitus and restored by rosiglitazone
Circulation
117
52-60
2008
Homo sapiens
Wu, M.; Yu, Z.; Fan, J.; Caron, A.; Whiteway, M.; Shen, S.H.
Functional dissection of human protease mu-calpain in cell migration using RNAi
FEBS Lett.
580
3246-3256
2006
Homo sapiens
Murphy, R.M.; Goodman, C.A.; McKenna, M.J.; Bennie, J.; Leikis, M.; Lamb, G.D.
Calpain-3 is autolyzed and hence activated in human skeletal muscle 24 h following a single bout of eccentric exercise
J. Appl. Physiol.
103
926-931
2007
Homo sapiens
Xu, L.; Deng, X.
Suppression of cancer cell migration and invasion by protein phosphatase 2A through dephosphorylation of micro- and m-calpains
J. Biol. Chem.
281
35567-35575
2006
Homo sapiens
Badugu, R.; Garcia, M.; Bondada, V.; Joshi, A.; Geddes, J.W.
N terminus of calpain 1 is a mitochondrial targeting sequence
J. Biol. Chem.
283
3409-3417
2008
Homo sapiens, Rattus norvegicus
Yaroslavskiy, B.B.; Sharrow, A.C.; Wells, A.; Robinson, L.J.; Blair, H.C.
Necessity of inositol (1,4,5)-trisphosphate receptor 1 and mu-calpain in NO-induced osteoclast motility
J. Cell Sci.
120
2884-2894
2007
Homo sapiens
Upla, P.; Marjomaeki, V.; Nissinen, L.; Nylund, C.; Waris, M.; Hyypiae, T.; Heino, J.
Calpain 1 and 2 are required for RNA replication of echovirus 1
J. Virol.
82
1581-1590
2008
Homo sapiens
Covington, M.D.; Arrington, D.D.; Schnellmann, R.G.
Calpain 10 is required for cell viability and is decreased in the aging kidney
Am. J. Physiol. Renal Physiol.
296
F478-F486
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Vissing, K.; Overgaard, K.; Nedergaard, A.; Fredsted, A.; Schjerling, P.
Effects of concentric and repeated eccentric exercise on muscle damage and calpain-calpastatin gene expression in human skeletal muscle
Eur. J. Appl. Physiol.
103
323-332
2008
Homo sapiens (P07384), Homo sapiens
Verburg, E.; Murphy, R.M.; Richard, I.; Lamb, G.D.
Involvement of calpains in Ca2+-induced disruption of excitation-contraction coupling in mammalian skeletal muscle fibers
Am. J. Physiol. Cell Physiol.
296
C1115-C1122
2009
Homo sapiens
Sergeev, I.N.
1,25-Dihydroxyvitamin D3 induces Ca2+-mediated apoptosis in adipocytes via activation of calpain and caspase-12
Biochem. Biophys. Res. Commun.
384
18-21
2009
Homo sapiens
Hayakawa, M.; Hayakawa, H.; Matsuyama, Y.; Tamemoto, H.; Okazaki, H.; Tominaga, S.
Mature interleukin-33 is produced by calpain-mediated cleavage in vivo
Biochem. Biophys. Res. Commun.
387
218-222
2009
Homo sapiens
Jiao, W.; McDonald, D.Q.; Coxon, J.M.; Parker, E.J.
Molecular modeling studies of peptide inhibitors highlight the importance of conformational prearrangement for inhibition of calpain
Biochemistry
49
5533-5539
2010
Homo sapiens
Zhang, P.; Sridharan, D.M.; Lambert, M.W.
Knockdown of micro-calpain in Fanconi Anemia, FA-A, cells by siRNA restores alphaII spectrin levels and corrects chromosomal instability and defective DNA interstrand cross-link repair
Biochemistry
49
5570-5581
2010
Homo sapiens
Mellgren, R.L.; Miyake, K.; Kramerova, I.; Spencer, M.J.; Bourg, N.; Bartoli, M.; Richard, I.; Greer, P.A.; McNeil, P.L.
Calcium-dependent plasma membrane repair requires m- or mu-calpain, but not calpain-3, the proteasome, or caspases
Biochim. Biophys. Acta
1793
1886-1893
2009
Homo sapiens
Kelly, J.C.; Cuerrier, D.; Graham, L.A.; Campbell, R.L.; Davies, P.L.
Profiling of calpain activity with a series of FRET-based substrates
Biochim. Biophys. Acta
1794
1505-1509
2009
Homo sapiens
Goncalves, I.; Nitulescu, M.; Saido, T.; Dias, N.; Pedro, L.; e Fernandes, J.; Ares, M.; Poern-Ares, I.
Activation of calpain-1 in human carotid artery atherosclerotic lesions
BMC Cardiovasc. Disord.
9
26
2009
Homo sapiens
Blachford, C.; Celic, A.; Petri, E.T.; Ehrlich, B.E.
Discrete proteolysis of neuronal calcium sensor-1 (NCS-1) by mu-calpain disrupts calcium binding
Cell Calcium
46
257-262
2009
Homo sapiens
Dean, P.; Muehlen, S.; Quitard, S.; Kenny, B.
The bacterial effectors EspG and EspG2 induce a destructive calpain activity that is kept in check by the co-delivered Tir effector
Cell. Microbiol.
12
1308-1321
2010
Homo sapiens
Murphy, R.M.
Calpains, skeletal muscle function and exercise
Clin. Exp. Pharmacol. Physiol.
37
385-391
2010
Homo sapiens, Rattus norvegicus
Pietsch, M.; Chua, K.C.; Abell, A.D.
Calpains: attractive targets for the development of synthetic inhibitors
Curr. Top. Med. Chem.
10
270-293
2010
Homo sapiens
Le Goff, E.; Vallentin, A.; Harmand, P.O.; Aldrian-Herrada, G.; Rebiere, B.; Roy, C.; Benyamin, Y.; Lebart, M.C.
Characterization of L-plastin interaction with beta integrin and its regulation by micro-calpain
Cytoskeleton (Hoboken)
67
286-296
2010
Homo sapiens
Roumes, H.; Leloup, L.; Dargelos, E.; Brustis, J.J.; Daury, L.; Cottin, P.
Calpains: markers of tumor aggressiveness?
Exp. Cell Res.
316
1587-1599
2010
Homo sapiens
Ravulapalli, R.; Campbell, R.L.; Gauthier, S.Y.; Dhe-Paganon, S.; Davies, P.L.
Distinguishing between calpain heterodimerization and homodimerization
FEBS J.
276
973-982
2009
Homo sapiens
Simonin, Y.; Disson, O.; Lerat, H.; Antoine, E.; Biname, F.; Rosenberg, A.R.; Desagher, S.; Lassus, P.; Bioulac-Sage, P.; Hibner, U.
Calpain activation by hepatitis C virus proteins inhibits the extrinsic apoptotic signaling pathway
Hepatology
50
1370-1379
2009
Homo sapiens
Martin-Villar, E.; Yurrita, M.M.; Fernandez-Munoz, B.; Quintanilla, M.; Renart, J.
Regulation of podoplanin/PA2.26 antigen expression in tumour cells. Involvement of calpain-mediated proteolysis
Int. J. Biochem. Cell Biol.
41
1421-1429
2009
Homo sapiens
Liu, L.; Xing, D.; Chen, W.R.
Micro-calpain regulates caspase-dependent and apoptosis inducing factor-mediated caspase-independent apoptotic pathways in cisplatin-induced apoptosis
Int. J. Cancer
125
2757-2766
2009
Homo sapiens
Wu, Y.; Zhang, L.; Jin, H.; Zhou, J.; Xie, Z.
The role of calpain-calpastatin system in the development of stress urinary incontinence
Int. Urogynecol. J. Pelvic. Floor Dysfunct.
21
63-68
2010
Homo sapiens
Lehti, M.; Kivelae, R.; Komi, P.; Komulainen, J.; Kainulainen, H.; Kyroelaeinen, H.
Effects of fatiguing jumping exercise on mRNA expression of titin-complex proteins and calpains
J. Appl. Physiol.
106
1419-1424
2009
Homo sapiens
Gafni, J.; Cong, X.; Chen, S.F.; Gibson, B.W.; Ellerby, L.M.
Calpain-1 cleaves and activates caspase-7
J. Biol. Chem.
284
25441-25449
2009
Homo sapiens
OConnell, M.P.; Fiori, J.L.; Baugher, K.M.; Indig, F.E.; French, A.D.; Camilli, T.C.; Frank, B.P.; Earley, R.; Hoek, K.S.; Hasskamp, J.H.; Elias, E.G.; Taub, D.D.; Bernier, M.; Weeraratna, A.T.
Wnt5A activates the calpain-mediated cleavage of filamin A
J. Invest. Dermatol.
129
1782-1789
2009
Homo sapiens
Kang, D.H.; Jun, K.Y.; Lee, J.P.; Pak, C.S.; Na, Y.; Kwon, Y.
Identification of 3-acetyl-2-aminoquinolin-4-one as a novel, nonpeptidic scaffold for specific calpain inhibitory activity
J. Med. Chem.
52
3093-3097
2009
Homo sapiens
Averna, M.; Stifanese, R.; De Tullio, R.; Beccaria, F.; Salamino, F.; Pontremoli, S.; Melloni, E.
Calpain-mediated activation of NO synthase in human neuroblastoma SK-N-BE cells
J. Neurochem.
110
412-421
2009
Homo sapiens
Wang, Y.; Kim, N.S.; Li, X.; Greer, P.A.; Koehler, R.C.; Dawson, V.L.; Dawson, T.M.
Calpain activation is not required for AIF translocation in PARP-1-dependent cell death (parthanatos)
J. Neurochem.
110
687-696
2009
Homo sapiens
Xu, J.; Kurup, P.; Zhang, Y.; Goebel-Goody, S.M.; Wu, P.H.; Hawasli, A.H.; Baum, M.L.; Bibb, J.A.; Lombroso, P.J.
Extrasynaptic NMDA receptors couple preferentially to excitotoxicity via calpain-mediated cleavage of STEP
J. Neurosci.
29
9330-9343
2009
Homo sapiens
Zadran, S.; Jourdi, H.; Rostamiani, K.; Qin, Q.; Bi, X.; Baudry, M.
Brain-derived neurotrophic factor and epidermal growth factor activate neuronal m-calpain via mitogen-activated protein kinase-dependent phosphorylation
J. Neurosci.
30
1086-1095
2010
Homo sapiens
Ma, H.; Tochigi, A.; Shearer, T.R.; Azuma, M.
Calpain inhibitor SNJ-1945 attenuates events prior to angiogenesis in cultured human retinal endothelial cells
J. Ocul. Pharmacol. Ther.
25
409-414
2009
Homo sapiens
Alonso, M.; Chicharro, R.; Miranda, C.; Aran, V.J.; Maestro, M.A.; Herradon, B.
X-ray diffraction, solution structure, and computational studies on derivatives of (3-sec-butyl-2,3-dihydro-1H-isoquinolin-4-ylidene)acetic acid: compounds with activity as calpain inhibitors
J. Org. Chem.
75
342-352
2010
Homo sapiens
Rudic, B.; Song, H.; Breedijk, A.; Brinkkoetter, P.; Beck, G.; Yard, B.; Ponelies, N.
Hypothermic preservation up-regulates calpain expression and increases ubiquitination in cultured vascular endothelial cells: influence of dopamine pretreatment
J. Surg. Res.
160
325-332
2010
Homo sapiens
Esteves, A.R.; Arduino, D.M.; Swerdlow, R.H.; Oliveira, C.R.; Cardoso, S.M.
Dysfunctional mitochondria uphold calpain activation: contribution to Parkinsons disease pathology
Neurobiol. Dis.
37
723-730
2010
Homo sapiens
Kulkarni, S.; Reddy, K.B.; Esteva, F.J.; Moore, H.C.; Budd, G.T.; Tubbs, R.R.
Calpain regulates sensitivity to trastuzumab and survival in HER2-positive breast cancer
Oncogene
29
1339-1350
2010
Homo sapiens
Chandramohanadas, R.; Davis, P.H.; Beiting, D.P.; Harbut, M.B.; Darling, C.; Velmourougane, G.; Lee, M.Y.; Greer, P.A.; Roos, D.S.; Greenbaum, D.C.
Apicomplexan parasites co-opt host calpains to facilitate their escape from infected cells
Science
324
794-797
2009
Homo sapiens
Kim, D.S.; Han, B.G.; Park, K.S.; Lee, B.I.; Kim, S.Y.; Bae, C.D.
I-kappaBalpha depletion by transglutaminase 2 and mu-calpain occurs in parallel with the ubiquitin-proteasome pathway
Biochem. Biophys. Res. Commun.
399
300-306
2010
Homo sapiens
Panigrahi, A.K.; Zhang, N.; Mao, Q.; Pati, D.
Calpain-1 cleaves Rad21 to promote sister chromatid separation
Mol. Cell. Biol.
31
4335-4347
2011
Homo sapiens
Prangsaengtong, O.; Senda, K.; Doki, Y.; Park, J.Y.; Jo, M.; Sakurai, H.; Shibahara, N.; Saiki, I.; Koizumi, K.
Calpain 1 and -2 play opposite roles in cord formation of lymphatic endothelial cells via eNOS regulation
Hum. Cell
25
36-44
2012
Homo sapiens
Averna, M.; De Tullio, R.; Pedrazzi, M.; Bavestrello, M.; Pellegrini, M.; Salamino, F.; Pontremoli, S.; Melloni, E.
Interaction between calpain-1 and HSP90: new insights into the regulation of localization and activity of the protease
PLoS ONE
10
e0116738
2015
Homo sapiens
Fan, X.; Zhang, Q.; You, C.; Qian, Y.; Gao, J.; Liu, P.; Chen, H.; Song, H.; Chen, Y.; Chen, K.; Zhou, Y.
Proteolysis of the human DNA polymerase delta smallest subunit p12 by mu-calpain in calcium-triggered apoptotic HeLa cells
PLoS ONE
9
e93642
2014
Homo sapiens
Jiang, S.; Shao, C.; Tang, F.; Wang, W.; Zhu, X.
Dynamin-like protein 1 cleavage by calpain in Alzheimers disease
Aging Cell
18
e12912
2019
Homo sapiens (P07384)
Campbell, J.S.; Hallett, M.B.
Active calpain in phagocytically competent human neutrophils electroinjection of fluorogenic calpain substrate
Biochem. Biophys. Res. Commun.
457
341-346
2015
Homo sapiens (P07384), Homo sapiens
Chen, Q.; Lesnefsky, E.J.
Heart mitochondria and calpain 1 Location, function, and targets
Biochim. Biophys. Acta
1852
2372-2378
2015
Homo sapiens (P07384)
Jantos, K.; Kling, A.; Mack, H.; Hornberger, W.; Moeller, A.; Nimmrich, V.; Lao, Y.; Nijsen, M.
Discovery of ABT-957 1-Benzyl-5-oxopyrrolidine-2-carboxamides as selective calpain inhibitors with enhanced metabolic stability
Bioorg. Med. Chem. Lett.
29
1968-1973
2019
Homo sapiens (P07384)
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