3.4.22.54: calpain-3
This is an abbreviated version!
For detailed information about calpain-3, go to the full flat file.
Word Map on EC 3.4.22.54
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3.4.22.54
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calpains
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dystrophy
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muscular
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limb-girdle
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girdle
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lgmd2a
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limb
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calpainopathy
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titin
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calpastatin
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myopathy
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dysferlin
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tender
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autolytic
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sarcomere
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mu-calpains
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sarcoglycans
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myofibrillar
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telethonin
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scapular
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alpha-sarcoglycan
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merosin
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autolyzed
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caveolin-3
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nebulin
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lumborum
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m-lines
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dysferlinopathy
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sarcoglycanopathy
- 3.4.22.54
- calpains
- dystrophy
- muscular
-
limb-girdle
-
girdle
-
lgmd2a
- limb
-
calpainopathy
- titin
- calpastatin
- myopathy
-
dysferlin
-
tender
-
autolytic
- sarcomere
- mu-calpains
-
sarcoglycans
- myofibrillar
-
telethonin
-
scapular
-
alpha-sarcoglycan
-
merosin
-
autolyzed
-
caveolin-3
-
nebulin
- lumborum
-
m-lines
-
dysferlinopathy
- sarcoglycanopathy
Reaction
broad endopeptidase activity =
Synonyms
C3DIV, calcium-activated neutral proteinase 3, Calp3, calpain 3, calpain 3 (p94), calpain 3 domain IV, calpain 3/p94, calpain L3, calpain M, calpain p94, calpain-3, calpain3, CANP 3, CAPN3, Cn94, MP78, Mp84, muscle calpain, muscle-specific calcium-activated neutral protease 3, muscle-specific calpain, nCL-1, p94, p94-calpain, p94/calpain 3, skeletal muscle-specific calpain
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 3.4.22.54 - calpain-3
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proteolytic modification
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insertion sequence 1 of muscle-specific calpain acts as an internal propeptide. Autoproteolysis serves to remove insertion sequence 1, making the active site available for hydrolysis of exogenous substrates and accessible to inhibitors
proteolytic modification
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P94 insertion sequence 1 is a propeptide that must be autoproteolytically cleaved to provide access of substrates and inhibitors to the enzyme's active site
proteolytic modification
insertion sequence IS1 interrupts the protease core and must be cleaved for activation and substrate binding