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Literature summary for 3.4.22.54 extracted from

  • Ojima, K.; Ono, Y.; Doi, N.; Yoshioka, K.; Kawabata, Y.; Labeit, S.; Sorimachi, H.
    Myogenic stage, sarcomere length, and protease activity modulate localization of muscle-specific calpain (2007), J. Biol. Chem., 282, 14493-14504.
    View publication on PubMed
Search for more literature for 3.4.22.54

Cloned(Commentary)

Cloned (Comment) Organism
expression in COS-7 cells Homo sapiens
expression in COS-7 cells Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens p94 proteolytic activity is involved in responses to muscle conditions, p94 inactivation causes limb-girdle muscular dystrophy ?
-
 ?
additional information Mus musculus p94 proteolytic activity is involved in responses to muscle conditions, p94 inactivation causes limb-girdle muscular dystrophy ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P20807
-
-
Mus musculus Q64691
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle cell from quadriceps femoris and the soleus muscles. A series of p94 splice variants is expressed immediately after muscle differentiation and differentially change localization during myofibrillogenesis. Endogenous N-terminal (but not C-terminal) domain of p94 is not only localized in the Z-bands but also directly bound to sarcomeric alpha-actinin. Incorporation of proteolytic N-terminal fragments of p94 into the Z-bands. In myofibrils localization of exogenously expressed p94 shifts from the M-line to N2A as the sarcomere lengthens beyond about 0.0026 and 0.0028 mm for wild-type and protease inactive p94, respectively Homo sapiens
-
skeletal muscle cell from quadriceps femoris and the soleus muscles. A series of p94 splice variants is expressed immediately after muscle differentiation and differentially change localization during myofibrillogenesis. Endogenous N-terminal (but not C-terminal) domain of p94 is not only localized in the Z-bands but also directly bound to sarcomeric alpha-actinin. Incorporation of proteolytic N-terminal fragments of p94 into the Z-bands. In myofibrils localization of exogenously expressed p94 shifts from the M-line to N2A as the sarcomere lengthens beyond about 0.0026 and 0.0028 mm for wild-type and protease inactive p94, respectively Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information p94 proteolytic activity is involved in responses to muscle conditions, p94 inactivation causes limb-girdle muscular dystrophy Homo sapiens ?
-
 ?
additional information p94 proteolytic activity is involved in responses to muscle conditions, p94 inactivation causes limb-girdle muscular dystrophy Mus musculus ?
-
 ?

Synonyms

Synonyms Comment Organism
p94/calpain 3
-
 Homo sapiens
p94/calpain 3
-
 Mus musculus