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CAPN3 — TTN

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: CAPN3 — TTN (direct interaction, two hybrid) Sorimachi et al., J Biol Chem 1995*
• IRef Biogrid Interaction: CAPN3 — TTN (direct interaction, two hybrid) Ono et al., J Biol Chem 1998*
• IRef Hprd Interaction: CAPN3 — TTN (in vivo) Sorimachi et al., Adv Exp Med Biol 2000*, Sorimachi et al., J Biol Chem 1995*, Kinbara et al., Arch Biochem Biophys 1997*, Ono et al., J Biol Chem 1998*, Kinbara et al., Biochem Pharmacol 1998*
• IRef Hprd Interaction: CAPN3 — TTN (in vitro) Sorimachi et al., Adv Exp Med Biol 2000*, Sorimachi et al., J Biol Chem 1995*, Kinbara et al., Arch Biochem Biophys 1997*, Ono et al., J Biol Chem 1998*, Kinbara et al., Biochem Pharmacol 1998*
• IRef Hprd Interaction: CAPN3 — TTN (two hybrid) Sorimachi et al., Adv Exp Med Biol 2000*, Sorimachi et al., J Biol Chem 1995*, Kinbara et al., Arch Biochem Biophys 1997*, Ono et al., J Biol Chem 1998*, Kinbara et al., Biochem Pharmacol 1998*
• IRef Intact Interaction: CAPN3 — TTN (physical association, two hybrid) Laure et al., FEBS J 2010*
• IRef Intact Interaction: CAPN3 — TTN (physical association, two hybrid fragment pooling approach) Blandin et al., Skeletal muscle 2013
• IRef Ophid Interaction: CAPN3 — TTN (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Lim et al., J Biol Chem 2004 (Necrosis) : Anthracyclines induce calpain dependent titin proteolysis and necrosis in cardiomyocytes
Kim et al., Biosci Biotechnol Biochem 1995 : The present data suggest that the degradation of connectin in muscle might be caused by mu-calpain in the early stage of aging, and then with time, this action is replaced by m-calpain or cathepsin D