◀ Back to CAPN2
CAPN2 — CAPNS1
Pathways - manually collected, often from reviews:
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Bind Interaction:
CAPN2
—
CAPNS1
Strobl et al., Proc Natl Acad Sci U S A 2000*, Masumoto et al., Acta Crystallogr D Biol Crystallogr 2000*, Reverter et al., Biol Chem 2001*, Reverter et al., Trends Cardiovasc Med 2001*
-
IRef Bind_translation Interaction:
CAPN2
—
CAPNS1
(x-ray crystallography)
Reverter et al., Trends Cardiovasc Med 2001*
-
IRef Biogrid Interaction:
CAPN2
—
CAPNS1
(association, x-ray crystallography)
Reverter et al., Biol Chem 2001*
-
IRef Hprd Interaction:
CAPN2
—
CAPNS1
(in vitro)
Strobl et al., Proc Natl Acad Sci U S A 2000*, Masumoto et al., Acta Crystallogr D Biol Crystallogr 2000*, Reverter et al., Biol Chem 2001*, Reverter et al., Trends Cardiovasc Med 2001*
-
IRef Intact Interaction:
CAPN2
—
CAPNS1
(direct interaction, x-ray crystallography)
Strobl et al., Proc Natl Acad Sci U S A 2000*
-
IRef Intact Interaction:
Complex of CAST-CAPN2-CAPNS1
(physical association, nuclear magnetic resonance)
Kiss et al., FEBS Lett 2008*
-
IRef Ophid Interaction:
CAPN2
—
CAPNS1
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
Text-mined interactions from Literome
Makowski et al., Res Commun Mol Pathol Pharmacol 1999
:
Calpain II was not
activated ( < 10 % ) by
Mg2+ or Mn2+
Wang et al., Oncogene 2003
(Breast Neoplasms) :
Treatment of ZR75 cultures with calcium+A23187 recapitulated the formation of the calcium/calpain induced LMW forms of cyclin E. Altered calcium homeostasis and/or inability of the endogenous calpain inhibitor to control the activity of high levels of the
calpain small subunit may
contribute to increased
calpain activity in breast tumors, causing abundant levels of LMW cyclin E
Shimizu et al., J Orthop Res 1991
:
Calpain I requires a low concentration of Ca2+ for activation, and
calpain II
requires a much higher Ca2+ concentration
Murachi et al., Prog Clin Biol Res 1990
:
Calpain I requires low ( or microM ) -Ca2+ for activation and
calpain II
requires high ( or mM ) -Ca2+
Bate et al., PloS one 2012
:
Calpain2 mediated cleavage of
talin between the head and rod domains has previously been shown to be important in FA turnover
Briz et al., J Neurosci 2013
:
Calpain-2 , but not calpain-1, treatment of brain homogenates
resulted in
PTEN degradation
Murachi et al., Adv Exp Med Biol 1989
:
Calpain I requires low Ca2+ for activation and
calpain II
requires high Ca2+
Cottin et al., Reprod Nutr Dev 1988
:
`` In vitro '' highly purified
Calpain II was optimally
activated by 2 mM
Ca2+ and had two subunits with a molecular weight of 80 kDa and 28 kDa