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ABL1 — CAT

Pathways - manually collected, often from reviews:

• OpenBEL Selventa BEL large corpus: CAT → ABL1 (increases) Cao et al., J Biol Chem 2003*
  Evidence: The results demonstrate that catalase, a major effector of the cellular defence against hydrogen peroxide, interacts with c-Abl and Arg. The results show that hydrogen peroxide induced binding of c-Abl and Arg to catalase. The SH3 domains of c-Abl and Arg bound directly to catalase at a 293 PFNP296 site. c-Abl and Arg phosphorylated catalase at Tyr-231 and Tyr-386 in vitro and in the response of cells to Hydrogen peroxide. The functional significance of the interaction is supported by the demons...

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

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: CAT — ABL1 (physical association, affinity chromatography technology) Cao et al., J Biol Chem 2003*
• IRef Biogrid Interaction: CAT — ABL1 (direct interaction, pull down) Cao et al., J Biol Chem 2003*
• IRef Biogrid Interaction: CAT — ABL1 (direct interaction, enzymatic study) Cao et al., J Biol Chem 2003*

Text-mined interactions from Literome

Cao et al., J Biol Chem 2003 : Catalase activity is regulated by c-Abl and Arg in the oxidative stress response ... These findings indicate that c-Abl and Arg regulate catalase and that this signaling pathway is of importance to apoptosis in the oxidative stress response
Cao et al., Biochemistry 2003 : These findings indicate that, in addition to stimulating catalase activity, c-Abl and Arg promote catalase degradation in the oxidative stress response
Rhee et al., Antioxid Redox Signal 2005 : c-Abl and Arg nonreceptor protein tyrosine kinases associate with catalase in cells treated with H ( 2 ) O ( 2 ) by mechanisms involving the SH3 domains of the kinases and the Pro ( 293 ) PheAsnPro motif of catalase and activate catalase by phosphorylating it on Tyr ( 231 ) and Tyr ( 386 )