IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Deregulation of proteasome function induces Abl-mediated cell death by uncoupling p130CAS and c-CrkII. Deregulation of proteasome function induces Abl-mediated cell death by uncoupling p130CAS and c-CrkII. J. Biol. Chem. (0021-9258) 2006 imex curation Holcomb M., Rufini A., Barila D., Klemke RL. BioCreative - Critical Assessment of Information Extraction systems in Biology rklemke@ucsd.edu 24-JAN-2007: Contacted by JYOTI. Only protein-protein interactions chlae-cos_7 Cercopithecus aethiops simian cells transformed with SV40 Grivet cos_7 cercopithecus aethiops, by transformation with SV40 anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Holcomb M., Rufini A., Barila D., Klemke RL. BioCreative - Critical Assessment of Information Extraction systems in Biology rklemke@ucsd.edu Accepted 2006-SEP-1 by DAVET. J. Biol. Chem. (0021-9258) 2006 Only protein-protein interactions imex curation crk_cerae_protein Cercopithecus aethiops Crk protein protein protein chlae Chlorocebus aethiops Cercopithecus aethiops Grivet Green monkey Similar to P46108 An amino acid sequence which is not represented in UniProt bcar1_cerae_protein Cercopithecus aethiops Cas (p130Cas) (Crk-associated substrate) protein protein chlae Chlorocebus aethiops Cercopithecus aethiops Grivet Green monkey Similar to P56945 An amino acid sequence which is not represented in UniProt bcar1-crk 1 2 unspecified role unspecified role prey prey 3 unspecified role unspecified role bait bait physical association physical association 2 C the increase in Crk Tyr221 phosphorylation in response to inhibition of the 26 S proteasome was associated with a 50% decrease in CAS-Crk coupling The increase in Crk Tyr221 phosphorylation in response to inhibition of the 26 S proteasome was associated with a 50% decrease in CAS-Crk coupling. Thus, inhibition of ubiquitin-mediated protein degradation specifically decreases CAS-Crk coupling. The interaction is only seen in the cells allowed to reattach to fibronectin-coated dishes and not those held in suspension.