PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15649357-5	2005	RESULTS: We show that the binding of activated Cdc42 to the Cool-2 dimer markedly enhances its ability to associate with GDP bound Rac1, resulting in a significant activation of Rac-GEF activity.	Guanosine Diphosphate	121-124	AKT serine/threonine kinase 1	Homo sapiens	131-134	
15649357-6	2005	While the Rac-specific GEF activity of Cool-2 is mediated through the Dbl homology (DH) domain from one monomer and the Pleckstrin homology domain from the other, activated Cdc42 interacts with the DH domain, most likely opposite the DH domain binding site for GDP bound Rac.	Guanosine Diphosphate	261-264	AKT serine/threonine kinase 1	Homo sapiens	10-13