Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin. Interacts with the GTP-bound form of RALA, RALB, CDC42 and RAC1. Interacts with REPS1 and REPS2 and this does not affect the Ral-binding activity. Interacts with DAB2IP. Interacts with catalytically active CCNB1 and CDK1 during mitosis. Interacts with EPN1, NUMB and TFAP2A during interphase and mitosis. Expressed ubiquitously but at low levels. Shows a strong expression in the erythrocytes. Note: This description may include information from UniProtKB.
Molecular Function: ATPase activity; ATPase activity, coupled to movement of substances; GTPase activator activity; protein binding; Rac GTPase binding; Ral GTPase binding; transmembrane transporter activity
Biological Process: chemotaxis; endocytosis; positive regulation of GTPase activity; regulation of GTPase activity; regulation of small GTPase mediated signal transduction; signal transduction; small GTPase mediated signal transduction; transmembrane transport; transport
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.