<unk>  acts as a molecular on/off switch, using protein dynamics. Once it is allosterically activated, it recruits and activates proteins necessary for the propagation of growth factors, as well as other cell signaling receptors like c-Raf and PI 3-kinase.<unk>  upregulates the GLUT1 glucose transporter, thereby contributing to the Warburg effect in cancer cells.<unk>  binds to GTP in its active state. It also possesses an intrinsic enzymatic activity which cleaves the terminal phosphate of the nucleotide, converting it to GDP. Upon conversion of GTP to GDP,<unk>  is deactivated. The rate of conversion is usually slow, but can be increased dramatically by an accessory protein of the GTPase-activating protein (GAP) class, for example RasGAP. In turn,<unk>  can bind to proteins of the Guanine Nucleotide Exchange Factor (GEF) class (such as SOS1), which forces the release of bound nucleotide (GDP). Subsequently,<unk>  binds GTP present in the cytosol and the GEF is released from ras-GTP. Other members of the Ras family include: HRAS and NRAS. These proteins all are regulated in the same manner and appear to differ in their sites of action within the cell.
KRAS
BRAF 
CoWIN
TFM-4AS-1
CDK13
ERCC2
Kras
WRAP53