Cytochrome p450, family 2, subfamily F, polypeptide 2 (CYP4F2) catalyzes the NADPH-dependent oxidation of the terminal carbon of long and very long-chain fatty acids, the side chains of vitamin K (K1, K2) and vitamin E (tocopherols and tocotrienols), arachidonic acid (AA), and leukotriene B4 (LTB4). CYP4F2 localizes to the endoplasmic reticulum of cells. Although it is predominantly expressed in the liver and kidneys, there is some evidence that CYP4F2 is expressed in human enteric microsomes [1, 2]. In the liver and kidneys, CYP4F2 catalyzes the synthesis of 20-hydroxyeicosatetraeonic acid (20-HETE) from AA. Hepatic CYP4F2 also regulates the bioavailability of vitamin K and vitamin E, catalyzes the inactivation of LTB4, and the bioactivation of the anti-malarial drug pafuramidine. Although initial studies of CYP4F2 were focused on its role as a regulator of LTB4 and 20-HETE, current investigations focus on how variants of CYP4F2 affect warfarin drug dosing and safety. A fully interactive version of this brief review can accessed at: http://www.pharmgkb.org/gene/PA27121.