Update on allele nomenclature for human cytochromes P450 and the human cytochrome P450 allele (CYP-allele) nomenclature database

Abstract

Interindividual variability in xenobiotic metabolism and drug response is extensive and genetic factors play an important role in this variation. A majority of clinically used drugs are substrates for the cytochrome P450 (CYP) enzyme system and interindividual variability in expression and function of these enzymes is a major factor for explaining individual susceptibility for adverse drug reactions and drug response. Because of the existence of many polymorphic CYP genes, for many of which the number of allelic variants is continually increasing, a universal and of ficial nomenclature system is important. Since 1999, all functionally relevant polymorphic CYP alleles are named and published on the Human Cytochrome P450 Allele (CYPallele) Nomenclature Web site ( http://www.cypalleles.ki.se ). Currently, the database covers nomenclature of more than 660 alleles in a total of 30 genes that includes 29 CYPs as well as the cytochrome P450 oxidoreductase (POR) gene. On the CYP-allele Web site, each gene has its own Webpage, which lists the alleles with their nucleotide changes, their functional consequences, and links to publications identifying or characterizing the alleles. CYP2D6, CYP2C9, CYP2C19, and CYP3A4 are the most important CYPs in terms of drug metabolism, which is also re flected in their corresponding highest number of Webpage hits at the CYP-allele Web site. The main advantage of the CYP-allele database is that it offers a rapid online publication of CYPalleles and their effects and provides an overview of peer-reviewed data to the scienti fic community. Here, we provide an update of the CYP-allele database and the associated nomenclature. © Springer Science+Business Media New York 2013.