Top ▲ Protein farnesyltransferase C

Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).


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Farnesyltransferase is a member of the prenyltransferases family which also includes geranylgeranyltransferase types I (EC and II (EC [2]. Protein farnesyltransferase catalyses the post-translational formation of a thioether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of a protein (ie to the CaaX motif, where 'a' is an aliphatic amino acid and 'X' is usually serine, methionine, alanine or glutamine; leucine for EC [4]. Farnesyltransferase is a dimer, composed of an alpha and beta subunit and requires Mg2+ and Zn2+ ions as cofactors. The active site is located between the subunits. Prenylation creates a hydrophobic domain on protein tails which acts as a membrane anchor.

Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, G-protein γ-subunits, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction.

In relation to the causative association between oncogenic Ras proteins and cancer, farnesyltransferase has become an important mechanistic drug discovery target.


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Targets of relevance to immunopharmacology are highlighted in blue

FNTA (farnesyltransferase, CAAX box, subunit alpha) Show summary » More detailed page go icon to follow link

FNTB (farnesyltransferase, CAAX box, subunit beta) Show summary » More detailed page go icon to follow link

Further reading

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How to cite this family page

Database page citation: Protein farnesyltransferase. Accessed on 25/07/2024. IUPHAR/BPS Guide to PHARMACOLOGY,

Concise Guide to PHARMACOLOGY citation:

Alexander SPH, Fabbro D, Kelly E, Mathie AA, Peters JA, Veale EL, Armstrong JF, Faccenda E, Harding SD, Davies JA et al. (2023) The Concise Guide to PHARMACOLOGY 2023/24: Enzymes. Br J Pharmacol. 180 Suppl 2:S289-373.