pro-RAS proteins are farnesylated

Stable Identifier
Reaction [transition]
Homo sapiens
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RAS proteins are isoprenylated at a CaaX motif in the hypervariable region, where a is an aliphatic amino acid and X is any amino acid (Casey et al, 1989; Dharmaiah et al, 2016; reviewed in Ahean et al, 2018). Geranylgeranylation is favoured when X is leucine, while all other amino acids at this position favour farnesylation by farnesyltransferase (Casey et al, 1989; Reid et al, 2004).
Literature References
PubMed ID Title Journal Year
15451670 Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity

Casey, PJ, Reid, TS, Beese, LS, Terry, KL

J. Mol. Biol. 2004
2682646 p21ras is modified by a farnesyl isoprenoid

Der, CJ, Solski, PA, Casey, PJ, Buss, JE

Proc. Natl. Acad. Sci. U.S.A. 1989
27791178 Structural basis of recognition of farnesylated and methylated KRAS4b by PDE╬┤

Dharmaiah, S, Bindu, L, Ghirlando, R, Frank, PH, McCormick, F, Gillette, WK, Tran, TH, Stephen, AG, Nissley, DV, Esposito, D, Simanshu, DK

Proc. Natl. Acad. Sci. U.S.A. 2016
29311131 Posttranslational Modifications of RAS Proteins

Philips, MR, Zhou, M, Ahearn, I

Cold Spring Harb Perspect Med 2018
Catalyst Activity

protein farnesyltransferase activity of FNTA:FNTB [cytosol]

This event is regulated
Orthologous Events
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