EC - Protein-S-isoprenylcysteine O-methyltransferase

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IntEnz Enzyme Nomenclature


Accepted name:
protein-S-isoprenylcysteine O-methyltransferase
Other names:
S-farnesylcysteine methyltransferase
farnesyl cysteine C-terminal methyltransferase
farnesyl-protein carboxymethyltransferase
farnesylated protein C-terminal O-methyltransferase
isoprenylated protein methyltransferase
prenylated protein methyltransferase
prenylcysteine carboxylmethyltransferase [misleading]
prenylcysteine carboxymethyltransferase [misleading]
prenylcysteine methyltransferase
protein S-farnesylcysteine C-terminal methyltransferase
protein C-terminal farnesylcysteine O-methyltransferase
Systematic name:
S-adenosyl-L-methionine:protein-C-terminal-S-farnesyl-L-cysteine O-methyltransferase



C-terminal S-geranylgeranylcysteine and S-geranylcysteine residues are also methylated, but more slowly.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004671
CAS Registry Number: 130731-20-3
UniProtKB/Swiss-Prot: (11) [show] [UniProt]


  1. Clarke, S., Vogel, J.P., Deschenes, R.J. and Stock, J.
    Posttranslational modification of the Ha-ras oncogene protein: evidence for a third class of protein carboxyl methyltransferases.
    Proc. Natl. Acad. Sci. USA 85: 4643-4647 (1988). [PMID: 3290900]
  2. Ota, I.M. and Clarke, S.
    Enzymatic methylation of 23-29-kDa bovine retinal rod outer segment membrane proteins. Evidence for methyl ester formation at carboxyl-terminal cysteinyl residues.
    J. Biol. Chem. 264: 12879-12884 (1989). [PMID: 2753892]
  3. Stephenson, R.C. and Clarke, S.
    Identification of a C-terminal protein carboxyl methyltransferase in rat liver membranes utilizing a synthetic farnesyl cysteine-containing peptide substrate.
    J. Biol. Chem. 265: 16248-16254 (1990). [PMID: 2398053]

[EC created 1992 (EC created 1972, modified 1983, modified 1989, part incorporated 1992)]