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CAAX box, alpha
CAAX farnesyltransferase subunit alpha
CAAX farnesyltransferase subunit beta
Farnesyltransferase, CAAX box, beta
Farnesyltransferase, subunit alpha
Protein farnesyltransferase subunit beta
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
RAS proteins prenyltransferase beta
Ras proteins prenyltransferase subunit alpha
type I protein geranyl-geranyltransferase subunit alpha
FNTA, also known as CAAX farnesyltransferase (FTase), attaches a farnesyl group from farnesyl pyrophosphate to cysteine residues at the fourth position from the C terminus of proteins that end in the so-called CAAX box, where C is cysteine, A is usually but not always an aliphatic amino acid, and X is typically methionine or serine. This type of posttranslational modification provides a mechanism for membrane localization of proteins that lack a transmembrane domain. This enzyme has the remarkable property of farnesylating peptides as short as four residues in length that conform to the CAAX consensus sequence.
FNTB, farnesyltransferase subunit beta, catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.
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