Aliases for FNTA Gene
- Farnesyltransferase, CAAX Box, Alpha 2 3
- Protein Prenyltransferase Alpha Subunit Repeat Containing 2 2 3
- Ras Proteins Prenyltransferase Subunit Alpha 3 4
- GGTase-I-Alpha 3 4
- FTase-Alpha 3 4
- Protein Farnesyltransferase/Geranylgeranyltransferase Type-1 Subunit Alpha 3
- Type I Protein Geranyl-Geranyltransferase Alpha Subunit 3
- Type I Protein Geranyl-Geranyltransferase Subunit Alpha 4
External Ids for FNTA Gene
Prenyltransferases can attach either a farnesyl group or a geranylgeranyl group in thioether linkage to the cysteine residue of proteins with a C-terminal CAAX box. CAAX geranylgeranyltransferase and CAAX farnesyltransferase are heterodimers that share the same alpha subunit but have different beta subunits. This gene encodes the alpha subunit of these transferases. Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 11 and 13. [provided by RefSeq, May 2010]
GeneCards Summary for FNTA Gene
FNTA (Farnesyltransferase, CAAX Box, Alpha) is a Protein Coding gene. Among its related pathways are Signaling by GPCR and Disease. GO annotations related to this gene include microtubule binding and protein farnesyltransferase activity. An important paralog of this gene is ENSG00000254673.
UniProtKB/Swiss-Prot for FNTA Gene
Essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. May positively regulate neuromuscular junction development downstream of MUSK via its function in RAC1 prenylation and activation.
Prenyltransferases are enzymes which transfer prenyl groups to acceptor molecules. The family contains farnesyltransferase (FT) and geranylgeranyltransferase 1 (GGT1), which attach a farnesyl group or a geranyl group respectively. This attachment permits membrane localization of proteins without a transmembrane domain, and occurs post-translationally. FTase and GGTase are heterodimeric enzymes, which both share an alpha-subunit and different beta-subunits. Both recognize a CAAX sequence present at the C-terminus of the target protein. Target proteins include Ras, which is suggestive of a role for prenylation in tumor development. Ras GTPases require farnesylation for malignant activity, and many of the downstream proteins it targets are also subject to farnesylation or geranylgeranylation in order to mediate the growth, survival and migration of tumor cells. Prenyltransferase inhibitors are therefore of interest in the development of cancer therapeutics. Farnesyltransferase inhibitors (FTIs) induce antitumor effects by inducing apoptosis and cell cycle arrest, and inhibiting cell proliferation, migration and angiogenesis. Geranylgeranyltransferase 1 inhibitors (GGTIs) also induce apoptosis and inhibit the growth of tumor cells.