FNTA

Farnesyltransferase, CAAX box, alpha
PDB rendering based on 1d8d.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1d8d​, 1d8e​, 1fpp​, 1ft1​, 1ft2​, 1jcq​, 1jcr​, 1jcs​, 1kzo​, 1kzp​, 1ld7​, 1ld8​, 1mzc​, 1n4p​, 1n4q​, 1n4r​, 1n4s​, 1n94​, 1n95​, 1n9a​, 1ni1​, 1nl4​, 1o1r​, 1o1s​, 1o1t​, 1o5m​, 1qbq​, 1s63​, 1s64​, 1sa4​, 1sa5​, 1tn6​, 1tn7​, 1tn8​, 1tnb​, 1tno​, 1tnu​, 1tny​, 1tnz​, 1x81​, 2bed​, 2f0y​, 2h6f​, 2h6g​, 2h6h​, 2h6i​, 2iej​
Identifiers
Symbols	FNTA ; FPTA; MGC99680; PGGT1A
External IDs	Template:OMIM5 Template:MGI HomoloGene: 1534
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Farnesyltransferase, CAAX box, alpha, also known as FNTA, is a human gene.

Prenyltransferases attach either a farnesyl group or a geranylgeranyl group in thioether linkage to the cysteine residue of protein's 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 encoding different isoforms.

Further reading

• Adamson P, Marshall CJ, Hall A, Tilbrook PA (1992). "Post-translational modifications of p21rho proteins". J. Biol. Chem. 267 (28): 20033–8. PMID 1400319.CS1 maint: Multiple names: authors list (link)
• Manne V, Roberts D, Tobin A; et al. (1990). "Identification and preliminary characterization of protein-cysteine farnesyltransferase". Proc. Natl. Acad. Sci. U.S.A. 87 (19): 7541–5. PMID 2217184.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Armstrong SA, Hannah VC, Goldstein JL, Brown MS (1995). "CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB". J. Biol. Chem. 270 (14): 7864–8. PMID 7713879.CS1 maint: Multiple names: authors list (link)
• Zhang FL, Diehl RE, Kohl NE; et al. (1994). "cDNA cloning and expression of rat and human protein geranylgeranyltransferase type-I". J. Biol. Chem. 269 (5): 3175–80. PMID 8106351.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Sinensky M, Fantle K, Trujillo M; et al. (1994). "The processing pathway of prelamin A.". J. Cell. Sci. 107 ( Pt 1): 61–7. PMID 8175923.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Andres DA, Milatovich A, Ozçelik T; et al. (1994). "cDNA cloning of the two subunits of human CAAX farnesyltransferase and chromosomal mapping of FNTA and FNTB loci and related sequences". Genomics. 18 (1): 105–12. doi:10.1006/geno.1993.1432. PMID 8276393.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Andres DA, Goldstein JL, Ho YK, Brown MS (1993). "Mutational analysis of alpha-subunit of protein farnesyltransferase. Evidence for a catalytic role". J. Biol. Chem. 268 (2): 1383–90. PMID 8419339.CS1 maint: Multiple names: authors list (link)
• Omer CA, Kral AM, Diehl RE; et al. (1993). "Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases". Biochemistry. 32 (19): 5167–76. PMID 8494894.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kawabata M, Imamura T, Miyazono K; et al. (1996). "Interaction of the transforming growth factor-beta type I receptor with farnesyl-protein transferase-alpha". J. Biol. Chem. 270 (50): 29628–31. PMID 8530343.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Wang T, Danielson PD, Li BY; et al. (1996). "The p21(RAS) farnesyltransferase alpha subunit in TGF-beta and activin signaling". Science. 271 (5252): 1120–2. PMID 8599089.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Nantais DE, Schwemmle M, Stickney JT; et al. (1996). "Prenylation of an interferon-gamma-induced GTP-binding protein: the human guanylate binding protein, huGBP1". J. Leukoc. Biol. 60 (3): 423–31. PMID 8830800.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. PMID 8889548.CS1 maint: Multiple names: authors list (link)
• Goalstone ML, Draznin B (1996). "Effect of insulin on farnesyltransferase activity in 3T3-L1 adipocytes". J. Biol. Chem. 271 (44): 27585–9. PMID 8910345.
• Prakash B, Praefcke GJ, Renault L; et al. (2000). "Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins". Nature. 403 (6769): 567–71. doi:10.1038/35000617. PMID 10676968.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Zeng Q, Si X, Horstmann H; et al. (2000). "Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome". J. Biol. Chem. 275 (28): 21444–52. doi:10.1074/jbc.M000453200. PMID 10747914.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ashar HR, James L, Gray K; et al. (2000). "Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules". J. Biol. Chem. 275 (39): 30451–7. doi:10.1074/jbc.M003469200. PMID 10852915.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Guenzi E, Töpolt K, Cornali E; et al. (2001). "The helical domain of GBP-1 mediates the inhibition of endothelial cell proliferation by inflammatory cytokines". EMBO J. 20 (20): 5568–77. doi:10.1093/emboj/20.20.5568. PMID 11598000.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Long SB, Hancock PJ, Kral AM; et al. (2001). "The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics". Proc. Natl. Acad. Sci. U.S.A. 98 (23): 12948–53. doi:10.1073/pnas.241407898. PMID 11687658.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bell IM, Gallicchio SN, Abrams M; et al. (2002). "3-Aminopyrrolidinone farnesyltransferase inhibitors: design of macrocyclic compounds with improved pharmacokinetics and excellent cell potency". J. Med. Chem. 45 (12): 2388–409. PMID 12036349.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Long SB, Casey PJ, Beese LS (2002). "Reaction path of protein farnesyltransferase at atomic resolution". Nature. 419 (6907): 645–50. doi:10.1038/nature00986. PMID 12374986.CS1 maint: Multiple names: authors list (link)