FNTA

Farnesyltransferase, CAAX box, alpha

PDB rendering based on 1d8d.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsFNTA ; FPTA; PGGT1A; PTAR2
External IDsOMIM: 134635 MGI: 104683 HomoloGene: 1534 IUPHAR: 2825 ChEMBL: 271 GeneCards: FNTA Gene
EC number2.5.1.58, 2.5.1.59
Orthologs
SpeciesHumanMouse
Entrez233914272
EnsemblENSG00000168522ENSMUSG00000015994
UniProtP49354Q61239
RefSeq (mRNA)NM_001018676NM_008033
RefSeq (protein)NP_002018NP_032059
Location (UCSC)Chr 8:
43.03 – 43.09 Mb		Chr 8:
26 – 26.02 Mb
PubMed search

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha is an enzyme that in humans is encoded by the FNTA gene.[1][2]

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.[2]

Interactions

FNTA has been shown to interact with TGF beta receptor 1.[3]

References

  1. ↑ Andres DA, Milatovich A, Ozcelik T, Wenzlau JM, Brown MS, Goldstein JL, Francke U (February 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.
  2. ↑ 2.0 2.1 "Entrez Gene: FNTA farnesyltransferase, CAAX box, alpha".
  3. ↑ Kawabata, M; Imamura T; Miyazono K; Engel M E; Moses H L (December 1995). "Interaction of the transforming growth factor-beta type I receptor with farnesyl-protein transferase-alpha". J. Biol. Chem. (UNITED STATES) 270 (50): 29628–31. doi:10.1074/jbc.270.50.29628. ISSN 0021-9258. PMID 8530343.

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.
  • 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. doi:10.1073/pnas.87.19.7541. PMC 54783. PMID 2217184.
  • 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. doi:10.1074/jbc.270.14.7864. PMID 7713879.
  • 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.
  • 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.
  • 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.
  • 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. doi:10.1021/bi00070a028. PMID 8494894.
  • 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. doi:10.1074/jbc.270.50.29628. PMID 8530343.
  • 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. doi:10.1126/science.271.5252.1120. PMID 8599089.
  • 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.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Goalstone ML, Draznin B (1996). "Effect of insulin on farnesyltransferase activity in 3T3-L1 adipocytes.". J. Biol. Chem. 271 (44): 27585–9. doi:10.1074/jbc.271.44.27585. 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.
  • 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.
  • 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.
  • 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. PMC 125279. PMID 11598000.
  • 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. PMC 60805. PMID 11687658.
  • 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. doi:10.1021/jm010531d. PMID 12036349.
  • 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.