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FNTA

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{{Short description|Protein-coding gene in the species Homo sapiens}}

{{for|the French trade union|National Federation of Agricultural Workers (France)}}

{{for|the ward in Cuba|Federación Nacional de Trabajadores Azucareros, Cuba}}

{{Infobox_gene}}

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha is an enzyme that in humans is encoded by the FNTA gene.{{cite journal |vauthors=Andres DA, Milatovich A, Ozcelik T, Wenzlau JM, Brown MS, Goldstein JL, Francke U | title = cDNA cloning of the two subunits of human CAAX farnesyltransferase and chromosomal mapping of FNTA and FNTB loci and related sequences | journal = Genomics | volume = 18 | issue = 1 | pages = 105–12 |date=February 1994 | pmid = 8276393 | doi = 10.1006/geno.1993.1432 | doi-access = free }}{{cite web | title = Entrez Gene: FNTA farnesyltransferase, CAAX box, alpha| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2339}}

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.

Interactions

FNTA has been shown to interact with TGF beta receptor 1.{{cite journal |doi=10.1074/jbc.270.50.29628 |last=Kawabata |first=M |author2=Imamura T |author3=Miyazono K |author4=Engel M E |author5=Moses H L |date=December 1995 |title=Interaction of the transforming growth factor-beta type I receptor with farnesyl-protein transferase-alpha |journal=J. Biol. Chem. |volume=270 |issue=50 |pages=29628–31 |location = UNITED STATES| issn = 0021-9258| pmid = 8530343 |doi-access=free }}

References

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Further reading

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  • {{cite journal |vauthors=Adamson P, Marshall CJ, Hall A, Tilbrook PA |title=Post-translational modifications of p21rho proteins. |journal=J. Biol. Chem. |volume=267 |issue= 28 |pages= 20033–8 |year= 1992 |doi=10.1016/S0021-9258(19)88661-1 |pmid= 1400319 |doi-access=free }}
  • {{cite journal |vauthors=Manne V, Roberts D, Tobin A |title=Identification and preliminary characterization of protein-cysteine farnesyltransferase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 19 |pages= 7541–5 |year= 1990 |pmid= 2217184 |doi=10.1073/pnas.87.19.7541 | pmc=54783 |display-authors=etal|bibcode=1990PNAS...87.7541M|doi-access=free }}
  • {{cite journal |vauthors=Armstrong SA, Hannah VC, Goldstein JL, Brown MS |title=CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB. |journal=J. Biol. Chem. |volume=270 |issue= 14 |pages= 7864–8 |year= 1995 |pmid= 7713879 |doi=10.1074/jbc.270.14.7864 |doi-access=free }}
  • {{cite journal |vauthors=Zhang FL, Diehl RE, Kohl NE |title=cDNA cloning and expression of rat and human protein geranylgeranyltransferase type-I. |journal=J. Biol. Chem. |volume=269 |issue= 5 |pages= 3175–80 |year= 1994 |doi=10.1016/S0021-9258(17)41845-X |pmid= 8106351 |display-authors=etal|doi-access=free }}
  • {{cite journal |vauthors=Sinensky M, Fantle K, Trujillo M |title=The processing pathway of prelamin A. | series=107 |journal=J. Cell Sci. |volume=( Pt 1) |pages= 61–7 |year= 1994 |doi=10.1242/jcs.107.1.61 |pmid= 8175923 |url=https://scholarworks.sjsu.edu/biol_pub/15 |display-authors=etal|url-access=subscription }}
  • {{cite journal |vauthors=Andres DA, Goldstein JL, Ho YK, Brown MS |title=Mutational analysis of alpha-subunit of protein farnesyltransferase. Evidence for a catalytic role. |journal=J. Biol. Chem. |volume=268 |issue= 2 |pages= 1383–90 |year= 1993 |doi=10.1016/S0021-9258(18)54087-4 |pmid= 8419339 |doi-access=free }}
  • {{cite journal |vauthors=Omer CA, Kral AM, Diehl RE |title=Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases. |journal=Biochemistry |volume=32 |issue= 19 |pages= 5167–76 |year= 1993 |pmid= 8494894 |doi=10.1021/bi00070a028 |display-authors=etal}}
  • {{cite journal |vauthors=Kawabata M, Imamura T, Miyazono K |title=Interaction of the transforming growth factor-beta type I receptor with farnesyl-protein transferase-alpha. |journal=J. Biol. Chem. |volume=270 |issue= 50 |pages= 29628–31 |year= 1996 |pmid= 8530343 |doi=10.1074/jbc.270.50.29628 |display-authors=etal|doi-access=free }}
  • {{cite journal |vauthors=Wang T, Danielson PD, Li BY |title=The p21(RAS) farnesyltransferase alpha subunit in TGF-beta and activin signaling. |journal=Science |volume=271 |issue= 5252 |pages= 1120–2 |year= 1996 |pmid= 8599089 |doi=10.1126/science.271.5252.1120 |display-authors=etal|bibcode=1996Sci...271.1120W |s2cid=83164753 }}
  • {{cite journal |vauthors=Nantais DE, Schwemmle M, Stickney JT |title=Prenylation of an interferon-gamma-induced GTP-binding protein: the human guanylate binding protein, huGBP1. |journal=J. Leukoc. Biol. |volume=60 |issue= 3 |pages= 423–31 |year= 1996 |pmid= 8830800 |doi= 10.1002/jlb.60.3.423|s2cid=33727864 |display-authors=etal}}
  • {{cite journal |vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 |doi-access=free }}
  • {{cite journal |vauthors=Goalstone ML, Draznin B |title=Effect of insulin on farnesyltransferase activity in 3T3-L1 adipocytes. |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27585–9 |year= 1996 |pmid= 8910345 |doi=10.1074/jbc.271.44.27585 |doi-access=free }}
  • {{cite journal |vauthors=Prakash B, Praefcke GJ, Renault L |title=Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. |journal=Nature |volume=403 |issue= 6769 |pages= 567–71 |year= 2000 |pmid= 10676968 |doi= 10.1038/35000617 |bibcode=2000Natur.403..567P |s2cid=4431592 |display-authors=etal}}
  • {{cite journal |vauthors=Zeng Q, Si X, Horstmann H |title=Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome. |journal=J. Biol. Chem. |volume=275 |issue= 28 |pages= 21444–52 |year= 2000 |pmid= 10747914 |doi= 10.1074/jbc.M000453200 |display-authors=etal|doi-access= free}}
  • {{cite journal |vauthors=Ashar HR, James L, Gray K |title=Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules. |journal=J. Biol. Chem. |volume=275 |issue= 39 |pages= 30451–7 |year= 2000 |pmid= 10852915 |doi= 10.1074/jbc.M003469200 |display-authors=etal|doi-access=free }}
  • {{cite journal |vauthors=Guenzi E, Töpolt K, Cornali E |title=The helical domain of GBP-1 mediates the inhibition of endothelial cell proliferation by inflammatory cytokines. |journal=EMBO J. |volume=20 |issue= 20 |pages= 5568–77 |year= 2001 |pmid= 11598000 |doi= 10.1093/emboj/20.20.5568 | pmc=125279 |display-authors=etal}}
  • {{cite journal |vauthors=Long SB, Hancock PJ, Kral AM |title=The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 23 |pages= 12948–53 |year= 2001 |pmid= 11687658 |doi= 10.1073/pnas.241407898 | pmc=60805 |display-authors=etal|bibcode=2001PNAS...9812948L |doi-access=free }}
  • {{cite journal |vauthors=Bell IM, Gallicchio SN, Abrams M |title=3-Aminopyrrolidinone farnesyltransferase inhibitors: design of macrocyclic compounds with improved pharmacokinetics and excellent cell potency. |journal=J. Med. Chem. |volume=45 |issue= 12 |pages= 2388–409 |year= 2002 |pmid= 12036349 |doi=10.1021/jm010531d |display-authors=etal}}
  • {{cite journal |vauthors=Long SB, Casey PJ, Beese LS |title=Reaction path of protein farnesyltransferase at atomic resolution. |journal=Nature |volume=419 |issue= 6907 |pages= 645–50 |year= 2002 |pmid= 12374986 |doi= 10.1038/nature00986 |bibcode=2002Natur.419..645L |s2cid=4412580 }}

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External links

  • {{PDBe-KB2|P49354|Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha}}

{{PDB Gallery|geneid=2339}}

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