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{{ | '''Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha''' is an [[enzyme]] that in humans is encoded by the ''FNTA'' [[gene]].<ref name="pmid8276393">{{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 | pmc = | doi = 10.1006/geno.1993.1432 }}</ref><ref name="entrez">{{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| accessdate = }}</ref> | ||
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| summary_text = 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.<ref name="entrez" | | summary_text = 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.<ref name="entrez"/> | ||
}} | }} | ||
==Interactions== | |||
FNTA has been shown to [[Protein-protein interaction|interact]] with [[TGF beta receptor 1]].<ref name=pmid8530343>{{cite journal |doi=10.1074/jbc.270.50.29628 |last=Kawabata |first=M |authorlink= |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 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 8530343 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> | |||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | | *{{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 |pmid= 1400319 |doi= }} | ||
*{{cite journal | | *{{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}} | ||
*{{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 }} | |||
*{{cite journal | | *{{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 |pmid= 8106351 |doi= |display-authors=etal}} | ||
*{{cite journal | | *{{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) |issue= |pages= 61–7 |year= 1994 |pmid= 8175923 |doi= |display-authors=etal}} | ||
*{{cite journal | | *{{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 |pmid= 8419339 |doi= }} | ||
*{{cite journal | | *{{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 | | *{{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}} | ||
*{{cite journal | | *{{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 }} | ||
*{{cite journal | | *{{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= |display-authors=etal}} | ||
*{{cite journal | | *{{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 }} | ||
*{{cite journal | | *{{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 }} | ||
*{{cite journal | | *{{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 |display-authors=etal}} | ||
*{{cite journal | | *{{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}} | ||
*{{cite journal | | *{{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}} | ||
*{{cite journal | | *{{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 | | *{{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 }} | ||
*{{cite journal | | *{{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 | | *{{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 }} | ||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=2339}} | |||
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Latest revision as of 08:41, 10 January 2019
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| External IDs | GeneCards: [1] | ||||||
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| Species | Human | Mouse | |||||
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| Location (UCSC) | n/a | n/a | |||||
| PubMed search | n/a | n/a | |||||
| Wikidata | |||||||
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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
- ↑ 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.
- ↑ 2.0 2.1 "Entrez Gene: FNTA farnesyltransferase, CAAX box, alpha".
- ↑ 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. Bibcode:1990PNAS...87.7541M. 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. Bibcode:1996Sci...271.1120W. 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. Bibcode:2001PNAS...9812948L. 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. Bibcode:2002Natur.419..645L. doi:10.1038/nature00986. PMID 12374986.
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