FNTA

FNTA
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1JCQ, 1LD7, 1LD8, 1MZC, 1S63, 1SA4, 1TN6, 2F0Y, 2H6F, 2H6G, 2H6H, 2H6I, 2IEJ, 3E37
Identifiers
Aliases	FNTA, FPTA, PGGT1A, PTAR2, farnesyltransferase, CAAX box, alpha
External IDs	OMIM: 134635; MGI: 104683; HomoloGene: 1534; GeneCards: FNTA; OMA:FNTA - orthologs
Gene location (Human)
Chr.	Chromosome 8 (human)
End	43,085,788 bp
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)
End	26,505,678 bp
RNA expression pattern
	Top expressed in
	gingival epithelium; ; olfactory bulb; ; subthalamic nucleus; ; inferior ganglion of vagus nerve; ; pancreatic ductal cell; ; amniotic fluid; ; parotid gland; ; skin of hip; ; germinal epithelium; ; trigeminal ganglion;
	Top expressed in
	medullary collecting duct; ; facial motor nucleus; ; fossa; ; Paneth cell; ; condyle; ; vestibular membrane of cochlear duct; ; renal corpuscle; ; substantia nigra; ; ciliary body; ; ureter;
	More reference expression data
	n/a
Gene ontology
Molecular function	transferase activity; protein prenyltransferase activity; protein geranylgeranyltransferase activity; microtubule binding; Rab geranylgeranyltransferase activity; receptor tyrosine kinase binding; alpha-tubulin binding; protein farnesyltransferase activity; acetylcholine receptor regulator activity; protein binding; prenyltransferase activity; CAAX-protein geranylgeranyltransferase activity;
Cellular component	cytoplasm; cytosol; protein farnesyltransferase complex; microtubule associated complex; CAAX-protein geranylgeranyltransferase complex; plasma membrane;
Biological process	positive regulation of tubulin deacetylation; protein prenylation; protein geranylgeranylation; neuromuscular junction development; skeletal muscle acetylcholine-gated channel clustering; positive regulation of deacetylase activity; protein farnesylation; transforming growth factor beta receptor signaling pathway; neurotransmitter receptor metabolic process; regulation of neurotransmitter receptor activity; regulation of rhodopsin mediated signaling pathway;
	Sources:Amigo / QuickGO
Orthologs
	2339
	14272
	ENSG00000168522
	ENSMUSG00000015994
	P49354
	Q61239
	NM_001018676; NM_001018677; NM_002027
	NM_008033
	NP_002018
	NP_032059
	Wikidata
View/Edit Human	View/Edit Mouse

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha is an enzyme that in humans is encoded by the FNTA gene.^[5]^[6]

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.^[6]

Interactions

FNTA has been shown to interact with TGF beta receptor 1.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000168522 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000015994 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ ^a ^b "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. 270 (50). UNITED STATES: 29628–31. doi:10.1074/jbc.270.50.29628. ISSN 0021-9258. PMID 8530343.

Adamson P, Marshall CJ, Hall A, Tilbrook PA (1992). "Post-translational modifications of p21rho proteins". J. Biol. Chem. 267 (28): 20033–8. doi:10.1016/S0021-9258(19)88661-1. 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. doi:10.1016/S0021-9258(17)41845-X. 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. doi:10.1242/jcs.107.1.61. 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. doi:10.1016/S0021-9258(18)54087-4. 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. S2CID 83164753.
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. doi:10.1002/jlb.60.3.423. PMID 8830800. S2CID 33727864.
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. Bibcode:2000Natur.403..567P. doi:10.1038/35000617. PMID 10676968. S2CID 4431592.
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. S2CID 4412580.

External links

Overview of all the structural information available in the PDB for UniProt: P49354 (Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha) at the PDBe-KB.

This article on a gene on human chromosome 8 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000168522 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000015994 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8276393-5] 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.

[entrez-6] "Entrez Gene: FNTA farnesyltransferase, CAAX box, alpha".

[pmid8530343-7] 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. 270 (50). UNITED STATES: 29628–31. doi:10.1074/jbc.270.50.29628. ISSN 0021-9258. PMID 8530343.

[1]

Interactions

References

Further reading

External links