FNTB

Protein farnesyltransferase subunit beta is an enzyme that in humans is encoded by the FNTB gene.[5][6]

FNTB
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	FNTB, FPTB, farnesyltransferase, CAAX box, beta
External IDs	OMIM: 134636 MGI: 1861305 HomoloGene: 1535 GeneCards: FNTB
Gene location (Human) Chr. Chromosome 14 (human)[1] Band 14q23.3 Start 64,986,895 bp[1] End 65,062,652 bp[1]
Gene location (Mouse) Chr. Chromosome 12 (mouse)[2] Band 12 C3|12 33.73 cM Start 76,765,589 bp[2] End 76,921,412 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • metal ion binding • transferase activity • prenyltransferase activity • catalytic activity • protein farnesyltransferase activity • GO:0001948 protein binding • farnesyltranstransferase activity • drug binding • zinc ion binding • isoprenoid binding • peptide binding Cellular component • cytosol • protein farnesyltransferase complex • microtubule associated complex • macromolecular complex Biological process • protein farnesylation • positive regulation of cell proliferation • negative regulation of cell proliferation • response to inorganic substance • response to organic cyclic compound • response to cytokine • wound healing • positive regulation of cell cycle • positive regulation of fibroblast proliferation • positive regulation of nitric-oxide synthase biosynthetic process • protein prenylation • regulation of fibroblast proliferation • regulation of rhodopsin mediated signaling pathway Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	2342	110606
Ensembl	ENSG00000257365	ENSMUSG00000033373
UniProt	P49356	Q8K2I1
RefSeq (mRNA)	NM_002028	NM_145927
RefSeq (protein)	NP_002019 NP_001189487 NP_001189488	NP_666039
Location (UCSC)	Chr 14: 64.99 – 65.06 Mb	Chr 12: 76.77 – 76.92 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

References

1. GRCh38: Ensembl release 89: ENSG00000257365 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000033373 - 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.
5. Andres DA, Milatovich A, Ozcelik T, Wenzlau JM, Brown MS, Goldstein JL, Francke U (Feb 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.
6. "Entrez Gene: FNTB farnesyltransferase, CAAX box, beta".

Further reading

• 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.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Sinensky M, Fantle K, Trujillo M, et al. (1994). "The processing pathway of prelamin A". J. Cell Sci. 107 (1): 61–7. PMID 8175923.
• 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.
• 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. doi:10.1002/jlb.60.3.423. PMID 8830800.
• 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.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Long SB, Casey PJ, Beese LS (1998). "Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate". Biochemistry. 37 (27): 9612–8. doi:10.1021/bi980708e. PMID 9657673.
• 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.
• Lobell RB, Omer CA, Abrams MT, et al. (2002). "Evaluation of farnesyl:protein transferase and geranylgeranyl:protein transferase inhibitor combinations in preclinical models". Cancer Res. 61 (24): 8758–68. PMID 11751396.
• 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.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• deSolms SJ, Ciccarone TM, MacTough SC, et al. (2003). "Dual protein farnesyltransferase-geranylgeranyltransferase-I inhibitors as potential cancer chemotherapeutic agents". J. Med. Chem. 46 (14): 2973–84. doi:10.1021/jm020587n. PMID 12825937.

External links

• Overview of all the structural information available in the PDB for UniProt: P49356 (Protein farnesyltransferase subunit beta) at the PDBe-KB.