FNTB

FNTB
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesFNTB, FPTB, farnesyltransferase, CAAX box, beta
External IDsMGI: 1861305 HomoloGene: 1535 GeneCards: FNTB
Gene location (Human)
Chr.Chromosome 14 (human)[1]
Band14q23.3Start64,986,720 bp[1]
End65,062,652 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

2342

110606

Ensembl

ENSG00000257365

ENSMUSG00000033373

UniProt

P49356

Q8K2I1

RefSeq (mRNA)

NM_002028

NM_145927

RefSeq (protein)

NP_002019

NP_666039

Location (UCSC)Chr 14: 64.99 – 65.06 MbChr 12: 76.77 – 76.92 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000257365 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000033373 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  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. 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.


This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.