FNTB

Protein-coding gene in the species Homo sapiens
FNTB
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1JCQ, 1LD7, 1LD8, 1MZC, 1S63, 1SA4, 1TN6, 2F0Y, 2H6F, 2H6G, 2H6H, 2H6I, 2IEJ, 3E37

Identifiers
AliasesFNTB, FPTB, farnesyltransferase, CAAX box, beta
External IDsOMIM: 134636; MGI: 1861305; HomoloGene: 1535; GeneCards: FNTB; OMA:FNTB - orthologs
Gene location (Mouse)
Chromosome 12 (mouse)
Chr.Chromosome 12 (mouse)[1]
Chromosome 12 (mouse)
Genomic location for FNTB
Genomic location for FNTB
Band12 C3|12 33.73 cMStart76,812,363 bp[1]
End76,968,186 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • corpus callosum

  • substantia nigra

  • gastrocnemius muscle

  • tibial nerve

  • skin of abdomen

  • right uterine tube

  • sural nerve

  • pituitary gland

  • hippocampus proper

  • vagina
Top expressed in
  • yolk sac

  • lip

  • genital tubercle

  • neural layer of retina

  • tail of embryo

  • muscle of thigh

  • esophagus

  • neural tube

  • cerebellar cortex

  • epiblast
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • metal ion binding
  • transferase activity
  • prenyltransferase activity
  • catalytic activity
  • protein farnesyltransferase activity
  • protein binding
  • farnesyltranstransferase activity
  • zinc ion binding
  • isoprenoid binding
  • peptide binding
Cellular component
  • cytosol
  • protein farnesyltransferase complex
  • microtubule associated complex
  • protein-containing complex
Biological process
  • protein farnesylation
  • positive regulation of cell population proliferation
  • negative regulation of cell population 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
SpeciesHumanMouse
Entrez

2342

110606

Ensembl

n/a

ENSMUSG00000033373

UniProt

P49356

Q8K2I1

RefSeq (mRNA)

NM_002028

NM_145927

RefSeq (protein)

NP_002019
NP_001189487
NP_001189488

NP_666039

Location (UCSC)n/aChr 12: 76.81 – 76.97 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Protein farnesyltransferase subunit beta is an enzyme that in humans is encoded by the FNTB gene.[4][5]

References

  1. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000033373 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ 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.
  5. ^ "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. Bibcode:1990PNAS...87.7541M. 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. doi:10.1242/jcs.107.1.61. 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. 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.
  • 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. 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.
  • 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. Bibcode:2002Natur.419..645L. doi:10.1038/nature00986. PMID 12374986. S2CID 4412580.
  • 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. Bibcode:2002PNAS...9916899M. 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.
  • v
  • t
  • e
  • 1d8d: CO-CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A K-RAS4B PEPTIDE SUBSTRATE AND FPP ANALOG AT 2.0A RESOLUTION
    1d8d: CO-CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A K-RAS4B PEPTIDE SUBSTRATE AND FPP ANALOG AT 2.0A RESOLUTION
  • 1d8e: Zinc-depleted FTase complexed with K-RAS4B peptide substrate and FPP analog.
    1d8e: Zinc-depleted FTase complexed with K-RAS4B peptide substrate and FPP analog.
  • 1fpp: PROTEIN FARNESYLTRANSFERASE COMPLEX WITH FARNESYL DIPHOSPHATE
    1fpp: PROTEIN FARNESYLTRANSFERASE COMPLEX WITH FARNESYL DIPHOSPHATE
  • 1ft1: CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE AT 2.25 ANGSTROMS RESOLUTION
    1ft1: CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE AT 2.25 ANGSTROMS RESOLUTION
  • 1ft2: CO-CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A FARNESYL DIPHOSPHATE SUBSTRATE
    1ft2: CO-CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A FARNESYL DIPHOSPHATE SUBSTRATE
  • 1jcq: CRYSTAL STRUCTURE OF HUMAN PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYL DIPHOSPHATE AND THE PEPTIDOMIMETIC INHIBITOR L-739,750
    1jcq: CRYSTAL STRUCTURE OF HUMAN PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYL DIPHOSPHATE AND THE PEPTIDOMIMETIC INHIBITOR L-739,750
  • 1jcr: CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH THE NON-SUBSTRATE TETRAPEPTIDE INHIBITOR CVFM AND FARNESYL DIPHOSPHATE SUBSTRATE
    1jcr: CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH THE NON-SUBSTRATE TETRAPEPTIDE INHIBITOR CVFM AND FARNESYL DIPHOSPHATE SUBSTRATE
  • 1jcs: CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH THE PEPTIDE SUBSTRATE TKCVFM AND AN ANALOG OF FARNESYL DIPHOSPHATE
    1jcs: CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH THE PEPTIDE SUBSTRATE TKCVFM AND AN ANALOG OF FARNESYL DIPHOSPHATE
  • 1kzo: PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYLATED K-RAS4B PEPTIDE PRODUCT AND FARNESYL DIPHOSPHATE SUBSTRATE BOUND SIMULTANEOUSLY
    1kzo: PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYLATED K-RAS4B PEPTIDE PRODUCT AND FARNESYL DIPHOSPHATE SUBSTRATE BOUND SIMULTANEOUSLY
  • 1kzp: PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A FARNESYLATED K-RAS4B PEPTIDE PRODUCT
    1kzp: PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A FARNESYLATED K-RAS4B PEPTIDE PRODUCT
  • 1ld7: Co-crystal structure of Human Farnesyltransferase with farnesyldiphosphate and inhibitor compound 66
    1ld7: Co-crystal structure of Human Farnesyltransferase with farnesyldiphosphate and inhibitor compound 66
  • 1ld8: Co-crystal structure of Human Farnesyltransferase with farnesyldiphosphate and inhibitor compound 49
    1ld8: Co-crystal structure of Human Farnesyltransferase with farnesyldiphosphate and inhibitor compound 49
  • 1mzc: Co-Crystal Structure Of Human Farnesyltransferase With Farnesyldiphosphate and Inhibitor Compound 33a
    1mzc: Co-Crystal Structure Of Human Farnesyltransferase With Farnesyldiphosphate and Inhibitor Compound 33a
  • 1n94: Aryl Tetrahydropyridine Inhbitors of Farnesyltransferase: Glycine, Phenylalanine and Histidine Derivates
    1n94: Aryl Tetrahydropyridine Inhbitors of Farnesyltransferase: Glycine, Phenylalanine and Histidine Derivates
  • 1n95: Aryl Tetrahydrophyridine Inhbitors of Farnesyltranferase: Glycine, Phenylalanine and Histidine Derivatives
    1n95: Aryl Tetrahydrophyridine Inhbitors of Farnesyltranferase: Glycine, Phenylalanine and Histidine Derivatives
  • 1n9a: Farnesyltransferase complex with tetrahydropyridine inhibitors
    1n9a: Farnesyltransferase complex with tetrahydropyridine inhibitors
  • 1ni1: Imidazole and cyanophenyl farnesyl transferase inhibitors
    1ni1: Imidazole and cyanophenyl farnesyl transferase inhibitors
  • 1nl4: Crystal Structure of Rat Farnesyl Transferase in Complex With A Potent Biphenyl Inhibitor
    1nl4: Crystal Structure of Rat Farnesyl Transferase in Complex With A Potent Biphenyl Inhibitor
  • 1o1r: Structure of FPT bound to GGPP
    1o1r: Structure of FPT bound to GGPP
  • 1o1s: Structure of FPT bound to isoprenoid analog 3b
    1o1s: Structure of FPT bound to isoprenoid analog 3b
  • 1o1t: Structure of FPT bound to the CVIM-FPP product
    1o1t: Structure of FPT bound to the CVIM-FPP product
  • 1o5m: Structure of FPT bound to the inhibitor SCH66336
    1o5m: Structure of FPT bound to the inhibitor SCH66336
  • 1qbq: STRUCTURE OF RAT FARNESYL PROTEIN TRANSFERASE COMPLEXED WITH A CVIM PEPTIDE AND ALPHA-HYDROXYFARNESYLPHOSPHONIC ACID.
    1qbq: STRUCTURE OF RAT FARNESYL PROTEIN TRANSFERASE COMPLEXED WITH A CVIM PEPTIDE AND ALPHA-HYDROXYFARNESYLPHOSPHONIC ACID.
  • 1s63: Human protein farnesyltransferase complexed with L-778,123 and FPP
    1s63: Human protein farnesyltransferase complexed with L-778,123 and FPP
  • 1sa4: human protein farnesyltransferase complexed with FPP and R115777
    1sa4: human protein farnesyltransferase complexed with FPP and R115777
  • 1sa5: Rat protein farnesyltransferase complexed with FPP and BMS-214662
    1sa5: Rat protein farnesyltransferase complexed with FPP and BMS-214662
  • 1tn6: Protein Farnesyltransferase Complexed with a Rap2a Peptide Substrate and a FPP Analog at 1.8A Resolution
    1tn6: Protein Farnesyltransferase Complexed with a Rap2a Peptide Substrate and a FPP Analog at 1.8A Resolution
  • 1tn7: Protein Farnesyltransferase Complexed with a TC21 Peptide Substrate and a FPP Analog at 2.3A Resolution
    1tn7: Protein Farnesyltransferase Complexed with a TC21 Peptide Substrate and a FPP Analog at 2.3A Resolution
  • 1tn8: Protein Farnesyltransferase Complexed with a H-Ras Peptide Substrate and a FPP Analog at 2.25A Resolution
    1tn8: Protein Farnesyltransferase Complexed with a H-Ras Peptide Substrate and a FPP Analog at 2.25A Resolution
  • 1x81: Farnesyl transferase structure of Jansen compound
    1x81: Farnesyl transferase structure of Jansen compound
  • 2bed: Structure of FPT bound to inhibitor SCH207736
    2bed: Structure of FPT bound to inhibitor SCH207736
  • 2f0y: Crystal Structure Of Human Protein Farnesyltransferase Complexed With Farnesyl Diphosphate and hydantoin derivative
    2f0y: Crystal Structure Of Human Protein Farnesyltransferase Complexed With Farnesyl Diphosphate and hydantoin derivative
  • 2h6f: Protein Farnesyltransferase Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.5A Resolution
    2h6f: Protein Farnesyltransferase Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.5A Resolution
  • 2h6g: W102T Protein Farnesyltransferase Mutant Complexed with a Geranylgeranylated DDPTASACVLS Peptide Product at 1.85A Resolution
    2h6g: W102T Protein Farnesyltransferase Mutant Complexed with a Geranylgeranylated DDPTASACVLS Peptide Product at 1.85A Resolution
  • 2h6h: Y365F Protein Farnesyltransferase Mutant Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.8A
    2h6h: Y365F Protein Farnesyltransferase Mutant Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.8A
  • 2h6i: W102T/Y365F Protein Farnesyltransferase Double Mutant Complexed with a Geranylgeranylated DDPTASACVLS Peptide Product at 3.0A
    2h6i: W102T/Y365F Protein Farnesyltransferase Double Mutant Complexed with a Geranylgeranylated DDPTASACVLS Peptide Product at 3.0A
  • 2iej: Human Protein Farnesyltransferase Complexed with Inhibitor Compound STN-48 And FPP Analog at 1.8A Resolution
    2iej: Human Protein Farnesyltransferase Complexed with Inhibitor Compound STN-48 And FPP Analog at 1.8A Resolution
Stub icon

This article on a gene on human chromosome 14 is a stub. You can help Wikipedia by expanding it.

  • v
  • t
  • e