FNTB

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; OMA:FNTB - orthologs
Gene location (Mouse) Chr. Chromosome 12 (mouse) [1] Band 12 C3|12 33.73 cM Start 76,812,363 bp [1] End 76,968,186 bp [1]
RNA expression pattern Bgee Human Mouse (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 Species Human Mouse 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/a Chr 12: 76.81 – 76.97 Mb PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

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

References

1. 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 .