Protein farnesyltransferase subunit beta

Details

Name
Protein farnesyltransferase subunit beta
Synonyms
  • 2.5.1.58
  • CAAX farnesyltransferase subunit beta
  • FTase-beta
  • Ras proteins prenyltransferase subunit beta
Gene Name
FNTB
Organism
Humans
Amino acid sequence
>lcl|BSEQ0004659|Protein farnesyltransferase subunit beta
MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFS
SYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQ
IVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREKLLQY
LYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIG
GVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCY
SFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDF
YHTCYCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPV
PGFEELKDETSAEPATD
Number of residues
437
Molecular Weight
48773.2
Theoretical pI
5.67
GO Classification
Functions
drug binding / farnesyltranstransferase activity / isoprenoid binding / peptide binding / protein farnesyltransferase activity / zinc ion binding
Processes
negative regulation of cell proliferation / phototransduction, visible light / positive regulation of cell cycle / positive regulation of fibroblast proliferation / positive regulation of nitric-oxide synthase biosynthetic process / protein farnesylation / regulation of rhodopsin mediated signaling pathway / response to cytokine / response to inorganic substance / response to organic cyclic compound / rhodopsin mediated signaling pathway / wound healing
Components
cytosol / microtubule associated complex / protein farnesyltransferase complex
General Function
Zinc ion binding
Specific Function
Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0016768|Protein farnesyltransferase subunit beta (FNTB)
ATGATCGCAAAAGTAGAAGAAAAGATCCAAGAGGTCTTCAGTTCTTACAAGTTCAACCAC
CTTGTACCAAGGCTTGTTTTGCAGAGGGAGAAGCACTTCCATTATCTGAAAAGAGGCCTT
CGACAACTGACAGATGCCTATGAGTGTCTGGATGCCAGCCGCCCATGGCTCTGCTATTGG
ATCCTGCACAGCTTGGAACTGCTAGATGAACCCATCCCCCAGATAGTGGCTACAGATGTG
TGTCAGTTCCTGGAGCTGTGTCAGAGCCCAGAAGGTGGCTTTGGAGGAGGACCCGGTCAG
TATCCACACCTTGCACCCACATATGCAGCAGTCAATGCATTGTGCATCATTGGCACCGAG
GAGGCCTATGACATCATTAACAGAGAGAAGCTTCTTCAGTATTTGTACTCCCTGAAGCAA
CCTGACGGCTCCTTTCTCATGCATGTCGGAGGTGAGGTGGATGTGAGAAGCGCATACTGT
GCTGCCTCCGTAGCCTCGCTGACCAACATCATCACTCCAGACCTCTTTGAGGGCACTGCT
GAATGGATAGCAAGGTGTCAGAACTGGGAAGGTGGCATTGGCGGGGTACCAGGGATGGAA
GCCCATGGTGGCTATACCTTCTGTGGCCTGGCCGCGCTGGTAATCCTCAAGAGGGAACGT
TCCTTGAACTTGAAGAGCTTATTACAATGGGTGACAAGCCGGCAGATGCGATTTGAAGGA
GGATTTCAGGGCCGCTGCAACAAGCTGGTGGATGGCTGCTACTCCTTCTGGCAGGCGGGG
CTCCTGCCCCTGCTCCACCGCGCACTGCACGCCCAAGGTGACCCTGCCCTTAGCATGAGC
CACTGGATGTTCCATCAGCAGGCCCTGCAGGAGTACATCCTGATGTGCTGCCAGTGCCCT
GCGGGGGGGCTTCTGGATAAACCTGGCAAGTCGCGTGATTTCTACCACACCTGCTACTGC
CTGAGCGGCCTGTCCATAGCCCAGCACTTCGGCAGCGGAGCCATGTTGCATGATGTGGTC
CTGGGTGTGCCCGAAAACGCTCTGCAGCCCACTCACCCAGTGTACAACATTGGACCAGAC
AAGGTGATCCAGGCCACTACATACTTTCTACAGAAGCCAGTCCCAGGTTTTGAGGAGCTT
AAGGATGAGACATCGGCAGAGCCTGCAACCGACTAG
Chromosome Location
14
Locus
14q23-q24
External Identifiers
ResourceLink
UniProtKB IDP49356
UniProtKB Entry NameFNTB_HUMAN
GenBank Gene IDL00635
GenAtlas IDFNTB
HGNC IDHGNC:3785
General References
  1. Omer CA, Kral AM, Diehl RE, Prendergast GC, Powers S, Allen CM, Gibbs JB, Kohl NE: Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases. Biochemistry. 1993 May 18;32(19):5167-76. [Article]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
  3. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [Article]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  5. Andres DA, Milatovich A, Ozcelik T, Wenzlau JM, Brown MS, Goldstein JL, Francke U: cDNA cloning of the two subunits of human CAAX farnesyltransferase and chromosomal mapping of FNTA and FNTB loci and related sequences. Genomics. 1993 Oct;18(1):105-12. [Article]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [Article]
  7. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  8. Long SB, Hancock PJ, Kral AM, Hellinga HW, Beese LS: 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. 2001 Nov 6;98(23):12948-53. Epub 2001 Oct 30. [Article]
  9. Bell IM, Gallicchio SN, Abrams M, Beese LS, Beshore DC, Bhimnathwala H, Bogusky MJ, Buser CA, Culberson JC, Davide J, Ellis-Hutchings M, Fernandes C, Gibbs JB, Graham SL, Hamilton KA, Hartman GD, Heimbrook DC, Homnick CF, Huber HE, Huff JR, Kassahun K, Koblan KS, Kohl NE, Lobell RB, Lynch JJ Jr, Robinson R, Rodrigues AD, Taylor JS, Walsh ES, Williams TM, Zartman CB: 3-Aminopyrrolidinone farnesyltransferase inhibitors: design of macrocyclic compounds with improved pharmacokinetics and excellent cell potency. J Med Chem. 2002 Jun 6;45(12):2388-409. [Article]
  10. deSolms SJ, Ciccarone TM, MacTough SC, Shaw AW, Buser CA, Ellis-Hutchings M, Fernandes C, Hamilton KA, Huber HE, Kohl NE, Lobell RB, Robinson RG, Tsou NN, Walsh ES, Graham SL, Beese LS, Taylor JS: Dual protein farnesyltransferase-geranylgeranyltransferase-I inhibitors as potential cancer chemotherapeutic agents. J Med Chem. 2003 Jul 3;46(14):2973-84. [Article]
  11. Reid TS, Terry KL, Casey PJ, Beese LS: Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity. J Mol Biol. 2004 Oct 15;343(2):417-33. [Article]
  12. Terry KL, Casey PJ, Beese LS: Conversion of protein farnesyltransferase to a geranylgeranyltransferase. Biochemistry. 2006 Aug 15;45(32):9746-55. [Article]
  13. Hast MA, Fletcher S, Cummings CG, Pusateri EE, Blaskovich MA, Rivas K, Gelb MH, Van Voorhis WC, Sebti SM, Hamilton AD, Beese LS: Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase. Chem Biol. 2009 Feb 27;16(2):181-92. doi: 10.1016/j.chembiol.2009.01.014. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04893AZD3409investigationalunknownDetails
DB04960TipifarnibinvestigationalunknownDetails
DB069532-CHLORO-5-(3-CHLORO-PHENYL)-6-[(4-CYANO-PHENYL)-(3-METHYL-3H-IMIDAZOL-4-YL)- METHOXYMETHYL]-NICOTINONITRILEexperimentalunknownDetails
DB07216(11S)-8-CHLORO-11-[1-(METHYLSULFONYL)PIPERIDIN-4-YL]-6-PIPERAZIN-1-YL-11H-BENZO[5,6]CYCLOHEPTA[1,2-B]PYRIDINEexperimentalunknownDetails
DB07227L-778123experimentalunknownDetails
DB07771[(3,7,11-TRIMETHYL-DODECA-2,6,10-TRIENYLOXYCARBAMOYL)-METHYL]-PHOSPHONIC ACIDexperimentalunknownDetails
DB07780Farnesyl diphosphateexperimentalunknownDetails
DB07841Geranylgeranyl diphosphateexperimentalunknownDetails
DB07895ALPHA-HYDROXYFARNESYLPHOSPHONIC ACIDexperimentalunknownDetails
DB08674(20S)-19,20,21,22-TETRAHYDRO-19-OXO-5H-18,20-ETHANO-12,14-ETHENO-6,10-METHENO-18H-BENZ[D]IMIDAZO[4,3-K][1,6,9,12]OXATRIAZA-CYCLOOCTADECOSINE-9-CARBONITRILEexperimentalunknownDetails
DB08676(20S)-19,20,22,23-TETRAHYDRO-19-OXO-5H,21H-18,20-ETHANO-12,14-ETHENO-6,10-METHENOBENZ[D]IMIDAZO[4,3-L][1,6,9,13]OXATRIAZACYCLONOADECOSINE-9-CARBONITRILEexperimentalunknownDetails
DB06448Lonafarnibapproved, investigationalyesinhibitorDetails