ID FPPS_HUMAN Reviewed; 419 AA. AC P14324; D3DV91; E9PCI9; Q96G29; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 4. DT 11-NOV-2015, entry version 179. DE RecName: Full=Farnesyl pyrophosphate synthase; DE Short=FPP synthase; DE Short=FPS; DE EC=2.5.1.10; DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase; DE AltName: Full=Dimethylallyltranstransferase; DE EC=2.5.1.1; DE AltName: Full=Farnesyl diphosphate synthase; DE AltName: Full=Geranyltranstransferase; GN Name=FDPS; Synonyms=FPS, KIAA1293; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=1968462; RA Wilkin D.J., Kutsunai S.Y., Edwards P.A.; RT "Isolation and sequence of the human farnesyl pyrophosphate synthetase RT cDNA. Coordinate regulation of the mRNAs for farnesyl pyrophosphate RT synthetase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, and 3- RT hydroxy-3-methylglutaryl coenzyme A synthase by phorbol ester."; RL J. Biol. Chem. 265:4607-4614(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=7584026; DOI=10.1093/dnares/1.1.27; RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., RA Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. I. RT The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by RT analysis of randomly sampled cDNA clones from human immature myeloid RT cell line KG-1."; RL DNA Res. 1:27-35(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-312 (ISOFORM 2). RG The MGC Project Team; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 74-419. RC TISSUE=Liver; RX PubMed=2690933; DOI=10.1021/bi00446a025; RA Sheares B.T., White S.S., Molowa D.T., Chan K., Ding V.D.-H., RA Kroon P.A., Bostedor R.G., Karkas J.D.; RT "Cloning, analysis, and bacterial expression of human farnesyl RT pyrophosphate synthetase and its regulation in Hep G2 cells."; RL Biochemistry 28:8129-8135(1989). RN [9] RP INTERACTION WITH HTLV-1 P13(II). RX PubMed=11773414; DOI=10.1128/JVI.76.3.1400-1414.2002; RA Lefebvre L., Vanderplasschen A., Ciminale V., Heremans H., RA Dangoisse O., Jauniaux J.-C., Toussaint J.-F., Zelnik V., Burny A., RA Kettmann R., Willems L.; RT "Oncoviral bovine leukemia virus G4 and human T-cell leukemia virus RT type 1 p13(II) accessory proteins interact with farnesyl pyrophosphate RT synthetase."; RL J. Virol. 76:1400-1414(2002). RN [10] RP INTERACTION WITH RSAD2, AND ENZYME REGULATION. RX PubMed=18005724; DOI=10.1016/j.chom.2007.06.009; RA Wang X., Hinson E.R., Cresswell P.; RT "The interferon-inducible protein viperin inhibits influenza virus RT release by perturbing lipid rafts."; RL Cell Host Microbe 2:96-105(2007). RN [11] RP REVIEW. RX PubMed=15827605; RA Szkopinska A., Plochocka D.; RT "Farnesyl diphosphate synthase; regulation of product specificity."; RL Acta Biochim. Pol. 52:45-55(2005). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123 AND LYS-353, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [19] RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 72-419, AND SUBUNIT. RX PubMed=16892359; DOI=10.1002/cmdc.200500059; RA Rondeau J.-M., Bitsch F., Bourgier E., Geiser M., Hemmig R., RA Kroemer M., Lehmann S., Ramage P., Rieffel S., Strauss A., Green J.R., RA Jahnke W.; RT "Structural basis for the exceptional in vivo efficacy of RT bisphosphonate drugs."; RL ChemMedChem 1:267-273(2006). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 67-419 IN COMPLEXES WITH RP MAGNESIUM IONS; RISEDRONATE AND ZOLEDRONATE, AND CATALYTIC ACTIVITY. RX PubMed=16684881; DOI=10.1073/pnas.0601643103; RA Kavanagh K.L., Guo K., Dunford J.E., Wu X., Knapp S., Ebetino F.H., RA Rogers M.J., Russell R.G., Oppermann U.; RT "The molecular mechanism of nitrogen-containing bisphosphonates as RT antiosteoporosis drugs."; RL Proc. Natl. Acad. Sci. U.S.A. 103:7829-7834(2006). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 67-419 IN COMPLEXES WITH RP MAGNESIUM AND BIPHOSPHONATES. RX PubMed=19309137; DOI=10.1021/ja808285e; RA Zhang Y., Cao R., Yin F., Hudock M.P., Guo R.-T., Krysiak K., RA Mukherjee S., Gao Y.-G., Robinson H., Song Y., No J.H., Bergan K., RA Leon A., Cass L., Goddard A., Chang T.-K., Lin F.-Y., Van Beek E., RA Papapoulos S., Wang A.H.-J., Kubo T., Ochi M., Mukkamala D., RA Oldfield E.; RT "Lipophilic bisphosphonates as dual farnesyl/geranylgeranyl RT diphosphate synthase inhibitors: an X-ray and NMR investigation."; RL J. Am. Chem. Soc. 131:5153-5162(2009). CC -!- FUNCTION: Key enzyme in isoprenoid biosynthesis which catalyzes CC the formation of farnesyl diphosphate (FPP), a precursor for CC several classes of essential metabolites including sterols, CC dolichols, carotenoids, and ubiquinones. FPP also serves as CC substrate for protein farnesylation and geranylgeranylation. CC Catalyzes the sequential condensation of isopentenyl pyrophosphate CC with the allylic pyrophosphates, dimethylallyl pyrophosphate, and CC then with the resultant geranylpyrophosphate to the ultimate CC product farnesyl pyrophosphate. CC -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl CC diphosphate = diphosphate + geranyl diphosphate. CC {ECO:0000269|PubMed:16684881}. CC -!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate CC = diphosphate + (2E,6E)-farnesyl diphosphate. CC {ECO:0000269|PubMed:16684881}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 3 Mg(2+) ions per subunit.; CC -!- ENZYME REGULATION: Inactivated by interferon-induced RSAD2. This CC inactivation may result of disruption of lipid rafts at the plasma CC membrane, and thus have an antiviral effect since many enveloped CC viruses need lipid rafts to bud efficiently out of the cell. CC {ECO:0000269|PubMed:18005724}. CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate CC biosynthesis; farnesyl diphosphate from geranyl diphosphate and CC isopentenyl diphosphate: step 1/1. CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate CC biosynthesis; geranyl diphosphate from dimethylallyl diphosphate CC and isopentenyl diphosphate: step 1/1. CC -!- SUBUNIT: Homodimer. Interacts with RSAD2. Interacts with HTLV-1 CC protein p13(II). {ECO:0000269|PubMed:11773414, CC ECO:0000269|PubMed:16892359, ECO:0000269|PubMed:18005724}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P14324-1; Sequence=Displayed; CC Name=2; CC IsoId=P14324-2; Sequence=VSP_046958; CC Note=Contains a N-acetylmethionine at position 1. CC {ECO:0000244|PubMed:19413330, ECO:0000244|PubMed:22223895, CC ECO:0000244|PubMed:22814378}; CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA03523.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J05262; AAA52423.1; -; mRNA. DR EMBL; D14697; BAA03523.2; ALT_INIT; mRNA. DR EMBL; AK291084; BAF83773.1; -; mRNA. DR EMBL; AL139410; CAI12715.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53076.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53077.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53078.1; -; Genomic_DNA. DR EMBL; BC010004; AAH10004.1; -; mRNA. DR EMBL; BQ062616; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; M29863; AAA35820.1; -; mRNA. DR CCDS; CCDS1110.1; -. [P14324-1] DR CCDS; CCDS44241.1; -. [P14324-2] DR PIR; A35726; A35726. DR RefSeq; NP_001129293.1; NM_001135821.1. [P14324-1] DR RefSeq; NP_001129294.1; NM_001135822.1. [P14324-2] DR RefSeq; NP_001229753.1; NM_001242824.1. [P14324-2] DR RefSeq; NP_001229754.1; NM_001242825.1. DR RefSeq; NP_001995.1; NM_002004.3. [P14324-1] DR RefSeq; XP_005245019.1; XM_005244962.1. [P14324-2] DR RefSeq; XP_005245020.1; XM_005244963.1. [P14324-2] DR UniGene; Hs.335918; -. DR PDB; 1YQ7; X-ray; 2.20 A; A=67-419. DR PDB; 1YV5; X-ray; 2.00 A; A=67-419. DR PDB; 1ZW5; X-ray; 2.30 A; A=67-419. DR PDB; 2F7M; X-ray; 2.30 A; F=72-419. DR PDB; 2F89; X-ray; 2.60 A; F=72-419. DR PDB; 2F8C; X-ray; 2.20 A; F=72-419. DR PDB; 2F8Z; X-ray; 2.60 A; F=72-419. DR PDB; 2F92; X-ray; 2.15 A; F=72-419. DR PDB; 2F94; X-ray; 1.94 A; F=72-419. DR PDB; 2F9K; X-ray; 2.06 A; F=72-419. DR PDB; 2OPM; X-ray; 2.40 A; A=67-419. DR PDB; 2OPN; X-ray; 2.70 A; A=67-419. DR PDB; 2QIS; X-ray; 1.80 A; A=67-419. DR PDB; 2RAH; X-ray; 2.00 A; A=67-419. DR PDB; 2VF6; X-ray; 2.10 A; A=67-419. DR PDB; 3B7L; X-ray; 1.95 A; A=67-419. DR PDB; 3CP6; X-ray; 1.95 A; A=67-419. DR PDB; 3N1V; X-ray; 2.18 A; F=72-419. DR PDB; 3N1W; X-ray; 2.56 A; F=72-419. DR PDB; 3N3L; X-ray; 2.74 A; F=72-419. DR PDB; 3N45; X-ray; 1.88 A; F=72-419. DR PDB; 3N46; X-ray; 2.35 A; F=72-419. DR PDB; 3N49; X-ray; 2.50 A; F=72-419. DR PDB; 3N5H; X-ray; 2.20 A; F=72-419. DR PDB; 3N5J; X-ray; 2.35 A; F=72-419. DR PDB; 3N6K; X-ray; 2.25 A; F=72-419. DR PDB; 3RYE; X-ray; 2.10 A; A=71-419. DR PDB; 3S4J; X-ray; 1.95 A; A=71-419. DR PDB; 4DEM; X-ray; 1.85 A; F=67-419. DR PDB; 4GA3; X-ray; 2.39 A; A=72-419. DR PDB; 4H5C; X-ray; 2.02 A; F=67-419. DR PDB; 4H5D; X-ray; 2.02 A; F=67-419. DR PDB; 4H5E; X-ray; 2.04 A; F=67-419. DR PDB; 4JVJ; X-ray; 2.80 A; F=67-419. DR PDB; 4KFA; X-ray; 1.98 A; A=67-419. DR PDB; 4KPD; X-ray; 1.96 A; A=67-419. DR PDB; 4KPJ; X-ray; 1.95 A; A=67-419. DR PDB; 4KQ5; X-ray; 2.40 A; A=67-419. DR PDB; 4KQS; X-ray; 1.97 A; A=67-419. DR PDB; 4KQU; X-ray; 2.07 A; A=67-419. DR PDB; 4L2X; X-ray; 2.55 A; F=67-419. DR PDB; 4LFV; X-ray; 2.00 A; F=67-419. DR PDB; 4LPG; X-ray; 2.35 A; F=67-419. DR PDB; 4LPH; X-ray; 2.30 A; F=67-419. DR PDB; 4N1Z; X-ray; 2.35 A; F=72-419. DR PDB; 4N9U; X-ray; 2.11 A; A=67-419. DR PDB; 4NFI; X-ray; 1.85 A; F=67-419. DR PDB; 4NFJ; X-ray; 2.05 A; F=67-419. DR PDB; 4NFK; X-ray; 1.85 A; F=67-419. DR PDB; 4NG6; X-ray; 2.35 A; A=67-419. DR PDB; 4NKE; X-ray; 1.46 A; A=67-419. DR PDB; 4NKF; X-ray; 2.00 A; A=67-419. DR PDB; 4NUA; X-ray; 1.43 A; A=67-419. DR PDB; 4OGU; X-ray; 2.10 A; A=67-419. DR PDB; 4P0V; X-ray; 2.40 A; A=73-419. DR PDB; 4P0W; X-ray; 2.41 A; A=72-419. DR PDB; 4P0X; X-ray; 2.50 A; A=72-419. DR PDB; 4PVX; X-ray; 2.18 A; F=67-419. DR PDB; 4PVY; X-ray; 2.05 A; F=67-419. DR PDB; 4Q23; X-ray; 1.98 A; A=67-419. DR PDB; 4QPF; X-ray; 1.59 A; A=67-419. DR PDB; 4QXS; X-ray; 1.90 A; F=67-419. DR PDB; 4RXA; X-ray; 2.20 A; A=72-419. DR PDBsum; 1YQ7; -. DR PDBsum; 1YV5; -. DR PDBsum; 1ZW5; -. DR PDBsum; 2F7M; -. DR PDBsum; 2F89; -. DR PDBsum; 2F8C; -. DR PDBsum; 2F8Z; -. DR PDBsum; 2F92; -. DR PDBsum; 2F94; -. DR PDBsum; 2F9K; -. DR PDBsum; 2OPM; -. DR PDBsum; 2OPN; -. DR PDBsum; 2QIS; -. DR PDBsum; 2RAH; -. DR PDBsum; 2VF6; -. DR PDBsum; 3B7L; -. DR PDBsum; 3CP6; -. DR PDBsum; 3N1V; -. DR PDBsum; 3N1W; -. DR PDBsum; 3N3L; -. DR PDBsum; 3N45; -. DR PDBsum; 3N46; -. DR PDBsum; 3N49; -. DR PDBsum; 3N5H; -. DR PDBsum; 3N5J; -. DR PDBsum; 3N6K; -. DR PDBsum; 3RYE; -. DR PDBsum; 3S4J; -. DR PDBsum; 4DEM; -. DR PDBsum; 4GA3; -. DR PDBsum; 4H5C; -. DR PDBsum; 4H5D; -. DR PDBsum; 4H5E; -. DR PDBsum; 4JVJ; -. DR PDBsum; 4KFA; -. DR PDBsum; 4KPD; -. DR PDBsum; 4KPJ; -. DR PDBsum; 4KQ5; -. DR PDBsum; 4KQS; -. DR PDBsum; 4KQU; -. DR PDBsum; 4L2X; -. DR PDBsum; 4LFV; -. DR PDBsum; 4LPG; -. DR PDBsum; 4LPH; -. DR PDBsum; 4N1Z; -. DR PDBsum; 4N9U; -. DR PDBsum; 4NFI; -. DR PDBsum; 4NFJ; -. DR PDBsum; 4NFK; -. DR PDBsum; 4NG6; -. DR PDBsum; 4NKE; -. DR PDBsum; 4NKF; -. DR PDBsum; 4NUA; -. DR PDBsum; 4OGU; -. DR PDBsum; 4P0V; -. DR PDBsum; 4P0W; -. DR PDBsum; 4P0X; -. DR PDBsum; 4PVX; -. DR PDBsum; 4PVY; -. DR PDBsum; 4Q23; -. DR PDBsum; 4QPF; -. DR PDBsum; 4QXS; -. DR PDBsum; 4RXA; -. DR ProteinModelPortal; P14324; -. DR SMR; P14324; 74-419. DR BioGrid; 108517; 28. DR DIP; DIP-50059N; -. DR IntAct; P14324; 5. DR MINT; MINT-2858951; -. DR STRING; 9606.ENSP00000349078; -. DR BindingDB; P14324; -. DR ChEMBL; CHEMBL1782; -. DR DrugBank; DB00630; Alendronate. DR DrugBank; DB00710; Ibandronate. DR DrugBank; DB00282; Pamidronate. DR DrugBank; DB00884; Risedronate. DR DrugBank; DB00399; Zoledronate. DR GuidetoPHARMACOLOGY; 644; -. DR PhosphoSite; P14324; -. DR BioMuta; FDPS; -. DR DMDM; 215274250; -. DR MaxQB; P14324; -. DR PaxDb; P14324; -. DR PRIDE; P14324; -. DR DNASU; 2224; -. DR Ensembl; ENST00000356657; ENSP00000349078; ENSG00000160752. [P14324-1] DR Ensembl; ENST00000368356; ENSP00000357340; ENSG00000160752. [P14324-1] DR Ensembl; ENST00000447866; ENSP00000391755; ENSG00000160752. [P14324-2] DR Ensembl; ENST00000467076; ENSP00000480142; ENSG00000160752. [P14324-2] DR Ensembl; ENST00000612683; ENSP00000478235; ENSG00000160752. [P14324-2] DR GeneID; 2224; -. DR KEGG; hsa:2224; -. DR UCSC; uc001fkc.2; human. [P14324-1] DR CTD; 2224; -. DR GeneCards; FDPS; -. DR H-InvDB; HIX0025342; -. DR HGNC; HGNC:3631; FDPS. DR HPA; HPA028200; -. DR MIM; 134629; gene. DR neXtProt; NX_P14324; -. DR PharmGKB; PA28075; -. DR eggNOG; KOG0711; Eukaryota. DR eggNOG; COG0142; LUCA. DR GeneTree; ENSGT00530000064127; -. DR HOGENOM; HOG000160912; -. DR HOVERGEN; HBG005741; -. DR InParanoid; P14324; -. DR KO; K00787; -. DR OMA; VIDSYKM; -. DR OrthoDB; EOG7W9RVG; -. DR PhylomeDB; P14324; -. DR TreeFam; TF300897; -. DR BioCyc; MetaCyc:ENSG00000160752-MONOMER; -. DR BRENDA; 2.5.1.10; 2681. DR Reactome; R-HSA-191273; Cholesterol biosynthesis. DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP). DR SABIO-RK; P14324; -. DR UniPathway; UPA00259; UER00368. DR UniPathway; UPA00260; UER00369. DR ChiTaRS; FDPS; human. DR EvolutionaryTrace; P14324; -. DR GenomeRNAi; 2224; -. DR NextBio; 9017; -. DR PRO; PR:P14324; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; P14324; -. DR CleanEx; HS_FDPS; -. DR ExpressionAtlas; P14324; baseline and differential. DR Genevisible; P14324; HS. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IBA:GO_Central. DR GO; GO:0004337; F:geranyltranstransferase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0006695; P:cholesterol biosynthetic process; TAS:Reactome. DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 1.10.600.10; -; 1. DR InterPro; IPR008949; Isoprenoid_synthase_dom. DR InterPro; IPR000092; Polyprenyl_synt. DR Pfam; PF00348; polyprenyl_synt; 1. DR SUPFAM; SSF48576; SSF48576; 1. DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; KW Cholesterol biosynthesis; Cholesterol metabolism; Complete proteome; KW Cytoplasm; Host-virus interaction; Isoprene biosynthesis; KW Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding; KW Polymorphism; Reference proteome; Steroid biosynthesis; KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; KW Transferase. FT CHAIN 1 419 Farnesyl pyrophosphate synthase. FT /FTId=PRO_0000123944. FT METAL 169 169 Magnesium 1. FT METAL 169 169 Magnesium 2. FT METAL 173 173 Magnesium 1. FT METAL 173 173 Magnesium 2. FT METAL 309 309 Magnesium 3. FT BINDING 123 123 Isopentenyl diphosphate. FT BINDING 126 126 Isopentenyl diphosphate. FT BINDING 162 162 Isopentenyl diphosphate. FT BINDING 178 178 Dimethylallyl diphosphate. FT BINDING 179 179 Isopentenyl diphosphate. FT BINDING 266 266 Dimethylallyl diphosphate. FT BINDING 267 267 Dimethylallyl diphosphate. FT BINDING 306 306 Dimethylallyl diphosphate. FT BINDING 323 323 Dimethylallyl diphosphate. FT BINDING 332 332 Dimethylallyl diphosphate. {ECO:0000250}. FT SITE 164 164 Important for determining product chain FT length. {ECO:0000250}. FT SITE 165 165 Important for determining product chain FT length. {ECO:0000250}. FT MOD_RES 123 123 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 353 353 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT VAR_SEQ 1 66 Missing (in isoform 2). FT {ECO:0000303|PubMed:1968462, FT ECO:0000303|Ref.7}. FT /FTId=VSP_046958. FT VARIANT 364 364 V -> A (in dbSNP:rs41314549). FT /FTId=VAR_061274. FT VARIANT 391 391 I -> V (in dbSNP:rs17456). FT /FTId=VAR_049644. FT CONFLICT 141 141 R -> K (in Ref. 7; BQ062616). FT {ECO:0000305}. FT CONFLICT 182 182 I -> T (in Ref. 1; AAA52423). FT {ECO:0000305}. FT CONFLICT 284 284 G -> R (in Ref. 7; BQ062616). FT {ECO:0000305}. FT HELIX 76 85 {ECO:0000244|PDB:4NUA}. FT HELIX 87 94 {ECO:0000244|PDB:4NUA}. FT HELIX 97 100 {ECO:0000244|PDB:4DEM}. FT HELIX 102 104 {ECO:0000244|PDB:4NUA}. FT HELIX 105 118 {ECO:0000244|PDB:4NUA}. FT STRAND 119 122 {ECO:0000244|PDB:4NUA}. FT HELIX 125 137 {ECO:0000244|PDB:4NUA}. FT HELIX 140 142 {ECO:0000244|PDB:4NUA}. FT HELIX 145 172 {ECO:0000244|PDB:4NUA}. FT STRAND 176 178 {ECO:0000244|PDB:4QXS}. FT HELIX 184 186 {ECO:0000244|PDB:4NUA}. FT TURN 188 190 {ECO:0000244|PDB:4NUA}. FT HELIX 191 193 {ECO:0000244|PDB:4NUA}. FT HELIX 194 213 {ECO:0000244|PDB:4NUA}. FT HELIX 219 243 {ECO:0000244|PDB:4NUA}. FT STRAND 246 248 {ECO:0000244|PDB:4JVJ}. FT HELIX 251 253 {ECO:0000244|PDB:4NUA}. FT HELIX 256 266 {ECO:0000244|PDB:4NUA}. FT HELIX 268 271 {ECO:0000244|PDB:4NUA}. FT HELIX 273 282 {ECO:0000244|PDB:4NUA}. FT HELIX 288 315 {ECO:0000244|PDB:4NUA}. FT HELIX 318 321 {ECO:0000244|PDB:4NUA}. FT TURN 327 331 {ECO:0000244|PDB:4NUA}. FT HELIX 335 343 {ECO:0000244|PDB:4NUA}. FT HELIX 346 355 {ECO:0000244|PDB:4NUA}. FT HELIX 361 373 {ECO:0000244|PDB:4NUA}. FT HELIX 376 398 {ECO:0000244|PDB:4NUA}. FT HELIX 404 414 {ECO:0000244|PDB:4NUA}. SQ SEQUENCE 419 AA; 48275 MW; 52934B80A808FB67 CRC64; MPLSRWLRSV GVFLLPAPYW APRERWLGSL RRPSLVHGYP VLAWHSARCW CQAWTEEPRA LCSSLRMNGD QNSDVYAQEK QDFVQHFSQI VRVLTEDEMG HPEIGDAIAR LKEVLEYNAI GGKYNRGLTV VVAFRELVEP RKQDADSLQR AWTVGWCVEL LQAFFLVADD IMDSSLTRRG QICWYQKPGV GLDAINDANL LEACIYRLLK LYCREQPYYL NLIELFLQSS YQTEIGQTLD LLTAPQGNVD LVRFTEKRYK SIVKYKTAFY SFYLPIAAAM YMAGIDGEKE HANAKKILLE MGEFFQIQDD YLDLFGDPSV TGKIGTDIQD NKCSWLVVQC LQRATPEQYQ ILKENYGQKE AEKVARVKAL YEELDLPAVF LQYEEDSYSH IMALIEQYAA PLPPAVFLGL ARKIYKRRK //