Full text data of FDPS
FDPS
(FPS, KIAA1293)
[Confidence: low (only semi-automatic identification from reviews)]
Farnesyl pyrophosphate synthase; FPP synthase; FPS; 2.5.1.10 ((2E,6E)-farnesyl diphosphate synthase; Dimethylallyltranstransferase; 2.5.1.1; Farnesyl diphosphate synthase; Geranyltranstransferase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Farnesyl pyrophosphate synthase; FPP synthase; FPS; 2.5.1.10 ((2E,6E)-farnesyl diphosphate synthase; Dimethylallyltranstransferase; 2.5.1.1; Farnesyl diphosphate synthase; Geranyltranstransferase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P14324
ID FPPS_HUMAN Reviewed; 419 AA.
AC P14324; D3DV91; E9PCI9; Q96G29;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-NOV-2008, sequence version 4.
DT 22-JAN-2014, entry version 158.
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;
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 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 MASS
RP SPECTROMETRY.
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 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 [16]
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 [17]
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 [18]
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 -!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate
CC = diphosphate + (2E,6E)-farnesyl diphosphate.
CC -!- COFACTOR: Binds 3 magnesium 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 -!- 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).
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 -!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA03523.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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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 PIR; A35726; A35726.
DR RefSeq; NP_001129293.1; NM_001135821.1.
DR RefSeq; NP_001129294.1; NM_001135822.1.
DR RefSeq; NP_001229753.1; NM_001242824.1.
DR RefSeq; NP_001229754.1; NM_001242825.1.
DR RefSeq; NP_001995.1; NM_002004.3.
DR RefSeq; XP_005245019.1; XM_005244962.1.
DR RefSeq; XP_005245020.1; XM_005244963.1.
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=72-419.
DR PDB; 3S4J; X-ray; 1.95 A; A=72-419.
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 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 ProteinModelPortal; P14324; -.
DR SMR; P14324; 74-419.
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 DMDM; 215274250; -.
DR PaxDb; P14324; -.
DR PRIDE; P14324; -.
DR DNASU; 2224; -.
DR Ensembl; ENST00000356657; ENSP00000349078; ENSG00000160752.
DR Ensembl; ENST00000368356; ENSP00000357340; ENSG00000160752.
DR Ensembl; ENST00000447866; ENSP00000391755; ENSG00000160752.
DR GeneID; 2224; -.
DR KEGG; hsa:2224; -.
DR UCSC; uc001fkc.2; human.
DR CTD; 2224; -.
DR GeneCards; GC01P155278; -.
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; COG0142; -.
DR HOGENOM; HOG000160912; -.
DR HOVERGEN; HBG005741; -.
DR InParanoid; P14324; -.
DR KO; K00787; -.
DR OMA; VALAMRM; -.
DR OrthoDB; EOG7W9RVG; -.
DR PhylomeDB; P14324; -.
DR BioCyc; MetaCyc:ENSG00000160752-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
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 ArrayExpress; P14324; -.
DR Bgee; P14324; -.
DR CleanEx; HS_FDPS; -.
DR Genevestigator; P14324; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006695; P:cholesterol biosynthetic process; TAS:Reactome.
DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR008949; Terpenoid_synth.
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 (By
FT similarity).
FT SITE 164 164 Important for determining product chain
FT length (By similarity).
FT SITE 165 165 Important for determining product chain
FT length (By similarity).
FT MOD_RES 123 123 N6-acetyllysine.
FT MOD_RES 353 353 N6-acetyllysine.
FT VAR_SEQ 1 66 Missing (in isoform 2).
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 CONFLICT 182 182 I -> T (in Ref. 1; AAA52423).
FT CONFLICT 284 284 G -> R (in Ref. 7; BQ062616).
FT HELIX 75 95
FT HELIX 97 100
FT HELIX 102 104
FT HELIX 105 118
FT STRAND 119 122
FT HELIX 125 137
FT HELIX 140 142
FT HELIX 145 172
FT STRAND 176 178
FT HELIX 184 186
FT TURN 188 190
FT HELIX 191 193
FT HELIX 194 213
FT HELIX 219 243
FT HELIX 251 253
FT HELIX 256 266
FT HELIX 268 271
FT HELIX 273 282
FT HELIX 288 315
FT HELIX 318 321
FT TURN 327 331
FT HELIX 335 343
FT HELIX 346 355
FT HELIX 361 373
FT HELIX 376 398
FT HELIX 404 414
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
//
ID FPPS_HUMAN Reviewed; 419 AA.
AC P14324; D3DV91; E9PCI9; Q96G29;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-NOV-2008, sequence version 4.
DT 22-JAN-2014, entry version 158.
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;
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 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 MASS
RP SPECTROMETRY.
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 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 [16]
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 [17]
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 [18]
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 -!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate
CC = diphosphate + (2E,6E)-farnesyl diphosphate.
CC -!- COFACTOR: Binds 3 magnesium 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 -!- 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).
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 -!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA03523.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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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 PIR; A35726; A35726.
DR RefSeq; NP_001129293.1; NM_001135821.1.
DR RefSeq; NP_001129294.1; NM_001135822.1.
DR RefSeq; NP_001229753.1; NM_001242824.1.
DR RefSeq; NP_001229754.1; NM_001242825.1.
DR RefSeq; NP_001995.1; NM_002004.3.
DR RefSeq; XP_005245019.1; XM_005244962.1.
DR RefSeq; XP_005245020.1; XM_005244963.1.
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=72-419.
DR PDB; 3S4J; X-ray; 1.95 A; A=72-419.
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 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 ProteinModelPortal; P14324; -.
DR SMR; P14324; 74-419.
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 DMDM; 215274250; -.
DR PaxDb; P14324; -.
DR PRIDE; P14324; -.
DR DNASU; 2224; -.
DR Ensembl; ENST00000356657; ENSP00000349078; ENSG00000160752.
DR Ensembl; ENST00000368356; ENSP00000357340; ENSG00000160752.
DR Ensembl; ENST00000447866; ENSP00000391755; ENSG00000160752.
DR GeneID; 2224; -.
DR KEGG; hsa:2224; -.
DR UCSC; uc001fkc.2; human.
DR CTD; 2224; -.
DR GeneCards; GC01P155278; -.
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; COG0142; -.
DR HOGENOM; HOG000160912; -.
DR HOVERGEN; HBG005741; -.
DR InParanoid; P14324; -.
DR KO; K00787; -.
DR OMA; VALAMRM; -.
DR OrthoDB; EOG7W9RVG; -.
DR PhylomeDB; P14324; -.
DR BioCyc; MetaCyc:ENSG00000160752-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
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 ArrayExpress; P14324; -.
DR Bgee; P14324; -.
DR CleanEx; HS_FDPS; -.
DR Genevestigator; P14324; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006695; P:cholesterol biosynthetic process; TAS:Reactome.
DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR008949; Terpenoid_synth.
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 (By
FT similarity).
FT SITE 164 164 Important for determining product chain
FT length (By similarity).
FT SITE 165 165 Important for determining product chain
FT length (By similarity).
FT MOD_RES 123 123 N6-acetyllysine.
FT MOD_RES 353 353 N6-acetyllysine.
FT VAR_SEQ 1 66 Missing (in isoform 2).
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 CONFLICT 182 182 I -> T (in Ref. 1; AAA52423).
FT CONFLICT 284 284 G -> R (in Ref. 7; BQ062616).
FT HELIX 75 95
FT HELIX 97 100
FT HELIX 102 104
FT HELIX 105 118
FT STRAND 119 122
FT HELIX 125 137
FT HELIX 140 142
FT HELIX 145 172
FT STRAND 176 178
FT HELIX 184 186
FT TURN 188 190
FT HELIX 191 193
FT HELIX 194 213
FT HELIX 219 243
FT HELIX 251 253
FT HELIX 256 266
FT HELIX 268 271
FT HELIX 273 282
FT HELIX 288 315
FT HELIX 318 321
FT TURN 327 331
FT HELIX 335 343
FT HELIX 346 355
FT HELIX 361 373
FT HELIX 376 398
FT HELIX 404 414
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
//
MIM
134629
*RECORD*
*FIELD* NO
134629
*FIELD* TI
*134629 FARNESYL DIPHOSPHATE SYNTHASE; FDPS
;;FARNESYLPYROPHOSPHATE SYNTHETASE; FPS
read more*FIELD* TX
DESCRIPTION
The isoprene biosynthetic pathway provides the cell with cholesterol,
ubiquinone, dolichol, and other nonsterol metabolites.
Farnesylpyrophosphate synthetase (EC 2.5.1.10) catalyzes the formation
of both geranyl and farnesylpyrophosphate from isopentenylpyrophosphate
and dimethylallyl pyrophosphate.
CLONING
Sheares et al. (1989) isolated and characterized a partial length cDNA
encoding FDPS. Wilkin et al. (1990) isolated and sequenced human cDNA
for this enzyme in the cholesterogenic pathway. Regulation of FDPS mRNA
levels parallels the regulation of mRNA levels for both HMG-CoA synthase
(142940) and HMG-CoA reductase (142910). Wilkin et al. (1990) found that
the mRNA levels for these enzymes were regulated in a coordinate manner
by phorbol esters.
GENE FUNCTION
By analysis of FDPS activity and protein in fractionated rat liver,
together with immunofluorescence and immunoelectron microscopy studies,
Krisans et al. (1994) demonstrated that FDPS is largely localized in
peroxisomes. They found that liver tissue from patients with the
peroxisomal deficiency diseases Zellweger syndrome (see 214100) and
neonatal adrenoleukodystrophy (see 601539) contained reduced activities
of FDPS and 4 other enzymes involved in isoprenoid synthesis. They
proposed that these enzymes are localized in peroxisomes.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the FDPS
gene to chromosome 1 (TMAP SHGC-2651).
Several genes with high sequence similarity to FDPS have been identified
(Sparkes et al., 1987; Heinzmann et al., 1989), all of which have been
found to be pseudogenes (Scott, 2006).
- Pseudogenes
By plus/minus screening of a rat liver cDNA library, Sparkes et al.
(1987) identified a gene that was coordinately regulated with HMG-CoA
reductase (142910) and HMG-CoA synthase (142940), suggesting that it may
be involved in cholesterol synthesis. It was provisionally identified as
cholesterol repressible protein-39. Using somatic cell hybrids and in
situ hybridization, Sparkes et al. (1987) mapped cholesterol repressible
protein genes in the human to 3 chromosomes: 1q24-q31 (CHR39A, later
determined to be the same as FDPSL1), 15q15-q21 (CHR39B, later
determined to be the same as FDPSL4), and Xq13-q21 (CHR39C, later
determined to be the same as FDPSL5).
Heinzmann et al. (1989) reported that the mouse and human genomes
contain multiple copies of genes with a high degree of sequence
similarity to farnesyl diphosphate synthase. One or more of these may
correspond to related phenyltransferases that catalyze the formation of
nonsterol isoprene compounds. In the human, by analysis of somatic
hybrids and by in situ hybridization (in the case of 3 of the 5 loci),
Heinzmann et al. (1989) localized 5 loci designated as FDPS-like genes:
FDPSL1 to 1q24-q31, FDPSL2 to chromosome 7, FDPSL3 to chromosome 14,
FDPSL4 to 15q14-q21, and FDPSL5 to Xq21-q22. All of these transcripts
have been found to be pseudogenes (Scott, 2006).
*FIELD* RF
1. Heinzmann, C.; Clarke, C. F.; Klisak, I.; Mohandas, T.; Sparkes,
R. S.; Edwards, P. A.; Lusis, A. J.: Dispersed family of human genes
with sequence similarity to farnesyl pyrophosphate synthetase. Genomics 5:
493-500, 1989.
2. Krisans, S. K.; Ericsson, J.; Edwards, P. A.; Keller, G. A.: Farnesyl-diphosphate
synthase is localized in peroxisomes. J. Biol. Chem. 269: 14165-14169,
1994.
3. Scott, A. F.: Personal Communication. Baltimore, Md. 11/9/2006.
4. Sheares, B. T.; White, S. S.; Molowa, D. T.; Chan, K.; Ding, V.
D.-H.; Kroon, P. A.; Bostedor, R. G.; Karkas, J. D.: Cloning, analysis,
and bacterial expression of human farnesyl pyrophosphate synthetase
and its regulation in Hep G2 cells. Biochemistry 28: 8129-8135,
1989.
5. Sparkes, R. S.; Klisak, I.; Mohandas, T.; Edwards, P. A.; Zollman,
S.; Clarke, C. F.; Lusis, A. J.: Assignment of genes that are expressed
during cholesterol synthesis to chromosomes 1q24-1q31, 15q15-15q21
and Xq13-Xq21. (Abstract) Cytogenet. Cell Genet. 46: 696 only, 1987.
6. Wilkin, D. J.; Kutsunai, S. Y.; Edwards, P. A.: Isolation and
sequence of the human farnesyl pyrophosphate synthetase cDNA: coordinate
regulation of the mRNAs for farnesyl pyrophosphate synthetase, 3-hydroxy-3-methylglutaryl
coenzyme A reductase, and 3-hydroxy-3-methylglutaryl coenzyme A synthase
by phorbol ester. J. Biol. Chem. 265: 4607-4614, 1990.
*FIELD* CN
Alan F. Scott - updated: 6/21/2004
*FIELD* CD
Victor A. McKusick: 5/28/1993
*FIELD* ED
alopez: 10/25/2012
carol: 11/9/2006
carol: 6/21/2004
mgross: 9/10/2001
carol: 8/20/1998
carol: 7/13/1993
carol: 6/8/1993
carol: 5/28/1993
*RECORD*
*FIELD* NO
134629
*FIELD* TI
*134629 FARNESYL DIPHOSPHATE SYNTHASE; FDPS
;;FARNESYLPYROPHOSPHATE SYNTHETASE; FPS
read more*FIELD* TX
DESCRIPTION
The isoprene biosynthetic pathway provides the cell with cholesterol,
ubiquinone, dolichol, and other nonsterol metabolites.
Farnesylpyrophosphate synthetase (EC 2.5.1.10) catalyzes the formation
of both geranyl and farnesylpyrophosphate from isopentenylpyrophosphate
and dimethylallyl pyrophosphate.
CLONING
Sheares et al. (1989) isolated and characterized a partial length cDNA
encoding FDPS. Wilkin et al. (1990) isolated and sequenced human cDNA
for this enzyme in the cholesterogenic pathway. Regulation of FDPS mRNA
levels parallels the regulation of mRNA levels for both HMG-CoA synthase
(142940) and HMG-CoA reductase (142910). Wilkin et al. (1990) found that
the mRNA levels for these enzymes were regulated in a coordinate manner
by phorbol esters.
GENE FUNCTION
By analysis of FDPS activity and protein in fractionated rat liver,
together with immunofluorescence and immunoelectron microscopy studies,
Krisans et al. (1994) demonstrated that FDPS is largely localized in
peroxisomes. They found that liver tissue from patients with the
peroxisomal deficiency diseases Zellweger syndrome (see 214100) and
neonatal adrenoleukodystrophy (see 601539) contained reduced activities
of FDPS and 4 other enzymes involved in isoprenoid synthesis. They
proposed that these enzymes are localized in peroxisomes.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the FDPS
gene to chromosome 1 (TMAP SHGC-2651).
Several genes with high sequence similarity to FDPS have been identified
(Sparkes et al., 1987; Heinzmann et al., 1989), all of which have been
found to be pseudogenes (Scott, 2006).
- Pseudogenes
By plus/minus screening of a rat liver cDNA library, Sparkes et al.
(1987) identified a gene that was coordinately regulated with HMG-CoA
reductase (142910) and HMG-CoA synthase (142940), suggesting that it may
be involved in cholesterol synthesis. It was provisionally identified as
cholesterol repressible protein-39. Using somatic cell hybrids and in
situ hybridization, Sparkes et al. (1987) mapped cholesterol repressible
protein genes in the human to 3 chromosomes: 1q24-q31 (CHR39A, later
determined to be the same as FDPSL1), 15q15-q21 (CHR39B, later
determined to be the same as FDPSL4), and Xq13-q21 (CHR39C, later
determined to be the same as FDPSL5).
Heinzmann et al. (1989) reported that the mouse and human genomes
contain multiple copies of genes with a high degree of sequence
similarity to farnesyl diphosphate synthase. One or more of these may
correspond to related phenyltransferases that catalyze the formation of
nonsterol isoprene compounds. In the human, by analysis of somatic
hybrids and by in situ hybridization (in the case of 3 of the 5 loci),
Heinzmann et al. (1989) localized 5 loci designated as FDPS-like genes:
FDPSL1 to 1q24-q31, FDPSL2 to chromosome 7, FDPSL3 to chromosome 14,
FDPSL4 to 15q14-q21, and FDPSL5 to Xq21-q22. All of these transcripts
have been found to be pseudogenes (Scott, 2006).
*FIELD* RF
1. Heinzmann, C.; Clarke, C. F.; Klisak, I.; Mohandas, T.; Sparkes,
R. S.; Edwards, P. A.; Lusis, A. J.: Dispersed family of human genes
with sequence similarity to farnesyl pyrophosphate synthetase. Genomics 5:
493-500, 1989.
2. Krisans, S. K.; Ericsson, J.; Edwards, P. A.; Keller, G. A.: Farnesyl-diphosphate
synthase is localized in peroxisomes. J. Biol. Chem. 269: 14165-14169,
1994.
3. Scott, A. F.: Personal Communication. Baltimore, Md. 11/9/2006.
4. Sheares, B. T.; White, S. S.; Molowa, D. T.; Chan, K.; Ding, V.
D.-H.; Kroon, P. A.; Bostedor, R. G.; Karkas, J. D.: Cloning, analysis,
and bacterial expression of human farnesyl pyrophosphate synthetase
and its regulation in Hep G2 cells. Biochemistry 28: 8129-8135,
1989.
5. Sparkes, R. S.; Klisak, I.; Mohandas, T.; Edwards, P. A.; Zollman,
S.; Clarke, C. F.; Lusis, A. J.: Assignment of genes that are expressed
during cholesterol synthesis to chromosomes 1q24-1q31, 15q15-15q21
and Xq13-Xq21. (Abstract) Cytogenet. Cell Genet. 46: 696 only, 1987.
6. Wilkin, D. J.; Kutsunai, S. Y.; Edwards, P. A.: Isolation and
sequence of the human farnesyl pyrophosphate synthetase cDNA: coordinate
regulation of the mRNAs for farnesyl pyrophosphate synthetase, 3-hydroxy-3-methylglutaryl
coenzyme A reductase, and 3-hydroxy-3-methylglutaryl coenzyme A synthase
by phorbol ester. J. Biol. Chem. 265: 4607-4614, 1990.
*FIELD* CN
Alan F. Scott - updated: 6/21/2004
*FIELD* CD
Victor A. McKusick: 5/28/1993
*FIELD* ED
alopez: 10/25/2012
carol: 11/9/2006
carol: 6/21/2004
mgross: 9/10/2001
carol: 8/20/1998
carol: 7/13/1993
carol: 6/8/1993
carol: 5/28/1993