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Farnesyl pyrophosphate synthase (FPP synthase) (FPS) (EC 2.5.1.10) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Geranyltranstransferase)

 FPPS_HUMAN              Reviewed;         419 AA.
P14324; D3DV91; E9PCI9; Q96G29;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 4.
28-MAR-2018, entry version 204.
RecName: Full=Farnesyl pyrophosphate synthase;
Short=FPP synthase;
Short=FPS;
EC=2.5.1.10;
AltName: Full=(2E,6E)-farnesyl diphosphate synthase;
AltName: Full=Dimethylallyltranstransferase;
EC=2.5.1.1;
AltName: Full=Farnesyl diphosphate synthase;
AltName: Full=Geranyltranstransferase;
Name=FDPS; Synonyms=FPS, KIAA1293;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=1968462;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=7584026; DOI=10.1093/dnares/1.1.27;
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.;
"Prediction of the coding sequences of unidentified human genes. I.
The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
analysis of randomly sampled cDNA clones from human immature myeloid
cell line KG-1.";
DNA Res. 1:27-35(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
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 T.-O., 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. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-312 (ISOFORM 2).
The MGC Project Team;
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 74-419.
TISSUE=Liver;
PubMed=2690933; DOI=10.1021/bi00446a025;
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).
[9]
INTERACTION WITH HTLV-1 P13(II).
PubMed=11773414; DOI=10.1128/JVI.76.3.1400-1414.2002;
Lefebvre L., Vanderplasschen A., Ciminale V., Heremans H.,
Dangoisse O., Jauniaux J.-C., Toussaint J.-F., Zelnik V., Burny A.,
Kettmann R., Willems L.;
"Oncoviral bovine leukemia virus G4 and human T-cell leukemia virus
type 1 p13(II) accessory proteins interact with farnesyl pyrophosphate
synthetase.";
J. Virol. 76:1400-1414(2002).
[10]
INTERACTION WITH RSAD2, AND ENZYME REGULATION.
PubMed=18005724; DOI=10.1016/j.chom.2007.06.009;
Wang X., Hinson E.R., Cresswell P.;
"The interferon-inducible protein viperin inhibits influenza virus
release by perturbing lipid rafts.";
Cell Host Microbe 2:96-105(2007).
[11]
REVIEW.
PubMed=15827605;
Szkopinska A., Plochocka D.;
"Farnesyl diphosphate synthase; regulation of product specificity.";
Acta Biochim. Pol. 52:45-55(2005).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123 AND LYS-353, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
INVOLVEMENT IN POROK9, AND VARIANT POROK9 GLN-179.
PubMed=26202976; DOI=10.7554/eLife.06322;
Zhang Z., Li C., Wu F., Ma R., Luan J., Yang F., Liu W., Wang L.,
Zhang S., Liu Y., Gu J., Hua W., Fan M., Peng H., Meng X., Song N.,
Bi X., Gu C., Zhang Z., Huang Q., Chen L., Xiang L., Xu J., Zheng Z.,
Jiang Z.;
"Genomic variations of the mevalonate pathway in porokeratosis.";
Elife 4:E06322-E06322(2015).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 72-419, AND SUBUNIT.
PubMed=16892359; DOI=10.1002/cmdc.200500059;
Rondeau J.-M., Bitsch F., Bourgier E., Geiser M., Hemmig R.,
Kroemer M., Lehmann S., Ramage P., Rieffel S., Strauss A., Green J.R.,
Jahnke W.;
"Structural basis for the exceptional in vivo efficacy of
bisphosphonate drugs.";
ChemMedChem 1:267-273(2006).
[21]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 67-419 IN COMPLEXES WITH
MAGNESIUM IONS; RISEDRONATE AND ZOLEDRONATE, AND CATALYTIC ACTIVITY.
PubMed=16684881; DOI=10.1073/pnas.0601643103;
Kavanagh K.L., Guo K., Dunford J.E., Wu X., Knapp S., Ebetino F.H.,
Rogers M.J., Russell R.G., Oppermann U.;
"The molecular mechanism of nitrogen-containing bisphosphonates as
antiosteoporosis drugs.";
Proc. Natl. Acad. Sci. U.S.A. 103:7829-7834(2006).
[22]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 67-419 IN COMPLEXES WITH
MAGNESIUM AND BIPHOSPHONATES.
PubMed=19309137; DOI=10.1021/ja808285e;
Zhang Y., Cao R., Yin F., Hudock M.P., Guo R.-T., Krysiak K.,
Mukherjee S., Gao Y.-G., Robinson H., Song Y., No J.H., Bergan K.,
Leon A., Cass L., Goddard A., Chang T.-K., Lin F.-Y., Van Beek E.,
Papapoulos S., Wang A.H.-J., Kubo T., Ochi M., Mukkamala D.,
Oldfield E.;
"Lipophilic bisphosphonates as dual farnesyl/geranylgeranyl
diphosphate synthase inhibitors: an X-ray and NMR investigation.";
J. Am. Chem. Soc. 131:5153-5162(2009).
-!- FUNCTION: Key enzyme in isoprenoid biosynthesis which catalyzes
the formation of farnesyl diphosphate (FPP), a precursor for
several classes of essential metabolites including sterols,
dolichols, carotenoids, and ubiquinones. FPP also serves as
substrate for protein farnesylation and geranylgeranylation.
Catalyzes the sequential condensation of isopentenyl pyrophosphate
with the allylic pyrophosphates, dimethylallyl pyrophosphate, and
then with the resultant geranylpyrophosphate to the ultimate
product farnesyl pyrophosphate.
-!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl
diphosphate = diphosphate + geranyl diphosphate.
{ECO:0000269|PubMed:16684881}.
-!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate
= diphosphate + (2E,6E)-farnesyl diphosphate.
{ECO:0000269|PubMed:16684881}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Binds 3 Mg(2+) ions per subunit.;
-!- ENZYME REGULATION: Inactivated by interferon-induced RSAD2. This
inactivation may result of disruption of lipid rafts at the plasma
membrane, and thus have an antiviral effect since many enveloped
viruses need lipid rafts to bud efficiently out of the cell.
{ECO:0000269|PubMed:18005724}.
-!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate
biosynthesis; farnesyl diphosphate from geranyl diphosphate and
isopentenyl diphosphate: step 1/1.
-!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate
biosynthesis; geranyl diphosphate from dimethylallyl diphosphate
and isopentenyl diphosphate: step 1/1.
-!- SUBUNIT: Homodimer. Interacts with RSAD2. Interacts with HTLV-1
protein p13(II). {ECO:0000269|PubMed:11773414,
ECO:0000269|PubMed:16892359, ECO:0000269|PubMed:18005724}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P14324-1; Sequence=Displayed;
Name=2;
IsoId=P14324-2; Sequence=VSP_046958;
Note=Contains a N-acetylmethionine at position 1.
{ECO:0000244|PubMed:19413330, ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378};
-!- DISEASE: Porokeratosis 9, multiple types (POROK9) [MIM:616631]: A
form of porokeratosis, a disorder of faulty keratinization
characterized by one or more atrophic patches surrounded by a
distinctive hyperkeratotic ridgelike border called the cornoid
lamella. The keratotic lesions can progress to overt cutaneous
neoplasms, typically squamous cell carcinomas. Multiple clinical
variants of porokeratosis are recognized, including porokeratosis
of Mibelli, linear porokeratosis, disseminated superficial actinic
porokeratosis, palmoplantar porokeratosis, and punctate
porokeratosis. Different clinical presentations can be observed
among members of the same family. Individuals expressing more than
one variant have also been reported.
{ECO:0000269|PubMed:26202976}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA03523.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; J05262; AAA52423.1; -; mRNA.
EMBL; D14697; BAA03523.2; ALT_INIT; mRNA.
EMBL; AK291084; BAF83773.1; -; mRNA.
EMBL; AL139410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53076.1; -; Genomic_DNA.
EMBL; CH471121; EAW53077.1; -; Genomic_DNA.
EMBL; CH471121; EAW53078.1; -; Genomic_DNA.
EMBL; BC010004; AAH10004.1; -; mRNA.
EMBL; BQ062616; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; M29863; AAA35820.1; -; mRNA.
CCDS; CCDS1110.1; -. [P14324-1]
CCDS; CCDS44241.1; -. [P14324-2]
PIR; A35726; A35726.
RefSeq; NP_001129293.1; NM_001135821.1. [P14324-1]
RefSeq; NP_001129294.1; NM_001135822.1. [P14324-2]
RefSeq; NP_001229753.1; NM_001242824.1. [P14324-2]
RefSeq; NP_001229754.1; NM_001242825.1.
RefSeq; NP_001995.1; NM_002004.3. [P14324-1]
RefSeq; XP_005245019.1; XM_005244962.1. [P14324-2]
RefSeq; XP_005245020.1; XM_005244963.1. [P14324-2]
UniGene; Hs.335918; -.
PDB; 1YQ7; X-ray; 2.20 A; A=67-419.
PDB; 1YV5; X-ray; 2.00 A; A=67-419.
PDB; 1ZW5; X-ray; 2.30 A; A=67-419.
PDB; 2F7M; X-ray; 2.30 A; F=72-419.
PDB; 2F89; X-ray; 2.60 A; F=72-419.
PDB; 2F8C; X-ray; 2.20 A; F=72-419.
PDB; 2F8Z; X-ray; 2.60 A; F=72-419.
PDB; 2F92; X-ray; 2.15 A; F=72-419.
PDB; 2F94; X-ray; 1.94 A; F=72-419.
PDB; 2F9K; X-ray; 2.06 A; F=72-419.
PDB; 2OPM; X-ray; 2.40 A; A=67-419.
PDB; 2OPN; X-ray; 2.70 A; A=67-419.
PDB; 2QIS; X-ray; 1.80 A; A=67-419.
PDB; 2RAH; X-ray; 2.00 A; A=67-419.
PDB; 2VF6; X-ray; 2.10 A; A=67-419.
PDB; 3B7L; X-ray; 1.95 A; A=67-419.
PDB; 3CP6; X-ray; 1.95 A; A=67-419.
PDB; 3N1V; X-ray; 2.18 A; F=72-419.
PDB; 3N1W; X-ray; 2.56 A; F=72-419.
PDB; 3N3L; X-ray; 2.74 A; F=72-419.
PDB; 3N45; X-ray; 1.88 A; F=72-419.
PDB; 3N46; X-ray; 2.35 A; F=72-419.
PDB; 3N49; X-ray; 2.50 A; F=72-419.
PDB; 3N5H; X-ray; 2.20 A; F=72-419.
PDB; 3N5J; X-ray; 2.35 A; F=72-419.
PDB; 3N6K; X-ray; 2.25 A; F=72-419.
PDB; 3RYE; X-ray; 2.10 A; A=71-419.
PDB; 3S4J; X-ray; 1.95 A; A=71-419.
PDB; 4DEM; X-ray; 1.85 A; F=67-419.
PDB; 4GA3; X-ray; 2.39 A; A=72-419.
PDB; 4H5C; X-ray; 2.02 A; F=67-419.
PDB; 4H5D; X-ray; 2.02 A; F=67-419.
PDB; 4H5E; X-ray; 2.04 A; F=67-419.
PDB; 4JVJ; X-ray; 2.80 A; F=67-419.
PDB; 4KFA; X-ray; 1.98 A; A=67-419.
PDB; 4KPD; X-ray; 1.96 A; A=67-419.
PDB; 4KPJ; X-ray; 1.95 A; A=67-419.
PDB; 4KQ5; X-ray; 2.40 A; A=67-419.
PDB; 4KQS; X-ray; 1.97 A; A=67-419.
PDB; 4KQU; X-ray; 2.07 A; A=67-419.
PDB; 4L2X; X-ray; 2.55 A; F=67-419.
PDB; 4LFV; X-ray; 2.00 A; F=67-419.
PDB; 4LPG; X-ray; 2.35 A; F=67-419.
PDB; 4LPH; X-ray; 2.30 A; F=67-419.
PDB; 4N1Z; X-ray; 2.35 A; F=72-419.
PDB; 4N9U; X-ray; 2.11 A; A=67-419.
PDB; 4NFI; X-ray; 1.85 A; F=67-419.
PDB; 4NFJ; X-ray; 2.05 A; F=67-419.
PDB; 4NFK; X-ray; 1.85 A; F=67-419.
PDB; 4NG6; X-ray; 2.35 A; A=67-419.
PDB; 4NKE; X-ray; 1.46 A; A=67-419.
PDB; 4NKF; X-ray; 2.00 A; A=67-419.
PDB; 4NUA; X-ray; 1.43 A; A=67-419.
PDB; 4OGU; X-ray; 2.10 A; A=67-419.
PDB; 4P0V; X-ray; 2.40 A; A=73-419.
PDB; 4P0W; X-ray; 2.41 A; A=72-419.
PDB; 4P0X; X-ray; 2.50 A; A=72-419.
PDB; 4PVX; X-ray; 2.18 A; F=67-419.
PDB; 4PVY; X-ray; 2.05 A; F=67-419.
PDB; 4Q23; X-ray; 1.98 A; A=67-419.
PDB; 4QPF; X-ray; 1.59 A; A=67-419.
PDB; 4QXS; X-ray; 1.90 A; F=67-419.
PDB; 4RXA; X-ray; 2.20 A; A=72-419.
PDB; 4XQR; X-ray; 2.15 A; F=67-419.
PDB; 4XQS; X-ray; 2.30 A; F=67-419.
PDB; 4XQT; X-ray; 2.10 A; F=67-419.
PDB; 5CG5; Other; 1.40 A; A=74-419.
PDB; 5CG6; Other; 1.70 A; A=74-419.
PDB; 5DGM; X-ray; 2.86 A; F=72-419.
PDB; 5DGN; X-ray; 2.08 A; F=72-419.
PDB; 5DGS; X-ray; 2.62 A; F=72-419.
PDB; 5DIQ; X-ray; 2.10 A; F=72-419.
PDB; 5DJP; X-ray; 2.40 A; F=72-419.
PDB; 5DJR; X-ray; 2.40 A; F=72-419.
PDB; 5DJV; X-ray; 2.30 A; F=72-419.
PDB; 5JA0; X-ray; 1.90 A; F=67-419.
PDB; 5JUZ; X-ray; 2.40 A; F=67-419.
PDB; 5JV0; X-ray; 2.40 A; F=67-419.
PDB; 5JV1; X-ray; 2.30 A; F=67-419.
PDB; 5JV2; X-ray; 2.30 A; F=67-419.
PDB; 5KSX; X-ray; 2.65 A; F=67-419.
PDBsum; 1YQ7; -.
PDBsum; 1YV5; -.
PDBsum; 1ZW5; -.
PDBsum; 2F7M; -.
PDBsum; 2F89; -.
PDBsum; 2F8C; -.
PDBsum; 2F8Z; -.
PDBsum; 2F92; -.
PDBsum; 2F94; -.
PDBsum; 2F9K; -.
PDBsum; 2OPM; -.
PDBsum; 2OPN; -.
PDBsum; 2QIS; -.
PDBsum; 2RAH; -.
PDBsum; 2VF6; -.
PDBsum; 3B7L; -.
PDBsum; 3CP6; -.
PDBsum; 3N1V; -.
PDBsum; 3N1W; -.
PDBsum; 3N3L; -.
PDBsum; 3N45; -.
PDBsum; 3N46; -.
PDBsum; 3N49; -.
PDBsum; 3N5H; -.
PDBsum; 3N5J; -.
PDBsum; 3N6K; -.
PDBsum; 3RYE; -.
PDBsum; 3S4J; -.
PDBsum; 4DEM; -.
PDBsum; 4GA3; -.
PDBsum; 4H5C; -.
PDBsum; 4H5D; -.
PDBsum; 4H5E; -.
PDBsum; 4JVJ; -.
PDBsum; 4KFA; -.
PDBsum; 4KPD; -.
PDBsum; 4KPJ; -.
PDBsum; 4KQ5; -.
PDBsum; 4KQS; -.
PDBsum; 4KQU; -.
PDBsum; 4L2X; -.
PDBsum; 4LFV; -.
PDBsum; 4LPG; -.
PDBsum; 4LPH; -.
PDBsum; 4N1Z; -.
PDBsum; 4N9U; -.
PDBsum; 4NFI; -.
PDBsum; 4NFJ; -.
PDBsum; 4NFK; -.
PDBsum; 4NG6; -.
PDBsum; 4NKE; -.
PDBsum; 4NKF; -.
PDBsum; 4NUA; -.
PDBsum; 4OGU; -.
PDBsum; 4P0V; -.
PDBsum; 4P0W; -.
PDBsum; 4P0X; -.
PDBsum; 4PVX; -.
PDBsum; 4PVY; -.
PDBsum; 4Q23; -.
PDBsum; 4QPF; -.
PDBsum; 4QXS; -.
PDBsum; 4RXA; -.
PDBsum; 4XQR; -.
PDBsum; 4XQS; -.
PDBsum; 4XQT; -.
PDBsum; 5CG5; -.
PDBsum; 5CG6; -.
PDBsum; 5DGM; -.
PDBsum; 5DGN; -.
PDBsum; 5DGS; -.
PDBsum; 5DIQ; -.
PDBsum; 5DJP; -.
PDBsum; 5DJR; -.
PDBsum; 5DJV; -.
PDBsum; 5JA0; -.
PDBsum; 5JUZ; -.
PDBsum; 5JV0; -.
PDBsum; 5JV1; -.
PDBsum; 5JV2; -.
PDBsum; 5KSX; -.
ProteinModelPortal; P14324; -.
SMR; P14324; -.
BioGrid; 108517; 50.
DIP; DIP-50059N; -.
IntAct; P14324; 8.
STRING; 9606.ENSP00000349078; -.
BindingDB; P14324; -.
ChEMBL; CHEMBL1782; -.
DrugBank; DB00630; Alendronic acid.
DrugBank; DB01785; Dimethylallyl Diphosphate.
DrugBank; DB07780; FARNESYL DIPHOSPHATE.
DrugBank; DB02552; Geranyl Diphosphate.
DrugBank; DB07841; GERANYLGERANYL DIPHOSPHATE.
DrugBank; DB00710; Ibandronate.
DrugBank; DB04714; ISOPENTENYL PYROPHOSPHATE.
DrugBank; DB02508; Isopentyl Pyrophosphate.
DrugBank; DB00282; Pamidronate.
DrugBank; DB00884; Risedronate.
DrugBank; DB00399; Zoledronic acid.
GuidetoPHARMACOLOGY; 644; -.
SwissLipids; SLP:000001248; -.
SwissLipids; SLP:000001252; -. [P14324-2]
iPTMnet; P14324; -.
PhosphoSitePlus; P14324; -.
SwissPalm; P14324; -.
BioMuta; FDPS; -.
DMDM; 215274250; -.
EPD; P14324; -.
MaxQB; P14324; -.
PaxDb; P14324; -.
PeptideAtlas; P14324; -.
PRIDE; P14324; -.
TopDownProteomics; P14324-1; -. [P14324-1]
DNASU; 2224; -.
Ensembl; ENST00000356657; ENSP00000349078; ENSG00000160752. [P14324-1]
Ensembl; ENST00000368356; ENSP00000357340; ENSG00000160752. [P14324-1]
Ensembl; ENST00000447866; ENSP00000391755; ENSG00000160752. [P14324-2]
Ensembl; ENST00000467076; ENSP00000480142; ENSG00000160752. [P14324-2]
Ensembl; ENST00000612683; ENSP00000478235; ENSG00000160752. [P14324-2]
GeneID; 2224; -.
KEGG; hsa:2224; -.
UCSC; uc001fkc.3; human. [P14324-1]
CTD; 2224; -.
DisGeNET; 2224; -.
EuPathDB; HostDB:ENSG00000160752.14; -.
GeneCards; FDPS; -.
H-InvDB; HIX0025342; -.
HGNC; HGNC:3631; FDPS.
HPA; HPA028200; -.
MalaCards; FDPS; -.
MIM; 134629; gene.
MIM; 616631; phenotype.
neXtProt; NX_P14324; -.
OpenTargets; ENSG00000160752; -.
PharmGKB; PA28075; -.
eggNOG; KOG0711; Eukaryota.
eggNOG; COG0142; LUCA.
GeneTree; ENSGT00900000141074; -.
HOGENOM; HOG000160912; -.
HOVERGEN; HBG005741; -.
InParanoid; P14324; -.
KO; K00787; -.
OMA; ITAPEDH; -.
OrthoDB; EOG091G0BPT; -.
PhylomeDB; P14324; -.
TreeFam; TF300897; -.
BioCyc; MetaCyc:ENSG00000160752-MONOMER; -.
BRENDA; 2.5.1.10; 2681.
Reactome; R-HSA-191273; Cholesterol biosynthesis.
Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
SABIO-RK; P14324; -.
UniPathway; UPA00259; UER00368.
UniPathway; UPA00260; UER00369.
ChiTaRS; FDPS; human.
EvolutionaryTrace; P14324; -.
GenomeRNAi; 2224; -.
PRO; PR:P14324; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000160752; -.
CleanEx; HS_FDPS; -.
ExpressionAtlas; P14324; baseline and differential.
Genevisible; P14324; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0004161; F:dimethylallyltranstransferase activity; IBA:GO_Central.
GO; GO:0004337; F:geranyltranstransferase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0006695; P:cholesterol biosynthetic process; TAS:Reactome.
GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IBA:GO_Central.
GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0045540; P:regulation of cholesterol biosynthetic process; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.10.600.10; -; 1.
InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
InterPro; IPR000092; Polyprenyl_synt.
InterPro; IPR033749; Polyprenyl_synt_CS.
Pfam; PF00348; polyprenyl_synt; 1.
SUPFAM; SSF48576; SSF48576; 1.
PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Cholesterol biosynthesis; Cholesterol metabolism; Complete proteome;
Cytoplasm; Disease mutation; Host-virus interaction;
Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism;
Magnesium; Metal-binding; Polymorphism; Reference proteome;
Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
Sterol metabolism; Transferase.
CHAIN 1 419 Farnesyl pyrophosphate synthase.
/FTId=PRO_0000123944.
METAL 169 169 Magnesium 1.
METAL 169 169 Magnesium 2.
METAL 173 173 Magnesium 1.
METAL 173 173 Magnesium 2.
METAL 309 309 Magnesium 3.
BINDING 123 123 Isopentenyl diphosphate.
BINDING 126 126 Isopentenyl diphosphate.
BINDING 162 162 Isopentenyl diphosphate.
BINDING 178 178 Dimethylallyl diphosphate.
BINDING 179 179 Isopentenyl diphosphate.
BINDING 266 266 Dimethylallyl diphosphate.
BINDING 267 267 Dimethylallyl diphosphate.
BINDING 306 306 Dimethylallyl diphosphate.
BINDING 323 323 Dimethylallyl diphosphate.
BINDING 332 332 Dimethylallyl diphosphate. {ECO:0000250}.
SITE 164 164 Important for determining product chain
length. {ECO:0000250}.
SITE 165 165 Important for determining product chain
length. {ECO:0000250}.
MOD_RES 123 123 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 353 353 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 66 Missing (in isoform 2).
{ECO:0000303|PubMed:1968462,
ECO:0000303|Ref.7}.
/FTId=VSP_046958.
VARIANT 179 179 R -> Q (in POROK9; dbSNP:rs863225241).
{ECO:0000269|PubMed:26202976}.
/FTId=VAR_075062.
VARIANT 364 364 V -> A (in dbSNP:rs41314549).
/FTId=VAR_061274.
VARIANT 391 391 I -> V (in dbSNP:rs17456).
/FTId=VAR_049644.
CONFLICT 141 141 R -> K (in Ref. 7; BQ062616).
{ECO:0000305}.
CONFLICT 182 182 I -> T (in Ref. 1; AAA52423).
{ECO:0000305}.
CONFLICT 284 284 G -> R (in Ref. 7; BQ062616).
{ECO:0000305}.
HELIX 76 85 {ECO:0000244|PDB:4NUA}.
HELIX 87 94 {ECO:0000244|PDB:4NUA}.
HELIX 97 100 {ECO:0000244|PDB:4DEM}.
HELIX 102 104 {ECO:0000244|PDB:4NUA}.
HELIX 105 118 {ECO:0000244|PDB:4NUA}.
STRAND 119 122 {ECO:0000244|PDB:4NUA}.
HELIX 125 137 {ECO:0000244|PDB:4NUA}.
HELIX 140 142 {ECO:0000244|PDB:4NUA}.
HELIX 145 172 {ECO:0000244|PDB:4NUA}.
STRAND 176 178 {ECO:0000244|PDB:4QXS}.
HELIX 184 186 {ECO:0000244|PDB:4NUA}.
TURN 188 190 {ECO:0000244|PDB:4NUA}.
HELIX 191 193 {ECO:0000244|PDB:4NUA}.
HELIX 194 213 {ECO:0000244|PDB:4NUA}.
HELIX 219 243 {ECO:0000244|PDB:4NUA}.
STRAND 246 248 {ECO:0000244|PDB:4JVJ}.
HELIX 251 253 {ECO:0000244|PDB:4NUA}.
HELIX 256 266 {ECO:0000244|PDB:4NUA}.
HELIX 268 271 {ECO:0000244|PDB:4NUA}.
HELIX 273 282 {ECO:0000244|PDB:4NUA}.
HELIX 288 315 {ECO:0000244|PDB:4NUA}.
HELIX 318 321 {ECO:0000244|PDB:4NUA}.
TURN 327 331 {ECO:0000244|PDB:4NUA}.
HELIX 335 343 {ECO:0000244|PDB:4NUA}.
HELIX 346 355 {ECO:0000244|PDB:4NUA}.
HELIX 361 373 {ECO:0000244|PDB:4NUA}.
HELIX 376 398 {ECO:0000244|PDB:4NUA}.
HELIX 404 414 {ECO:0000244|PDB:4NUA}.
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


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