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P14324 (FPPS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Farnesyl pyrophosphate synthase

Short name=FPP synthase
Short name=FPS
EC=2.5.1.10
Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase
Dimethylallyltranstransferase
EC=2.5.1.1
Farnesyl diphosphate synthase
Geranyltranstransferase
Gene names
Name:FDPS
Synonyms:FPS, KIAA1293
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.18

Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate. Ref.18

Cofactor

Binds 3 magnesium 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. Ref.10

Pathway

Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.

Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.

Subunit structure

Homodimer. Interacts with RSAD2. Interacts with HTLV-1 protein p13(II). Ref.9 Ref.10 Ref.17

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the FPP/GGPP synthase family.

Sequence caution

The sequence BAA03523.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCholesterol biosynthesis
Cholesterol metabolism
Host-virus interaction
Isoprene biosynthesis
Lipid biosynthesis
Lipid metabolism
Steroid biosynthesis
Steroid metabolism
Sterol biosynthesis
Sterol metabolism
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandMagnesium
Metal-binding
   Molecular functionTransferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol biosynthetic process

Traceable author statement. Source: Reactome

farnesyl diphosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

geranyl diphosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

small molecule metabolic process

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functiondimethylallyltranstransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

geranyltranstransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P14324-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P14324-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 419419Farnesyl pyrophosphate synthase
PRO_0000123944

Sites

Metal binding1691Magnesium 1
Metal binding1691Magnesium 2
Metal binding1731Magnesium 1
Metal binding1731Magnesium 2
Metal binding3091Magnesium 3
Binding site1231Isopentenyl diphosphate
Binding site1261Isopentenyl diphosphate
Binding site1621Isopentenyl diphosphate
Binding site1781Dimethylallyl diphosphate
Binding site1791Isopentenyl diphosphate
Binding site2661Dimethylallyl diphosphate
Binding site2671Dimethylallyl diphosphate
Binding site3061Dimethylallyl diphosphate
Binding site3231Dimethylallyl diphosphate
Binding site3321Dimethylallyl diphosphate By similarity
Site1641Important for determining product chain length By similarity
Site1651Important for determining product chain length By similarity

Amino acid modifications

Modified residue1231N6-acetyllysine; alternate Ref.13
Modified residue1231N6-succinyllysine; alternate By similarity
Modified residue3531N6-acetyllysine Ref.13

Natural variations

Alternative sequence1 – 6666Missing in isoform 2.
VSP_046958
Natural variant3641V → A.
Corresponds to variant rs41314549 [ dbSNP | Ensembl ].
VAR_061274
Natural variant3911I → V.
Corresponds to variant rs17456 [ dbSNP | Ensembl ].
VAR_049644

Experimental info

Sequence conflict1411R → K in BQ062616. Ref.7
Sequence conflict1821I → T in AAA52423. Ref.1
Sequence conflict2841G → R in BQ062616. Ref.7

Secondary structure

................................................... 419
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 4.
Checksum: 52934B80A808FB67

FASTA41948,275
        10         20         30         40         50         60 
MPLSRWLRSV GVFLLPAPYW APRERWLGSL RRPSLVHGYP VLAWHSARCW CQAWTEEPRA 

        70         80         90        100        110        120 
LCSSLRMNGD QNSDVYAQEK QDFVQHFSQI VRVLTEDEMG HPEIGDAIAR LKEVLEYNAI 

       130        140        150        160        170        180 
GGKYNRGLTV VVAFRELVEP RKQDADSLQR AWTVGWCVEL LQAFFLVADD IMDSSLTRRG 

       190        200        210        220        230        240 
QICWYQKPGV GLDAINDANL LEACIYRLLK LYCREQPYYL NLIELFLQSS YQTEIGQTLD 

       250        260        270        280        290        300 
LLTAPQGNVD LVRFTEKRYK SIVKYKTAFY SFYLPIAAAM YMAGIDGEKE HANAKKILLE 

       310        320        330        340        350        360 
MGEFFQIQDD YLDLFGDPSV TGKIGTDIQD NKCSWLVVQC LQRATPEQYQ ILKENYGQKE 

       370        380        390        400        410 
AEKVARVKAL YEELDLPAVF LQYEEDSYSH IMALIEQYAA PLPPAVFLGL ARKIYKRRK 

« Hide

Isoform 2 [UniParc].

Checksum: 15B19F2A5C51B166
Show »

FASTA35340,532

References

« Hide 'large scale' references
[1]"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."
Wilkin D.J., Kutsunai S.Y., Edwards P.A.
J. Biol. Chem. 265:4607-4614(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"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."
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Bone marrow.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Muscle.
[7]The MGC Project Team
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-312 (ISOFORM 2).
[8]"Cloning, analysis, and bacterial expression of human farnesyl pyrophosphate synthetase and its regulation in Hep G2 cells."
Sheares B.T., White S.S., Molowa D.T., Chan K., Ding V.D.-H., Kroon P.A., Bostedor R.G., Karkas J.D.
Biochemistry 28:8129-8135(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-419.
Tissue: Liver.
[9]"Oncoviral bovine leukemia virus G4 and human T-cell leukemia virus type 1 p13(II) accessory proteins interact with farnesyl pyrophosphate synthetase."
Lefebvre L., Vanderplasschen A., Ciminale V., Heremans H., Dangoisse O., Jauniaux J.-C., Toussaint J.-F., Zelnik V., Burny A., Kettmann R., Willems L.
J. Virol. 76:1400-1414(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HTLV-1 P13(II).
[10]"The interferon-inducible protein viperin inhibits influenza virus release by perturbing lipid rafts."
Wang X., Hinson E.R., Cresswell P.
Cell Host Microbe 2:96-105(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RSAD2, ENZYME REGULATION.
[11]"Farnesyl diphosphate synthase; regulation of product specificity."
Szkopinska A., Plochocka D.
Acta Biochim. Pol. 52:45-55(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123 AND LYS-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs."
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.
ChemMedChem 1:267-273(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 72-419, SUBUNIT.
[18]"The molecular mechanism of nitrogen-containing bisphosphonates as antiosteoporosis drugs."
Kavanagh K.L., Guo K., Dunford J.E., Wu X., Knapp S., Ebetino F.H., Rogers M.J., Russell R.G., Oppermann U.
Proc. Natl. Acad. Sci. U.S.A. 103:7829-7834(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 67-419 IN COMPLEXES WITH MAGNESIUM IONS; RISEDRONATE AND ZOLEDRONATE, CATALYTIC ACTIVITY.
[19]"Lipophilic bisphosphonates as dual farnesyl/geranylgeranyl diphosphate synthase inhibitors: an X-ray and NMR investigation."
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. expand/collapse author list , Papapoulos S., Wang A.H.-J., Kubo T., Ochi M., Mukkamala D., Oldfield E.
J. Am. Chem. Soc. 131:5153-5162(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 67-419 IN COMPLEXES WITH MAGNESIUM AND BIPHOSPHONATES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05262 mRNA. Translation: AAA52423.1.
D14697 mRNA. Translation: BAA03523.2. Different initiation.
AK291084 mRNA. Translation: BAF83773.1.
AL139410 Genomic DNA. Translation: CAI12715.1.
CH471121 Genomic DNA. Translation: EAW53076.1.
CH471121 Genomic DNA. Translation: EAW53077.1.
CH471121 Genomic DNA. Translation: EAW53078.1.
BC010004 mRNA. Translation: AAH10004.1.
BQ062616 mRNA. No translation available.
M29863 mRNA. Translation: AAA35820.1.
PIRA35726.
RefSeqNP_001129293.1. NM_001135821.1.
NP_001129294.1. NM_001135822.1.
NP_001229753.1. NM_001242824.1.
NP_001229754.1. NM_001242825.1.
NP_001995.1. NM_002004.3.
XP_005245019.1. XM_005244962.1.
XP_005245020.1. XM_005244963.1.
UniGeneHs.335918.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YQ7X-ray2.20A67-419[»]
1YV5X-ray2.00A67-419[»]
1ZW5X-ray2.30A67-419[»]
2F7MX-ray2.30F72-419[»]
2F89X-ray2.60F72-419[»]
2F8CX-ray2.20F72-419[»]
2F8ZX-ray2.60F72-419[»]
2F92X-ray2.15F72-419[»]
2F94X-ray1.94F72-419[»]
2F9KX-ray2.06F72-419[»]
2OPMX-ray2.40A67-419[»]
2OPNX-ray2.70A67-419[»]
2QISX-ray1.80A67-419[»]
2RAHX-ray2.00A67-419[»]
2VF6X-ray2.10A67-419[»]
3B7LX-ray1.95A67-419[»]
3CP6X-ray1.95A67-419[»]
3N1VX-ray2.18F72-419[»]
3N1WX-ray2.56F72-419[»]
3N3LX-ray2.74F72-419[»]
3N45X-ray1.88F72-419[»]
3N46X-ray2.35F72-419[»]
3N49X-ray2.50F72-419[»]
3N5HX-ray2.20F72-419[»]
3N5JX-ray2.35F72-419[»]
3N6KX-ray2.25F72-419[»]
3RYEX-ray2.10A72-419[»]
3S4JX-ray1.95A72-419[»]
4DEMX-ray1.85F67-419[»]
4GA3X-ray2.39A72-419[»]
4H5CX-ray2.02F67-419[»]
4H5DX-ray2.02F67-419[»]
4H5EX-ray2.04F67-419[»]
4JVJX-ray2.80F67-419[»]
4L2XX-ray2.55F67-419[»]
ProteinModelPortalP14324.
SMRP14324. Positions 74-419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108517. 15 interactions.
IntActP14324. 5 interactions.
MINTMINT-2858951.
STRING9606.ENSP00000349078.

Chemistry

BindingDBP14324.
ChEMBLCHEMBL1782.
DrugBankDB00630. Alendronate.
DB00710. Ibandronate.
DB00282. Pamidronate.
DB00884. Risedronate.
DB00399. Zoledronate.
GuidetoPHARMACOLOGY644.

PTM databases

PhosphoSiteP14324.

Polymorphism databases

DMDM215274250.

Proteomic databases

PaxDbP14324.
PRIDEP14324.

Protocols and materials databases

DNASU2224.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356657; ENSP00000349078; ENSG00000160752. [P14324-1]
ENST00000368356; ENSP00000357340; ENSG00000160752. [P14324-1]
ENST00000447866; ENSP00000391755; ENSG00000160752. [P14324-2]
GeneID2224.
KEGGhsa:2224.
UCSCuc001fkc.2. human. [P14324-1]

Organism-specific databases

CTD2224.
GeneCardsGC01P155278.
H-InvDBHIX0025342.
HGNCHGNC:3631. FDPS.
HPAHPA028200.
MIM134629. gene.
neXtProtNX_P14324.
PharmGKBPA28075.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0142.
HOGENOMHOG000160912.
HOVERGENHBG005741.
InParanoidP14324.
KOK00787.
OMAVALAMRM.
OrthoDBEOG7W9RVG.
PhylomeDBP14324.
TreeFamTF300897.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000160752-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP14324.
UniPathwayUPA00259; UER00368.
UPA00260; UER00369.

Gene expression databases

ArrayExpressP14324.
BgeeP14324.
CleanExHS_FDPS.
GenevestigatorP14324.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
InterProIPR000092. Polyprenyl_synt.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMSSF48576. SSF48576. 1 hit.
PROSITEPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFDPS. human.
EvolutionaryTraceP14324.
GenomeRNAi2224.
NextBio9017.
PROP14324.
SOURCESearch...

Entry information

Entry nameFPPS_HUMAN
AccessionPrimary (citable) accession number: P14324
Secondary accession number(s): D3DV91, E9PCI9, Q96G29
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 161 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM