P14324 (FPPS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Protein existence	Evidence 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.14 Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate. Ref.14
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 envelopped viruses need lipid rafts to bud efficiently out of the cell. Ref.9
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.8 Ref.9 Ref.13
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the FPP/GGPP synthase family.
Caution	It is uncertain whether Met-1 or Met-67 is the initiator.
Sequence caution	The sequence AAA52423.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA03523.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cholesterol biosynthesis Host-virus interaction Isoprene biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Magnesium Metal-binding
Molecular function	Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Traceable author statement. Source: Reactome interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW isoprenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay. Source: HPA
Molecular function	dimethylallyltranstransferase activity Inferred from electronic annotation. Source: EC geranyltranstransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 419

419

Farnesyl pyrophosphate synthase

PRO_0000123944

Sites

Metal binding

169

1

Magnesium 1

Metal binding

169

1

Magnesium 2

Metal binding

173

1

Magnesium 1

Metal binding

173

1

Magnesium 2

Metal binding

309

1

Magnesium 3

Binding site

123

1

Isopentenyl diphosphate

Binding site

126

1

Isopentenyl diphosphate

Binding site

162

1

Isopentenyl diphosphate

Binding site

178

1

Dimethylallyl diphosphate

Binding site

179

1

Isopentenyl diphosphate

Binding site

266

1

Dimethylallyl diphosphate

Binding site

267

1

Dimethylallyl diphosphate

Binding site

306

1

Dimethylallyl diphosphate

Binding site

323

1

Dimethylallyl diphosphate

Binding site

332

1

Dimethylallyl diphosphate By similarity

Site

164

1

Important for determining product chain length By similarity

Site

165

1

Important for determining product chain length By similarity

Amino acid modifications

Modified residue

123

1

N6-acetyllysine Ref.11

Modified residue

353

1

N6-acetyllysine Ref.11

Natural variations

Natural variant

364

1

V → A.
Corresponds to variant rs41314549 [ dbSNP | Ensembl ].

VAR_061274

Natural variant

391

1

I → V.
Corresponds to variant rs17456 [ dbSNP | Ensembl ].

VAR_049644

Experimental info

Sequence conflict

65

1

L → H in AAA52423. Ref.6

Sequence conflict

182

1

I → T in AAA52423. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

419

Helix Strand Turn

Details...

Helix

80 – 95

16

Helix

105 – 119

15

Helix

125 – 137

13

Helix

140 – 142

3

Helix

145 – 172

28

Helix

184 – 186

3

Turn

188 – 190

3

Helix

191 – 193

3

Helix

194 – 213

20

Helix

219 – 242

24

Helix

251 – 253

3

Helix

256 – 266

11

Helix

268 – 271

4

Helix

273 – 282

10

Helix

288 – 315

28

Helix

318 – 321

4

Turn

327 – 331

5

Helix

335 – 341

7

Helix

346 – 355

10

Helix

361 – 374

14

Helix

376 – 398

23

Helix

404 – 414

11

Sequences

	Sequence		Length	Mass (Da)
	P14324 [UniParc]. Last modified November 25, 2008. Version 4. Checksum: 52934B80A808FB67	FASTA	419	48,275
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 7584026] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[2]	"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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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. , 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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle.
[6]	"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: 1968462] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 65-419.
[7]	"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: 2690933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-419. Tissue: Liver.
[8]	"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: 11773414] [Abstract] Cited for: INTERACTION WITH HTLV-1 P13(II).
[9]	"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: 18005724] [Abstract] Cited for: INTERACTION WITH RSAD2, ENZYME REGULATION.
[10]	"Farnesyl diphosphate synthase; regulation of product specificity." Szkopinska A., Plochocka D. Acta Biochim. Pol. 52:45-55(2005) [PubMed: 15827605] [Abstract] Cited for: REVIEW.
[11]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123 AND LYS-353, MASS SPECTROMETRY.
[12]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"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: 16892359] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 72-419, SUBUNIT.
[14]	"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: 16684881] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 67-419 IN COMPLEXES WITH MAGNESIUM IONS; RISEDRONATE AND ZOLEDRONATE, CATALYTIC ACTIVITY.
[15]	"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. , Papapoulos S., Wang A.H.-J., Kubo T., Ochi M., Mukkamala D., Oldfield E. J. Am. Chem. Soc. 131:5153-5162(2009) [PubMed: 19309137] [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

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.
J05262 mRNA. Translation: AAA52423.1. Different initiation.
M29863 mRNA. Translation: AAA35820.1.

IPI

IPI00914566.

PIR

A35726.

RefSeq

NP_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.

UniGene

Hs.335918.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YQ7	X-ray	2.20	A	67-419	[»]
1YV5	X-ray	2.00	A	67-419	[»]
1ZW5	X-ray	2.30	A	67-419	[»]
2F7M	X-ray	2.30	F	72-419	[»]
2F89	X-ray	2.60	F	72-419	[»]
2F8C	X-ray	2.20	F	72-419	[»]
2F8Z	X-ray	2.60	F	72-419	[»]
2F92	X-ray	2.15	F	72-419	[»]
2F94	X-ray	1.94	F	72-419	[»]
2F9K	X-ray	2.06	F	72-419	[»]
2OPM	X-ray	2.40	A	67-419	[»]
2OPN	X-ray	2.70	A	67-419	[»]
2QIS	X-ray	1.80	A	67-419	[»]
2RAH	X-ray	2.00	A	67-419	[»]
2VF6	X-ray	2.10	A	67-419	[»]
3B7L	X-ray	1.95	A	67-419	[»]
3CP6	X-ray	1.95	A	67-419	[»]
3N1V	X-ray	2.18	F	72-419	[»]
3N1W	X-ray	2.56	F	72-419	[»]
3N3L	X-ray	2.74	F	72-419	[»]
3N45	X-ray	1.88	F	72-419	[»]
3N46	X-ray	2.35	F	72-419	[»]
3N49	X-ray	2.50	F	72-419	[»]
3N5H	X-ray	2.20	F	72-419	[»]
3N5J	X-ray	2.35	F	72-419	[»]
3N6K	X-ray	2.25	F	72-419	[»]
3RYE	X-ray	2.10	A	72-419	[»]
3S4J	X-ray	1.95	A	72-419	[»]

ProteinModelPortal

P14324.

SMR

P14324. Positions 74-416.

ModBase

Search...

Protein-protein interaction databases

IntAct

P14324. 5 interactions.

MINT

MINT-2858951.

STRING

P14324.

PTM databases

PhosphoSite

P14324.

Polymorphism databases

DMDM

215274250.

Proteomic databases

PRIDE

P14324.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000356657; ENSP00000349078; ENSG00000160752.
ENST00000368356; ENSP00000357340; ENSG00000160752.

GeneID

2224.

KEGG

hsa:2224.

UCSC

uc001fkd.1. human.

Organism-specific databases

CTD

2224.

GeneCards

GC01P155278.

H-InvDB

HIX0199817.

HGNC

HGNC:3631. FDPS.

HPA

HPA028200.

MIM

134629. gene.

neXtProt

NX_P14324.

PharmGKB

PA28075.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17911.

HOGENOM

HBG328346.

HOVERGEN

HBG005741.

InParanoid

P14324.

OMA

RDFMAVF.

OrthoDB

EOG4ZGPCS.

PhylomeDB

P14324.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000160752-MONOMER.

Reactome

REACT_22258. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

P14324.

Bgee

P14324.

CleanEx

HS_FDPS.

Genevestigator

P14324.

GermOnline

ENSG00000160752. Homo sapiens.

Family and domain databases

InterPro

IPR000092. Polyprenyl_synt.
IPR008949. Terpenoid_synth.
[Graphical view]

Gene3D

G3DSA:1.10.600.10. Terpenoid_synth. 1 hit.

KO

K00787.

Pfam

PF00348. polyprenyl_synt. 1 hit.
[Graphical view]

SUPFAM

SSF48576. Terpenoid_synth. 1 hit.

PROSITE

PS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00630. Alendronate.
DB00710. Ibandronate.
DB00282. Pamidronate.
DB00884. Risedronate.
DB00399. Zoledronate.

SOURCE

Search...

Entry information

Entry name

FPPS_HUMAN

Accession

Primary (citable) accession number: P14324
Secondary accession number(s): D3DV91, Q96G29

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	November 25, 2008
Last modified:	January 25, 2012
This is version 138 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.