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Protein

Farnesyl pyrophosphate synthase

Gene

FDPS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate.1 Publication
Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate.1 Publication

Cofactori

Mg2+Note: Binds 3 Mg2+ ions per subunit.

Enzyme regulationi

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.1 Publication

Pathwayi: farnesyl diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Geranylgeranyl pyrophosphate synthase (GGPS1), Farnesyl pyrophosphate synthase (FDPS)
This subpathway is part of the pathway farnesyl diphosphate biosynthesis, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate, the pathway farnesyl diphosphate biosynthesis and in Isoprenoid biosynthesis.

Pathwayi: geranyl diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Geranylgeranyl pyrophosphate synthase (GGPS1), Farnesyl pyrophosphate synthase (FDPS)
This subpathway is part of the pathway geranyl diphosphate biosynthesis, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate, the pathway geranyl diphosphate biosynthesis and in Isoprenoid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei123Isopentenyl diphosphate1
Binding sitei126Isopentenyl diphosphate1
Binding sitei162Isopentenyl diphosphate1
Sitei164Important for determining product chain lengthBy similarity1
Sitei165Important for determining product chain lengthBy similarity1
Metal bindingi169Magnesium 11
Metal bindingi169Magnesium 21
Metal bindingi173Magnesium 11
Metal bindingi173Magnesium 21
Binding sitei178Dimethylallyl diphosphate1
Binding sitei179Isopentenyl diphosphate1
Binding sitei266Dimethylallyl diphosphate1
Binding sitei267Dimethylallyl diphosphate1
Binding sitei306Dimethylallyl diphosphate1
Metal bindingi309Magnesium 31
Binding sitei323Dimethylallyl diphosphate1
Binding sitei332Dimethylallyl diphosphateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Cholesterol biosynthesis, Cholesterol metabolism, Host-virus interaction, Isoprene biosynthesis, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000160752-MONOMER.
ZFISH:ENSG00000160752-MONOMER.
BRENDAi2.5.1.10. 2681.
ReactomeiR-HSA-191273. Cholesterol biosynthesis.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
SABIO-RKP14324.
UniPathwayiUPA00259; UER00368.
UPA00260; UER00369.

Chemistry databases

SwissLipidsiSLP:000001248.
SLP:000001252. [P14324-2]

Names & Taxonomyi

Protein namesi
Recommended name:
Farnesyl pyrophosphate synthase (EC:2.5.1.10)
Short name:
FPP synthase
Short name:
FPS
Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase
Dimethylallyltranstransferase (EC:2.5.1.1)
Farnesyl diphosphate synthase
Geranyltranstransferase
Gene namesi
Name:FDPS
Synonyms:FPS, KIAA1293
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3631. FDPS.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Porokeratosis 9, multiple types (POROK9)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:616631
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075062179R → Q in POROK9. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2224.
MIMi616631. phenotype.
OpenTargetsiENSG00000160752.
PharmGKBiPA28075.

Chemistry databases

ChEMBLiCHEMBL1782.
DrugBankiDB00630. Alendronate.
DB00710. Ibandronate.
DB00282. Pamidronate.
DB00884. Risedronate.
DB00399. Zoledronate.
GuidetoPHARMACOLOGYi644.

Polymorphism and mutation databases

BioMutaiFDPS.
DMDMi215274250.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001239441 – 419Farnesyl pyrophosphate synthaseAdd BLAST419

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei123N6-acetyllysineCombined sources1
Modified residuei353N6-acetyllysineCombined sources1
Isoform 2 (identifier: P14324-2)
Modified residuei1N-acetylmethionineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP14324.
MaxQBiP14324.
PaxDbiP14324.
PeptideAtlasiP14324.
PRIDEiP14324.
TopDownProteomicsiP14324-1. [P14324-1]

PTM databases

iPTMnetiP14324.
PhosphoSitePlusiP14324.
SwissPalmiP14324.

Expressioni

Gene expression databases

BgeeiENSG00000160752.
CleanExiHS_FDPS.
ExpressionAtlasiP14324. baseline and differential.
GenevisibleiP14324. HS.

Organism-specific databases

HPAiHPA028200.

Interactioni

Subunit structurei

Homodimer. Interacts with RSAD2. Interacts with HTLV-1 protein p13(II).3 Publications

Protein-protein interaction databases

BioGridi108517. 49 interactors.
DIPiDIP-50059N.
IntActiP14324. 6 interactors.
MINTiMINT-2858951.
STRINGi9606.ENSP00000349078.

Chemistry databases

BindingDBiP14324.

Structurei

Secondary structure

1419
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi76 – 85Combined sources10
Helixi87 – 94Combined sources8
Helixi97 – 100Combined sources4
Helixi102 – 104Combined sources3
Helixi105 – 118Combined sources14
Beta strandi119 – 122Combined sources4
Helixi125 – 137Combined sources13
Helixi140 – 142Combined sources3
Helixi145 – 172Combined sources28
Beta strandi176 – 178Combined sources3
Helixi184 – 186Combined sources3
Turni188 – 190Combined sources3
Helixi191 – 193Combined sources3
Helixi194 – 213Combined sources20
Helixi219 – 243Combined sources25
Beta strandi246 – 248Combined sources3
Helixi251 – 253Combined sources3
Helixi256 – 266Combined sources11
Helixi268 – 271Combined sources4
Helixi273 – 282Combined sources10
Helixi288 – 315Combined sources28
Helixi318 – 321Combined sources4
Turni327 – 331Combined sources5
Helixi335 – 343Combined sources9
Helixi346 – 355Combined sources10
Helixi361 – 373Combined sources13
Helixi376 – 398Combined sources23
Helixi404 – 414Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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-ray2.10A71-419[»]
3S4JX-ray1.95A71-419[»]
4DEMX-ray1.85F67-419[»]
4GA3X-ray2.39A72-419[»]
4H5CX-ray2.02F67-419[»]
4H5DX-ray2.02F67-419[»]
4H5EX-ray2.04F67-419[»]
4JVJX-ray2.80F67-419[»]
4KFAX-ray1.98A67-419[»]
4KPDX-ray1.96A67-419[»]
4KPJX-ray1.95A67-419[»]
4KQ5X-ray2.40A67-419[»]
4KQSX-ray1.97A67-419[»]
4KQUX-ray2.07A67-419[»]
4L2XX-ray2.55F67-419[»]
4LFVX-ray2.00F67-419[»]
4LPGX-ray2.35F67-419[»]
4LPHX-ray2.30F67-419[»]
4N1ZX-ray2.35F72-419[»]
4N9UX-ray2.11A67-419[»]
4NFIX-ray1.85F67-419[»]
4NFJX-ray2.05F67-419[»]
4NFKX-ray1.85F67-419[»]
4NG6X-ray2.35A67-419[»]
4NKEX-ray1.46A67-419[»]
4NKFX-ray2.00A67-419[»]
4NUAX-ray1.43A67-419[»]
4OGUX-ray2.10A67-419[»]
4P0VX-ray2.40A73-419[»]
4P0WX-ray2.41A72-419[»]
4P0XX-ray2.50A72-419[»]
4PVXX-ray2.18F67-419[»]
4PVYX-ray2.05F67-419[»]
4Q23X-ray1.98A67-419[»]
4QPFX-ray1.59A67-419[»]
4QXSX-ray1.90F67-419[»]
4RXAX-ray2.20A72-419[»]
4XQRX-ray2.15F67-419[»]
4XQSX-ray2.30F67-419[»]
4XQTX-ray2.10F67-419[»]
5CG5Other1.40A74-419[»]
5CG6Other1.70A74-419[»]
5DGMX-ray2.86F72-419[»]
5DGNX-ray2.08F72-419[»]
5DGSX-ray2.62F72-419[»]
5DIQX-ray2.10F72-419[»]
5DJPX-ray2.40F72-419[»]
5DJRX-ray2.40F72-419[»]
5DJVX-ray2.30F72-419[»]
ProteinModelPortaliP14324.
SMRiP14324.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14324.

Family & Domainsi

Sequence similaritiesi

Belongs to the FPP/GGPP synthase family.Curated

Phylogenomic databases

eggNOGiKOG0711. Eukaryota.
COG0142. LUCA.
GeneTreeiENSGT00850000132366.
HOGENOMiHOG000160912.
HOVERGENiHBG005741.
InParanoidiP14324.
KOiK00787.
OMAiRMAGVTD.
OrthoDBiEOG091G0BPT.
PhylomeDBiP14324.
TreeFamiTF300897.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR000092. Polyprenyl_synt.
IPR033749. Polyprenyl_synt_CS.
[Graphical view]
PfamiPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
PROSITEiPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P14324-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MPLSRWLRSV GVFLLPAPYW APRERWLGSL RRPSLVHGYP VLAWHSARCW
60 70 80 90 100
CQAWTEEPRA LCSSLRMNGD QNSDVYAQEK QDFVQHFSQI VRVLTEDEMG
110 120 130 140 150
HPEIGDAIAR LKEVLEYNAI GGKYNRGLTV VVAFRELVEP RKQDADSLQR
160 170 180 190 200
AWTVGWCVEL LQAFFLVADD IMDSSLTRRG QICWYQKPGV GLDAINDANL
210 220 230 240 250
LEACIYRLLK LYCREQPYYL NLIELFLQSS YQTEIGQTLD LLTAPQGNVD
260 270 280 290 300
LVRFTEKRYK SIVKYKTAFY SFYLPIAAAM YMAGIDGEKE HANAKKILLE
310 320 330 340 350
MGEFFQIQDD YLDLFGDPSV TGKIGTDIQD NKCSWLVVQC LQRATPEQYQ
360 370 380 390 400
ILKENYGQKE AEKVARVKAL YEELDLPAVF LQYEEDSYSH IMALIEQYAA
410
PLPPAVFLGL ARKIYKRRK
Length:419
Mass (Da):48,275
Last modified:November 25, 2008 - v4
Checksum:i52934B80A808FB67
GO
Isoform 2 (identifier: P14324-2) [UniParc]FASTAAdd to basket

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

Show »
Length:353
Mass (Da):40,532
Checksum:i15B19F2A5C51B166
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti141R → K in BQ062616 (Ref. 7) Curated1
Sequence conflicti182I → T in AAA52423 (PubMed:1968462).Curated1
Sequence conflicti284G → R in BQ062616 (Ref. 7) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075062179R → Q in POROK9. 1 Publication1
Natural variantiVAR_061274364V → A.Corresponds to variant rs41314549dbSNPEnsembl.1
Natural variantiVAR_049644391I → V.Corresponds to variant rs17456dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0469581 – 66Missing in isoform 2. 2 PublicationsAdd BLAST66

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1110.1. [P14324-1]
CCDS44241.1. [P14324-2]
PIRiA35726.
RefSeqiNP_001129293.1. NM_001135821.1. [P14324-1]
NP_001129294.1. NM_001135822.1. [P14324-2]
NP_001229753.1. NM_001242824.1. [P14324-2]
NP_001229754.1. NM_001242825.1.
NP_001995.1. NM_002004.3. [P14324-1]
XP_005245019.1. XM_005244962.1. [P14324-2]
XP_005245020.1. XM_005244963.1. [P14324-2]
UniGeneiHs.335918.

Genome annotation databases

EnsembliENST00000356657; ENSP00000349078; ENSG00000160752. [P14324-1]
ENST00000368356; ENSP00000357340; ENSG00000160752. [P14324-1]
ENST00000447866; ENSP00000391755; ENSG00000160752. [P14324-2]
ENST00000467076; ENSP00000480142; ENSG00000160752. [P14324-2]
ENST00000612683; ENSP00000478235; ENSG00000160752. [P14324-2]
GeneIDi2224.
KEGGihsa:2224.
UCSCiuc001fkc.3. human. [P14324-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1110.1. [P14324-1]
CCDS44241.1. [P14324-2]
PIRiA35726.
RefSeqiNP_001129293.1. NM_001135821.1. [P14324-1]
NP_001129294.1. NM_001135822.1. [P14324-2]
NP_001229753.1. NM_001242824.1. [P14324-2]
NP_001229754.1. NM_001242825.1.
NP_001995.1. NM_002004.3. [P14324-1]
XP_005245019.1. XM_005244962.1. [P14324-2]
XP_005245020.1. XM_005244963.1. [P14324-2]
UniGeneiHs.335918.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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-ray2.10A71-419[»]
3S4JX-ray1.95A71-419[»]
4DEMX-ray1.85F67-419[»]
4GA3X-ray2.39A72-419[»]
4H5CX-ray2.02F67-419[»]
4H5DX-ray2.02F67-419[»]
4H5EX-ray2.04F67-419[»]
4JVJX-ray2.80F67-419[»]
4KFAX-ray1.98A67-419[»]
4KPDX-ray1.96A67-419[»]
4KPJX-ray1.95A67-419[»]
4KQ5X-ray2.40A67-419[»]
4KQSX-ray1.97A67-419[»]
4KQUX-ray2.07A67-419[»]
4L2XX-ray2.55F67-419[»]
4LFVX-ray2.00F67-419[»]
4LPGX-ray2.35F67-419[»]
4LPHX-ray2.30F67-419[»]
4N1ZX-ray2.35F72-419[»]
4N9UX-ray2.11A67-419[»]
4NFIX-ray1.85F67-419[»]
4NFJX-ray2.05F67-419[»]
4NFKX-ray1.85F67-419[»]
4NG6X-ray2.35A67-419[»]
4NKEX-ray1.46A67-419[»]
4NKFX-ray2.00A67-419[»]
4NUAX-ray1.43A67-419[»]
4OGUX-ray2.10A67-419[»]
4P0VX-ray2.40A73-419[»]
4P0WX-ray2.41A72-419[»]
4P0XX-ray2.50A72-419[»]
4PVXX-ray2.18F67-419[»]
4PVYX-ray2.05F67-419[»]
4Q23X-ray1.98A67-419[»]
4QPFX-ray1.59A67-419[»]
4QXSX-ray1.90F67-419[»]
4RXAX-ray2.20A72-419[»]
4XQRX-ray2.15F67-419[»]
4XQSX-ray2.30F67-419[»]
4XQTX-ray2.10F67-419[»]
5CG5Other1.40A74-419[»]
5CG6Other1.70A74-419[»]
5DGMX-ray2.86F72-419[»]
5DGNX-ray2.08F72-419[»]
5DGSX-ray2.62F72-419[»]
5DIQX-ray2.10F72-419[»]
5DJPX-ray2.40F72-419[»]
5DJRX-ray2.40F72-419[»]
5DJVX-ray2.30F72-419[»]
ProteinModelPortaliP14324.
SMRiP14324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108517. 49 interactors.
DIPiDIP-50059N.
IntActiP14324. 6 interactors.
MINTiMINT-2858951.
STRINGi9606.ENSP00000349078.

Chemistry databases

BindingDBiP14324.
ChEMBLiCHEMBL1782.
DrugBankiDB00630. Alendronate.
DB00710. Ibandronate.
DB00282. Pamidronate.
DB00884. Risedronate.
DB00399. Zoledronate.
GuidetoPHARMACOLOGYi644.
SwissLipidsiSLP:000001248.
SLP:000001252. [P14324-2]

PTM databases

iPTMnetiP14324.
PhosphoSitePlusiP14324.
SwissPalmiP14324.

Polymorphism and mutation databases

BioMutaiFDPS.
DMDMi215274250.

Proteomic databases

EPDiP14324.
MaxQBiP14324.
PaxDbiP14324.
PeptideAtlasiP14324.
PRIDEiP14324.
TopDownProteomicsiP14324-1. [P14324-1]

Protocols and materials databases

DNASUi2224.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356657; ENSP00000349078; ENSG00000160752. [P14324-1]
ENST00000368356; ENSP00000357340; ENSG00000160752. [P14324-1]
ENST00000447866; ENSP00000391755; ENSG00000160752. [P14324-2]
ENST00000467076; ENSP00000480142; ENSG00000160752. [P14324-2]
ENST00000612683; ENSP00000478235; ENSG00000160752. [P14324-2]
GeneIDi2224.
KEGGihsa:2224.
UCSCiuc001fkc.3. human. [P14324-1]

Organism-specific databases

CTDi2224.
DisGeNETi2224.
GeneCardsiFDPS.
H-InvDBHIX0025342.
HGNCiHGNC:3631. FDPS.
HPAiHPA028200.
MIMi134629. gene.
616631. phenotype.
neXtProtiNX_P14324.
OpenTargetsiENSG00000160752.
PharmGKBiPA28075.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0711. Eukaryota.
COG0142. LUCA.
GeneTreeiENSGT00850000132366.
HOGENOMiHOG000160912.
HOVERGENiHBG005741.
InParanoidiP14324.
KOiK00787.
OMAiRMAGVTD.
OrthoDBiEOG091G0BPT.
PhylomeDBiP14324.
TreeFamiTF300897.

Enzyme and pathway databases

UniPathwayiUPA00259; UER00368.
UPA00260; UER00369.
BioCyciMetaCyc:ENSG00000160752-MONOMER.
ZFISH:ENSG00000160752-MONOMER.
BRENDAi2.5.1.10. 2681.
ReactomeiR-HSA-191273. Cholesterol biosynthesis.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
SABIO-RKP14324.

Miscellaneous databases

ChiTaRSiFDPS. human.
EvolutionaryTraceiP14324.
GenomeRNAii2224.
PROiP14324.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000160752.
CleanExiHS_FDPS.
ExpressionAtlasiP14324. baseline and differential.
GenevisibleiP14324. HS.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR000092. Polyprenyl_synt.
IPR033749. Polyprenyl_synt_CS.
[Graphical view]
PfamiPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
PROSITEiPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFPPS_HUMAN
AccessioniPrimary (citable) accession number: P14324
Secondary accession number(s): D3DV91, E9PCI9, Q96G29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 191 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.