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Protein

Farnesyl pyrophosphate synthase

Gene

FDPS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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.

Activity 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. Farnesyl pyrophosphate synthase (FDPS), Geranylgeranyl pyrophosphate synthase (GGPS1)
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. Farnesyl pyrophosphate synthase (FDPS), Geranylgeranyl pyrophosphate synthase (GGPS1)
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

  • dimethylallyltranstransferase activity Source: GO_Central
  • geranyltranstransferase activity Source: GO_Central
  • metal ion binding Source: UniProtKB-KW
  • RNA binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processCholesterol biosynthesis, Cholesterol metabolism, Host-virus interaction, Isoprene biosynthesis, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000160752-MONOMER
BRENDAi2.5.1.10 2681
ReactomeiR-HSA-191273 Cholesterol biosynthesis
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
SABIO-RKiP14324
UniPathwayi
UPA00259;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

EuPathDBiHostDB:ENSG00000160752.14
HGNCiHGNC:3631 FDPS
MIMi134629 gene
neXtProtiNX_P14324

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 PublicationCorresponds to variant dbSNP:rs863225241EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2224
MalaCardsiFDPS
MIMi616631 phenotype
OpenTargetsiENSG00000160752
Orphaneti79152 Disseminated superficial actinic porokeratosis
PharmGKBiPA28075

Chemistry databases

ChEMBLiCHEMBL1782
DrugBankiDB00630 Alendronic acid
DB01785 Dimethylallyl Diphosphate
DB07780 FARNESYL DIPHOSPHATE
DB02552 Geranyl Diphosphate
DB07841 GERANYLGERANYL DIPHOSPHATE
DB00710 Ibandronate
DB04714 ISOPENTENYL PYROPHOSPHATE
DB02508 Isopentyl Pyrophosphate
DB00282 Pamidronate
DB00884 Risedronate
DB00399 Zoledronic acid
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-acetylmethionine1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP14324
MaxQBiP14324
PaxDbiP14324
PeptideAtlasiP14324
PRIDEiP14324
ProteomicsDBi53046
TopDownProteomicsiP14324-1 [P14324-1]

PTM databases

iPTMnetiP14324
PhosphoSitePlusiP14324
SwissPalmiP14324

Expressioni

Gene expression databases

BgeeiENSG00000160752 Expressed in 231 organ(s), highest expression level in right adrenal gland
CleanExiHS_FDPS
ExpressionAtlasiP14324 baseline and differential
GenevisibleiP14324 HS

Organism-specific databases

HPAiHPA028200

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi108517, 85 interactors
DIPiDIP-50059N
IntActiP14324, 12 interactors
STRINGi9606.ENSP00000349078

Chemistry databases

BindingDBiP14324

Structurei

Secondary structure

1419
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
GeneTreeiENSGT00900000141074
HOGENOMiHOG000160912
HOVERGENiHBG005741
InParanoidiP14324
KOiK00787
OMAiKHSFIVI
OrthoDBiEOG091G0BPT
PhylomeDBiP14324
TreeFamiTF300897

Family and domain databases

Gene3Di1.10.600.10, 1 hit
InterProiView protein in InterPro
IPR008949 Isoprenoid_synthase_dom_sf
IPR000092 Polyprenyl_synt
IPR033749 Polyprenyl_synt_CS
PfamiView protein in Pfam
PF00348 polyprenyl_synt, 1 hit
SUPFAMiSSF48576 SSF48576, 1 hit
PROSITEiView protein in PROSITE
PS00723 POLYPRENYL_SYNTHASE_1, 1 hit
PS00444 POLYPRENYL_SYNTHASE_2, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

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

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WVN4A0A087WVN4_HUMAN
Farnesyl pyrophosphate synthase
FDPS
274Annotation score:
A0A087X1D8A0A087X1D8_HUMAN
Farnesyl pyrophosphate synthase
FDPS
174Annotation score:
A0A087X090A0A087X090_HUMAN
Farnesyl diphosphate synthase (Farn...
FDPS hCG_1997329
248Annotation score:
A0A087WTP2A0A087WTP2_HUMAN
Farnesyl pyrophosphate synthase
FDPS
80Annotation score:

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 PublicationCorresponds to variant dbSNP:rs863225241EnsemblClinVar.1
Natural variantiVAR_061274364V → A. Corresponds to variant dbSNP:rs41314549Ensembl.1
Natural variantiVAR_049644391I → V. Corresponds to variant dbSNP:rs17456Ensembl.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 No translation available.
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

Similar proteinsi

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 No translation available.
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[»]
5JA0X-ray1.90F67-419[»]
5JUZX-ray2.40F67-419[»]
5JV0X-ray2.40F67-419[»]
5JV1X-ray2.30F67-419[»]
5JV2X-ray2.30F67-419[»]
5KSXX-ray2.65F67-419[»]
5YGIX-ray2.18A72-419[»]
ProteinModelPortaliP14324
SMRiP14324
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108517, 85 interactors
DIPiDIP-50059N
IntActiP14324, 12 interactors
STRINGi9606.ENSP00000349078

Chemistry databases

BindingDBiP14324
ChEMBLiCHEMBL1782
DrugBankiDB00630 Alendronic acid
DB01785 Dimethylallyl Diphosphate
DB07780 FARNESYL DIPHOSPHATE
DB02552 Geranyl Diphosphate
DB07841 GERANYLGERANYL DIPHOSPHATE
DB00710 Ibandronate
DB04714 ISOPENTENYL PYROPHOSPHATE
DB02508 Isopentyl Pyrophosphate
DB00282 Pamidronate
DB00884 Risedronate
DB00399 Zoledronic acid
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
ProteomicsDBi53046
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
EuPathDBiHostDB:ENSG00000160752.14
GeneCardsiFDPS
H-InvDBiHIX0025342
HGNCiHGNC:3631 FDPS
HPAiHPA028200
MalaCardsiFDPS
MIMi134629 gene
616631 phenotype
neXtProtiNX_P14324
OpenTargetsiENSG00000160752
Orphaneti79152 Disseminated superficial actinic porokeratosis
PharmGKBiPA28075
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0711 Eukaryota
COG0142 LUCA
GeneTreeiENSGT00900000141074
HOGENOMiHOG000160912
HOVERGENiHBG005741
InParanoidiP14324
KOiK00787
OMAiKHSFIVI
OrthoDBiEOG091G0BPT
PhylomeDBiP14324
TreeFamiTF300897

Enzyme and pathway databases

UniPathwayi
UPA00259;UER00368

UPA00260;UER00369

BioCyciMetaCyc:ENSG00000160752-MONOMER
BRENDAi2.5.1.10 2681
ReactomeiR-HSA-191273 Cholesterol biosynthesis
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
SABIO-RKiP14324

Miscellaneous databases

ChiTaRSiFDPS human
EvolutionaryTraceiP14324
GenomeRNAii2224
PROiPR:P14324
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000160752 Expressed in 231 organ(s), highest expression level in right adrenal gland
CleanExiHS_FDPS
ExpressionAtlasiP14324 baseline and differential
GenevisibleiP14324 HS

Family and domain databases

Gene3Di1.10.600.10, 1 hit
InterProiView protein in InterPro
IPR008949 Isoprenoid_synthase_dom_sf
IPR000092 Polyprenyl_synt
IPR033749 Polyprenyl_synt_CS
PfamiView protein in Pfam
PF00348 polyprenyl_synt, 1 hit
SUPFAMiSSF48576 SSF48576, 1 hit
PROSITEiView protein in PROSITE
PS00723 POLYPRENYL_SYNTHASE_1, 1 hit
PS00444 POLYPRENYL_SYNTHASE_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiFPPS_HUMAN
AccessioniPrimary (citable) accession number: P14324
Secondary accession number(s): D3DV91, E9PCI9, Q96G29
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 25, 2008
Last modified: November 7, 2018
This is version 209 of the entry and version 4 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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