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UniProtKB - P14324 (FPPS_HUMAN)

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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.

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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
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
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
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, 50 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
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

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
OMAiITAPEDH
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

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 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

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: July 18, 2018
This is version 207 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. 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

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