UniProtKB - P14324 (FPPS_HUMAN)
Protein
Farnesyl pyrophosphate synthase
Gene
FDPS
Organism
Homo sapiens (Human)
Status
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 = (2E)-geranyl diphosphate + diphosphate1 PublicationEC:2.5.1.11 Publication
- (2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate1 PublicationEC:2.5.1.101 Publication
Cofactori
Mg2+1 PublicationNote: Binds 2 Mg2+ ions per subunit.1 Publication
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
: farnesyl diphosphate biosynthesis Pathwayi
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:
- Farnesyl pyrophosphate synthase (FDPS), Geranylgeranyl pyrophosphate synthase (GGPS1)
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:
- Farnesyl pyrophosphate synthase (FDPS), Geranylgeranyl pyrophosphate synthase (GGPS1)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 123 | Isopentenyl diphosphateCombined sources1 Publication | 1 | |
Binding sitei | 126 | Isopentenyl diphosphateCombined sources1 Publication | 1 | |
Binding sitei | 162 | Isopentenyl diphosphateCombined sources1 Publication | 1 | |
Sitei | 164 | Important for determining product chain lengthBy similarity | 1 | |
Sitei | 165 | Important for determining product chain lengthBy similarity | 1 | |
Metal bindingi | 169 | Magnesium 1Combined sources1 Publication | 1 | |
Metal bindingi | 169 | Magnesium 2Combined sources1 Publication | 1 | |
Metal bindingi | 173 | Magnesium 1Combined sources1 Publication | 1 | |
Metal bindingi | 173 | Magnesium 2Combined sources1 Publication | 1 | |
Binding sitei | 178 | Dimethylallyl diphosphate | 1 | |
Binding sitei | 179 | Isopentenyl diphosphateCombined sources1 Publication | 1 | |
Binding sitei | 266 | Dimethylallyl diphosphate | 1 | |
Binding sitei | 267 | Dimethylallyl diphosphate | 1 | |
Binding sitei | 306 | Dimethylallyl diphosphate | 1 | |
Binding sitei | 323 | Dimethylallyl diphosphate | 1 | |
Binding sitei | 332 | Dimethylallyl diphosphateBy similarity | 1 |
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
- cholesterol biosynthetic process Source: Reactome
- farnesyl diphosphate biosynthetic process Source: GO_Central
- geranyl diphosphate biosynthetic process Source: UniProtKB-UniPathway
- regulation of cholesterol biosynthetic process Source: Reactome
- viral process Source: UniProtKB-KW
Keywordsi
Molecular function | Transferase |
Biological process | Cholesterol biosynthesis, Cholesterol metabolism, Host-virus interaction, Isoprene biosynthesis, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | MetaCyc:ENSG00000160752-MONOMER |
BRENDAi | 2.5.1.10, 2681 |
PathwayCommonsi | P14324 |
Reactomei | R-HSA-191273, Cholesterol biosynthesis R-HSA-2426168, Activation of gene expression by SREBF (SREBP) |
SABIO-RKi | P14324 |
UniPathwayi | UPA00259;UER00368 UPA00260;UER00369 |
Chemistry databases
SwissLipidsi | SLP:000001248 SLP:000001252 [P14324-2] |
Names & Taxonomyi
Protein namesi | |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000160752.14 |
HGNCi | HGNC:3631, FDPS |
MIMi | 134629, gene |
neXtProti | NX_P14324 |
Subcellular locationi
Other locations
Cytosol
- cytosol Source: HPA
Nucleus
- nucleoplasm Source: HPA
Other locations
- cytoplasm Source: GO_Central
Keywords - Cellular componenti
CytoplasmPathology & 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.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_075062 | 179 | R → Q in POROK9. 1 PublicationCorresponds to variant dbSNP:rs863225241EnsemblClinVar. | 1 |
Keywords - Diseasei
Disease mutationOrganism-specific databases
DisGeNETi | 2224 |
MalaCardsi | FDPS |
MIMi | 616631, phenotype |
OpenTargetsi | ENSG00000160752 |
Orphaneti | 79152, Disseminated superficial actinic porokeratosis |
PharmGKBi | PA28075 |
Miscellaneous databases
Pharosi | P14324, Tclin |
Chemistry databases
ChEMBLi | CHEMBL1782 |
DrugBanki | DB00630, Alendronic acid DB01785, Dimethylallyl Diphosphate DB07780, Farnesyl diphosphate DB02552, Geranyl Diphosphate DB07841, Geranylgeranyl diphosphate DB00710, Ibandronate DB06255, Incadronic acid DB04714, ISOPENTENYL PYROPHOSPHATE DB02508, Isopentyl Pyrophosphate DB06548, Minodronic acid DB00282, Pamidronic acid DB00884, Risedronic acid DB00399, Zoledronic acid |
DrugCentrali | P14324 |
GuidetoPHARMACOLOGYi | 644 |
Polymorphism and mutation databases
BioMutai | FDPS |
DMDMi | 215274250 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000123944 | 1 – 419 | Farnesyl pyrophosphate synthaseAdd BLAST | 419 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
---|---|---|---|---|---|
Modified residuei | 123 | N6-acetyllysineCombined sources | 1 | ||
Modified residuei | 353 | N6-acetyllysineCombined sources | 1 | ||
Isoform 2 (identifier: P14324-2) | |||||
Modified residuei | 1 | N-acetylmethionineCurated | 1 |
Keywords - PTMi
AcetylationProteomic databases
EPDi | P14324 |
jPOSTi | P14324 |
MassIVEi | P14324 |
MaxQBi | P14324 |
PaxDbi | P14324 |
PeptideAtlasi | P14324 |
PRIDEi | P14324 |
ProteomicsDBi | 19455 53046 [P14324-1] |
TopDownProteomicsi | P14324-1 [P14324-1] |
PTM databases
iPTMneti | P14324 |
MetOSitei | P14324 |
PhosphoSitePlusi | P14324 |
SwissPalmi | P14324 |
Expressioni
Gene expression databases
Bgeei | ENSG00000160752, Expressed in right adrenal gland and 244 other tissues |
ExpressionAtlasi | P14324, baseline and differential |
Genevisiblei | P14324, HS |
Organism-specific databases
HPAi | ENSG00000160752, Low tissue specificity |
Interactioni
Subunit structurei
Homodimer.
Interacts with RSAD2.
3 Publications(Microbial infection) Interacts with HTLV-1 protein p13(II).
1 PublicationBinary interactionsi
Hide detailsP14324
With | #Exp. | IntAct |
---|---|---|
ABHD16A [O95870] | 3 | EBI-948245,EBI-348517 |
RNF19B [Q6ZMZ0] | 3 | EBI-948245,EBI-2466594 |
SLC30A2 [Q9BRI3] | 3 | EBI-948245,EBI-8644112 |
SSMEM1 [Q8WWF3] | 3 | EBI-948245,EBI-17280858 |
Protein-protein interaction databases
BioGRIDi | 108517, 104 interactors |
DIPi | DIP-50059N |
IntActi | P14324, 33 interactors |
STRINGi | 9606.ENSP00000349078 |
Chemistry databases
BindingDBi | P14324 |
Miscellaneous databases
RNActi | P14324, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P14324 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P14324 |
Family & Domainsi
Sequence similaritiesi
Belongs to the FPP/GGPP synthase family.Curated
Phylogenomic databases
eggNOGi | KOG0711, Eukaryota |
GeneTreei | ENSGT00900000141074 |
HOGENOMi | CLU_028376_0_1_1 |
InParanoidi | P14324 |
OMAi | MDTIGGL |
OrthoDBi | 1066656at2759 |
PhylomeDBi | P14324 |
TreeFami | TF300897 |
Family and domain databases
CDDi | cd00685, Trans_IPPS_HT, 1 hit |
Gene3Di | 1.10.600.10, 1 hit |
InterProi | View protein in InterPro IPR008949, Isoprenoid_synthase_dom_sf IPR000092, Polyprenyl_synt IPR033749, Polyprenyl_synt_CS |
Pfami | View protein in Pfam PF00348, polyprenyl_synt, 1 hit |
SUPFAMi | SSF48576, SSF48576, 1 hit |
PROSITEi | View protein in PROSITE PS00723, POLYPRENYL_SYNTHASE_1, 1 hit PS00444, POLYPRENYL_SYNTHASE_2, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis 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 sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A087WVN4 | A0A087WVN4_HUMAN | Farnesyl pyrophosphate synthase | FDPS | 274 | Annotation score: | ||
A0A087X1D8 | A0A087X1D8_HUMAN | Farnesyl pyrophosphate synthase | FDPS | 174 | Annotation score: | ||
A0A087X090 | A0A087X090_HUMAN | Farnesyl diphosphate synthase (Farn... | FDPS hCG_1997329 | 248 | Annotation score: | ||
A0A087WTP2 | A0A087WTP2_HUMAN | Farnesyl pyrophosphate synthase | FDPS | 80 | Annotation score: |
Sequence cautioni
The sequence BAA03523 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 141 | R → K in BQ062616 (Ref. 7) Curated | 1 | |
Sequence conflicti | 182 | I → T in AAA52423 (PubMed:1968462).Curated | 1 | |
Sequence conflicti | 284 | G → R in BQ062616 (Ref. 7) Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_075062 | 179 | R → Q in POROK9. 1 PublicationCorresponds to variant dbSNP:rs863225241EnsemblClinVar. | 1 | |
Natural variantiVAR_061274 | 364 | V → A. Corresponds to variant dbSNP:rs41314549EnsemblClinVar. | 1 | |
Natural variantiVAR_049644 | 391 | I → V. Corresponds to variant dbSNP:rs17456Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_046958 | 1 – 66 | Missing in isoform 2. 2 PublicationsAdd BLAST | 66 |
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 |
CCDSi | CCDS1110.1 [P14324-1] CCDS44241.1 [P14324-2] |
PIRi | A35726 |
RefSeqi | NP_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 XP_005245020.1, XM_005244963.1 |
Genome annotation databases
Ensembli | ENST00000356657; ENSP00000349078; ENSG00000160752 [P14324-1] ENST00000368356; ENSP00000357340; ENSG00000160752 [P14324-1] ENST00000447866; ENSP00000391755; ENSG00000160752 [P14324-2] ENST00000467076; ENSP00000480142; ENSG00000160752 [P14324-2] ENST00000612683; ENSP00000478235; ENSG00000160752 [P14324-2] |
GeneIDi | 2224 |
KEGGi | hsa:2224 |
UCSCi | uc001fkc.3, human [P14324-1] |
Keywords - Coding sequence diversityi
Alternative splicing, PolymorphismSimilar 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 |
CCDSi | CCDS1110.1 [P14324-1] CCDS44241.1 [P14324-2] |
PIRi | A35726 |
RefSeqi | NP_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 XP_005245020.1, XM_005244963.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | 71-419 | [»] | |
3S4J | X-ray | 1.95 | A | 71-419 | [»] | |
4DEM | X-ray | 1.85 | F | 67-419 | [»] | |
4GA3 | X-ray | 2.39 | A | 72-419 | [»] | |
4H5C | X-ray | 2.02 | F | 67-419 | [»] | |
4H5D | X-ray | 2.02 | F | 67-419 | [»] | |
4H5E | X-ray | 2.04 | F | 67-419 | [»] | |
4JVJ | X-ray | 2.80 | F | 67-419 | [»] | |
4KFA | X-ray | 1.98 | A | 67-419 | [»] | |
4KPD | X-ray | 1.96 | A | 67-419 | [»] | |
4KPJ | X-ray | 1.95 | A | 67-419 | [»] | |
4KQ5 | X-ray | 2.40 | A | 67-419 | [»] | |
4KQS | X-ray | 1.97 | A | 67-419 | [»] | |
4KQU | X-ray | 2.07 | A | 67-419 | [»] | |
4L2X | X-ray | 2.55 | F | 67-419 | [»] | |
4LFV | X-ray | 2.00 | F | 67-419 | [»] | |
4LPG | X-ray | 2.35 | F | 67-419 | [»] | |
4LPH | X-ray | 2.30 | F | 67-419 | [»] | |
4N1Z | X-ray | 2.35 | F | 72-419 | [»] | |
4N9U | X-ray | 2.11 | A | 67-419 | [»] | |
4NFI | X-ray | 1.85 | F | 67-419 | [»] | |
4NFJ | X-ray | 2.05 | F | 67-419 | [»] | |
4NFK | X-ray | 1.85 | F | 67-419 | [»] | |
4NG6 | X-ray | 2.35 | A | 67-419 | [»] | |
4NKE | X-ray | 1.46 | A | 67-419 | [»] | |
4NKF | X-ray | 2.00 | A | 67-419 | [»] | |
4NUA | X-ray | 1.43 | A | 67-419 | [»] | |
4OGU | X-ray | 2.10 | A | 67-419 | [»] | |
4P0V | X-ray | 2.40 | A | 73-419 | [»] | |
4P0W | X-ray | 2.41 | A | 72-419 | [»] | |
4P0X | X-ray | 2.50 | A | 72-419 | [»] | |
4PVX | X-ray | 2.18 | F | 67-419 | [»] | |
4PVY | X-ray | 2.05 | F | 67-419 | [»] | |
4Q23 | X-ray | 1.98 | A | 67-419 | [»] | |
4QPF | X-ray | 1.59 | A | 67-419 | [»] | |
4QXS | X-ray | 1.90 | F | 67-419 | [»] | |
4RXA | X-ray | 2.20 | A | 72-419 | [»] | |
4XQR | X-ray | 2.15 | F | 67-419 | [»] | |
4XQS | X-ray | 2.30 | F | 67-419 | [»] | |
4XQT | X-ray | 2.10 | F | 67-419 | [»] | |
5CG5 | Other | 1.40 | A | 74-419 | [»] | |
5CG6 | Other | 1.70 | A | 74-419 | [»] | |
5DGM | X-ray | 2.86 | F | 72-419 | [»] | |
5DGN | X-ray | 2.08 | F | 72-419 | [»] | |
5DGS | X-ray | 2.62 | F | 72-419 | [»] | |
5DIQ | X-ray | 2.10 | F | 72-419 | [»] | |
5DJP | X-ray | 2.40 | F | 72-419 | [»] | |
5DJR | X-ray | 2.40 | F | 72-419 | [»] | |
5DJV | X-ray | 2.30 | F | 72-419 | [»] | |
5JA0 | X-ray | 1.90 | F | 67-419 | [»] | |
5JUZ | X-ray | 2.40 | F | 67-419 | [»] | |
5JV0 | X-ray | 2.40 | F | 67-419 | [»] | |
5JV1 | X-ray | 2.30 | F | 67-419 | [»] | |
5JV2 | X-ray | 2.30 | F | 67-419 | [»] | |
5KSX | X-ray | 2.65 | F | 67-419 | [»] | |
5YGI | X-ray | 2.18 | A | 72-419 | [»] | |
6N7Y | X-ray | 2.00 | F | 67-419 | [»] | |
6N7Z | X-ray | 2.55 | F | 67-419 | [»] | |
6N82 | X-ray | 2.00 | F | 67-419 | [»] | |
6N83 | X-ray | 2.00 | F | 67-419 | [»] | |
6OAG | X-ray | 2.30 | F | 67-419 | [»] | |
6OAH | X-ray | 2.20 | F | 67-419 | [»] | |
SMRi | P14324 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 108517, 104 interactors |
DIPi | DIP-50059N |
IntActi | P14324, 33 interactors |
STRINGi | 9606.ENSP00000349078 |
Chemistry databases
BindingDBi | P14324 |
ChEMBLi | CHEMBL1782 |
DrugBanki | DB00630, Alendronic acid DB01785, Dimethylallyl Diphosphate DB07780, Farnesyl diphosphate DB02552, Geranyl Diphosphate DB07841, Geranylgeranyl diphosphate DB00710, Ibandronate DB06255, Incadronic acid DB04714, ISOPENTENYL PYROPHOSPHATE DB02508, Isopentyl Pyrophosphate DB06548, Minodronic acid DB00282, Pamidronic acid DB00884, Risedronic acid DB00399, Zoledronic acid |
DrugCentrali | P14324 |
GuidetoPHARMACOLOGYi | 644 |
SwissLipidsi | SLP:000001248 SLP:000001252 [P14324-2] |
PTM databases
iPTMneti | P14324 |
MetOSitei | P14324 |
PhosphoSitePlusi | P14324 |
SwissPalmi | P14324 |
Polymorphism and mutation databases
BioMutai | FDPS |
DMDMi | 215274250 |
Proteomic databases
EPDi | P14324 |
jPOSTi | P14324 |
MassIVEi | P14324 |
MaxQBi | P14324 |
PaxDbi | P14324 |
PeptideAtlasi | P14324 |
PRIDEi | P14324 |
ProteomicsDBi | 19455 53046 [P14324-1] |
TopDownProteomicsi | P14324-1 [P14324-1] |
Protocols and materials databases
Antibodypediai | 34190, 370 antibodies |
DNASUi | 2224 |
Genome annotation databases
Ensembli | ENST00000356657; ENSP00000349078; ENSG00000160752 [P14324-1] ENST00000368356; ENSP00000357340; ENSG00000160752 [P14324-1] ENST00000447866; ENSP00000391755; ENSG00000160752 [P14324-2] ENST00000467076; ENSP00000480142; ENSG00000160752 [P14324-2] ENST00000612683; ENSP00000478235; ENSG00000160752 [P14324-2] |
GeneIDi | 2224 |
KEGGi | hsa:2224 |
UCSCi | uc001fkc.3, human [P14324-1] |
Organism-specific databases
CTDi | 2224 |
DisGeNETi | 2224 |
EuPathDBi | HostDB:ENSG00000160752.14 |
GeneCardsi | FDPS |
HGNCi | HGNC:3631, FDPS |
HPAi | ENSG00000160752, Low tissue specificity |
MalaCardsi | FDPS |
MIMi | 134629, gene 616631, phenotype |
neXtProti | NX_P14324 |
OpenTargetsi | ENSG00000160752 |
Orphaneti | 79152, Disseminated superficial actinic porokeratosis |
PharmGKBi | PA28075 |
HUGEi | Search... |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0711, Eukaryota |
GeneTreei | ENSGT00900000141074 |
HOGENOMi | CLU_028376_0_1_1 |
InParanoidi | P14324 |
OMAi | MDTIGGL |
OrthoDBi | 1066656at2759 |
PhylomeDBi | P14324 |
TreeFami | TF300897 |
Enzyme and pathway databases
UniPathwayi | UPA00259;UER00368 UPA00260;UER00369 |
BioCyci | MetaCyc:ENSG00000160752-MONOMER |
BRENDAi | 2.5.1.10, 2681 |
PathwayCommonsi | P14324 |
Reactomei | R-HSA-191273, Cholesterol biosynthesis R-HSA-2426168, Activation of gene expression by SREBF (SREBP) |
SABIO-RKi | P14324 |
Miscellaneous databases
BioGRID-ORCSi | 2224, 393 hits in 855 CRISPR screens |
ChiTaRSi | FDPS, human |
EvolutionaryTracei | P14324 |
GenomeRNAii | 2224 |
Pharosi | P14324, Tclin |
PROi | PR:P14324 |
RNActi | P14324, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000160752, Expressed in right adrenal gland and 244 other tissues |
ExpressionAtlasi | P14324, baseline and differential |
Genevisiblei | P14324, HS |
Family and domain databases
CDDi | cd00685, Trans_IPPS_HT, 1 hit |
Gene3Di | 1.10.600.10, 1 hit |
InterProi | View protein in InterPro IPR008949, Isoprenoid_synthase_dom_sf IPR000092, Polyprenyl_synt IPR033749, Polyprenyl_synt_CS |
Pfami | View protein in Pfam PF00348, polyprenyl_synt, 1 hit |
SUPFAMi | SSF48576, SSF48576, 1 hit |
PROSITEi | View protein in PROSITE PS00723, POLYPRENYL_SYNTHASE_1, 1 hit PS00444, POLYPRENYL_SYNTHASE_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | FPPS_HUMAN | |
Accessioni | P14324Primary (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: | December 2, 2020 | |
This is version 224 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | 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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations