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P14324

- FPPS_HUMAN

UniProt

P14324 - FPPS_HUMAN

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Protein

Farnesyl pyrophosphate synthase

Gene

FDPS

Organism
Homo sapiens (Human)
Status
Reviewed - 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 Mg(2+) 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei123 – 1231Isopentenyl diphosphate
Binding sitei126 – 1261Isopentenyl diphosphate
Binding sitei162 – 1621Isopentenyl diphosphate
Sitei164 – 1641Important for determining product chain lengthBy similarity
Sitei165 – 1651Important for determining product chain lengthBy similarity
Metal bindingi169 – 1691Magnesium 1
Metal bindingi169 – 1691Magnesium 2
Metal bindingi173 – 1731Magnesium 1
Metal bindingi173 – 1731Magnesium 2
Binding sitei178 – 1781Dimethylallyl diphosphate
Binding sitei179 – 1791Isopentenyl diphosphate
Binding sitei266 – 2661Dimethylallyl diphosphate
Binding sitei267 – 2671Dimethylallyl diphosphate
Binding sitei306 – 3061Dimethylallyl diphosphate
Metal bindingi309 – 3091Magnesium 3
Binding sitei323 – 3231Dimethylallyl diphosphate
Binding sitei332 – 3321Dimethylallyl diphosphateBy similarity

GO - Molecular functioni

  1. dimethylallyltranstransferase activity Source: UniProtKB-EC
  2. geranyltranstransferase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW
  4. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. cholesterol biosynthetic process Source: Reactome
  2. farnesyl diphosphate biosynthetic process Source: UniProtKB-UniPathway
  3. geranyl diphosphate biosynthetic process Source: UniProtKB-UniPathway
  4. small molecule metabolic process Source: Reactome
  5. viral process Source: UniProtKB-KW
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.
ReactomeiREACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_9405. Cholesterol biosynthesis.
SABIO-RKP14324.
UniPathwayiUPA00259; UER00368.
UPA00260; UER00369.

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
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3631. FDPS.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. mitochondrion Source: Ensembl
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28075.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 419419Farnesyl pyrophosphate synthasePRO_0000123944Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei123 – 1231N6-acetyllysine; alternate1 Publication
Modified residuei123 – 1231N6-succinyllysine; alternateBy similarity
Modified residuei353 – 3531N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP14324.
PaxDbiP14324.
PRIDEiP14324.

PTM databases

PhosphoSiteiP14324.

Expressioni

Gene expression databases

BgeeiP14324.
CleanExiHS_FDPS.
GenevestigatoriP14324.

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. 15 interactions.
IntActiP14324. 5 interactions.
MINTiMINT-2858951.
STRINGi9606.ENSP00000349078.

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi75 – 9521Combined sources
Helixi97 – 1004Combined sources
Helixi102 – 1043Combined sources
Helixi105 – 11814Combined sources
Beta strandi119 – 1224Combined sources
Helixi125 – 13713Combined sources
Helixi140 – 1423Combined sources
Helixi145 – 17228Combined sources
Beta strandi176 – 1783Combined sources
Helixi184 – 1863Combined sources
Turni188 – 1903Combined sources
Helixi191 – 1933Combined sources
Helixi194 – 21320Combined sources
Helixi219 – 24325Combined sources
Beta strandi246 – 2483Combined sources
Helixi251 – 2533Combined sources
Helixi256 – 26611Combined sources
Helixi268 – 2714Combined sources
Helixi273 – 28210Combined sources
Helixi288 – 31528Combined sources
Helixi318 – 3214Combined sources
Turni327 – 3315Combined sources
Helixi335 – 3439Combined sources
Helixi346 – 35510Combined sources
Helixi361 – 37313Combined sources
Helixi376 – 39823Combined sources
Helixi404 – 41411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4P0VX-ray2.40A73-419[»]
4P0WX-ray2.41A72-419[»]
4P0XX-ray2.50A72-419[»]
ProteinModelPortaliP14324.
SMRiP14324. Positions 74-419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14324.

Family & Domainsi

Sequence similaritiesi

Belongs to the FPP/GGPP synthase family.Curated

Phylogenomic databases

eggNOGiCOG0142.
GeneTreeiENSGT00530000064127.
HOGENOMiHOG000160912.
HOVERGENiHBG005741.
InParanoidiP14324.
KOiK00787.
OMAiLEACYGR.
OrthoDBiEOG7W9RVG.
PhylomeDBiP14324.
TreeFamiTF300897.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR000092. Polyprenyl_synt.
IPR008949. Terpenoid_synth.
[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. Align

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 BAA03523.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411R → K in BQ062616. 1 PublicationCurated
Sequence conflicti182 – 1821I → T in AAA52423. (PubMed:1968462)Curated
Sequence conflicti284 – 2841G → R in BQ062616. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti364 – 3641V → A.
Corresponds to variant rs41314549 [ dbSNP | Ensembl ].
VAR_061274
Natural varianti391 – 3911I → V.
Corresponds to variant rs17456 [ dbSNP | Ensembl ].
VAR_049644

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6666Missing in isoform 2. 2 PublicationsVSP_046958Add
BLAST

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.2. human. [P14324-1]

Polymorphism databases

DMDMi215274250.

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 .
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. [P14324-2 ]
XP_005245020.1. XM_005244963.1. [P14324-2 ]
UniGenei Hs.335918.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
4P0V X-ray 2.40 A 73-419 [» ]
4P0W X-ray 2.41 A 72-419 [» ]
4P0X X-ray 2.50 A 72-419 [» ]
ProteinModelPortali P14324.
SMRi P14324. Positions 74-419.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108517. 15 interactions.
IntActi P14324. 5 interactions.
MINTi MINT-2858951.
STRINGi 9606.ENSP00000349078.

Chemistry

BindingDBi P14324.
ChEMBLi CHEMBL1782.
DrugBanki DB00630. Alendronate.
DB00710. Ibandronate.
DB00282. Pamidronate.
DB00884. Risedronate.
DB00399. Zoledronate.
GuidetoPHARMACOLOGYi 644.

PTM databases

PhosphoSitei P14324.

Polymorphism databases

DMDMi 215274250.

Proteomic databases

MaxQBi P14324.
PaxDbi P14324.
PRIDEi P14324.

Protocols and materials databases

DNASUi 2224.
Structural Biology Knowledgebase Search...

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.2. human. [P14324-1 ]

Organism-specific databases

CTDi 2224.
GeneCardsi GC01P155278.
H-InvDB HIX0025342.
HGNCi HGNC:3631. FDPS.
HPAi HPA028200.
MIMi 134629. gene.
neXtProti NX_P14324.
PharmGKBi PA28075.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0142.
GeneTreei ENSGT00530000064127.
HOGENOMi HOG000160912.
HOVERGENi HBG005741.
InParanoidi P14324.
KOi K00787.
OMAi LEACYGR.
OrthoDBi EOG7W9RVG.
PhylomeDBi P14324.
TreeFami TF300897.

Enzyme and pathway databases

UniPathwayi UPA00259 ; UER00368 .
UPA00260 ; UER00369 .
BioCyci MetaCyc:ENSG00000160752-MONOMER.
Reactomei REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_9405. Cholesterol biosynthesis.
SABIO-RK P14324.

Miscellaneous databases

ChiTaRSi FDPS. human.
EvolutionaryTracei P14324.
GenomeRNAii 2224.
NextBioi 9017.
PROi P14324.
SOURCEi Search...

Gene expression databases

Bgeei P14324.
CleanExi HS_FDPS.
Genevestigatori P14324.

Family and domain databases

Gene3Di 1.10.600.10. 1 hit.
InterProi IPR000092. Polyprenyl_synt.
IPR008949. Terpenoid_synth.
[Graphical view ]
Pfami PF00348. polyprenyl_synt. 1 hit.
[Graphical view ]
SUPFAMi SSF48576. SSF48576. 1 hit.
PROSITEi PS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Muscle.
  7. The MGC Project Team
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-312 (ISOFORM 2).
  8. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-419.
    Tissue: Liver.
  9. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTLV-1 P13(II).
  10. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RSAD2, ENZYME REGULATION.
  11. "Farnesyl diphosphate synthase; regulation of product specificity."
    Szkopinska A., Plochocka D.
    Acta Biochim. Pol. 52:45-55(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123 AND LYS-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 72-419, SUBUNIT.
  18. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 67-419 IN COMPLEXES WITH MAGNESIUM IONS; RISEDRONATE AND ZOLEDRONATE, CATALYTIC ACTIVITY.
  19. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 67-419 IN COMPLEXES WITH MAGNESIUM AND BIPHOSPHONATES.

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 26, 2014
This is version 168 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

External Data

Dasty 3