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P14324

- FPPS_HUMAN

UniProt

P14324 - FPPS_HUMAN

Protein

Farnesyl pyrophosphate synthase

Gene

FDPS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 4 (25 Nov 2008)
      Previous versions | rss
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    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

    Binds 3 magnesium 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

    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

    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

    ArrayExpressiP14324.
    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 – 9521
    Helixi97 – 1004
    Helixi102 – 1043
    Helixi105 – 11814
    Beta strandi119 – 1224
    Helixi125 – 13713
    Helixi140 – 1423
    Helixi145 – 17228
    Beta strandi176 – 1783
    Helixi184 – 1863
    Turni188 – 1903
    Helixi191 – 1933
    Helixi194 – 21320
    Helixi219 – 24325
    Beta strandi246 – 2483
    Helixi251 – 2533
    Helixi256 – 26611
    Helixi268 – 2714
    Helixi273 – 28210
    Helixi288 – 31528
    Helixi318 – 3214
    Turni327 – 3315
    Helixi335 – 3439
    Helixi346 – 35510
    Helixi361 – 37313
    Helixi376 – 39823
    Helixi404 – 41411

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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.
    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

    MPLSRWLRSV GVFLLPAPYW APRERWLGSL RRPSLVHGYP VLAWHSARCW    50
    CQAWTEEPRA LCSSLRMNGD QNSDVYAQEK QDFVQHFSQI VRVLTEDEMG 100
    HPEIGDAIAR LKEVLEYNAI GGKYNRGLTV VVAFRELVEP RKQDADSLQR 150
    AWTVGWCVEL LQAFFLVADD IMDSSLTRRG QICWYQKPGV GLDAINDANL 200
    LEACIYRLLK LYCREQPYYL NLIELFLQSS YQTEIGQTLD LLTAPQGNVD 250
    LVRFTEKRYK SIVKYKTAFY SFYLPIAAAM YMAGIDGEKE HANAKKILLE 300
    MGEFFQIQDD YLDLFGDPSV TGKIGTDIQD NKCSWLVVQC LQRATPEQYQ 350
    ILKENYGQKE AEKVARVKAL YEELDLPAVF LQYEEDSYSH IMALIEQYAA 400
    PLPPAVFLGL ARKIYKRRK 419
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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]
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 [» ]
    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 ]
    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.
    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

    ArrayExpressi P14324.
    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

    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: October 1, 2014
    This is version 166 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