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P37268

- FDFT_HUMAN

UniProt

P37268 - FDFT_HUMAN

Protein

Squalene synthase

Gene

FDFT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    2 farnesyl diphosphate + NAD(P)H = squalene + 2 diphosphate + NAD(P)+.

    Cofactori

    Magnesium.

    Pathwayi

    GO - Molecular functioni

    1. farnesyl-diphosphate farnesyltransferase activity Source: Reactome
    2. oxidoreductase activity Source: UniProtKB-KW
    3. squalene synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular lipid metabolic process Source: Reactome
    2. cholesterol biosynthetic process Source: Reactome
    3. farnesyl diphosphate metabolic process Source: Ensembl
    4. isoprenoid biosynthetic process Source: UniProtKB-KW
    5. small molecule metabolic process Source: Reactome
    6. steroid biosynthetic process Source: ProtInc

    Keywords - Molecular functioni

    Oxidoreductase, Transferase

    Keywords - Biological processi

    Cholesterol biosynthesis, Cholesterol metabolism, Isoprene biosynthesis, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

    Keywords - Ligandi

    Magnesium, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01329-MONOMER.
    ReactomeiREACT_116145. PPARA activates gene expression.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_9405. Cholesterol biosynthesis.
    SABIO-RKP37268.
    UniPathwayiUPA00767; UER00751.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Squalene synthase (EC:2.5.1.21)
    Short name:
    SQS
    Short name:
    SS
    Alternative name(s):
    FPP:FPP farnesyltransferase
    Farnesyl-diphosphate farnesyltransferase
    Gene namesi
    Name:FDFT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:3629. FDFT1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: HPA
    2. endoplasmic reticulum membrane Source: Reactome
    3. integral component of membrane Source: ProtInc

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28073.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 417417Squalene synthasePRO_0000067443Add
    BLAST

    Proteomic databases

    MaxQBiP37268.
    PaxDbiP37268.
    PeptideAtlasiP37268.
    PRIDEiP37268.

    PTM databases

    PhosphoSiteiP37268.

    Expressioni

    Gene expression databases

    ArrayExpressiP37268.
    BgeeiP37268.
    CleanExiHS_FDFT1.
    GenevestigatoriP37268.

    Organism-specific databases

    HPAiHPA008874.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi108516. 18 interactions.
    IntActiP37268. 9 interactions.
    MINTiMINT-1401726.
    STRINGi9606.ENSP00000220584.

    Structurei

    Secondary structure

    1
    417
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi38 – 5114
    Helixi52 – 543
    Helixi55 – 595
    Helixi65 – 8420
    Helixi90 – 10314
    Turni117 – 1193
    Helixi120 – 1234
    Helixi125 – 13410
    Helixi137 – 15620
    Helixi157 – 1593
    Helixi165 – 17511
    Helixi177 – 18913
    Beta strandi191 – 1933
    Helixi195 – 1995
    Helixi201 – 21818
    Helixi220 – 2256
    Helixi233 – 2364
    Turni237 – 2393
    Helixi243 – 2475
    Helixi249 – 2513
    Helixi252 – 26716
    Helixi270 – 2789
    Helixi283 – 30321
    Helixi307 – 3104
    Helixi318 – 32710
    Beta strandi328 – 3303
    Helixi331 – 34616
    Helixi356 – 36813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EZFX-ray2.15A/B/C31-370[»]
    3ASXX-ray2.00A31-370[»]
    3LEEX-ray3.20A/B/C/D/E/F31-370[»]
    3Q2ZX-ray2.00A31-370[»]
    3Q30X-ray2.00A31-370[»]
    3V66X-ray1.80A31-370[»]
    3VJ8X-ray1.52A31-370[»]
    3VJ9X-ray1.52A31-370[»]
    3VJAX-ray1.76A/B31-370[»]
    3VJBX-ray2.05A/B/C/D/E/F31-370[»]
    3VJCX-ray1.89A/B/C/D/E/F31-370[»]
    3WC9X-ray2.82A/B/C/D/E/F31-370[»]
    3WCDX-ray2.75A/B/C/D/E/F31-370[»]
    3WCFX-ray2.22A/B/C/D/E/F31-370[»]
    3WCHX-ray2.50A/B/C/D/E/F31-370[»]
    3WCIX-ray2.30A/B/C/D/E/F31-370[»]
    3WCJX-ray2.20A/B/C/D/E/F31-370[»]
    3WCLX-ray2.24A/B/C/D/E/F31-370[»]
    3WCMX-ray2.06A/B/C/D/E/F31-370[»]
    3WEFX-ray2.35A/B/C/D/E/F31-370[»]
    3WEGX-ray1.75A31-370[»]
    3WEHX-ray1.87A31-370[»]
    3WEIX-ray1.79A31-370[»]
    3WEJX-ray2.00A31-370[»]
    3WEKX-ray1.85A31-370[»]
    ProteinModelPortaliP37268.
    SMRiP37268. Positions 35-369.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP37268.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei284 – 30421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei384 – 40421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phytoene/squalene synthase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1562.
    HOVERGENiHBG002370.
    InParanoidiP37268.
    KOiK00801.
    OMAiEMRHAVC.
    PhylomeDBiP37268.
    TreeFamiTF105316.

    Family and domain databases

    Gene3Di1.10.600.10. 1 hit.
    InterProiIPR002060. Squ/phyt_synthse.
    IPR006449. Squal_synth.
    IPR019845. Squalene/phytoene_synthase_CS.
    IPR008949. Terpenoid_synth.
    [Graphical view]
    PfamiPF00494. SQS_PSY. 1 hit.
    [Graphical view]
    SUPFAMiSSF48576. SSF48576. 1 hit.
    TIGRFAMsiTIGR01559. squal_synth. 1 hit.
    PROSITEiPS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit.
    PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P37268-1) [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

    MEFVKCLGHP EEFYNLVRFR IGGKRKVMPK MDQDSLSSSL KTCYKYLNQT    50
    SRSFAAVIQA LDGEMRNAVC IFYLVLRALD TLEDDMTISV EKKVPLLHNF 100
    HSFLYQPDWR FMESKEKDRQ VLEDFPTISL EFRNLAEKYQ TVIADICRRM 150
    GIGMAEFLDK HVTSEQEWDK YCHYVAGLVG IGLSRLFSAS EFEDPLVGED 200
    TERANSMGLF LQKTNIIRDY LEDQQGGREF WPQEVWSRYV KKLGDFAKPE 250
    NIDLAVQCLN ELITNALHHI PDVITYLSRL RNQSVFNFCA IPQVMAIATL 300
    AACYNNQQVF KGAVKIRKGQ AVTLMMDATN MPAVKAIIYQ YMEEIYHRIP 350
    DSDPSSSKTR QIISTIRTQN LPNCQLISRS HYSPIYLSFV MLLAALSWQY 400
    LTTLSQVTED YVQTGEH 417
    Length:417
    Mass (Da):48,115
    Last modified:October 1, 1994 - v1
    Checksum:iD36CBC8382F827EC
    GO
    Isoform 2 (identifier: P37268-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-64: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:353
    Mass (Da):40,770
    Checksum:i45DC1E8B9F179D2B
    GO
    Isoform 3 (identifier: P37268-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-85: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:332
    Mass (Da):38,317
    Checksum:iD58BAF0FA5DC6E5F
    GO
    Isoform 4 (identifier: P37268-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-111: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:306
    Mass (Da):35,101
    Checksum:iC237E92AAE66264A
    GO
    Isoform 5 (identifier: P37268-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         128-170: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:374
    Mass (Da):43,060
    Checksum:iC9F61FDC11FAA49B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti353 – 3531D → N in AAB33404. (PubMed:7864626)Curated
    Sequence conflicti402 – 4021T → A in CAA48896. (PubMed:8294001)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti45 – 451K → R Influences plasma cholesterol levels; associated with increased total cholesterol and non-high-density lipoprotein cholesterol. 2 Publications
    Corresponds to variant rs11549147 [ dbSNP | Ensembl ].
    VAR_011786
    Natural varianti392 – 3921L → P.
    Corresponds to variant rs1804473 [ dbSNP | Ensembl ].
    VAR_011787

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 111111Missing in isoform 4. 1 PublicationVSP_056517Add
    BLAST
    Alternative sequencei1 – 8585Missing in isoform 3. 1 PublicationVSP_056282Add
    BLAST
    Alternative sequencei1 – 6464Missing in isoform 2. 1 PublicationVSP_056283Add
    BLAST
    Alternative sequencei128 – 17043Missing in isoform 5. 1 PublicationVSP_056518Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06070 mRNA. Translation: AAA60582.1.
    L06105 mRNA. Translation: AAA36645.1.
    X69141 mRNA. Translation: CAA48896.1.
    S76822 mRNA. Translation: AAB33404.1.
    AK057726 mRNA. Translation: BAG51957.1.
    AK293545 mRNA. Translation: BAH11529.1.
    AK296043 mRNA. Translation: BAG58807.1.
    AK300059 mRNA. Translation: BAG61868.1.
    AK315993 mRNA. Translation: BAH14364.1.
    AK316351 mRNA. Translation: BAH14722.1.
    AK316531 mRNA. Translation: BAH14902.1.
    AK316534 mRNA. Translation: BAH14905.1.
    AC069185 Genomic DNA. No translation available.
    BC003573 mRNA. Translation: AAH03573.1.
    BC009251 mRNA. Translation: AAH09251.1.
    BC029641 mRNA. Translation: AAH29641.1.
    CCDSiCCDS5985.1.
    PIRiA45998.
    I38245.
    I52090.
    RefSeqiNP_001274671.1. NM_001287742.1.
    NP_001274672.1. NM_001287743.1.
    NP_001274673.1. NM_001287744.1.
    NP_001274674.1. NM_001287745.1.
    NP_001274676.1. NM_001287747.1.
    NP_001274677.1. NM_001287748.1.
    NP_001274678.1. NM_001287749.1.
    NP_001274679.1. NM_001287750.1.
    NP_001274680.1. NM_001287751.1.
    NP_001274685.1. NM_001287756.1.
    NP_004453.3. NM_004462.4.
    UniGeneiHs.593928.

    Genome annotation databases

    EnsembliENST00000220584; ENSP00000220584; ENSG00000079459.
    ENST00000443614; ENSP00000390367; ENSG00000079459.
    ENST00000525777; ENSP00000436069; ENSG00000079459.
    ENST00000528812; ENSP00000431749; ENSG00000079459.
    ENST00000538689; ENSP00000444248; ENSG00000079459.
    GeneIDi2222.
    KEGGihsa:2222.
    UCSCiuc003wuh.3. human.

    Polymorphism databases

    DMDMi585126.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06070 mRNA. Translation: AAA60582.1 .
    L06105 mRNA. Translation: AAA36645.1 .
    X69141 mRNA. Translation: CAA48896.1 .
    S76822 mRNA. Translation: AAB33404.1 .
    AK057726 mRNA. Translation: BAG51957.1 .
    AK293545 mRNA. Translation: BAH11529.1 .
    AK296043 mRNA. Translation: BAG58807.1 .
    AK300059 mRNA. Translation: BAG61868.1 .
    AK315993 mRNA. Translation: BAH14364.1 .
    AK316351 mRNA. Translation: BAH14722.1 .
    AK316531 mRNA. Translation: BAH14902.1 .
    AK316534 mRNA. Translation: BAH14905.1 .
    AC069185 Genomic DNA. No translation available.
    BC003573 mRNA. Translation: AAH03573.1 .
    BC009251 mRNA. Translation: AAH09251.1 .
    BC029641 mRNA. Translation: AAH29641.1 .
    CCDSi CCDS5985.1.
    PIRi A45998.
    I38245.
    I52090.
    RefSeqi NP_001274671.1. NM_001287742.1.
    NP_001274672.1. NM_001287743.1.
    NP_001274673.1. NM_001287744.1.
    NP_001274674.1. NM_001287745.1.
    NP_001274676.1. NM_001287747.1.
    NP_001274677.1. NM_001287748.1.
    NP_001274678.1. NM_001287749.1.
    NP_001274679.1. NM_001287750.1.
    NP_001274680.1. NM_001287751.1.
    NP_001274685.1. NM_001287756.1.
    NP_004453.3. NM_004462.4.
    UniGenei Hs.593928.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EZF X-ray 2.15 A/B/C 31-370 [» ]
    3ASX X-ray 2.00 A 31-370 [» ]
    3LEE X-ray 3.20 A/B/C/D/E/F 31-370 [» ]
    3Q2Z X-ray 2.00 A 31-370 [» ]
    3Q30 X-ray 2.00 A 31-370 [» ]
    3V66 X-ray 1.80 A 31-370 [» ]
    3VJ8 X-ray 1.52 A 31-370 [» ]
    3VJ9 X-ray 1.52 A 31-370 [» ]
    3VJA X-ray 1.76 A/B 31-370 [» ]
    3VJB X-ray 2.05 A/B/C/D/E/F 31-370 [» ]
    3VJC X-ray 1.89 A/B/C/D/E/F 31-370 [» ]
    3WC9 X-ray 2.82 A/B/C/D/E/F 31-370 [» ]
    3WCD X-ray 2.75 A/B/C/D/E/F 31-370 [» ]
    3WCF X-ray 2.22 A/B/C/D/E/F 31-370 [» ]
    3WCH X-ray 2.50 A/B/C/D/E/F 31-370 [» ]
    3WCI X-ray 2.30 A/B/C/D/E/F 31-370 [» ]
    3WCJ X-ray 2.20 A/B/C/D/E/F 31-370 [» ]
    3WCL X-ray 2.24 A/B/C/D/E/F 31-370 [» ]
    3WCM X-ray 2.06 A/B/C/D/E/F 31-370 [» ]
    3WEF X-ray 2.35 A/B/C/D/E/F 31-370 [» ]
    3WEG X-ray 1.75 A 31-370 [» ]
    3WEH X-ray 1.87 A 31-370 [» ]
    3WEI X-ray 1.79 A 31-370 [» ]
    3WEJ X-ray 2.00 A 31-370 [» ]
    3WEK X-ray 1.85 A 31-370 [» ]
    ProteinModelPortali P37268.
    SMRi P37268. Positions 35-369.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108516. 18 interactions.
    IntActi P37268. 9 interactions.
    MINTi MINT-1401726.
    STRINGi 9606.ENSP00000220584.

    Chemistry

    BindingDBi P37268.
    ChEMBLi CHEMBL3338.
    GuidetoPHARMACOLOGYi 645.

    PTM databases

    PhosphoSitei P37268.

    Polymorphism databases

    DMDMi 585126.

    Proteomic databases

    MaxQBi P37268.
    PaxDbi P37268.
    PeptideAtlasi P37268.
    PRIDEi P37268.

    Protocols and materials databases

    DNASUi 2222.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000220584 ; ENSP00000220584 ; ENSG00000079459 .
    ENST00000443614 ; ENSP00000390367 ; ENSG00000079459 .
    ENST00000525777 ; ENSP00000436069 ; ENSG00000079459 .
    ENST00000528812 ; ENSP00000431749 ; ENSG00000079459 .
    ENST00000538689 ; ENSP00000444248 ; ENSG00000079459 .
    GeneIDi 2222.
    KEGGi hsa:2222.
    UCSCi uc003wuh.3. human.

    Organism-specific databases

    CTDi 2222.
    GeneCardsi GC08P011653.
    H-InvDB HIX0168873.
    HGNCi HGNC:3629. FDFT1.
    HPAi HPA008874.
    MIMi 184420. gene.
    neXtProti NX_P37268.
    PharmGKBi PA28073.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1562.
    HOVERGENi HBG002370.
    InParanoidi P37268.
    KOi K00801.
    OMAi EMRHAVC.
    PhylomeDBi P37268.
    TreeFami TF105316.

    Enzyme and pathway databases

    UniPathwayi UPA00767 ; UER00751 .
    BioCyci MetaCyc:HS01329-MONOMER.
    Reactomei REACT_116145. PPARA activates gene expression.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_9405. Cholesterol biosynthesis.
    SABIO-RK P37268.

    Miscellaneous databases

    ChiTaRSi FDFT1. human.
    EvolutionaryTracei P37268.
    GenomeRNAii 2222.
    NextBioi 9013.
    PROi P37268.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P37268.
    Bgeei P37268.
    CleanExi HS_FDFT1.
    Genevestigatori P37268.

    Family and domain databases

    Gene3Di 1.10.600.10. 1 hit.
    InterProi IPR002060. Squ/phyt_synthse.
    IPR006449. Squal_synth.
    IPR019845. Squalene/phytoene_synthase_CS.
    IPR008949. Terpenoid_synth.
    [Graphical view ]
    Pfami PF00494. SQS_PSY. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48576. SSF48576. 1 hit.
    TIGRFAMsi TIGR01559. squal_synth. 1 hit.
    PROSITEi PS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit.
    PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Conservation between human and fungal squalene synthetases: similarities in structure, function, and regulation."
      Robinson G.W., Tsay Y.H., Kienzle B.K., Smith-Monroy C.A., Bishop R.W.
      Mol. Cell. Biol. 13:2706-2717(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Transcriptional regulation by lovastatin and 25-hydroxycholesterol in HepG2 cells and molecular cloning and expression of the cDNA for the human hepatic squalene synthase."
      Jiang G., McKenzie T.L., Conrad D.G., Shechter I.
      J. Biol. Chem. 268:12818-12824(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    3. "Cloning, expression and characterisation of the cDNA encoding human hepatic squalene synthase, and its relationship to phytoene synthase."
      Summers C., Karst F., Charles A.D.
      Gene 136:185-192(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    4. "Expression, purification, and characterization of the human squalene synthase: use of yeast and baculoviral systems."
      Soltis D.A., McMahon G., Caplan S.L., Dudas D.A., Chamberlin H.A., Vattay A., Dottavio D., Rucker M.L., Engstrom R.G., Cornell-Kennon S.A.
      Arch. Biochem. Biophys. 316:713-723(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    5. "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] (ISOFORMS 2; 3; 4 AND 5).
      Tissue: Cerebellum, Pericardium, Subthalamic nucleus and Uterus.
    6. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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), VARIANT ARG-45.
      Tissue: Lung, Muscle and Urinary bladder.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Crystal structure of human squalene synthase. A key enzyme in cholesterol biosynthesis."
      Pandit J., Danley D.E., Schulte G.K., Mazzalupo S., Pauly T.A., Hayward C.M., Hamanaka E.S., Thompson J.F., Harwood H.J. Jr.
      J. Biol. Chem. 275:30610-30617(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 39-370.
    10. "K45R variant of squalene synthase increases total cholesterol levels in two study samples from a French Canadian population."
      Do R., Pare G., Montpetit A., Hudson T.J., Gaudet D., Engert J.C.
      Hum. Mutat. 29:689-694(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ARG-45, ASSOCIATION WITH PLASMA CHOLESTEROL LEVELS.

    Entry informationi

    Entry nameiFDFT_HUMAN
    AccessioniPrimary (citable) accession number: P37268
    Secondary accession number(s): B3KQ95
    , B4DJE5, B4DT56, B7Z1J3, Q96GT0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 156 of the entry and version 1 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, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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