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P37268 (FDFT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Squalene synthase

Short name=SQS
Short name=SS
EC=2.5.1.21
Alternative name(s):
FPP:FPP farnesyltransferase
Farnesyl-diphosphate farnesyltransferase
Gene names
Name:FDFT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Magnesium.

Pathway

Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3.

Subunit structure

Monomer By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the phytoene/squalene synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 417417Squalene synthase
PRO_0000067443

Regions

Transmembrane284 – 30421Helical; Potential
Transmembrane384 – 40421Helical; Potential

Natural variations

Natural variant451K → R Influences plasma cholesterol levels; associated with increased total cholesterol and non-high-density lipoprotein cholesterol. Ref.5 Ref.8
Corresponds to variant rs11549147 [ dbSNP | Ensembl ].
VAR_011786
Natural variant3921L → P.
Corresponds to variant rs1804473 [ dbSNP | Ensembl ].
VAR_011787

Experimental info

Sequence conflict3531D → N in AAB33404. Ref.4
Sequence conflict4021T → A in CAA48896. Ref.3

Secondary structure

............................................... 417
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37268 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: D36CBC8382F827EC

FASTA41748,115
        10         20         30         40         50         60 
MEFVKCLGHP EEFYNLVRFR IGGKRKVMPK MDQDSLSSSL KTCYKYLNQT SRSFAAVIQA 

        70         80         90        100        110        120 
LDGEMRNAVC IFYLVLRALD TLEDDMTISV EKKVPLLHNF HSFLYQPDWR FMESKEKDRQ 

       130        140        150        160        170        180 
VLEDFPTISL EFRNLAEKYQ TVIADICRRM GIGMAEFLDK HVTSEQEWDK YCHYVAGLVG 

       190        200        210        220        230        240 
IGLSRLFSAS EFEDPLVGED TERANSMGLF LQKTNIIRDY LEDQQGGREF WPQEVWSRYV 

       250        260        270        280        290        300 
KKLGDFAKPE NIDLAVQCLN ELITNALHHI PDVITYLSRL RNQSVFNFCA IPQVMAIATL 

       310        320        330        340        350        360 
AACYNNQQVF KGAVKIRKGQ AVTLMMDATN MPAVKAIIYQ YMEEIYHRIP DSDPSSSKTR 

       370        380        390        400        410 
QIISTIRTQN LPNCQLISRS HYSPIYLSFV MLLAALSWQY LTTLSQVTED YVQTGEH 

« Hide

References

« Hide 'large scale' references
[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].
[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].
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].
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].
Tissue: Liver.
[5]"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], VARIANT ARG-45.
Tissue: Lung, Muscle and Urinary bladder.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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.
[8]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L06070 mRNA. Translation: AAA60582.1.
L06105 mRNA. Translation: AAA36645.1.
X69141 mRNA. Translation: CAA48896.1.
S76822 mRNA. Translation: AAB33404.1.
BC003573 mRNA. Translation: AAH03573.1.
BC009251 mRNA. Translation: AAH09251.1.
BC029641 mRNA. Translation: AAH29641.1.
PIRA45998.
I38245.
I52090.
RefSeqNP_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.
UniGeneHs.593928.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EZFX-ray2.15A/B/C35-370[»]
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[»]
ProteinModelPortalP37268.
SMRP37268. Positions 35-369.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108516. 18 interactions.
IntActP37268. 9 interactions.
MINTMINT-1401726.
STRING9606.ENSP00000220584.

Chemistry

BindingDBP37268.
ChEMBLCHEMBL3338.
GuidetoPHARMACOLOGY645.

PTM databases

PhosphoSiteP37268.

Polymorphism databases

DMDM585126.

Proteomic databases

PaxDbP37268.
PeptideAtlasP37268.
PRIDEP37268.

Protocols and materials databases

DNASU2222.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000220584; ENSP00000220584; ENSG00000079459.
GeneID2222.
KEGGhsa:2222.
UCSCuc003wuh.3. human.

Organism-specific databases

CTD2222.
GeneCardsGC08P011653.
H-InvDBHIX0168873.
HGNCHGNC:3629. FDFT1.
HPAHPA008874.
MIM184420. gene.
neXtProtNX_P37268.
PharmGKBPA28073.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1562.
HOVERGENHBG002370.
InParanoidP37268.
KOK00801.
OMAEMRHAVC.
PhylomeDBP37268.
TreeFamTF105316.

Enzyme and pathway databases

BioCycMetaCyc:HS01329-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP37268.
UniPathwayUPA00767; UER00751.

Gene expression databases

ArrayExpressP37268.
BgeeP37268.
CleanExHS_FDFT1.
GenevestigatorP37268.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
InterProIPR002060. Squ/phyt_synthse.
IPR006449. Squal_synth.
IPR019845. Squalene/phytoene_synthase_CS.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamPF00494. SQS_PSY. 1 hit.
[Graphical view]
SUPFAMSSF48576. SSF48576. 1 hit.
TIGRFAMsTIGR01559. squal_synth. 1 hit.
PROSITEPS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit.
PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFDFT1. human.
EvolutionaryTraceP37268.
GenomeRNAi2222.
NextBio9013.
PROP37268.
SOURCESearch...

Entry information

Entry nameFDFT_HUMAN
AccessionPrimary (citable) accession number: P37268
Secondary accession number(s): Q96GT0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: March 19, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM