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P37268

- FDFT_HUMAN

UniProt

P37268 - FDFT_HUMAN

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Protein

Squalene synthase

Gene

FDFT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

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. isoprenoid biosynthetic process Source: UniProtKB-KW
  4. small molecule metabolic process Source: Reactome
  5. steroid biosynthetic process Source: ProtInc
Complete GO annotation...

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

Topology

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

GO - Cellular componenti

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

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

PaxDbiP37268.
PeptideAtlasiP37268.
PRIDEiP37268.

PTM databases

PhosphoSiteiP37268.

Expressioni

Gene expression databases

BgeeiP37268.
CleanExiHS_FDFT1.
ExpressionAtlasiP37268. baseline and differential.
GenevestigatoriP37268.

Organism-specific databases

HPAiHPA008874.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi108516. 24 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 – 5114Combined sources
Helixi52 – 543Combined sources
Helixi55 – 595Combined sources
Helixi65 – 8420Combined sources
Helixi90 – 10314Combined sources
Turni117 – 1193Combined sources
Helixi120 – 1234Combined sources
Helixi125 – 13410Combined sources
Helixi137 – 15620Combined sources
Helixi157 – 1593Combined sources
Helixi165 – 17511Combined sources
Helixi177 – 18913Combined sources
Beta strandi191 – 1933Combined sources
Helixi195 – 1995Combined sources
Helixi201 – 21818Combined sources
Helixi220 – 2256Combined sources
Helixi233 – 2364Combined sources
Turni237 – 2393Combined sources
Helixi243 – 2475Combined sources
Helixi249 – 2513Combined sources
Helixi252 – 26716Combined sources
Helixi270 – 2789Combined sources
Helixi283 – 30321Combined sources
Helixi307 – 3104Combined sources
Helixi318 – 32710Combined sources
Beta strandi328 – 3303Combined sources
Helixi331 – 34616Combined sources
Helixi356 – 36813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

Family & Domainsi

Sequence similaritiesi

Belongs to the phytoene/squalene synthase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1562.
GeneTreeiENSGT00390000016034.
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

        10         20         30         40         50
MEFVKCLGHP EEFYNLVRFR IGGKRKVMPK MDQDSLSSSL KTCYKYLNQT
60 70 80 90 100
SRSFAAVIQA LDGEMRNAVC IFYLVLRALD TLEDDMTISV EKKVPLLHNF
110 120 130 140 150
HSFLYQPDWR FMESKEKDRQ VLEDFPTISL EFRNLAEKYQ TVIADICRRM
160 170 180 190 200
GIGMAEFLDK HVTSEQEWDK YCHYVAGLVG IGLSRLFSAS EFEDPLVGED
210 220 230 240 250
TERANSMGLF LQKTNIIRDY LEDQQGGREF WPQEVWSRYV KKLGDFAKPE
260 270 280 290 300
NIDLAVQCLN ELITNALHHI PDVITYLSRL RNQSVFNFCA IPQVMAIATL
310 320 330 340 350
AACYNNQQVF KGAVKIRKGQ AVTLMMDATN MPAVKAIIYQ YMEEIYHRIP
360 370 380 390 400
DSDPSSSKTR QIISTIRTQN LPNCQLISRS HYSPIYLSFV MLLAALSWQY
410
LTTLSQVTED YVQTGEH
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:
EMBLi
GenBanki
DDBJi
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. [P37268-1]
PIRiA45998.
I38245.
I52090.
RefSeqiNP_001274671.1. NM_001287742.1. [P37268-1]
NP_001274672.1. NM_001287743.1. [P37268-1]
NP_001274673.1. NM_001287744.1. [P37268-2]
NP_001274674.1. NM_001287745.1. [P37268-2]
NP_001274676.1. NM_001287747.1. [P37268-2]
NP_001274677.1. NM_001287748.1. [P37268-2]
NP_001274678.1. NM_001287749.1. [P37268-2]
NP_001274679.1. NM_001287750.1.
NP_001274680.1. NM_001287751.1. [P37268-3]
NP_001274685.1. NM_001287756.1.
NP_004453.3. NM_004462.4. [P37268-1]
UniGeneiHs.593928.

Genome annotation databases

EnsembliENST00000220584; ENSP00000220584; ENSG00000079459. [P37268-1]
ENST00000443614; ENSP00000390367; ENSG00000079459. [P37268-5]
ENST00000525777; ENSP00000436069; ENSG00000079459. [P37268-3]
ENST00000528643; ENSP00000431649; ENSG00000079459. [P37268-3]
ENST00000528812; ENSP00000431749; ENSG00000079459. [P37268-2]
ENST00000530664; ENSP00000432331; ENSG00000079459. [P37268-2]
ENST00000538689; ENSP00000444248; ENSG00000079459. [P37268-2]
ENST00000615631; ENSP00000481481; ENSG00000079459. [P37268-1]
ENST00000618539; ENSP00000480828; ENSG00000079459. [P37268-1]
ENST00000622850; ENSP00000484122; ENSG00000079459. [P37268-2]
ENST00000623368; ENSP00000485229; ENSG00000079459. [P37268-2]
GeneIDi2222.
KEGGihsa:2222.
UCSCiuc003wuh.3. human. [P37268-1]

Polymorphism databases

DMDMi585126.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [P37268-1 ]
PIRi A45998.
I38245.
I52090.
RefSeqi NP_001274671.1. NM_001287742.1. [P37268-1 ]
NP_001274672.1. NM_001287743.1. [P37268-1 ]
NP_001274673.1. NM_001287744.1. [P37268-2 ]
NP_001274674.1. NM_001287745.1. [P37268-2 ]
NP_001274676.1. NM_001287747.1. [P37268-2 ]
NP_001274677.1. NM_001287748.1. [P37268-2 ]
NP_001274678.1. NM_001287749.1. [P37268-2 ]
NP_001274679.1. NM_001287750.1.
NP_001274680.1. NM_001287751.1. [P37268-3 ]
NP_001274685.1. NM_001287756.1.
NP_004453.3. NM_004462.4. [P37268-1 ]
UniGenei Hs.593928.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. 24 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

PaxDbi P37268.
PeptideAtlasi P37268.
PRIDEi P37268.

Protocols and materials databases

DNASUi 2222.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000220584 ; ENSP00000220584 ; ENSG00000079459 . [P37268-1 ]
ENST00000443614 ; ENSP00000390367 ; ENSG00000079459 . [P37268-5 ]
ENST00000525777 ; ENSP00000436069 ; ENSG00000079459 . [P37268-3 ]
ENST00000528643 ; ENSP00000431649 ; ENSG00000079459 . [P37268-3 ]
ENST00000528812 ; ENSP00000431749 ; ENSG00000079459 . [P37268-2 ]
ENST00000530664 ; ENSP00000432331 ; ENSG00000079459 . [P37268-2 ]
ENST00000538689 ; ENSP00000444248 ; ENSG00000079459 . [P37268-2 ]
ENST00000615631 ; ENSP00000481481 ; ENSG00000079459 . [P37268-1 ]
ENST00000618539 ; ENSP00000480828 ; ENSG00000079459 . [P37268-1 ]
ENST00000622850 ; ENSP00000484122 ; ENSG00000079459 . [P37268-2 ]
ENST00000623368 ; ENSP00000485229 ; ENSG00000079459 . [P37268-2 ]
GeneIDi 2222.
KEGGi hsa:2222.
UCSCi uc003wuh.3. human. [P37268-1 ]

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.
GeneTreei ENSGT00390000016034.
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 35469327.
PROi P37268.
SOURCEi Search...

Gene expression databases

Bgeei P37268.
CleanExi HS_FDFT1.
ExpressionAtlasi P37268. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 158 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