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Human Metabolome Database Version 2.5

 

Showing metabocard for Squalene (HMDB00256)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:48
Accession Number HMDB00256
Secondary Accession Numbers Not Available
Common Name Squalene
Description A natural raw material found in human sebum (5%) and in shark-liver oil. An unsaturated aliphatic hydrocarbon (carotenoid) with six unconjugated double bonds. (Hawley's Condensed Chemical Reference) Biological Source: Found in fish liver oils, yeast lipids and many vegetable oils, e.g. palm oil, cottonseed oil, rapeseed oil. Volatile component of scent material from Saguinus oedipus (cotton-top tamarin monkey) and Saguinus fuscicollis (saddle-back tamarin monkey). Component of adult human sebum principally responsible for the fixing of fingerprints (ChemNetBase) Squalene is a natural organic compound originally obtained for commercial purposes primarily from shark liver oil, though there are botanical sources as well, including rice bran, wheat germ, and olives. All higher organisms produce squalene, including humans. It is a hydrocarbon and a triterpene. -- Wikipedia; Squalene is the biochemical precursor to the whole family of steroids. Oxidation of one of the terminal double bonds of squalene yields 2,3-squalene oxide which undergoes enzyme-catalyzed cyclization to afford lanosterol, which is then elaborated into cholesterol and other steroids. -- Wikipedia; Squalene is a low density compound often stored in the bodies of cartilaginous fishes such as sharks, which lack a swim bladder and must therefore reduce their body density with fats and oils. Squalene, which is stored mainly in the shark's liver, is lighter than water with a specific gravity of 0.855. -- Wikipedia Uses: Bactericide. Intermediate in the manufacture of pharmaceuticals, rubber chemicals and coloring materials (Physical Constants of Chemical Substances)
Synonyms
  1. (E,E,E,E)-Squalene
  2. (all-E)-2,6,10,15,19,23-hexamethyl-2,6,10,14,18,22-Tetracosahexaene
  3. 2,6,10,15,19,23-Hexamethyl-2,6,10,14,18,22-tetracosahexaene
  4. Nikko Squalane EX
  5. Spinacen
  6. Spinacene
  7. Squalen
  8. Squalene
  9. all-trans-Squalene
  10. trans-Squalene
Chemical IUPAC Name (2E,6E,10E,14E,18E)-2,6,10,15,19,23-hexamethyl-2,6,10,14,18,22-Tetracosahexaene
Chemical Formula C30H50
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Miscellanous
Class
  • Alkanes and Alkenes
Sub Class
  • Long chain alkenes
Family
  • Mammalian Metabolite
Species
  • alkene
Biofunction
  • Component of Terpenoid biosynthesis
Application
—
Source
  • Endogenous
Average Molecular Weight 410.718
Monoisotopic Molecular Weight 410.391266
Isomeric SMILES CC(C)=C/CCC(C)=C/CCC(C)=CCCC=C(/C)CCC=C(/C)CCC=C(/C)C
Canonical SMILES CC(C)=CCCC(C)=CCCC(C)=CCCC=C(C)CCC=C(C)CCC=C(C)C
KEGG Compound ID C00751 Link Image
BioCyc ID SQUALENE Link Image
BiGG ID 35878 Link Image
Wikipedia Link Squalene Link Image
NuGOwiki Link HMDB00256 Link Image
Metagene Link HMDB00256 Link Image
METLIN ID 197 Link Image
PubChem Compound 1105 Link Image
PubChem Substance 3184 Link Image
ChEBI ID 15440 Link Image
CAS Registry Number 111-02-4
InChI Identifier InChI=1/C30H50/c1-25(2)15-11-19-29(7)23-13-21-27(5)17-9-10-18-28(6)22-14-24-30(8)20-12-16-26(3)4/h15-18,23-24H,9-14,19-22H2,1-8H3/b27-17+,28-18+,29-23-,30-24+
Synthesis Reference Peng, Wanxi; Li, Kaifu. Method of preparation of squalene. Faming Zhuanli Shenqing Gongkai Shuomingshu (2006), 9pp.
Melting Point (Experimental) -75 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.05e-12 mg/mL [MEYLAN,WM et al. (1996)]; 5.02e-04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Liquid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 8.64 [Predicted by ALOGPS]; 8.3 [Predicted by PubChem via XLOGP]; 14.12 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane (Predicted from LogP)
  • endoplasmic reticulum
Biofluid Location
  • Blood
Tissue Location
Tissue References
Chylomicrons —
Fibroblasts —
Liver —
Skin —
Stratum Corneum —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 1.58 +/- 0.063 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Rajaratnam RA, Gylling H, Miettinen TA: Serum squalene in postmenopausal women without and with coronary artery disease. Atherosclerosis. 1999 Sep;146(1):61-4. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 2.22 +/- 0.063 uM
Age Adult:>18 yrs old
Sex Female
Condition Normal
Comments Postmenopausal women with coronary artery disease
References
  • Rajaratnam RA, Gylling H, Miettinen TA: Serum squalene in postmenopausal women without and with coronary artery disease. Atherosclerosis. 1999 Sep;146(1):61-4. [PubMed Link Image]
Associated Disorders
Condition References
Normal
  • Rajaratnam RA, Gylling H, Miettinen TA: Serum squalene in postmenopausal women without and with coronary artery disease. Atherosclerosis. 1999 Sep;146(1):61-4. [PubMed Link Image]
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Steroid Biosynthesis SMP00023 Link Image map00100 Link Image
General References
  1. Strauss JS, Stranieri AM, Farrell LN, Downing DT: The effect of marked inhibition of sebum production with 13cis-retinoic acid on skin surface lipid composition. J Invest Dermatol. 1980 Feb;74(2):66-7. [PubMed Link Image]
  2. Grimes DS, Hindle E, Dyer T: Sunlight, cholesterol and coronary heart disease. QJM. 1996 Aug;89(8):579-89. [PubMed Link Image]
  3. Relas H, Gylling H, Miettinen TA: Dietary squalene increases cholesterol synthesis measured with serum non-cholesterol sterols after a single oral dose in humans. Atherosclerosis. 2000 Oct;152(2):377-83. [PubMed Link Image]
  4. Nikkila K, Hockerstedt K, Miettinen TA: Serum and hepatic cholestanol, squalene and noncholesterol sterols in man: a study on liver transplantation. Hepatology. 1992 May;15(5):863-70. [PubMed Link Image]
  5. Gylling H, Relas H, Miettinen HE, Radhakrishnan R, Miettinen TA: Delayed postprandial retinyl palmitate and squalene removal in a patient heterozygous for apolipoprotein A-IFIN mutation (Leu 159-->Arg) and low HDL cholesterol level without coronary artery disease. Atherosclerosis. 1996 Dec 20;127(2):239-43. [PubMed Link Image]
  6. Rajaratnam RA, Gylling H, Miettinen TA: Independent association of serum squalene and noncholesterol sterols with coronary artery disease in postmenopausal women. J Am Coll Cardiol. 2000 Apr;35(5):1185-91. [PubMed Link Image]
  7. Rajaratnam RA, Gylling H, Miettinen TA: Serum squalene in postmenopausal women without and with coronary artery disease. Atherosclerosis. 1999 Sep;146(1):61-4. [PubMed Link Image]
  8. Thiele JJ, Weber SU, Packer L: Sebaceous gland secretion is a major physiologic route of vitamin E delivery to skin. J Invest Dermatol. 1999 Dec;113(6):1006-10. [PubMed Link Image]
  9. Relas H, Gylling H, Miettinen TA: Effect of stanol ester on postabsorptive squalene and retinyl palmitate. Metabolism. 2000 Apr;49(4):473-8. [PubMed Link Image]
  10. Gylling H, Vuoristo M, Farkkila M, Miettinen TA: The metabolism of cholestanol in primary biliary cirrhosis. J Hepatol. 1996 Apr;24(4):444-51. [PubMed Link Image]
  11. Chiba K, Yoshizawa K, Makino I, Kawakami K, Onoue M: Changes in the levels of glutathione after cellular and cutaneous damage induced by squalene monohydroperoxide. J Biochem Mol Toxicol. 2001;15(3):150-8. [PubMed Link Image]
  12. Nosaka Y, Yamanishi Y, Hirayama C: Biliary squalene levels in hepatobiliary disease. Gastroenterol Jpn. 1985 Aug;20(4):338-43. [PubMed Link Image]
  13. Kohno Y, Egawa Y, Itoh S, Nagaoka S, Takahashi M, Mukai K: Kinetic study of quenching reaction of singlet oxygen and scavenging reaction of free radical by squalene in n-butanol. Biochim Biophys Acta. 1995 Apr 28;1256(1):52-6. [PubMed Link Image]
  14. Wikipedia Link Image
Metabolic Enzymes
  1. Squalene monooxygenase
  2. Squalene synthetase
  3. SEC14-like protein 2
  4. Putative uncharacterized protein DKFZp686B0215
  5. SEC14-like protein 3
  6. SEC14-like protein 4
Enzyme 1 [top]
Enzyme 1 ID 5385
Enzyme 1 Name Squalene monooxygenase
Enzyme 1 Synonyms
  1. Squalene epoxidase
  2. SE
Enzyme 1 Gene Name SQLE
Enzyme 1 Protein Sequence >Squalene monooxygenase 
MWTFLGIATFTYFYKKFGDFITLANREVLLCVLVFLSLGLVLSYRCRHRNGGLLGRQRSG
SQFALFSDILSGLPFIGFFWAKSPPESENKEQLGARRRRKGTNISETSLIGTAACTSTSS
QNDPEVIIVGAGVLGSALVAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGL
GDTVEGLDAQVVNGYMIHDQESKSEVQIPYPLSENNQVQSGRAFHHGRFIMSLRKAAMAE
PNAKFIEGVVLQLLEEDDVVMGVQYKDKETGDIKELHAPLTVVADGLFSKFRKSLVSNKV
SVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYRISSSETRVLVDIRGEMPRNLREYM
VEKIYPQIPDHLKEPFLEATDNSHLRSMLASFLPPSSVKKRGVLLLGDAYNMRHPLTGGG
MTVAFKDIKLWRKLLKGIPDLYDDAAIFEANKSFYWARKTSHSFVVNILAQALYELFSAT
DDSLHQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLALIGHFFAVAIYAVYFCFKSEPW
ITKPRALLSSSAVLYKACSVIFPLIYSEMKYMVH
Enzyme 1 Number of Residues 574
Enzyme 1 Molecular Weight 63940
Enzyme 1 Theoretical pI 9.12
Enzyme 1 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Coenzyme transport and metabolism
Enzyme 1 Specific Function Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway
Enzyme 1 Pathways
Enzyme 1 Reactions
  • squalene + AH2 + O2 = (S)-squalene-2,3-epoxide + A + H2O
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 20-40 61-81 123-143 546-566
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 2443316 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q14534 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ERG1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1725 bp 
ATGTGGACTTTTCTGGGCATTGCCACTTTCACCTATTTTTATAAGAAGTTCGGGGACTTC
ATCACTTTGGCCAACAGGGAGGTCCTGTTGTGCGTGCTGGTGTTCCTCTCGCTGGGCCTG
GTGCTCTCCTACCGCTGTCGCCACCGAAACGGGGGTCTCCTCGGGCGCCAGCGGAGCGGC
TCCCAGTTCGCCCTCTTCTCGGATATTCTCTCAGGCCTGCCTTTCATTGGCTTCTTCTGG
GCCAAATCCCCCCCTGAATCAGAAAATAAGGAGCAGCTCGGGGCCAGGAGGCGCAGAAAA
GGAACCAATATTTCAGAAACAAGCTTAATAGGAACAGCTGCCTGTACATCAACATCTTCT
CAGAATGACCCAGAAGTTATCATCGTGGGAGCTGGCGTGCTTGGCTCTGCTTTGGTAGCT
GTGCTTTCCAGAGATGGAAGAAAGGTGACAGTCATTGAGAGAGACTTAAAAGAGCCTGAC
AGAATAGTTGGAGAATTCCTGCAGCCGGGTGGTTATCATGTTCTCAAAGACCTTGGTCTT
GGAGATACAGTGGAAGGTCTTGATGCCCAGGTTGTAAATGGTTACATGATTCATGATCAG
GAAAGCAAATCAGAGGTTCAGATTCCTTACCCTCTGTCAGAAAACAATCAAGTGCAGAGT
GGAAGAGCTTTCCATCACGGAAGATTCATCATGAGTCTCCGGAAAGCAGCTATGGCAGAG
CCCAATGCAAAGTTTATTGAAGGTGTTGTGTTACAGTTATTAGAGGAAGATGATGTTGTG
ATGGGAGTTCAGTACAAGGATAAAGAGACTGGAGATATCAAGGAACTCCATGCTCCACTG
ACTGTTGTTGCAGATGGGCTTTTCTCCAAGTTCAGGAAAAGCCTGGTCTCCAATAAAGTT
TCTGTATCATCTCATTTTGTTGGCTTTCTTATGAAGAATGCACCACAGTTTAAAGCAAAT
CATGCTGAACTTATTTTAGCTAACCCGAGTCCAGTTCTCATCTACCGGATTTCATCCAGT
GAAACTCGAGTACTTGTTGACATTAGAGGAGAAATGCCAAGGAATTTAAGAGAATACATG
GTTGAAAAAATTTACCCACAAATACCTGATCACCTGAAAGAACCATTCTTAGAAGCCACT
GACAATTCTCATCTGAGGTCCATGCTAGCAAGCTTCCTTCCTCCTTCATCAGTGAAGAAA
CGAGGTGTTCTTCTTTTGGGAGACGCATATAATATGAGGCATCCACTTACTGGTGGAGGA
ATGACTGTTGCTTTTAAAGATATAAAACTATGGAGAAAACTGCTAAAGGGTATCCCTGAC
CTTTATGATGATGCAGCTATTTTCGAGGCCAACAAATCATTTTACTGGGCAAGAAAAACA
TCTCATTCCTTTGTCGTGAATATCCTTGCTCAGGCTCTTTATGAATTATTTTCTGCCACA
GATGATTCCCTGCATCAACTAAGAAAAGCCTGTTTTCTTTATTTCAAACTTGGTGGCGAA
TGTGTTGCGGGTCCTGTTGGGCTGCTTTCTGTATTGTCTCCTAACCCTCTAGCTTTAATT
GGACACTTCTTTGCTGTTGCAATCTATGCCGTGTATTTTTGCTTTAAGTCAGAACCTTGG
ATTACAAAACCTCGAGCCCTTCTCAGTAGTAGTGCTGTATTGTACAAAGCGTGTTCTGTA
ATATTTCCTCTAATTTACTCAGAAATGAAGTATATGGTTCATTAA
Enzyme 1 GenBank Gene ID D78130 Link Image
Enzyme 1 GeneCard ID SQLE Link Image
Enzyme 1 GenAtlas ID SQLE Link Image
Enzyme 1 HGNC ID HGNC:11279 Link Image
Enzyme 1 Chromosome Location 8
Enzyme 1 Locus 8q24.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Nagai M, Sakakibara J, Wakui K, Fukushima Y, Igarashi S, Tsuji S, Arakawa M, Ono T: Localization of the squalene epoxidase gene (SQLE) to human chromosome region 8q24.1. Genomics. 1997 Aug 15;44(1):141-3. [PubMed Link Image]
  2. Nakamura Y, Sakakibara J, Izumi T, Shibata A, Ono T: Transcriptional regulation of squalene epoxidase by sterols and inhibitors in HeLa cells. J Biol Chem. 1996 Apr 5;271(14):8053-6. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5492
Enzyme 2 Name Squalene synthetase
Enzyme 2 Synonyms
  1. SQS
  2. SS
  3. Farnesyl-diphosphate farnesyltransferase
  4. FPP:FPP farnesyltransferase
Enzyme 2 Gene Name FDFT1
Enzyme 2 Protein Sequence >Squalene synthetase 
MEFVKCLGHPEEFYNLVRFRIGGKRKVMPKMDQDSLSSSLKTCYKYLNQTSRSFAAVIQA
LDGEMRNAVCIFYLVLRALDTLEDDMTISVEKKVPLLHNFHSFLYQPDWRFMESKEKDRQ
VLEDFPTISLEFRNLAEKYQTVIADICRRMGIGMAEFLDKHVTSEQEWDKYCHYVAGLVG
IGLSRLFSASEFEDPLVGEDTERANSMGLFLQKTNIIRDYLEDQQGGREFWPQEVWSRYV
KKLGDFAKPENIDLAVQCLNELITNALHHIPDVITYLSRLRNQSVFNFCAIPQVMAIATL
AACYNNQQVFKGAVKIRKGQAVTLMMDATNMPAVKAIIYQYMEEIYHRIPDSDPSSSKTR
QIISTIRTQNLPNCQLISRSHYSPIYLSFVMLLAALSWQYLTTLSQVTEDYVQTGEH
Enzyme 2 Number of Residues 417
Enzyme 2 Molecular Weight 48116
Enzyme 2 Theoretical pI 6.51
Enzyme 2 GO Classification
Function
  • catalytic activity
  • farnesyl-diphosphate farnesyltransferase activity
  • farnesyltranstransferase activity
  • prenyltransferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • biosynthesis
  • lipid biosynthesis
  • metabolism
  • physiological process
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 2 General Function Lipid transport and metabolism
Enzyme 2 Specific Function 2 farnesyl diphosphate = diphosphate + presqualene diphosphate
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 2 farnesyl diphosphate = diphosphate + presqualene diphosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 284-304 384-404
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 292510 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P37268 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name FDFT_HUMAN Link Image
Enzyme 2 PDB ID 1EZF Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1254 bp 
ATGGAGTTCGTGAAATGCCTTGGCCACCCCGAAGAGTTCTACAACCTGGTGCGCTTCCGG
ATCGGGGGCAAGCGGAAGGTGATGCCCAAGATGGACCAGGACTCGCTCAGCAGCAGCCTG
AAAACTTGCTACAAGTATCTCAATCAGACCAGTCGCAGTTTCGCAGCTGTTATCCAGGCG
CTGGATGGGGAAATGCGCAACGCAGTGTGCATATTTTATCTGGTTCTCCGAGCTCTGGAC
ACACTGGAAGATGACATGACCATCAGTGTGGAAAAGAAGGTCCCGCTGTTACACAACTTT
CACTCTTTCCTTTACCAACCAGACTGGCGGTTCATGGAGAGCAAGGAGAAGGATCGCCAG
GTGCTGGAGGACTTCCCAACGATCTCCCTTGAGTTTAGAAATCTGGCTGAGAAATACCAA
ACAGTGATTGCCGACATTTGCCGGAGAATGGGCATTGGGATGGCAGAGTTTTTGGATAAG
CATGTGACCTCTGAACAGGAGTGGGACAAGTACTGCCACTATGTTGCTGGGCTGGTCGGA
ATTGGCCTTTCCCGTCTTTTCTCAGCCTCAGAGTTTGAAGACCCCTTAGTTGGTGAAGAT
ACAGAACGTGCCAACTCTATGGGCCTGTTTCTGCAGAAAACAAACATCATCCGTGACTAT
CTGGAAGACCAGCAAGGAGGAAGAGAGTTCTGGCCTCAAGAGGTTTGGAGCAGGTATGTT
AAGAAGTTAGGGGATTTTGCTAAGCCGGAGAATATTGACTTGGCCGTGCAGTGCCTGAAT
GAACTTATAACCAATGCACTGCACCACATCCCAGATGTCATCACCTACCTTTCGAGACTC
AGAAACCAGAGTGTGTTTAACTTCTGCGCTATTCCACAGGTGATGGCCATTGCCACTTTG
GCTGCCTGTTATAATAACCAGCAGGTGTTCAAAGGGGCAGTGAAGATTCGGAAAGGGCAA
GCAGTGACCCTGATGATGGATGCCACCAATATGCCAGCTGTCAAAGCCATCATATATCAG
TATATGGAAGAGATTTATCATAGAATCCCCGACTCAGACCCATCTTCTAGCAAAACAAGG
CAGATCATCTCCACCATCCGGACGCAGAATCTTCCCAACTGTCAGCTGATTTCCCGAAGC
CACTACTCCCCCATCTACCTGTCGTTTGTCATGCTTTTGGCTGCCCTGAGCTGGCAGTAC
CTGACCACTCTCTCCCAGGTAACAGAAGACTATGTTCAGACTGGAGAACACTGA
Enzyme 2 GenBank Gene ID L06070 Link Image
Enzyme 2 GeneCard ID FDFT1 Link Image
Enzyme 2 GenAtlas ID FDFT1 Link Image
Enzyme 2 HGNC ID HGNC:3629 Link Image
Enzyme 2 Chromosome Location 8
Enzyme 2 Locus 8p23.1-p22
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Robinson GW, Tsay YH, Kienzle BK, Smith-Monroy CA, Bishop RW: Conservation between human and fungal squalene synthetases: similarities in structure, function, and regulation. Mol Cell Biol. 1993 May;13(5):2706-17. [PubMed Link Image]
  2. Jiang G, McKenzie TL, Conrad DG, Shechter I: Transcriptional regulation by lovastatin and 25-hydroxycholesterol in HepG2 cells and molecular cloning and expression of the cDNA for the human hepatic squalene synthase. J Biol Chem. 1993 Jun 15;268(17):12818-24. [PubMed Link Image]
  3. Summers C, Karst F, Charles AD: Cloning, expression and characterisation of the cDNA encoding human hepatic squalene synthase, and its relationship to phytoene synthase. Gene. 1993 Dec 22;136(1-2Che):185-92. [PubMed Link Image]
  4. Soltis DA, McMahon G, Caplan SL, Dudas DA, Chamberlin HA, Vattay A, Dottavio D, Rucker ML, Engstrom RG, Cornell-Kennon SA, et al.: Expression, purification, and characterization of the human squalene synthase: use of yeast and baculoviral systems. Arch Biochem Biophys. 1995 Feb 1;316(2):713-23. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 7051
Enzyme 3 Name SEC14-like protein 2
Enzyme 3 Synonyms
  1. Alpha-tocopherol-associated protein
  2. TAP
  3. hTAP
  4. Supernatant protein factor
  5. SPF
  6. Squalene transfer protein
Enzyme 3 Gene Name SEC14L2
Enzyme 3 Protein Sequence >SEC14-like protein 2 
MSGRVGDLSPRQKEALAKFRENVQDVLPALPNPDDYFLLRWLRARSFDLQKSEAMLRKHV
EFRKQKDIDNIISWQPPEVIQQYLSGGMCGYDLDGCPVWYDIIGPLDAKGLLFSASKQDL
LRTKMRECELLLQECAHQTTKLGRKVETITIIYDCEGLGLKHLWKPAVEAYGEFLCMFEE
NYPETLKRLFVVKAPKLFPVAYNLIKPFLSEDTRKKIMVLGANWKEVLLKHISPDQVPVE
YGGTMTDPDGNPKCKSKINYGGDIPRKYYVRDQVKQQYEHSVQISRGSSHQVEYEILFPG
CVLRWQFMSDGADVGFGIFLKTKMGERQRAGEMTEVLPNQRYNSHLVPEDGTLTCSDPGI
YVLRFDNTYSFIHAKKVNFTVEVLLPDKASEEKMKQLGAGTPK
Enzyme 3 Number of Residues 403
Enzyme 3 Molecular Weight 46146
Enzyme 3 Theoretical pI 7.94
Enzyme 3 GO Classification
Function
  • carrier activity
  • protein carrier activity
  • transporter activity
Process
  • cellular physiological process
  • intracellular protein transport
  • physiological process
  • protein transport
  • transport
Component
  • cell
  • intracellular
  • membrane
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Carrier protein. Binds to some hydrophobic molecules and promotes their transfer between the different cellular sites. Binds with high affinity to alpha-tocopherol. Also binds with a weaker affinity to other tocopherols and to tocotrienols. May have a transcriptional activatory activity via its association with alpha-tocopherol. Probably recognizes and binds some squalene structure, suggesting that it may regulate cholesterol biosynthesis by increasing the transfer of squalene to a metabolic active pool in the cell
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 5596693 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O76054 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name S14L2_HUMAN Link Image
Enzyme 3 PDB ID 1OLM Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1212 bp 
ATGAGCGGCAGAGTCGGCGATCTGAGCCCCAGGCAGAAGGAGGCATTGGCCAAGTTTCGG
GAGAATGTCCAGGATGTGCTGCCGGCCCTGCCGAATCCAGATGACTATTTTCTCCTGCGT
TGGCTCCGAGCCAGAAGCTTCGACCTGCAGAAGTCGGAGGCCATGCTCCGGAAGCATGTG
GAGTTCCGAAAGCAAAAGGACATTGACAACATCATTAGCTGGCAGCCTCCAGAGGTGATC
CAACAGTATCTGTCAGGGGGTATGTGTGGCTATGACCTGGATGGCTGCCCAGTCTGGTAC
GACATAATTGGACCTCTGGATGCCAAGGGTCTGCTGTTCTCAGCCTCCAAACAGGACCTG
CTGAGGACCAAGATGCGGGAGTGTGAGCTGCTTCTGCAAGAGTGTGCCCACCAGACCACA
AAGTTGGGGAGGAAGGTGGAGACCATCACCATAATTTATGACTGCGAGGGGCTTGGCCTC
AAGCATCTCTGGAAGCCTGCTGTGGAGGCCTATGGAGAGTTTCTCTGCATGTTTGAGGAA
AATTATCCCGAAACACTGAAGCGTCTTTTTGTTGTTAAAGCCCCCAAACTGTTTCCTGTG
GCCTATAACCTCATCAAACCCTTCCTGAGTGAGGACACTCGTAAGAAGATCATGGTCCTG
GGAGCAAATTGGAAGGAGGTTTTACTGAAACATATCAGCCCTGACCAGGTGCCTGTGGAG
TATGGGGGCACCATGACTGACCCTGATGGAAACCCCAAGTGCAAATCCAAGATCAACTAC
GGGGGTGACATCCCCAGGAAGTATTATGTGCGAGACCAGGTGAAACAGCAGTATGAACAC
AGCGTGCAGATTTCCCGTGGCTCCTCCCACCAAGTGGAGTATGAGATCCTCTTCCCTGGC
TGTGTCCTCAGGTGGCAGTTTATGTCAGATGGAGCGGATGTTGGTTTTGGGATTTTCCTG
AAGACCAAGATGGGAGAGAGGCAGCGGGCAGGGGAGATGACAGAGGTGCTGCCCAACCAG
AGGTACAACTCCCACCTGGTCCCTGAAGATGGGACCCTCACCTGCAGTGATCCTGGCATC
TATGTCCTGCGGTTTGACAACACCTACAGCTTCATTCATGCCAAGAAGGTCAATTTCACT
GTGGAGGTCCTGCTTCCAGACAAAGCCTCAGAAGAGAAGATGAAACAGCTGGGGGCAGGC
ACCCCGAAATAA
Enzyme 3 GenBank Gene ID AL096881 Link Image
Enzyme 3 GeneCard ID SEC14L2 Link Image
Enzyme 3 GenAtlas ID SEC14L2 Link Image
Enzyme 3 HGNC ID HGNC:10699 Link Image
Enzyme 3 Chromosome Location 22
Enzyme 3 Locus 22q12.2
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Zimmer S, Stocker A, Sarbolouki MN, Spycher SE, Sassoon J, Azzi A: A novel human tocopherol-associated protein: cloning, in vitro expression, and characterization. J Biol Chem. 2000 Aug 18;275(33):25672-80. [PubMed Link Image]
  2. Yamauchi J, Iwamoto T, Kida S, Masushige S, Yamada K, Esashi T: Tocopherol-associated protein is a ligand-dependent transcriptional activator. Biochem Biophys Res Commun. 2001 Jul 13;285(2):295-9. [PubMed Link Image]
  3. Hirosawa M, Nagase T, Ishikawa K, Kikuno R, Nomura N, Ohara O: Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain. DNA Res. 1999 Oct 29;6(5):329-36. [PubMed Link Image]
  4. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 13008
Enzyme 4 Name Putative uncharacterized protein DKFZp686B0215
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name DKFZp686B0215
Enzyme 4 Protein Sequence >Putative uncharacterized protein DKFZp686B0215 
MWTFLGIATFTYFYKKFGDFITLANREVLLCVLVFLSLGLVLSYRCRHRNGGLLGRQQSG
SQFALFSDILSGLPFIGFFWAKSPPESENKEQLEARRRRKGTNISETSLIGTAACTSTSS
QNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGL
GDTVEGLDAQVVNGYMIHDQESKSEVQIPYPLSENNQVQSGRAFHHGRFIMSLRKAAMAE
PNAKFIEGVVLQLLEEDDVVMGVQYKDKETGDIKELHAPLTVVADGLFSKFRKSLVSNKV
SVSSHFVGFLMKNAPQFKANHAELILANPGPVLIYQISSSETRVLVDIRGEMPRNLREYM
VEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGG
MTVAFKDIKLWRKLLKGIPDLYDDAAIFEAKKSFYWARKTSHSFVVNILAQALYELFSAT
DDSLHQLGKACFLYFKLGGECVAGPVGLLSVLSPNPLVLIGHFFAVAIYAVYFCFKSEPW
ITKPRALLSSGAVLYKACSVIFPLIYSEMKYMVH
Enzyme 4 Number of Residues 574
Enzyme 4 Molecular Weight 63795
Enzyme 4 Theoretical pI 8.73
Enzyme 4 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 4 General Function Coenzyme transport and metabolism
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 57997512 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q5HYI4 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name Q5HYI4_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID BX647605 Link Image
Enzyme 4 GeneCard ID Q5HYI4 Link Image
Enzyme 4 GenAtlas ID DKFZp686B0215 Link Image
Enzyme 4 HGNC ID HGNC:11279 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 17073
Enzyme 5 Name SEC14-like protein 3
Enzyme 5 Synonyms
  1. Tocopherol-associated protein 2
Enzyme 5 Gene Name SEC14L3
Enzyme 5 Protein Sequence >SEC14-like protein 3 
MSGRVGDLSPKQAETLAKFRENVQDVLPALPNPDDYFLLRWLRARNFDLQKSEALLRKYM
EFRKTMDIDHILDWQPPEVIQKYMPGGLCGYDRDGCPVWYDIIGPLDPKGLLFSVTKQDL
LKTKMRDCERILHECDLQTERLGKKIETIVMIFDCEGLGLKHFWKPLVEVYQEFFGLLEE
NYPETLKFMLIVKATKLFPVGYNLMKPFLSEDTRRKIIVLGNNWKEGLLKLISPEELPAQ
FGGTLTDPDGNPKCLTKINYGGEIPKSMYVRDQVKTQYEHSVQINRGSSHQVEYEILFPG
CVLRWQFSSDGADIGFGVFLKTKMGERQRAGEMTDVLPSQRYNAHMVPEDGNLTCSEAGV
YVLRFDNTYSFVHAKKVSFTVEVLLPDEGMQKYDKELTPV
Enzyme 5 Number of Residues 400
Enzyme 5 Molecular Weight 46049
Enzyme 5 Theoretical pI 5.97
Enzyme 5 GO Classification
Function
  • carrier activity
  • protein carrier activity
  • transporter activity
Process
  • cellular physiological process
  • intracellular protein transport
  • physiological process
  • protein transport
  • transport
Component
  • cell
  • intracellular
  • membrane
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Probable hydrophobic ligand-binding protein; may play a role in the transport of hydrophobic ligands like tocopherol, squalene and phospholipids
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID Q9UDX4 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name S14L3_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AY158086 Link Image
Enzyme 5 GeneCard ID Q9UDX4 Link Image
Enzyme 5 GenAtlas ID SEC14L3 Link Image
Enzyme 5 HGNC ID HGNC:18655 Link Image
Enzyme 5 Chromosome Location 22
Enzyme 5 Locus 22q12.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Kempna P, Zingg JM, Ricciarelli R, Hierl M, Saxena S, Azzi A: Cloning of novel human SEC14p-like proteins: ligand binding and functional properties. Free Radic Biol Med. 2003 Jun 1;34(11):1458-72. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 17074
Enzyme 6 Name SEC14-like protein 4
Enzyme 6 Synonyms
  1. Tocopherol-associated protein 3
Enzyme 6 Gene Name SEC14L4
Enzyme 6 Protein Sequence >SEC14-like protein 4 
MSSRVGDLSPQQQEALARFRENLQDLLPILPNADDYFLLRWLRARNFDLQKSEDMLRRHM
EFRKQQDLDNIVTWQPPEVIQLYDSGGLCGYDYEGCPVYFNIIGSLDPKGLLLSASKQDM
IRKRIKVCELLLHECELQTQKLGRKIEMALMVFDMEGLSLKHLWKPAVEVYQQFFSILEA
NYPETLKNLIVIRAPKLFPVAFNLVKSFMSEETRRKIVILGDNWKQELTKFISPDQLPVE
FGGTMTDPDGNPKCLTKINYGGEVPKSYYLCEQVRLQYEHTRSVGRGSSLQVENEILFPG
CVLRWQFASDGGDIGFGVFLKTKMGEQQSAREMTEVLPSQRYNAHMVPEDGSLTCLQAGV
YVLRFDNTYSRMHAKKLSYTVEVLLPDKASEETLQSLKAMRPSPTQ
Enzyme 6 Number of Residues 406
Enzyme 6 Molecular Weight 46644
Enzyme 6 Theoretical pI 6.52
Enzyme 6 GO Classification
Function
  • carrier activity
  • protein carrier activity
  • transporter activity
Process
  • cellular physiological process
  • intracellular protein transport
  • physiological process
  • protein transport
  • transport
Component
  • cell
  • intracellular
  • membrane
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Probable hydrophobic ligand-binding protein; may play a role in the transport of hydrophobic ligands like tocopherol, squalene and phospholipids
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID Q9UDX3 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name S14L4_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID AY158085 Link Image
Enzyme 6 GeneCard ID Q9UDX3 Link Image
Enzyme 6 GenAtlas ID SEC14L4 Link Image
Enzyme 6 HGNC ID HGNC:20627 Link Image
Enzyme 6 Chromosome Location 22
Enzyme 6 Locus 22q12.2
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Kempna P, Zingg JM, Ricciarelli R, Hierl M, Saxena S, Azzi A: Cloning of novel human SEC14p-like proteins: ligand binding and functional properties. Free Radic Biol Med. 2003 Jun 1;34(11):1458-72. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available