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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 Link Image
SDF File Show Link Image
PDB File Show Link Image
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 synthase
  3. Serine palmitoyltransferase 1
  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
MWTFLGIATFTYFYKKFGDFITLANREVLLCVLVFLSLGLVLSYRCRHRNGGLLGRQQSG
SQFALFSDILSGLPFIGFFWAKSPPESENKEQLEARRRRKGTNISETSLIGTAACTSTSS
QNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGL
GDTVEGLDAQVVNGYMIHDQESKSEVQIPYPLSENNQVQSGRAFHHGRFIMSLRKAAMAE
PNAKFIEGVVLQLLEEDDVVMGVQYKDKETGDIKELHAPLTVVADGLFSKFRKSLVSNKV
SVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVLVDIRGEMPRNLREYM
VEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGG
MTVAFKDIKLWRKLLKGIPDLYDDAAIFEAKKSFYWARKTSHSFVVNILAQALYELFSAT
DDSLHQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLVLIGHFFAVAIYAVYFCFKSEPW
ITKPRALLSSGAVLYKACSVIFPLIYSEMKYMVH
Enzyme 1 Number of Residues 574
Enzyme 1 Molecular Weight 63922.5
Enzyme 1 Theoretical pI 8.87
Enzyme 1 GO Classification
Function
  • FAD or FADH2 binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • monooxygenase activity
  • nucleoside binding
  • oxidoreductase activity
  • purine nucleoside binding
  • squalene monooxygenase activity
Process
  • metabolic process
  • oxidation reduction
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 1 General Function Involved in oxidoreductase activity
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 [RN:R02873]
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 62865635 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
GTGCTCTCCTACCGCTGTCGCCACCGAAACGGGGGTCTCCTCGGGCGCCAGCAGAGCGGC
TCCCAGTTCGCCCTCTTCTCGGATATTCTCTCAGGCCTGCCTTTCATTGGCTTCTTCTGG
GCCAAATCCCCCCCTGAATCAGAAAATAAGGAGCAGCTCGAGGCCAGGAGGCGCAGAAAA
GGAACCAATATTTCAGAAACAAGCTTAATAGGAACAGCTGCCTGTACATCAACATCTTCT
CAGAATGACCCAGAAGTTATCATCGTGGGAGCTGGCGTGCTTGGCTCTGCTTTGGCAGCT
GTGCTTTCCAGAGATGGAAGAAAGGTGACAGTCATTGAGAGAGACTTAAAAGAGCCTGAC
AGAATAGTTGGAGAATTCCTGCAGCCGGGTGGTTATCATGTTCTCAAAGACCTTGGTCTT
GGAGATACAGTGGAAGGTCTTGATGCCCAGGTTGTAAATGGTTACATGATTCATGATCAG
GAAAGCAAATCAGAGGTTCAGATTCCTTACCCTCTGTCAGAAAACAATCAAGTGCAGAGT
GGAAGAGCTTTCCATCACGGAAGATTCATCATGAGTCTCCGGAAAGCAGCTATGGCAGAG
CCCAATGCAAAGTTTATTGAAGGTGTTGTGTTACAGTTATTAGAGGAAGATGATGTTGTG
ATGGGAGTTCAGTACAAGGATAAAGAGACTGGAGATATCAAGGAACTCCATGCTCCACTG
ACTGTTGTTGCAGATGGGCTTTTCTCCAAGTTCAGGAAAAGCCTGGTCTCCAATAAAGTT
TCTGTATCATCTCATTTTGTTGGCTTTCTTATGAAGAATGCACCACAGTTTAAAGCAAAT
CATGCTGAACTTATTTTAGCTAACCCGAGTCCAGTTCTCATCTACCAGATTTCATCCAGT
GAAACTCGAGTACTTGTTGACATTAGAGGAGAAATGCCAAGGAATTTAAGAGAATACATG
GTTGAAAAAATTTACCCACAAATACCTGATCACCTGAAAGAACCATTCTTAGAAGCCACT
GACAATTCTCATCTGAGGTCCATGCCAGCAAGCTTCCTTCCTCCTTCATCAGTGAAGAAA
CGAGGTGTTCTTCTTTTGGGAGACGCATATAATATGAGGCATCCACTTACTGGTGGAGGA
ATGACTGTTGCTTTTAAAGATATAAAACTATGGAGAAAACTGCTAAAGGGTATCCCTGAC
CTTTATGATGATGCAGCTATTTTCGAGGCCAAAAAATCATTTTACTGGGCAAGAAAAACA
TCTCATTCCTTTGTCGTGAATATCCTTGCTCAGGCTCTTTATGAATTATTTTCTGCCACA
GATGATTCCCTGCATCAACTAAGAAAAGCCTGTTTTCTTTATTTCAAACTTGGTGGCGAA
TGTGTTGCGGGTCCTGTTGGGCTGCTTTCTGTATTGTCTCCTAACCCTCTAGTTTTAATT
GGACACTTCTTTGCTGTTGCAATCTATGCCGTGTATTTTTGCTTTAAGTCAGAACCTTGG
ATTACAAAACCTCGAGCCCTTCTCAGTAGTGGTGCTGTATTGTACAAAGCGTGTTCTGTA
ATATTTCCTCTAATTTACTCAGAAATGAAGTATATGGTTCATTAA
Enzyme 1 GenBank Gene ID NM_003129.3 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. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  3. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed Link Image]
  4. 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 synthase
Enzyme 2 Synonyms
  1. SQS
  2. SS
  3. FPP:FPP farnesyltransferase
  4. Farnesyl-diphosphate farnesyltransferase
Enzyme 2 Gene Name FDFT1
Enzyme 2 Protein Sequence >Squalene synthase
MEFVKCLGHPEEFYNLVRFRIGGKRKVMPKMDQDSLSSSLKTCYKYLNQTSRSFAAVIQA
LDGEMRNAVCIFYLVLRALDTLEDDMTISVEKKVPLLHNFHSFLYQPDWRFMESKEKDRQ
VLEDFPTISLEFRNLAEKYQTVIADICRRMGIGMAEFLDKHVTSEQEWDKYCHYVAGLVG
IGLSRLFSASEFEDPLVGEDTERANSMGLFLQKTNIIRDYLEDQQGGREFWPQEVWSRYV
KKLGDFAKPENIDLAVQCLNELITNALHHIPDVITYLSRLRNQSVFNFCAIPQVMAIATL
AACYNNQQVFKGAVKIRKGQAVTLMMDATNMPAVKAIIYQYMEEIYHRIPDSDPSSSKTR
QIISTIRTQNLPNCQLISRSHYSPIYLSFVMLLAALSWQYLTTLSQVTEDYVQTGEH
Enzyme 2 Number of Residues 417
Enzyme 2 Molecular Weight 48114.9
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
  • biosynthetic process
  • lipid biosynthetic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 2 General Function Involved in transferase activity
Enzyme 2 Specific Function 2 farnesyl diphosphate = diphosphate + presqualene diphosphate
Enzyme 2 Pathways
Enzyme 2 Reactions
  • (1) (1a) 2 farnesyl diphosphate = diphosphate + presqualene diphosphate [RN:R00702]
  • (2) (1b) presqualene diphosphate + NAD(P)H + H+ = squalene + diphosphate + NAD(P)+ [RN:R02872]
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 Not Available
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]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Pandit J, Danley DE, Schulte GK, Mazzalupo S, Pauly TA, Hayward CM, Hamanaka ES, Thompson JF, Harwood HJ Jr: Crystal structure of human squalene synthase. A key enzyme in cholesterol biosynthesis. J Biol Chem. 2000 Sep 29;275(39):30610-7. [PubMed Link Image]
  7. Do R, Pare G, Montpetit A, Hudson TJ, Gaudet D, Engert JC: K45R variant of squalene synthase increases total cholesterol levels in two study samples from a French Canadian population. Hum Mutat. 2008 May;29(5):689-94. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 7051
Enzyme 3 Name Serine palmitoyltransferase 1
Enzyme 3 Synonyms
  1. Long chain base biosynthesis protein 1
  2. LCB 1
  3. Serine-palmitoyl-CoA transferase 1
  4. SPT 1
  5. SPT1
Enzyme 3 Gene Name SPTLC1
Enzyme 3 Protein Sequence >Serine palmitoyltransferase 1
MATATEQWVLVEMVQALYEAPAYHLILEGILILWIIRLLFSKTYKLQERSDLTVKEKEEL
IEEWQPEPLVPPVPKDHPALNYNIVSGPPSHKTVVNGKECINFASFNFLGLLDNPRVKAA
ALASLKKYGVGTCGPRGFYGTFDVHLDLEDRLAKFMKTEEAIIYSYGFATIASAIPAYSK
RGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDQKNPRKARVTRR
FIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGINIDDI
DLISANMENALASIGGFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENP
GIFAVLKEKCGQIHKALQGISGLKVVGESLSPAFHLQLEESTGSREQDVRLLQEIVDQCM
NRSIALTQARYLEKEEKCLPPPSIRVVVTVEQTEEELERAASTIKEVAQAVLL
Enzyme 3 Number of Residues 473
Enzyme 3 Molecular Weight 52743.4
Enzyme 3 Theoretical pI 5.87
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • pyridoxal phosphate binding
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthetic process
  • metabolic process
Component
Enzyme 3 General Function Involved in transferase activity, transferring nitrogenous groups
Enzyme 3 Specific Function Serine palmitoyltransferase (SPT). The heterodimer formed with LCB2 (SPTLC2 or SPTLC3) constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2- SSSPTA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SSSPTA isozyme uses both C14-CoA and C16- CoA as substrates, with a slight preference for C14-CoA. The SPTLC1-SPTLC2-SSSPTB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SSSPTB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 [RN:R01281]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 16-36
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 2564247 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O15269 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name SPTC1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1422 bp
ATGGCGACCGCCACGGAGCAGTGGGTTCTGGTGGAGATGGTACAGGCGCTTTACGAGGCT
CCTGCTTACCATCTTATTTTGGAAGGGATTCTGATCCTCTGGATAATCAGACTTCTTTTC
TCTAAGACTTACAAATTACAAGAACGATCTGATCTTACAGTCAAGGAAAAAGAAGAACTG
ATTGAAGAGTGGCAACCAGAACCTCTTGTTCCTCCTGTCCCAAAAGACCATCCTGCTCTC
AACTACAACATCGTTTCAGGCCCTCCAAGCCACAAAACTGTGGTGAATGGAAAAGAATGT
ATAAACTTCGCCTCATTTAATTTTCTTGGATTGTTGGATAACCCTAGGGTTAAGGCAGCA
GCTTTAGCATCTCTAAAGAAGTATGGCGTGGGGACTTGTGGACCCAGAGGATTTTATGGC
ACATTTGATGTTCATTTGGATTTGGAAGACCGCCTGGCAAAATTTATGAAGACAGAAGAA
GCCATTATATACTCATATGGATTTGCCACCATAGCCAGTGCTATTCCTGCTTACTCTAAA
AGAGGGGACATTGTTTTTGTAGATAGAGCTGCCTGCTTTGCTATTCAGAAAGGATTACAG
GCATCCCGTAGTGACATTAAGTTATTTAAGCATAATGACATGGCTGACCTCGAGCGACTA
CTAAAAGAACAAGAGATCGAAGATCAAAAGAATCCTCGCAAGGCTCGTGTAACTCGGCGT
TTCATTGTAGTAGAAGGATTGTATATGAATACTGGAACTATTTGTCCTCTTCCAGAATTG
GTTAAGTTAAAATACAAATACAAAGCAAGAATCTTCCTGGAGGAAAGCCTTTCATTTGGA
GTCCTAGGAGAGCATGGCCGAGGAGTCACTGAACACTATGGAATCAATATTGATGATATT
GATCTTATCAGTGCCAACATGGAGAATGCACTTGCTTCTATTGGAGGTTTCTGCTGTGGC
AGGTCTTTTGTAATTGACCATCAGCGACTTTCCGGCCAGGGATACTGCTTTTCAGCTTCG
TTACCTCCCCTGTTAGCTGCTGCAGCAATTGAGGCCCTCAACATCATGGAAGAGAATCCA
GGTATTTTTGCAGTGTTGAAGGAAAAGTGCGGACAAATTCATAAAGCTTTACAAGGCATT
TCTGGATTAAAAGTGGTGGGGGAGTCCCTTTCTCCAGCCTTTCACCTACAACTGGAAGAG
AGCACTGGGTCTCGCGAGCAAGATGTCAGACTGCTTCAGGAAATTGTAGATCAATGCATG
AACAGAAGTATTGCATTAACTCAGGCGCGCTACTTGGAGAAAGAAGAGAAGTGTCTCCCT
CCTCCCAGCATTCGGGTTGTGGTCACGGTGGAACAAACAGAGGAAGAACTGGAGAGAGCT
GCGTCCACCATCAAGGAGGTAGCCCAGGCCGTCCTGCTCTAG
Enzyme 3 GenBank Gene ID Y08685 Link Image
Enzyme 3 GeneCard ID SPTLC1 Link Image
Enzyme 3 GenAtlas ID SPTLC1 Link Image
Enzyme 3 HGNC ID HGNC:11277 Link Image
Enzyme 3 Chromosome Location 9
Enzyme 3 Locus 9q22.2
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Weiss B, Stoffel W: Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis. Eur J Biochem. 1997 Oct 1;249(1):239-47. [PubMed Link Image]
  2. Dawkins JL, Hulme DJ, Brahmbhatt SB, Auer-Grumbach M, Nicholson GA: Mutations in SPTLC1, encoding serine palmitoyltransferase, long chain base subunit-1, cause hereditary sensory neuropathy type I. Nat Genet. 2001 Mar;27(3):309-12. [PubMed Link Image]
  3. 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 TO, 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: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  5. Hornemann T, Richard S, Rutti MF, Wei Y, von Eckardstein A: Cloning and initial characterization of a new subunit for mammalian serine-palmitoyltransferase. J Biol Chem. 2006 Dec 8;281(49):37275-81. Epub 2006 Oct 4. [PubMed Link Image]
  6. Han G, Gupta SD, Gable K, Niranjanakumari S, Moitra P, Eichler F, Brown RH Jr, Harmon JM, Dunn TM: Identification of small subunits of mammalian serine palmitoyltransferase that confer distinct acyl-CoA substrate specificities. Proc Natl Acad Sci U S A. 2009 May 19;106(20):8186-91. Epub 2009 May 5. [PubMed Link Image]
  7. Breslow DK, Collins SR, Bodenmiller B, Aebersold R, Simons K, Shevchenko A, Ejsing CS, Weissman JS: Orm family proteins mediate sphingolipid homeostasis. Nature. 2010 Feb 25;463(7284):1048-53. [PubMed Link Image]
  8. Verhoeven K, Coen K, De Vriendt E, Jacobs A, Van Gerwen V, Smouts I, Pou-Serradell A, Martin JJ, Timmerman V, De Jonghe P: SPTLC1 mutation in twin sisters with hereditary sensory neuropathy type I. Neurology. 2004 Mar 23;62(6):1001-2. [PubMed Link Image]
  9. Meggouh F, Bienfait HM, Weterman MA, de Visser M, Baas F: Charcot-Marie-Tooth disease due to a de novo mutation of the RAB7 gene. Neurology. 2006 Oct 24;67(8):1476-8. [PubMed Link Image]
  10. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [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 63793.4
Enzyme 4 Theoretical pI 8.73
Enzyme 4 GO Classification
Function
  • FAD or FADH2 binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • monooxygenase activity
  • nucleoside binding
  • oxidoreductase activity
  • purine nucleoside binding
  • squalene monooxygenase activity
Process
  • metabolic process
  • oxidation reduction
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 4 General Function Involved in oxidoreductase activity
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 >1725 bp
ATGTGGACTTTTCTGGGCATTGCCACTTTCACCTATTTTTATAAGAAGTTCGGGGACTTC
ATCACTTTGGCCAACAGGGAGGTCCTGTTGTGCGTGCTGGTGTTCCTCTCGCTGGGCCTG
GTGCTCTCCTACCGCTGTCGCCACCGAAACGGGGGTCTCCTCGGGCGCCAGCAGAGCGGC
TCCCAGTTCGCCCTCTTCTCGGATATTCTCTCAGGCCTGCCTTTCATTGGCTTCTTCTGG
GCCAAATCCCCCCCTGAATCAGAAAATAAGGAGCAGCTCGAGGCCAGGAGGCGCAGAAAA
GGAACCAATATTTCAGAAACAAGCTTAATAGGAACAGCTGCCTGTACATCAACATCTTCT
CAGAATGACCCAGAAGTTATCATCGTGGGAGCTGGCGTGCTTGGCTCTGCTTTGGCAGCT
GTGCTTTCCAGAGATGGAAGAAAGGTGACAGTCATTGAGAGAGACTTAAAAGAGCCTGAC
AGAATAGTTGGAGAATTCCTGCAGCCGGGTGGTTATCATGTTCTCAAAGACCTTGGTCTT
GGAGATACAGTGGAAGGTCTTGATGCCCAGGTTGTAAATGGTTACATGATTCATGATCAG
GAAAGCAAATCAGAGGTTCAGATTCCTTACCCTCTGTCAGAAAACAATCAAGTGCAGAGT
GGAAGAGCTTTCCATCACGGAAGATTCATCATGAGTCTCCGGAAAGCAGCTATGGCAGAG
CCCAATGCAAAGTTTATTGAAGGTGTTGTGTTACAGTTATTAGAGGAAGATGATGTTGTG
ATGGGAGTTCAGTACAAGGATAAAGAGACTGGAGATATCAAGGAACTCCATGCTCCACTG
ACTGTTGTTGCAGATGGGCTTTTCTCCAAGTTCAGGAAAAGCCTGGTCTCCAATAAAGTT
TCTGTATCATCTCATTTTGTTGGCTTTCTTATGAAGAATGCACCACAGTTTAAAGCAAAT
CATGCTGAACTTATTTTAGCTAACCCGGGTCCAGTTCTCATCTACCAGATTTCATCCAGT
GAAACTCGAGTACTTGTTGACATTAGAGGAGAAATGCCAAGGAATTTAAGAGAATACATG
GTTGAAAAAATTTACCCACAAATACCTGATCACCTGAAAGAACCATTCTTAGAAGCCACT
GACAATTCTCATCTGAGGTCCATGCCAGCAAGCTTCCTTCCTCCTTCATCAGTGAAGAAA
CGAGGTGTTCTTCTTTTGGGAGACGCATATAATATGAGGCATCCACTTACTGGTGGAGGA
ATGACTGTTGCTTTTAAAGATATAAAACTATGGAGAAAACTGCTAAAGGGTATCCCTGAC
CTTTATGATGATGCAGCTATTTTCGAGGCCAAAAAATCATTTTACTGGGCAAGAAAAACA
TCTCATTCCTTTGTCGTGAATATCCTTGCTCAGGCTCTTTATGAATTATTTTCTGCCACA
GATGATTCCCTGCATCAACTAGGAAAAGCCTGTTTTCTTTATTTCAAACTTGGTGGCGAA
TGTGTTGCGGGTCCTGTTGGGCTGCTTTCTGTATTGTCTCCTAACCCTCTAGTTTTAATT
GGACACTTCTTTGCTGTTGCAATCTATGCCGTGTATTTTTGCTTTAAGTCAGAACCTTGG
ATTACAAAACCTCGAGCCCTTCTCAGTAGTGGTGCTGTATTGTACAAAGCGTGTTCTGTA
ATATTTCCTCTAATTTACTCAGAAATGAAGTATATGGTTCATTAA
Enzyme 4 GenBank Gene ID BX647605 Link Image
Enzyme 4 GeneCard ID DKFZp686B0215 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 46047.8
Enzyme 5 Theoretical pI 5.97
Enzyme 5 GO Classification
Function
  • transporter activity
Process
  • establishment of localization
  • transport
Component
  • cell part
  • intracellular
Enzyme 5 General Function Involved in transporter activity
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 >1203 bp
ATGAGCGGCCGAGTTGGAGACCTGAGCCCCAAACAGGCAGAGACCCTGGCCAAGTTCCGA
GAAAACGTCCAGGATGTGCTTCCTGCCCTGCCCAACCCTGATGATTATTTCCTTCTACGC
TGGCTCCGAGCTCGGAATTTTGACTTGCAGAAGTCGGAGGCTTTGCTCCGCAAGTACATG
GAGTTCCGGAAGACCATGGATATTGACCATATCCTTGATTGGCAGCCCCCAGAGGTGATC
CAGAAGTACATGCCTGGGGGCCTGTGTGGCTATGACCGTGATGGCTGCCCCGTGTGGTAT
GACATCATTGGGCCACTTGATCCCAAGGGGTTGCTCTTCTCAGTCACCAAGCAGGACCTG
CTCAAGACCAAGATGAGGGACTGTGAGCGCATCCTGCATGAGTGTGACCTGCAGACAGAG
AGGCTAGGGAAGAAGATTGAGACCATCGTGATGATATTTGACTGTGAGGGCCTGGGACTG
AAACACTTCTGGAAACCTCTGGTAGAAGTGTACCAGGAGTTCTTTGGCCTCCTTGAAGAG
AATTACCCAGAGACCCTGAAGTTCATGCTCATCGTGAAAGCTACCAAACTGTTCCCTGTG
GGCTACAACCTCATGAAGCCATTCCTGAGTGAGGACACTCGCAGGAAAATTATTGTGTTG
GGAAATAACTGGAAGGAAGGTTTGCTGAAACTCATCAGTCCTGAGGAACTGCCTGCCCAG
TTTGGGGGCACCCTGACTGACCCAGATGGGAACCCCAAATGTTTAACCAAGATTAACTAT
GGCGGGGAGATCCCCAAGTCCATGTACGTGCGGGACCAGGTGAAGACTCAGTACGAGCAC
TCGGTGCAGATCAACCGCGGCTCATCACACCAAGTGGAATACGAGATCCTATTTCCAGGC
TGCGTTCTCAGGTGGCAGTTCTCATCTGATGGTGCGGACATCGGCTTCGGAGTTTTCCTG
AAGACCAAGATGGGGGAGCGACAGCGGGCAGGGGAGATGACAGATGTTCTACCCAGCCAG
CGCTATAACGCCCACATGGTGCCCGAGGATGGGAACCTCACCTGCTCAGAGGCCGGCGTC
TATGTCCTACGCTTCGACAACACCTATAGCTTTGTCCACGCCAAGAAGGTCAGCTTCACA
GTGGAGGTCCTGCTCCCTGACGAGGGCATGCAGAAATATGATAAGGAGCTCACCCCTGTC
TAG
Enzyme 5 GenBank Gene ID AY158086 Link Image
Enzyme 5 GeneCard ID SEC14L3 Link Image
Enzyme 5 GenAtlas ID SEC14L3 Link Image
Enzyme 5 HGNC ID HGNC:18655 Link Image
Enzyme 5 Chromosome Location 2
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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [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 46643.4
Enzyme 6 Theoretical pI 6.52
Enzyme 6 GO Classification
Function
  • transporter activity
Process
  • establishment of localization
  • transport
Component
  • cell part
  • intracellular
Enzyme 6 General Function Involved in transporter activity
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 >1221 bp
ATGAGCAGCCGAGTCGGGGACCTGAGCCCCCAGCAGCAGGAAGCGCTGGCCAGGTTCCGG
GAGAACCTCCAGGACCTGCTGCCCATACTGCCCAATGCTGATGACTACTTCCTCCTGCGC
TGGCTGCGAGCTCGAAACTTTGACCTGCAGAAATCCGAAGACATGCTCCGAAGGCACATG
GAGTTCCGGAAGCAACAAGACCTGGACAACATTGTCACATGGCAGCCCCCTGAGGTCATC
CAGCTGTATGACTCGGGTGGTCTTTGTGGCTACGACTACGAAGGCTGCCCTGTGTACTTC
AACATCATTGGGTCCCTCGACCCCAAGGGTCTCCTGCTGTCAGCCTCCAAGCAGGATATG
ATCCGGAAGCGCATCAAAGTCTGTGAGCTGCTGTTGCATGAGTGTGAGCTGCAAACTCAG
AAGCTGGGCAGGAAGATCGAGATGGCGCTGATGGTGTTTGACATGGAGGGGCTGAGCCTG
AAACACCTGTGGAAGCCAGCTGTGGAGGTCTACCAGCAGTTTTTTAGCATCCTGGAAGCA
AATTATCCTGAGACCCTGAAGAATTTAATTGTTATTCGAGCCCCAAAACTGTTCCCCGTG
GCCTTCAACTTGGTCAAGTCGTTCATGAGTGAGGAGACACGCAGGAAGATTGTGATTCTG
GGAGACAACTGGAAGCAGGAGCTGACAAAATTCATCAGCCCCGACCAGCTGCCTGTGGAG
TTTGGGGGGACCATGACTGACCCCGATGGCAACCCCAAGTGCCTGACCAAGATCAACTAT
GGGGGTGAGGTGCCCAAGAGCTACTACCTGTGCGAGCAGGTGAGGCTGCAGTATGAGCAC
ACGAGGTCCGTGGGCCGCGGCTCCTCCCTGCAGGTGGAGAACGAGATCCTGTTCCCGGGC
TGTGTGCTCAGGTGGCAGTTTGCTTCAGATGGTGGGGACATCGGCTTTGGGGTTTTCCTG
AAGACCAAGATGGGGGAGCAGCAGAGTGCTAGGGAGATGACGGAGGTGCTGCCCAGCCAG
CGCTACAATGCCCACATGGTGCCTGAGGATGGGAGCCTCACCTGCCTCCAGGCTGGCGTC
TATGTCCTGCGCTTCGACAACACCTACAGCCGGATGCATGCCAAGAAGCTCAGCTACACT
GTGGAGGTGCTGCTTCCCGACAAGGCCTCTGAGGAGACGCTGCAGAGTCTCAAGGCGATG
AGACCCTCCCCAACACAGTGA
Enzyme 6 GenBank Gene ID AY158085 Link Image
Enzyme 6 GeneCard ID SEC14L4 Link Image
Enzyme 6 GenAtlas ID SEC14L4 Link Image
Enzyme 6 HGNC ID HGNC:20627 Link Image
Enzyme 6 Chromosome Location 2
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