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Human Metabolome Database Version 2.5

 

Showing metabocard for Chenodeoxycholic acid (HMDB00518)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-26 12:57:13
Accession Number HMDB00518
Secondary Accession Numbers Not Available
Common Name Chenodeoxycholic acid
Description A bile acid. Bile acids are steroid acids found predominantly in bile of mammals. The distinction between different bile acids is minute, depends only on presence or absence of hydroxyl groups on positions 3, 7, and 12. Bile acids are physiological detergents that facilitate excretion, absorption, and transport of fats and sterols in the intestine and liver. Bile acids are also steroidal amphipathic molecules derived from the catabolism of cholesterol. They modulate bile flow and lipid secretion, are essential for the absorption of dietary fats and vitamins, and have been implicated in the regulation of all the key enzymes involved in cholesterol homeostasis. Bile acids recirculate through the liver, bile ducts, small intestine and portal vein to form an enterohepatic circuit. They exist as anions at physiological pH and, consequently, require a carrier for transport across the membranes of the enterohepatic tissues. The unique detergent properties of bile acids are essential for the digestion and intestinal absorption of hydrophobic nutrients. Bile acids have potent toxic properties (e.g., membrane disruption) and there are a plethora of mechanisms to limit their accumulation in blood and tissues. (PMID: 11316487, 16037564, 12576301, 11907135) Usually conjugated with either glycine or taurine. It acts as a detergent to solubilize fats for intestinal absorption and is reabsorbed by the small intestine. It is used as cholagogue, a choleretic laxative, and to prevent or dissolve gallstones.
Synonyms
  1. (+)-chenodeoxycholate
  2. (+)-chenodeoxycholic acid
  3. (3a,5b,7a)-3,7-dihydroxy-cholan-24-oate
  4. (3a,5b,7a)-3,7-dihydroxy-cholan-24-oic acid
  5. 3a,7a-dihydroxy-5b,14a,17b-cholanate
  6. 3a,7a-dihydroxy-5b,14a,17b-cholanic acid
  7. 3a,7a-dihydroxy-5b-cholan-24-oate
  8. 3a,7a-dihydroxy-5b-cholan-24-oic acid
  9. 3a,7a-dihydroxy-5b-cholanate
  10. 3a,7a-dihydroxy-5b-cholanic acid
  11. 7a-Hydroxy-desoxycholsaeure
  12. Chenodeoxycholate
  13. Chenodesoxycholsaeure
Chemical IUPAC Name (4R)-4-[(3R,5S,7R,8S,9S,10R,13R,14S,17R)-3,7-dihydroxy-10,13-dimethyl-2,3,4
Chemical Formula C24H40O4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Cholesterols and derivatives
Class
  • Bile Acids
Sub Class
  • Dihydroxy bile acids
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • carboxylic acid
Biofunction
  • Fat solubilization and Waste products
Application
—
Source
  • Endogenous
Average Molecular Weight 392.572
Monoisotopic Molecular Weight 392.292664
Isomeric SMILES C[C@H](CCC(O)=O)[C@H]1CC[C@H]2[C@@H]3[C@H](O)C[C@@H]4C[C@H](O)CC[C@]4(C)[C@H]3CC[C@]12C
Canonical SMILES CC(CCC(O)=O)C1CCC2C3C(O)CC4CC(O)CCC4(C)C3CCC12C
KEGG Compound ID C02528 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Chenodeoxycholic acid Link Image
NuGOwiki Link HMDB00518 Link Image
Metagene Link HMDB00518 Link Image
METLIN ID 207 Link Image
PubChem Compound 10133 Link Image
PubChem Substance 8157307 Link Image
ChEBI ID 16755 Link Image
CAS Registry Number 474-25-9
InChI Identifier InChI=1/C24H40O4/c1-14(4-7-21(27)28)17-5-6-18-22-19(9-11-24(17,18)3)23(2)10-8-16(25)12-15(23)13-20(22)26/h14-20,22,25-26H,4-13H2,1-3H3,(H,27,28)/t14-,15+,16-,17-,18+,19+,20-,22+,23+,24-/m1/s1
Synthesis Reference Sato, Yoshio; Ikekawa, Nobuo. Preparation of chenodeoxycholic acid. Journal of Organic Chemistry (1959), 24 1367-8.
Melting Point (Experimental) 165-167 oC
Experimental Water Solubility 0.0899 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 0.0197 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity 4.15 [SANGSTER (1993)] Source: PhysProp
Predicted LogP/Hydrophobicity 3.01 [Predicted by ALOGPS]; 4.9 [Predicted by PubChem via XLOGP] 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)
Biofluid Location
  • Bile
  • Blood
  • Urine
Tissue Location
Tissue References
Fibroblasts —
Liver —
Concentrations (Normal)
Biofluid Bile
Value 5530 (5400-5660) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Tadano T, Kanoh M, Matsumoto M, Sakamoto K, Kamano T: Studies of serum and feces bile acids determination by gas chromatography-mass spectrometry. Rinsho Byori. 2006 Feb;54(2):103-10. [PubMed Link Image]
Biofluid Blood
Value 0.98 +/- 0.66 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 1.35 +/- 0.27 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Smith JL, Lewindon PJ, Hoskins AC, Pereira TN, Setchell KD, O'Connell NC, Shepherd RW, Ramm GA: Endogenous ursodeoxycholic acid and cholic acid in liver disease due to cystic fibrosis. Hepatology. 2004 Jun;39(6):1673-82. [PubMed Link Image]
Biofluid Blood
Value 1.8 +/- 0.4 uM
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Gustafsson J, Alvelius G, Bjorkhem I, Nemeth A: Bile acid metabolism in extrahepatic biliary atresia: lithocholic acid in stored dried blood collected at neonatal screening. Ups J Med Sci. 2006;111(1):131-6. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 2.83 +/- 0.42 uM
Age Adult:>18 yrs old
Sex Both
Condition Cystic fibrosis
Comments Cystic fibrosis associated with liver disease (CFLD)
References
  • Smith JL, Lewindon PJ, Hoskins AC, Pereira TN, Setchell KD, O'Connell NC, Shepherd RW, Ramm GA: Endogenous ursodeoxycholic acid and cholic acid in liver disease due to cystic fibrosis. Hepatology. 2004 Jun;39(6):1673-82. [PubMed Link Image]
Biofluid Blood
Value 2.75 +/- 0.56 uM
Age Children:1-13 yrs old
Sex Both
Condition Cystic fibrosis
Comments Not Available
References
  • Smith JL, Lewindon PJ, Hoskins AC, Pereira TN, Setchell KD, O'Connell NC, Shepherd RW, Ramm GA: Endogenous ursodeoxycholic acid and cholic acid in liver disease due to cystic fibrosis. Hepatology. 2004 Jun;39(6):1673-82. [PubMed Link Image]
Biofluid Blood
Value 7.4 +/- 2.5 uM
Age Newborn:0-30 days old
Sex Both
Condition Biliary atresia
Comments Not Available
References
  • Gustafsson J, Alvelius G, Bjorkhem I, Nemeth A: Bile acid metabolism in extrahepatic biliary atresia: lithocholic acid in stored dried blood collected at neonatal screening. Ups J Med Sci. 2006;111(1):131-6. [PubMed Link Image]
Biofluid Blood
Value 22.0 (3.3-46.3) uM
Age Adult:>18 yrs old
Sex Both
Condition Primary biliary cirrhosis
Comments Patients with biliary cirrhosis before ursodeoxycholic acid treatment
References
  • Batta AK, Arora R, Salen G, Tint GS, Eskreis D, Katz S: Characterization of serum and urinary bile acids in patients with primary biliary cirrhosis by gas-liquid chromatography-mass spectrometry: effect of ursodeoxycholic acid treatment. J Lipid Res. 1989 Dec;30(12):1953-62. [PubMed Link Image]
Biofluid Blood
Value 11.0 (0.8-28.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Primary biliary cirrhosis
Comments Patients with biliary cirrhosis after ursodeoxycholic acid treatment
References
  • Batta AK, Arora R, Salen G, Tint GS, Eskreis D, Katz S: Characterization of serum and urinary bile acids in patients with primary biliary cirrhosis by gas-liquid chromatography-mass spectrometry: effect of ursodeoxycholic acid treatment. J Lipid Res. 1989 Dec;30(12):1953-62. [PubMed Link Image]
Biofluid Urine
Value 1.4 (0.14-2.9) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Primary biliary cirrhosis
Comments Patients with biliary cirrhosis before ursodeoxycholic acid treatment
References
  • Batta AK, Arora R, Salen G, Tint GS, Eskreis D, Katz S: Characterization of serum and urinary bile acids in patients with primary biliary cirrhosis by gas-liquid chromatography-mass spectrometry: effect of ursodeoxycholic acid treatment. J Lipid Res. 1989 Dec;30(12):1953-62. [PubMed Link Image]
Biofluid Urine
Value 1.1 (0.04-3.3) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Primary biliary cirrhosis
Comments Patients with biliary cirrhosis after ursodeoxycholic acid treatment
References
  • Batta AK, Arora R, Salen G, Tint GS, Eskreis D, Katz S: Characterization of serum and urinary bile acids in patients with primary biliary cirrhosis by gas-liquid chromatography-mass spectrometry: effect of ursodeoxycholic acid treatment. J Lipid Res. 1989 Dec;30(12):1953-62. [PubMed Link Image]
Biofluid Urine
Value 0.0092 +/- 0.013 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Biliary atresia
Comments Not Available
References
  • Nittono H, Obinata K, Nakatsu N, Watanabe T, Niijima S, Sasaki H, Arisaka O, Kato H, Yabuta K, Miyano T: Sulfated and nonsulfated bile acids in urine of patients with biliary atresia: analysis of bile acids by high-performance liquid chromatography. J Pediatr Gastroenterol Nutr. 1986 Jan;5(1):23-9. [PubMed Link Image]
Associated Disorders
Condition References
Biliary atresia
Cystic fibrosis
  • Smith JL, Lewindon PJ, Hoskins AC, Pereira TN, Setchell KD, O'Connell NC, Shepherd RW, Ramm GA: Endogenous ursodeoxycholic acid and cholic acid in liver disease due to cystic fibrosis. Hepatology. 2004 Jun;39(6):1673-82. [PubMed Link Image]
Primary biliary cirrhosis
  • Batta AK, Arora R, Salen G, Tint GS, Eskreis D, Katz S: Characterization of serum and urinary bile acids in patients with primary biliary cirrhosis by gas-liquid chromatography-mass spectrometry: effect of ursodeoxycholic acid treatment. J Lipid Res. 1989 Dec;30(12):1953-62. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Bile Acid Biosynthesis SMP00035 Link Image map00120 Link Image
General References
  1. Fiorucci S, Antonelli E, Morelli A: Nitric oxide and portal hypertension: a nitric oxide-releasing derivative of ursodeoxycholic acid that selectively releases nitric oxide in the liver. Dig Liver Dis. 2003 May;35 Suppl 2:S61-9. [PubMed Link Image]
  2. Meyers RL, Book LS, O'Gorman MA, Jackson WD, Black RE, Johnson DG, Matlak ME: High-dose steroids, ursodeoxycholic acid, and chronic intravenous antibiotics improve bile flow after Kasai procedure in infants with biliary atresia. J Pediatr Surg. 2003 Mar;38(3):406-11. [PubMed Link Image]
  3. Soderdahl G, Nowak G, Duraj F, Wang FH, Einarsson C, Ericzon BG: Ursodeoxycholic acid increased bile flow and affects bile composition in the early postoperative phase following liver transplantation. Transpl Int. 1998;11 Suppl 1:S231-8. [PubMed Link Image]
  4. Nobilis M, Pour M, Kunes J, Kopecky J, Kvetina J, Svoboda Z, Sladkova K, Vortel J: High-performance liquid chromatographic determination of ursodeoxycholic acid after solid phase extraction of blood serum and detection-oriented derivatization. J Pharm Biomed Anal. 2001 Mar;24(5-6):937-46. [PubMed Link Image]
  5. Dohmen K, Mizuta T, Nakamuta M, Shimohashi N, Ishibashi H, Yamamoto K: Fenofibrate for patients with asymptomatic primary biliary cirrhosis. World J Gastroenterol. 2004 Mar 15;10(6):894-8. [PubMed Link Image]
  6. Lupton JR, Steinbach G, Chang WC, O'Brien BC, Wiese S, Stoltzfus CL, Glober GA, Wargovich MJ, McPherson RS, Winn RJ: Calcium supplementation modifies the relative amounts of bile acids in bile and affects key aspects of human colon physiology. J Nutr. 1996 May;126(5):1421-8. [PubMed Link Image]
  7. Hillaire S, Ballet F, Franco D, Setchell KD, Poupon R: Effects of ursodeoxycholic acid and chenodeoxycholic acid on human hepatocytes in primary culture. Hepatology. 1995 Jul;22(1):82-7. [PubMed Link Image]
  8. Kitani K, Kanai S, Ivy GO, Carrillo MC: Pharmacological modifications of endogenous antioxidant enzymes with special reference to the effects of deprenyl: a possible antioxidant strategy. Mech Ageing Dev. 1999 Nov;111(2-3):211-21. [PubMed Link Image]
  9. Smith JL, Lewindon PJ, Hoskins AC, Pereira TN, Setchell KD, O'Connell NC, Shepherd RW, Ramm GA: Endogenous ursodeoxycholic acid and cholic acid in liver disease due to cystic fibrosis. Hepatology. 2004 Jun;39(6):1673-82. [PubMed Link Image]
  10. Reyes H, Sjovall J: Bile acids and progesterone metabolites in intrahepatic cholestasis of pregnancy. Ann Med. 2000 Mar;32(2):94-106. [PubMed Link Image]
  11. Stark M, Jornvall H, Johansson J: Isolation and characterization of hydrophobic polypeptides in human bile. Eur J Biochem. 1999 Nov;266(1):209-14. [PubMed Link Image]
  12. Hofmann AF: The continuing importance of bile acids in liver and intestinal disease. Arch Intern Med. 1999 Dec 13-27;159(22):2647-58. [PubMed Link Image]
  13. Morton DH, Salen G, Batta AK, Shefer S, Tint GS, Belchis D, Shneider B, Puffenberger E, Bull L, Knisely AS: Abnormal hepatic sinusoidal bile acid transport in an Amish kindred is not linked to FIC1 and is improved by ursodiol. Gastroenterology. 2000 Jul;119(1):188-95. [PubMed Link Image]
  14. Virovic L, Supanc V, Duvnjak M: [Primary sclerosing cholangitis--diagnosis and therapy] Acta Med Croatica. 2003;57(3):207-19. [PubMed Link Image]
  15. Gatzen M, Pausch J: [Treatment of cholestatic liver diseases] Med Klin (Munich). 2002 Mar 15;97(3):152-9. [PubMed Link Image]
  16. Eriksson LS, Olsson R, Glauman H, Prytz H, Befrits R, Ryden BO, Einarsson K, Lindgren S, Wallerstedt S, Weden M: Ursodeoxycholic acid treatment in patients with primary biliary cirrhosis. A Swedish multicentre, double-blind, randomized controlled study. Scand J Gastroenterol. 1997 Feb;32(2):179-86. [PubMed Link Image]
  17. Lindblad A, Glaumann H, Strandvik B: A two-year prospective study of the effect of ursodeoxycholic acid on urinary bile acid excretion and liver morphology in cystic fibrosis-associated liver disease. Hepatology. 1998 Jan;27(1):166-74. [PubMed Link Image]
  18. Kowdley KV: Ursodeoxycholic acid therapy in hepatobiliary disease. Am J Med. 2000 Apr 15;108(6):481-6. [PubMed Link Image]
  19. Azer SA, Coverdale SA, Byth K, Farrell GC, Stacey NH: Sequential changes in serum levels of individual bile acids in patients with chronic cholestatic liver disease. J Gastroenterol Hepatol. 1996 Mar;11(3):208-15. [PubMed Link Image]
  20. Tadano T, Kanoh M, Matsumoto M, Sakamoto K, Kamano T: Studies of serum and feces bile acids determination by gas chromatography-mass spectrometry. Rinsho Byori. 2006 Feb;54(2):103-10. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Aldo-keto reductase family 1 member C1
  2. Aldo-keto reductase family 1 member C2
  3. Solute carrier organic anion transporter family member 1B3
  4. Solute carrier organic anion transporter family member 1B1
  5. Canalicular multispecific organic anion transporter 2
  6. Bile salt export pump
  7. Ileal sodium/bile acid cotransporter
  8. Sodium/bile acid cotransporter
  9. Solute carrier organic anion transporter family member 1A2
  10. Bile acyl-CoA synthetase
  11. Solute carrier organic anion transporter family member 4A1
  12. Gastrotropin
  13. cDNA FLJ41040 fis, clone LIVER1000017, highly similar to Bile acyl-CoA synthetase (EC 6.2.1.7)
Enzyme 1 [top]
Enzyme 1 ID 5623
Enzyme 1 Name Aldo-keto reductase family 1 member C1
Enzyme 1 Synonyms
  1. 20-alpha- hydroxysteroid dehydrogenase
  2. 20-alpha-HSD
  3. Trans- 1,2-dihydrobenzene-1,2-diol dehydrogenase
  4. High- affinity hepatic bile acid-binding protein
  5. HBAB
  6. Chlordecone reductase homolog HAKRC
  7. Dihydrodiol dehydrogenase 1/2
  8. DD1/DD2
Enzyme 1 Gene Name AKR1C1
Enzyme 1 Protein Sequence >Aldo-keto reductase family 1 member C1 
MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV
SVKPGEEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQLEMILNKP
GLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN
RNVRYLTLDIFAGPPNYPFSDEY
Enzyme 1 Number of Residues 323
Enzyme 1 Molecular Weight 36789
Enzyme 1 Theoretical pI 7.99
Enzyme 1 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
—
Component
—
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Converts progesterone to its inactive form, 20alpha- dihydroxyprogesterone (20alpha-OHP). In the liver and intestine, may have a role in the transport of bile. May have a role in monitoring the intrahepatic bile acid concentration. May play a role in myelin formation
Enzyme 1 Pathways
Enzyme 1 Reactions
  • trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 181549 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q04828 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name AK1C1_HUMAN Link Image
Enzyme 1 PDB ID 1MRQ Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >972 bp 
ATGGATTCGAAATATCAGTGTGTGAAGCTGAATGATGGTCACTTCATGCCTGTCCTGGGA
TTTGGCACCTATGCGCCTGCAGAGGTTCCTAAAAGTAAAGCTTTAGAGGCCACCAAATTG
GCAATTGAAGCTGGCTTCCGCCATATTGATTCTGCTCATTTATACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTGAAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGTGCAATTCCCATCGACCAGAGTTGGTCCGACCAGCCTTGGAA
AGGTCACTGAAAAATCTTCAATTGGATTATGTTGACCTCTACCTTATTCATTTTCCAGTG
TCTGTAAAGCCAGGTGAGGAAGTGATCCCAAAAGATGAAAATGGAAAAATACTATTTGAC
ACAGTGGATCTCTGTGCCACGTGGGAGGCCGTGGAGAAGTGTAAAGATGCAGGATTGGCC
AAGTCCATCGGGGTGTCCAACTTCAACCGCAGGCAGCTGGAGATGATCCTCAACAAGCCA
GGGCTCAAGTACAAGCCTGTCTGCAACCAGGTGGAATGTCATCCTTACTTCAACCAGAGA
AAACTGCTGGATTTCTGCAAGTCAAAAGACATTGTTCTGGTTGCCTATAGTGCTCTGGGA
TCCCACCGAGAAGAACCATGGGTGGACCCGAACTCCCCGGTGCTCTTGGAGGACCCAGTC
CTTTGTGCCTTGGCAAAAAAGCACAAGCGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTACAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGCATCAGACAGAAC
GTGCAGGTGTTTGAATTCCAGTTGACTTCAGAGGAGATGAAAGCCATAGATGGCCTAAAC
AGAAATGTGCGATATTTGACCCTTGATATTTTTGCTGGCCCCCCTAATTATCCATTTTCT
GATGAATATTAA
Enzyme 1 GenBank Gene ID M86609 Link Image
Enzyme 1 GeneCard ID AKR1C1 Link Image
Enzyme 1 GenAtlas ID AKR1C1 Link Image
Enzyme 1 HGNC ID HGNC:384 Link Image
Enzyme 1 Chromosome Location 10
Enzyme 1 Locus 10p15-p14
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Stolz A, Hammond L, Lou H, Takikawa H, Ronk M, Shively JE: cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family. J Biol Chem. 1993 May 15;268(14):10448-57. [PubMed Link Image]
  2. Lou H, Hammond L, Sharma V, Sparkes RS, Lusis AJ, Stolz A: Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding. J Biol Chem. 1994 Mar 18;269(11):8416-22. [PubMed Link Image]
  3. Khanna M, Qin KN, Cheng KC: Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans. J Steroid Biochem Mol Biol. 1995 Jun;53(1-6):41-6. [PubMed Link Image]
  4. Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed Link Image]
  5. Zhang Y, Dufort I, Rheault P, Luu-The V: Characterization of a human 20alpha-hydroxysteroid dehydrogenase. J Mol Endocrinol. 2000 Oct;25(2):221-8. [PubMed Link Image]
  6. Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed Link Image]
  7. Deyashiki Y, Ogasawara A, Nakayama T, Nakanishi M, Miyabe Y, Sato K, Hara A: Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder. Biochem J. 1994 Apr 15;299 ( Pt 2):545-52. [PubMed Link Image]
  8. Couture JF, Legrand P, Cantin L, Luu-The V, Labrie F, Breton R: Human 20alpha-hydroxysteroid dehydrogenase: crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids. J Mol Biol. 2003 Aug 15;331(3):593-604. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5624
Enzyme 2 Name Aldo-keto reductase family 1 member C2
Enzyme 2 Synonyms
  1. Trans-1,2- dihydrobenzene-1,2-diol dehydrogenase
  2. Type III 3- alpha-hydroxysteroid dehydrogenase
  3. 3-alpha-HSD3
  4. Chlordecone reductase homolog HAKRD
  5. Dihydrodiol dehydrogenase/bile acid-binding protein
  6. DD/BABP
  7. Dihydrodiol dehydrogenase 2
  8. DD2
Enzyme 2 Gene Name AKR1C2
Enzyme 2 Protein Sequence >Aldo-keto reductase family 1 member C2 
MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV
SVKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNHRLLEMILNKP
GLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN
RNVRYLTLDIFAGPPNYPFSDEY
Enzyme 2 Number of Residues 323
Enzyme 2 Molecular Weight 36736
Enzyme 2 Theoretical pI 7.55
Enzyme 2 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
—
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Works in concert with the 5alpha/5beta-steroid reductases to convert steroid hormones into the 3alpha/5alpha and 3alpha/5beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5alpha-DHT) to 5-alpha-androstane-3alpha,17beta-diol (3-alpha-diol)
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 531160 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P52895 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name AK1C2_HUMAN Link Image
Enzyme 2 PDB ID 1IHI Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >972 bp 
ATGGATTCGAAATACCAGTGTGTGAAGCTGAATGATGGTCACTTCATGCCTGTCCTGGGA
TTTGGCACCTATGCGCCTGCAGAGGTTCCTAAAAGTAAAGCTCTAGAGGCCGTCAAATTG
GCAATAGAAGCCGGGTTCCACCATATTGATTCTGCACATGTTTACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTGAAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGAGCAATTCCCATCGACCAGAGTTGGTCCGACCAGCCTTGGAA
AGGTCACTGAAAAATCTTCAATTGGACTATGTTGACCTCTATCTTATTCATTTTCCAGTG
TCTGTAAAGCCAGGTGAGGAAGTGATCCCAAAAGATGAAAATGGAAAAATACTATTTGAC
ACAGTGGATCTCTGTGCCACGTGGGAGGCCATGGAGAAGTGTAAAGATGCAGGATTGGCC
AAGTCCATCGGGGTGTCCAACTTCAACCACAGGCTGCTGGAGATGATCCTCAACAAGCCA
GGGCTCAAGTACAAGCCTGTCTGCAACCAGGTGGAATGTCATCCTTACTTCAACCAGAGA
AAACTGCTGGATTTCTGCAAGTCAAAAGACATTGTTCTGGTTGCCTATAGTGCTCTGGGA
TCCCATCGAGAAGAACCATGGGTGGACCCGAACTCCCCGGTGCTCTTGGAGGACCCAGTC
CTTTGTGCCTTGGCAAAAAAGCACAAGCGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTGCAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGCATCAGACAGAAC
GTGCAGGTGTTTGAATTCCAGTTGACTTCAGAGGAGATGAAAGCCATAGATGGCCTAAAC
AGAAATGTGCGATATTTGACCCTTGATATTTTTGCTGGCCCCCCTAATTATCCATTTTCT
GATGAATATTAA
Enzyme 2 GenBank Gene ID U05598 Link Image
Enzyme 2 GeneCard ID AKR1C2 Link Image
Enzyme 2 GenAtlas ID AKR1C2 Link Image
Enzyme 2 HGNC ID HGNC:385 Link Image
Enzyme 2 Chromosome Location 10
Enzyme 2 Locus 10p15-p14
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Ciaccio PJ, Tew KD: cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase. Biochim Biophys Acta. 1994 Jun 28;1186(1-2):129-32. [PubMed Link Image]
  2. Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed Link Image]
  3. Qin KN, Khanna M, Cheng KC: Structure of a gene coding for human dihydrodiol dehydrogenase/bile acid-binding protein. Gene. 1994 Nov 18;149(2):357-61. [PubMed Link Image]
  4. Shiraishi H, Ishikura S, Matsuura K, Deyashiki Y, Ninomiya M, Sakai S, Hara A: Sequence of the cDNA of a human dihydrodiol dehydrogenase isoform (AKR1C2) and tissue distribution of its mRNA. Biochem J. 1998 Sep 1;334 ( Pt 2):399-405. [PubMed Link Image]
  5. Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5684
Enzyme 3 Name Solute carrier organic anion transporter family member 1B3
Enzyme 3 Synonyms
  1. Solute carrier family 21 member 8
  2. Organic anion transporter 8
  3. Organic anion-transporting polypeptide 8
  4. OATP8
  5. Liver-specific organic anion transporter 2
  6. LST-2
Enzyme 3 Gene Name SLCO1B3
Enzyme 3 Protein Sequence >Solute carrier organic anion transporter family member 1B3 
MDQHQHLNKTAESASSEKKKTRRCNGFKMFLAALSFSYIAKALGGIIMKISITQIERRFD
ISSSLAGLIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCLLMGTGSILTSLPHFFMGY
YRYSKETHINPSENSTSSLSTCLINQTLSFNGTSPEIVEKDCVKESGSHMWIYVFMGNML
RGIGETPIVPLGISYIDDFAKEGHSSLYLGSLNAIGMIGPVIGFALGSLFAKMYVDIGYV
DLSTIRITPKDSRWVGAWWLGFLVSGLFSIISSIPFFFLPKNPNKPQKERKISLSLHVLK
TNDDRNQTANLTNQGKNVTKNVTGFFQSLKSILTNPLYVIFLLLTLLQVSSFIGSFTYVF
KYMEQQYGQSASHANFLLGIITIPTVATGMFLGGFIIKKFKLSLVGIAKFSFLTSMISFL
FQLLYFPLICESKSVAGLTLTYDGNNSVASHVDVPLSYCNSECNCDESQWEPVCGNNGIT
YLSPCLAGCKSSSGIKKHTVFYNCSCVEVTGLQNRNYSAHLGECPRDNTCTRKFFIYVAI
QVINSLFSATGGTTFILLTVKIVQPELKALAMGFQSMVIRTLGGILAPIYFGALIDKTCM
KWSTNSCGAQGACRIYNSVFFGRVYLGLSIALRFPALVLYIVFIFAMKKKFQGKDTKASD
NERKVMDEANLEFLNNGEHFVPSAGTDSKTCNLDMQDNAAAN
Enzyme 3 Number of Residues 702
Enzyme 3 Molecular Weight 77404
Enzyme 3 Theoretical pI 8.95
Enzyme 3 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Mediates the Na(+)-independent transport of organic anions such as 17-beta-glucuronosyl estradiol, taurocholate, triiodothyronine (T3), leukotriene C4, dehydroepiandrosterone sulfate (DHEAS), methotrexate and sulfobromophthalein (BSP)
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 30-50 65-85 97-117 171-191 207-227 259-279 336-356 377-397 410-430 538-558 575-595 626-646
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 9188300 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q9NPD5 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name SO1B3_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >84 bp 
ATGGACCAACATCAACATTTGAATAAAACAGCAGAGTCAGCATCTTCAGAGAAAAAGAAA
ACAAGACGCTGCAATGGATTCAAG
Enzyme 3 GenBank Gene ID AJ400763 Link Image
Enzyme 3 GeneCard ID SLCO1B3 Link Image
Enzyme 3 GenAtlas ID SLCO1B3 Link Image
Enzyme 3 HGNC ID HGNC:10961 Link Image
Enzyme 3 Chromosome Location 12
Enzyme 3 Locus 12p12
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Konig J, Cui Y, Nies AT, Keppler D: Localization and genomic organization of a new hepatocellular organic anion transporting polypeptide. J Biol Chem. 2000 Jul 28;275(30):23161-8. [PubMed Link Image]
  2. Abe T, Unno M, Onogawa T, Tokui T, Kondo TN, Nakagomi R, Adachi H, Fujiwara K, Okabe M, Suzuki T, Nunoki K, Sato E, Kakyo M, Nishio T, Sugita J, Asano N, Tanemoto M, Seki M, Date F, Ono K, Kondo Y, Shiiba K, Suzuki M, Ohtani H, Shimosegawa T, Iinuma K, Nagura H, Ito S, Matsuno S: LST-2, a human liver-specific organic anion transporter, determines methotrexate sensitivity in gastrointestinal cancers. Gastroenterology. 2001 Jun;120(7):1689-99. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5692
Enzyme 4 Name Solute carrier organic anion transporter family member 1B1
Enzyme 4 Synonyms
  1. Solute carrier family 21 member 6
  2. Sodium-independent organic anion- transporting polypeptide 2
  3. OATP 2
  4. Liver-specific organic anion transporter 1
  5. LST-1
  6. OATP-C
Enzyme 4 Gene Name SLCO1B1
Enzyme 4 Protein Sequence >Solute carrier organic anion transporter family member 1B1 
MDQNQHLNKTAEAQPSENKKTRYCNGLKMFLAALSLSFIAKTLGAIIMKSSIIHIERRFE
ISSSLVGFIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCFIMGIGGVLTALPHFFMGY
YRYSKETNINSSENSTSTLSTCLINQILSLNRASPEIVGKGCLKESGSYMWIYVFMGNML
RGIGETPIVPLGLSYIDDFAKEGHSSLYLGILNAIAMIGPIIGFTLGSLFSKMYVDIGYV
DLSTIRITPTDSRWVGAWWLNFLVSGLFSIISSIPFFFLPQTPNKPQKERKASLSLHVLE
TNDEKDQTANLTNQGKNITKNVTGFFQSFKSILTNPLYVMFVLLTLLQVSSYIGAFTYVF
KYVEQQYGQPSSKANILLGVITIPIFASGMFLGGYIIKKFKLNTVGIAKFSCFTAVMSLS
FYLLYFFILCENKSVAGLTMTYDGNNPVTSHRDVPLSYCNSDCNCDESQWEPVCGNNGIT
YISPCLAGCKSSSGNKKPIVFYNCSCLEVTGLQNRNYSAHLGECPRDDACTRKFYFFVAI
QVLNLFFSALGGTSHVMLIVKIVQPELKSLALGFHSMVIRALGGILAPIYFGALIDTTCI
KWSTNNCGTRGSCRTYNSTSFSRVYLGLSSMLRVSSLVLYIILIYAMKKKYQEKDINASE
NGSVMDEANLESLNKNKHFVPSAGADSETHC
Enzyme 4 Number of Residues 691
Enzyme 4 Molecular Weight 76450
Enzyme 4 Theoretical pI 8.68
Enzyme 4 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 4 General Function Carbohydrate transport and metabolism
Enzyme 4 Specific Function Mediates the Na(+)-independent transport of organic anions such as pravastatin, taurocholate, methotrexate, dehydroepiandrosterone sulfate, 17-beta-glucuronosyl estradiol, estrone sulfate, prostaglandin E2, thromboxane B2, leukotriene C3, leukotriene E4, thyroxine and triiodothyronine. May play an important role in the clearance of bile acids and organic anions from the liver
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 97-117 207-227 259-279 336-356 376-396 410-430 575-595
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 5051630 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9Y6L6 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SO1B1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2076 bp 
ATGGACCAAAATCAACATTTGAATAAAACAGCAGAGGCACAACCTTCAGAGAATAAGAAA
ACAAGATACTGCAATGGATTGAAGATGTTCTTGGCAGCTCTGTCACTCAGCTTTATTGCT
AAGACACTAGGTGCAATTATTATGAAAAGTTCCATCATTCATATAGAACGGAGATTTGAG
ATATCCTCTTCTCTTGTTGGTTTTATTGACGGAAGCTTTGAAATTGGAAATTTGCTTGTG
ATTGTATTTGTGAGTTACTTTGGATCCAAACTACATAGACCAAAGTTAATTGGAATCGGT
TGTTTCATTATGGGAATTGGAGGTGTTTTGACTGCTTTGCCACATTTCTTCATGGGATAT
TACAGGTATTCTAAAGAAACTAATATCAATTCATCAGAAAATTCAACATCGACCTTATCC
ACTTGTTTAATTAATCAAATTTTATCACTCAATAAAGCATCACCTGAGATAGTGGGAAAA
GGTTGTTTAAAGGAATCTGGGTCATACATGTGGATATATGTGTTCATGGGTAATATGCTT
CGTGGAATAGGGGAGACTCCCATAGTACCACTGGGGCTTTCTTACATTGATGATTTCGCT
AAAGAAGGACATTCTTCTTTGTATTTAGGTATATTGAATGCAATAGCAATGATTGGTCCA
ATCATTGGCTTTACCCTGGGATCTCTGTTTTCTAAAATGTACGTGGATATTGGATATGTT
AATCTAAGCACTATCAGGATAACTCCTACTGATTCTCGATGGGTTGGAGCTTGGTGGCTT
AATTTCCTTGTGTCTGGACTATTCTCCATTATTTCTTCCATACCATTCTTTTTCTTGCCC
CAAACTCCAAATAAACCACAAAAAGAAAGAAAAGCTTCACTGTCTTTGCATGTGCTGGAA
ACAAATGATGAAAAGGATCAAACAGCTAATTTGACCAATCAAGGAAAAAATATTACCAAA
AATGTGACTGGTTTTTTCCAGTCTTTTAAAAGCATCCTTACTAATCCCCTGTATGTTATG
TTTGTGCTTTTGACGTTGTTACAAGTAAGCAGCTATATTGGTGCTTTTACTTATGTCTTC
AAATACGTAGAGCAACAGTATGGTCAGCCTTCATCTAAGGCTAACATCTTATTGGGAGTC
ATAACCATACCTATTTTTGCAAGTGGAATGTTTTTAGGAGGATATATCATTAAAAAATTC
AAACTGAACACCGTTGGAATTGCCAAATTCTCATGTTTTACTGCTGTGATGTCATTGTCC
TTTTACCTATTATATTTTTTCATACTCTGTGAAAACAAATCAGTTGCCGGACTAACCATG
ACCTATGATGGAAATAATCCAGTGACATCTCATAGAGATGTACCACTTTCTTATTGCAAC
TCAGACTGCAATTGTGATGAAAGTCAATGGGAACCAGTCTGTGGAAACAATGGAATAACT
TACATCTCACCCTGTCTAGCAGGTTGCAAATCTTCAAGTGGCAATAAAAAGCCTATAGTG
TTTTACAACTGCAGTTGTTTGGAAGTAACTGGTCTCCAGAACAGAAATTACTCAGCCCAT
TTGGGTGAATGCCCAAGAGATGATGCTTGTACAAGGAAATTTTACTTTTTTGTTGCAATA
CAAGTCTTGAATTTATTTTTCTCTGCACTTGGAGGCACCTCACATGTCATGCTGATTGTT
AAAATTGTTCAACCTGAATTGAAATCACTTGCACTGGGTTTCCACTCAATGGTTATACGA
GCACTAGGAGGAATTCTAGCTCCTATATATTTTGGGGCTCTGATTGATACAACGTGTATA
AAGTGGTCCACCAACAACTGTGGCACACGTGGGTCATGTAGGACATATAATTCCACATCA
TTTTCAAGGGTCTACTTGGGCTTGTCTTCAATGTTAAGAGTCTCATCACTTGTTTTATAT
ATTATATTAATTTATGCCATGAAGAAAAAATATCAAGAGAAAGATATCAATGCATCAGAA
AATGGAAGTGTCATGGATGAAGCAAACTTAGAATCCTTAAATAAAAATAAACATTTTGTC
CCTTCTGCTGGGGCAGATAGTGAAACACATTGTTAA
Enzyme 4 GenBank Gene ID AF060500 Link Image
Enzyme 4 GeneCard ID SLCO1B1 Link Image
Enzyme 4 GenAtlas ID SLCO1B1 Link Image
Enzyme 4 HGNC ID HGNC:10959 Link Image
Enzyme 4 Chromosome Location 12
Enzyme 4 Locus 12p
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Abe T, Kakyo M, Tokui T, Nakagomi R, Nishio T, Nakai D, Nomura H, Unno M, Suzuki M, Naitoh T, Matsuno S, Yawo H: Identification of a novel gene family encoding human liver-specific organic anion transporter LST-1. J Biol Chem. 1999 Jun 11;274(24):17159-63. [PubMed Link Image]
  2. Hsiang B, Zhu Y, Wang Z, Wu Y, Sasseville V, Yang WP, Kirchgessner TG: A novel human hepatic organic anion transporting polypeptide (OATP2). Identification of a liver-specific human organic anion transporting polypeptide and identification of rat and human hydroxymethylglutaryl-CoA reductase inhibitor transporters. J Biol Chem. 1999 Dec 24;274(52):37161-8. [PubMed Link Image]
  3. Konig J, Cui Y, Nies AT, Keppler D: A novel human organic anion transporting polypeptide localized to the basolateral hepatocyte membrane. Am J Physiol Gastrointest Liver Physiol. 2000 Jan;278(1):G156-64. [PubMed Link Image]
  4. Konig J, Cui Y, Nies AT, Keppler D: Localization and genomic organization of a new hepatocellular organic anion transporting polypeptide. J Biol Chem. 2000 Jul 28;275(30):23161-8. [PubMed Link Image]
  5. Tirona RG, Leake BF, Merino G, Kim RB: Polymorphisms in OATP-C: identification of multiple allelic variants associated with altered transport activity among European- and African-Americans. J Biol Chem. 2001 Sep 21;276(38):35669-75. Epub 2001 Jul 26. [PubMed Link Image]
  6. Michalski C, Cui Y, Nies AT, Nuessler AK, Neuhaus P, Zanger UM, Klein K, Eichelbaum M, Keppler D, Konig J: A naturally occurring mutation in the SLC21A6 gene causing impaired membrane localization of the hepatocyte uptake transporter. J Biol Chem. 2002 Nov 8;277(45):43058-63. Epub 2002 Aug 23. [PubMed Link Image]
  7. Nozawa T, Nakajima M, Tamai I, Noda K, Nezu J, Sai Y, Tsuji A, Yokoi T: Genetic polymorphisms of human organic anion transporters OATP-C (SLC21A6) and OATP-B (SLC21A9): allele frequencies in the Japanese population and functional analysis. J Pharmacol Exp Ther. 2002 Aug;302(2):804-13. [PubMed Link Image]
Enzyme 4 Metabolite References
  1. Michalski C, Cui Y, Nies AT, Nuessler AK, Neuhaus P, Zanger UM, Klein K, Eichelbaum M, Keppler D, Konig J: A naturally occurring mutation in the SLC21A6 gene causing impaired membrane localization of the hepatocyte uptake transporter. J Biol Chem. 2002 Nov 8;277(45):43058-63. Epub 2002 Aug 23. [PubMed Link Image]
Enzyme 5 [top]
Enzyme 5 ID 7519
Enzyme 5 Name Canalicular multispecific organic anion transporter 2
Enzyme 5 Synonyms
  1. ATP-binding cassette sub-family C member 3
  2. Multidrug resistance-associated protein 3
  3. Multi-specific organic anion transporter-D
  4. MOAT-D
Enzyme 5 Gene Name ABCC3
Enzyme 5 Protein Sequence >Canalicular multispecific organic anion transporter 2 
MDALCGSGELGSKFWDSNLSVHTENPDLTPCFQNSLLAWVPCIYLWVALPCYLLYLRHHC
RGYIILSHLSKLKMVLGVLLWCVSWADLFYSFHGLVHGRAPAPVFFVTPLVVGVTMLLAT
LLIQYERLQGVQSSGVLIIFWFLCVVCAIVPFRSKILLAKAEGEISDPFRFTTFYIHFAL
VLSALILACFREKPPFFSAKNVDPNPYPETSAGFLSRLFFWWFTKMAIYGYRHPLEEKDL
WSLKEEDRSQMVVQQLLEAWRKQEKQTARHKASAAPGKNASGEDEVLLGARPRPRKPSFL
KALLATFGSSFLISACFKLIQDLLSFINPQLLSILIRFISNPMAPSWWGFLVAGLMFLCS
MMQSLILQHYYHYIFVTGVKFRTGIMGVIYRKALVITNSVKRASTVGEIVNLMSVDAQRF
MDLAPFLNLLWSAPLQIILAIYFLWQNLGPSVLAGVAFMVLLIPLNGAVAVKMRAFQVKQ
MKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTAAYLHTTTTFTWM
CSPFLVTLITLWVYVYVDPNNVLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLK
RIQQFLSQEELDPQSVERKTISPGYAITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVV
GPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQNCTLQENVLFGKALNPKRY
QQTLEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSA
VDSHVAKHIFDHVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQ
RNGSFANFLCNYAPDEDQGHLEDSWTALEGAEDKEALLIEDTLSNHTDLTDNDPVTYVVQ
KQFMRQLSALSSDGEGQGRPVPRRHLGPSEKVQVTEAKADGALTQEEKAAIGTVELSVFW
DYAKAVGLCTTLAICLLYVGQSAAAIGANVWLSAWTNDAMADSRQNNTSLRLGVYAALGI
LQGFLVMLAAMAMAAGGIQAARVLHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVD
EVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLAVLYTLVQRFYAATSRQLKRLE
SVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDANQRSCYPYIISNRWLSIGVE
FVGNCVVLFAALFAVIGRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERV
KEYSKTETEAPWVVEGSRPPEGWPPRGEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVG
IVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPILFSGTL
RMNLDPFGSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARAL
LRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGV
VAEFDSPANLIAARGIFYGMARDAGLA
Enzyme 5 Number of Residues 1527
Enzyme 5 Molecular Weight 169345
Enzyme 5 Theoretical pI 7.20
Enzyme 5 GO Classification
Function
  • ATP binding
  • ATPase activity
  • ATPase activity, coupled to transmembrane movement of substances
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 5 General Function Defense mechanisms
Enzyme 5 Specific Function May act as an inducible transporter in the biliary and intestinal excretion of organic anions
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 33-53 74-94 100-120 133-153 172-192 303-323 350-370 427-447 451-471 534-554 577-597 964-984 1022-1042 1086-1106 1108-1128 1200-1220 1223-1243
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 3132270 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID O15438 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name MRP3_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >4584 bp 
ATGGACGCCCTGTGCGGTTCCGGGGAGCTCGGCTCCAAGTTCTGGGACTCCAACCTGTCT
GTGCACACAGAAAACCCGGACCTCACTCCCTGCTTCCAGAACTCCCTGCTGGCCTGGGTG
CCCTGCATCTACCTGTGGGTCGCCCTGCCCTGCTACTTGCTCTACCTGCGGCACCATTGT
CGTGGCTACATCATCCTCTCCCACCTGTCCAAGCTCAAGATGGTCCTGGGTGTCCTGCTG
TGGTGCGTCTCCTGGGCAGACCTTTTTTACTCCTTCCATGGCCTGGTCCATGGCCGGGCC
CCTGCCCCTGTTTTCTTTGTCACCCCCTTGGTGGTGGGGGTCACCATGCTGCTGGCCACC
CTGCTGATACAGTATGAGCGGCTGCAGGGCGTACAGTCTTCGGGGGTCCTCATTATCTTC
TGGTTCCTGTGTGTGGTCTGCGCCATCGTCCCATTCCGCTCCAAGATCCTTTTAGCCAAG
GCAGAGGGTGAGATCTCAGACCCCTTCCGCTTCACCACCTTCTACATCCACTTTGCCCTG
GTACTCTCTGCCCTCATCTTGGCCTGCTTCAGGGAGAAACCTCCATTTTTCTCCGCAAAG
AATGTCGACCCTAACCCCTACCCTGAGACCAGCGCTGGCTTTCTCTCCCGCCTGTTTTTC
TGGTGGTTCACAAAGATGGCCATCTATGGCTACCGGCATCCCCTGGAGGAGAAGGACCTC
TGGTCCCTAAAGGAAGAGGACAGATCCCAGATGGTGGTGCAGCAGCTGCTGGAGGCATGG
AGGAAGCAGGAAAAGCAGACGGCACGACACAAGGCTTCAGCAGCACCTGGGAAAAATGCC
TCCGGCGAGGACGAGGTGCTGCTGGGTGCCCGGCCCAGGCCCCGGAAGCCCTCCTTCCTG
AAGGCCCTGCTGGCCACCTTCGGCTCCAGCTTCCTCATCAGTGCCTGCTTCAAGCTTATC
CAGGACCTGCTCTCCTTCATCAATCCACAGCTGCTCAGCATCCTGATCAGGTTTATCTCC
AACCCCATGGCCCCCTCCTGGTGGGGCTTCCTGGTGGCTGGGCTGATGTTCCTGTGCTCC
ATGATGCAGTCGCTGATCTTACAACACTATTACCACTACATCTTTGTGACTGGGGTGAAG
TTTCGTACTGGGATCATGGGTGTCATCTACAGGAAGGCTCTGGTTATCACCAACTCAGTC
AAACGTGCGTCCACTGTGGGGGAAATTGTCAACCTCATGTCAGTGGATGCCCAGCGCTTC
ATGGACCTTGCCCCCTTCCTCAATCTGCTGTGGTCAGCACCCCTGCAGATCATCCTGGCG
ATCTACTTCCTCTGGCAGAACCTAGGTCCCTCTGTCCTGGCTGGAGTCGCTTTCATGGTC
TTGCTGATTCCACTCAACGGAGCTGTGGCCGTGAAGATGCGCGCCTTCCAGGTAAAGCAA
ATGAAATTGAAGGACTCGCGCATCAAGCTGATGAGTGAGATCCTGAACGGCATCAAGGTG
CTGAAGCTGTACGCCTGGGAGCCCAGCTTCCTGAAGCAGGTGGAGGGCATCAGGCAGGGT
GAGCTCCAGCTGCTGCGCACGGCGGCCTACCTCCACACCACAACCACCTTCACCTGGATG
TGCAGCCCCTTCCTGGTGACCCTGATCACCCTCTGGGTGTACGTGTACGTGGACCCAAAC
AATGTGCTGGACGCCGAGAAGGCCTATGTGTCTGTGTCCTTGTTTAATATCTTAAGACTT
CCCCTCAACATGCTGCCCCAGTTAATCAGCAACCTGACTCAGGCCAGTGTGTCTCTGAAA
CGGATCCAGCAATTCCTGAGCCAAGAGGAACTTGACCCCCAGAGTGTGGAAAGAAAGACC
ATCTCCCCAGGCTATGCCATCACCATACACAGTGGCACCTTCACCTGGGCCCAGGACCTG
CCCCCCACTCTGCACAGCCTAGACATCCAGGTCCCGAAAGGGGCACTGGTGGCCGTGGTG
GGGCCTGTGGGCTGTGGGAAGTCCTCCCTGGTGTCTGCCCTGCTGGGAGAGATGGAGAAG
CTAGAAGGCAAAGTGCACATGAAGGGCTCCGTGGCCTATGTGCCCCAGCAGGCATGGATC
CAGAACTGCACTCTTCAGGAAAACGTGCTTTTCGGCAAAGCCCTGAACCCCAAGCGCTAC
CAGCAGACTCTGGAGGCCTGTGCCTTGCTAGCTGACCTGGAGATGCTGCCTGGTGGGGAT
CAGACAGAGATTGGAGAGAAGGGCATTAACCTGTCTGGGGGCCAGCGGCAGCGGGTCAGT
CTGGCTCGAGCTGTTTACAGTGATGCCGATATTTTCTTGCTGGATGACCCACTGTCCGCG
GTGGACTCTCATGTGGCCAAGCACATCTTTGACCACGTCATCGGGCCAGAAGGCGTGCTG
GCAGGCAAGACGCGAGTGCTGGTGACGCACGGCATTAGCTTCCTGCCCCAGACAGACTTC
ATCATTGTGCTAGCTGATGGACAGGTGTCTGAGATGGGCCCGTACCCAGCCCTGCTGCAG
CGCAACGGCTCCTTTGCCAACTTTCTCTGCAACTATGCCCCCGATGAGGACCAAGGGCAC
CTGGAGGACAGCTGGACCGCGTTGGAAGGTGCAGAGGATAAGGAGGCACTGCTGATTGAA
GACACACTCAGCAACCACACGGATCTGACAGACAATGATCCAGTCACCTATGTGGTCCAG
AAGCAGTTTATGAGACAGCTGAGTGCCCTGTCCTCAGATGGGGAGGGACAGGGTCGGCCT
GTACCCCGGAGGCACCTGGGTCCATCAGAGAAGGTGCAGGTGACAGAGGCGAAGGCAGAT
GGGGCACTGACCCAGGAGGAGAAAGCAGCCATTGGCACTGTGGAGCTCAGTGTGTTCTGG
GATTATGCCAAGGCCGTGGGGCTCTGTACCACGCTGGCCATCTGTCTCCTGTATGTGGGT
CAAAGTGCGGCTGCCATTGGAGCCAATGTGTGGCTCAGTGCCTGGACAAATGATGCCATG
GCAGACAGTAGACAGAACAACACTTCCCTGAGGCTGGGCGTCTATGCTGCTTTAGGAATT
CTGCAAGGGTTCTTGGTGATGCTGGCAGCCATGGCCATGGCAGCGGGTGGCATCCAGGCT
GCCCGTGTGTTGCACCAGGCACTGCTGCACAACAAGATACGCTCGCCACAGTCCTTCTTT
GACACCACACCATCAGGCCGCATCCTGAACTGCTTCTCCAAGGACATCTATGTCGTTGAT
GAGGTTCTGGCCCCTGTCATCCTCATGCTGCTCAATTCCTTCTTCAACGCCATCTCCACT
CTTGTGGTCATCATGGCCAGCACGCCGCTCTTCACTGTGGTCATCCTGCCCCTGGCTGTG
CTCTACACCTTAGTGCAGCGCTTCTATGCAGCCACATCACGGCAACTGAAGCGGCTGGAA
TCAGTCAGCCGCTCACCTATCTACTCCCACTTTTCGGAGACAGTGACTGGTGCCAGTGTC
ATCCGGGCCTACAACCGCAGCCGGGATTTTGAGATCATCAGTGATACTAAGGTGGATGCC
AACCAGAGAAGCTGCTACCCCTACATCATCTCCAACCGGTGGCTGAGCATCGGAGTGGAG
TTCGTGGGGAACTGCGTGGTGCTCTTTGCTGCACTATTTGCCGTCATCGGGAGGAGCAGC
CTGAACCCGGGGCTGGTGGGCCTTTCTGTGTCCTACTCCTTGCAGGTGACATTTGCTCTG
AACTGGATGATACGAATGATGTCAGATTTGGAATCTAACATCGTGGCTGTGGAGAGGGTC
AAGGAGTACTCCAAGACAGAGACAGAGGCGCCCTGGGTGGTGGAAGGCAGCCGCCCTCCC
GAAGGTTGGCCCCCACGTGGGGAGGTGGAGTTCCGGAATTATTCTGTGCGCTACCGGCCG
GGCCTAGACCTGGTGCTGAGAGACCTGAGTCTGCATGTGCATGGTGGCGAGAAGGTGGGG
ATCGTGGGCCGCACTGGGGCTGGCAAGTCTTCCATGACCCTTTGCCTGTTCCGCATCCTG
GAGGCGGCAAAGGGTGAAATCCGCATTGATGGCCTCAATGTGGCAGACATCGGCCTCCAT
GACCTGCGCTCTCAGCTGACCATCATCCCGCAGGACCCCATCCTGTTCTCGGGGACCCTG
CGCATGAACCTGGACCCCTTCGGCAGCTACTCAGAGGAGGACATTTGGTGGGCTTTGGAG
CTGTCCCACCTGCACACGTTTGTGAGCTCCCAGCCGGCAGGCCTGGACTTCCAGTGCTCA
GAGGGCGGGGAGAATCTCAGCGTGGGCCAGAGGCAGCTCGTGTGCCTGGCCCGAGCCCTG
CTCCGCAAGAGCCGCATCCTGGTTTTAGACGAGGCCACAGCTGCCATCGACCTGGAGACT
GACAACCTCATCCAGGCTACCATCCGCACCCAGTTTGATACCTGCACTGTCCTGACCATC
GCACACCGGCTTAACACTATCATGGACTACACCAGGGTCCTGGTCCTGGACAAAGGAGTA
GTAGCTGAGTTTGATTCTCCAGCCAACCTCATTGCAGCTAGAGGCATCTTCTACGGGATG
GCCAGAGATGCTGGACTTGCCTAA
Enzyme 5 GenBank Gene ID AB010887 Link Image
Enzyme 5 GeneCard ID ABCC3 Link Image
Enzyme 5 GenAtlas ID ABCC3 Link Image
Enzyme 5 HGNC ID HGNC:54 Link Image
Enzyme 5 Chromosome Location 17
Enzyme 5 Locus 17q22
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Kiuchi Y, Suzuki H, Hirohashi T, Tyson CA, Sugiyama Y: cDNA cloning and inducible expression of human multidrug resistance associated protein 3 (MRP3). FEBS Lett. 1998 Aug 14;433(1-2):149-52. [PubMed Link Image]
  2. Konig J, Rost D, Cui Y, Keppler D: Characterization of the human multidrug resistance protein isoform MRP3 localized to the basolateral hepatocyte membrane. Hepatology. 1999 Apr;29(4):1156-63. [PubMed Link Image]
  3. Uchiumi T, Hinoshita E, Haga S, Nakamura T, Tanaka T, Toh S, Furukawa M, Kawabe T, Wada M, Kagotani K, Okumura K, Kohno K, Akiyama S, Kuwano M: Isolation of a novel human canalicular multispecific organic anion transporter, cMOAT2/MRP3, and its expression in cisplatin-resistant cancer cells with decreased ATP-dependent drug transport. Biochem Biophys Res Commun. 1998 Nov 9;252(1):103-10. [PubMed Link Image]
  4. Fromm MF, Leake B, Roden DM, Wilkinson GR, Kim RB: Human MRP3 transporter: identification of the 5'-flanking region, genomic organization and alternative splice variants. Biochim Biophys Acta. 1999 Jan 8;1415(2):369-74. [PubMed Link Image]
  5. Belinsky MG, Bain LJ, Balsara BB, Testa JR, Kruh GD: Characterization of MOAT-C and MOAT-D, new members of the MRP/cMOAT subfamily of transporter proteins. J Natl Cancer Inst. 1998 Nov 18;90(22):1735-41. [PubMed Link Image]
  6. Kool M, de Haas M, Scheffer GL, Scheper RJ, van Eijk MJ, Juijn JA, Baas F, Borst P: Analysis of expression of cMOAT (MRP2), MRP3, MRP4, and MRP5, homologues of the multidrug resistance-associated protein gene (MRP1), in human cancer cell lines. Cancer Res. 1997 Aug 15;57(16):3537-47. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 7531
Enzyme 6 Name Bile salt export pump
Enzyme 6 Synonyms
  1. ATP-binding cassette sub-family B member 11
Enzyme 6 Gene Name ABCB11
Enzyme 6 Protein Sequence >Bile salt export pump 
MSDSVILRSIKKFGEENDGFESDKSYNNDKKSRLQDEKKGDGVRVGFFQLFRFSSSTDIW
LMFVGSLCAFLHGIAQPGVLLIFGTMTDVFIDYDVELQELQIPGKACVNNTIVWTNSSLN
QNMTNGTRCGLLNIESEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFR
RIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWK
LTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKRE
VERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYAVAFWYGSTLVLDEGEYTPGTLV
QIFLSVIVGALNLGNASPCLEAFATGRAAATSIFETIDRKPIIDCMSEDGYKLDRIKGEI
EFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVT
VDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNF
IMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEV
LSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQSQG
NQALNEEDIKDATEDDMLARTFSRGSYQDSLRASIRQRSKSQLSYLVHEPPLAVVDHKST
YEEDRKDKDIPVQEEVEPAPVRRILKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQIL
GTFSIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAML
GQDIAWFDDLRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKL
SLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFI
EALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHFSYVFRV
ISAVVLSATALGRAFSYTPSYAKAKISAARFFQLLDRQPPISVYNTAGEKWDNFQGKIDF
VDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMID
GHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDF
VMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVA
LDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLVTTGSPI
S
Enzyme 6 Number of Residues 1321
Enzyme 6 Molecular Weight 146395
Enzyme 6 Theoretical pI 6.52
Enzyme 6 GO Classification
Function
  • ATP binding
  • ATPase activity
  • ATPase activity, coupled to transmembrane movement of substances
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 6 General Function Defense mechanisms
Enzyme 6 Specific Function Involved in the ATP-dependent secretion of bile salts into the canaliculus of hepatocytes
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 63-83 148-168 216-236 241-261 320-340 354-374 756-776 795-815 870-890 891-911 980-1000 1012-1032
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 3873243 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID O95342 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name ABCBB_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >3966 bp 
ATGTCTGACTCAGTAATTCTTCGAAGTATAAAGAAATTTGGAGAGGAGAATGATGGTTTT
GAGTCAGATAAATCATATAATAATGATAAGAAATCAAGGTTACAAGATGAGAAGAAAGGT
GATGGCGTTAGAGTTGGCTTCTTTCAATTGTTTCGGTTTTCTTCATCAACTGACATTTGG
CTGATGTTTGTGGGAAGTTTGTGTGCATTTCTCCATGGAATAGCCCAGCCAGGCGTGCTA
CTCATTTTTGGCACAATGACAGATGTTTTTATTGACTACGACGTTGAGTTACAAGAACTC
CAGATTCCAGGAAAAGCATGTGTGAATAACACCATTGTATGGACTAACAGTTCCCTCAAC
CAGAACATGACAAATGGAACACGTTGTGGGTTGCTGAACATCGAGAGCGAAATGATCAAA
TTTGCCAGTTACTATGCTGGAATTGCTGTCGCAGTACTTATCACAGGATATATTCAAATA
TGCTTTTGGGTCATTGCCGCAGCTCGTCAGATACAGAAAATGAGAAAATTTTACTTTAGG
AGAATAATGAGAATGGAAATAGGGTGGTTTGACTGCAATTCAGTGGGGGAGCTGAATACA
AGATTCTCTGATGATATTAATAAAATCAATGATGCCATAGCTGACCAAATGGCCCTTTTC
ATTCAGCGCATGACCTCGACCATCTGTGGTTTCCTGTTGGGATTTTTCAGGGGTTGGAAA
CTGACCTTGGTTATTATTTCTGTCAGCCCTCTCATTGGGATTGGAGCAGCCACCATTGGT
CTGAGTGTGTCCAAGTTTACGGACTATGAGCTGAAGGCCTATGCCAAAGCAGGGGTGGTG
GCTGATGAAGTCATTTCATCAATGAGAACAGTGGCTGCTTTTGGTGGTGAGAAAAGAGAG
GTTGAAAGGTATGAGAAAAATCTTGTGTTCGCCCAGCGTTGGGGAATTAGAAAAGGAATA
GTGATGGGATTCTTTACTGGATTCGTGTGGTGTCTCATCTTTTTGTGTTATGCAGTGGCC
TTCTGGTACGGCTCCACACTTGTCCTGGATGAAGGAGAATATACACCAGGAACCCTTGTC
CAGATTTTCCTCAGTGTCATAGTAGGAGCTTTAAATCTTGGCAATGCCTCTCCTTGTTTG
GAAGCCTTTGCAACTGGACGTGCAGCAGCCACCAGCATTTTTGAGACAATAGACAGGAAA
CCCATCATTGACTGCATGTCAGAAGATGGTTACAAGTTGGATCGAATCAAGGGTGAAATT
GAATTCCATAATGTGACCTTCCATTATCCTTCCAGACCAGAGGTGAAGATTCTAAATGAC
CTCAACATGGTCATTAAACCAGGGGAAATGACAGCTCTGGTAGGACCCAGTGGAGCTGGA
AAAAGTACAGCACTGCAACTCATTCAGCGATTCTATGACCCCTGTGAAGGAATGGTGACC
GTGGATGGCCATGACATTCGCTCTCTTAACATTCAGTGGCTTAGAGATCAGATTGGGATA
GTGGAGCAAGAGCCAGTTCTGTTCTCTACCACCATTGCAGAAAATATTCGCTATGGCAGA
GAAGATGCAACAATGGAAGACATAGTCCAAGCTGCCAAGGAGGCCAATGCCTACAACTTC
ATCATGGACCTGCCACAGCAATTTGACACCCTTGTTGGAGAAGGAGGAGGCCAGATGAGT
GGTGGCCAGAAACAAAGGGTAGCTATCGCCAGAGCCCTCATCCGAAATCCCAAGATTCTG
CTTTTGGACATGGCCACCTCAGCTCTGGACAATGAGAGTGAAGCCATGGTGCAAGAAGTG
CTGAGTAAGATTCAGCATGGGCACACAATCATTTCAGTTGCTCATCGCTTGTCTACGGTC
AGAGCTGCAGATACCATCATTGGTTTTGAACATGGCACTGCAGTGGAAAGAGGGACCCAT
GAAGAATTACTGGAAAGGAAAGGTGTTTACTTCACTCTAGTGACTTTGCAAAGCCAGGGA
AATCAAGCTCTTAATGAAGAGGACATAAAGGATGCAACTGAAGATGACATGCTTGCGAGG
ACCTTTAGCAGAGGGAGCTACCAGGATAGTTTAAGGGCTTCCATCCGGCAACGCTCCAAG
TCTCAGCTTTCTTACCTGGTGCACGAACCTCCATTAGCTGTTGTAGATCATAAGTCTACC
TATGAAGAAGATAGAAAGGACAAGGACATTCCTGTGCAGGAAGAAGTTGAACCTGCCCCA
GTTAGGAGGATTCTGAAATTCAGTGCTCCAGAATGGCCCTACATGCTGGTAGGGTCTGTG
GGTGCAGCTGTGAACGGGACAGTCACACCCTTGTATGCCTTTTTATTCAGCCAGATTCTT
GGGACTTTTTCAATTCCTGATAAAGAGGAACAAAGGTCACAGATCAATGGTGTGTGCCTA
CTTTTTGTAGCAATGGGCTGTGTATCTCTTTTCACCCAATTTCTACAGGGATATGCCTTT
GCTAAATCTGGGGAGCTCCTAACAAAAAGGCTACGTAAATTTGGTTTCAGGGCAATGCTG
GGGCAAGATATTGCCTGGTTTGATGACCTCAGAAATAGCCCTGGAGCATTGACAACAAGA
CTTGCTACAGATGCTTCCCAAGTTCAAGGGGCTGCCGGCTCTCAGATCGGGATGATAGTC
AATTCCTTCACTAACGTCACTGTGGCCATGATCATTGCCTTCTCCTTTAGCTGGAAGCTG
AGCCTGGTCATCTTGTGCTTCTTCCCCTTCTTGGCTTTATCAGGAGCCACACAGACCAGG
ATGTTGACAGGATTTGCCTCTCGAGATAAGCAGGCCCTGGAGATGGTGGGACAGATTACA
AATGAAGCCCTCAGTAACATCCGCACTGTTGCTGGAATTGGAAAGGAGAGGCGGTTCATT
GAAGCACTTGAGACTGAGCTGGAGAAGCCCTTCAAGACAGCCATTCAGAAAGCCAATATT
TACGGATTCTGCTTTGCCTTTGCCCAGTGCATCATGTTTATTGCGAATTCTGCTTCCTAC
AGATATGGAGGTTACTTAATCTCCAATGAGGGGCTCCATTTCAGCTATGTGTTCAGGGTG
ATCTCTGCAGTTGTACTGAGTGCAACAGCTCTTGGAAGAGCCTTCTCTTACACCCCAAGT
TATGCAAAAGCTAAAATATCAGCTGCACGCTTTTTTCAACTGCTGGACCGACAACCCCCA
ATCAGTGTATACAATACTGCAGGTGAAAAATGGGACAACTTCCAGGGGAAGATTGATTTT
GTTGATTGTAAATTTACATATCCTTCTCGACCTGACTCGCAAGTTCTGAATGGTCTCTCA
GTGTCGATTAGTCCAGGGCAGACACTGGCGTTTGTTGGGAGCAGTGGATGTGGCAAAAGC
ACTAGCATTCAGCTGTTGGAACGTTTCTATGATCCTGATCAAGGGAAGGTGATGATAGAT
GGTCATGACAGCAAAAAAGTAAATGTCCAGTTCCTCCGCTCAAACATTGGAATTGTTTCC
CAGGAACCAGTGTTGTTTGCCTGTAGCATAATGGACAATATCAAGTATGGAGACAACACC
AAAGAAATTCCCATGGAAAGAGTCATAGCAGCTGCAAAACAGGCTCAGCTGCATGATTTT
GTCATGTCACTCCCAGAGAAATATGAAACTAACGTTGGGTCCCAGGGGTCTCAACTCTCT
AGAGGGGAGAAACAACGCATTGCTATTGCTCGGGCCATTGTACGAGATCCTAAAATCTTG
CTACTAGATGAAGCCACTTCTGCCTTAGACACAGAAAGTGAAAAGACGGTGCAGGTTGCT
CTAGACAAAGCCAGAGAGGGTCGGACCTGCATTGTCATTGCCCATCGCTTGTCCACCATC
CAGAACGCGGATATCATTGCTGTCATGGCACAGGGGGTGGTGATTGAAAAGGGGACCCAT
GAAGAACTGATGGCCCAAAAAGGAGCCTACTACAAACTAGTCACCACTGGATCCCCCATC
AGTTGA
Enzyme 6 GenBank Gene ID AF091582 Link Image
Enzyme 6 GeneCard ID ABCB11 Link Image
Enzyme 6 GenAtlas ID ABCB11 Link Image
Enzyme 6 HGNC ID HGNC:42 Link Image
Enzyme 6 Chromosome Location 2
Enzyme 6 Locus 2q24
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Strautnieks SS, Bull LN, Knisely AS, Kocoshis SA, Dahl N, Arnell H, Sokal E, Dahan K, Childs S, Ling V, Tanner MS, Kagalwalla AF, Nemeth A, Pawlowska J, Baker A, Mieli-Vergani G, Freimer NB, Gardiner RM, Thompson RJ: A gene encoding a liver-specific ABC transporter is mutated in progressive familial intrahepatic cholestasis. Nat Genet. 1998 Nov;20(3):233-8. [PubMed Link Image]
  2. Saito S, Iida A, Sekine A, Miura Y, Ogawa C, Kawauchi S, Higuchi S, Nakamura Y: Three hundred twenty-six genetic variations in genes encoding nine members of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the Japanese population. J Hum Genet. 2002;47(1):38-50. [PubMed Link Image]
  3. Chen HL, Chang PS, Hsu HC, Ni YH, Hsu HY, Lee JH, Jeng YM, Shau WY, Chang MH: FIC1 and BSEP defects in Taiwanese patients with chronic intrahepatic cholestasis with low gamma-glutamyltranspeptidase levels. J Pediatr. 2002 Jan;140(1):119-24. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 7956
Enzyme 7 Name Ileal sodium/bile acid cotransporter
Enzyme 7 Synonyms
  1. Ileal Na(+/bile acid cotransporter
  2. Na(+-dependent ileal bile acid transporter
  3. Ileal sodium-dependent bile acid transporter
  4. ISBT
  5. IBAT
  6. Apical sodium- dependent bile acid transporter
  7. ASBT
  8. Sodium/taurocholate cotransporting polypeptide, ileal
  9. Solute carrier family 10 member 2
Enzyme 7 Gene Name SLC10A2
Enzyme 7 Protein Sequence >Ileal sodium/bile acid cotransporter 
MNDPNSCVDNATVCSGASCVVPESNFNNILSVVLSTVLTILLALVMFSMGCNVEIKKFLG
HIKRPWGICVGFLCQFGIMPLTGFILSVAFDILPLQAVVVLIIGCCPGGTASNILAYWVD
GDMDLSVSMTTCSTLLALGMMPLCLLIYTKMWVDSGSIVIPYDNIGTSLVALVVPVSIGM
FVNHKWPQKAKIILKIGSIAGAILIVLIAVVGGILYQSAWIIAPKLWIIGTIFPVAGYSL
GFLLARIAGLPWYRCRTVAFETGMQNTQLCSTIVQLSFTPEELNVVFTFPLIYSIFQLAF
AAIFLGFYVAYKKCHGKNKAEIPESKENGTEPESSFYKANGGFQPDEK
Enzyme 7 Number of Residues 348
Enzyme 7 Molecular Weight 37698
Enzyme 7 Theoretical pI 7.13
Enzyme 7 GO Classification
Function
  • bile acid:sodium symporter activity
  • organic acid transporter activity
  • organic acid:sodium symporter activity
  • transporter activity
Process
  • anion transport
  • cation transport
  • cellular physiological process
  • ion transport
  • monovalent inorganic cation transport
  • organic anion transport
  • physiological process
  • sodium ion transport
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Plays a critical role in the sodium-dependent reabsorption of bile acids from the lumen of the small intestine. Plays a key role in cholesterol metabolism
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 29-49 83-103 127-147 158-178 196-216 225-245 285-305
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 595399 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q12908 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name NTCP2_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1047 bp 
ATGAATGATCCGAACAGCTGTGTGGACAATGCAACAGTTTGCTCTGGTGCATCCTGTGTG
GTACCTGAGAGCAATTTCAATAACATCCTAAGTGTGGTCCTAAGTACGGTGCTGACCATC
CTGTTGGCCTTGGTGATGTTCTCCATGGGATGCAACGTGGAAATCAAGAAATTTCTAGGG
CACATAAAGCGGCCGTGGGGCATTTGTGTTGGCTTCCTCTGTCAGTTTGGAATCATGCCC
CTCACAGGATTCATCCTGTCGGTGGCCTTTGACATCCTCCCGCTCCAGGCCGTAGTGGTG
CTCATTATAGGATGCTGCCCTGGAGGAACTGCCTCCAATATCTTGGCCTATTGGGTCGAT
GGCGACATGGACCTGAGCGTCAGCATGACCACATGCTCCACACTGCTTGCCCTCGGAATG
ATGCCGCTGTGCCTCCTTATCTATACCAAAATGTGGGTCGACTCTGGGAGCATCGTAATT
CCCTATGATAACATAGGTACATCTCTGGTTGCTCTCGTTGTTCCTGTTTCCATTGGAATG
TTTGTTAATCACAAATGGCCCCAAAAAGCAAAGATCATACTTAAAATTGGGTCCATCGCG
GGCGCCATCCTCATTGTGCTCATAGCTGTGGTTGGAGGAATATTGTACCAAAGCGCCTGG
ATCATTGCTCCCAAACTGTGGATTATAGGAACAATATTTCCTGTGGCGGGTTACTCCCTG
GGGTTTCTTCTGGCTAGAATTGCTGGTCTACCCTGGTACAGGTGCCGAACGGTTGCTTTT
GAAACGGGGATGCAGAACACGCAGCTATGTTCCACCATCGTTCAGCTCTCCTTCACTCCT
GAGGAGCTCAATGTCGTATTCACCTTCCCGCTCATCTACAGCATTTTCCAGCTCGCCTTT
GCCGCAATATTCTTAGGATTTTATGTGGCATACAAGAAATGTCATGGAAAAAACAAGGCA
GAAATTCCAGAGAGCAAAGAAAATGGAACGGAGCCAGAGTCATCGTTTTATAAGGCAAAT
GGAGGATTTCAACCTGACGAAAAGTAG
Enzyme 7 GenBank Gene ID U10417 Link Image
Enzyme 7 GeneCard ID SLC10A2 Link Image
Enzyme 7 GenAtlas ID SLC10A2 Link Image
Enzyme 7 HGNC ID HGNC:10906 Link Image
Enzyme 7 Chromosome Location 13
Enzyme 7 Locus 13q33
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Wong MH, Oelkers P, Dawson PA: Identification of a mutation in the ileal sodium-dependent bile acid transporter gene that abolishes transport activity. J Biol Chem. 1995 Nov 10;270(45):27228-34. [PubMed Link Image]
  2. Oelkers P, Kirby LC, Heubi JE, Dawson PA: Primary bile acid malabsorption caused by mutations in the ileal sodium-dependent bile acid transporter gene (SLC10A2). J Clin Invest. 1997 Apr 15;99(8):1880-7. [PubMed Link Image]
  3. Chumakov I, Blumenfeld M, Guerassimenko O, Cavarec L, Palicio M, Abderrahim H, Bougueleret L, Barry C, Tanaka H, La Rosa P, Puech A, Tahri N, Cohen-Akenine A, Delabrosse S, Lissarrague S, Picard FP, Maurice K, Essioux L, Millasseau P, Grel P, Debailleul V, Simon AM, Caterina D, Dufaure I, Malekzadeh K, Belova M, Luan JJ, Bouillot M, Sambucy JL, Primas G, Saumier M, Boubkiri N, Martin-Saumier S, Nasroune M, Peixoto H, Delaye A, Pinchot V, Bastucci M, Guillou S, Chevillon M, Sainz-Fuertes R, Meguenni S, Aurich-Costa J, Cherif D, Gimalac A, Van Duijn C, Gauvreau D, Ouellette G, Fortier I, Raelson J, Sherbatich T, Riazanskaia N, Rogaev E, Raeymaekers P, Aerssens J, Konings F, Luyten W, Macciardi F, Sham PC, Straub RE, Weinberger DR, Cohen N, Cohen D: Genetic and physiological data implicating the new human gene G72 and the gene for D-amino acid oxidase in schizophrenia. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13675-80. Epub 2002 Oct 3. [PubMed Link Image]
  4. Montagnani M, Love MW, Rossel P, Dawson PA, Qvist P: Absence of dysfunctional ileal sodium-bile acid cotransporter gene mutations in patients with adult-onset idiopathic bile acid malabsorption. Scand J Gastroenterol. 2001 Oct;36(10):1077-80. [PubMed Link Image]
Enzyme 7 Metabolite References
  1. Kramer W, Girbig F, Glombik H, Corsiero D, Stengelin S, Weyland C: Identification of a ligand-binding site in the Na+/bile acid cotransporting protein from rabbit ileum. J Biol Chem. 2001 Sep 21;276(38):36020-7. Epub 2001 Jul 10. [PubMed Link Image]
Enzyme 8 [top]
Enzyme 8 ID 8049
Enzyme 8 Name Sodium/bile acid cotransporter
Enzyme 8 Synonyms
  1. Na(+/bile acid cotransporter
  2. Na(+/taurocholate transport protein
  3. Sodium/taurocholate cotransporting polypeptide
  4. Solute carrier family 10 member 1
  5. Cell growth-inhibiting gene 29 protein
Enzyme 8 Gene Name SLC10A1
Enzyme 8 Protein Sequence >Sodium/bile acid cotransporter 
MEAHNASAPFNFTLPPNFGKRPTDLALSVILVFMLFFIMLSLGCTMEFSKIKAHLWKPKG
LAIALVAQYGIMPLTAFVLGKVFRLKNIEALAILVCGCSPGGNLSNVFSLAMKGDMNLSI
VMTTCSTFCALGMMPLLLYIYSRGIYDGDLKDKVPYKGIVISLVLVLIPCTIGIVLKSKR
PQYMRYVIKGGMIIILLCSVAVTVLSAINVGKSIMFAMTPLLIATSSLMPFIGFLLGYVL
SALFCLNGRCRRTVSMETGCQNVQLCSTILNVAFPPEVIGPLFFFPLLYMIFQLGEGLLL
IAIFWCYEKFKTPKDKTKMIYTAATTEETIPGALGNGTYKGEDCSPCTA
Enzyme 8 Number of Residues 349
Enzyme 8 Molecular Weight 38120
Enzyme 8 Theoretical pI 8.94
Enzyme 8 GO Classification
Function
  • bile acid:sodium symporter activity
  • organic acid transporter activity
  • organic acid:sodium symporter activity
  • transporter activity
Process
  • anion transport
  • cation transport
  • cellular physiological process
  • ion transport
  • monovalent inorganic cation transport
  • organic anion transport
  • physiological process
  • sodium ion transport
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function The hepatic sodium/bile acid uptake system exhibits broad substrate specificity and transports various non-bile acid organic compounds as well. It is strictly dependent on the extracellular presence of sodium
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 25-45 60-80 91-111 120-140 156-176 191-211 220-240 283-303
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 410214 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q14973 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name NTCP_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1050 bp 
ATGGAGGCCCACAACGCGTCTGCCCCATTCAACTTCACCCTGCCACCCAACTTTGGCAAG
CGCCCCACAGACCTGGCACTGAGCGTCATCCTGGTGTTCATGTTGTTCTTCATCATGCTC
TCGCTGGGCTGCACCATGGAGTTCAGCAAGATCAAGGCTCACTTATGGAAGCCTAAAGGG
CTGGCCATCGCCCTGGTGGCACAGTATGGCATCATGCCCCTCACGGCCTTTGTGCTGGGC
AAGGTCTTCCGGCTGAAGAACATTGAGGCACTGGCCATCTTGGTCTGTGGCTGCTCACCT
GGAGGGAACCTGTCCAATGTCTTCAGTCTGGCCATGAAGGGGGACATGAACCTCAGCATT
GTGATGACCACCTGCTCCACCTTCTGTGCCCTTGGCATGATGCCTCTCCTCCTGTACATC
TACTCCAGGGGGATCTATGATGGGGACCTGAAGGACAAGGTGCCCTATAAAGGCATCGTG
ATATCACTGGTCCTGGTTCTCATTCCTTGCACCATAGGGATCGTCCTCAAATCCAAACGG
CCACAATACATGCGCTATGTCATCAAGGGAGGGATGATCATCATTCTCTTGTGCAGTGTG
GCCGTCACAGTTCTCTCTGCCATCAATGTGGGGAAGAGCATCATGTTTGCCATGACACCA
CTCTTGATTGCCACCTCCTCCCTGATGCCTTTTATTGGCTTTCTGCTGGGTTATGTTCTC
TCTGCTCTCTTCTGCCTCAATGGACGGTGCAGACGCACTGTCAGCATGGAGACTGGATGC
CAAAATGTCCAACTCTGTTCCACCATCCTCAATGTGGCCTTTCCACCTGAAGTCATTGGA
CCACTTTTCTTCTTTCCCCTCCTCTACATGATTTTCCAGCTTGGAGAAGGGCTTCTCCTC
ATTGCCATATTTTGGTGCTATGAGAAATTCAAGACTCCCAAGGATAAAACAAAAATGATC
TACACAGCTGCCACAACTGAAGAAACAATTCCAGGAGCTCTGGGAAATGGCACCTACAAA
GGGGAGGACTGCTCCCCTTGCACAGCCTAG
Enzyme 8 GenBank Gene ID L21893 Link Image
Enzyme 8 GeneCard ID SLC10A1 Link Image
Enzyme 8 GenAtlas ID SLC10A1 Link Image
Enzyme 8 HGNC ID HGNC:10905 Link Image
Enzyme 8 Chromosome Location 14
Enzyme 8 Locus 14q24.1
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Hagenbuch B, Meier PJ: Molecular cloning, chromosomal localization, and functional characterization of a human liver Na+/bile acid cotransporter. J Clin Invest. 1994 Mar;93(3):1326-31. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 8186
Enzyme 9 Name Solute carrier organic anion transporter family member 1A2
Enzyme 9 Synonyms
  1. Solute carrier family 21 member 3
  2. Sodium-independent organic anion transporter
  3. Organic anion-transporting polypeptide 1
  4. OATP1
  5. OATP- A
Enzyme 9 Gene Name SLCO1A2
Enzyme 9 Protein Sequence >Solute carrier organic anion transporter family member 1A2 
MGETEKRIETHRIRCLSKLKMFLLAITCAFVSKTLSGSYMNSMLTQIERQFNIPTSLVGF
INGSFEIGNLLLIIFVSYFGTKLHRPIMIGIGCVVMGLGCFLKSLPHFLMNQYEYESTVS
VSGNLSSNSFLCMENGTQILRPTQDPSECTKEVKSLMWVYVLVGNIVRGMGETPILPLGI
SYIEDFAKFENSPLYIGLVETGAIIGPLIGLLLASFCANVYVDTGFVNTDDLIITPTDTR
WVGAWWFGFLICAGVNVLTAIPFFFLPNTLPKEGLETNADIIKNENEDKQKEEVKKEKYG
ITKDFLPFMKSLSCNPIYMLFILVSVIQFNAFVNMISFMPKYLEQQYGISSSDAIFLMGI
YNLPPICIGYIIGGLIMKKFKITVKQAAHIGCWLSLLEYLLYFLSFLMTCENSSVVGINT
SYEGIPQDLYVENDIFADCNVDCNCPSKIWDPVCGNNGLSYLSACLAGCETSIGTGINMV
FQNCSCIQTSGNSSAVLGLCDKGPDCSLMLQYFLILSAMSSFIYSLAAIPGYMVLLRCMK
SEEKSLGVGLHTFCTRVFAGIPAPIYFGALMDSTCLHWGTLKCGESGACRIYDSTTFRYI
YLGLPAALRGSSFVPALIILILLRKCHLPGENASSGTELIETKVKGKENECKDIYQKSTV
LKDDELKTKL
Enzyme 9 Number of Residues 670
Enzyme 9 Molecular Weight 74146
Enzyme 9 Theoretical pI 5.75
Enzyme 9 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Mediates the Na(+)-independent transport of organic anions such as sulfobromophthalein (BSP) and conjugated (taurocholate) and unconjugated (cholate) bile acids
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-36
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 885978 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P46721 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name SO1A2_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >2013 bp 
ATGGGAGAAACTGAGAAAAGAATTGAAACCCATAGAATAAGATGTCTTTCCAAGTTGAAG
ATGTTTCTGTTGGCAATAACATGTGCATTTGTATCCAAAACACTGTCTGGATCTTATATG
AATTCCATGCTCACACAAATAGAGAGACAATTCAACATCCCAACATCTCTAGTTGGATTC
ATTAATGGAAGCTTTGAGATTGGAAATCTTTTGTTGATTATATTTGTGAGTTATTTTGGA
ACCAAACTGCATAGACCTATAATGATTGGCATTGGATGTGTGGTTATGGGCTTAGGCTGT
TTCTTAAAATCACTACCTCATTTCCTCATGAACCAATATGAATATGAATCTACAGTTTCA
GTTTCAGGCAACTTGTCCTCAAACAGTTTCTTGTGTATGGAAAATGGAACCCAGATTTTA
AGACCAACGCAGGATCCATCAGAGTGTACAAAGGAAGTTAAATCATTAATGTGGGTGTAC
GTCCTAGTAGGCAATATTGTACGTGGAATGGGTGAAACTCCCATCCTGCCTTTGGGTATT
TCCTATATAGAAGATTTTGCCAAATTTGAAAATTCTCCTTTATATATTGGGCTTGTAGAA
ACAGGAGCTATTATTGGTCCTTTGATTGGACTTTTGTTGGCATCATTCTGTGCAAATGTT
TATGTTGACACTGGATTTGTGAACACAGATGATCTGATCATAACTCCCACTGACACTCGT
TGGGTCGGTGCATGGTGGTTTGGCTTTCTGATTTGTGCAGGAGTTAACGTGCTCACTGCC
ATTCCTTTTTTCTTTTTGCCCAACACACTTCCAAAGGAAGGACTAGAGACTAATGCTGAC
ATCATTAAAAATGAAAATGAAGACAAACAAAAAGAAGAGGTCAAGAAGGAAAAATATGGA
ATCACTAAAGATTTTCTACCTTTCATGAAAAGTCTTTCCTGCAATCCAATTTATATGCTT
TTCATACTTGTAAGTGTGATACAGTTCAATGCATTCGTTAACATGATCTCCTTCATGCCT
AAATACCTAGAACAGCAATATGGAATATCATCTTCAGATGCAATCTTTCTAATGGGTATT
TATAACTTACCTCCAATATGTATTGGATATATAATTGGTGGTTTAATTATGAAGAAGTTC
AAGATTACTGTCAAACAAGCTGCCCACATAGGATGTTGGTTATCCTTACTTGAGTATCTT
CTCTATTTTTTATCTTTTCTCATGACTTGTGAAAATTCTTCAGTTGTTGGAATAAATACC
TCTTATGAAGGAATTCCACAAGATTTATATGTGGAAAATGACATCTTTGCTGATTGCAAT
GTGGATTGCAACTGTCCATCTAAAATATGGGATCCTGTGTGTGGAAACAATGGCTTGTCA
TATCTGTCAGCTTGTCTTGCTGGTTGTGAGACATCCATTGGAACGGGAATAAACATGGTG
TTCCAAAATTGCAGCTGTATTCAAACATCAGGAAATTCATCTGCAGTTCTTGGGCTGTGC
GACAAAGGACCTGACTGTTCCTTGATGCTCCAGTACTTCCTAATCTTGTCAGCGATGAGC
AGTTTCATTTATTCTTTGGCTGCCATACCTGGATATATGGTTCTCTTGAGGTGTATGAAA
TCTGAAGAGAAGTCCCTTGGTGTGGGATTACATACATTTTGCACAAGAGTATTTGCTGGC
ATTCCTGCACCTATATATTTTGGCGCTTTAATGGATTCCACATGTTTACACTGGGGAACT
TTGAAATGTGGTGAGTCAGGGGCATGCAGGATATATGATTCCACCACCTTCAGATACATC
TACCTCGGATTGCCGGCAGCACTAAGAGGATCAAGCTTTGTTCCAGCCTTAATCATCTTA
ATTCTTTTGAGGAAGTGTCATCTACCTGGTGAAAATGCCTCTTCAGGAACAGAGCTTATA
GAGACAAAAGTCAAAGGGAAGGAAAATGAGTGCAAAGATATATACCAAAAGTCCACGGTT
TTGAAAGATGATGAATTGAAAACTAAATTGTAA
Enzyme 9 GenBank Gene ID U21943 Link Image
Enzyme 9 GeneCard ID SLCO1A2 Link Image
Enzyme 9 GenAtlas ID SLCO1A2 Link Image
Enzyme 9 HGNC ID HGNC:10956 Link Image
Enzyme 9 Chromosome Location 12
Enzyme 9 Locus 12p12
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Kullak-Ublick GA, Hagenbuch B, Stieger B, Schteingart CD, Hofmann AF, Wolkoff AW, Meier PJ: Molecular and functional characterization of an organic anion transporting polypeptide cloned from human liver. Gastroenterology. 1995 Oct;109(4):1274-82. [PubMed Link Image]
  2. Konig J, Cui Y, Nies AT, Keppler D: Localization and genomic organization of a new hepatocellular organic anion transporting polypeptide. J Biol Chem. 2000 Jul 28;275(30):23161-8. [PubMed Link Image]
  3. Speek M: Antisense promoter of human L1 retrotransposon drives transcription of adjacent cellular genes. Mol Cell Biol. 2001 Mar;21(6):1973-85. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 8587
Enzyme 10 Name Bile acyl-CoA synthetase
Enzyme 10 Synonyms
  1. BACS
  2. Bile acid CoA ligase
  3. BA-CoA ligase
  4. BAL
  5. Cholate--CoA ligase
  6. Very long-chain acyl-CoA synthetase homolog 2
  7. VLCSH2
  8. VLCS-H2
  9. Very long chain acyl-CoA synthetase-related protein
  10. VLACS-related
  11. VLACSR
  12. Fatty-acid- coenzyme A ligase, very long-chain 3
  13. Fatty acid transport protein 5
  14. FATP-5
  15. Solute carrier family 27 member 5
Enzyme 10 Gene Name SLC27A5
Enzyme 10 Protein Sequence >Bile acyl-CoA synthetase 
MGVRQQLALLLLLLLLLWGLGQPVWPVAVALTLRWLLGDPTCCVLLGLAMLARPWLGPWV
PHGLSLAAAALALTLLPARLPPGLRWLPADVIFLAKILHLGLKIRGCLSRQPPDTFVDAF
ERRARAQPGRALLVWTGPGAGSVTFGELDARACQAAWALKAELGDPASLCAGEPTALLVL
ASQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILP
KLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTG
LPKPAILTHERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAP
KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQ
QRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAEPVRDN
QGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMD
REGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVQ
LAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFNVGIVVD
PLFVLDNRAQSFRPLTAEMYQAVCEGTWRL
Enzyme 10 Number of Residues 690
Enzyme 10 Molecular Weight 75386
Enzyme 10 Theoretical pI 7.70
Enzyme 10 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 10 General Function Lipid transport and metabolism
Enzyme 10 Specific Function Acyl-CoA synthetase involved in bile acid metabolism. Proposed to catalyze the first step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi by activating them to their CoA thioesters. Seems to activate secondary bile acids entering the liver from the enterohepatic circulation. In vitro, also activates 3-alpha,7- alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol
Enzyme 10 Pathways
Enzyme 10 Reactions
  • ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-21
Enzyme 10 Transmembrane Regions
  • 9-29 31-51 56-76
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 4768277 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q9Y2P5 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name S27A5_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >2073 bp 
ATGGGTGTCAGGCAACAGTTGGCCTTGCTGCTGCTGCTGCTGCTCCTGCTCTGGGGCCTG
GGGCAGCCAGTGTGGCCAGTCGCTGTGGCCTTGACCCTGCGCTGGCTCCTGGGGGATCCC
ACATGTTGCGTGCTACTTGGGCTGGCCATGTTAGCACGGCCCTGGCTCGGCCCCTGGGTG
CCCCATGGGCTGAGCCTGGCAGCTGCGGCCCTGGCACTAACCCTCCTGCCAGCACGGCTG
CCCCCAGGACTACGCTGGCTGCCGGCTGATGTGATCTTCTTGGCCAAGATCCTCCACCTG
GGCCTGAAGATCAGGGGATGCTTGAGCCGGCAGCCGCCTGACACCTTTGTAGATGCCTTC
GAGCGGCGAGCACGAGCGCAGCCTGGCAGGGCACTCTTGGTGTGGACGGGGCCTGGGGCC
GGCTCAGTCACCTTTGGTGAGCTGGATGCCCGGGCCTGCCAGGCGGCATGGGCCCTGAAG
GCTGAGCTGGGTGACCCTGCGAGCCTGTGTGCCGGGGAGCCTACTGCCCTCCTTGTGCTG
GCTTCCCAGGCCGTTCCAGCCCTGTGTATGTGGCTGGGGCTGGCCAAGCTGGGCTGCCCA
ACAGCCTGGATCAACCCGCATGGCCGGGGGATGCCCCTGGCGCACTCTGTGCTGAGCTCT
GGGGCCCGGGTGCTGGTGGTGGACCCAGACCTCCGGGAGAGCCTGGAGGAGATCCTTCCC
AAGCTGCAGGCTGAGAACATCCGCTGCTTCTACCTCAGCCATACCTCCCCTACACCAGGG
GTGGGGGCTCTGGGGGCTGCCCTGGATGCAGCGCCCTCCCACCCAGTGCCTGCTGACCTG
CGTGCTGGGATCACATGGAGAAGCCCTGCCCTCTTCATCTATACCTCGGGGACCACTGGC
CTCCCGAAGCCAGCCATCCTCACGCATGAGCGGGTACTGCAGATGAGCAAGATGCTGTCC
TTATCTGGGGCCACAGCTGATGATGTGGTTTACACGGTCCTGCCTCTGTACCACGTGATG
GGACTTGTCGTTGGGATCCTCGGCTGCTTAGATCTCGGAGCCACCTGTGTTCTGGCCCCC
AAGTTCTCTACTTCCTGCTTCTGGGATGACTGTCGGCAGCATGGCGTGACAGTGATCCTG
TATGTGGGCGAGCTCCTGCGGTACTTGTGTAACATTCCCCAGCAACCAGAGGACCGGACA
CATACAGTCCGCCTGGCAATGGGCAATGGACTACGGGCTGATGTGTGGGAGACCTTCCAG
CAGCGCTTCGGTCCTATTCGGATCTGGGAAGTCTACGGCTCCACAGAAGGCAACATGGGC
TTAGTCAACTATGTGGGGCGCTGCGGGGCCCTGGGCAAGATGAGCTGCCTCCTCCGAATG
CTGTCCCCCTTTGAGCTGGTGCAGTTCGACATGGAGGCGGCGGAGCCTGTGAGGGACAAT
CAGGGCTTCTGCATCCCTGTAGGGCTAGGGGAGCCGGGGCTGCTGCTGACCAAGGTGGTA
AGCCAGCAACCCTTCGTGGGCTACCGCGGCCCCCGAGAGCTGTCGGAACGGAAGCTGGTG
CGCAACGTGCGGCAATCGGGCGACGTTTACTACAACACCGGGGACGTACTGGCCATGGAC
CGCGAAGGCTTCCTCTACTTCCGCGACCGCCTCGGGGACACCTTCCGATGGAAGGGCGAG
AACGTGTCCACGCACGAGGTGGAGGGCGTGTTGTCGCAGGTGGACTTCTTGCAACAGGTT
AACGTGTATGGCGTGTGCGTGCCAGGTTGTGAGGGTAAGGTGGGCATGGCTGCTGTGCAG
CTAGCCCCCGGCCAGACTTTCGACGGGGAGAAGTTGTACCAGCACGTTCGCGCTTGGCTC
CCTGCCTACGCTACCCCCCATTTCATCCGCATCCAGGACGCCATGGAGGTCACCAGCACG
TTCAAACTGATGAAGACCCGGTTGGTGCGTGAGGGCTTCAATGTGGGGATCGTGGTTGAC
CCTCTGTTTGTACTGGACAACCGGGCCCAGTCCTTCCGGCCCCTGACGGCAGAAATGTAC
CAGGCTGTGTGTGAGGGAACCTGGAGGCTCTGA
Enzyme 10 GenBank Gene ID AF064255 Link Image
Enzyme 10 GeneCard ID SLC27A5 Link Image
Enzyme 10 GenAtlas ID SLC27A5 Link Image
Enzyme 10 HGNC ID HGNC:10999 Link Image
Enzyme 10 Chromosome Location 19
Enzyme 10 Locus 19q13.43
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Steinberg SJ, Wang SJ, McGuinness MC, Watkins PA: Human liver-specific very-long-chain acyl-coenzyme A synthetase: cDNA cloning and characterization of a second enzymatically active protein. Mol Genet Metab. 1999 Sep;68(1):32-42. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 8766
Enzyme 11 Name Solute carrier organic anion transporter family member 4A1
Enzyme 11 Synonyms
  1. Solute carrier family 21 member 12
  2. Sodium-independent organic anion transporter E
  3. Organic anion-transporting polypeptide E
  4. OATP-E
  5. Colon organic anion transporter
  6. Organic anion transporter polypeptide-related protein 1
  7. OATP-RP1
  8. OATPRP1
  9. POAT
Enzyme 11 Gene Name SLCO4A1
Enzyme 11 Protein Sequence >Solute carrier organic anion transporter family member 4A1 
MPLHQLGDKPLTFPSPNSAMENGLDHTPPSRRASPGTPLSPGSLRSAAHSPLDTSKQPLC
QLWAEKHGARGTHEVRYVSAGQSVACGWWAFAPPCLQVLNTPKGILFFLCAAAFLQGMTV
NGFINTVITSLERRYDLHSYQSGLIASSYDIAACLCLTFVSYFGGSGHKPRWLGWGVLLM
GTGSLVFALPHFTAGRYEVELDAGVRTCPANPGAVCADSTSGLSRYQLVFMLGQFLHGVG
ATPLYTLGVTYLDENVKSSCSPVYIAIFYTAAILGPAAGYLIGGALLNIYTEMGRRTELT
TESPLWVGAWWVGFLGSGAAAFFTAVPILGYPRQLPGSQRYAVMRAAEMHQLKDSSRGEA
SNPDFGKTIRDLPLSIWLLLKNPTFILLCLAGATEATLITGMSTFSPKFLESQFSLSASE
AATLFGYLVVPAGGGGTFLGGFFVNKLRLRGSAVIKFCLFCTVVSLLGILVFSLHCPSVP
MAGVTASYGGSLLPEGHLNLTAPCNAACSCQPEHYSPVCGSDGLMYFSLCHAGCPAATET
NVDGQKVYRDCSCIPQNLSSGFGHATAGKCTSTCQRKPLLLVFIFVVIFFTFLSSIPALT
ATLRCVRDPQRSFALGIQWIVVRILGGIPGPIAFGWVIDKACLLWQDQCGQQGSCLVYQN
SAMSRYILIMGLLYKVLGVLFFAIACFLYKPLSESSDGLETCLPSQSSAPDSATDSQLQS
SV
Enzyme 11 Number of Residues 722
Enzyme 11 Molecular Weight 77194
Enzyme 11 Theoretical pI 7.85
Enzyme 11 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Mediates the Na(+)-independent transport of organic anions such as the thyroid hormones T3 (triiodo-L-thyronine), T4 (thyroxine) and rT3, and of estrone-3-sulfate and taurocholate
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-188
Enzyme 11 Transmembrane Regions
  • 104-124 144-164 172-192 229-249 263-283 309-329 372-392 424-444 454-474 579-599 617-637 667-687
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 6683743 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q96BD0 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name SO4A1_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >2169 bp 
ATGCCCCTGCATCAGCTGGGGGACAAGCCGCTCACCTTCCCCAGCCCCAACTCAGCCATG
GAAAACGGGCTTGACCACACCCCACCCAGCAGGAGGGCATCCCCGGGCACACCCCTGAGC
CCCGGCTCCCTCCGCTCCGCTGCCCATAGCCCCCTGGACACCAGCAAGCAGCCCCTCTGC
CAGCTCTGGGCCGAGAAGCATGGCGCCCGGGGGACCCATGAGGTGCGGTACGTCTCGGCC
GGGCAGAGCGTGGCGTGCGGCTGGTGGGCCTTCGCACCGCCGTGCCTGCAGGTCCTCAAC
ACGCCCAAGGGCATCCTGTTCTTCCTGTGTGCGGCCGCATTCCTGCAGGGGATGACTGTG
AATGGCTTCATCAACACAGTCATCACCTCCCTGGAGCGCCGCTATGACCTGCACAGCTAC
CAGAGCGGGCTCATCGCCAGCTCCTACGACATTGCCGCCTGCCTCTGCCTCACCTTCGTC
AGCTACTTCGGGGGCTCAGGGCACAAGCCGCGCTGGCTGGGCTGGGGCGTGCTGCTTATG
GGCACGGGGTCGCTGGTGTTCGCGCTGCCCCACTTCACGGCTGGCCGCTATGAGGTGGAG
TTGGACGCGGGTGTCAGGACGTGCCCTGCCAACCCCGGCGCGGTGTGTGCGGACAGCACC
TCGGGCCTGTCCCGCTACCAGCTGGTCTTCATGCTGGGCCAGTTCCTGCATGGCGTGGGT
GCCACACCCCTCTACACGCTGGGCGTCACCTACCTGGATGAGAACGTCAAGTCCAGCTGC
TCGCCCGTCTACATTGCCATCTTCTACACAGCGGCCATCCTGGGCCCAGCTGCCGGCTAC
CTGATTGGAGGTGCCCTGCTGAATATCTACACGGAAATGGGCCGACGGACGGAGCTGACC
ACCGAGAGCCCACTGTGGGTCGGCGCCTGGTGGGTCGGCTTCCTGGGCTCTGGGGCCGCT
GCTTTCTTCACCGCCGTTCCCATCCTTGGTTACCCTCGGCAGCTGCCAGGCTCCCAGCGC
TACGCGGTCATGAGAGCGGCGGAAATGCACCAGTTGAAGGACAGCAGCCGTGGGGAGGCG
AGCAACCCGGACTTTGGGAAAACCATCAGAGACCTGCCTCTCTCCATCTGGCTCCTGCTG
AAGAACCCCACGTTCATCCTGCTCTGCCTGGCCGGGGCCACCGAGGCCACTCTCATCACC
GGCATGTCCACGTTCAGCCCCAAGTTCTTGGAGTCCCAGTTCAGCCTGAGTGCCTCAGAA
GCTGCCACCTTGTTTGGGTACCTGGTGGTGCCAGCGGGTGGTGGCGGCACCTTCCTGGGC
GGCTTCTTTGTGAACAAGCTCAGGCTCCGGGGCTCCGCGGTCATCAAGTTCTGCCTGTTC
TGCACCGTTGTCAGCCTGCTGGGCATCCTCGTCTTCTCACTGCACTGCCCCAGTGTGCCC
ATGGCGGGCGTCACAGCCAGCTACGGCGGGAGCCTCCTGCCCGAAGGCCACCTGAACCTA
ACGGCTCCCTGCAACGCTGCCTGCAGCTGCCAGCCAGAACACTACAGCCCTGTGTGCGGC
TCGGACGGCCTCATGTACTTCTCACTGTGCCACGCAGGGTGCCCTGCAGCCACGGAGACG
AATGTGGACGGCCAGAAGGTGTACCGAGACTGTAGCTGTATCCCTCAGAATCTTTCCTCT
GGTTTTGGCCATGCCACTGCAGGGAAATGCACTTCAACTTGTCAGAGAAAGCCCCTCCTT
CTGGTTTTCATATTCGTTGTAATTTTCTTTACATTCCTCAGCAGCATTCCTGCACTAACG
GCAACTCTACGATGTGTCCGTGACCCTCAGAGATCCTTTGCCCTGGGAATCCAGTGGATT
GTAGTTAGAATACTAGGGGGCATCCCGGGGCCCATCGCCTTCGGCTGGGTGATCGACAAG
GCCTGTCTGCTGTGGCAGGACCAGTGTGGCCAGCAGGGCTCCTGCTTGGTGTACCAGAAT
TCGGCCATGAGCCGCTACATACTCATCATGGGGCTCCTGTACAAGGTGCTGGGCGTCCTC
TTCTTTGCCATAGCCTGCTTCTTATACAAGCCCCTGTCGGAGTCTTCAGATGGCCTGGAA
ACTTGTCTGCCCAGCCAGTCCTCAGCCCCTGACAGTGCCACAGATAGCCAGCTCCAGAGC
AGCGTCTGA
Enzyme 11 GenBank Gene ID AB031051 Link Image
Enzyme 11 GeneCard ID SLCO4A1 Link Image
Enzyme 11 GenAtlas ID SLCO4A1 Link Image
Enzyme 11 HGNC ID HGNC:10953 Link Image
Enzyme 11 Chromosome Location 20
Enzyme 11 Locus 20q13.33
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Tamai I, Nezu J, Uchino H, Sai Y, Oku A, Shimane M, Tsuji A: Molecular identification and characterization of novel members of the human organic anion transporter (OATP) family. Biochem Biophys Res Commun. 2000 Jun 24;273(1):251-60. [PubMed Link Image]
  2. Fujiwara K, Adachi H, Nishio T, Unno M, Tokui T, Okabe M, Onogawa T, Suzuki T, Asano N, Tanemoto M, Seki M, Shiiba K, Suzuki M, Kondo Y, Nunoki K, Shimosegawa T, Iinuma K, Ito S, Matsuno S, Abe T: Identification of thyroid hormone transporters in humans: different molecules are involved in a tissue-specific manner. Endocrinology. 2001 May;142(5):2005-12. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 14865
Enzyme 12 Name Gastrotropin
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name FABP6
Enzyme 12 Protein Sequence >MAFTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTWSQHYSGGHTMTNKFTVGKES 
NIQTMGGKTFKATVQMEGGKLVVNFPNYHQTSEIVGDKLVEVSTIGGVTYERVSKRLA
Enzyme 12 Number of Residues 128
Enzyme 12 Molecular Weight 14371
Enzyme 12 Theoretical pI 6.81
Enzyme 12 GO Classification
Function
  • binding
  • lipid binding
Process
  • cellular physiological process
  • physiological process
  • transport
Component
—
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Ileal protein which stimulates gastric acid and pepsinogen secretion. Seems to be able to bind to bile salts and bilirubins
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 894183 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P51161 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name FABP6_HUMAN Link Image
Enzyme 12 PDB ID 1O1V Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >387 bp 
ATGGCTTTCACCGGCAAGTTCGAGATGGAGAGTGAGAAGAATTATGATGAGTTCATGAAG
CTCCTTGGGATCTCCAGCGATGTAATCGAAAAGGCCCGCAACTTCAAGATCGTCACGGAG
GTGCAGCAGGATGGGCAGGACTTCACTTGGTCCCAGCACTACTCCGGGGGCCACACCATG
ACCAACAAGTTCACTGTTGGCAAGGAAAGCAACATACAGACAATGGGGGGCAAGACGTTC
AAGGCCACTGTGCAGATGGAGGGCGGGAAGCTGGTGGTGAATTTCCCCAACTATCACCAG
ACCTCAGAGATCGTGGGTGACAAGCTGGTGGAGGTCTCCACCATCGGAGGCGTGACCTAT
GAGCGCGTGAGCAAGAGACTGGCCTAA
Enzyme 12 GenBank Gene ID U19869 Link Image
Enzyme 12 GeneCard ID P51161 Link Image
Enzyme 12 GenAtlas ID FABP6 Link Image
Enzyme 12 HGNC ID HGNC:3561 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Oelkers P, Dawson PA: Cloning and chromosomal localization of the human ileal lipid-binding protein. Biochim Biophys Acta. 1995 Jul 13;1257(2):199-202. [PubMed Link Image]
  2. Fujita M, Fujii H, Kanda T, Sato E, Hatakeyama K, Ono T: Molecular cloning, expression, and characterization of a human intestinal 15-kDa protein. Eur J Biochem. 1995 Oct 15;233(2):406-13. [PubMed Link Image]
Enzyme 12 Metabolite References
  1. Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed Link Image]
Enzyme 13 [top]
Enzyme 13 ID 16445
Enzyme 13 Name cDNA FLJ41040 fis, clone LIVER1000017, highly similar to Bile acyl-CoA synthetase (EC 6.2.1.7)
Enzyme 13 Synonyms
  1. SubName: Solute carrier family 27 (Fatty acid transporter), member 5
Enzyme 13 Gene Name SLC27A5
Enzyme 13 Protein Sequence >cDNA FLJ41040 fis, clone LIVER1000017, highly similar to Bile acyl-CoA synthetase (EC 6.2.1.7) 
MGVRQQLALLLLLLLLLWGLGQPVWPVAVALTLRWLLGDPTCCVLLGLAMLARPWLGPWV
PHGLSLAAAALALTLLPARLPPGLRWLPADVIFLAKILHLGLKIRGCLSRQPPDTFVDAF
ERRARAQPGRALLVWTGPGAGSVTFGELDARACQAAWALKAELGDPASLCAGEPTALLVL
ASQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILP
KLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTG
LPKPAILTHERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAP
KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQ
QRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAEPVRDN
QGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMD
REGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVQ
LAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFNVGIVVD
PLFVLDNRAQSFRPLTAEMYQAVCEGTWRL
Enzyme 13 Number of Residues 690
Enzyme 13 Molecular Weight 75386
Enzyme 13 Theoretical pI 7.70
Enzyme 13 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 13 General Function Lipid transport and metabolism
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions
  • (1) ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA [RN:R02794]
  • (2) ATP + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate + CoA = AMP + diphosphate + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA [RN:R04580] ALL_REAC R02794 R04580
  • (other) R03974 R04507
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein Not Available
Enzyme 13 UniProtKB/Swiss-Prot ID B3KVP6 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name B3KVP6_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence Not Available
Enzyme 13 GenBank Gene ID AK123036 Link Image
Enzyme 13 GeneCard ID B3KVP6 Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location 19
Enzyme 13 Locus 19q13.43
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available