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Human Metabolome Database Version 2.5

 

Showing metabocard for Prostaglandin E2 (HMDB01220)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-19 13:11:17
Accession Number HMDB01220
Secondary Accession Numbers Not Available
Common Name Prostaglandin E2
Description Dinoprostone is a naturally occurring prostaglandin E2 (PGE2) and the most common and most biologically active of the mammalian prostaglandins. It has important effects in labour and also stimulates osteoblasts to release factors which stimulate bone resorption by osteoclasts (a type of bone cell that removes bone tissue by removing the bone's mineralized matrix). PGE2 has been shown to increase vasodilation and cAMP production, to enhance the effects of bradykinin and histamine, induction of uterine contractions and of platelet aggregation. PGE2 is also responsible for maintaining the open passageway of the fetal ductus arteriosus; decreasing T-cell proliferation and lymphocyte migration and activating the secretion of IL-1α and IL-2. PGE2 exhibits both pro- and anti-inflammatory effects, particularly on dendritic cells (DC). Depending on the nature of maturation signals, PGE2 has different and sometimes opposite effects on DC biology. PGE2 exerts an inhibitory action, reducing the maturation of DC and their ability to present antigen. PGE2 has also been shown to stimulate DC and promote IL-12 production when given in combination with TNF-alpha. PGE2 is an environmentally bioactive substance. Its action is prolonged and sustained by other factors especially IL-10. It modulates the activities of professional DC by acting on their differentiation, maturation and their ability to secrete cytokines. PGE2 is a potent inducer of IL-10 in bone marrow-derived DC (BM-DC), and PGE2-induced IL-10 is a key regulator of the BM-DC pro-inflammatory phenotype. (PMID: 16978535) Dinoprostone is a naturally occurring prostaglandin E2 (PGE2) and the most common and most biologically active of the mammalian prostaglandins. It has important effects in labour and also stimulates osteoblasts to release factors which stimulate bone resorption by osteoclasts (a type of bone cell that removes bone tissue by removing the bone's mineralized matrix). PGE2 has been shown to increase vasodilation and cAMP production, to enhance the effects of bradykinin and histamine, to induce uterine contractions and to activate platelet aggregation. PGE2 is also responsible for maintaining the open passageway of the fetal ductus arteriosus; decreasing T-cell proliferation and lymphocyte migration and activating the secretion of IL-1alpha and IL-2. PGE2 exhibits both pro- and anti-inflammatory effects, particularly on dendritic cells (DC). Depending on the nature of maturation signals, PGE2 has different and sometimes opposite effects on DC biology. PGE2 exerts an inhibitory action, reducing the maturation of DC and their ability to present antigen. PGE2 has also been shown to stimulate DC and promote IL-12 production when given in combination with TNF-alpha. PGE2 is an environmentally bioactive substance. Its action is prolonged and sustained by other factors especially IL-10. It modulates the activities of professional DC by acting on their differentiation, maturation and their ability to secrete cytokines. PGE2 is a potent inducer of IL-10 in bone marrow-derived DC (BM-DC), and PGE2-induced IL-10 is a key regulator of the BM-DC pro-inflammatory phenotype. (PMID: 16978535) Prostaglandins are eicosanoids. The eicosanoids consist of the prostaglandins (PGs), thromboxanes (TXs), leukotrienes (LTs) and lipoxins (LXs). The PGs and TXs are collectively identified as prostanoids. Prostaglandins were originally shown to be synthesized in the prostate gland, thromboxanes from platelets (thrombocytes) and leukotrienes from leukocytes, hence the derivation of their names. All mammalian cells except erythrocytes synthesize eicosanoids. These molecules are extremely potent, able to cause profound physiological effects at very dilute concentrations. All eicosanoids function locally at the site of synthesis, through receptor-mediated G-protein linked signaling pathways.
Synonyms
  1. (-)-Prostaglandin E2
  2. 5-trans-PGE2
  3. Dinoprostone
  4. Dinoprostonum
  5. Glandin
  6. Minprositin E2
  7. Minprostin E2
  8. PGE2
  9. Prepidil
  10. Prostaglandin E
  11. Prostaglandin E2
  12. Prostaglandin E2alpha
  13. Prostarmon E
  14. Prostin
  15. Prostin E2
  16. l-Prostaglandin E2
  17. (5Z,13E)-(15S)-11alpha,15-Dihydroxy-9-oxoprosta-5,13-dienoate
  18. (5Z,13E)-(15S)-11alpha,15-Dihydroxy-9-oxoprost-13-enoate
  19. (5Z,13E)-(15S)-11alpha,15-Dihydroxy-9-oxoprosta-5,13-dienoic acid
  20. (5Z,13E)-(15S)-11alpha,15-Dihydroxy-9-oxoprost-13-enoic acid
  21. (5Z,13E,15S)-11-alpha,15-dihydroxy-9-oxoprost-5,13-dienoic acid
  22. (5Z,13E,15S)-11-alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
Chemical IUPAC Name (E)-7-[(1S,2S,3R)-3-hydroxy-2-[(E,3S)-3-hydroxyoct-1-enyl]-5-oxo-cyclopentyl]hept-5-enoic acid
Chemical Formula C20H32O5
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Prostanoids
Sub Class
  • Prostaglandins
Family
  • Mammalian Metabolite
Species
  • ketone
  • secondary alcohol
  • carboxylic acid
  • alkene
Biofunction
  • Component of Prostaglandin and leukotriene metabolism
Application
Source
  • Endogenous
Average Molecular Weight 352.465
Monoisotopic Molecular Weight 352.224976
Isomeric SMILES CCCCC[C@H](O)C=C[C@H]1[C@H](O)CC(=O)[C@@H]1CC=C/CCCC(O)=O
Canonical SMILES CCCCCC(O)C=CC1C(O)CC(=O)C1CC=CCCCC(O)=O
KEGG Compound ID C00584 Link Image
BioCyc ID 5Z13E-15S-1115-DIHYDROXY-9-OXOPROS Link Image
BiGG ID 35424 Link Image
Wikipedia Link Dinoprostone Link Image
NuGOwiki Link HMDB01220 Link Image
Metagene Link HMDB01220 Link Image
METLIN ID 6089 Link Image
PubChem Compound 5280360 Link Image
PubChem Substance 8616235 Link Image
ChEBI ID 15551 Link Image
CAS Registry Number 363-24-6
InChI Identifier InChI=1/C20H32O5/c1-2-3-6-9-15(21)12-13-17-16(18(22)14-19(17)23)10-7-4-5-8-11-20(24)25/h4,7,12-13,15-17,19,21,23H,2-3,5-6,8-11,14H2,1H3,(H,24,25)/b7-4-,13-12+/t15-,16+,17+,19+/m0/s1
Synthesis Reference Corey, Elias J.; Weinshenker, Ned M.; Schaaf, Thomas K.; Huber, Willy. Stereo-controlled synthesis of dl-prostaglandins F2a and E2. Journal of the American Chemical Society (1969), 91(20), 5675-7.
Melting Point (Experimental) 67 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.0581 mg/mL [MEYLAN,WM et al. (1996)]; 0.044 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity 2.82 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity 3.31 [Predicted by ALOGPS]; 2.79 [Predicted by PubChem via XLOGP] 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 (Bruker)
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 Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane
  • Cytoplasm
  • endoplasmic reticulum
  • Extracellular
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Brain
Fibroblasts
Placenta
Skin
Concentrations (Normal)
Biofluid Blood
Value 0.001 +/- 0.000053 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Sanchez-Moreno C, Cano MP, de Ancos B, Plaza L, Olmedilla B, Granado F, Martin A: High-pressurized orange juice consumption affects plasma vitamin C, antioxidative status and inflammatory markers in healthy humans. J Nutr. 2003 Jul;133(7):2204-9. [PubMed Link Image]
Biofluid Blood
Value 0.0009 +/- 0.000060 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Sanchez-Moreno C, Cano MP, de Ancos B, Plaza L, Olmedilla B, Granado F, Martin A: High-pressurized orange juice consumption affects plasma vitamin C, antioxidative status and inflammatory markers in healthy humans. J Nutr. 2003 Jul;133(7):2204-9. [PubMed Link Image]
Biofluid Blood
Value 0.00218 +/- 0.00287 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Oxygenated lipids were quantified by Theresa L. Pedersen and John W. Newman at the USDA’s Western Human Nutrition Research Center, Davis, CA, and Lipomics Technologies, Inc.
References
  • Psychogios N, Hau DD, Peng J, Guo AC, Mandal R, Bouatra S, Sinelnikov I, Krishnamurthy R, Eisner R, Gautam B, Young N, Xia J, Knox C, Dong E, Huang P, Hollander Z, Pedersen TL, Smith SR, Bamforth F, Greiner R, McManus B, Newman JW, Goodfriend T, Wishart DS: The human serum metabolome. PLoS One. 2011 Feb 16;6(2):e16957. [PubMed Link Image]
  • Wishart DS, Knox C, Guo AC, Eisner R, Young N, Gautam B, Hau DD, Psychogios N, Dong E, Bouatra S, Mandal R, Sinelnikov I, Xia J, Jia L, Cruz JA, Lim E, Sobsey CA, Shrivastava S, Huang P, Liu P, Fang L, Peng J, Fradette R, Cheng D, Tzur D, Clements M, Lewis A, De Souza A, Zuniga A, Dawe M, Xiong Y, Clive D, Greiner R, Nazyrova A, Shaykhutdinov R, Li L, Vogel HJ, Forsythe I: HMDB: a knowledgebase for the human metabolome. Nucleic Acids Res. 2008 Oct 25. [PubMed Link Image]
Biofluid Blood
Value 3.7E-5 +/- 1.2E-5 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Quehenberger O, Armando AM, Brown AH, Milne SB, Myers DS, Merrill AH, Bandyopadhyay S, Jones KN, Kelly S, Shaner RL, Sullards CM, Wang E, Murphy RC, Barkley RM, Leiker TJ, Raetz CR, Guan Z, Laird GM, Six DA, Russell DW, McDonald JG, Subramaniam S, Fahy E, Dennis EA: Lipidomics reveals a remarkable diversity of lipids in human plasma. J Lipid Res. 2010 Nov;51(11):3299-305. Epub 2010 Jul 29. [PubMed Link Image]
Biofluid CSF
Value 0.0013 +/- 0.0020 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 CSF
Value 0 - 0.02 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Almer G, Teismann P, Stevic Z, Halaschek-Wiener J, Deecke L, Kostic V, Przedborski S: Increased levels of the pro-inflammatory prostaglandin PGE2 in CSF from ALS patients. Neurology. 2002 Apr 23;58(8):1277-9. [PubMed Link Image]
Biofluid CSF
Value <5.110e-05 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal (control)
Comments Not Available
References
  • Romero SD, Chyatte D, Byer DE, Romero JC, Yaksh TL: Measurement of prostaglandins in the cerebrospinal fluid in cat, dog, and man. J Neurochem. 1984 Dec;43(6):1642-9. [PubMed Link Image]
Biofluid Urine
Value 0.000057 +/- 0.000020 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 0.00012 +/- 0.000025 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 0.0098 +/- 0.0011 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Farker K, Schweer H, Vollandt R, Nassr N, Nagel U, Seyberth HW, Hoffmann A, Oettel M: Measurements of urinary prostaglandins in young ovulatory women during the menstrual cycle and in postmenopausal women. Prostaglandins. 1997 Sep;54(3):655-64. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid CSF
Value 35.0 +/- 10.0 uM
Age Adult:>18 yrs old
Sex N/A
Condition Amyotrophic lateral sclerosis
Comments Not Available
References
  • Almer G, Teismann P, Stevic Z, Halaschek-Wiener J, Deecke L, Kostic V, Przedborski S: Increased levels of the pro-inflammatory prostaglandin PGE2 in CSF from ALS patients. Neurology. 2002 Apr 23;58(8):1277-9. [PubMed Link Image]
Biofluid CSF
Value 4.543e-05 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Westcott JY, Murphy RC, Stenmark K: Eicosanoids in human ventricular cerebrospinal fluid following severe brain injury. Prostaglandins. 1987 Dec;34(6):877-87. [PubMed Link Image]
Biofluid CSF
Value 9.937e-05 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Westcott JY, Murphy RC, Stenmark K: Eicosanoids in human ventricular cerebrospinal fluid following severe brain injury. Prostaglandins. 1987 Dec;34(6):877-87. [PubMed Link Image]
Biofluid CSF
Value 5.962e-06 +/- 4.259e-07 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Griffin DE, Wesselingh SL, McArthur JC: Elevated central nervous system prostaglandins in human immunodeficiency virus-associated dementia. Ann Neurol. 1994 May;35(5):592-7. [PubMed Link Image]
Biofluid CSF
Value 4.826e-06 +/- 6.246e-07 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Griffin DE, Wesselingh SL, McArthur JC: Elevated central nervous system prostaglandins in human immunodeficiency virus-associated dementia. Ann Neurol. 1994 May;35(5):592-7. [PubMed Link Image]
Biofluid CSF
Value 6.246e-05 +/- 0.000165 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Westcott JY, Murphy RC, Stenmark K: Eicosanoids in human ventricular cerebrospinal fluid following severe brain injury. Prostaglandins. 1987 Dec;34(6):877-87. [PubMed Link Image]
Biofluid CSF
Value 0.00716 (0.000116-0.0142) uM
Age N/A
Sex N/A
Comments Not Available
References
  • Westcott JY, Murphy RC, Stenmark K: Eicosanoids in human ventricular cerebrospinal fluid following severe brain injury. Prostaglandins. 1987 Dec;34(6):877-87. [PubMed Link Image]
Biofluid CSF
Value 5.650e-05 +/- 3.975e-06 uM
Age Adult:>18 yrs old
Sex Female
Comments Not Available
References
  • Hsu MM, Chou YY, Chang YC, Chou TC, Wong CS: An analysis of excitatory amino acids, nitric oxide, and prostaglandin E2 in the cerebrospinal fluid of pregnant women: the effect on labor pain. Anesth Analg. 2001 Nov;93(5):1293-6. [PubMed Link Image]
Biofluid CSF
Value 5.724e-05 +/- 5.337e-06 uM
Age Adult:>18 yrs old
Sex Female
Comments Not Available
References
  • Hsu MM, Chou YY, Chang YC, Chou TC, Wong CS: An analysis of excitatory amino acids, nitric oxide, and prostaglandin E2 in the cerebrospinal fluid of pregnant women: the effect on labor pain. Anesth Analg. 2001 Nov;93(5):1293-6. [PubMed Link Image]
Biofluid Urine
Value 0.015 +/- 0.002 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Condition Normal
Comments Not Available
References
  • Farker K, Schweer H, Vollandt R, Nassr N, Nagel U, Seyberth HW, Hoffmann A, Oettel M: Measurements of urinary prostaglandins in young ovulatory women during the menstrual cycle and in postmenopausal women. Prostaglandins. 1997 Sep;54(3):655-64. [PubMed Link Image]
Associated Disorders
Condition References
Amyotrophic lateral sclerosis
  • Almer G, Teismann P, Stevic Z, Halaschek-Wiener J, Deecke L, Kostic V, Przedborski S: Increased levels of the pro-inflammatory prostaglandin PGE2 in CSF from ALS patients. Neurology. 2002 Apr 23;58(8):1277-9. [PubMed Link Image]
Normal
  • Farker K, Schweer H, Vollandt R, Nassr N, Nagel U, Seyberth HW, Hoffmann A, Oettel M: Measurements of urinary prostaglandins in young ovulatory women during the menstrual cycle and in postmenopausal women. Prostaglandins. 1997 Sep;54(3):655-64. [PubMed Link Image]
OMIM ID
  • 105400 Link Image (Amyotrophic lateral sclerosis)
Pathways
Name SMPDB Link KEGG Link
Arachidonic Acid Metabolism SMP00075 Link Image map00590 Link Image
General References
  1. Ilzecka J: Prostaglandin E2 is increased in amyotrophic lateral sclerosis patients. Acta Neurol Scand. 2003 Aug;108(2):125-9. [PubMed Link Image]
  2. Catanzarite VA: Prophylactic intramyometrial carboprost tromethamine does not substantially reduce blood loss relative to intramyometrial oxytocin at routine cesarean section. Am J Perinatol. 1990 Jan;7(1):39-42. [PubMed Link Image]
  3. Waschbisch A, Fiebich BL, Akundi RS, Schmitz ML, Hoozemans JJ, Candelario-Jalil E, Virtainen N, Veerhuis R, Slawik H, Yrjanheikki J, Hull M: Interleukin-1 beta-induced expression of the prostaglandin E-receptor subtype EP3 in U373 astrocytoma cells depends on protein kinase C and nuclear factor-kappaB. J Neurochem. 2006 Feb;96(3):680-93. Epub 2006 Jan 9. [PubMed Link Image]
  4. Seo JY, Kim EK, Lee SH, Park KC, Kim KH, Eun HC, Chung JH: Enhanced expression of cylooxygenase-2 by UV in aged human skin in vivo. Mech Ageing Dev. 2003 Aug-Sep;124(8-9):903-10. [PubMed Link Image]
  5. Amato F, Rizzuto G, Nicoletti A, Senatore M, Roberti R: [Isolated peripheral arterial ischaemia and medullary neurostimulation: case report] G Ital Nefrol. 2003 Mar-Apr;20(2):200-4. [PubMed Link Image]
  6. Laitinen K, Arvola T, Moilanen E, Lampi AM, Ruuska T, Isolauri E: Characterization of breast milk received by infants with gross blood in stools. Biol Neonate. 2005;87(1):66-72. Epub 2004 Nov 9. [PubMed Link Image]
  7. Yamada M, Ogata M, Kawai M, Mashima Y, Nishida T: Substance P in human tears. Cornea. 2003 Oct;22(7 Suppl):S48-54. [PubMed Link Image]
  8. Choi SH, Langenbach R, Bosetti F: Cyclooxygenase-1 and -2 enzymes differentially regulate the brain upstream NF-kappa B pathway and downstream enzymes involved in prostaglandin biosynthesis. J Neurochem. 2006 Aug;98(3):801-11. Epub 2006 Jun 19. [PubMed Link Image]
  9. Schmitz T, Dallot E, Leroy MJ, Breuiller-Fouche M, Ferre F, Cabrol D: EP(4) receptors mediate prostaglandin E(2)-stimulated glycosaminoglycan synthesis in human cervical fibroblasts in culture. Mol Hum Reprod. 2001 Apr;7(4):397-402. [PubMed Link Image]
  10. Christidis N, Kopp S, Ernberg M: The effect on mechanical pain threshold over human muscles by oral administration of granisetron and diclofenac-sodium. Pain. 2005 Feb;113(3):265-70. [PubMed Link Image]
  11. Konopka T, Rutkowska M, Hirnle L, Kopec W, Karolewska E: The secretion of prostaglandin E2 and interleukin 1-beta in women with periodontal diseases and preterm low-birth-weight. Bull Group Int Rech Sci Stomatol Odontol. 2003 Jan-Apr;45(1):18-28. [PubMed Link Image]
  12. Iizuka H, Ohkawara A, Ishibashi Y: Human skin epidermal adenylate cyclase systems: defective beta-adrenergic responsiveness in the involved epidermis of Darier's disease. Curr Probl Dermatol. 1983;11:45-58. [PubMed Link Image]
  13. Greaves MW: Does ultraviolet-evoked prostaglandin formation protect skin from actinic cancer? Lancet. 1978 Jan 28;1(8057):189. [PubMed Link Image]
  14. Wikipedia Link Image
Metabolic Enzymes
  1. Carbonyl reductase [NADPH] 1
  2. Carbonyl reductase [NADPH] 3
  3. 15-hydroxyprostaglandin dehydrogenase [NAD+]
  4. Prostaglandin E synthase
  5. Solute carrier organic anion transporter family member 1B1
  6. Prostaglandin E2 receptor EP1 subtype
  7. Prostaglandin E2 receptor EP4 subtype
  8. Prostaglandin E synthase 2
  9. cDNA, FLJ95780, Homo sapiens carbonyl reductase 1 (CBR1), mRNA (Carbonyl reductase 1, isoform CRA_d)
  10. Prostaglandin E2 receptor EP3 subtype
  11. Prostaglandin E2 receptor EP2 subtype
  12. Solute carrier family 22 member 7
  13. cDNA FLJ32487 fis, clone SKNSH1000002, highly similar to Prostaglandin E synthase 2 (EC 5.3.99.3)
  14. CUGBP Elav-like family member 2
  15. cDNA, FLJ79474, highly similar to Prostaglandin E2 receptor, EP3 subtype (Prostaglandin E receptor 3 (Subtype EP3), isoform CRA_d)
Enzyme 1 [top]
Enzyme 1 ID 5304
Enzyme 1 Name Carbonyl reductase [NADPH] 1
Enzyme 1 Synonyms
  1. 15-hydroxyprostaglandin dehydrogenase [NADP+]
  2. NADPH-dependent carbonyl reductase 1
  3. Prostaglandin 9-ketoreductase
  4. Prostaglandin-E(2) 9-reductase
Enzyme 1 Gene Name CBR1
Enzyme 1 Protein Sequence >Carbonyl reductase [NADPH] 1
MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFH
QLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRD
VCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTK
KGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKA
TKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW
Enzyme 1 Number of Residues 277
Enzyme 1 Molecular Weight 30374.7
Enzyme 1 Theoretical pI 8.49
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 1 General Function Involved in oxidoreductase activity
Enzyme 1 Specific Function NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate + NADP+ = (13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate + NADPH + H+ [RN:R04552]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID P16152 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name CBR1_HUMAN Link Image
Enzyme 1 PDB ID 1WMA Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >834 bp
ATGTCGTCCGGCATCCATGTAGCGCTGGTGACTGGAGGCAACAAGGGCATCGGCTTGGCC
ATCGTGCGCGACCTGTGCCGGCTGTTCTCGGGGGACGTGGTGCTCACGGCGCGGGACGTG
ACGCGGGGCCAGGCGGCCGTACAGCAGCTGCAGGCGGAGGGCCTGAGCCCGCGCTTCCAC
CAGCTGGACATCGACGATCTGCAGAGCATCCGCGCCCTGCGCGACTTCCTGCGCAAGGAG
TACGGGGGCCTGGACGTGCTGGTCAACAACGCGGGCATCGCCTTCAAGGTTGCTGATCCC
ACACCCTTTCATATTCAAGCTGAAGTGACGATGAAAACAAATTTCTTTGGTACCCGAGAT
GTGTGCACAGAATTACTCCCTCTAATAAAACCCCAAGGGAGAGTGGTGAACGTATCTAGC
ATCATGAGCGTCAGAGCCCTTAAAAGCTGCAGCCCAGAGCTGCAGCAGAAGTTCCGCAGT
GAGACCATCACTGAGGAGGAGCTGGTGGGGCTCATGAACAAGTTTGTGGAGGATACAAAG
AAGGGAGTGCACCAGAAGGAGGGCTGGCCCAGCAGCGCATACGGGGTGACGAAGATTGGC
GTCACCGTTCTGTCCAGGATCCACGCCAGGAAACTGAGTGAGCAGAGGAAAGGGGACAAG
ATCCTCCTGAATGCCTGCTGCCCAGGGTGGGTGAGAACTGACATGGCGGGACCCAAGGCC
ACCAAGAGCCCAGAAGAAGGTGCAGAGACCCCTGTGTACTTGGCCCTTTTGCCCCCAGAT
GCTGAGGGTCCCCATGGACAATTTGTTTCAGAGAAGAGAGTTGAACAGTGGTGA
Enzyme 1 GenBank Gene ID J04056 Link Image
Enzyme 1 GeneCard ID CBR1 Link Image
Enzyme 1 GenAtlas ID CBR1 Link Image
Enzyme 1 HGNC ID HGNC:1548 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 21q22.13
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Wermuth B, Bohren KM, Heinemann G, von Wartburg JP, Gabbay KH: Human carbonyl reductase. Nucleotide sequence analysis of a cDNA and amino acid sequence of the encoded protein. J Biol Chem. 1988 Nov 5;263(31):16185-8. [PubMed Link Image]
  2. Forrest GL, Akman S, Krutzik S, Paxton RJ, Sparkes RS, Doroshow J, Felsted RL, Glover CJ, Mohandas T, Bachur NR: Induction of a human carbonyl reductase gene located on chromosome 21. Biochim Biophys Acta. 1990 Apr 6;1048(2-3):149-55. [PubMed Link Image]
  3. Forrest GL, Akman S, Doroshow J, Rivera H, Kaplan WD: Genomic sequence and expression of a cloned human carbonyl reductase gene with daunorubicin reductase activity. Mol Pharmacol. 1991 Oct;40(4):502-7. [PubMed Link Image]
  4. Watanabe K, Sugawara C, Ono A, Fukuzumi Y, Itakura S, Yamazaki M, Tashiro H, Osoegawa K, Soeda E, Nomura T: Mapping of a novel human carbonyl reductase, CBR3, and ribosomal pseudogenes to human chromosome 21q22.2. Genomics. 1998 Aug 15;52(1):95-100. [PubMed Link Image]
  5. 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]
  6. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
  7. 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]
  8. Krook M, Ghosh D, Stromberg R, Carlquist M, Jornvall H: Carboxyethyllysine in a protein: native carbonyl reductase/NADP(+)-dependent prostaglandin dehydrogenase. Proc Natl Acad Sci U S A. 1993 Jan 15;90(2):502-6. [PubMed Link Image]
  9. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  10. Gonzalez-Covarrubias V, Kalabus JL, Blanco JG: Inhibition of polymorphic human carbonyl reductase 1 (CBR1) by the cardioprotectant flavonoid 7-monohydroxyethyl rutoside (monoHER). Pharm Res. 2008 Jul;25(7):1730-4. Epub 2008 May 1. [PubMed Link Image]
  11. Tanaka M, Bateman R, Rauh D, Vaisberg E, Ramachandani S, Zhang C, Hansen KC, Burlingame AL, Trautman JK, Shokat KM, Adams CL: An unbiased cell morphology-based screen for new, biologically active small molecules. PLoS Biol. 2005 May;3(5):e128. Epub 2005 Apr 5. [PubMed Link Image]
  12. Bateman R, Rauh D, Shokat KM: Glutathione traps formaldehyde by formation of a bicyclo[4.4.1]undecane adduct. Org Biomol Chem. 2007 Oct 21;5(20):3363-7. Epub 2007 Aug 29. [PubMed Link Image]
  13. Bateman RL, Rauh D, Tavshanjian B, Shokat KM: Human carbonyl reductase 1 is an S-nitrosoglutathione reductase. J Biol Chem. 2008 Dec 19;283(51):35756-62. Epub 2008 Sep 29. [PubMed Link Image]
  14. Gonzalez-Covarrubias V, Ghosh D, Lakhman SS, Pendyala L, Blanco JG: A functional genetic polymorphism on human carbonyl reductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH binding affinity. Drug Metab Dispos. 2007 Jun;35(6):973-80. Epub 2007 Mar 7. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5306
Enzyme 2 Name Carbonyl reductase [NADPH] 3
Enzyme 2 Synonyms
  1. NADPH-dependent carbonyl reductase 3
Enzyme 2 Gene Name CBR3
Enzyme 2 Protein Sequence >Carbonyl reductase [NADPH] 3
MSSCSRVALVTGANRGIGLAIARELCRQFSGDVVLTARDVARGQAAVQQLQAEGLSPRFH
QLDIDDLQSIRALRDFLRKEYGGLNVLVNNAAVAFKSDDPMPFDIKAEMTLKTNFFATRN
MCNELLPIMKPHGRVVNISSLQCLRAFENCSEDLQERFHSETLTEGDLVDLMKKFVEDTK
NEVHEREGWPNSPYGVSKLGVTVLSRILARRLDEKRKADRILVNACCPGPVKTDMDGKDS
IRTVEEGAETPVYLALLPPDATEPQGQLVHDKVVQNW
Enzyme 2 Number of Residues 277
Enzyme 2 Molecular Weight 30850.0
Enzyme 2 Theoretical pI 6.06
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 2 General Function Involved in oxidoreductase activity
Enzyme 2 Specific Function Has low NADPH-dependent oxidoreductase activity towards 4-benzoylpyridine and menadione (in vitro)
Enzyme 2 Pathways
Enzyme 2 Reactions
  • R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+ [RN:R03557]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 3702679 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O75828 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CBR3_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >834 bp
ATGTCGTCCGGCATCCATGTAGCGCTGGTGACTGGAGGCAACAAGGGCATCGGCTTGGCC
ATCGTGCGCGACCTGTGCCGGCTGTTCTCGGGGGACGTGGTGCTCACGGCGCGGGACGTG
ACGCGGGGCCAGGCGGCCGTACAGCAGCTGCAGGCGGAGGGCCTGAGCCCGCGCTTCCAC
CAGCTGGACATCGACGATCTGCAGAGCATCCGCGCCCTGCGCGACTTCCTGCGCAAGGAG
TACGGGGGCCTGGACGTGCTGGTCAACAACGCGGGCATCGCCTTCAAGGTTGCTGATCCC
ACACCCTTTCATATTCAAGCTGAAGTGACGATGAAAACAAATTTCTTTGGTACCCGAGAT
GTGTGCACAGAATTACTCCCTCTAATAAAACCCCAAGGGAGAGTGGTGAACGTATCTAGC
ATCATGAGCGTCAGAGCCCTTAAAAGCTGCAGCCCAGAGCTGCAGCAGAAGTTCCGCAGT
GAGACCATCACTGAGGAGGAGCTGGTGGGGCTCATGAACAAGTTTGTGGAGGATACAAAG
AAGGGAGTGCACCAGAAGGAGGGCTGGCCCAGCAGCGCATACGGGGTGACGAAGATTGGC
GTCACCGTTCTGTCCAGGATCCACGCCAGGAAACTGAGTGAGCAGAGGAAAGGGGACAAG
ATCCTCCTGAATGCCTGCTGCCCAGGGTGGGTGAGAACTGACATGGCGGGACCCAAGGCC
ACCAAGAGCCCAGAAGAAGGTGCAGAGACCCCTGTGTACTTGGCCCTTTTGCCCCCAGAT
GCTGAGGGTCCCCATGGACAATTTGTTTCAGAGAAGAGAGTTGAACAGTGGTGA
Enzyme 2 GenBank Gene ID AB003151 Link Image
Enzyme 2 GeneCard ID CBR3 Link Image
Enzyme 2 GenAtlas ID CBR3 Link Image
Enzyme 2 HGNC ID HGNC:1549 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 21q22.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Watanabe K, Sugawara C, Ono A, Fukuzumi Y, Itakura S, Yamazaki M, Tashiro H, Osoegawa K, Soeda E, Nomura T: Mapping of a novel human carbonyl reductase, CBR3, and ribosomal pseudogenes to human chromosome 21q22.2. Genomics. 1998 Aug 15;52(1):95-100. [PubMed Link Image]
  2. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [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]
  4. Miura T, Nishinaka T, Terada T: Different functions between human monomeric carbonyl reductase 3 and carbonyl reductase 1. Mol Cell Biochem. 2008 Aug;315(1-2):113-21. Epub 2008 May 21. [PubMed Link Image]
  5. Lakhman SS, Ghosh D, Blanco JG: Functional significance of a natural allelic variant of human carbonyl reductase 3 (CBR3). Drug Metab Dispos. 2005 Feb;33(2):254-7. Epub 2004 Nov 10. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5307
Enzyme 3 Name 15-hydroxyprostaglandin dehydrogenase [NAD+]
Enzyme 3 Synonyms
  1. 15-PGDH
  2. Prostaglandin dehydrogenase 1
Enzyme 3 Gene Name HPGD
Enzyme 3 Protein Sequence >15-hydroxyprostaglandin dehydrogenase [NAD+]
MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLF
IQCDVADQQQLRDTFRKVVDHFGRLDILVNNAGVNNEKNWEKTLQINLVSVISGTYLGLD
YMSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASKHGIVGFTRSAALAANLMNSGVRLNA
ICPGFVNTAILESIEKEENMGQYIEYKDHIKDMIKYYGILDPPLIANGLITLIEDDALNG
AIMKITTSKGIHFQDYDTTPFQAKTQ
Enzyme 3 Number of Residues 266
Enzyme 3 Molecular Weight 28977.1
Enzyme 3 Theoretical pI 5.65
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 3 General Function Involved in oxidoreductase activity
Enzyme 3 Specific Function Prostaglandin inactivation. Contributes to the regulation of events that are under the control of prostaglandin levels. Catalyzes the NAD-dependent dehydrogenation of lipoxin A4 to form 15-oxo-lipoxin A4. Inhibits in vivo proliferation of colon cancer cells
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • (5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+ = (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+ [RN:R02580]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 189054417 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P15428 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PGDH_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >801 bp
ATGCACGTGAACGGCAAAGTGGCGCTGGTGACCGGCGCGGCTCAGGGCATAGGCAGAGCC
TTTGCAGAGGCGCTGCTGCTTAAGGGCGCCAAGGTAGCGCTGGTGGATTGGAATCTTGAA
GCAGGTGTACAGTGTAAAGCTGCCCTGGATGAGCAGTTTGAACCTCAGAAGACTCTGTTC
ATCCAGTGCGATGTGGCTGACCAGCAACAACTGAGAGACACTTTTAGAAAAGTTGTAGAC
CACTTTGGAAGACTGGACATTTTGGTCAATAATGCTGGAGTGAATAATGAGAAAAACTGG
GAAAAAACTCTGCAAATTAATTTGGTTTCTGTTATCAGTGGAACCTATCTTGGTTTGGAT
TACATGAGTAAGCAAAATGGAGGTGAAGGCGGCATCATTATCAATATGTCATCTTTAGCA
GGACTCATGCCCGTTGCACAGCAGCCGGTTTATTGTGCTTCAAAGCATGGCATAGTTGGA
TTCACACGCTCAGCAGCGTTGGCTGCTAATCTTATGAACAGTGGTGTGAGACTGAATGCC
ATTTGTCCAGGCTTTGTTAACACAGCCATCCTTGAATCAATTGAAAAAGAAGAAAACATG
GGACAATATATAGAATATAAGGATCATATCAAGGATATGATTAAATACTATGGAATTTTG
GACCCACCATTGATTGCCAATGGATTGATAACACTCATTGAAGATGATGCTTTAAATGGT
GCTATTATGAAGATCACAACTTCTAAGGGAATTCATTTTCAAGACTATGATACAACTCCA
TTTCAAGCAAAAACCCAATGA
Enzyme 3 GenBank Gene ID AK314624 Link Image
Enzyme 3 GeneCard ID HPGD Link Image
Enzyme 3 GenAtlas ID HPGD Link Image
Enzyme 3 HGNC ID HGNC:5154 Link Image
Enzyme 3 Chromosome Location 4
Enzyme 3 Locus 4q34-q35
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Krook M, Marekov L, Jornvall H: Purification and structural characterization of placental NAD(+)-linked 15-hydroxyprostaglandin dehydrogenase. The primary structure reveals the enzyme to belong to the short-chain alcohol dehydrogenase family. Biochemistry. 1990 Jan 23;29(3):738-43. [PubMed Link Image]
  2. Ensor CM, Yang JY, Okita RT, Tai HH: Cloning and sequence analysis of the cDNA for human placental NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase. J Biol Chem. 1990 Sep 5;265(25):14888-91. [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. 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]
  5. Ensor CM, Tai HH: Site-directed mutagenesis of the conserved tyrosine 151 of human placental NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase yields a catalytically inactive enzyme. Biochem Biophys Res Commun. 1991 Apr 30;176(2):840-5. [PubMed Link Image]
  6. Clish CB, Levy BD, Chiang N, Tai HH, Serhan CN: Oxidoreductases in lipoxin A4 metabolic inactivation: a novel role for 15-onoprostaglandin 13-reductase/leukotriene B4 12-hydroxydehydrogenase in inflammation. J Biol Chem. 2000 Aug 18;275(33):25372-80. [PubMed Link Image]
  7. Patel FA, Funder JW, Challis JR: Mechanism of cortisol/progesterone antagonism in the regulation of 15-hydroxyprostaglandin dehydrogenase activity and messenger ribonucleic acid levels in human chorion and placental trophoblast cells at term. J Clin Endocrinol Metab. 2003 Jun;88(6):2922-33. [PubMed Link Image]
  8. Yan M, Rerko RM, Platzer P, Dawson D, Willis J, Tong M, Lawrence E, Lutterbaugh J, Lu S, Willson JK, Luo G, Hensold J, Tai HH, Wilson K, Markowitz SD: 15-Hydroxyprostaglandin dehydrogenase, a COX-2 oncogene antagonist, is a TGF-beta-induced suppressor of human gastrointestinal cancers. Proc Natl Acad Sci U S A. 2004 Dec 14;101(50):17468-73. Epub 2004 Dec 1. [PubMed Link Image]
  9. Cho H, Huang L, Hamza A, Gao D, Zhan CG, Tai HH: Role of glutamine 148 of human 15-hydroxyprostaglandin dehydrogenase in catalytic oxidation of prostaglandin E2. Bioorg Med Chem. 2006 Oct 1;14(19):6486-91. Epub 2006 Jul 7. [PubMed Link Image]
  10. Krook M, Ghosh D, Duax W, Jornvall H: Three-dimensional model of NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase and relationships to the NADP(+)-dependent enzyme (carbonyl reductase). FEBS Lett. 1993 May 10;322(2):139-42. [PubMed Link Image]
  11. Uppal S, Diggle CP, Carr IM, Fishwick CW, Ahmed M, Ibrahim GH, Helliwell PS, Latos-Bielenska A, Phillips SE, Markham AF, Bennett CP, Bonthron DT: Mutations in 15-hydroxyprostaglandin dehydrogenase cause primary hypertrophic osteoarthropathy. Nat Genet. 2008 Jun;40(6):789-93. Epub 2008 May 25. [PubMed Link Image]
  12. Tariq M, Azeem Z, Ali G, Chishti MS, Ahmad W: Mutation in the HPGD gene encoding NAD+ dependent 15-hydroxyprostaglandin dehydrogenase underlies isolated congenital nail clubbing (ICNC). J Med Genet. 2009 Jan;46(1):14-20. Epub 2008 Sep 19. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5308
Enzyme 4 Name Prostaglandin E synthase
Enzyme 4 Synonyms
  1. Microsomal glutathione S-transferase 1-like 1
  2. MGST1-L1
  3. p53-induced gene 12 protein
Enzyme 4 Gene Name PTGES
Enzyme 4 Protein Sequence >Prostaglandin E synthase
MPAHSLVMSSPALPAFLLCSTLLVIKMYVVAIITGQVRLRKKAFANPEDALRHGGPQYCR
SDPDVERCLRAHRNDMETIYPFLFLGFVYSFLGPNPFVAWMHFLVFLVGRVAHTVAYLGK
LRAPIRSVTYTLAQLPCASMALQILWEAARHL
Enzyme 4 Number of Residues 152
Enzyme 4 Molecular Weight 17102.1
Enzyme 4 Theoretical pI 9.77
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Involved in prostaglandin-E synthase activity
Enzyme 4 Specific Function (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15- hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11-alpha,15- dihydroxy-9-oxoprosta-5,13-dienoate
Enzyme 4 Pathways
Enzyme 4 Reactions
  • (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13- dienoate = (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate [RN:R02265]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 13-33 79-99
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 4758910 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O14684 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PTGES_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >459 bp
ATGCCTGCCCACAGCCTGGTGATGAGCAGCCCGGCCCTCCCGGCCTTCCTGCTCTGCAGC
ACGCTGCTGGTCATCAAGATGTACGTGGTGGCCATCATCACGGGCCAAGTGAGGCTGCGG
AAGAAGGCCTTTGCCAACCCCGAGGATGCCCTGAGACACGGAGGCCCCCAGTATTGCAGG
AGCGACCCCGACGTGGAACGCTGCCTCAGGGCCCACCGGAACGACATGGAGACCATCTAC
CCCTTCCTTTTCCTGGGCTTCGTCTACTCCTTTCTGGGTCCTAACCCTTTTGTCGCCTGG
ATGCACTTCCTGGTCTTCCTCGTGGGCCGTGTGGCACACACCGTGGCCTACCTGGGGAAG
CTGCGGGCACCCATCCGCTCCGTGACCTACACCCTGGCCCAGCTCCCCTGCGCCTCCATG
GCTCTGCAGATCCTCTGGGAAGCGGCCCGCCACCTGTGA
Enzyme 4 GenBank Gene ID NM_004878.4 Link Image
Enzyme 4 GeneCard ID PTGES Link Image
Enzyme 4 GenAtlas ID PTGES Link Image
Enzyme 4 HGNC ID HGNC:9599 Link Image
Enzyme 4 Chromosome Location 9
Enzyme 4 Locus 9q34.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Polyak K, Xia Y, Zweier JL, Kinzler KW, Vogelstein B: A model for p53-induced apoptosis. Nature. 1997 Sep 18;389(6648):300-5. [PubMed Link Image]
  2. Jakobsson PJ, Thoren S, Morgenstern R, Samuelsson B: Identification of human prostaglandin E synthase: a microsomal, glutathione-dependent, inducible enzyme, constituting a potential novel drug target. Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7220-5. [PubMed Link Image]
  3. Forsberg L, Leeb L, Thoren S, Morgenstern R, Jakobsson P: Human glutathione dependent prostaglandin E synthase: gene structure and regulation. FEBS Lett. 2000 Apr 7;471(1):78-82. [PubMed Link Image]
  4. 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]
  5. Ouellet M, Falgueyret JP, Ear PH, Pen A, Mancini JA, Riendeau D, Percival MD: Purification and characterization of recombinant microsomal prostaglandin E synthase-1. Protein Expr Purif. 2002 Dec;26(3):489-95. [PubMed Link Image]
  6. Thoren S, Weinander R, Saha S, Jegerschold C, Pettersson PL, Samuelsson B, Hebert H, Hamberg M, Morgenstern R, Jakobsson PJ: Human microsomal prostaglandin E synthase-1: purification, functional characterization, and projection structure determination. J Biol Chem. 2003 Jun 20;278(25):22199-209. Epub 2003 Apr 2. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5692
Enzyme 5 Name Solute carrier organic anion transporter family member 1B1
Enzyme 5 Synonyms
  1. Liver-specific organic anion transporter 1
  2. LST-1
  3. OATP-C
  4. Sodium-independent organic anion-transporting polypeptide 2
  5. OATP-2
  6. Solute carrier family 21 member 6
Enzyme 5 Gene Name SLCO1B1
Enzyme 5 Protein Sequence >Solute carrier organic anion transporter family member 1B1
MDQNQHLNKTAEAQPSENKKTRYCNGLKMFLAALSLSFIAKTLGAIIMKSSIIHIERRFE
ISSSLVGFIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCFIMGIGGVLTALPHFFMGY
YRYSKETNINSSENSTSTLSTCLINQILSLNRASPEIVGKGCLKESGSYMWIYVFMGNML
RGIGETPIVPLGLSYIDDFAKEGHSSLYLGILNAIAMIGPIIGFTLGSLFSKMYVDIGYV
DLSTIRITPTDSRWVGAWWLNFLVSGLFSIISSIPFFFLPQTPNKPQKERKASLSLHVLE
TNDEKDQTANLTNQGKNITKNVTGFFQSFKSILTNPLYVMFVLLTLLQVSSYIGAFTYVF
KYVEQQYGQPSSKANILLGVITIPIFASGMFLGGYIIKKFKLNTVGIAKFSCFTAVMSLS
FYLLYFFILCENKSVAGLTMTYDGNNPVTSHRDVPLSYCNSDCNCDESQWEPVCGNNGIT
YISPCLAGCKSSSGNKKPIVFYNCSCLEVTGLQNRNYSAHLGECPRDDACTRKFYFFVAI
QVLNLFFSALGGTSHVMLIVKIVQPELKSLALGFHSMVIRALGGILAPIYFGALIDTTCI
KWSTNNCGTRGSCRTYNSTSFSRVYLGLSSMLRVSSLVLYIILIYAMKKKYQEKDINASE
NGSVMDEANLESLNKNKHFVPSAGADSETHC
Enzyme 5 Number of Residues 691
Enzyme 5 Molecular Weight 76448.0
Enzyme 5 Theoretical pI 8.68
Enzyme 5 GO Classification
Function
  • transporter activity
Process
  • establishment of localization
  • transport
Component
  • cell part
  • membrane
Enzyme 5 General Function Involved in transporter activity
Enzyme 5 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 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 97-117 207-227 259-279 336-356 376-396 410-430 575-595
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 5006265 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q9Y6L6 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name SO1B1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2076 bp
ATGGACCAAAATCAACATTTGAATAAAACAGCAGAGGCACAACCTTCAGAGAATAAGAAA
ACAAGATACTGCAATGGATTGAAGATGTTCTTGGCAGCTCTGTCACTCAGCTTTATTGCT
AAGACACTAGGTGCAATTATTATGAAAAGTTCCATCATTCATATAGAACGGAGATTTGAG
ATATCCTCTTCTCTTGTTGGTTTTATTGACGGAAGCTTTGAAATTGGAAATTTGCTTGTG
ATTGTATTTGTGAGTTACTTTGGATCCAAACTACATAGACCAAAGTTAATTGGAATCGGT
TGTTTCATTATGGGAATTGGAGGTGTTTTGACTGCTTTGCCACATTTCTTCATGGGATAT
TACAGGTATTCTAAAGAAACTAATATCAATTCATCAGAAAATTCAACATCGACCTTATCC
ACTTGTTTAATTAATCAAATTTTATCACTCAATAGAGCATCACCTGAGATAGTGGGAAAA
GGTTGTTTAAAGGAATCTGGGTCATACATGTGGATATATGTGTTCATGGGTAATATGCTT
CGTGGAATAGGGGAGACTCCCATAGTACCACTGGGGCTTTCTTACATTGATGATTTCGCT
AAAGAAGGACATTCTTCTTTGTATTTAGGTATATTGAATGCAATAGCAATGATTGGTCCA
ATCATTGGCTTTACCCTGGGATCTCTGTTTTCTAAAATGTACGTGGATATTGGATATGTA
GATCTAAGCACTATCAGGATAACTCCTACTGATTCTCGATGGGTTGGAGCTTGGTGGCTT
AATTTCCTTGTGTCTGGACTATTCTCCATTATTTCTTCCATACCATTCTTTTTCTTGCCC
CAAACTCCAAATAAACCACAAAAAGAAAGAAAAGCTTCACTGTCTTTGCATGTGCTGGAA
ACAAATGATGAAAAGGATCAAACAGCTAATTTGACCAATCAAGGAAAAAATATTACCAAA
AATGTGACTGGTTTTTTCCAGTCTTTTAAAAGCATCCTTACTAATCCCCTGTATGTTATG
TTTGTGCTTTTGACGTTGTTACAAGTAAGCAGCTATATTGGTGCTTTTACTTATGTCTTC
AAATACGTAGAGCAACAGTATGGTCAGCCTTCATCTAAGGCTAACATCTTATTGGGAGTC
ATAACCATACCTATTTTTGCAAGTGGAATGTTTTTAGGAGGATATATCATTAAAAAATTC
AAACTGAACACCGTTGGAATTGCCAAATTCTCATGTTTTACTGCTGTGATGTCATTGTCC
TTTTACCTATTATATTTTTTCATACTCTGTGAAAACAAATCAGTTGCCGGACTAACCATG
ACCTATGATGGAAATAATCCAGTGACATCTCATAGAGATGTACCACTTTCTTATTGCAAC
TCAGACTGCAATTGTGATGAAAGTCAATGGGAACCAGTCTGTGGAAACAATGGAATAACT
TACATCTCACCCTGTCTAGCAGGTTGCAAATCTTCAAGTGGCAATAAAAAGCCTATAGTG
TTTTACAACTGCAGTTGTTTGGAAGTAACTGGTCTCCAGAACAGAAATTACTCAGCCCAT
TTGGGTGAATGCCCAAGAGATGATGCTTGTACAAGGAAATTTTACTTTTTTGTTGCAATA
CAAGTCTTGAATTTATTTTTCTCTGCACTTGGAGGCACCTCACATGTCATGCTGATTGTT
AAAATTGTTCAACCTGAATTGAAATCACTTGCACTGGGTTTCCACTCAATGGTTATACGA
GCACTAGGAGGAATTCTAGCTCCAATATATTTTGGGGCTCTGATTGATACAACGTGTATA
AAGTGGTCCACCAACAACTGTGGCACACGTGGGTCATGTAGGACATATAATTCCACATCA
TTTTCAAGGGTCTACTTGGGCTTGTCTTCAATGTTAAGAGTCTCATCACTTGTTTTATAT
ATTATATTAATTTATGCCATGAAGAAAAAATATCAAGAGAAAGATATCAATGCATCAGAA
AATGGAAGTGTCATGGATGAAGCAAACTTAGAATCCTTAAATAAAAATAAACATTTTGTC
CCTTCTGCTGGGGCAGATAGTGAAACACATTGTTAA
Enzyme 5 GenBank Gene ID AB026257 Link Image
Enzyme 5 GeneCard ID SLCO1B1 Link Image
Enzyme 5 GenAtlas ID SLCO1B1 Link Image
Enzyme 5 HGNC ID HGNC:10959 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 12p
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 7876
Enzyme 6 Name Prostaglandin E2 receptor EP1 subtype
Enzyme 6 Synonyms
  1. PGE receptor EP1 subtype
  2. PGE2 receptor EP1 subtype
  3. Prostanoid EP1 receptor
Enzyme 6 Gene Name PTGER1
Enzyme 6 Protein Sequence >Prostaglandin E2 receptor EP1 subtype
MSPCGPLNLSLAGEATTCAAPWVPNTSAVPPSGASPALPIFSMTLGAVSNLLALALLAQA
AGRLRRRRSAATFLLFVASLLATDLAGHVIPGALVLRLYTAGRAPAGGACHFLGGCMVFF
GLCPLLLGCGMAVERCVGVTRPLLHAARVSVARARLALAAVAAVALAVALLPLARVGRYE
LQYPGTWCFIGLGPPGGWRQALLAGLFASLGLVALLAALVCNTLSGLALLRARWRRRSRR
PPPASGPDSRRRWGAHGPRSASASSASSIASASTFFGGSRSSGSARRARAHDVEMVGQLV
GIMVVSCICWSPMLVLVALAVGGWSSTSLQRPLFLAVRLASWNQILDPWVYILLRQAVLR
QLLRLLPPRAGAKGGPAGLGLTPSAWEASSLRSSRHSGLSHF
Enzyme 6 Number of Residues 402
Enzyme 6 Molecular Weight 41800.7
Enzyme 6 Theoretical pI 12.22
Enzyme 6 GO Classification
Function
  • G-protein coupled receptor activity
  • icosanoid receptor activity
  • molecular transducer activity
  • prostaglandin E receptor activity
  • prostaglandin receptor activity
  • prostanoid receptor activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 6 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 6 Specific Function Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(q) proteins which activate a phosphatidylinositol-calcium second messenger system. May play a role as an important modulator of renal function. Implicated the smooth muscle contractile response to PGE2 in various tissues
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 36-62 73-96 112-133 156-177 202-227 295-321 333-354
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 30526194 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P34995 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PE2R1_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1209 bp
ATGAGCCCTTGCGGGCCCCTCAACCTGAGCCTGGCGGGCGAGGCGACCACATGCGCGGCG
CCCTGGGTCCCCAACACGTCGGCCGTGCCGCCGTCGGGCGCTTCGCCCGCGCTGCCCATC
TTCTCCATGACGCTGGGCGCCGTGTCCAACCTGCTGGCGCTGGCGCTGCTGGCGCAGGCC
GCGGGCCGCCTGCGACGCCGCCGCTCGGCCACCACCTTCCTGCTGTTCGTGGCCAGCCTG
CTGGCCACCGACCTGGCGGGCCACGTGATCCCGGGCGCGCTGGTGCTGCGTCTGTACACT
GCGGGGCGCGCTCCGGCCGGCGGGGCCTGCCACTTCCTGGGCGGCTGCATGGTCTTCTTC
GGCCTGTGCCCGCTGCTGCTGGGCTGTGGCATGGCCGTGGAGCGCTGCGTGGGCGTCACG
CGGCCGCTGCTCCACGCCGCGCGGGTCTCGGTCGCCCGCGCGCGCCTGGCGCTGGCCGCG
GTGGCCGCGGTGGCCTTGGCCGTGGCGCTGCTGCCGCTGGCGCGCGTGGGCCGCTATGAG
CTGCAGTACCCGGGCACGTGGTGCTTCATCGGCCTGGGTCCCCCGGGCGGCTGGCGCCAG
GCACTGCTTGCTGGCCTCTTCGCCAGCCTCGGCCTGGTCGCGCTCCTCGCCGCGCTGGTG
TGCAACACGCTCAGCGGCCTGGCCCTGCTACGCGCCCGCTGGCGACGCCGCTCCCGACGG
CCTCCCCCGGCCTCAGGCCCCGACAGCCGGCGTCGCTGGGGGGCGCACGGACCCCGCTCG
GCCTCCGCCTCGTCCGCCTCGTCCATCGCTTCGGCCTCCACCTTCTTTGGCGGCTCTCGG
AGCAGCGGCTCGGCACGCAGAGCTCGCGCCCACGACGTGGAGATGGTGGGCCAGCTTGTC
GGTATCATGGTGGTGTCGTGCATCTGCTGGAGCCCAATGCTGGTGTTGGTGGCGCTGGCC
GTCGGCGGCTGGAGCTCTACCTCCCTGCAGCGGCCACTGTTCCTGGCCGTGCGCCTTGCC
TCCTGGAACCAGATCCTGGACCCTTGGGTGTACATCCTACTGCGCCAGGCCGTGCTGCGC
CAACTGCTTCGCCTCTTGCCCCCGAGGGCCGGAGCCAAGGGCGGCCCCGCGGGGCTGGGC
CTAACACCGAGCGCCTGGGAGGCCAGCTCGCTGCGCAGCTCCCGGCACAGCGGCCTCAGC
CACTTCTAA
Enzyme 6 GenBank Gene ID AY275470 Link Image
Enzyme 6 GeneCard ID PTGER1 Link Image
Enzyme 6 GenAtlas ID PTGER1 Link Image
Enzyme 6 HGNC ID HGNC:9593 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 19p13.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Funk CD, Furci L, FitzGerald GA, Grygorczyk R, Rochette C, Bayne MA, Abramovitz M, Adam M, Metters KM: Cloning and expression of a cDNA for the human prostaglandin E receptor EP1 subtype. J Biol Chem. 1993 Dec 15;268(35):26767-72. [PubMed Link Image]
  2. 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 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 8295
Enzyme 7 Name Prostaglandin E2 receptor EP4 subtype
Enzyme 7 Synonyms
  1. PGE receptor EP4 subtype
  2. PGE2 receptor EP4 subtype
  3. Prostanoid EP4 receptor
Enzyme 7 Gene Name PTGER4
Enzyme 7 Protein Sequence >Prostaglandin E2 receptor EP4 subtype
MSTPGVNSSASLSPDRLNSPVTIPAVMFIFGVVGNLVAIVVLCKSRKEQKETTFYTLVCG
LAVTDLLGTLLVSPVTIATYMKGQWPGGQPLCEYSTFILLFFSLSGLSIICAMSVERYLA
INHAYFYSHYVDKRLAGLTLFAVYASNVLFCALPNMGLGSSRLQYPDTWCFIDWTTNVTA
HAAYSYMYAGFSSFLILATVLCNVLVCGALLRMHRQFMRRTSLGTEQHHAAAAASVASRG
HPAASPALPRLSDFRRRRSFRRIAGAEIQMVILLIATSLVVLICSIPLVVRVFVNQLYQP
SLEREVSKNPDLQAIRIASVNPILDPWIYILLRKTVLSKAIEKIKCLFCRIGGSRRERSG
QHCSDSQRTSSAMSGHSRSFISRELKEISSTSQTLLPDLSLPDLSENGLGGRNLLPGVPG
MGLAQEDTTSLRTLRISETSDSSQGQDSESVLLVDEAGGSGRAGPAPKGSSLQVTFPSET
LNLSEKCI
Enzyme 7 Number of Residues 488
Enzyme 7 Molecular Weight 53118.8
Enzyme 7 Theoretical pI 8.91
Enzyme 7 GO Classification
Function
  • G-protein coupled receptor activity
  • icosanoid receptor activity
  • molecular transducer activity
  • prostaglandin E receptor activity
  • prostaglandin receptor activity
  • prostanoid receptor activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 7 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 7 Specific Function Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. Has a relaxing effect on smooth muscle. May play an important role in regulating renal hemodynamics, intestinal epithelial transport, adrenal aldosterone secretion, and uterine function
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 20-43 56-79 97-115 136-160 185-211 268-295 313-332
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID P35408 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PE2R4_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1467 bp
ATGTCCACTCCCGGGGTCAATTCGTCCGCCTCCTTGAGCCCCGACCGGCTGAACAGCCCA
GTGACCATCCCGGCGGTGATGTTCATCTTCGGGGTGGTGGGCAACCTGGTGGCCATCGTG
GTGCTGTGCAAGTCGCGCAAGGAGCAGAAGGAGACGACCTTCTACACGCTGGTATGTGGG
CTGGCTGTCACCGACCTGTTGGGCACTTTGTTGGTGAGCCCGGTGACCATCGCCACGTAC
ATGAAGGGCCAATGGCCCGGGGGCCAGCCGCTGTGCGAGTACAGCACCTTCATTCTGCTC
TTCTTCAGCCTGTCCGGCCTCAGCATCATCTGCGCCATGAGTGTCGAGCGCTACCTGGCC
ATCAACCATGCCTATTTCTACAGCCACTACGTGGACAAGCGATTGGCGGGCCTCACGCTC
TTTGCAGTCTATGCGTCCAACGTGCTCTTTTGCGCGCTGCCCAACATGGGTCTCGGTAGC
TCGCGGCTGCAGTACCCAGACACCTGGTGCTTCATCGACTGGACCACCAACGTGACGGCG
CACGCCGCCTACTCCTACATGTACGCGGGCTTCAGCTCCTTCCTCATTCTCGCCACCGTC
CTCTGCAACGTGCTTGTGTGCGGCGCGCTGCTCCGCATGCACCGCCAGTTCATGCGCCGC
ACCTCGCTGGGCACCGAGCAGCACCACGCGGCCGCGGCCGCCTCGGTTGCCTCCCGGGGC
CACCCCGCTGCCTCCCCAGCCTTGCCGCGCCTCAGCGACTTTCGGCGCCGCCGGAGCTTC
CGCCGCATCGCGGGCGCCGAGATCCAGATGGTCATCTTACTCATTGCCACCTCCCTGGTG
GTGCTCATCTGCTCCATCCCGCTCGTGGTGCGAGTATTCGTCAACCAGTTATATCAGCCA
AGTTTGGAGCGAGAAGTCAGTAAAAATCCAGATTTGCAGGCCATCCGAATTGCTTCTGTG
AACCCCATCCTAGACCCCTGGATATATATCCTCCTGAGAAAGACAGTGCTCAGTAAAGCA
ATAGAGAAGATCAAATGCCTCTTCTGCCGCATTGGCGGGTCCCGCAGGGAGCGCTCCGGA
CAGCACTGCTCAGACAGTCAAAGGACATCTTCTGCCATGTCAGGCCACTCTCGCTCCTTC
ATCTCCCGGGAGCTGAAGGAGATCAGCAGTACATCTCAGACCCTCCTGCCAGACCTCTCA
CTGCCAGACCTCAGTGAAAATGGCCTTGGAGGCAGGAATTTGCTTCCAGGTGTGCCTGGC
ATGGGCCTGGCCCAGGAAGACACCACCTCACTGAGGACTTTGCGAATATCAGAGACCTCA
GACTCTTCACAGGGTCAGGACTCAGAGAGTGTCTTACTGGTGGATGAGGCTGGTGGGAGC
GGCAGGGCTGGGCCTGCCCCTAAGGGGAGCTCCCTGCAAGTCACATTTCCCAGTGAAACA
CTGAACTTATCAGAAAAATGTATATAA
Enzyme 7 GenBank Gene ID L28175 Link Image
Enzyme 7 GeneCard ID PTGER4 Link Image
Enzyme 7 GenAtlas ID PTGER4 Link Image
Enzyme 7 HGNC ID HGNC:9596 Link Image
Enzyme 7 Chromosome Location 5
Enzyme 7 Locus 5p13.1
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Bastien L, Sawyer N, Grygorczyk R, Metters KM, Adam M: Cloning, functional expression, and characterization of the human prostaglandin E2 receptor EP2 subtype. J Biol Chem. 1994 Apr 22;269(16):11873-7. [PubMed Link Image]
  2. An S, Yang J, Xia M, Goetzl EJ: Cloning and expression of the EP2 subtype of human receptors for prostaglandin E2. Biochem Biophys Res Commun. 1993 Nov 30;197(1):263-70. [PubMed Link Image]
  3. Foord SM, Marks B, Stolz M, Bufflier E, Fraser NJ, Lee MG: The structure of the prostaglandin EP4 receptor gene and related pseudogenes. Genomics. 1996 Jul 1;35(1):182-8. [PubMed Link Image]
  4. Mori K, Tanaka I, Kotani M, Miyaoka F, Sando T, Muro S, Sasaki Y, Nakagawa O, Ogawa Y, Usui T, Ozaki S, Ichikawa A, Narumiya S, Nakao K: Gene expression of the human prostaglandin E receptor EP4 subtype: differential regulation in monocytoid and lymphoid lineage cells by phorbol ester. J Mol Med. 1996 Jun;74(6):333-6. [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. Takayama K, Sukhova GK, Chin MT, Libby P: A novel prostaglandin E receptor 4-associated protein participates in antiinflammatory signaling. Circ Res. 2006 Mar 3;98(4):499-504. Epub 2006 Jan 19. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 11165
Enzyme 8 Name Prostaglandin E synthase 2
Enzyme 8 Synonyms
  1. Microsomal prostaglandin E synthase 2
  2. mPGES-2
  3. Prostaglandin E synthase 2 truncated form
Enzyme 8 Gene Name PTGES2
Enzyme 8 Protein Sequence >Prostaglandin E synthase 2
MDPAARVVRALWPGGCALAWRLGGRPQPLLPTQSRAGFAGAAGGPSPVAAARKGSPRLLG
AAALALGGALGLYHTARWHLRAQDLHAERSAAQLSLSSRLQLTLYQYKTCPFCSKVRAFL
DFHALPYQVVEVNPVRRAEIKFSSYRKVPILVAQEGESSQQLNDSSVIISALKTYLVSGQ
PLEEIITYYPAMKAVNEQGKEVTEFGNKYWLMLNEKEAQQVYGGKEARTEEMKWRQWADD
WLVHLISPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQ
DNVREDLYEAADKWVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQ
PWYLRVERAITEASPAH
Enzyme 8 Number of Residues 377
Enzyme 8 Molecular Weight 41942.8
Enzyme 8 Theoretical pI 9.50
Enzyme 8 GO Classification
Function
  • catalytic activity
  • disulfide oxidoreductase activity
  • electron carrier activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on a sulfur group of donors
  • protein disulfide oxidoreductase activity
Process
  • cell redox homeostasis
  • cellular homeostasis
  • cellular process
Component
Enzyme 8 General Function Involved in electron carrier activity
Enzyme 8 Specific Function Isomerase that catalyzes the conversion of unstable intermediate of prostaglandin E2 H2 (PGH2) into the more stable prostaglandin E2 (PGE2) form. May also have transactivation activity toward IFN-gamma (IFNG), possibly via an interaction with CEBPB; however, the relevance of transcription activation activity remains unclear
Enzyme 8 Pathways
Enzyme 8 Reactions
  • (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13- dienoate = (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate [RN:R02265]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 58-74
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 10436397 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9H7Z7 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PGES2_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1134 bp
ATGGACCCGGCTGCGCGGGTGGTGCGGGCGCTGTGGCCTGGTGGGTGCGCCTTGGCCTGG
AGGCTGGGAGGCCGCCCCCAGCCGCTGCTACCCACGCAGAGCCGGGCTGGCTTCGCGGGG
GCGGCGGGCGGCCCGAGCCCCGTGGCTGCAGCTCGTAAGGGGAGCCCGCGGCTGCTGGGA
GCTGCGGCGCTGGCCCTGGGGGGAGCCCTGGGGCTGTACCACACGGCGCGGTGGCACCTG
CGCGCCCAGGACCTCCACGCAGAGCGCTCAGCCGCGCAGCTCTCCCTGTCCAGCCGCCTG
CAGCTGACCCTGTACCAGTACAAGACGTGTCCCTTCTGCAGCAAGGTCCGAGCCTTCCTC
GACTTCCATGCCCTGCCCTACCAGGTGGTGGAGGTGAACCCTGTGCGCAGGGCTGAGATC
AAGTTCTCCTCCTACAGAAAGGTGCCCATCCTGGTGGCCCAGGAAGGAGAAAGCTCGCAA
CAACTAAATGACTCCTCTGTCATCATCAGCGCCCTCAAGACCTACCTGGTGTCGGGGCAG
CCCCTGGAAGAGATCATCACCTACTACCCAGCCATGAAGGCTGTGAACGAGCAGGGCAAG
GAGGTGACCGAGTTCGGCAATAAGTACTGGCTCATGCTCAACGAGAAGGAGGCCCAGCAA
GTGTATGGTGGGAAGGAGGCCAGGACGGAGGAGATGAAGTGGCGGCAGTGGGCGGACGAC
TGGCTGGTGCACCTGATCTCCCCCAATGTGTACCGCACGCCCACCGAGGCTCTGGCGTCC
TTTGACTACATTGTCCGCGAGGGCAAGTTCGGAGCCGTGGAGGGTGCCGTGGCCAAGTAC
ATGGGTGCAGCGGCCATGTACCTCATCAGCAAGCGACTCAAGAGCAGGCACCGCCTCCAG
GACAACGTGCGCGAGGACCTCTATGAGGCTGCTGACAAGTGGGTGGCTGCTGTGGGCAAG
GACCGGCCCTTCATGGGGGGCCAGAAGCCGAATCTCGCTGATTTGGCGGTGTATGGCGTG
CTGCGTGTGATGGAGGGGCTGGATGCATTCGATGACCTGATGCAGCACACGCACATCCAG
CCCTGGTACCTGCGGGTGGAGAGGGCCATCACCGAGGCCTCCCCAGCGCACTGA
Enzyme 8 GenBank Gene ID AK024100 Link Image
Enzyme 8 GeneCard ID PTGES2 Link Image
Enzyme 8 GenAtlas ID PTGES2 Link Image
Enzyme 8 HGNC ID HGNC:17822 Link Image
Enzyme 8 Chromosome Location 9
Enzyme 8 Locus 9q34.11
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. 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]
  2. 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]
  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]
  4. Tanikawa N, Ohmiya Y, Ohkubo H, Hashimoto K, Kangawa K, Kojima M, Ito S, Watanabe K: Identification and characterization of a novel type of membrane-associated prostaglandin E synthase. Biochem Biophys Res Commun. 2002 Mar 8;291(4):884-9. [PubMed Link Image]
  5. Watanabe K, Ohkubo H, Niwa H, Tanikawa N, Koda N, Ito S, Ohmiya Y: Essential 110Cys in active site of membrane-associated prostaglandin E synthase-2. Biochem Biophys Res Commun. 2003 Jun 27;306(2):577-81. [PubMed Link Image]
  6. Murakami M, Nakashima K, Kamei D, Masuda S, Ishikawa Y, Ishii T, Ohmiya Y, Watanabe K, Kudo I: Cellular prostaglandin E2 production by membrane-bound prostaglandin E synthase-2 via both cyclooxygenases-1 and -2. J Biol Chem. 2003 Sep 26;278(39):37937-47. Epub 2003 Jun 30. [PubMed Link Image]
  7. Lehner B, Sanderson CM: A protein interaction framework for human mRNA degradation. Genome Res. 2004 Jul;14(7):1315-23. [PubMed Link Image]
  8. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 12989
Enzyme 9 Name cDNA, FLJ95780, Homo sapiens carbonyl reductase 1 (CBR1), mRNA (Carbonyl reductase 1, isoform CRA_d)
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name CBR1
Enzyme 9 Protein Sequence >cDNA, FLJ95780, Homo sapiens carbonyl reductase 1 (CBR1)
MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFH
QLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRD
VCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTK
KGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKA
TKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW
Enzyme 9 Number of Residues 277
Enzyme 9 Molecular Weight 30375
Enzyme 9 Theoretical pI Not Available
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function Not Available
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID B2RBZ7 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name B2RBZ7_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID Not Available
Enzyme 9 GeneCard ID B2RBZ7 Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 13649
Enzyme 10 Name Prostaglandin E2 receptor EP3 subtype
Enzyme 10 Synonyms
  1. PGE receptor EP3 subtype
  2. PGE2 receptor EP3 subtype
  3. PGE2-R
  4. Prostanoid EP3 receptor
Enzyme 10 Gene Name PTGER3
Enzyme 10 Protein Sequence >Prostaglandin E2 receptor EP3 subtype
MKETRGYGGDAPFCTRLNHSYTGMWAPERSAEARGNLTRPPGSGEDCGSVSVAFPITMLL
TGFVGNALAMLLVSRSYRRRESKRKKSFLLCIGWLALTDLVGQLLTTPVVIVVYLSKQRW
EHIDPSGRLCTFFGLTMTVFGLSSLFIASAMAVERALAIRAPHWYASHMKTRATRAVLLG
VWLAVLAFALLPVLGVGQYTVQWPGTWCFISTGRGGNGTSSSHNWGNLFFASAFAFLGLL
ALTVTFSCNLATIKALVSRCRAKATASQSSAQWGRITTETAIQLMGIMCVLSVCWSPLLI
MMLKMIFNQTSVEHCKTHTEKQKECNFFLIAVRLASLNQILDPWVYLLLRKILLRKFCQI
RYHTNNYASSSTSLPCQCSSTLMWSDHLER
Enzyme 10 Number of Residues 390
Enzyme 10 Molecular Weight 43309.3
Enzyme 10 Theoretical pI 10.05
Enzyme 10 GO Classification
Function
  • G-protein coupled receptor activity
  • icosanoid receptor activity
  • molecular transducer activity
  • prostaglandin E receptor activity
  • prostaglandin receptor activity
  • prostanoid receptor activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 10 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 10 Specific Function Receptor for prostaglandin E2 (PGE2); the EP3 receptor may be involved in inhibition of gastric acid secretion, modulation of neurotransmitter release in central and peripheral neurons, inhibition of sodium and water reabsorption in kidney tubulus and contraction in uterine smooth muscle. The activity of this receptor can couple to both the inhibition of adenylate cyclase mediated by G-I proteins, and to an elevation of intracellular calcium. The various isoforms have identical ligand binding properties but can interact with different second messenger systems
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • 54-78 92-112 132-153 176-197 228-253 284-307 328-349
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 186659506 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P43115 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PE2R3_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1173 bp
ATGAAGGAGACCCGGGGCTACGGAGGGGATGCCCCCTTCTGCACCCGCCTCAACCACTCC
TACACAGGCATGTGGGCGCCCGAGCGTTCCGCCGAGGCGCGGGGCAACCTCACGCGCCCT
CCAGGGTCTGGCGAGGATTGCGGATCGGTGTCCGTGGCCTTCCCGATCACCATGCTGCTC
ACTGGTTTCGTGGGCAACGCACTGGCCATGCTGCTCGTGTCGCGCAGCTACCGGCGCCGG
GAGAGCAAGCGCAAGAAGTCCTTCCTGCTGTGCATCGGCTGGCTGGCGCTCACCGACCTG
GTCGGGCAGCTTCTCACCACCCCGGTCGTCATCGTCGTGTACCTGTCCAAGCAGCGTTGG
GAGCACATCGACCCGTCGGGGCGGCTCTGCACCTTTTTCGGGCTGACCATGACTGTTTTC
GGGCTCTCCTCGTTGTTCATCGCCAGCGCCATGGCCGTCGAGCGGGCGCTGGCCATCAGG
GCGCCGCACTGGTATGCGAGCCACATGAAGACGCGTGCCACCCGCGCTGTGCTGCTCGGC
GTGTGGCTGGCCGTGCTCGCCTTCGCCCTGCTGCCGGTGCTGGGCGTGGGCCAGTACACC
GTCCAGTGGCCCGGGACGTGGTGCTTCATCAGCACCGGGCGAGGGGGCAACGGGACTAGC
TCTTCGCATAACTGGGGCAACCTTTTCTTCGCCTCTGCCTTTGCCTTCCTGGGGCTCTTG
GCGCTGACAGTCACCTTTTCCTGCAACCTGGCCACCATTAAGGCCCTGGTGTCCCGCTGC
CGGGCCAAGGCCACGGCATCTCAGTCCAGTGCCCAGTGGGGCCGCATCACGACCGAGACG
GCCATTCAGCTTATGGGGATCATGTGCGTGCTGTCGGTCTGCTGGTCTCCGCTCCTGATA
ATGATGTTGAAAATGATCTTCAATCAGACATCAGTTGAGCACTGCAAGACACACACGGAG
AAGCAGAAAGAATGCAACTTCTTCTTAATAGCTGTTCGCCTGGCTTCACTGAACCAGATC
TTGGATCCTTGGGTTTACCTGCTGTTAAGAAAGATCCTTCTTCGAAAGTTTTGCCAGATC
AGGTACCACACAAACAACTATGCATCCAGCTCCACCTCCTTACCCTGCCAGTGTTCCTCA
ACCTTGATGTGGAGCGACCATTTGGAAAGATGA
Enzyme 10 GenBank Gene ID NM_001126044.1 Link Image
Enzyme 10 GeneCard ID PTGER3 Link Image
Enzyme 10 GenAtlas ID PTGER3 Link Image
Enzyme 10 HGNC ID HGNC:9595 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 1p31.2
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Adam M, Boie Y, Rushmore TH, Muller G, Bastien L, McKee KT, Metters KM, Abramovitz M: Cloning and expression of three isoforms of the human EP3 prostanoid receptor. FEBS Lett. 1994 Jan 31;338(2):170-4. [PubMed Link Image]
  2. Schmid A, Thierauch KH, Schleuning WD, Dinter H: Splice variants of the human EP3 receptor for prostaglandin E2. Eur J Biochem. 1995 Feb 15;228(1):23-30. [PubMed Link Image]
  3. Yang J, Xia M, Goetzl EJ, An S: Cloning and expression of the EP3-subtype of human receptors for prostaglandin E2. Biochem Biophys Res Commun. 1994 Feb 15;198(3):999-1006. [PubMed Link Image]
  4. Kunapuli SP, Fen Mao G, Bastepe M, Liu-Chen LY, Li S, Cheung PP, DeRiel JK, Ashby B: Cloning and expression of a prostaglandin E receptor EP3 subtype from human erythroleukaemia cells. Biochem J. 1994 Mar 1;298 ( Pt 2):263-7. [PubMed Link Image]
  5. An S, Yang J, So SW, Zeng L, Goetzl EJ: Isoforms of the EP3 subtype of human prostaglandin E2 receptor transduce both intracellular calcium and cAMP signals. Biochemistry. 1994 Dec 6;33(48):14496-502. [PubMed Link Image]
  6. Kotani M, Tanaka I, Ogawa Y, Usui T, Mori K, Ichikawa A, Narumiya S, Yoshimi T, Nakao K: Molecular cloning and expression of multiple isoforms of human prostaglandin E receptor EP3 subtype generated by alternative messenger RNA splicing: multiple second messenger systems and tissue-specific distributions. Mol Pharmacol. 1995 Nov;48(5):869-79. [PubMed Link Image]
  7. Regan JW, Bailey TJ, Donello JE, Pierce KL, Pepperl DJ, Zhang D, Kedzie KM, Fairbairn CE, Bogardus AM, Woodward DF, et al.: Molecular cloning and expression of human EP3 receptors: evidence of three variants with differing carboxyl termini. Br J Pharmacol. 1994 Jun;112(2):377-85. [PubMed Link Image]
  8. Kotani M, Tanaka I, Ogawa Y, Usui T, Tamura N, Mori K, Narumiya S, Yoshimi T, Nakao K: Structural organization of the human prostaglandin EP3 receptor subtype gene (PTGER3). Genomics. 1997 Mar 15;40(3):425-34. [PubMed Link Image]
  9. 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]
  10. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [PubMed Link Image]
  11. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  12. 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]
  13. Kotelevets L, Foudi N, Louedec L, Couvelard A, Chastre E, Norel X: A new mRNA splice variant coding for the human EP3-I receptor isoform. Prostaglandins Leukot Essent Fatty Acids. 2007 Oct-Nov;77(3-4):195-201. Epub 2007 Nov 19. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 13867
Enzyme 11 Name Prostaglandin E2 receptor EP2 subtype
Enzyme 11 Synonyms
  1. PGE receptor EP2 subtype
  2. PGE2 receptor EP2 subtype
  3. Prostanoid EP2 receptor
Enzyme 11 Gene Name PTGER2
Enzyme 11 Protein Sequence >Prostaglandin E2 receptor EP2 subtype
MGNASNDSQSEDCETRQWLPPGESPAISSVMFSAGVLGNLIALALLARRWRGDVGCSAGR
RSSLSLFHVLVTELVFTDLLGTCLISPVVLASYARNQTLVALAPESRACTYFAFAMTFFS
LATMLMLFAMALERYLSIGHPYFYQRRVSRSGGLAVLPVIYAVSLLFCSLPLLDYGQYVQ
YCPGTWCFIRHGRTAYLQLYATLLLLLIVSVLACNFSVILNLIRMHRRSRRSRCGPSLGS
GRGGPGARRRGERVSMAEETDHLILLAIMTITFAVCSLPFTIFAYMNETSSRKEKWDLQA
LRFLSINSIIDPWVFAILRPPVLRLMRSVLCCRISLRTQDATQTSCSTQSDASKQADL
Enzyme 11 Number of Residues 358
Enzyme 11 Molecular Weight 39759.9
Enzyme 11 Theoretical pI 9.19
Enzyme 11 GO Classification
Function
  • G-protein coupled receptor activity
  • icosanoid receptor activity
  • molecular transducer activity
  • prostaglandin E receptor activity
  • prostaglandin receptor activity
  • prostanoid receptor activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 11 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 11 Specific Function Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. The subsequent raise in intracellular cAMP is responsible for the relaxing effect of this receptor on smooth muscle
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • 24-47 66-91 112-132 152-176 199-223 263-286 300-323
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 5524235 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P43116 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name PE2R2_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1077 bp
ATGGGCAATGCCTCCAATGACTCCCAGTCTGAGGACTGCGAGACGCGACAGTGGCTTCCC
CCAGGCGAAAGCCCAGCCATCAGCTCCGTCATGTTCTCGGCCGGGGTGCTGGGGAACCTC
ATAGCACTGGCGCTGCTGGCGCGCCGCTGGCGGGGGGACGTGGGGTGCAGCGCCGGCCGC
AGGAGCTCCCTCTCCTTGTTCCACGTGCTGGTGACCGAGCTGGTGTTCACCGACCTGCTC
GGGACCTGCCTCATCAGCCCAGTGGTACTGGCTTCGTACGCGCGGAACCAGACCCTGGTG
GCACTGGCGCCCGAGAGCCGCGCGTGCACCTACTTCGCTTTCGCCATGACCTTCTTCAGC
CTGGCCACGATGCTCATGCTCTTCGCCATGGCCCTGGAGCGCTACCTCTCGATCGGGCAC
CCCTACTTCTACCAGCGCCGCGTCTCGGCCTCCGGGGGCCTGGCCGTGCTGCCTGTCATC
TATGCAGTCTCCCTGCTCTTCTGCTCGCTGCCGCTGCTGGACTATGGGCAGTACGTCCAG
TACTGCCCCGGGACCTGGTGCTTCATCCGGCACGGGCGGACCGCTTACCTGCAGCTGTAC
GCCACCCTGCTGCTGCTTCTCATTGTCTCGGTGCTCGCCTGCAACTTCAGTGTCATTCTC
AACCTCATCCGCATGCACCGCCGAAGCCGGAGAAGCCGCTGCGGACCTTCCCTGGGCAGT
GGCCGGGGCGGCCCCGGGGCCCGCAGGAGAGGGGAAAGGGTGTCCATGGCGGAGGAGACG
GACCACCTCATTCTCCTGGCTATCATGACCATCACCTTCGCCGTCTGCTCCTTGCCTTTC
ACGATTTTTGCATATATGAATGAAACCTCTTCCCGAAAGGAAAAATGGGACCTCCAAGCT
CTTAGGTTTTTATCAATTAATTCAATAATTGACCCTTGGGTCTTTGCCATCCTTAGGCCT
CCTGTTCTGAGACTAATGCGTTCAGTCCTCTGTTGTCGGATTTCATTAAGAACACAAGAT
GCAACACAAACTTCCTGTTCTACACAGTCAGATGCCAGTAAACAGGCTGACCTTTGA
Enzyme 11 GenBank Gene ID AF134202 Link Image
Enzyme 11 GeneCard ID PTGER2 Link Image
Enzyme 11 GenAtlas ID PTGER2 Link Image
Enzyme 11 HGNC ID HGNC:9594 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 14q22
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Regan JW, Bailey TJ, Pepperl DJ, Pierce KL, Bogardus AM, Donello JE, Fairbairn CE, Kedzie KM, Woodward DF, Gil DW: Cloning of a novel human prostaglandin receptor with characteristics of the pharmacologically defined EP2 subtype. Mol Pharmacol. 1994 Aug;46(2):213-20. [PubMed Link Image]
  2. Smock SL, Pan LC, Castleberry TA, Lu B, Mather RJ, Owen TA: Cloning, structural characterization, and chromosomal localization of the gene encoding the human prostaglandin E(2) receptor EP2 subtype. Gene. 1999 Sep 17;237(2):393-402. [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 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 14810
Enzyme 12 Name Solute carrier family 22 member 7
Enzyme 12 Synonyms
  1. Novel liver transporter
  2. Organic anion transporter 2
  3. hOAT2
Enzyme 12 Gene Name SLC22A7
Enzyme 12 Protein Sequence >Solute carrier family 22 member 7
MGFEELLEQVGGFGPFQLRNVALLALPRVLLPLHFLLPIFLAAVPAHRCALPGAPANFSH
QDVWLEAHLPREPDGTLSSCLRFAYPQALPNTTLGEERQSRGELEDEPATVPCSQGWEYD
HSEFSSTIATESQWDLVCEQKGLNRAASTFFFAGVLVGAVAFGYLSDRFGRRRLLLVAYV
STLVLGLASAASVSYVMFAITRTLTGSALAGFTIIVMPLELEWLDVEHRTVAGVLSSTFW
TGGVMLLALVGYLIRDWRWLLLAVTLPCAPGILSLWWVPESARWLLTQGHVKEAHRYLLH
CARLNGRPVCEDSFSQEAVSKVAAGERVVRRPSYLDLFRTPRLRHISLCCVVVWFGVNFS
YYGLSLDVSGLGLNVYQTQLLFGAVELPSKLLVYLSVRYAGRRLTQAGTLLGTALAFGTR
LLVSSDMKSWSTVLAVMGKAFSEAAFTTAYLFTSELYPTVLRQTGMGLTALVGRLGGSLA
PLAALLDGVWLSLPKLTYGGIALLAAGTALLLPETRQAQLPETIQDVERKSAPTSLQEEE
MPMKQVQN
Enzyme 12 Number of Residues 548
Enzyme 12 Molecular Weight 60025.0
Enzyme 12 Theoretical pI 7.03
Enzyme 12 GO Classification
Function
  • ion transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 12 General Function Involved in transmembrane transport
Enzyme 12 Specific Function Mediates sodium-independent multispecific organic anion transport. Transport of prostaglandin E2, prostaglandin F2, tetracycline, bumetanide, estrone sulfate, glutarate, dehydroepiandrosterone sulfate, allopurinol, 5-fluorouracil, paclitaxel, L-ascorbic acid, salicylate, ethotrexate, and alpha- ketoglutarate
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • 21-41 146-166 180-200 204-224 234-254 259-279 346-366 376-397 404-423 432-452 466-486 493-513
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID Q9Y694 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name S22A7_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1647 bp
ATGGGCTTTGAGGAGCTGCTGGAGCAGGTGGGCGGCTTTGGGCCCTTCCAACTGCGGAAT
GTGGCACTGCTGGCCCTGCCCCGAGTGCTGCTACCACTGCACTTCCTCCTGCCCATCTTC
CTGGCTGCCGTGCCTGCCCACCGATGTGCCCTGCCGGGTGCCCCTGCCAACTTCAGCCAT
CAGGATGTGTGGCTGGAGGCCCATCTTCCCCGGGAGCCTGATGGCACGCTCAGCTCCTGC
CTCCGCTTTGCCTATCCCCAGGCTCTCCCCAACACCACGTTGGGGGAAGAAAGGCAGAGC
CGTGGGGAGCTGGAGGATGAACCTGCCACAGTGCCCTGCTCTCAGGGCTGGGAGTACGAC
CACTCAGAATTCTCCTCTACCATTGCAACTGAGTCCCAGTGGGATCTGGTGTGTGAGCAG
AAAGGTCTGAACAGAGCTGCGTCCACTTTCTTCTTCGCCGGTGTGCTGGTGGGGGCTGTG
GCCTTTGGATATCTGTCCGACAGGTTTGGGCGGCGGCGTCTGCTGCTGGTAGCCTACGTG
AGTACCCTGGTGCTGGGCCTGGCATCTGCAGCCTCCGTCAGCTATGTAATGTTTGCCATC
ACCCGCACCCTTACTGGCTCAGCCCTGGCTGGTTTTACCATCATCGTGATGCCACTGGAG
CTGGAGTGGCTGGATGTGGAGCACCGCACCGTGGCTGGAGTCCTGAGCAGCACCTTCTGG
ACAGGGGGCGTGATGCTGCTGGCACTGGTTGGGTACCTGATACGGGACTGGCGATGGCTT
CTGCTAGCTGTCACCCTGCCTTGTGCCCCAGGCATCCTCAGCCTCTGGTGGGTGCCTGAG
TCTGCACGCTGGCTTCTGACCCAAGGCCATGTGAAAGAGGCCCACAGGTACTTGCTCCAC
TGTGCCAGGCTCAATGGGCGGCCAGTGTGTGAGGACAGCTTCAGCCAGGAGGCTGTGAGC
AAAGTGGCCGCCGGGGAACGGGTGGTCCGAAGACCTTCATACCTAGACCTGTTCCGCACA
CCACGGCTCCGACACATCTCACTGTGCTGCGTGGTGGTGTGGTTCGGAGTGAACTTCTCC
TATTACGGCCTGAGTCTGGATGTGTCGGGGCTGGGGCTGAACGTGTACCAGACACAGCTG
TTGTTCGGGGCTGTGGAACTGCCCTCCAAGCTGCTGGTCTACTTGTCGGTGCGCTACGCA
GGACGCCGCCTCACGCAAGCCGGGACACTGCTGGGCACGGCCCTGGCGTTCGGCACTAGA
CTGCTAGTGTCCTCCGATATGAAGTCCTGGAGCACTGTCCTGGCAGTGATGGGGAAAGCT
TTTTCTGAAGCTGCCTTCACCACTGCTTACCTGTTCACTTCAGAGTTGTACCCTACGGTG
CTCAGACAGACAGGGATGGGGCTGACTGCACTGGTGGGCCGGCTGGGGGGCTCTTTGGCC
CCACTGGCGGCCTTGCTAGATGGAGTGTGGCTGTCACTGCCCAAGCTTACTTATGGGGGG
ATCGCCCTGCTGGCTGCCGGCACCGCCCTCCTGCTGCCAGAGACGAGGCAGGCACAGCTG
CCAGAGACCATCCAGGACGTGGAGAGAAAGAGTGCCCCAACCAGTCTTCAGGAGGAAGAG
ATGCCCATGAAGCAGGTCCAGAACTAA
Enzyme 12 GenBank Gene ID AF097518 Link Image
Enzyme 12 GeneCard ID SLC22A7 Link Image
Enzyme 12 GenAtlas ID SLC22A7 Link Image
Enzyme 12 HGNC ID HGNC:10971 Link Image
Enzyme 12 Chromosome Location 6
Enzyme 12 Locus 6p21.1
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. 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]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [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]
  4. Sun W, Wu RR, van Poelje PD, Erion MD: Isolation of a family of organic anion transporters from human liver and kidney. Biochem Biophys Res Commun. 2001 May 4;283(2):417-22. [PubMed Link Image]
  5. Enomoto A, Takeda M, Shimoda M, Narikawa S, Kobayashi Y, Kobayashi Y, Yamamoto T, Sekine T, Cha SH, Niwa T, Endou H: Interaction of human organic anion transporters 2 and 4 with organic anion transport inhibitors. J Pharmacol Exp Ther. 2002 Jun;301(3):797-802. [PubMed Link Image]
  6. Kimura H, Takeda M, Narikawa S, Enomoto A, Ichida K, Endou H: Human organic anion transporters and human organic cation transporters mediate renal transport of prostaglandins. J Pharmacol Exp Ther. 2002 Apr;301(1):293-8. [PubMed Link Image]
  7. Babu E, Takeda M, Narikawa S, Kobayashi Y, Yamamoto T, Cha SH, Sekine T, Sakthisekaran D, Endou H: Human organic anion transporters mediate the transport of tetracycline. Jpn J Pharmacol. 2002 Jan;88(1):69-76. [PubMed Link Image]
  8. Kobayashi Y, Ohshiro N, Sakai R, Ohbayashi M, Kohyama N, Yamamoto T: Transport mechanism and substrate specificity of human organic anion transporter 2 (hOat2 [SLC22A7]). J Pharm Pharmacol. 2005 May;57(5):573-8. [PubMed Link Image]
  9. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 16494
Enzyme 13 Name cDNA FLJ32487 fis, clone SKNSH1000002, highly similar to Prostaglandin E synthase 2 (EC 5.3.99.3)
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name Not Available
Enzyme 13 Protein Sequence >cDNA FLJ32487 fis, clone SKNSH1000002, highly similar to Prostaglandin E synthase 2 (EC 5.3.99.3)
MDPAARVVRALWPGGCALAWRLGGRPQPLLPTQSRAGFAGAAGGPSPVAAARKGSPRLLG
AAALALGGALGLYHTARWHLRAQDLHAERSAAQLSLSSRLQLTLYQYKTCPFCSKVRALL
DFHALPYQVVEVNPVRRAEIKFSSYRKVPILVAQEGESSQQLNDSSVIISALKTYLVSGQ
PLEEIITYYPAMKAVNEQGKEVTEFGNKYWLMLNEKEAQQVYGGKEARTEEMKWRQWADD
WLVHLIFPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQ
DNVREDLYEAADKWVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQ
PWYLRVERAITEASPAH
Enzyme 13 Number of Residues 377
Enzyme 13 Molecular Weight 41968.8
Enzyme 13 Theoretical pI 9.50
Enzyme 13 GO Classification
Function
  • catalytic activity
  • disulfide oxidoreductase activity
  • electron carrier activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on a sulfur group of donors
  • protein disulfide oxidoreductase activity
Process
  • cell redox homeostasis
  • cellular homeostasis
  • cellular process
Component
Enzyme 13 General Function Involved in electron carrier activity
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 193787031 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID B3KPZ2 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name B3KPZ2_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1134 bp
ATGGACCCGGCTGCGCGGGTGGTGCGGGCGCTGTGGCCTGGTGGGTGCGCCTTGGCCTGG
AGGCTGGGAGGCCGCCCCCAGCCGCTGCTACCCACGCAGAGCCGGGCTGGCTTCGCGGGG
GCGGCGGGCGGCCCGAGCCCCGTGGCTGCAGCTCGTAAGGGGAGCCCGCGGCTGCTGGGA
GCTGCGGCGCTGGCCCTGGGGGGAGCCCTGGGGCTGTACCACACGGCGCGGTGGCACCTG
CGCGCCCAGGACCTCCACGCAGAGCGCTCAGCCGCGCAGCTCTCCCTGTCCAGCCGCCTG
CAGCTGACCCTGTACCAGTACAAGACGTGTCCCTTCTGCAGCAAGGTCCGAGCCCTCCTC
GACTTCCATGCCCTGCCCTACCAGGTGGTGGAGGTGAACCCTGTGCGCAGGGCTGAGATC
AAGTTCTCCTCCTACAGAAAGGTGCCCATCCTGGTGGCCCAGGAAGGAGAAAGCTCGCAA
CAACTAAATGACTCCTCTGTCATCATCAGCGCCCTCAAGACCTACCTGGTGTCGGGGCAG
CCCCTGGAAGAGATCATCACCTACTACCCAGCCATGAAGGCTGTGAACGAGCAGGGCAAG
GAGGTGACCGAGTTCGGCAATAAGTACTGGCTCATGCTCAACGAGAAGGAGGCCCAGCAA
GTGTATGGTGGGAAGGAGGCCAGGACGGAGGAGATGAAGTGGCGGCAGTGGGCGGACGAC
TGGCTGGTGCACCTGATCTTCCCCAATGTGTACCGCACGCCCACCGAGGCTCTGGCGTCC
TTTGACTACATTGTCCGCGAGGGCAAGTTCGGAGCCGTGGAGGGTGCCGTGGCCAAGTAC
ATGGGTGCAGCGGCCATGTACCTCATCAGCAAGCGACTCAAGAGCAGGCACCGCCTCCAG
GACAACGTGCGCGAGGACCTCTATGAGGCTGCTGACAAGTGGGTGGCTGCTGTGGGCAAG
GACCGGCCCTTCATGGGGGGCCAGAAGCCGAATCTCGCTGATTTGGCGGTGTATGGCGTG
CTGCGTGTGATGGAGGGGCTGGATGCATTCGATGACCTGATGCAGCACACGCACATCCAG
CCCTGGTACCTGCGGGTGGAGAGGGCCATCACCGAGGCCTCCCCAGCGCACTGA
Enzyme 13 GenBank Gene ID AK057049 Link Image
Enzyme 13 GeneCard ID Not Available
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID HGNC:17822 Link Image
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs Not Available
Enzyme 13 General References
  1. 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]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 17036
Enzyme 14 Name CUGBP Elav-like family member 2
Enzyme 14 Synonyms
  1. CELF-2
  2. Bruno-like protein 3
  3. CUG triplet repeat RNA-binding protein 2
  4. CUG-BP2
  5. CUG-BP- and ETR-3-like factor 2
  6. ELAV-type RNA-binding protein 3
  7. ETR-3
  8. Neuroblastoma apoptosis-related RNA-binding protein
  9. hNAPOR
  10. RNA-binding protein BRUNOL-3
Enzyme 14 Gene Name CELF2
Enzyme 14 Protein Sequence >CUGBP Elav-like family member 2
MRCPKSAVTMRNEELLLSNGTANKMNGALDHSDQPDPDAIKMFVGQIPRSWSEKELKELF
EPYGAVYQINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNIKTLPGMHHPIQMKP
ADSEKSNAVEDRKLFIGMVSKKCNENDIRVMFSPFGQIEECRILRGPDGLSRGCAFVTFS
TRAMAQNAIKAMHQSQTMEGCSSPIVVKFADTQKDKEQRRLQQQLAQQMQQLNTATWGNL
TGLGGLTPQYLALLQQATSSSNLGAFSGIQQMAGMNALQLQNLATLAAAAAAAQTSATST
NANPLSTTSSALGALTSPVAASTPNSTAGAAMNSLTSLGTLQGLAGATVGLNNINALAGM
AALNGGLGATGLTNGTAGTMDALTQAYSGIQQYAAAALPTLYSQSLLQQQSAAGSQKEGP
EGANLFIYHLPQEFGDQDILQMFMPFGNVISAKVFIDKQTNLSKCFGFVSYDNPVSAQAA
IQAMNGFQIGMKRLKVQLKRSKNDSKPY
Enzyme 14 Number of Residues 508
Enzyme 14 Molecular Weight 54284.4
Enzyme 14 Theoretical pI 9.01
Enzyme 14 GO Classification
Function
  • RNA binding
  • binding
  • nucleic acid binding
  • nucleotide binding
Process
Component
Enzyme 14 General Function Involved in nucleotide binding
Enzyme 14 Specific Function RNA-binding protein implicated in the regulation of several post-transcriptional events. Involved in pre-mRNA alternative splicing, mRNA translation and stability. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of TNNT2 in embryonic, but not adult, skeletal muscle. Activates TNNT2 exon 5 inclusion by antagonizing the repressive effect of PTB. Acts as both an activator and repressor of a pair of coregulated exons:promotes inclusion of the smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs. Promotes inclusion of exonS 21 and exclusion of exon 5 of the NMDA receptor R1 pre- mRNA. Involved in the apoB RNA editing activity. Increases COX2 mRNA stability and inhibits COX2 mRNA translation in epithelial cells after radiation injury. Modulates the cellular apoptosis program by regulating COX2-mediated prostaglandin E2 (PGE2) expression. Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK. Binds to the muscle-specific splicing enhancer (MSE) intronic sites flanking the TNNT2 alternative exon 5. Binds preferentially to UG-rich sequences, in particular UG repeat and UGUU motifs. Binds to apoB mRNA, specifically to AU-rich sequences located immediatly upstream of the edited cytidine. Binds AU-rich sequences in the 3'-UTR of COX2 mRNA. Binds to an intronic RNA element responsible for the silencing of exon 21 splicing. Binds to (CUG)n repeats
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 68303647 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID O95319 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name CELF2_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1527 bp
ATGCGCTGTCCCAAATCCGCTGTTACTATGAGAAATGAAGAGCTGCTTTTAAGTAACGGC
ACAGCCAACAAGATGAACGGAGCTTTGGATCACTCAGACCAACCAGACCCAGATGCCATT
AAGATGTTTGTCGGACAGATCCCCCGGTCATGGTCGGAAAAGGAGCTGAAAGAACTTTTT
GAGCCTTACGGAGCCGTCTACCAGATCAACGTCCTCCGGGACCGGAGTCAGAACCCTCCG
CAGAGTAAAGGTTGTTGTTTCGTAACATTTTATACAAGAAAAGCTGCACTTGAGGCCCAG
AATGCACTGCACAATATTAAAACTTTACCTGGGATGCATCATCCCATTCAGATGAAACCT
GCAGATAGTGAAAAGTCCAACGCTGTGGAAGACAGAAAATTGTTCATAGGAATGGTATCG
AAGAAATGTAATGAGAACGACATCAGGGTGATGTTCTCTCCATTTGGCCAGATAGAAGAA
TGCCGGATCCTCCGGGGACCTGATGGGCTGAGTCGAGGCTGTGCGTTTGTCACATTTTCT
ACAAGGGCAATGGCACAGAATGCAATCAAAGCCATGCATCAGTCTCAGACCATGGAGGGC
TGCTCTTCACCTATCGTGGTGAAGTTTGCTGACACTCAGAAGGACAAAGAGCAAAGGCGC
CTCCAGCAGCAGCTCGCTCAGCAGATGCAGCAGCTCAACACTGCCACCTGGGGGAACCTG
ACAGGGCTGGGCGGACTGACCCCACAGTATCTGGCGCTCCTGCAGCAGGCCACCTCCTCC
AGCAACCTGGGTGCGTTCAGCGGCATTCAACAAATGGCAGGCATGAATGCTTTACAGTTG
CAGAACCTGGCGACGCTGGCTGCTGCTGCAGCTGCGGCCCAGACCTCAGCCACCAGCACC
AATGCAAACCCTCTCTCTACCACGAGCAGCGCCCTGGGAGCCCTCACGAGTCCCGTGGCT
GCTTCAACCCCCAACTCCACTGCTGGTGCAGCCATGAACTCCTTGACCTCTCTCGGGACT
CTGCAAGGACTGGCTGGAGCCACTGTTGGACTGAATAATATTAATGCACTAGCAGGTATG
GCGGCTCTGAATGGAGGACTTGGCGCCACAGGCTTGACGAATGGCACGGCTGGCACCATG
GACGCCCTCACCCAGGCCTACTCAGGAATTCAACAGTACGCAGCCGCCGCGCTGCCCACT
CTGTACAGCCAGAGCCTGCTGCAGCAGCAGAGCGCTGCAGGCAGCCAGAAGGAAGGTCCA
GAGGGGGCAAACCTCTTTATTTACCACCTTCCACAGGAATTTGGAGACCAGGACATTCTG
CAGATGTTCATGCCTTTTGGAAATGTTATCTCTGCTAAAGTCTTCATTGACAAACAGACC
AATCTGAGCAAGTGCTTTGGTTTTGTTAGCTACGACAATCCAGTCTCTGCACAAGCTGCT
ATCCAAGCTATGAATGGCTTTCAGATCGGCATGAAACGCTTGAAGGTGCAGCTGAAGCGT
TCCAAAAACGACAGCAAACCTTACTGA
Enzyme 14 GenBank Gene ID NM_001025077.2 Link Image
Enzyme 14 GeneCard ID CELF2 Link Image
Enzyme 14 GenAtlas ID CELF2 Link Image
Enzyme 14 HGNC ID HGNC:2550 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 10p13
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Choi DK, Ito T, Mitsui Y, Sakaki Y: Fluorescent differential display analysis of gene expression in apoptotic neuroblastoma cells. Gene. 1998 Nov 26;223(1-2):21-31. [PubMed Link Image]
  2. Choi DK, Ito T, Tsukahara F, Hirai M, Sakaki Y: Developmentally-regulated expression of mNapor encoding an apoptosis-induced ELAV-type RNA binding protein. Gene. 1999 Sep 3;237(1):135-42. [PubMed Link Image]
  3. Good PJ, Chen Q, Warner SJ, Herring DC: A family of human RNA-binding proteins related to the Drosophila Bruno translational regulator. J Biol Chem. 2000 Sep 15;275(37):28583-92. [PubMed Link Image]
  4. Li D, Bachinski LL, Roberts R: Genomic organization and isoform-specific tissue expression of human NAPOR (CUGBP2) as a candidate gene for familial arrhythmogenic right ventricular dysplasia. Genomics. 2001 Jun 15;74(3):396-401. [PubMed Link Image]
  5. 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]
  6. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  7. 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]
  8. Timchenko LT, Miller JW, Timchenko NA, DeVore DR, Datar KV, Lin L, Roberts R, Caskey CT, Swanson MS: Identification of a (CUG)n triplet repeat RNA-binding protein and its expression in myotonic dystrophy. Nucleic Acids Res. 1996 Nov 15;24(22):4407-14. [PubMed Link Image]
  9. Anant S, Henderson JO, Mukhopadhyay D, Navaratnam N, Kennedy S, Min J, Davidson NO: Novel role for RNA-binding protein CUGBP2 in mammalian RNA editing. CUGBP2 modulates C to U editing of apolipoprotein B mRNA by interacting with apobec-1 and ACF, the apobec-1 complementation factor. J Biol Chem. 2001 Dec 14;276(50):47338-51. Epub 2001 Sep 27. [PubMed Link Image]
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  11. Charlet-B N, Logan P, Singh G, Cooper TA: Dynamic antagonism between ETR-3 and PTB regulates cell type-specific alternative splicing. Mol Cell. 2002 Mar;9(3):649-58. [PubMed Link Image]
  12. Gromak N, Matlin AJ, Cooper TA, Smith CW: Antagonistic regulation of alpha-actinin alternative splicing by CELF proteins and polypyrimidine tract binding protein. RNA. 2003 Apr;9(4):443-56. [PubMed Link Image]
  13. Singh G, Charlet-B N, Han J, Cooper TA: ETR-3 and CELF4 protein domains required for RNA binding and splicing activity in vivo. Nucleic Acids Res. 2004 Feb 18;32(3):1232-41. Print 2004. [PubMed Link Image]
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Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 17127
Enzyme 15 Name cDNA, FLJ79474, highly similar to Prostaglandin E2 receptor, EP3 subtype (Prostaglandin E receptor 3 (Subtype EP3), isoform CRA_d)
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name PTGER3
Enzyme 15 Protein Sequence >cDNA, FLJ79474, highly similar to Prostaglandin E2 receptor, EP3 subtype (Prostaglandin E receptor 3 (Subtype EP3), isoform CRA_d)
MKETRGYGGDAPFCTRLNHSYTGMWAPERSAEARGNLTRPPGSGEDCGSVSVAFPITMLL
TGFVGNALAMLLVSRSYRRRESKRKKSFLLCIGWLALTDLVGQLLTTPVVIVVYLSKQRW
EHIDPSGRLCTFFGLTMTVFGLSSLFIASAMAVERALAIRAPHWYASHMKTRATRAVLLG
VWLAVLAFALLPVLGVGQYTVQWPGTWCFISTGRGGNGTSSSHNWGNLFFASAFAFLGLL
ALTVTFSCNLATIKALVSRCRAKATASQSSAQWGRITTETAIQLMGIMCVLSVCWSPLLI
MMLKMIFNQTSVEHCKTHTEKQKECNFFLIAVRLASLNQILDPWVYLLLRKILLRKFCQI
RYHTNNYASSSTSLPCQCSSTLMWSDHLER
Enzyme 15 Number of Residues 390
Enzyme 15 Molecular Weight 43310
Enzyme 15 Theoretical pI 10.05
Enzyme 15 GO Classification
Function
  • G-protein coupled receptor activity
  • icosanoid receptor activity
  • prostaglandin E receptor activity
  • prostaglandin receptor activity
  • prostanoid receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 15 General Function Not Available
Enzyme 15 Specific Function Not Available
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID B0AZN4 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name B0AZN4_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence Not Available
Enzyme 15 GenBank Gene ID AK315825 Link Image
Enzyme 15 GeneCard ID B0AZN4 Link Image
Enzyme 15 GenAtlas ID Not Available
Enzyme 15 HGNC ID Not Available
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References Not Available
Enzyme 15 Metabolite References Not Available