| 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 |
- (-)-Prostaglandin E2
- 5-trans-PGE2
- Dinoprostone
- Dinoprostonum
- Glandin
- Minprositin E2
- Minprostin E2
- PGE2
- Prepidil
- Prostaglandin E
- Prostaglandin E2
- Prostaglandin E2alpha
- Prostarmon E
- Prostin
- Prostin E2
- l-Prostaglandin E2
- (5Z,13E)-(15S)-11alpha,15-Dihydroxy-9-oxoprosta-5,13-dienoate
- (5Z,13E)-(15S)-11alpha,15-Dihydroxy-9-oxoprost-13-enoate
- (5Z,13E)-(15S)-11alpha,15-Dihydroxy-9-oxoprosta-5,13-dienoic acid
- (5Z,13E)-(15S)-11alpha,15-Dihydroxy-9-oxoprost-13-enoic acid
- (5Z,13E,15S)-11-alpha,15-dihydroxy-9-oxoprost-5,13-dienoic acid
- (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 |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
|
| Class |
|
| Sub Class |
|
| Family |
|
| Species |
- ketone
- secondary alcohol
- carboxylic acid
- alkene
|
| Biofunction |
- Component of Prostaglandin and leukotriene metabolism
|
| Application |
| — |
| Source |
|
|
| 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  |
| BioCyc ID |
5Z13E-15S-1115-DIHYDROXY-9-OXOPROS  |
| BiGG ID |
35424  |
| Wikipedia Link |
Dinoprostone  |
| NuGOwiki Link |
HMDB01220  |
| Metagene Link |
HMDB01220  |
| METLIN ID |
6089  |
| PubChem Compound |
5280360  |
| PubChem Substance |
8616235  |
| ChEBI ID |
15551  |
| 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 |
| SDF File |
Show |
| PDB File |
Show |
| 2D Structure |
|
| 3D Structure |
|
| Experimental PDB ID |
Not Available |
| Experimental 1H NMR Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| Experimental 13C NMR Spectrum |
Not Available |
| Experimental 13C HSQC Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| 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
]
|
| 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
]
|
| 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 |
- Nikolaos Psychogios, David D. Hau, Jun Peng, An Chi Guo, Rupasri Mandal, Souhaila Bouatra, Igor Sinelnikov, Ramanarayan Krishnamurthy, Roman Eisner, Bijaya Gautam, Nelson Young, Jinaguo Xia, Craig Knox, Ying Wei Dong, Paul Huang, Janet McManus, Theresa Pedersen, Fiona Bamforth, Russ Greiner, Bruce McManus, John Newman, David S. Wishart, The Human Serum Metabolome, PLoS ONE (Submitted).
- 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
]
|
| 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
]
|
| 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
]
|
|
| 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
]
|
| 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
]
|
|
| 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
]
|
| 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
]
|
|
| OMIM ID |
- 105400
(Amyotrophic lateral sclerosis)
|
| Pathways |
|
| General References |
- Ilzecka J: Prostaglandin E2 is increased in amyotrophic lateral sclerosis patients. Acta Neurol Scand. 2003 Aug;108(2):125-9. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- Yamada M, Ogata M, Kawai M, Mashima Y, Nishida T: Substance P in human tears. Cornea. 2003 Oct;22(7 Suppl):S48-54. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- Greaves MW: Does ultraviolet-evoked prostaglandin formation protect skin from actinic cancer? Lancet. 1978 Jan 28;1(8057):189. [PubMed
]
- Wikipedia

|
| Metabolic Enzymes |
- Carbonyl reductase [NADPH] 3
- 15-hydroxyprostaglandin dehydrogenase [NAD+]
- Prostaglandin E synthase
- Solute carrier organic anion transporter family member 1B1
- Prostaglandin E2 receptor, EP1 subtype
- Prostaglandin E2 receptor, EP4 subtype
- Prostaglandin E synthase 2
- cDNA, FLJ95780, Homo sapiens carbonyl reductase 1 (CBR1), mRNA (Carbonyl reductase 1, isoform CRA_d)
- Prostaglandin E2 receptor EP3 subtype
- Prostaglandin E2 receptor EP2 subtype
- Solute carrier family 22 member 7
- cDNA FLJ32487 fis, clone SKNSH1000002, highly similar to Prostaglandin E synthase 2 (EC 5.3.99.3)
- CUG-BP- and ETR-3-like factor 2
- 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 |
5306 |
| Enzyme 1 Name |
Carbonyl reductase [NADPH] 3 |
| Enzyme 1 Synonyms |
- NADPH-dependent carbonyl reductase 3
|
| Enzyme 1 Gene Name |
CBR3 |
| Enzyme 1 Protein Sequence |
>Carbonyl reductase [NADPH] 3
MSSCSRVALVTGANRGIGLAIARELCRQFSGDVVLTARDVARGQAAVQQLQAEGLSPRFH
QLDIDDLQSIRALRDFLRKEYGGLNVLVNNAAVAFKSDDPMPFDIKAEMTLKTNFFATRN
MCNELLPIMKPHGRVVNISSLQCLRAFENCSEDLQERFHSETLTEGDLVDLMKKFVEDTK
NEVHEREGWPNSPYGVSKLGVTVLSRILARRLDEKRKADRILVNACCPGPVKTDMDGKDS
IRTVEEGAETPVYLALLPPDATEPQGQLVHDKVVQNW
|
| Enzyme 1 Number of Residues |
277 |
| Enzyme 1 Molecular Weight |
30851 |
| Enzyme 1 Theoretical pI |
6.06 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Lipid transport and metabolism |
| Enzyme 1 Specific Function |
R-CHOH-R' + NADP(+) = R-CO-R' + NADPH |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
3702689  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
O75828  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
CBR3_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>834 bp
ATGTCGTCCTGCAGCCGCGTGGCGCTGGTGACCGGGGCCAACAGGGGCATCGGCTTGGCC
ATCGCGCGCGAACTGTGCCGACAGTTCTCTGGGGATGTGGTGCTCACCGCGCGGGACGTG
GCGCGGGGCCAGGCGGCCGTGCAGCAGCTGCAGGCGGAGGGCCTGAGCCCGCGCTTCCAC
CAACTGGACATCGACGACTTGCAGAGCATCCGCGCCCTGCGCGACTTCCTGCGCAAGGAG
TACGGGGGGCTCAACGTACTGGTCAACAACGCGGCCGTCGCCTTCAAGAGTGATGATCCA
ATGCCCTTTGACATTAAAGCTGAGATGACACTGAAGACAAATTTTTTTGCCACTAGAAAC
ATGTGCAACGAGTTACTGCCGATAATGAAACCTCATGGGAGAGTGGTGAATATCAGTAGT
TTGCAGTGTTTAAGGGCTTTTGAAAACTGCAGTGAAGATCTGCAGGAAAGGTTCCACAGT
GAGACACTCACAGAAGGAGACCTGGTGGATCTCATGAAAAAGTTTGTGGAGGACACAAAA
AATGAGGTGCATGAGAGGGAAGGCTGGCCCAACTCACCTTATGGGGTGTCCAAGTTGGGG
GTCACGGTCTTATCGAGGATCCTGGCCAGGCGTCTGGATGAGAAGAGGAAAGCTGACAGG
ATTCTGGTGAATGCGTGCTGCCCAGGACCAGTGAAGACAGACATGGATGGGAAAGACAGC
ATCAGGACTGTGGAGGAGGGGGCTGAGACCCCTGTCTACTTGGCCCTCTTGCCTCCAGAT
GCCACTGAGCCACAAGGCCAGTTGGTCCATGACAAAGTTGTGCAAAACTGGTAA
|
| Enzyme 1 GenBank Gene ID |
AB004854  |
| Enzyme 1 GeneCard ID |
CBR3  |
| Enzyme 1 GenAtlas ID |
CBR3  |
| Enzyme 1 HGNC ID |
HGNC:1549  |
| Enzyme 1 Chromosome Location |
Not Available |
| Enzyme 1 Locus |
Not Available |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- 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
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5307 |
| Enzyme 2 Name |
15-hydroxyprostaglandin dehydrogenase [NAD+] |
| Enzyme 2 Synonyms |
- PGDH
- Prostaglandin dehydrogenase 1
|
| Enzyme 2 Gene Name |
HPGD |
| Enzyme 2 Protein Sequence |
>15-hydroxyprostaglandin dehydrogenase [NAD+]
MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLF
IQCDVADQQQLRDTFRKVVDHFGRLDILVNNAGVNNEKNWEKTLQINLVSVISGTYLGLD
YMSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASKHGIVGFTRSAALAANLMNSGVRLNA
ICPGFVNTAILESIEKEENMGQYIEYKDHIKDMIKYYGILDPPLIANGLITLIEDDALNG
AIMKITTSKGIHFQDYDTTPFQAKTQ
|
| Enzyme 2 Number of Residues |
266 |
| Enzyme 2 Molecular Weight |
28978 |
| Enzyme 2 Theoretical pI |
5.65 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Lipid transport and metabolism |
| Enzyme 2 Specific Function |
Inactivation of prostaglandins |
| Enzyme 2 Pathways |
Not Available |
| Enzyme 2 Reactions |
- (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate + NAD+ = (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate + NADH + H+
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
1203984  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P15428  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
PGDH_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>801 bp
ATGCACGTGAACGGCAAAGTGGCGCTGGTGACCGGCGCGGCTCAGGGCATAGGCAGAGCC
TTTGCAGAGGCGCTGCTGCTTAAGGGCGCCAAGGTAGCGCTGGTGGATTGGAATCTTGAA
GCAGGTGTACAGTGTAAAGCTGCCCTGCATGAGCAATTTGAACCTCAGAAGACTCTGTTC
ATCCAGTGCGATGTGGCTGACCAGCAACAACTGAGAGACACTTTTAGAAAAGTTGTAGAC
CACTTTGGAAGACTGGACATTTTGGTCAATAATGCTGGAGTGAATAATGAGAAAAACTGG
GAAAAAACTCTGCAAATTAATTTGGTTTCTGTTATCAGTGGAACCTATCTTGGTTTGGAT
TACATGAGTAAGCAAAATGGAGGTGAAGGCGGCATCATTATCAATATGTCATCTTTAGCA
GGACTCATGCCCGTTGCACAGCAGCCGGTTTATTGTGCTTCAAAGCATGGCATAGTTGGA
TTCACACGCTCAGCAGCGTTGGCTGCTAATCTTATGAACAGTGGTGTGAGACTGAATGCC
ATTTGTCCAGGCTTTGTTAACACAGCCATCCTTGAATCAATTGAAAAAGAAGAAAACATG
GGACAATATATAGAATATAAGGATCATATCAAGGATATGATTAAATACTATGGAATTTTG
GACCCACCATTGATTGCCAATGGATTGATAACACTCATTGAAGATGATGCTTTAAATGGT
GCTATTATGAAGATCACAACTTCTAAGGGAATTCATTTTCAAGACTATGATACAACTCCA
TTTCAAGCAAAAACCCAATGA
|
| Enzyme 2 GenBank Gene ID |
L76465  |
| Enzyme 2 GeneCard ID |
HPGD  |
| Enzyme 2 GenAtlas ID |
HPGD  |
| Enzyme 2 HGNC ID |
HGNC:5154  |
| Enzyme 2 Chromosome Location |
4 |
| Enzyme 2 Locus |
4q34-q35 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5308 |
| Enzyme 3 Name |
Prostaglandin E synthase |
| Enzyme 3 Synonyms |
- Microsomal glutathione S- transferase 1-like 1
- MGST1-L1
- p53-induced apoptosis protein 12
|
| Enzyme 3 Gene Name |
PTGES |
| Enzyme 3 Protein Sequence |
>Prostaglandin E synthase
MPAHSLVMSSPALPAFLLCSTLLVIKMYVVAIITGQVRLRKKAFANPEDALRHGGPQYCR
SDPDVERCLRAHRNDMETIYPFLFLGFVYSFLGPNPFVAWMHFLVFLVGRVAHTVAYLGK
LRAPIRSVTYTLAQLPCASMALQILWEAARHL
|
| Enzyme 3 Number of Residues |
152 |
| Enzyme 3 Molecular Weight |
17103 |
| Enzyme 3 Theoretical pI |
9.77 |
| Enzyme 3 GO Classification |
Not Available |
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 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 3 Pathways |
|
| Enzyme 3 Reactions |
- (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
Not Available |
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
2415308  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
O14684  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
PTGES_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>462 bp
ATGCCTGCCCACAGCCTGGTGATGAGCAGCCCGGCCCTCCCGGCCTTCCTGCTCTGCAGC
ACGCTGCTGGTCATCAAGATGTACGTGGTGGCCATCATCACGGGCCAAGTGAGGCTGCGG
AAGAAGGCCTTTGCCAACCCCGAGGATGCCCTGAGACACGGAGGAGGCCCCCAGTATTGC
AGGAGCGACCCCGACGTGGAACGCTGCCTCAGGGCCCACCGGAACGACATGGAGACCATC
TACCCCTTCCTTTTCCTGGGCTTCGTCTACTCCTTTCTGGGTCCTAACCCTTTTGTCGCC
TGGATGCACTTCCTGGTCTTCCTCGTGGGCCGTGTGGCACACACCGTGGCCTACCTGGGG
AAGCTGCGGGCACCCATCCGCTCCGTGACCTACACCCTGGCCCAGCTCCCCTGCGCCTCC
ATGGCTCTGCAGATCCTCTGGGAAGCGGCCCGCCACCTGTGA
|
| Enzyme 3 GenBank Gene ID |
AF010316  |
| Enzyme 3 GeneCard ID |
PTGES  |
| Enzyme 3 GenAtlas ID |
PTGES  |
| Enzyme 3 HGNC ID |
HGNC:9599  |
| Enzyme 3 Chromosome Location |
9 |
| Enzyme 3 Locus |
9q34.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- 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
]
- 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
]
- 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
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5692 |
| Enzyme 4 Name |
Solute carrier organic anion transporter family member 1B1 |
| Enzyme 4 Synonyms |
- Solute carrier family 21 member 6
- Sodium-independent organic anion- transporting polypeptide 2
- OATP 2
- Liver-specific organic anion transporter 1
- LST-1
- OATP-C
|
| Enzyme 4 Gene Name |
SLCO1B1 |
| Enzyme 4 Protein Sequence |
>Solute carrier organic anion transporter family member 1B1
MDQNQHLNKTAEAQPSENKKTRYCNGLKMFLAALSLSFIAKTLGAIIMKSSIIHIERRFE
ISSSLVGFIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCFIMGIGGVLTALPHFFMGY
YRYSKETNINSSENSTSTLSTCLINQILSLNRASPEIVGKGCLKESGSYMWIYVFMGNML
RGIGETPIVPLGLSYIDDFAKEGHSSLYLGILNAIAMIGPIIGFTLGSLFSKMYVDIGYV
DLSTIRITPTDSRWVGAWWLNFLVSGLFSIISSIPFFFLPQTPNKPQKERKASLSLHVLE
TNDEKDQTANLTNQGKNITKNVTGFFQSFKSILTNPLYVMFVLLTLLQVSSYIGAFTYVF
KYVEQQYGQPSSKANILLGVITIPIFASGMFLGGYIIKKFKLNTVGIAKFSCFTAVMSLS
FYLLYFFILCENKSVAGLTMTYDGNNPVTSHRDVPLSYCNSDCNCDESQWEPVCGNNGIT
YISPCLAGCKSSSGNKKPIVFYNCSCLEVTGLQNRNYSAHLGECPRDDACTRKFYFFVAI
QVLNLFFSALGGTSHVMLIVKIVQPELKSLALGFHSMVIRALGGILAPIYFGALIDTTCI
KWSTNNCGTRGSCRTYNSTSFSRVYLGLSSMLRVSSLVLYIILIYAMKKKYQEKDINASE
NGSVMDEANLESLNKNKHFVPSAGADSETHC
|
| Enzyme 4 Number of Residues |
691 |
| Enzyme 4 Molecular Weight |
76450 |
| Enzyme 4 Theoretical pI |
8.68 |
| Enzyme 4 GO Classification |
| Function |
|
| Process |
- cellular physiological process
- physiological process
- transport
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 4 General Function |
Carbohydrate transport and metabolism |
| Enzyme 4 Specific Function |
Mediates the Na(+)-independent transport of organic anions such as pravastatin, taurocholate, methotrexate, dehydroepiandrosterone sulfate, 17-beta-glucuronosyl estradiol, estrone sulfate, prostaglandin E2, thromboxane B2, leukotriene C3, leukotriene E4, thyroxine and triiodothyronine. May play an important role in the clearance of bile acids and organic anions from the liver |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
- 97-117
207-227
259-279
336-356
376-396
410-430
575-595
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
5051630  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q9Y6L6  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
SO1B1_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>2076 bp
ATGGACCAAAATCAACATTTGAATAAAACAGCAGAGGCACAACCTTCAGAGAATAAGAAA
ACAAGATACTGCAATGGATTGAAGATGTTCTTGGCAGCTCTGTCACTCAGCTTTATTGCT
AAGACACTAGGTGCAATTATTATGAAAAGTTCCATCATTCATATAGAACGGAGATTTGAG
ATATCCTCTTCTCTTGTTGGTTTTATTGACGGAAGCTTTGAAATTGGAAATTTGCTTGTG
ATTGTATTTGTGAGTTACTTTGGATCCAAACTACATAGACCAAAGTTAATTGGAATCGGT
TGTTTCATTATGGGAATTGGAGGTGTTTTGACTGCTTTGCCACATTTCTTCATGGGATAT
TACAGGTATTCTAAAGAAACTAATATCAATTCATCAGAAAATTCAACATCGACCTTATCC
ACTTGTTTAATTAATCAAATTTTATCACTCAATAAAGCATCACCTGAGATAGTGGGAAAA
GGTTGTTTAAAGGAATCTGGGTCATACATGTGGATATATGTGTTCATGGGTAATATGCTT
CGTGGAATAGGGGAGACTCCCATAGTACCACTGGGGCTTTCTTACATTGATGATTTCGCT
AAAGAAGGACATTCTTCTTTGTATTTAGGTATATTGAATGCAATAGCAATGATTGGTCCA
ATCATTGGCTTTACCCTGGGATCTCTGTTTTCTAAAATGTACGTGGATATTGGATATGTT
AATCTAAGCACTATCAGGATAACTCCTACTGATTCTCGATGGGTTGGAGCTTGGTGGCTT
AATTTCCTTGTGTCTGGACTATTCTCCATTATTTCTTCCATACCATTCTTTTTCTTGCCC
CAAACTCCAAATAAACCACAAAAAGAAAGAAAAGCTTCACTGTCTTTGCATGTGCTGGAA
ACAAATGATGAAAAGGATCAAACAGCTAATTTGACCAATCAAGGAAAAAATATTACCAAA
AATGTGACTGGTTTTTTCCAGTCTTTTAAAAGCATCCTTACTAATCCCCTGTATGTTATG
TTTGTGCTTTTGACGTTGTTACAAGTAAGCAGCTATATTGGTGCTTTTACTTATGTCTTC
AAATACGTAGAGCAACAGTATGGTCAGCCTTCATCTAAGGCTAACATCTTATTGGGAGTC
ATAACCATACCTATTTTTGCAAGTGGAATGTTTTTAGGAGGATATATCATTAAAAAATTC
AAACTGAACACCGTTGGAATTGCCAAATTCTCATGTTTTACTGCTGTGATGTCATTGTCC
TTTTACCTATTATATTTTTTCATACTCTGTGAAAACAAATCAGTTGCCGGACTAACCATG
ACCTATGATGGAAATAATCCAGTGACATCTCATAGAGATGTACCACTTTCTTATTGCAAC
TCAGACTGCAATTGTGATGAAAGTCAATGGGAACCAGTCTGTGGAAACAATGGAATAACT
TACATCTCACCCTGTCTAGCAGGTTGCAAATCTTCAAGTGGCAATAAAAAGCCTATAGTG
TTTTACAACTGCAGTTGTTTGGAAGTAACTGGTCTCCAGAACAGAAATTACTCAGCCCAT
TTGGGTGAATGCCCAAGAGATGATGCTTGTACAAGGAAATTTTACTTTTTTGTTGCAATA
CAAGTCTTGAATTTATTTTTCTCTGCACTTGGAGGCACCTCACATGTCATGCTGATTGTT
AAAATTGTTCAACCTGAATTGAAATCACTTGCACTGGGTTTCCACTCAATGGTTATACGA
GCACTAGGAGGAATTCTAGCTCCTATATATTTTGGGGCTCTGATTGATACAACGTGTATA
AAGTGGTCCACCAACAACTGTGGCACACGTGGGTCATGTAGGACATATAATTCCACATCA
TTTTCAAGGGTCTACTTGGGCTTGTCTTCAATGTTAAGAGTCTCATCACTTGTTTTATAT
ATTATATTAATTTATGCCATGAAGAAAAAATATCAAGAGAAAGATATCAATGCATCAGAA
AATGGAAGTGTCATGGATGAAGCAAACTTAGAATCCTTAAATAAAAATAAACATTTTGTC
CCTTCTGCTGGGGCAGATAGTGAAACACATTGTTAA
|
| Enzyme 4 GenBank Gene ID |
AF060500  |
| Enzyme 4 GeneCard ID |
SLCO1B1  |
| Enzyme 4 GenAtlas ID |
SLCO1B1  |
| Enzyme 4 HGNC ID |
HGNC:10959  |
| Enzyme 4 Chromosome Location |
12 |
| Enzyme 4 Locus |
12p |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
7876 |
| Enzyme 5 Name |
Prostaglandin E2 receptor, EP1 subtype |
| Enzyme 5 Synonyms |
- Prostanoid EP1 receptor
- PGE receptor, EP1 subtype
|
| Enzyme 5 Gene Name |
PTGER1 |
| Enzyme 5 Protein Sequence |
>Prostaglandin E2 receptor, EP1 subtype
MSPCGPLNLSLAGEATTCAAPWVPNTSAVPPSGASPALPIFSMTLGAVSNLLALALLAQA
AGRLRRRRSAATFLLFVASLLATDLAGHVIPGALVLRLYTAGRAPAGGACHFLGGCMVFF
GLCPLLLGCGMAVERCVGVTRPLLHAARVSVARARLALAAVAAVALAVALLPLARVGRYE
LQYPGTWCFIGLGPPGGWRQALLAGLFASLGLVALLAALVCNTLSGLALLRARWRRRSRR
PPPASGPDSRRRWGAHGPRSASASSASSIASASTFFGGSRSSGSARRARAHDVEMVGQLV
GIMVVSCICWSPMLVLVALAVGGWSSTSLQRPLFLAVRLASWNQILDPWVYILLRQAVLR
QLLRLLPPRAGAKGGPAGLGLTPSAWEASSLRSSRHSGLSHF
|
| Enzyme 5 Number of Residues |
402 |
| Enzyme 5 Molecular Weight |
41802 |
| Enzyme 5 Theoretical pI |
12.22 |
| Enzyme 5 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 5 General Function |
Not Available |
| Enzyme 5 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 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
- 36-62
73-96
112-133
156-177
202-227
295-321
333-354
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
410209  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P34995  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
PE2R1_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1209 bp
ATGAGCCCTTGCGGGCCCCTCAACCTGAGCCTGGCGGGCGAGGCGACCACATGCGCGGCG
CCCTGGGTCCCCAACACGTCGGCCGTGCCGCCGTCGGGCGCTTCGCCCGCGCTGCCCATC
TTCTCCATGACGCTGGGCGCCGTGTCCAACCTGCTGGCGCTGGCGCTGCTGGCGCAGGCC
GCGGGCCGCCTGCGACGCCGCCGCTCGGCCACCACCTTCCTGCTGTTCGTGGCCAGCCTG
CTGGCCACCGACCTGGCGGGCCACGTGATCCCGGGCGCGCTGGTGCTGCGTCTGTACACT
GCGGGGCGCGCTCCGGCCGGCGGGGCCTGCCACTTCCTGGGCGGCTGCATGGTCTTCTTC
GGCCTGTGCCCGCTGCTGCTGGGCTGTGGCATGGCCGTGGAGCGCTGCGTGGGCGTCACG
CGGCCGCTGCTCCACGCCGCGCGGGTCTCGGTCGCCCGCGCGCGCCTGGCGCTGGCCGCG
GTGGCCGCGGTGGCCTTGGCCGTGGCGCTGCTGCCGCTGGCGCGCGTGGGCCGCTATGAG
CTGCAGTACCCGGGCACGTGGTGCTTCATCGGCCTGGGTCCCCCGGGCGGCTGGCGCCAG
GCACTGCTTGCTGGCCTCTTCGCCAGCCTCGGCCTGGTCGCGCTCCTCGCCGCGCTGGTG
TGCAACACGCTCAGCGGCCTGGCCCTGCATCGCGCCCGCTGGCGACGCCGCTCCCGACGG
CCTCCCCCGGCCTCAGGCCCCGACAGCCGGCGTCGCTGGGGGGCGCACGGACCCCGCTCG
GCCTCCGCCTCGTCCGCCTCGTCCATCGCTTCGGCCTCCACCTTCTTTGGCGGCTCTCGG
AGCAGCGGCTCGGCACGCAGAGCTCGCGCCCACGACGTGGAGATGGTGGGCCAGCTTGTC
GGTATCATGGTGGTGTCGTGCATCTGCTGGAGCCCAATGCTGGTGTTGGTGGCGCTGGCC
GTCGGCGGCTGGAGCTCTACCTCCCTGCAGCGGCCACTGTTCCTGGCCGTGCGCCTTGCC
TCCTGGAACCAGATCCTGGACCCTTGGGTGTACATCCTACTGCGCCAGGCCGTGCTGCGC
CAACTGCTTCGCCTCTTGCCCCCGAGGGCCGGAGCCAAGGGCGGCCCCGCGGGGCTGGGC
CTAACACCGAGCGCCTGGGAGGCCAGCTCGCTGCGCAGCTCCCGGCACAGCGGCCTCAGC
CACTTCTAA
|
| Enzyme 5 GenBank Gene ID |
L22647  |
| Enzyme 5 GeneCard ID |
PTGER1  |
| Enzyme 5 GenAtlas ID |
PTGER1  |
| Enzyme 5 HGNC ID |
HGNC:9593  |
| Enzyme 5 Chromosome Location |
19 |
| Enzyme 5 Locus |
19p13.1 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- 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
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
8295 |
| Enzyme 6 Name |
Prostaglandin E2 receptor, EP4 subtype |
| Enzyme 6 Synonyms |
- Prostanoid EP4 receptor
- PGE receptor, EP4 subtype
|
| Enzyme 6 Gene Name |
PTGER4 |
| Enzyme 6 Protein Sequence |
>Prostaglandin E2 receptor, EP4 subtype
MSTPGVNSSASLSPDRLNSPVTIPAVMFIFGVVGNLVAIVVLCKSRKEQKETTFYTLVCG
LAVTDLLGTLLVSPVTIATYMKGQWPGGQPLCEYSTFILLFFSLSGLSIICAMSVERYLA
INHAYFYSHYVDKRLAGLTLFAVYASNVLFCALPNMGLGSSRLQYPDTWCFIDWTTNVTA
HAAYSYMYAGFSSFLILATVLCNVLVCGALLRMHRQFMRRTSLGTEQHHAAAAASVASRG
HPAASPALPRLSDFRRRRSFRRIAGAEIQMVILLIATSLVVLICSIPLVVRVFVNQLYQP
SLEREVSKNPDLQAIRIASVNPILDPWIYILLRKTVLSKAIEKIKCLFCRIGGSRRERSG
QHCSDSQRTSSAMSGHSRSFISRELKEISSTSQTLLPDLSLPDLSENGLGGRNLLPGVPG
MGLAQEDTTSLRTLRISETSDSSQGQDSESVLLVDEAGGSGRAGPAPKGSSLQVTFPSET
LNLSEKCI
|
| Enzyme 6 Number of Residues |
488 |
| Enzyme 6 Molecular Weight |
53120 |
| Enzyme 6 Theoretical pI |
8.91 |
| Enzyme 6 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 6 General Function |
Not Available |
| Enzyme 6 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 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
Not Available |
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
Not Available |
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
452496  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P35408  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
PE2R4_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 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 6 GenBank Gene ID |
L28175  |
| Enzyme 6 GeneCard ID |
PTGER4  |
| Enzyme 6 GenAtlas ID |
PTGER4  |
| Enzyme 6 HGNC ID |
HGNC:9596  |
| Enzyme 6 Chromosome Location |
5 |
| Enzyme 6 Locus |
5p13.1 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
11165 |
| Enzyme 7 Name |
Prostaglandin E synthase 2 |
| Enzyme 7 Synonyms |
- Microsomal prostaglandin E synthase 2
- mPGES-2[Contains: Prostaglandin E synthase 2 truncated form]
|
| Enzyme 7 Gene Name |
PTGES2 |
| Enzyme 7 Protein Sequence |
>Prostaglandin E synthase 2
MDPAARVVRALWPGGCALAWRLGGRPQPLLPTQSRAGFAGAAGGPSPVAAARKGSPRLLG
AAALALGGALGLYHTARWHLRAQDLHAERSAAQLSLSSRLQLTLYQYKTCPFCSKVRAFL
DFHALPYQVVEVNPVRRAEIKFSSYRKVPILVAQEGESSQQLNDSSVIISALKTYLVSGQ
PLEEIITYYPAMKAVNEQGKEVTEFGNKYWLMLNEKEAQQVYGGKEARTEEMKWRQWADD
WLVHLISPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQ
DNVREDLYEAADKWVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQ
PWYLRVERAITEASPAH
|
| Enzyme 7 Number of Residues |
377 |
| Enzyme 7 Molecular Weight |
41944 |
| Enzyme 7 Theoretical pI |
Not Available |
| Enzyme 7 GO Classification |
| Function |
- electron transporter activity
- transporter activity
|
| Process |
- cell homeostasis
- cell redox homeostasis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- homeostasis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Not Available |
| Enzyme 7 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 7 Pathways |
|
| Enzyme 7 Reactions |
- Prostaglandin H2 <==> Prostaglandin E2
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
10436397  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q9H7Z7  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
PGES2_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
Not Available |
| Enzyme 7 GenBank Gene ID |
AK024100  |
| Enzyme 7 GeneCard ID |
Not Available |
| Enzyme 7 GenAtlas ID |
PTGES2  |
| Enzyme 7 HGNC ID |
HGNC:17822  |
| Enzyme 7 Chromosome Location |
Not Available |
| Enzyme 7 Locus |
Not Available |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- 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
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
12989 |
| Enzyme 8 Name |
cDNA, FLJ95780, Homo sapiens carbonyl reductase 1 (CBR1), mRNA (Carbonyl reductase 1, isoform CRA_d) |
| Enzyme 8 Synonyms |
Not Available |
| Enzyme 8 Gene Name |
CBR1 |
| Enzyme 8 Protein Sequence |
>cDNA, FLJ95780, Homo sapiens carbonyl reductase 1 (CBR1)
MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFH
QLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRD
VCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTK
KGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKA
TKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW
|
| Enzyme 8 Number of Residues |
277 |
| Enzyme 8 Molecular Weight |
30375 |
| Enzyme 8 Theoretical pI |
Not Available |
| Enzyme 8 GO Classification |
Not Available |
| Enzyme 8 General Function |
Not Available |
| Enzyme 8 Specific Function |
Not Available |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
Not Available |
| Enzyme 8 Pfam Domain Function |
Not Available |
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
Not Available |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
B2RBZ7  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
B2RBZ7_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
Not Available |
| Enzyme 8 GenBank Gene ID |
Not Available |
| Enzyme 8 GeneCard ID |
B2RBZ7  |
| Enzyme 8 GenAtlas ID |
Not Available |
| Enzyme 8 HGNC ID |
Not Available |
| Enzyme 8 Chromosome Location |
Not Available |
| Enzyme 8 Locus |
Not Available |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
Not Available |
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
13649 |
| Enzyme 9 Name |
Prostaglandin E2 receptor EP3 subtype |
| Enzyme 9 Synonyms |
- Prostanoid EP3 receptor
- PGE receptor, EP3 subtype
- PGE2-R
|
| Enzyme 9 Gene Name |
PTGER3 |
| Enzyme 9 Protein Sequence |
>Prostaglandin E2 receptor EP3 subtype
MKETRGYGGDAPFCTRLNHSYTGMWAPERSAEARGNLTRPPGSGEDCGSVSVAFPITMLL
TGFVGNALAMLLVSRSYRRRESKRKKSFLLCIGWLALTDLVGQLLTTPVVIVVYLSKQRW
EHIDPSGRLCTFFGLTMTVFGLSSLFIASAMAVERALAIRAPHWYASHMKTRATRAVLLG
VWLAVLAFALLPVLGVGQYTVQWPGTWCFISTGRGGNGTSSSHNWGNLFFASAFAFLGLL
ALTVTFSCNLATIKALVSRCRAKATASQSSAQWGRITTETAIQLMGIMCVLSVCWSPLLI
MMLKMIFNQTSVEHCKTHTEKQKECNFFLIAVRLASLNQILDPWVYLLLRKILLRKFCQI
RYHTNNYASSSTSLPCQCSSTLMWSDHLER
|
| Enzyme 9 Number of Residues |
390 |
| Enzyme 9 Molecular Weight |
43310 |
| Enzyme 9 Theoretical pI |
10.05 |
| Enzyme 9 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 9 General Function |
Not Available |
| Enzyme 9 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 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
Not Available |
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
- 54-78
92-112
132-153
176-197
228-253
284-307
328-349
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
545304  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P43115  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
PE2R3_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1167 bp
ATGAAGGAGACCCGGGGCTACGGAGGGGATGCCCCCTTCTGCACCCGCCTCAACCACTCC
TACACAGGCATGTGGGCGCCCGAGCGTTCCGCCGAGGCGCGGGGCAACCTCACGCGCCCT
CCAGGGTCTGGCGAGGATTGCGGATCGGTGTCCGTGGCCTTCCCGATCACCATGCTGCTC
ACTGGTTTCGTGGGCAACGCACTGGCCATGCTGCTCGTGTCGCGCAGCTACCGGCGCCGG
GAGAGCAAGCGCAAGAAGTCCTTCCTGCTGTGCATCGGCTGGCTGGCGCTCACCGACCTG
GTCGGGCAGCTTCTCACCACCCCGGTCGTCATCGTCGTGTACCTGTCCAAGCAGCGTTGG
GAGCACATCGACCCGTCGGGGCGGCTCTGCACCTTTTTCGGGCTGACCATGACTGTTTTC
GGGCTCTCCTCGTTGTTCATCGCCAGCGCCATGGCCGTCGAGCGGGCGCTGGCCATCAGG
GCGCCGCACTGGTATGCGAGCCACATGAAGACGCGTGCCACCCGCGCTGTGCTGCTCGGC
GTGTGGCTGGCCGTGCTCGCCTTCGCCCTGCTGCCGGTGCTGGGCGTGGGCCAGTACACC
GTCCAGTGGCCCGGGACGTGGTGCTTCATCAGCACCGGGCGAGGGGGCAACGGGACTAGC
TCTTCGCATAACTGGGGCAACCTTTTCTTCGCCTCTGCCTTTGCCTTCCTGGGGCTCTTG
GCGCTGACAGTCACCTTTTCCTGCAACCTGGCCACCATTAAGGCCCTGGTGTCCCGCTGC
CGGGCCAAGGCCACGGCATCTCAGTCCAGTGCCCAGTGGGGCCGCATCACGACCGAGACG
GCCATTCAGCTTATGGGGATCATGTGCGTGCTGTCGGTCTGCTGGTCTCCGCTCCTGATA
ATGATGTTGAAAATGATCTTCAATCAGACATCAGTTGAGCACTGCAAGACACACACGGAG
AAGCAGAAAGAATGCAACTTCTTCTTAATAGCTGTTCGCCTGGCTTCACTGAACCAGATC
TTGGATCCTTGGGTTTACCTGCTGTTAAGAAAGATCCTTCTTCGAAAGTTTTGCCAGGTA
GCAAATGCTGTCTCCAGCTGCTCTAATGATGGACAGAAAGGGCAGCCTATCTCATTATCT
AATGAAATAATACAGACAGAAGCATGA
|
| Enzyme 9 GenBank Gene ID |
S69200  |
| Enzyme 9 GeneCard ID |
P43115  |
| Enzyme 9 GenAtlas ID |
PTGER3  |
| Enzyme 9 HGNC ID |
HGNC:9595  |
| Enzyme 9 Chromosome Location |
Not Available |
| Enzyme 9 Locus |
Not Available |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
13867 |
| Enzyme 10 Name |
Prostaglandin E2 receptor EP2 subtype |
| Enzyme 10 Synonyms |
- Prostanoid EP2 receptor
- PGE receptor, EP2 subtype
|
| Enzyme 10 Gene Name |
PTGER2 |
| Enzyme 10 Protein Sequence |
>Prostaglandin E2 receptor EP2 subtype
MGNASNDSQSEDCETRQWLPPGESPAISSVMFSAGVLGNLIALALLARRWRGDVGCSAGR
RSSLSLFHVLVTELVFTDLLGTCLISPVVLASYARNQTLVALAPESRACTYFAFAMTFFS
LATMLMLFAMALERYLSIGHPYFYQRRVSRSGGLAVLPVIYAVSLLFCSLPLLDYGQYVQ
YCPGTWCFIRHGRTAYLQLYATLLLLLIVSVLACNFSVILNLIRMHRRSRRSRCGPSLGS
GRGGPGARRRGERVSMAEETDHLILLAIMTITFAVCSLPFTIFAYMNETSSRKEKWDLQA
LRFLSINSIIDPWVFAILRPPVLRLMRSVLCCRISLRTQDATQTSCSTQSDASKQADL
|
| Enzyme 10 Number of Residues |
358 |
| Enzyme 10 Molecular Weight |
39761 |
| Enzyme 10 Theoretical pI |
9.19 |
| Enzyme 10 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
- thromboxane receptor 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 10 General Function |
Not Available |
| Enzyme 10 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 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
Not Available |
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
- 24-47
66-91
112-132
152-176
199-223
263-286
300-323
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
632650  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P43116  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
PE2R2_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1077 bp
ATGGGCAATGCCTCCAATGACTCCCAGTCTGAGGACTGCGAGACGCGACAGTGGCTTCCC
CCAGGCGAAAGCCCAGCCATCAGCTCCGTCATGTTCTCGGCCGGGGTGCTGGGGAACCTC
ATAGCACTGGCGCTGCTGGCGCGCCGCTGGCGGGGGGACGTGGGGTGCAGCGCCGGCCGC
AGGAGCTCCCTCTCCTTGTTCCACGTGCTGGTGACCGAGCTGGTGTTCACCGACCTGCTC
GGGACCTGCCTCATCAGCCCAGTGGTACTGGCTTCGTACGCGCGGAACCAGACCCTGGTG
GCACTGGCGCCCGAGAGCCGCGCGTGCACCTACTTCGCTTTCGCCATGACCTTCTTCAGC
CTGGCCACGATGCTCATGCTCTTCGCCATGGCCCTGGAGCGCTACCTCTCGATCGGGCAC
CCCTACTTCTACCAGCGCCGCGTCTCGGCCTCCGGGGGCCTGGCCGTGCTGCCTGTCATC
TATGCAGTCTCCCTGCTCTTCTGCTCGCTGCCGCTGCTGGACTATGGGCAGTACGTCCAG
TACTGCCCCGGGACCTGGTGCTTCATCCGGCACGGGCGGACCGCTTACCTGCAGCTGTAC
GCCACCCTGCTGCTGCTTCTCATTGTCTCGGTGCTCGCCTGCAACTTCAGTGTCATTCTC
AACCTCATCCGCATGCACCGCCGAAGCCGGAGAAGCCGCTGCGGACCTTCCCTGGGCAGT
GGCCGGGGCGGCCCCGGGGCCCGCAGGAGAGGGGAAAGGGTGTCCATGGCGGAGGAGACG
GACCACCTCATTCTCCTGGCTATCATGACCATCACCTTCGCCGTCTGCTCCTTGCCTTTC
ACGATTTTTGCATATATGAATGAAACCTCTTCCCGAAAGGAAAAATGGGACCTCCAAGCT
CTTAGGTTTTTATCAATTAATTCAATAATTGACCCTTGGGTCTTTGCCATCCTTAGGCCT
CCTGTTCTGAGACTAATGCGTTCAGTCCTCTGTTGTCGGATTTCATTAAGAACACAAGAT
GCAACACAAACTTCCTGTTCTACACAGTCAGATGCCAGTAAACAGGCTGACCTTTGA
|
| Enzyme 10 GenBank Gene ID |
U19487  |
| Enzyme 10 GeneCard ID |
P43116  |
| Enzyme 10 GenAtlas ID |
PTGER2  |
| Enzyme 10 HGNC ID |
HGNC:9594  |
| Enzyme 10 Chromosome Location |
14 |
| Enzyme 10 Locus |
14q22 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- 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
]
- 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
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
14810 |
| Enzyme 11 Name |
Solute carrier family 22 member 7 |
| Enzyme 11 Synonyms |
Not Available |
| Enzyme 11 Gene Name |
SLC22A7 |
| Enzyme 11 Protein Sequence |
>Solute carrier family 22 member 7
MGFEELLEQVGGFGPFQLRNVALLALPRVLLPLHFLLPIFLAAVPAHRCALPGAPANFSH
QDVWLEAHLPREPDGTLSSCLRFAYPQALPNTTLGEERQSRGELEDEPATVPCSQGWEYD
HSEFSSTIATESQWDLVCEQKGLNRAASTFFFAGVLVGAVAFGYLSDRFGRRRLLLVAYV
STLVLGLASAASVSYVMFAITRTLTGSALAGFTIIVMPLELEWLDVEHRTVAGVLSSTFW
TGGVMLLALVGYLIRDWRWLLLAVTLPCAPGILSLWWVPESARWLLTQGHVKEAHRYLLH
CARLNGRPVCEDSFSQEAVSKVAAGERVVRRPSYLDLFRTPRLRHISLCCVVVWFGVNFS
YYGLSLDVSGLGLNVYQTQLLFGAVELPSKLLVYLSVRYAGRRLTQAGTLLGTALAFGTR
LLVSSDMKSWSTVLAVMGKAFSEAAFTTAYLFTSELYPTVLRQTGMGLTALVGRLGGSLA
PLAALLDGVWLSLPKLTYGGIALLAAGTALLLPETRQAQLPETIQDVERKSAPTSLQEEE
MPMKQVQN
|
| Enzyme 11 Number of Residues |
548 |
| Enzyme 11 Molecular Weight |
60026 |
| Enzyme 11 Theoretical pI |
7.03 |
| Enzyme 11 GO Classification |
| Function |
- ion transporter activity
- transporter activity
|
| Process |
- cellular physiological process
- ion transport
- physiological process
- transport
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 11 General Function |
Carbohydrate transport and metabolism |
| Enzyme 11 Specific Function |
Not Available |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
Not Available |
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
- 22-44
- 143-165
- 175-197
- 204-221
- 231-253
- 260-279
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
5001689  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q9Y694  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
Q9Y694_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 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 11 GenBank Gene ID |
AF097518  |
| Enzyme 11 GeneCard ID |
Q9Y694  |
| Enzyme 11 GenAtlas ID |
SLC22A7  |
| Enzyme 11 HGNC ID |
HGNC:10971  |
| Enzyme 11 Chromosome Location |
Not Available |
| Enzyme 11 Locus |
Not Available |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
16494 |
| Enzyme 12 Name |
cDNA FLJ32487 fis, clone SKNSH1000002, highly similar to Prostaglandin E synthase 2 (EC 5.3.99.3) |
| Enzyme 12 Synonyms |
Not Available |
| Enzyme 12 Gene Name |
Not Available |
| Enzyme 12 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 12 Number of Residues |
377 |
| Enzyme 12 Molecular Weight |
41970 |
| Enzyme 12 Theoretical pI |
9.50 |
| Enzyme 12 GO Classification |
| Function |
- electron transporter activity
- transporter activity
|
| Process |
- cell homeostasis
- cell redox homeostasis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- homeostasis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 12 General Function |
Not Available |
| Enzyme 12 Specific Function |
Not Available |
| Enzyme 12 Pathways |
Not Available |
| Enzyme 12 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] ALL_REAC R02265
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
Not Available |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
B3KPZ2  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
B3KPZ2_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
Not Available |
| Enzyme 12 GenBank Gene ID |
AK057049  |
| Enzyme 12 GeneCard ID |
B3KPZ2  |
| Enzyme 12 GenAtlas ID |
Not Available |
| Enzyme 12 HGNC ID |
Not Available |
| Enzyme 12 Chromosome Location |
Not Available |
| Enzyme 12 Locus |
Not Available |
| Enzyme 12 SNPs |
Not Available |
| Enzyme 12 General References |
Not Available |
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
17036 |
| Enzyme 13 Name |
CUG-BP- and ETR-3-like factor 2 |
| Enzyme 13 Synonyms |
- CELF-2
- Bruno-like protein 3
- RNA-binding protein BRUNOL-3
- CUG triplet repeat RNA-binding protein 2
- CUG-BP2
- ELAV-type RNA-binding protein 3
- ETR-3
- Neuroblastoma apoptosis-related RNA-binding protein
- hNAPOR
|
| Enzyme 13 Gene Name |
CUGBP2 |
| Enzyme 13 Protein Sequence |
>CUG-BP- and ETR-3-like factor 2
MRCPKSAVTMRNEELLLSNGTANKMNGALDHSDQPDPDAIKMFVGQIPRSWSEKELKELF
EPYGAVYQINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNIKTLPGMHHPIQMKP
ADSEKSNAVEDRKLFIGMVSKKCNENDIRVMFSPFGQIEECRILRGPDGLSRGCAFVTFS
TRAMAQNAIKAMHQSQTMEGCSSPIVVKFADTQKDKEQRRLQQQLAQQMQQLNTATWGNL
TGLGGLTPQYLALLQQATSSSNLGAFSGIQQMAGMNALQLQNLATLAAAAAAAQTSATST
NANPLSTTSSALGALTSPVAASTPNSTAGAAMNSLTSLGTLQGLAGATVGLNNINALAGM
AALNGGLGATGLTNGTAGTMDALTQAYSGIQQYAAAALPTLYSQSLLQQQSAAGSQKEGP
EGANLFIYHLPQEFGDQDILQMFMPFGNVISAKVFIDKQTNLSKCFGFVSYDNPVSAQAA
IQAMNGFQIGMKRLKVQLKRSKNDSKPY
|
| Enzyme 13 Number of Residues |
508 |
| Enzyme 13 Molecular Weight |
54285 |
| Enzyme 13 Theoretical pI |
9.01 |
| Enzyme 13 GO Classification |
| Function |
- RNA binding
- binding
- nucleic acid binding
- nucleotide binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 13 General Function |
Not Available |
| Enzyme 13 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 (By similarity). 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 (By similarity). Binds to an intronic RNA element responsible for the silencing of exon 21 splicing (By similarity). Binds to (CUG)n repeats (By similarity) |
| Enzyme 13 Pathways |
Not Available |
| Enzyme 13 Reactions |
Not Available |
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
Not Available |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
O95319  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
CELF2_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
Not Available |
| Enzyme 13 GenBank Gene ID |
AF090694  |
| Enzyme 13 GeneCard ID |
O95319  |
| Enzyme 13 GenAtlas ID |
CUGBP2  |
| Enzyme 13 HGNC ID |
HGNC:2550  |
| Enzyme 13 Chromosome Location |
10 |
| Enzyme 13 Locus |
10p13 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- Ladd AN, Charlet N, Cooper TA: The CELF family of RNA binding proteins is implicated in cell-specific and developmentally regulated alternative splicing. Mol Cell Biol. 2001 Feb;21(4):1285-96. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
17127 |
| Enzyme 14 Name |
cDNA, FLJ79474, highly similar to Prostaglandin E2 receptor, EP3 subtype (Prostaglandin E receptor 3 (Subtype EP3), isoform CRA_d) |
| Enzyme 14 Synonyms |
Not Available |
| Enzyme 14 Gene Name |
PTGER3 |
| Enzyme 14 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 14 Number of Residues |
390 |
| Enzyme 14 Molecular Weight |
43310 |
| Enzyme 14 Theoretical pI |
10.05 |
| Enzyme 14 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 14 General Function |
Not Available |
| Enzyme 14 Specific Function |
Not Available |
| Enzyme 14 Pathways |
Not Available |
| Enzyme 14 Reactions |
Not Available |
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
Not Available |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
B0AZN4  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
B0AZN4_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
Not Available |
| Enzyme 14 GenBank Gene ID |
AK315825  |
| Enzyme 14 GeneCard ID |
B0AZN4  |
| Enzyme 14 GenAtlas ID |
Not Available |
| Enzyme 14 HGNC ID |
Not Available |
| Enzyme 14 Chromosome Location |
Not Available |
| Enzyme 14 Locus |
Not Available |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
Not Available |
| Enzyme 14 Metabolite References |
Not Available |