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Human Metabolome Database Version 2.5

 

Showing metabocard for Thromboxane A2 (HMDB01452)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-07-28 13:56:49
Accession Number HMDB01452
Secondary Accession Numbers Not Available
Common Name Thromboxane A2
Description An unstable intermediate between the prostaglandin endoperoxides and thromboxane B2. The compound has a bicyclic oxaneoxetane structure. It is a potent inducer of platelet aggregation and causes vasoconstriction. It is the principal component of rabbit aorta contracting substance (RCS). Thromboxanes 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. (1S-(1alpha,3alpha,3R*),4beta(Z),5alpha)-7-(3-(3-hydroxy-1-octenyl)-2,6-dioxabicyclo(3.1.1)hept-4-yl)-5-Heptenoate
  2. (1S-(1alpha,3alpha,3R*),4beta(Z),5alpha)-7-(3-(3-hydroxy-1-octenyl)-2,6-dioxabicyclo(3.1.1)hept-4-yl)-5-Heptenoic acid
  3. (5Z)-7-[(1S,3R,4S,5S)-3-[(1E,3S)-3-hydroxy-1-octenyl]-2,6-dioxabicyclo[3.1.1]hept-4-yl]-5-Heptenoate
  4. (5Z)-7-[(1S,3R,4S,5S)-3-[(1E,3S)-3-hydroxy-1-octenyl]-2,6-dioxabicyclo[3.1.1]hept-4-yl]-5-Heptenoic acid
  5. (5Z,13E)-(15S)-9,11-epoxy-15-hydroxythromba-5,13-dienoate
  6. (5Z,13E)-(15S)-9-alpha,11-alpha-Epoxy-15-hydroxythromboxa-5,13-dienoate
  7. (5Z,13E)-(15S)-9a,11a-epoxy-15-Hydroxythromboxa-5,13-dienoate
  8. (5Z,13E)-(15S)-9a,11a-epoxy-15-Hydroxythromboxa-5,13-dienoic acid
  9. (5Z,13E)-(15S)-9alpha,11alpha-epoxy-15-hydroxythromboxa-5,13-dienoate
  10. (5Z,9alpha,11alpha,13E,15S)-9,11-Epoxy-15-hydroxythromboxa-5,13-dien-1-oate
  11. (5Z,9alpha,11alpha,13E,15S)-9,11-Epoxy-15-hydroxythromboxa-5,13-dien-1-oic acid
  12. (5Z,9alpha,11alpha,13E,15S)-9,11-epoxy-15-hydroxy-Thromboxa-5,13-dien-1-oate
  13. (5Z,9alpha,11alpha,13E,15S)-9,11-epoxy-15-hydroxy-Thromboxa-5,13-dien-1-oic acid
  14. 7-[3-(3-hydroxy-1-octenyl)-2,6-dioxabicyclo[3.1.1]hept-4-yl]-[1S-[1alpha,3alpha(1E,3R*),4beta(Z),5alpha]]-5-Heptenoate
  15. 7-[3-(3-hydroxy-1-octenyl)-2,6-dioxabicyclo[3.1.1]hept-4-yl]-[1S-[1alpha,3alpha(1E,3R*),4beta(Z),5alpha]]-5-Heptenoic acid
  16. 9S,11S-epoxy,15S-hydroxy-thromboxa-5Z,13E-dien-1-oate
  17. 9S,11S-epoxy,15S-hydroxy-thromboxa-5Z,13E-dien-1-oic acid
  18. RCS
  19. Rabbit aorta contracting substance
  20. TXA-2
  21. TXA2
  22. cid
  23. (5Z,13E)-(15S)-9,11-epoxy-15-hydroxythromba-5,13-dienoic acid
  24. (5Z,13E)-(15S)-9-alpha,11-alpha-Epoxy-15-hydroxythromboxa-5,13-dienoic acid
  25. (5Z,13E)-(15S)-9alpha,11alpha-epoxy-15-hydroxythromboxa-5,13-dienoic acid
Chemical IUPAC Name 7-[3-(3-hydroxyoct-1-enyl)-4,6-dioxabicyclo[3.1.1]hept-2-yl]hept-5-enoic acid
Chemical Formula C20H32O5
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Prostanoids
Sub Class
  • Thromboxanes
Family
  • Mammalian Metabolite
Species
  • acetal
  • secondary alcohol
  • carboxylic acid
  • alkene
  • heterocyclic compound
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 352.465
Monoisotopic Molecular Weight 352.224976
Isomeric SMILES CCCCC[C@H](O)C=C[C@H]1O[C@H]2C[C@H](O2)[C@@H]1CC=C/CCCC(O)=O
Canonical SMILES CCCCCC(O)C=CC1OC2CC(O2)C1CC=CCCCC(O)=O
KEGG Compound ID C02198 Link Image
BioCyc ID ALPHA11-ALPHA-EPOXY-15-HYDROXYTHROMBA Link Image
BiGG ID 39305 Link Image
Wikipedia Link Thromboxane A2 Link Image
NuGOwiki Link HMDB01452 Link Image
Metagene Link HMDB01452 Link Image
METLIN ID 6253 Link Image
PubChem Compound 42475 Link Image
PubChem Substance 5266 Link Image
ChEBI ID 15627 Link Image
CAS Registry Number 57576-52-0
InChI Identifier InChI=1/C20H32O5/c1-2-3-6-9-15(21)12-13-17-16(18-14-20(24-17)25-18)10-7-4-5-8-11-19(22)23/h4,7,12-13,15-18,20-21H,2-3,5-6,8-11,14H2,1H3,(H,22,23)/b7-4-,13-12+/t15-,16+,17+,18-,20+/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.0469 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 4.31 [Predicted by ALOGPS]; 4.2 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
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 Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Not Available
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane (Predicted from LogP)
  • Cytoplasm
  • endoplasmic reticulum
  • Extracellular
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Platelet
Smooth Muscle
Concentrations (Normal)
Biofluid Blood
Value 0.00024 +/- 0.000036 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Akimova EV: Prostacyclin and thromboxane A2 levels in children and adolescents with an inherited predisposition to coronary heart disease: a family study. Coron Artery Dis. 1994 Sep;5(9):761-5. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.00045 +/- 0.000047 uM
Age Children:1-13 yrs old
Sex Both
Condition Coronary heart disease
Comments Not Available
References
  • Akimova EV: Prostacyclin and thromboxane A2 levels in children and adolescents with an inherited predisposition to coronary heart disease: a family study. Coron Artery Dis. 1994 Sep;5(9):761-5. [PubMed Link Image]
Biofluid CSF
Value 0.0029 (0.00021-0.0136) uM
Age N/A
Sex N/A
Comments Not Available
References
  • Bogusiewicz A, Stratton SL, Ellison DA, Mock DM: Biotin accounts for less than half of all biotin and biotin metabolites in the cerebrospinal fluid of children. Am J Clin Nutr. 2008 Nov;88(5):1291-6. [PubMed Link Image]
Biofluid CSF
Value 0.00346 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Bogusiewicz A, Stratton SL, Ellison DA, Mock DM: Biotin accounts for less than half of all biotin and biotin metabolites in the cerebrospinal fluid of children. Am J Clin Nutr. 2008 Nov;88(5):1291-6. [PubMed Link Image]
Biofluid CSF
Value 0.00062 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Bogusiewicz A, Stratton SL, Ellison DA, Mock DM: Biotin accounts for less than half of all biotin and biotin metabolites in the cerebrospinal fluid of children. Am J Clin Nutr. 2008 Nov;88(5):1291-6. [PubMed Link Image]
Biofluid CSF
Value 0.00237 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Bogusiewicz A, Stratton SL, Ellison DA, Mock DM: Biotin accounts for less than half of all biotin and biotin metabolites in the cerebrospinal fluid of children. Am J Clin Nutr. 2008 Nov;88(5):1291-6. [PubMed Link Image]
Biofluid CSF
Value 0.00057 (0.0005-0.00063) uM
Age N/A
Sex N/A
Comments Not Available
References
  • Bogusiewicz A, Stratton SL, Ellison DA, Mock DM: Biotin accounts for less than half of all biotin and biotin metabolites in the cerebrospinal fluid of children. Am J Clin Nutr. 2008 Nov;88(5):1291-6. [PubMed Link Image]
Biofluid Urine
Value 0.00078 +/- 0.00035 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Hepatocellular carcinoma
Comments Not Available
References
  • Matsumata T, Yamamoto K, Shirabe K, Shimada M, Sugimachi K, Takesue F, Muto Y, Ikeda T: Urinary excretion of prostaglandins and renal function after hepatic resection. Hepatogastroenterology. 1997 May-Jun;44(15):774-8. [PubMed Link Image]
Associated Disorders
Condition References
Coronary heart disease
  • Akimova EV: Prostacyclin and thromboxane A2 levels in children and adolescents with an inherited predisposition to coronary heart disease: a family study. Coron Artery Dis. 1994 Sep;5(9):761-5. [PubMed Link Image]
Hepatocellular carcinoma
  • Matsumata T, Yamamoto K, Shirabe K, Shimada M, Sugimachi K, Takesue F, Muto Y, Ikeda T: Urinary excretion of prostaglandins and renal function after hepatic resection. Hepatogastroenterology. 1997 May-Jun;44(15):774-8. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Arachidonic Acid Metabolism SMP00075 Link Image map00590 Link Image
General References
  1. Wu X, Dev A, Leong AB: Zileuton, a 5-lipoxygenase inhibitor, increases production of thromboxane A2 and platelet aggregation in patients with asthma. Am J Hematol. 2003 Sep;74(1):23-5. [PubMed Link Image]
  2. Feldman M, Cryer B, Rushin K, Betancourt J: A comparison of every-third-day versus daily low-dose aspirin therapy on serum thromboxane concentrations in healthy men and women. Clin Appl Thromb Hemost. 2001 Jan;7(1):53-7. [PubMed Link Image]
  3. Kobayashi T, Suzuki J, Watanabe M, Suzuki S, Yoshida K, Kume K, Suzuki H: Changes in platelet calcium concentration by thromboxane A2 stimulation in patients with nephrotic syndrome of childhood. Nephron. 1997;77(3):309-14. [PubMed Link Image]
  4. Amari T, Kubo K, Kobayashi T, Sekiguchi M: Effects of recombinant human superoxide dismutase on tumor necrosis factor-induced lung injury in awake sheep. J Appl Physiol. 1993 Jun;74(6):2641-8. [PubMed Link Image]
  5. Hada S, Hashizume M, Yoshioka F, Nishii S, Yasunaga K: [Measurement of platelet thromboxane A2/prostaglandin H2 receptor in asthmatic patients] Arerugi. 1993 May;42(5):609-16. [PubMed Link Image]
  6. Cattaneo M, Lombardi R, Zighetti ML, Gachet C, Ohlmann P, Cazenave JP, Mannucci PM: Deficiency of (33P)2MeS-ADP binding sites on platelets with secretion defect, normal granule stores and normal thromboxane A2 production. Evidence that ADP potentiates platelet secretion independently of the formation of large platelet aggregates and thromboxane A2 production. Thromb Haemost. 1997 May;77(5):986-90. [PubMed Link Image]
  7. Schror K: The effect of prostaglandins and thromboxane A2 on coronary vessel tone--mechanisms of action and therapeutic implications. Eur Heart J. 1993 Nov;14 Suppl I:34-41. [PubMed Link Image]
  8. Marttunen MB, Pyrhonen S, Tiitinen AE, Viinikka LU, Ylikorkala O: Effect of antiestrogen regimen on prostacyclin and thromboxane A2 in postmenopausal patients with breast cancer: evidence of significance of hypertension, smoking or previous use of estrogen therapy. Prostaglandins. 1996 Oct;52(4):317-26. [PubMed Link Image]
  9. Tanaka K, Roberts MH, Yamamoto N, Sugiura H, Uehara M, Mao XQ, Shirakawa T, Hopkin JM: Genetic variants of the receptors for thromboxane A2 and IL-4 in atopic dermatitis. Biochem Biophys Res Commun. 2002 Apr 5;292(3):776-80. [PubMed Link Image]
  10. Leonhardt A, Bernert S, Watzer B, Schmitz-Ziegler G, Seyberth HW: Low-dose aspirin in pregnancy: maternal and neonatal aspirin concentrations and neonatal prostanoid formation. Pediatrics. 2003 Jan;111(1):e77-81. [PubMed Link Image]
  11. Sheu JR, Hsiao G, Shen MY, Lin WY, Tzeng CR: The hyperaggregability of platelets from normal pregnancy is mediated through thromboxane A2 and cyclic AMP pathways. Clin Lab Haematol. 2002 Apr;24(2):121-9. [PubMed Link Image]
  12. Djellas Y, Manganello JM, Antonakis K, Le Breton GC: Identification of Galpha13 as one of the G-proteins that couple to human platelet thromboxane A2 receptors. J Biol Chem. 1999 May 14;274(20):14325-30. [PubMed Link Image]
  13. Rocca B, Ranelletti FO, Maggiano N, Ciabattoni G, De Cristofaro R, Landolfi R: Inherited macrothrombocytopenia with distinctive platelet ultrastructural and functional features. Thromb Haemost. 2000 Jan;83(1):35-41. [PubMed Link Image]
  14. Liel N, Nathan I, Yermiyahu T, Zolotov Z, Lieberman JR, Dvilansky A, Halushka PV: Increased platelet thromboxane A2/prostaglandin H2 receptors in patients with pregnancy induced hypertension. Thromb Res. 1993 May 1;70(3):205-10. [PubMed Link Image]
  15. Modesti PA, Colella A, Cecioni I, Costoli A, Biagini D, Migliorini A, Neri Serneri GG: Increased number of thromboxane A2-prostaglandin H2 platelet receptors in active unstable angina and causative role of enhanced thrombin formation. Am Heart J. 1995 May;129(5):873-9. [PubMed Link Image]
  16. Storlien LH, Kriketos AD, Calvert GD, Baur LA, Jenkins AB: Fatty acids, triglycerides and syndromes of insulin resistance. Prostaglandins Leukot Essent Fatty Acids. 1997 Oct;57(4-5):379-85. [PubMed Link Image]
  17. Wennmalm A, Benthin G, Granstrom EF, Persson L, Winell S: Maintained hyperexcretion of thromboxane A2 metabolite in healthy young cigarette smokers: results from a prospective study in randomly sampled males with stable smoking habits. Clin Physiol. 1993 May;13(3):257-64. [PubMed Link Image]
  18. Ogawa S, Takeuchi K, Sugimura K, Sato C, Fukuda M, Lee R, Ito S, Sato T: The 5-HT2 receptor antagonist sarpogrelate reduces urinary and plasma levels of thromboxane A2 and urinary albumin excretion in non-insulin-dependent diabetes mellitus patients. Clin Exp Pharmacol Physiol. 1999 May-Jun;26(5-6):461-4. [PubMed Link Image]
  19. Michelson AD, Wencel-Drake JD, Kestin AS, Barnard MR: Platelet activation results in a redistribution of glycoprotein IV (CD36). Arterioscler Thromb. 1994 Jul;14(7):1193-201. [PubMed Link Image]
  20. Komiotis D, Wencel-Drake JD, Dieter JP, Lim CT, Le Breton GC: Labeling of human platelet plasma membrane thromboxane A2/prostaglandin H2 receptors using SQB, a novel biotinylated receptor probe. Biochem Pharmacol. 1996 Sep 13;52(5):763-70. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Thromboxane-A synthase
  2. Thromboxane A2 receptor
  3. HCG14925, isoform CRA_a
Enzyme 1 [top]
Enzyme 1 ID 6879
Enzyme 1 Name Thromboxane-A synthase
Enzyme 1 Synonyms
  1. TXA synthase
  2. TXS
  3. Cytochrome P450 5A1
Enzyme 1 Gene Name TBXAS1
Enzyme 1 Protein Sequence >Thromboxane-A synthase
MEALGFLKLEVNGPMVTVALSVALLALLKWYSTSAFSRLEKLGLRHPKPSPFIGNLTFFR
QGFWESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSV
ADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQR
CYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPRPILVLLLSFPSIMVPLA
RILPNKNRDELNGFFNKLIRNVIALRDQQAAEERRRDFLQMVLDARHSASPMGVQDFDIV
RDVFSSTGCKPNPSRQHQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATN
PDCQEKLLREVDVFKEKHMAPEFCSLEEGLPYLDMVIAETLRMYPPAFRFTREAAQDCEV
LGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCL
GVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSALGPKNGVYIKIVSR
Enzyme 1 Number of Residues 533
Enzyme 1 Molecular Weight 60517.7
Enzyme 1 Theoretical pI 7.68
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 1 General Function Involved in monooxygenase activity
Enzyme 1 Specific Function (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15- hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-9-alpha,11-alpha- epoxy-15-hydroxythromboxa-5,13-dienoate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13- dienoate = (5Z,13E)-(15S)-9alpha,11alpha-epoxy-15-hydroxythromboxa-5,13- dienoate [RN:R02268]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 11-31 76-96 224-244 336-356
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 195972896 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P24557 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name THAS_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1605 bp
ATGATGGAAGCCTTGGGGTTTCTAAAATTGGAAGTGAATGGCCCCATGGTGACGGTGGCC
CTGTCAGTGGCTCTCTTGGCCCTCCTGAAATGGTACTCCACATCAGCATTCTCAAGACTG
GAGAAGTTAGGCCTCAGACATCCCAAGCCTTCTCCTTTCATTGGAAACTTGACATTTTTC
CGCCAGGGTTTTTGGGAAAGCCAAATGGAGCTCAGAAAGCTGTATGGACCTCTGTGTGGG
TACTATCTTGGTCGTCGGATGTTTATTGTTATTTCTGAGCCAGACATGATCAAGCAGGTG
TTGGTTGAGAACTTCAGTAACTTTACCAACAGAATGGCGTCGGGTTTGGAGTTCAAGTCG
GTAGCCGACAGCGTTCTGTTTTTACGTGACAAAAGATGGGAAGAGGTCAGAGGTGCCCTG
ATGTCTGCTTTCAGTCCTGAAAAGCTGAACGAGATGGTTCCCCTCATCAGCCAAGCCTGC
GACCTTCTCCTGGCTCATTTAAAACGCTATGCGGAATCTGGGGACGCATTTGACATCCAG
AGGTGCTACTGCAATTACACCACAGATGTGGTTGCCAGCGTCGCCTTTGGCACCCCGGTG
GACTCCTGGCAGGCCCCTGAGGATCCCTTTGTGAAACACTGCAAGCGTTTCTTCGAATTC
TGCATCCCCAGACCTATCCTGGTTTTACTCTTATCATTTCCATCCATAATGGTCCCACTG
GCCCGGATTTTGCCCAATAAGAACCGAGACGAACTGAATGGCTTTTTTAACAAACTCATT
AGGAATGTGATTGCCTTGCGGGACCAGCAAGCTGCCGAAGAGAGGCGGAGAGACTTCCTC
CAAATGGTCCTGGATGCCCGACATTCTGCAAGTCCCATGGGCGTGCAAGACTTTGACATC
GTCAGAGACGTTTTCTCCTCTACTGGGTGCAAGCCGAACCCTTCCCGGCAACACCAGCCC
AGCCCTATGGCCAGGCCTTTGACTGTGGATGAGATTGTGGGCCAGGCCTTCATCTTCCTC
ATCGCTGGCTATGAAATCATCACCAACACACTTTCTTTTGCCACCTACCTACTGGCCACC
AACCCTGACTGCCAAGAGAAGCTTCTGAGAGAGGTAGACGTTTTTAAGGAGAAACACATG
GCCCCTGAGTTCTGCAGCCTCGAGGAAGGCCTGCCCTATCTGGACATGGTGATTGCAGAG
ACGCTGAGGATGTACCCGCCAGCTTTCAGATTCACACGGGAGGCAGCTCAGGACTGCGAG
GTGCTGGGGCAGCGCATCCCCGCAGGCGCTGTGCTAGAGATGGCCGTGGGTGCCCTGCAC
CATGACCCTGAGCACTGGCCAAGCCCGGAGACCTTCAACCCTGAAAGGTTCACGGCTGAG
GCCCGGCAGCAGCACCGGCCCTTCACGTACCTGCCCTTCGGGGCCGGCCCACGGAGCTGC
CTCGGGGTGCGTCTAGGGCTGCTTGAGGTCAAGTTGACACTGCTCCACGTGCTGCACAAG
TTCCGGTTCCAAGCCTGCCCTGAGACCCAGGTACCGCTGCAGCTAGAATCCAAATCTGCC
CTAGGTCCAAAAAATGGTGTCTATATCAAGATCGTATCCCGCTGA
Enzyme 1 GenBank Gene ID NM_001130966 Link Image
Enzyme 1 GeneCard ID TBXAS1 Link Image
Enzyme 1 GenAtlas ID TBXAS1 Link Image
Enzyme 1 HGNC ID HGNC:11609 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7q34-q35
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Yokoyama C, Miyata A, Ihara H, Ullrich V, Tanabe T: Molecular cloning of human platelet thromboxane A synthase. Biochem Biophys Res Commun. 1991 Aug 15;178(3):1479-84. [PubMed Link Image]
  2. Ohashi K, Ruan KH, Kulmacz RJ, Wu KK, Wang LH: Primary structure of human thromboxane synthase determined from the cDNA sequence. J Biol Chem. 1992 Jan 15;267(2):789-93. [PubMed Link Image]
  3. Miyata A, Yokoyama C, Ihara H, Bandoh S, Takeda O, Takahashi E, Tanabe T: Characterization of the human gene (TBXAS1) encoding thromboxane synthase. Eur J Biochem. 1994 Sep 1;224(2):273-9. [PubMed Link Image]
  4. Chevalier D, Lo-Guidice JM, Sergent E, Allorge D, Debuysere H, Ferrari N, Libersa C, Lhermitte M, Broly F: Identification of genetic variants in the human thromboxane synthase gene (CYP5A1). Mutat Res. 2001 Jan;432(3-4):61-7. [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. Wang LH, Ohashi K, Wu KK: Isolation of partial complementary DNA encoding human thromboxane synthase. Biochem Biophys Res Commun. 1991 May 31;177(1):286-91. [PubMed Link Image]
  7. Nusing R, Schneider-Voss S, Ullrich V: Immunoaffinity purification of human thromboxane synthase. Arch Biochem Biophys. 1990 Aug 1;280(2):325-30. [PubMed Link Image]
  8. Ruan KH, Wang LH, Wu KK, Kulmacz RJ: Amino-terminal topology of thromboxane synthase in the endoplasmic reticulum. J Biol Chem. 1993 Sep 15;268(26):19483-90. [PubMed Link Image]
  9. Mestel F, Oetliker O, Beck E, Felix R, Imbach P, Wagner HP: Severe bleeding associated with defective thromboxane synthetase. Lancet. 1980 Jan 19;1(8160):157. [PubMed Link Image]
  10. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  11. Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed Link Image]
  12. Saito S, Iida A, Sekine A, Kawauchi S, Higuchi S, Ogawa C, Nakamura Y: Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population. J Hum Genet. 2003;48(5):249-70. Epub 2003 Apr 29. [PubMed Link Image]
  13. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
  14. Genevieve D, Proulle V, Isidor B, Bellais S, Serre V, Djouadi F, Picard C, Vignon-Savoye C, Bader-Meunier B, Blanche S, de Vernejoul MC, Legeai-Mallet L, Fischer AM, Le Merrer M, Dreyfus M, Gaussem P, Munnich A, Cormier-Daire V: Thromboxane synthase mutations in an increased bone density disorder (Ghosal syndrome). Nat Genet. 2008 Mar;40(3):284-6. Epub 2008 Feb 10. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 7481
Enzyme 2 Name Thromboxane A2 receptor
Enzyme 2 Synonyms
  1. TXA2-R
  2. Prostanoid TP receptor
Enzyme 2 Gene Name TBXA2R
Enzyme 2 Protein Sequence >Thromboxane A2 receptor
MWPNGSSLGPCFRPTNITLEERRLIASPWFAASFCVVGLASNLLALSVLAGARQGGSHTR
SSFLTFLCGLVLTDFLGLLVTGTIVVSQHAALFEWHAVDPGCRLCRFMGVVMIFFGLSPL
LLGAAMASERYLGITRPFSRPAVASQRRAWATVGLVWAAALALGLLPLLGVGRYTVQYPG
SWCFLTLGAESGDVAFGLLFSMLGGLSVGLSFLLNTVSVATLCHVYHGQEAAQQRPRDSE
VEMMAQLLGIMVVASVCWLPLLVFIAQTVLRNPPAMSPAGQLSRTTEKELLIYLRVATWN
QILDPWVYILFRRAVLRRLQPRLSTRPRSLSLQPQLTQRSGLQ
Enzyme 2 Number of Residues 343
Enzyme 2 Molecular Weight 37430.7
Enzyme 2 Theoretical pI 10.09
Enzyme 2 GO Classification
Function
  • G-protein coupled receptor activity
  • icosanoid receptor activity
  • molecular transducer activity
  • prostanoid receptor activity
  • receptor activity
  • signal transducer activity
  • thromboxane receptor 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 2 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 2 Specific Function Receptor for thromboxane A2 (TXA2), a potent stimulator of platelet aggregation. The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system. In the kidney, the binding of TXA2 to glomerular TP receptors causes intense vasoconstriction. Activates phospholipase C. Isoform 1 activates adenylyl cyclase. Isoform 2 inhibits adenylyl cyclase
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 30-52 67-87 107-128 150-172 194-219 247-270 290-311
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID P21731 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name TA2R_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1032 bp
ATGTGGCCCAACGGCAGTTCCCTGGGGCCCTGTTTCCGGCCCACAAACATTACCCTGGAG
GAGAGACGGCTGATCGCCTCGCCCTGGTTCGCCGCCTCCTTCTGCGTGGTGGGCCTGGCC
TCCAACCTGCTGGCCCTGAGCGTGCTGGCGGGCGCGCGGCAGGGGGGTTCGCACACGCGC
TCCTCCTTCCTCACCTTCCTCTGCGGCCTCGTCCTCACCGACTTCCTGGGGCTGCTGGTG
ACCGGTACCATCGTGGTGTCCCAGCACGCCGCGCTCTTCGAGTGGCACGCCGTGGACCCT
GGCTGCCGTCTCTGTCGCTTCATGGGCGTCGTCATGATCTTCTTCGGCCTGTCCCCGCTG
CTGCTGGGGGCCGCCATGGCCTCAGAGCGCTACCTGGGTATCACCCGGCCCTTCTCGCGC
CCGGCGGTCGCCTCGCAGCGCCGCGCCTGGGCCACCGTGGGGCTGGTGTGGGCGGCCGCG
CTGGCGCTGGGCCTGCTGCCCCTGCTGGGCGTGGGTCGCTACACCGTGCAATACCCGGGG
TCCTGGTGCTTCCTGACGCTGGGCGCCGAGTCCGGGGACGTGGCCTTCGGGCTGCTCTTC
TCCATGCTGGGCGGCCTCTCGGTCGGGCTGTCCTTCCTGCTGAACACGGTCAGCGTGGCC
ACCCTGTGCCACGTCTACCACGGGCAGGAGGCGGCCCAGCAGCGTCCCCGGGACTCCGAG
GTGGAGATGATGGCTCAGCTCCTGGGGATCATGGTGGTGGCCAGCGTGTGTTGGCTGCCC
CTTCTGGTCTTCATTGCCCAGACAGTGCTGCGAAACCCGCCTGCCATGAGCCCCGCCGGG
CAGCTGTCCCGCACCACGGAGAAGGAGCTGCTCATCTACTTGCGCGTGGCCACCTGGAAC
CAGATCCTGGACCCCTGGGTGTATATCCTGTTCCGCCGCGCCGTGCTCCGGCGTCTCCAG
CCTCGCCTCAGCACCCGGCCCAGGTCGCTGTCCCTCCAGCCCCAGCTCACGCAGCGCTCC
GGGCTGCAGTAG
Enzyme 2 GenBank Gene ID D38081 Link Image
Enzyme 2 GeneCard ID TBXA2R Link Image
Enzyme 2 GenAtlas ID TBXA2R Link Image
Enzyme 2 HGNC ID HGNC:11608 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 19p13.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Hirata M, Hayashi Y, Ushikubi F, Yokota Y, Kageyama R, Nakanishi S, Narumiya S: Cloning and expression of cDNA for a human thromboxane A2 receptor. Nature. 1991 Feb 14;349(6310):617-20. [PubMed Link Image]
  2. Nusing RM, Hirata M, Kakizuka A, Eki T, Ozawa K, Narumiya S: Characterization and chromosomal mapping of the human thromboxane A2 receptor gene. J Biol Chem. 1993 Nov 25;268(33):25253-9. [PubMed Link Image]
  3. Raychowdhury MK, Yukawa M, Collins LJ, McGrail SH, Kent KC, Ware JA: Alternative splicing produces a divergent cytoplasmic tail in the human endothelial thromboxane A2 receptor. J Biol Chem. 1994 Jul 29;269(30):19256-61. [PubMed Link Image]
  4. Raychowdhury MK, Yukawa M, Collins LJ, McGrail SH, Kent KC, Ware JA: Alternative splicing produces a divergent cytoplasmic tail in the human endothelial thromboxane A2 receptor. J Biol Chem. 1995 Mar 24;270(12):7011. [PubMed Link Image]
  5. D'Angelo DD, Davis MG, Ali S, Dorn GW 2nd: Cloning and pharmacologic characterization of a thromboxane A2 receptor from K562 (human chronic myelogenous leukemia) cells. J Pharmacol Exp Ther. 1994 Nov;271(2):1034-41. [PubMed Link Image]
  6. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [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. Hirata T, Ushikubi F, Kakizuka A, Okuma M, Narumiya S: Two thromboxane A2 receptor isoforms in human platelets. Opposite coupling to adenylyl cyclase with different sensitivity to Arg60 to Leu mutation. J Clin Invest. 1996 Feb 15;97(4):949-56. [PubMed Link Image]
  9. Funk CD, Furci L, Moran N, Fitzgerald GA: Point mutation in the seventh hydrophobic domain of the human thromboxane A2 receptor allows discrimination between agonist and antagonist binding sites. Mol Pharmacol. 1993 Nov;44(5):934-9. [PubMed Link Image]
  10. Sasaki M, Sukegawa J, Miyosawa K, Yanagisawa T, Ohkubo S, Nakahata N: Low expression of cell-surface thromboxane A2 receptor beta-isoform through the negative regulation of its membrane traffic by proteasomes. Prostaglandins Other Lipid Mediat. 2007 Jun;83(4):237-49. Epub 2006 Dec 27. [PubMed Link Image]
  11. Tokue S, Sasaki M, Nakahata N: Thromboxane A2-induced signal transduction is negatively regulated by KIAA1005 that directly interacts with thromboxane A2 receptor. Prostaglandins Other Lipid Mediat. 2009 Jun;89(1-2):8-15. Epub 2009 Feb 13. [PubMed Link Image]
  12. Hirata T, Kakizuka A, Ushikubi F, Fuse I, Okuma M, Narumiya S: Arg60 to Leu mutation of the human thromboxane A2 receptor in a dominantly inherited bleeding disorder. J Clin Invest. 1994 Oct;94(4):1662-7. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 12988
Enzyme 3 Name HCG14925, isoform CRA_a
Enzyme 3 Synonyms
  1. SubName: Thromboxane A synthase 1 (Platelet, cytochrome P450, family 5, subfamily A) isoform TXS-I variant
Enzyme 3 Gene Name Not Available
Enzyme 3 Protein Sequence >HCG14925, isoform CRA_a
MMEALGFLKLEVNGPMVTVALSVALLALLKWYSTSAFSRLEKLGLRHPKPSPFIGNLTFF
RQGFWESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKS
VADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQ
RCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPRPILVLLLSFPSIMVPL
ARILPNKNRDELNGFFNKLIRNVIALRDQQAAEERRRDFLQMVLDARHSASPMGVQDFDI
VRDVFSSTGCKPNPSRQHQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLAT
NPDCQEKLLREVDVFKEKHMAPEFCSLEEGLPYLDMVIAETLRMYPPAFRFTREAAQDCE
VLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSC
LGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSALGPKNGVYIKIVSR
Enzyme 3 Number of Residues 534
Enzyme 3 Molecular Weight 60648.9
Enzyme 3 Theoretical pI 7.68
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 3 General Function Involved in monooxygenase activity
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 62898664 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q53F23 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name Q53F23_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1605 bp
ATGATGGAAGCCTTGGGGTTTCTAAAATTGGAAGTGAATGGCCCCATGGTGACGGTGGCC
CTGTCAGTGGCTCTCTTGGCCCTCCTGAAATGGTACTCCACATCAGCATTCTCAAGACTG
GAGAAGTTAGGCCTCAGACATCCCAAGCCTTCTCCTTTCATTGGAAACTTGACATTTTTC
CGCCAGGGTTTTTGGGAAAGCCAAATGGAGCTCAGAAAGCTGTATGGACCTCTGTGTGGG
TACTATCTTGGTCGTCGGATGTTTATTGTTATTTCTGAGCCAGACATGATCAAGCAGGTG
TTGGTTGAGAACTTCAGTAACTTTACCAACAGAATGGCGTCGGGTTTGGAGTTCAAGTCG
GTAGCCGACAGCGTTCTGTTTTTACGTGACAAAAGATGGGAAGAGGTCAGAGGTGCCCTG
ATGTCTGCTTTCAGTCCTGAAAAGCTGAACGAGATGGTTCCCCTCATCAGCCAAGCCTGC
GACCTTCTCCTGGCTCATTTAAAACGCTATGCGGAATCTGGGGACGCATTTGACATCCAG
AGGTGCTACTGCAATTACACCACAGATGTGGTTGCCAGCGTCGCCTTTGGCACCCCGGTG
GACTCCTGGCAGGCCCCTGAGGATCCCTTTGTGAAACACTGCAAGCGTTTCTTCGAATTC
TGCATCCCCAGACCTATCCTGGTTTTACTCTTATCATTTCCATCCATAATGGTCCCACTG
GCCCGGATTTTGCCCAATAAGAACCGAGACGAACTGAATGGCTTTTTTAACAAACTCATT
AGGAATGTGATTGCCTTGCGGGACCAGCAAGCTGCCGAAGAGAGGCGGAGAGACTTCCTC
CAAATGGTCCTGGATGCCCGACATTCTGCAAGTCCCATGGGCGTGCAAGACTTTGACATC
GTCAGAGACGTTTTCTCCTCTACTGGGTGCAAGCCGAACCCTTCCCGGCAACACCAGCCC
AGCCCTATGGCCAGGCCTTTGACTGTGGATGAGATTGTGGGCCAGGCCTTCATCTTCCTC
ATCGCTGGCTATGAAATCATCACCAACACACTTTCTTTTGCCACCTACCTACTGGCCACC
AACCCTGACTGCCAAGAGAAGCTTCTGAGAGAGGTAGACGTTTTTAAGGAGAAACACATG
GCCCCTGAGTTCTGCAGCCTCGAGGAAGGCCTGCCCTATCTGGACATGGTGATTGCAGAG
ACGCTGAGGATGTACCCGCCAGCTTTCAGATTCACACGGGAGGCAGCTCAGGACTGCGAG
GTGCTGGGGCAGCGCATCCCCGCAGGCGCTGTGCTAGAGATGGCCGTGGGTGCCCTGCAC
CATGACCCTGAGCACTGGCCAAGCCCGGAGACCTTCAACCCTGAAAGGTTCACGGCTGAG
GCCCGGCAGCAGCACCGGCCCTTCACGTACCTGCCCTTCGGGGCCGGCCCACGGAGCTGC
CTCGGGGTGCGTCTAGGGCTGCTTGAGGTCAAGTTGACACTGCTCCACGTGCTGCACAAG
TTCCGGTTCCAAGCCTGCCCTGAGACCCAGGTACCGCTGCAGCTAGAATCCAAATCTGCC
CTAGGTCCAAAAAATGGTGTCTATATCAAGATCGTATCCCGCTGA
Enzyme 3 GenBank Gene ID AK223466 Link Image
Enzyme 3 GeneCard ID Not Available
Enzyme 3 GenAtlas ID hCG_14925 Link Image
Enzyme 3 HGNC ID HGNC:11609 Link Image
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs Not Available
Enzyme 3 General References
  1. Maruyama K, Sugano S: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994 Jan 28;138(1-2):171-4. [PubMed Link Image]
  2. Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997 Oct 24;200(1-2):149-56. [PubMed Link Image]
  3. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available