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Human Metabolome Database Version 2.5

 

Showing metabocard for Uracil (HMDB00300)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-12 13:44:00
Accession Number HMDB00300
Secondary Accession Numbers Not Available
Common Name Uracil
Description Uracil is a common naturally occurring pyrimidine found in RNA, it base pairs with adenine and is replaced by thymine in DNA. Methylation of uracil produces thymine. Uracil's use in the body is to help carry out the synthesis of many enzymes necessary for cell function through bonding with riboses and phosphates. Uracil serves as allosteric regulator and coenzyme for many important biochemical reactions. UDP and UTP regulate CPSase II activity in animals. UDP-glucose regulates the conversion of glucose to galactose in the liver and other tissues in the process of carbohydrate metabolism. Uracil is also involved in the biosynthesis of polysaccharides and the transportation of sugars containing aldehydes
Synonyms
  1. 2,4-Dihydroxypyrimidine
  2. 2,4-Dioxopyrimidine
  3. 2,4-Pyrimidinediol
  4. 2,4-Pyrimidinedione
  5. Hybar X
  6. Pirod
  7. Pyrod
  8. Uracil
Chemical IUPAC Name 2,4(1H,3H)-Pyrimidinedione
Chemical Formula C4H4N2O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Pyrimidines and Derivatives
Sub Class
  • Hydroxy pyrimidines
Family
  • Mammalian Metabolite
Species
  • oxo(het)arene
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of beta-Alanine metabolism
  • Component of Pantothenate and CoA biosynthesis
  • Component of Pyrimidine metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 112.087
Monoisotopic Molecular Weight 112.027275
Isomeric SMILES O=C1NC=CC(=O)N1
Canonical SMILES O=C1NC=CC(=O)N1
KEGG Compound ID C00106 Link Image
BioCyc ID URACIL Link Image
BiGG ID 33879 Link Image
Wikipedia Link Uracil Link Image
NuGOwiki Link HMDB00300 Link Image
Metagene Link HMDB00300 Link Image
METLIN ID 258 Link Image
PubChem Compound 1174 Link Image
PubChem Substance 6912247 Link Image
ChEBI ID 17568 Link Image
CAS Registry Number 66-22-8
InChI Identifier InChI=1/C4H4N2O2/c7-3-1-2-5-4(8)6-3/h1-2H,(H2,5,6,7,8)
Synthesis Reference Burckhalter, J. H.; Scarborough, Homer C. The synthesis of uracils as anticonvulsants. Journal of the American Pharmaceutical Association (1912-1977) (1955), 44 545-50.
Melting Point (Experimental) 330 oC
Experimental Water Solubility 3.6 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 26.5 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -1.07 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -1.20 [Predicted by ALOGPS]; -0.9 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1BD4 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • Extracellular
Biofluid Location
  • Amniotic Fluid
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
All Tissues —
Concentrations (Normal)
Biofluid Amniotic Fluid
Value 0.87 +/- 0.69 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid Blood
Value 0.17 (0.097-0.26) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Jiang H, Jiang J, Hu P, Hu Y: Measurement of endogenous uracil and dihydrouracil in plasma and urine of normal subjects by liquid chromatography-tandem mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2002 Mar 25;769(1):169-76. [PubMed Link Image]
Biofluid Blood
Value 2.10 +/- 1.02 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid CSF
Value 0.1 +/- 0.2 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • van Kuilenburg AB, Meinsma R, Beke E, Assmann B, Ribes A, Lorente I, Busch R, Mayatepek E, Abeling NG, van Cruchten A, Stroomer AE, van Lenthe H, Zoetekouw L, Kulik W, Hoffmann GF, Voit T, Wevers RA, Rutsch F, van Gennip AH: beta-Ureidopropionase deficiency: an inborn error of pyrimidine degradation associated with neurological abnormalities. Hum Mol Genet. 2004 Nov 15;13(22):2793-801. Epub 2004 Sep 22. [PubMed Link Image]
Biofluid Urine
Value 4.99 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Hofmann U, Schwab M, Seefried S, Marx C, Zanger UM, Eichelbaum M, Murdter TE: Sensitive method for the quantification of urinary pyrimidine metabolites in healthy adults by gas chromatography-tandem mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2003 Jul 5;791(1-2):371-80. [PubMed Link Image]
Biofluid Urine
Value 10.13 +/- 5.43 umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid Urine
Value 6.81 +/- 5.09 umol/mmol creatinine
Age Adolescent:13-18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid Urine
Value 12.29 +/- 5.78 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid Urine
Value 2.5 (2.37-3.5) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
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 12.0 (2.0-22.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Biofluid Urine
Value 12.0 (2.0-22.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Concentrations (Abnormal)
Biofluid Blood
Value 2.25 +/- 0.98 uM
Age Adult:>18 yrs old
Sex Both
Condition Canavan disease
Comments Not Available
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid Urine
Value 20.24 +/- 7.24 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Canavan disease
Comments Not Available
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid Urine
Value 35.0 (20.0-50.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Argininemia
Comments Not Available
References
Biofluid Urine
Value 265.0 (30.0-500.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
Biofluid Urine
Value 100.0 (50.0-150.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Dihydropyrimidine dehydrogenase deficiency
Comments Not Available
References
Biofluid Urine
Value 6.00 +/- 4.00 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Hypertension
Comments Not Available
References
  • Hayashi K, Kidouchi K, Sumi S, Mizokami M, Orito E, Kumada K, Ueda R, Wada Y: Possible prediction of adverse reactions to pyrimidine chemotherapy from urinary pyrimidine levels and a case of asymptomatic adult dihydropyrimidinuria. Clin Cancer Res. 1996 Dec;2(12):1937-41. [PubMed Link Image]
Biofluid Urine
Value 5.00 +/- 4.00 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
  • Hayashi K, Kidouchi K, Sumi S, Mizokami M, Orito E, Kumada K, Ueda R, Wada Y: Possible prediction of adverse reactions to pyrimidine chemotherapy from urinary pyrimidine levels and a case of asymptomatic adult dihydropyrimidinuria. Clin Cancer Res. 1996 Dec;2(12):1937-41. [PubMed Link Image]
Biofluid Urine
Value 8.00 +/- 13.00 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
  • Hayashi K, Kidouchi K, Sumi S, Mizokami M, Orito E, Kumada K, Ueda R, Wada Y: Possible prediction of adverse reactions to pyrimidine chemotherapy from urinary pyrimidine levels and a case of asymptomatic adult dihydropyrimidinuria. Clin Cancer Res. 1996 Dec;2(12):1937-41. [PubMed Link Image]
Biofluid Urine
Value 7.00 +/- 6.00 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
  • Hayashi K, Kidouchi K, Sumi S, Mizokami M, Orito E, Kumada K, Ueda R, Wada Y: Possible prediction of adverse reactions to pyrimidine chemotherapy from urinary pyrimidine levels and a case of asymptomatic adult dihydropyrimidinuria. Clin Cancer Res. 1996 Dec;2(12):1937-41. [PubMed Link Image]
Biofluid Urine
Value 6.6 +/- 2.5 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
  • Hayashi K, Kidouchi K, Sumi S, Mizokami M, Orito E, Kumada K, Ueda R, Wada Y: Possible prediction of adverse reactions to pyrimidine chemotherapy from urinary pyrimidine levels and a case of asymptomatic adult dihydropyrimidinuria. Clin Cancer Res. 1996 Dec;2(12):1937-41. [PubMed Link Image]
Associated Disorders
Condition References
Argininemia
Canavan disease
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Dihydropyrimidine dehydrogenase deficiency
Hypertension
  • Hayashi K, Kidouchi K, Sumi S, Mizokami M, Orito E, Kumada K, Ueda R, Wada Y: Possible prediction of adverse reactions to pyrimidine chemotherapy from urinary pyrimidine levels and a case of asymptomatic adult dihydropyrimidinuria. Clin Cancer Res. 1996 Dec;2(12):1937-41. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Beta-Alanine Metabolism SMP00007 Link Image map00410 Link Image
Pyrimidine Metabolism SMP00046 Link Image map00240 Link Image
General References
  1. Spector T, Harrington JA, Porter DJ: 5-Ethynyluracil (776C85): inactivation of dihydropyrimidine dehydrogenase in vivo. Biochem Pharmacol. 1993 Dec 14;46(12):2243-8. [PubMed Link Image]
  2. Hofmann U, Schwab M, Seefried S, Marx C, Zanger UM, Eichelbaum M, Murdter TE: Sensitive method for the quantification of urinary pyrimidine metabolites in healthy adults by gas chromatography-tandem mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2003 Jul 5;791(1-2):371-80. [PubMed Link Image]
  3. Mani S, Kugler JW, Sciortino DF, Garcia JC, Ansari RH, Humerickhouse R, Michelassi F, Posner MC, Shulman KL, Schilsky RL, List M, Vokes EE, Benner S: Phase II trial of uracil/tegafur (UFT) plus leucovorin in patients with advanced pancreatic carcinoma: a University of Chicago phase II consortium study. Ann Oncol. 1998 Sep;9(9):1035-7. [PubMed Link Image]
  4. Tomita T, Tajima T, Ishibashi M, Tagaya N, Aoki H, Itoh S, Kadowaki A, Kogure H, Tajima Y: [Study on the concentrations of 5-fluorouracil (5-FU), tegafur (ET) and uracil in bile: comparison of UFT or FT] Gan To Kagaku Ryoho. 1989 Dec;16(12):3755-62. [PubMed Link Image]
  5. Duthie SJ, McMillan P: Uracil misincorporation in human DNA detected using single cell gel electrophoresis. Carcinogenesis. 1997 Sep;18(9):1709-14. [PubMed Link Image]
  6. Bayer AS, Galpin JE, Theofilopoulos AN, Guze LB: Neurological disease associated with Mycoplasma pneumoniae pneumonitis: demonstration of viable Mycoplasma pneumoniae in cerebrospinal fluid and blood by radioisotopic and immunofluorescent tissue culture techniques. Ann Intern Med. 1981 Jan;94(1):15-20. [PubMed Link Image]
  7. Feliu J, Mel R, Borrega P, Lopez Gomez L, Escudero P, Dorta J, Castro J, Vazquez-Estevez SE, Bolanos M, Espinosa E, Gonzalez Baron M: Phase II study of a fixed dose-rate infusion of gemcitabine associated with uracil/tegafur in advanced carcinoma of the pancreas. Ann Oncol. 2002 Nov;13(11):1756-62. [PubMed Link Image]
  8. Jakobs C, Sweetman L, Nyhan WL, Gruenke L, Craig JC, Wadman SK: Stable isotope dilution analysis of orotic acid and uracil in amniotic fluid. Clin Chim Acta. 1984 Nov 15;143(2):123-33. [PubMed Link Image]
  9. van Lenthe H, van Kuilenburg AB, Ito T, Bootsma AH, van Cruchten A, Wada Y, van Gennip AH: Defects in pyrimidine degradation identified by HPLC-electrospray tandem mass spectrometry of urine specimens or urine-soaked filter paper strips. Clin Chem. 2000 Dec;46(12):1916-22. [PubMed Link Image]
  10. Mashiyama ST, Courtemanche C, Elson-Schwab I, Crott J, Lee BL, Ong CN, Fenech M, Ames BN: Uracil in DNA, determined by an improved assay, is increased when deoxynucleosides are added to folate-deficient cultured human lymphocytes. Anal Biochem. 2004 Jul 1;330(1):58-69. [PubMed Link Image]
  11. DeAngelis LM, Kreis W, Chan K, Dantis E, Akerman S: Pharmacokinetics of ara-C and ara-U in plasma and CSF after high-dose administration of cytosine arabinoside. Cancer Chemother Pharmacol. 1992;29(3):173-7. [PubMed Link Image]
  12. Stover PJ, Garza C: Bringing individuality to public health recommendations. J Nutr. 2002 Aug;132(8 Suppl):2476S-2480S. [PubMed Link Image]
  13. Sweatman BC, Farrant RD, Holmes E, Ghauri FY, Nicholson JK, Lindon JC: 600 MHz 1H-NMR spectroscopy of human cerebrospinal fluid: effects of sample manipulation and assignment of resonances. J Pharm Biomed Anal. 1993 Aug;11(8):651-64. [PubMed Link Image]
  14. Allgayer H, Kolb M, Stuber V, Kruis W: Effects of bile acids on base hydroxylation in a model of human colonic mucosal DNA. Cancer Detect Prev. 2002;26(1):85-9. [PubMed Link Image]
  15. Duthie SJ, Hawdon A: DNA instability (strand breakage, uracil misincorporation, and defective repair) is increased by folic acid depletion in human lymphocytes in vitro. FASEB J. 1998 Nov;12(14):1491-7. [PubMed Link Image]
  16. van Kuilenburg AB, van Lenthe H, Loffler M, van Gennip AH: Analysis of pyrimidine synthesis "de novo" intermediates in urine and dried urine filter- paper strips with HPLC-electrospray tandem mass spectrometry. Clin Chem. 2004 Nov;50(11):2117-24. Epub 2004 Sep 16. [PubMed Link Image]
  17. Hanaue H, Kurosawa T, Kitano Y, Miyakawa S, Nemoto A, Yamamoto H, Asagoe T, Takada T, Yasuda H, Shikata J: Anticancer drug distribution in lymph and blood during adjuvant chemotherapy after surgery for gastric carcinoma. A study with a combined preparation of 1-(2-tetrahydrofuryl)-5-fluorouracil and uracil. Cancer. 1987 May 1;59(9):1571-6. [PubMed Link Image]
  18. Jiang H, Jiang J, Hu P, Hu Y: Measurement of endogenous uracil and dihydrouracil in plasma and urine of normal subjects by liquid chromatography-tandem mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2002 Mar 25;769(1):169-76. [PubMed Link Image]
  19. Wikipedia Link Image
Metabolic Enzymes
  1. Uridine phosphorylase 1
  2. Uridine phosphorylase 2
  3. Purine nucleoside phosphorylase
  4. Thymidine phosphorylase precursor
  5. Dihydropyrimidine dehydrogenase [NADP+] precursor
  6. cDNA FLJ77390 (Putative uncharacterized protein RP11-311P8.3)
  7. cDNA, FLJ95575, highly similar to Homo sapiens endothelial cell growth factor 1 (platelet-derived) (ECGF1), mRNA
  8. Uracil phosphoribosyltransferase
  9. Uracil nucleotide/cysteinyl leukotriene receptor
Enzyme 1 [top]
Enzyme 1 ID 5801
Enzyme 1 Name Uridine phosphorylase 1
Enzyme 1 Synonyms
  1. UrdPase 1
  2. UPase 1
Enzyme 1 Gene Name UPP1
Enzyme 1 Protein Sequence >Uridine phosphorylase 1 
MAATGANAEKAESHNDCPVRLLNPNIAKMKEDILYHFNLTTSRHNFPALFGDVKFVCVGG
SPSRMKAFIRCVGAELGLDCPGRDYPNICAGTDRYAMYKVGPVLSVSHGMGIPSISIMLH
ELIKLLYYARCSNVTIIRIGTSGGIGLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKT
DLNKKLVQELLLCSAELSEFTTVVGNTMCTLDFYEGQGRLDGALCSYTEKDKQAYLEAAY
AAGVRNIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDQISSPRNVLSEYQQRPQRLVS
YFIKKKLSKA
Enzyme 1 Number of Residues 310
Enzyme 1 Molecular Weight 33935
Enzyme 1 Theoretical pI 7.95
Enzyme 1 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
  • uridine phosphorylase activity
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside metabolism
  • nucleotide catabolism
  • nucleotide metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 1 General Function Nucleotide transport and metabolism
Enzyme 1 Specific Function Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1- phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis
Enzyme 1 Pathways
Enzyme 1 Reactions
  • uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1050525 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q16831 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name UPP1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >933 bp 
ATGGCGGCCACGGGAGCCAATGCAGAGAAAGCTGAAAGTCACAATGATTGCCCCGTCAGA
CTTTTAAATCCAAACATAGCAAAAATGAAAGAAGATATTCTCTATCATTTCAATCTCACC
ACTAGCAGACACAATTTCCCAGCCTTGTTTGGAGATGTGAAGTTTGTGTGTGTTGGTGGA
AGCCCCTCCCGGATGAAAGCCTTCATCAGGTGCGTTGGTGCAGAGCTGGGCCTTGACTGC
CCAGGTAGAGACTATCCCAACATCTGTGCGGGAACTGACCGCTATGCCATGTATAAAGTA
GGACCGGTGCTGTCTGTCAGTCATGGTATGGGCATTCCTTCTATCTCAATCATGTTGCAT
GAGCTCATAAAGCTGCTGTACTATGCCCGGTGCTCCAACGTCACTATCATCCGCATTGGC
ACTTCTGGTGGGATAGGTCTGGAGCCCGGCACTGTGGTCATAACAGAGCAGGCAGTGGAT
ACCTGCTTCAAGGCAGAGTTTGAGCAGATTGTCCTGGGGAAGCGGGTCATCCGGAAAACG
GACCTTAACAAGAAGCTGGTGCAGGAGCTGTTGCTGTGTTCTGCAGAGCTGAGCGAGTTC
ACCACAGTGGTGGGGAACACCATGTGCACCTTGGACTTCTATGAAGGGCAAGGCCGTCTG
GATGGGGCTCTCTGCTCCTACACGGAGAAGGACAAGCAGGCGTATCTGGAGGCAGCCTAT
GCAGCCGGCGTCCGCAATATCGAGATGGAGTCCTCGGTGTTTGCCGCCATGTGCAGCGCC
TGCGGCCTCCAAGCGGCCGTGGTGTGTGTCACCCTCCTGAACCGCCTGGAAGGGGACCAG
ATCAGCAGCCCTCGCAATGTGCTCAGCGAGTACCAGCAGAGGCCGCAGCGGCTGGTGAGC
TACTTCATCAAGAAGAAACTGAGCAAGGCCTGA
Enzyme 1 GenBank Gene ID X90858 Link Image
Enzyme 1 GeneCard ID UPP1 Link Image
Enzyme 1 GenAtlas ID UPP1 Link Image
Enzyme 1 HGNC ID HGNC:12576 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7p12.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Watanabe S, Uchida T: Cloning and expression of human uridine phosphorylase. Biochem Biophys Res Commun. 1995 Nov 2;216(1):265-72. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5804
Enzyme 2 Name Uridine phosphorylase 2
Enzyme 2 Synonyms
  1. UrdPase 2
  2. UPase 2
Enzyme 2 Gene Name UPP2
Enzyme 2 Protein Sequence >Uridine phosphorylase 2 
MASVIPASNRSMRSDRNTYVGKRFVHVKNPYLDLMDEDILYHLDLGTKTHNLPAMFGDVK
FVCVGGSPNRMKAFALFMHKELGFEEAEEDIKDICAGTDRYCMYKTGPVLAISHGMGIPS
ISIMLHELIKLLHHARCCDVTIIRIGTSGGIGIAPGTVVITDIAVDSFFKPRFEQVILDN
IVTRSTELDKELSEELFNCSKEIPNFPTLVGHTMCTYDFYEGQGRLDGALCSFSREKKLD
YLKRAFKAGVRNIEMESTVFAAMCGLCGLKAAVVCVTLLDRLDCDQINLPHDVLVEYQQR
PQLLISNFIRRRLGLCD
Enzyme 2 Number of Residues 317
Enzyme 2 Molecular Weight 35528
Enzyme 2 Theoretical pI 6.66
Enzyme 2 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
  • uridine phosphorylase activity
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside metabolism
  • nucleotide catabolism
  • nucleotide metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 2 General Function Nucleotide transport and metabolism
Enzyme 2 Specific Function Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1- phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis. Shows substrate specificity and accept uridine, deoxyuridine, and thymidine as well as the two pyrimidine nucleoside analogs 5-fluorouridine and 5-fluoro-2(')-deoxyuridine as substrates
Enzyme 2 Pathways
Enzyme 2 Reactions
  • uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 32306848 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O95045 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name UPP2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >954 bp 
ATGGCTTCAGTTATACCTGCCTCCAATAGGTCCATGAGATCTGACAGGAATACATATGTT
GGAAAAAGGTTTGTTCACGTTAAAAATCCTTACTTGGATTTGATGGATGAAGACATTCTC
TATCACTTGGATCTGGGAACAAAAACACACAACCTACCAGCAATGTTCGGAGATGTAAAG
TTCGTCTGTGTCGGTGGGAGCCCCAACAGAATGAAAGCATTTGCACTGTTTATGCACAAG
GAGCTCGGGTTTGAGGAAGCTGAAGAAGACATAAAAGACATCTGTGCTGGGACAGACAGA
TACTGTATGTACAAAACCGGGCCTGTGCTCGCCATCAGTCACGGCATGGGCATCCCCTCC
ATTTCTATTATGCTTCATGAACTCATCAAATTACTCCACCATGCACGGTGCTGCGATGTC
ACCATTATTAGAATCGGTACATCAGGGGGAATAGGGATGGCACCAGGACGTGTTGTAATA
ACGGATATAGCTGTAGACTCCTTCTTTAAGCCCCGGTTTGAACAGGTCATTTTGGACAAC
ATTGTCACCCGAAGTACTGAACTGGACAAAGAACTGTCTGAAGAACTGTTCAACTGTAGC
AAAGAAATCCCCAACTTCCCAACCCTCGTTGGACATACAATGTGTACCTATGATTTTTAT
GAAGGCCAAGGGCGACTAGATGGAGCACTGTGCTCCTTTTCCAGAGAAAAAAAGTTAGAC
TACTTGAAGAGAGCATTTAAAGCTGGTGTCAGGAATATTGAAATGGGAATCTACAGTGTT
TGCAGTATGTGTGGACTCTGTGGTCTAAAAGCTGCTGTGGTCTGTGTGACACTTCTCGAC
AGACTCGACTGTGATCAGATCAACTTGCCTCATGATGTCCTGGTGGAGTACCAGCAACGG
CCTCAGCTCCTAATCTCCAACTTCATCAGACGGCGGCTTGGACTTTGTGACTAG
Enzyme 2 GenBank Gene ID AY225131 Link Image
Enzyme 2 GeneCard ID UPP2 Link Image
Enzyme 2 GenAtlas ID UPP2 Link Image
Enzyme 2 HGNC ID HGNC:23061 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 2q24.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Johansson M: Identification of a novel human uridine phosphorylase. Biochem Biophys Res Commun. 2003 Jul 18;307(1):41-6. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5805
Enzyme 3 Name Purine nucleoside phosphorylase
Enzyme 3 Synonyms
  1. Inosine phosphorylase
  2. PNP
Enzyme 3 Gene Name NP
Enzyme 3 Protein Sequence >Purine nucleoside phosphorylase 
MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRST
VPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGL
NPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQ
MGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSL
ITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
Enzyme 3 Number of Residues 289
Enzyme 3 Molecular Weight 32118
Enzyme 3 Theoretical pI 6.95
Enzyme 3 GO Classification
Function
  • catalytic activity
  • purine-nucleoside phosphorylase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
—
Enzyme 3 General Function Nucleotide transport and metabolism
Enzyme 3 Specific Function Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
Enzyme 3 Pathways
Enzyme 3 Reactions
  • purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 35565 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P00491 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PNPH_HUMAN Link Image
Enzyme 3 PDB ID 1RT9 Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >870 bp 
ATGGAGAACGGATACACCTATGAAGATTATAAGAACACTGCAGAATGGCTTCTGTCTCAT
ACTAAGCACCGACCTCAAGTTGCAATAATCTGTGGTTCTGGATTAGGAGGTCTGACTGAT
AAATTAACTCAGGCCCAGATCTTTGACTACAGTGAAATCCCCAACTTTCCTCGAAGTACA
GTGCCAGGTCATGCTGGCCGACTGGTGTTTGGGTTCCTGAATGGCAGGGCCTGTGTGATG
ATGCAGGGCAGGTTCCACATGTATGAAGGGTACCCACTCTGGAAGGTGACATTCCCAGTG
AGGGTTTTCCACCTTCTGGGTGTGGACACCCTGGTAGTCACCAATGCAGCAGGAGGGCTG
AACCCCAAGTTTGAGGTTGGAGATATCATGCTGATCCGTGACCATATCAACCTACCTGGT
TTCAGTGGTCAGAACCCTCTCAGAGGGCCCAATGATGAAAGGTTTGGAGATCGTTTCCCT
GCCATGTCTGATGCCTACGACCGGACTATGAGGCAGAGGGCTCTCAGTACCTGGAAACAA
ATGGGGGAGCAACGTGAGCTACAGGAAGGCACCTATGTGATGGTGGCAGGCCCCAGCTTT
GAGACTGTGGCAGAATGTCGTGTGCTGCAGAAGCTGGGAGCAGACGCTGTTGGCATGAGT
ACAGTACCAGAAGTTATCGTTGCACGGCACTGTGGACTTCGAGTCTTTGGCTTCTCACTC
ATCACTAACAAGGTCATCATGGATTATGAAAGCCTGGAGAAGGCCAACCATGAAGAAGTC
TTAGCAGCTGGCAAACAAGCTGCACAGAAATTGGAACAGTTTGTCTCCATTCTTATGGCC
AGCATTCCACTCCCTGACAAAGCCAGTTGA
Enzyme 3 GenBank Gene ID X00737 Link Image
Enzyme 3 GeneCard ID NP Link Image
Enzyme 3 GenAtlas ID NP Link Image
Enzyme 3 HGNC ID HGNC:7892 Link Image
Enzyme 3 Chromosome Location 14
Enzyme 3 Locus 14q13.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Williams SR, Goddard JM, Martin DW Jr: Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization. Nucleic Acids Res. 1984 Jul 25;12(14):5779-87. [PubMed Link Image]
  2. Williams SR, Gekeler V, McIvor RS, Martin DW Jr: A human purine nucleoside phosphorylase deficiency caused by a single base change. J Biol Chem. 1987 Feb 15;262(5):2332-8. [PubMed Link Image]
  3. Yu L, Kalla K, Guthrie E, Vidrine A, Klimecki WT: Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans. Environ Health Perspect. 2003 Aug;111(11):1421-7. [PubMed Link Image]
  4. Ealick SE, Rule SA, Carter DC, Greenhough TJ, Babu YS, Cook WJ, Habash J, Helliwell JR, Stoeckler JD, Parks RE Jr, et al.: Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. J Biol Chem. 1990 Jan 25;265(3):1812-20. [PubMed Link Image]
  5. Aust MR, Andrews LG, Barrett MJ, Norby-Slycord CJ, Markert ML: Molecular analysis of mutations in a patient with purine nucleoside phosphorylase deficiency. Am J Hum Genet. 1992 Oct;51(4):763-72. [PubMed Link Image]
  6. Pannicke U, Tuchschmid P, Friedrich W, Bartram CR, Schwarz K: Two novel missense and frameshift mutations in exons 5 and 6 of the purine nucleoside phosphorylase (PNP) gene in a severe combined immunodeficiency (SCID) patient. Hum Genet. 1996 Dec;98(6):706-9. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5806
Enzyme 4 Name Thymidine phosphorylase precursor
Enzyme 4 Synonyms
  1. TdRPase
  2. TP
  3. Platelet-derived endothelial cell growth factor
  4. PD-ECGF
  5. Gliostatin
Enzyme 4 Gene Name ECGF1
Enzyme 4 Protein Sequence >Thymidine phosphorylase precursor 
MAALMTPGTGAPPAPGDFSGEGSQGLPDPSPEPKQLPELIRMKRDGGRLSEADIRGFVAA
VVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQQLVDKHSTGG
VGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQA
GCCIVGQSEQLVPADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAA
VFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKPLGRCVGHALEVEEALLCMDGAGPP
DLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPGLARAL
CSGSPAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVG
AELLVDVGQRLRRGTPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAPSPFAELVLPP
QQ
Enzyme 4 Number of Residues 482
Enzyme 4 Molecular Weight 49956
Enzyme 4 Theoretical pI 5.19
Enzyme 4 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • pyrimidine base metabolism
Component
—
Enzyme 4 General Function Nucleotide transport and metabolism
Enzyme 4 Specific Function Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis
Enzyme 4 Pathways
Enzyme 4 Reactions
  • thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 189701 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P19971 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name TYPH_HUMAN Link Image
Enzyme 4 PDB ID 1UOU Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1449 bp 
ATGGCAGCCTTGATGACCCCGGGAACCGGGGCCCCACCCGCGCCTGGTGACTTCTCCGGG
GAAGGGAGCCAGGGACTTCCCGACCCTTCGCCAGAGCCCAAGCAGCTCCCGGAGCTGATC
CGCATGAAGCGAGACGGAGGCCGCCTGAGCGAAGCGGACATCAGGGGCTTCGTGGCCGCT
GTGGTGAATGGGAGCGCGCAGGGCGCACAGATCGGGGCCATGCTGATGGCCATCCGACTT
CGGGGCATGGATCTGGAGGAGACCTCGGTGCTGACCCAGGCCCTGGCTCAGTCGGGACAG
CAGCTGGAGTGGCCAGAGGCCTGGCGCCAGCAGCTTGTGGACAAGCATTCCACAGGGGGT
GTGGGTGACAAGGTCAGCCTGGTCCTCGCACCTGCCCTGGCGGCATGTGGCTGCAAGGTG
CCAATGATCAGCGGACGTGGTCTGGGGCACACAGGAGGCACCTTGGATAAGCTGGAGTCT
ATTCCTGGATTCAATGTCATCCAGAGCCCAGAGCAGATGCAAGTGCTGCTGGACCAGGCG
GGCTGCTGTATCGTGGGTCAGAGTGAGCAGCTGGTTCCTGCGGACGGAATCCTATATGCA
GCCAGAGATGTGACAGCCACCGTGGACAGCCTGCCACTCATCACAGCCTCCATTCTCAGT
AAGAAACTCGTGGAGGGGCTGTCCGCTCTGGTGGTGGACGTTAAGTTCGGAGGGGCCGCC
GTCTTCCCCAACCAGGAGCAGGCCCGGGAGCTGGCAAAGACGCTGGTTGGCGTGGGAGCC
AGCCTAGGGCTTCGGGTCGCGGCAGCGCTGACCGCCATGGACAAGCCCCTGGGTCGCTGC
GTGGGCCACGCCCTGGAGGTGGAGGAGGCGCTGCTCTGCATGGACGGCGCAGGCCCGCCA
GACTTAAGGGACCTGGTCACCACGCTCGGGGGCGCCCTGCTCTGGCTCAGCGGACACGCG
GGGACTCAGGCTCAGGGCGCTGCCCGGGTGGCCGCGGCGCTGGACGACGGCTCGGCCCTT
GGCCGCTTCGAGCGGATGCTGGCGGCGCAGGGCGTGGATCCCGGTCTGGCCCGAGCCCTG
TGCTCGGGAAGTCCCGCAGAACGCCGGCAGCTGCTGCCTCGCGCCCGGGAGCAGGAGGAG
CTGCTGGCGCCCGCAGATGGCACCGTGGAGCTGGTCCGGGCGCTGCCGCTGGCGCTGGTG
CTGCACGAGCTCGGGGCCGGGCGCAGCCGCGCTGGGGAGCCGCTCCGCCTGGGGGTGGGC
GCAGAGCTGCTGGTCGACGTGGGTCAGAGGCTGCGCCGTGGGACCCCCTGGCTCCGCGTG
CACCGGGACGGCCCCGCGCTCAGCGGCCCGCAGAGCCGCGCCCTGCAGGAGGCGCTCGTA
CTCTCCGACCGCGCGCCATTCGCCGCCCCCTCGCCCTTCGCAGAGCTCGTTCTGCCGCCG
CAGCAATAA
Enzyme 4 GenBank Gene ID M63193 Link Image
Enzyme 4 GeneCard ID ECGF1 Link Image
Enzyme 4 GenAtlas ID ECGF1 Link Image
Enzyme 4 HGNC ID HGNC:3148 Link Image
Enzyme 4 Chromosome Location 22
Enzyme 4 Locus 22q13|22q13.33
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Ishikawa F, Miyazono K, Hellman U, Drexler H, Wernstedt C, Hagiwara K, Usuki K, Takaku F, Risau W, Heldin CH: Identification of angiogenic activity and the cloning and expression of platelet-derived endothelial cell growth factor. Nature. 1989 Apr 13;338(6216):557-62. [PubMed Link Image]
  2. Furukawa T, Yoshimura A, Sumizawa T, Haraguchi M, Akiyama S, Fukui K, Ishizawa M, Yamada Y: Angiogenic factor. Nature. 1992 Apr 23;356(6371):668. [PubMed Link Image]
  3. Asai K, Nakanishi K, Isobe I, Eksioglu YZ, Hirano A, Hama K, Miyamoto T, Kato T: Neurotrophic action of gliostatin on cortical neurons. Identity of gliostatin and platelet-derived endothelial cell growth factor. J Biol Chem. 1992 Oct 5;267(28):20311-6. [PubMed Link Image]
  4. Usuki K, Saras J, Waltenberger J, Miyazono K, Pierce G, Thomason A, Heldin CH: Platelet-derived endothelial cell growth factor has thymidine phosphorylase activity. Biochem Biophys Res Commun. 1992 May 15;184(3):1311-6. [PubMed Link Image]
  5. Nishino I, Spinazzola A, Hirano M: Thymidine phosphorylase gene mutations in MNGIE, a human mitochondrial disorder. Science. 1999 Jan 29;283(5402):689-92. [PubMed Link Image]
  6. Gamez J, Ferreiro C, Accarino ML, Guarner L, Tadesse S, Marti RA, Andreu AL, Raguer N, Cervera C, Hirano M: Phenotypic variability in a Spanish family with MNGIE. Neurology. 2002 Aug 13;59(3):455-7. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6002
Enzyme 5 Name Dihydropyrimidine dehydrogenase [NADP+] precursor
Enzyme 5 Synonyms
  1. DPD
  2. DHPDHase
  3. Dihydrouracil dehydrogenase
  4. Dihydrothymine dehydrogenase
Enzyme 5 Gene Name DPYD
Enzyme 5 Protein Sequence >Dihydropyrimidine dehydrogenase [NADP+] precursor 
MAPVLSKDSADIESILALNPRTQTHATLCSTSAKKLDKKHWKRNPDKNCFNCEKLENNFD
DIKHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDN
PLGLTCGMVCPTSDLCVGGCNLYATEEGPINIGGLQQFATEVFKAMSIPQIRNPSLPPPE
KMSEAYSAKIALFGAGPASISCASFLARLGYSDITIFEKQEYVGGLSTSEIPQFRLPYDV
VNFEIELMKDLGVKIICGKSLSVNEMTLSTLKEKGYKAAFIGIGLPEPNKDAIFQGLTQD
QGFYTSKDFLPLVAKGSKAGMCACHSPLPSIRGVVIVLGAGDTAFDCATSALRCGARRVF
IVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTEQDETGKWN
EDEDQMVHLKADVVISAFGSVLSDPKVKEALSPIKFNRWGLPEVDPETMQTSEAWVFAGG
DVVGLANTTVESVNDGKQASWYIHKYVQSQYGASVSAKPELPLFYTPIDLVDISVEMAGL
KFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRGTTSGPMY
GPGQSSFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDS
GADALELNLSCPHGMGERGMGLACGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSI
ARAAKEGGANGVTATNTVSGLMGLKSDGTPWPAVGIAKRTTYGGVSGTAIRPIALRAVTS
IARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYL
KSIEELQDWDGQSPATVSHQKGKPVPRIAELMDKKLPSFGPYLEQRKKIIAENKIRLKEQ
NVAFSPLKRSCFIPKRPIPTIKDVIGKALQYLGTFGELSNVEQVVAMIDEEMCINCGKCY
MTCNDSGYQAIQFDPETHLPTITDTCTGCTLCLSVCPIVDCIKMVSRTTPYEPKRGVPLS
VNPVC
Enzyme 5 Number of Residues 1025
Enzyme 5 Molecular Weight 111375
Enzyme 5 Theoretical pI 7.05
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • dihydroorotate dehydrogenase activity
  • dihydroorotate oxidase activity
  • disulfide oxidoreductase activity
  • electron transporter activity
  • ion binding
  • iron ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
  • transition metal ion binding
  • transporter activity
Process
  • 'de novo' pyrimidine base biosynthesis
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • nucleobase metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • pyrimidine base biosynthesis
  • pyrimidine base metabolism
Component
  • cell
  • cytoplasm
  • intracellular
  • membrane
Enzyme 5 General Function Amino acid transport and metabolism
Enzyme 5 Specific Function Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil
Enzyme 5 Pathways
Enzyme 5 Reactions
  • 5,6-dihydrouracil + NADP+ = uracil + NADPH + H+
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 558305 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q12882 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name DPYD_HUMAN Link Image
Enzyme 5 PDB ID 1GTE Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >3078 bp 
ATGGCCCCTGTGCTCAGTAAGGACTCGGCGGACATCGAGAGTATCCTGGCTTTAAATCCT
CGAACACAAACTCATGCAACTCTGTGTTCCACTTCGGCCAAGAAATTAGACAAGAAACAT
TGGAAAAGAAATCCTGATAAGAACTGCTTTAATTGTGAGAAGCTGGAGAATAATTTTGAT
GACATCAAGCACACGACTCTTGGTGAGCGAGGAGCTCTCCGAGAAGCAATGAGATGCCTG
AAATGTGCAGATGCCCCGTGTCAGAAGAGCTGTCCAACTAATCTTGATATTAAATCATTC
ATCACAAGTATTGCAAACAAGAACTATTATGGAGCTGCTAAGATGATATTTTCTGACAAC
CCACTTGGTCTGACTTGTGGAATGGTATGTCCAACCTCTGATCTATGTGTAGGTGGATGC
AATTTATATGCCACTGAAGAGGGACCCATTAATATTGGTGGATTGCAGCAATTTGCTACT
GAGGTATTCAAAGCAATGAGTATCCCACAGATCAGAAATCCTTCGCTGCCTCCCCCAGAA
AAAATGTCTGAAGCCTATTCTGCAAAGATTGCTCTTTTTGGTGCTGGGCCTGCAAGTATA
AGTTGTGCTTCCTTTTTGGCTCGATTGGGGTACTCTGACATCACTATATTTGAAAAACAA
GAATATGTTGGTGGTTTAAGTACTTCTGAAATTCCTCAGTTCCGGCTGCCGTATGATGTA
GTGAATTTTGAGATTGAGCTAATGAAGGACCTTGGTGTAAAGATAATTTGCGGTAAAAGC
CTTTCAGTGAATGAAATGACTCTTAGCACTTTGAAAGAAAAAGGCTACAAAGCTGCTTTC
ATTGGAATAGGTTTGCCAGAACCCAATAAAGATGCCATCTTCCAAGGCCTGACGCAGGAC
CAGGGGTTTTATACATCCAAAGACTTTTTGCCACTTGTAGCCAAAGGCAGTAAAGCAGGA
ATGTGCGCCTGTCACTCTCCATTGCCATCGATACGGGGAGTCGTGATTGTACTTGGAGCT
GGAGACACTGCCTTCGACTGTGCAACATCTGCTCTACGTTGTGGAGCTCGCCGAGTGTTC
ATCGTCTTCAGAAAAGGCTTTGTTAATATAAGAGCTGTCCCTGAGGAGATGGAGCTTGCT
AAGGAAGAAAAGTGTGAATTTCTGCCATTCCTGTCCCCACGGAAGGTTATAGTAAAAGGT
GGGAGAATTGTTGCTATGCAGTTTGTTCGGACAGAGCAAGATGAAACTGGAAAATGGAAT
GAAGATGAAGATCAGATGGTCCATCTGAAAGCCGATGTGGTCATCAGTGCCTTTGGTTCA
GTTCTGAGTGATCCTAAAGTAAAAGAAGCCTTGAGCCCTATAAAATTTAACAGATGGGGT
CTCCCAGAAGTAGATCCAGAAACTATGCAAACTAGTGAAGCATGGGTATTTGCAGGTGGT
GATGTCGTTGGTTTGGCTAACACTACAGTGGAATCGGTGAATGATGGAAAGCAAGCTTCT
TGGTACATTCACAAATACGTACAGTCACAATATGGAGCTTCCGTTTCTGCCAAGCCTGAA
CTACCCCTCTTTTACACTCCTATTGATCTGGTGGACATTAGTGTAGAAATGGCCGGATTG
AAGTTTATAAATCCTTTTGGTCTTGCTAGCGCAACTCCAGCCACCAGCACATCAATGATT
CGAAGAGCTTTTGAAGCTGGATGGGGTTTTGCCCTCACCAAAACTTTCTCTCTTGATAAG
GACATTGTGACAAATGTTTCCCCCAGAATCATCCGGGGAACCACCTCTGGCCCCATGTAT
GGCCCTGGACAAAGCTCCTTTCTGAATATTGAGCTCATCAGTGAGAAAACGGCTGCATAT
TGGTGTCAAAGTGTCACTGAACTAAAGGCTGACTTCCCAGACAACATTGTGATTGCTAGC
ATTATGTGCAGTTACAATAAAAATGACTGGACGGAACTTGCCAAGAAGTCTGAGGATTCT
GGAGCAGATGCCCTGGAGTTAAATTTATCATGTCCACATGGCATGGGAGAAAGAGGAATG
GGCCTGGCCTGTGGGCAGGATCCAGAGCTGGTGCGGAACATCTGCCGCTGGGTTAGGCAA
GCTGTTCAGATTCCTTTTTTTGCCAAGCTGACCCCAAATGTCACTGATATTGTGAGCATC
GCAAGAGCTGCAAAGGAAGGTGGTGCCAATGGCGTTACAGCCACCAACACTGTCTCAGGT
CTGATGGGATTAAAATCTGATGGCACACCTTGGCCAGCAGTGGGGATTGCAAAGCGAACT
ACATATGGAGGAGTGTCTGGGACAGCAATCAGACCTATTGCTTTGAGAGCTGTGACCTCC
ATTGCTCGTGCTCTGCCTGGATTTCCCATTTTGGCTACTGGTGGAATTGACTCTGCTGAA
AGTGGTCTTCAGTTTCTCCATAGTGGTGCTTCCGTCCTCCAGGTATGCAGTGCCATTCAG
AATCAGGATTTCACTGTGATCGAAGACTACTGCACTGGCCTCAAAGCCCTGCTTTATCTG
AAAAGCATTGAAGAACTACAAGACTGGGATGGACAGAGTCCAGCTACTGTGAGTCACCAG
AAAGGGAAACCAGTTCCACGTATAGCTGAACTCATGGACAAGAAACTGCCAAGTTTTGGA
CCTTATCTGGAACAGCGCAAGAAAATCATAGCAGAAAACAAGATTAGACTGAAAGAACAA
AATGTAGCTTTTTCACCACTTAAGAGAAGCTGTTTTATCCCCAAAAGGCCTATTCCTACC
ATCAAGGATGTAATAGGAAAAGCACTGCAGTACCTTGGAACATTTGGTGAATTGAGCAAC
GTAGAGCAAGTTGTGGCTATGATTGATGAAGAAATGTGTATCAACTGTGGTAAATGCTAC
ATGACCTGTAATGATTCTGGCTACCAGGCTATACAGTTTGATCCAGAAACCCACCTGCCC
ACCATAACCGACACTTGTACAGGCTGTACTCTGTGTCTCAGTGTTTGCCCTATTGTCGAC
TGCATCAAAATGGTTTCCAGGACAACACCTTATGAACCAAAGAGAGGCGTACCCTTATCT
GTGAATCCGGTGTGTTAA
Enzyme 5 GenBank Gene ID U09178 Link Image
Enzyme 5 GeneCard ID DPYD Link Image
Enzyme 5 GenAtlas ID DPYD Link Image
Enzyme 5 HGNC ID HGNC:3012 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 1p22
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Yokota H, Fernandez-Salguero P, Furuya H, Lin K, McBride OW, Podschun B, Schnackerz KD, Gonzalez FJ: cDNA cloning and chromosome mapping of human dihydropyrimidine dehydrogenase, an enzyme associated with 5-fluorouracil toxicity and congenital thymine uraciluria. J Biol Chem. 1994 Sep 16;269(37):23192-6. [PubMed Link Image]
  2. Johnson MR, Wang K, Tillmanns S, Albin N, Diasio RB: Structural organization of the human dihydropyrimidine dehydrogenase gene. Cancer Res. 1997 May 1;57(9):1660-3. [PubMed Link Image]
  3. Ogura K, Nishiyama T, Takubo H, Kato A, Okuda H, Arakawa K, Fukushima M, Nagayama S, Kawaguchi Y, Watabe T: Suicidal inactivation of human dihydropyrimidine dehydrogenase by (E)-5-(2-bromovinyl)uracil derived from the antiviral, sorivudine. Cancer Lett. 1998 Jan 9;122(1-2):107-13. [PubMed Link Image]
  4. Vreken P, Van Kuilenburg AB, Meinsma R, Smit GP, Bakker HD, De Abreu RA, van Gennip AH: A point mutation in an invariant splice donor site leads to exon skipping in two unrelated Dutch patients with dihydropyrimidine dehydrogenase deficiency. J Inherit Metab Dis. 1996;19(5):645-54. [PubMed Link Image]
  5. Fernandez-Salguero PM, Sapone A, Wei X, Holt JR, Jones S, Idle JR, Gonzalez FJ: Lack of correlation between phenotype and genotype for the polymorphically expressed dihydropyrimidine dehydrogenase in a family of Pakistani origin. Pharmacogenetics. 1997 Apr;7(2):161-3. [PubMed Link Image]
  6. Lu ZH, Zhang R, Diasio RB: Purification and characterization of dihydropyrimidine dehydrogenase from human liver. J Biol Chem. 1992 Aug 25;267(24):17102-9. [PubMed Link Image]
  7. Vreken P, Van Kuilenburg AB, Meinsma R, van Gennip AH: Dihydropyrimidine dehydrogenase (DPD) deficiency: identification and expression of missense mutations C29R, R886H and R235W. Hum Genet. 1997 Dec;101(3):333-8. [PubMed Link Image]
  8. Vreken P, Van Kuilenburg AB, Meinsma R, van Gennip AH: Identification of novel point mutations in the dihydropyrimidine dehydrogenase gene. J Inherit Metab Dis. 1997 Jul;20(3):335-8. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 15250
Enzyme 6 Name cDNA FLJ77390 (Putative uncharacterized protein RP11-311P8.3)
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name RP11-311P8.3
Enzyme 6 Protein Sequence >cDNA FLJ77390 (Putative uncharacterized protein RP11-311P8.3) 
MATELQCPDSMPCHNQQVNSASTPSPEQLRPGDLILDHAGGNRASRAKVILLTGYAHSSL
PAELDSGACGGSSLNSEGNSGSGDSSSYDAPAGNSFLEDCELSRQIGAQLKLLPMNDQIR
ELQTIIRDKTASRGDFMFSADRLIRLVVEEGLNQLPYKECMVTTPTGYKYEGVKFEKGNC
GVSIMRSGEAMEQGLRDCCRSIRIGKILIQSDEETQRAKVYYAKFPPDIYRRKVLLMYPI
LSTGNTVIEAVKVLIEHGVQPSVIILLSLFSTPHGAKSIIQEFPEITILTTEVHPVAPTH
FGQKYFGTD
Enzyme 6 Number of Residues 309
Enzyme 6 Molecular Weight 33787
Enzyme 6 Theoretical pI 5.91
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Nucleotide transport and metabolism
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function Not Available
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 158259509 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID A8KAF9 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name A8KAF9_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >930 bp 
ATGGCCACGGAGTTACAGTGTCCGGACTCCATGCCCTGTCACAACCAGCAAGTAAACTCT
GCCTCAACCCCAAGTCCCGAGCAGCTGCGACCTGGCGATCTGATCCTGGACCACGCAGGG
GGAAACAGAGCCTCCAGGGCCAAGGTGATTCTCCTCACGGGGTACGCCCATTCTAGCCTG
CCGGCCGAGCTGGACTCTGGGGCCTGCGGCGGCTCCAGCCTCAACTCAGAGGGCAACAGT
GGTAGTGGTGACAGTAGCAGCTATGACGCACCAGCTGGCAACTCCTTCCTAGAGGACTGC
GAACTCTCCCGGCAGATCGGGGCGCAGCTTAAGCTGCTGCCTATGAATGATCAGATACGG
GAGCTACAGACCATCATCCGGGACAAGACAGCCAGTAGAGGTGACTTCATGTTTTCTGCG
GATCGTTTGATCAGACTTGTTGTGGAAGAGGGATTGAATCAGCTGCCATATAAAGAATGC
ATGGTGACCACTCCAACAGGGTACAAGTATGAAGGAGTGAAATTTGAGAAGGGAAATTGT
GGGGTCAGCATAATGAGAAGCGGTGAGGCAATGGAACAAGGTTTACGAGACTGCTGTCGA
TCCATACGAATTGGAAAGATCCTGATTCAGAGTGATGAGGAGACACAAAGAGCCAAAGTA
TATTATGCCAAATTCCCCCCAGACATTTACCGGAGAAAAGTCCTTCTGATGTATCCAATT
CTCAGCACTGGAAATACTGTAATTGAAGCTGTAAAGGTTCTTATAGAACATGGAGTTCAA
CCCAGTGTTATCATCCTACTCAGTCTGTTCTCCACTCCTCATGGTGCCAAATCAATCATT
CAGGAGTTTCCAGAGATCACAATTTTAACTACTGAAGTTCATCCTGTTGCACCTACACAT
TTTGGACAGAAATACTTTGGAACAGACTAA
Enzyme 6 GenBank Gene ID AK293024 Link Image
Enzyme 6 GeneCard ID A8KAF9 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 16421
Enzyme 7 Name cDNA, FLJ95575, highly similar to Homo sapiens endothelial cell growth factor 1 (platelet-derived) (ECGF1), mRNA
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name Not Available
Enzyme 7 Protein Sequence >cDNA, FLJ95575, highly similar to Homo sapiens endothelial cell growth factor 1 (platelet-derived) (ECGF1), mRNA 
MAALMTPGTGAPPAPGDFSGEGSQGLPDPSPEPKQLPELIRMKRDGGRLSEADIRGFVAA
VVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQQLVDKHSTGG
VGDKVSLVLAPALAACGCKVPVISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQA
GCCIVGQSEQLVPADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAA
VFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKPLGRCVGHALEVEEALLCMDGAGPP
DLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPGLARAL
CSGSPAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVG
AELLVDVGQRLRRGTPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAPSPFAELVLPP
QQ
Enzyme 7 Number of Residues 482
Enzyme 7 Molecular Weight 49924
Enzyme 7 Theoretical pI 5.19
Enzyme 7 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • pyrimidine base metabolism
Component
—
Enzyme 7 General Function Nucleotide transport and metabolism
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID B2RBL3 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name B2RBL3_HUMAN Link Image
Enzyme 7 PDB ID 1UOU Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID AK314716 Link Image
Enzyme 7 GeneCard ID B2RBL3 Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs Not Available
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 16943
Enzyme 8 Name Uracil phosphoribosyltransferase
Enzyme 8 Synonyms
  1. UMP pyrophosphorylase
  2. UPRTase
Enzyme 8 Gene Name UPRT
Enzyme 8 Protein Sequence >Uracil phosphoribosyltransferase 
MATELQCPDSMPCHNQQVNSASTPSPEQLRPGDLILDHAGGNRASRAKVILLTGYAHSSL
PAELDSGACGGSSLNSEGNSGSGDSSSYDAPAGNSFLEDCELSRQIGAQLKLLPMNDQIR
ELQTIIRDKTASRGDFMFSADRLIRLVVEEGLNQLPYKECMVTTPTGYKYEGVKFEKGNC
GVSIMRSGEAMEQGLRDCCRSIRIGKILIQSDEETQRAKVYYAKFPPDIYRRKVLLMYPI
LSTGNTVIEAVKVLIEHGVQPSVIILLSLFSTPHGAKSIIQEFPEITILTTEVHPVAPTH
FGQKYFGTD
Enzyme 8 Number of Residues 309
Enzyme 8 Molecular Weight 33787
Enzyme 8 Theoretical pI 5.91
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Nucleotide transport and metabolism
Enzyme 8 Specific Function UMP + diphosphate = uracil + 5-phospho-alpha- D-ribose 1-diphosphate
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function Not Available
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID Q96BW1 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name UPP_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AK056354 Link Image
Enzyme 8 GeneCard ID Q96BW1 Link Image
Enzyme 8 GenAtlas ID UPRT Link Image
Enzyme 8 HGNC ID HGNC:28334 Link Image
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 17045
Enzyme 9 Name Uracil nucleotide/cysteinyl leukotriene receptor
Enzyme 9 Synonyms
  1. UDP/CysLT receptor
  2. G-protein coupled receptor 17
  3. P2Y-like receptor
  4. R12
Enzyme 9 Gene Name GPR17
Enzyme 9 Protein Sequence >Uracil nucleotide/cysteinyl leukotriene receptor 
MSKRSWWAGSRKPPREMLKLSGSDSSQSMNGLEVAPPGLITNFSLATAEQCGQETPLENM
LFASFYLLDFILALVGNTLALWLFIRDHKSGTPANVFLMHLAVADLSCVLVLPTRLVYHF
SGNHWPFGEIACRLTGFLFYLNMYASIYFLTCISADRFLAIVHPVKSLKLRRPLYAHLAC
AFLWVVVAVAMAPLLVSPQTVQTNHTVVCLQLYREKASHHALVSLAVAFTFPFITTVTCY
LLIIRSLRQGLRVEKRLKTKAVRMIAIVLAIFLVCFVPYHVNRSVYVLHYRSHGASCATQ
RILALANRITSCLTSLNGALDPIMYFFVAEKFRHALCNLLCGKRLKGPPPSFEGKTNESS
LSAKSEL
Enzyme 9 Number of Residues 367
Enzyme 9 Molecular Weight 40990
Enzyme 9 Theoretical pI 9.82
Enzyme 9 GO Classification
Function
  • G-protein coupled receptor activity
  • nucleotide receptor activity, G-protein coupled
  • purinergic nucleotide receptor activity, G-protein coupled
  • 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 Dual specificity receptor for uracil nucleotides and cysteinyl leukotrienes (CysLTs). Signals through G(i) and inhibition of adenylyl cyclase. May mediate brain damage by nucleotides and CysLTs following ischemia
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • 65-85 93-113 134-154 176-196 224-244 261-281 309-329
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID Q13304 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name GPR17_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID U33447 Link Image
Enzyme 9 GeneCard ID Q13304 Link Image
Enzyme 9 GenAtlas ID GPR17 Link Image
Enzyme 9 HGNC ID HGNC:4471 Link Image
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Raport CJ, Schweickart VL, Chantry D, Eddy RL Jr, Shows TB, Godiska R, Gray PW: New members of the chemokine receptor gene family. J Leukoc Biol. 1996 Jan;59(1):18-23. [PubMed Link Image]
  2. Blasius R, Weber RG, Lichter P, Ogilvie A: A novel orphan G protein-coupled receptor primarily expressed in the brain is localized on human chromosomal band 2q21. J Neurochem. 1998 Apr;70(4):1357-65. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available