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Human Metabolome Database Version 2.5

 

Showing metabocard for Deoxyguanosine (HMDB00085)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-07 12:16:10
Accession Number HMDB00085
Secondary Accession Numbers Not Available
Common Name Deoxyguanosine
Description A nucleoside consisting of the base guanine and the sugar deoxyribose. It is like guanosine, but with one oxygen atom removed. It is a nucleoside component of DNA. Deoxyguanosine can be converted to 8-hydroxy-deoxyguanosine (8-OHdG) due to hydroxyl radical attack at the C8 of guanine. 8-OHdG is a sensitive marker of the DNA damage This damage, if left unrepaired, has been proposed to contribute to mutagenicity and cancer promotion.
Synonyms
  1. 2'-Deoxyguanosine
  2. 2'-deoxy-Guanosine
  3. 2-Deoxyguanosine
  4. 9-(2-Deoxy-b-D-erythro-pentofuranosyl)guanine
  5. 9-(2-deoxy-b-D-erythro-pentofuranosyl)-Guanine
  6. Deoxyguanosine
  7. Desoxyguanosine
  8. Guanine deoxy nucleoside
  9. Guanine deoxyriboside
  10. 9-(2-Deoxy-beta-delta-erythro-pentofuranosyl)guanine
  11. 9-(2-deoxy-beta-delta-erythro-pentofuranosyl)-Guanine
Chemical IUPAC Name 2-amino-9-[4-hydroxy-5-(hydroxymethyl)oxolan-2-yl]-3H-purin-6-one
Chemical Formula C10H13N5O4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleoside Analogues
Sub Class
  • Deoxy nucleosides
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • secondary alcohol
  • primary amine
  • primary aromatic amine
  • oxo(het)arene
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Purine metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 267.241
Monoisotopic Molecular Weight 267.096741
Isomeric SMILES NC1=NC2=C(N=CN2[C@H]2C[C@H](O)[C@@H](CO)O2)C(=O)N1
Canonical SMILES NC1=NC2=C(N=CN2C2CC(O)C(CO)O2)C(=O)N1
KEGG Compound ID C00330 Link Image
BioCyc ID DEOXYGUANOSINE Link Image
BiGG ID 34637 Link Image
Wikipedia Link Deoxyguanosine Link Image
NuGOwiki Link HMDB00085 Link Image
Metagene Link HMDB00085 Link Image
METLIN ID 3395 Link Image
PubChem Compound 187790 Link Image
PubChem Substance 841363 Link Image
ChEBI ID 17172 Link Image
CAS Registry Number 961-07-9
InChI Identifier InChI=1/C10H13N5O4/c11-10-13-8-7(9(18)14-10)12-3-15(8)6-1-4(17)5(2-16)19-6/h3-6,16-17H,1-2H2,(H3,11,13,14,18)/t4-,5+,6+/m0/s1
Synthesis Reference Noguchi, Toshitada; Hamamoto, Tomoki; Okuyama, Kiyoshi; Shibuya, Susumu. Process for producing 2'-deoxyguanosine. PCT Int. Appl. (2003), 31 pp.
Melting Point (Experimental) 300 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 12.0 mg/mL [MEYLAN,WM et al. (1996)]; 11.5 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -1.30 [BALZARINI,JM ET AL. (1989)] Source: PhysProp
Predicted LogP/Hydrophobicity -1.75 [Predicted by ALOGPS]; -1.1 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • Nucleus
  • Extracellular
  • lysosome
  • mitochondria
Biofluid Location
  • Blood
  • Urine
Tissue Location
Tissue References
All Tissues —
Concentrations (Normal)
Biofluid Urine
Value <1.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Wevers RA, Engelke UF, Moolenaar SH, Brautigam C, de Jong JG, Duran R, de Abreu RA, van Gennip AH: 1H-NMR spectroscopy of body fluids: inborn errors of purine and pyrimidine metabolism. Clin Chem. 1999 Apr;45(4):539-48. [PubMed Link Image]
Biofluid Urine
Value 1.00 (0.00-2.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Hartmann S, Okun JG, Schmidt C, Langhans CD, Garbade SF, Burgard P, Haas D, Sass JO, Nyhan WL, Hoffmann GF: Comprehensive detection of disorders of purine and pyrimidine metabolism by HPLC with electrospray ionization tandem mass spectrometry. Clin Chem. 2006 Jun;52(6):1127-37. Epub 2006 Apr 13. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 11.0 (2.0-20.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Purine nucleoside phosphorylase deficiency
Comments Not Available
References
  • Gandhi V, Kilpatrick JM, Plunkett W, Ayres M, Harman L, Du M, Bantia S, Davisson J, Wierda WG, Faderl S, Kantarjian H, Thomas D: A proof-of-principle pharmacokinetic, pharmacodynamic, and clinical study with purine nucleoside phosphorylase inhibitor immucillin-H (BCX-1777, forodesine). Blood. 2005 Dec 15;106(13):4253-60. Epub 2005 Aug 30. [PubMed Link Image]
Biofluid Urine
Value 177.0-322.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex N/A
Condition Purine nucleoside phosphorylase deficiency
Comments Not Available
References
  • Wevers RA, Engelke UF, Moolenaar SH, Brautigam C, de Jong JG, Duran R, de Abreu RA, van Gennip AH: 1H-NMR spectroscopy of body fluids: inborn errors of purine and pyrimidine metabolism. Clin Chem. 1999 Apr;45(4):539-48. [PubMed Link Image]
Associated Disorders
Condition References
Purine nucleoside phosphorylase deficiency
OMIM ID
  • 164050 Link Image (Purine nucleoside phosphorylase deficiency)
Pathways
Name SMPDB Link KEGG Link
Purine Metabolism SMP00050 Link Image map00230 Link Image
General References
  1. Gao K, Henning SM, Niu Y, Youssefian AA, Seeram NP, Xu A, Heber D: The citrus flavonoid naringenin stimulates DNA repair in prostate cancer cells. J Nutr Biochem. 2006 Feb;17(2):89-95. Epub 2005 Jun 20. [PubMed Link Image]
  2. Podmore K, Farmer PB, Herbert KE, Jones GD, Martin EA: 32P-postlabelling approaches for the detection of 8-oxo-2'-deoxyguanosine-3'-monophosphate in DNA. Mutat Res. 1997 Aug 1;378(1-2):139-49. [PubMed Link Image]
  3. Shibata T, Iio K, Kawai Y, Shibata N, Kawaguchi M, Toi S, Kobayashi M, Kobayashi M, Yamamoto K, Uchida K: Identification of a lipid peroxidation product as a potential trigger of the p53 pathway. J Biol Chem. 2006 Jan 13;281(2):1196-204. Epub 2005 Oct 26. [PubMed Link Image]
  4. Gackowski D, Ciecierski M, Jawien A, Olinski R: Background level of 8-oxo-2'-deoxyguanosine in lymphocyte DNA does not correlate with the concentration of antioxidant vitamins in blood plasma. Acta Biochim Pol. 2001;48(2):535-9. [PubMed Link Image]
  5. Takamura-Enya T, Watanabe M, Totsuka Y, Kanazawa T, Matsushima-Hibiya Y, Koyama K, Sugimura T, Wakabayashi K: Mono(ADP-ribosyl)ation of 2'-deoxyguanosine residue in DNA by an apoptosis-inducing protein, pierisin-1, from cabbage butterfly. Proc Natl Acad Sci U S A. 2001 Oct 23;98(22):12414-9. Epub 2001 Oct 9. [PubMed Link Image]
  6. Palozza P, Serini S, Di Nicuolo F, Boninsegna A, Torsello A, Maggiano N, Ranelletti FO, Wolf FI, Calviello G, Cittadini A: beta-Carotene exacerbates DNA oxidative damage and modifies p53-related pathways of cell proliferation and apoptosis in cultured cells exposed to tobacco smoke condensate. Carcinogenesis. 2004 Aug;25(8):1315-25. Epub 2004 Apr 8. [PubMed Link Image]
  7. Zaidi SN, Laidlaw I, Howell A, Potten CS, Cooper DP, O'Connor PJ: Normal human breast xenografts activate N-nitrosodimethylamine: identification of potential target cells for an environmental nitrosamine. Br J Cancer. 1992 Jul;66(1):79-83. [PubMed Link Image]
  8. Gackowski D, Banaszkiewicz Z, Rozalski R, Jawien A, Olinski R: Persistent oxidative stress in colorectal carcinoma patients. Int J Cancer. 2002 Oct 1;101(4):395-7. [PubMed Link Image]
  9. Araki S, Hayashi M, Tamagawa K, Saito M, Kato S, Komori T, Sakakihara Y, Mizutani T, Oda M: Neuropathological analysis in spinal muscular atrophy type II. Acta Neuropathol (Berl). 2003 Nov;106(5):441-8. Epub 2003 Jul 25. [PubMed Link Image]
  10. Kato I, Ren J, Heilbrun LK, Djuric Z: Intra- and inter-individual variability in measurements of biomarkers for oxidative damage in vivo: Nutrition and Breast Health Study. Biomarkers. 2006 Mar-Apr;11(2):143-52. [PubMed Link Image]
  11. Izzedine H, Launay-Vacher V, Aymard G, Legrand M, Deray G: Pharmacokinetics of abacavir in HIV-1-infected patients with impaired renal function. Nephron. 2001 Sep;89(1):62-7. [PubMed Link Image]
  12. Wevers RA, Engelke UF, Moolenaar SH, Brautigam C, de Jong JG, Duran R, de Abreu RA, van Gennip AH: 1H-NMR spectroscopy of body fluids: inborn errors of purine and pyrimidine metabolism. Clin Chem. 1999 Apr;45(4):539-48. [PubMed Link Image]
  13. Bowen P, Chen L, Stacewicz-Sapuntzakis M, Duncan C, Sharifi R, Ghosh L, Kim HS, Christov-Tzelkov K, van Breemen R: Tomato sauce supplementation and prostate cancer: lycopene accumulation and modulation of biomarkers of carcinogenesis. Exp Biol Med (Maywood). 2002 Nov;227(10):886-93. [PubMed Link Image]
  14. Staal GE, Stoop JW, Zegers BJ, Siegenbeek van Heukelom LH, van der Vlist MJ, Wadman SK, Martin DW: Erythrocyte metabolism in purine nucleoside phosphorylase deficiency after enzyme replacement therapy by infusion of erythrocytes. J Clin Invest. 1980 Jan;65(1):103-8. [PubMed Link Image]
  15. Blair IA: Lipid hydroperoxide-mediated DNA damage. Exp Gerontol. 2001 Sep;36(9):1473-81. [PubMed Link Image]
  16. Schramm VL: Development of transition state analogues of purine nucleoside phosphorylase as anti-T-cell agents. Biochim Biophys Acta. 2002 Jul 18;1587(2-3):107-17. [PubMed Link Image]
  17. Schilderman PA, Rhijnsburger E, Zwingmann I, Kleinjans JC: Induction of oxidative DNA damages and enhancement of cell proliferation in human lymphocytes in vitro by butylated hydroxyanisole. Carcinogenesis. 1995 Mar;16(3):507-12. [PubMed Link Image]
  18. Kaneko T, Tahara S: Formation of 8-oxo-2'-deoxyguanosine in the DNA of human diploid fibroblasts by treatment with linoleic acid hydroperoxide and ferric ion. Lipids. 2000 Sep;35(9):961-5. [PubMed Link Image]
  19. Hou SM, Nori P, Fang JL, Vaca CE: Methylglyoxal induces hprt mutation and DNA adducts in human T-lymphocytes in vitro. Environ Mol Mutagen. 1995;26(4):286-91. [PubMed Link Image]
  20. Bialkowski K, Kowara R, Windorbska W, Olinski R: 8-Oxo-2'-deoxyguanosine level in lymphocytes DNA of cancer patients undergoing radiotherapy. Cancer Lett. 1996 Jan 19;99(1):93-7. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Cytosolic 5'-nucleotidase 1B
  2. Cytosolic 5'-nucleotidase 1A
  3. 5'(3')-deoxyribonucleotidase, cytosolic type
  4. 5'(3')-deoxyribonucleotidase, mitochondrial precursor
  5. Cytosolic purine 5'-nucleotidase
  6. Purine nucleoside phosphorylase
  7. Thymidine phosphorylase precursor
  8. Deoxyguanosine kinase, mitochondrial precursor
  9. Cytosolic 5'-nucleotidase III
  10. cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
  11. cDNA, FLJ95575, highly similar to Homo sapiens endothelial cell growth factor 1 (platelet-derived) (ECGF1), mRNA
  12. cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
Enzyme 1 [top]
Enzyme 1 ID 5232
Enzyme 1 Name Cytosolic 5'-nucleotidase 1B
Enzyme 1 Synonyms
  1. Cytosolic 5'-nucleotidase IB
  2. cN1B
  3. cN-IB
  4. Autoimmune infertility-related protein
Enzyme 1 Gene Name NT5C1B
Enzyme 1 Protein Sequence >Cytosolic 5'-nucleotidase 1B 
MSQTSLKQKKNEPGMRSSKESLEAEKRKESDKTGVRLSNQMRRAVNPNHSLRCCPFQGHS
SCRRCLCAAEGTALGPCHTIRIYIHMCLLWEQGQQITMMRGSQESSLRKTDSRGYLVRSQ
WSRISRSPSTKAPSIDEPRSRNTSAKLPSSSTSSRTPSTSPSLHDSSPPPLSGQPSLQPP
ASPQLPRSLDSRPPTPPEPDPGSRRSTKMQENPEAWAQGIVREIRQTRDSQPLEYSRTSP
TEWKSSSQRRGIYPASTQLDRNSLSEQQQQQREDEDDYEAAYWASMRSFYEKNPSCSRPW
PPKPKNAITIALSSCALFNMVDGRKIYEQEGLEKYMEYQLTNENVILTPGPAFRFVKALQ
YVNARLRDLYPDEQDLFDIVLMTNNHAQVGVRLINSVNHYGLLIDRFCLTGGKDPIGYLK
AYLTNLYIAADSEKVQEAIQEGIASATMFDGAKDMAYCDTQLRVAFDGDAVLFSDESEHF
TKEHGLDKFFQYDTLCESKPLAQGPLKGFLEDLGRLQKKFYAKNERLLCPIRTYLVTARS
AASSGARVLKTLRRWGLEIDEALFLAGAPKSPILVKIRPHIFFDDHMFHIEGAQRLGSIA
AYGFNKKFSS
Enzyme 1 Number of Residues 610
Enzyme 1 Molecular Weight 68804
Enzyme 1 Theoretical pI 9.03
Enzyme 1 GO Classification
Function
  • 5'-nucleotidase activity
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleotidase activity
  • nucleotide binding
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Helps to regulate adenosine levels
Enzyme 1 Pathways
Enzyme 1 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + 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 13774961 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q96P26 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name 5NT1B_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1699 bp 
GGGCAAAAATGTGGATAACAACAAAAGAATTTCAACAGGTAAAAAAATGAGTCAAACATC
TCTCAAACAGAAAAAGAATGAGCCCGGAATGAGGTCCTCAAAAGAGAGTCTAGAAGCAGA
AAAAAGAAAGGAATCTGACAAAACAGGAGTTCGTCTGAGCAATCAGGGATCACAAGAATC
ATCACTGCGGAAGACAGACTCTCGAGGGTACCTTGTGCGCAGTCAATGGTCTAGAATATC
CCGGAGCCCATCCACCAAGGCTCCATCCATAGATGAGCCTAGAAGCAGGAACACCAGTGC
TAAGCTCCCCAGCAGCTCCACGAGCTCCCGGACTCCATCCACCTCCCCAAGCCTGCATGA
CTCCTCACCGCCGCCGCTGTCCGGGCAGCCCTCGCTCCAGCCACCCGCGTCGCCCCAGCT
GCCCCGGTCGCTGGACTCGCGGCCTCCCACGCCCCCAGAGCCCGATCCTGGCTCCCGGCG
CAGCACCAAAATGCAAGAAAATCCGGAGGCCTGGGCCCAAGGCATCGTGCGGGAAATCCG
CCAGACCCGGGACTCGCAGCCGCTGGAATATTCGCGCACGTCCCCCACCGAGTGGAAGTC
CTCCAGCCAGCGCAGGGGGATCTACCCCGCCTCCACCCAGCTGGACCGCAACTCTCTGTC
CGAGCAGCAGCAGCAGCAGCGGGAGGACGAAGACGACTACGAAGCTGCCTACTGGGCATC
CATGAAGTCGTTCTACGAAAAGAACCCGAGCTGCTGGCGCCCCTGGCCGCCCAAACCCAA
GAACGCCATCACCATTGCTCTCTCATCCTGCGCGCTCTTCAACATGGTGGACGGCAGGAA
AATCTACGAGCAAGAGGGTCTGGAAAAGTACATGGAGTATCAGCTCACCAATGAGAACGT
CATCCTGACCCCGGGCCCGGCGTTCCGTTTCGTCAAGGCACTACAGTATGTCAATGCTAG
ACTCCGTGATCTATATCCTGATGAACAGGACTTATTTGATATTGTACTGATGACTAATAA
CCATGCCCAAGTGGGAGTGCGGCTTATAAACAGCGTCAATCACTACGGCTTACTGATTGA
CCGCTTCTGTCTGACCGGGGGAAAAGACCCCATTGGCTATTTGAAGGCATATCTTACCAA
CTTGTATATTGCTGCAGATTCTGAAAAAGTGCAAGAGGCAATACAAGAAGGTATTGCCTC
TGCGACAATGTTTGATGGAGCCAAAGACATGGCTTACTGTGACACTCAGCTCCGTGTAGC
CTTTGATGGGGATGCTGTCCTCTTCTCTGATGAGTCTGAACATTTTACCAAGGAGCATGG
GCTGGACAAATTCTTCCAGTATGATACATTATGTGAAAGTAAGCCTCTTGCTCAGGGTCC
CCTAAAAGGCTTTCTGGAAGATTTAGGCAGACTGCAAAAGAAGTTCTATGCCAAAAATGA
ACGGTTACTTTGTCCTATCAGGACCTACCTGGTTACAGCTAGGAGTGCAGCCAGTTCAGG
CGCCCGTGTGCTGAAAACCTTCCGACGCTGGGGTCTAGAGATAGACGAAGCTCTTTTCCT
TGCTGGAGCCCCCAAAAGTCCCATCTTGGTGAAGATCCGGCCCCACATCTTCTTTGATGA
CCACATGTTCCACATTGAAGGGGCACAGAGGTTAGGTTCCATCGCAGCTTATGGCTTTAA
TAAAAAATTCAGTAGTTAG
Enzyme 1 GenBank Gene ID AF356185 Link Image
Enzyme 1 GeneCard ID NT5C1B Link Image
Enzyme 1 GenAtlas ID NT5C1B Link Image
Enzyme 1 HGNC ID HGNC:17818 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2p24.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Sala-Newby GB, Newby AC: Cloning of a mouse cytosolic 5'-nucleotidase-I identifies a new gene related to human autoimmune infertility-related protein. Biochim Biophys Acta. 2001 Oct 31;1521(1-3):12-8. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5233
Enzyme 2 Name Cytosolic 5'-nucleotidase 1A
Enzyme 2 Synonyms
  1. Cytosolic 5'-nucleotidase IA
  2. cN1A
  3. cN-IA
  4. cN-I
Enzyme 2 Gene Name NT5C1A
Enzyme 2 Protein Sequence >Cytosolic 5'-nucleotidase 1A 
MEPGQPREPQEPREPGPGAETAAAPVWEEAKIFYDNLAPKKKPKSPKPQNAVTIAVSSRA
LFRMDEEQQIYTEQGVEEYVRYQLEHENEPFSPGPAFPFVKALEAVNRRLRELYPDSEDV
FDIVLMTNNHAQVGVRLINSINHYDLFIERFCMTGGNSPICYLKAYHTNLYLSADAEKVR
EAIDEGIAAATIFSPSRDVVVSQSQLRVAFDGDAVLFSDESERIVKAHGLDRFFEHEKAH
ENKPLAQGPLKGFLEALGRLQKKFYSKGLRLECPIRTYLVTARSAASSGARALKTLRSWG
LETDEALFLAGAPKGPLLEKIRPHIFFDDQMFHVAGAQEMGTVAAHVPYGVAQTPRRTAP
AKQAPSAQ
Enzyme 2 Number of Residues 368
Enzyme 2 Molecular Weight 41021
Enzyme 2 Theoretical pI 6.52
Enzyme 2 GO Classification
Function
  • 5'-nucleotidase activity
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleotidase activity
  • nucleotide binding
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides and has a broad substrate specificity. Helps to regulate adenosine levels in heart during ischemia and hypoxia
Enzyme 2 Pathways
Enzyme 2 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + 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 12659324 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9BXI3 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name 5NT1A_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1107 bp 
ATGGAACCTGGGCAGCCCCGGGAGCCCCAGGAGCCCCGCGAGCCCGGGCCAGGAGCGGAG
ACCGCTGCGGCCCCGGTCTGGGAGGAAGCCAAGATTTTCTACGACAACCTCGCGCCCAAG
AAGAAACCCAAATCGCCCAAGCCTCAGAATGCAGTCACCATCGCTGTGTCCTCCCGAGCC
TTGTTTCGCATGGACGAGGAGCAGCAGATCTACACGGAGCAGGGCGTGGAGGAGTACGTG
CGCTACCAGCTGGAACATGAGAACGAACCCTTCAGTCCCGGGCCAGCCTTCCCTTTTGTG
AAGGCTCTGGAGGCCGTGAACAGGCGGCTGCGGGAGCTGTACCCTGATAGTGAGGACGTC
TTCGACATCGTCCTCATGACTAACAACCATGCTCAAGTGGGTGTCCGCCTCATCAACAGT
ATCAACCACTATGACCTGTTCATCGAGAGGTTCTGCATGACAGGTGGGAACAGCCCGATC
TGCTACCTCAAGGCCTATCACACCAACCTCTACTTGTCAGCCGATGCGGAAAAAGTGCGA
GAAGCCATTGATGAGGGGATCGCAGCTGCCACCATCTTCAGCCCCAGCAGGGATGTGGTT
GTGTCCCAGAGTCAGCTGCGCGTGGCCTTCGATGGGGACGCCGTGCTCTTCTCGGACGAG
TCGGAGCGCATCGTCAAGGCCCACGGGCTGGACCGATTCTTCGAGCATGAGAAGGCCCAC
GAGAACAAGCCTCTGGCTCAGGGCCCCTTAAAGGGCTTTCTGGAGGCACTGGGTAGGTTG
CAGAAGAAGTTCTACTCCAAAGGCCTGCGGCTGGAGTGCCCAATTCGTACCTACTTGGTG
ACAGCACGCAGTGCAGCCAGTTCCGGGGCCCGGGCTCTCAAGACCCTGCGCAGCTGGGGC
CTGGAGACAGATGAAGCCTTGTTCCTTGCTGGAGCGCCCAAGGGCCCTCTCCTTGAGAAG
ATCCGCCCACACATCTTCTTTGATGACCAGATGTTCCATGTGGCTGGGGCTCAGGAGATG
GGCACTGTGGCCGCCCATGTGCCTTATGGTGTGGCACAGACACCCCGGCGGACTGCACCT
GCAAAGCAGGCCCCATCTGCACAGTAG
Enzyme 2 GenBank Gene ID AF331801 Link Image
Enzyme 2 GeneCard ID NT5C1A Link Image
Enzyme 2 GenAtlas ID NT5C1A Link Image
Enzyme 2 HGNC ID HGNC:17819 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p34.3-p33
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Hunsucker SA, Spychala J, Mitchell BS: Human cytosolic 5'-nucleotidase I: characterization and role in nucleoside analog resistance. J Biol Chem. 2001 Mar 30;276(13):10498-504. Epub 2000 Dec 22. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5234
Enzyme 3 Name 5'(3')-deoxyribonucleotidase, cytosolic type
Enzyme 3 Synonyms
  1. Cytosolic 5',3'-pyrimidine nucleotidase
  2. Deoxy-5'-nucleotidase 1
  3. dNT-1
Enzyme 3 Gene Name NT5C
Enzyme 3 Protein Sequence >5'(3')-deoxyribonucleotidase, cytosolic type 
MARSVRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRALRPDLADK
VASVYEAPGFFLDLEPIPGALDAVREMNDLPDTQVFICTSPLLKYHHCVGEKYRWVEQHL
GPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFTCCHNRHLVLPPTRRRL
LSWSDNWREILDSKRGAAQRE
Enzyme 3 Number of Residues 201
Enzyme 3 Molecular Weight 23383
Enzyme 3 Theoretical pI 6.63
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP
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 7524492 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q8TCD5 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name NT5C_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >606 bp 
ATGGCGCGGAGCGTGCGCGTGCTGGTGGACATGGACGGCGTCCTGGCCGACTTCGAGGCC
GGCCTCCTGCGGGGCTTCCGCCGCCGCTTCCCTGAGGAGCCGCACGTGCCGCTGGAGCAA
CGCCGCGGCTTCCTGGCCCGCGAGCAGTACCGCGCCCTGCGGCCCGACCTGGCGGATAAA
GTGGCCAGTGTGTACGAAGCCCCGGGCTTTTTCCTGGACCTGGAGCCCATCCCGGGAGCC
TTGGACGCTGTGCGGGAGATGAACGACCTACCGGACACGCAGGTCTTCATCTGCACCAGC
CCCCTGCTGAAGTACCACCACTGTGTGGGTGAGAAGTACCGCTGGGTGGAGCAGCACCTG
GGGCCCCAGTTCGTAGAACGAATTATCCTGACAAGGGACAAGACGGTGGTCTTGGGGGAC
CTGCTCATTGATGACAAGGACACAGTTCGAGGCCAGGAGGAGACCCCAAGCTGGGAGCAC
ATCTTGTTCACCTGCTGCCACAATCGGCACCTGGTCCTGCCCCCGACAAGGAGACGGCTG
CTCTCCTGGAGTGACAACTGGAGGGAGATCTTAGATAGCAAGCGCGGAGCTGCGCAGCGG
GAATGA
Enzyme 3 GenBank Gene ID AF154829 Link Image
Enzyme 3 GeneCard ID NT5C Link Image
Enzyme 3 GenAtlas ID NT5C Link Image
Enzyme 3 HGNC ID HGNC:17144 Link Image
Enzyme 3 Chromosome Location 17
Enzyme 3 Locus 17q25.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Rampazzo C, Johansson M, Gallinaro L, Ferraro P, Hellman U, Karlsson A, Reichard P, Bianchi V: Mammalian 5'(3')-deoxyribonucleotidase, cDNA cloning, and overexpression of the enzyme in Escherichia coli and mammalian cells. J Biol Chem. 2000 Feb 25;275(8):5409-15. [PubMed Link Image]
  2. Rampazzo C, Kost-Alimova M, Ruzzenente B, Dumanski JP, Bianchi V: Mouse cytosolic and mitochondrial deoxyribonucleotidases: cDNA cloning of the mitochondrial enzyme, gene structures, chromosomal mapping and comparison with the human orthologs. Gene. 2002 Jul 10;294(1-2):109-17. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5236
Enzyme 4 Name 5'(3')-deoxyribonucleotidase, mitochondrial precursor
Enzyme 4 Synonyms
  1. 5',3'-nucleotidase, mitochondrial
  2. Deoxy-5'-nucleotidase 2
  3. dNT-2
Enzyme 4 Gene Name NT5M
Enzyme 4 Protein Sequence >5'(3')-deoxyribonucleotidase, mitochondrial precursor 
MIRLGGWCARRLCSAAVPAGRRGAAGGLGLAGGRALRVLVDMDGVLADFEGGFLRKFRAR
FPDQPFIALEDRRGFWVSEQYGRLRPGLSEKAISIWESKNFFFELEPLPGAVEAVKEMAS
LQNTDVFICTSPIKMFKYCPYEKYAWVEKYFGPDFLEQIVLTRDKTVVSADLLIDDRPDI
TGAEPTPSWEHVLFTACHNQHLQLQPPRRRLHSWADDWKAILDSKRPC
Enzyme 4 Number of Residues 228
Enzyme 4 Molecular Weight 25862
Enzyme 4 Theoretical pI 8.12
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Dephosphorylates specifically the 5' and 2'(3')- phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-15
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 9408106 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9NPB1 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name NT5M_HUMAN Link Image
Enzyme 4 PDB ID 1Q92 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >687 bp 
ATGATCCGGCTGGGCGGCTGGTGTGCGCGGCGGCTCTGCAGCGCGGCGGTTCCCGCGGGG
CGGCGCGGGGCGGCGGGCGGGCTGGGCCTGGCGGGAGGCCGCGCCCTACGGGTGCTGGTG
GACATGGACGGCGTGCTGGCTGACTTCGAGGGCGGATTCCTCAGGAAGTTCCGCGCGCGC
TTTCCCGACCAGCCCTTCATCGCGCTGGAGGACCGGCGCGGCTTCTGGGTGTCGGAGCAG
TACGGCCGCCTGCGGCCAGGGCTGAGCGAGAAGGCCATCAGCATTTGGGAGTCAAAGAAT
TTCTTTTTTGAACTTGAGCCTCTGCCAGGGGCCGTGGAAGCTGTCAAGGAGATGGCCAGC
CTACAAAACACTGACGTCTTCATCTGCACAAGCCCCATCAAGATGTTCAAGTACTGTCCC
TATGAGAAGTATGCCTGGGTGGAGAAGTACTTTGGCCCTGACTTTCTGGAGCAGATTGTG
CTGACCAGAGACAAGACCGTGGTCTCTGCTGACCTTCTCATAGACGACCGGCCGGACATC
ACAGGGGCCGAGCCAACCCCCAGCTGGGAGCATGTCCTCTTCACCGCCTGCCACAACCAG
CACCTGCAGCTGCAGCCCCCCCGCCGCAGGCTGCACTCGTGGGCGGACGACTGGAAGGCC
ATTCTGGACAGCAAGCGGCCCTGCTGA
Enzyme 4 GenBank Gene ID AJ277557 Link Image
Enzyme 4 GeneCard ID NT5M Link Image
Enzyme 4 GenAtlas ID NT5M Link Image
Enzyme 4 HGNC ID HGNC:15769 Link Image
Enzyme 4 Chromosome Location 17
Enzyme 4 Locus 17p11.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Rampazzo C, Gallinaro L, Milanesi E, Frigimelica E, Reichard P, Bianchi V: A deoxyribonucleotidase in mitochondria: involvement in regulation of dNTP pools and possible link to genetic disease. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8239-44. [PubMed Link Image]
  2. Rinaldo-Matthis A, Rampazzo C, Reichard P, Bianchi V, Nordlund P: Crystal structure of a human mitochondrial deoxyribonucleotidase. Nat Struct Biol. 2002 Oct;9(10):779-87. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5237
Enzyme 5 Name Cytosolic purine 5'-nucleotidase
Enzyme 5 Synonyms
  1. 5'-nucleotidase cytosolic II
Enzyme 5 Gene Name NT5C2
Enzyme 5 Protein Sequence >Cytosolic purine 5'-nucleotidase 
MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLV
CAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTS
CETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMK
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLA
PQEITHCHDEDDDEEEEEEEE
Enzyme 5 Number of Residues 561
Enzyme 5 Molecular Weight 64970
Enzyme 5 Theoretical pI 6.05
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5-prime-monophosphate (IMP) and other purine nucleotides
Enzyme 5 Pathways
Enzyme 5 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 633071 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P49902 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name 5NTC_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1686 bp 
ATGTCGACCTCCTGGAGTGATCGGTTACAGAATGCAGCAGATATGCCTGCTAACATGGAT
AAGCATGCCCTGAAAAAGTATCGTCGAGAAGCCTATCATCGGGTGTTTGTGAACCGAAGT
TTAGCAATGGAAAAGATAAAGTGTTTTGGTTTTGATATGGATTATACCCTTGCTGTGTAC
AAGTCCCCAGAGTATGAGTCCCTTGGTTTTGAGCTTACTGTGGAGAGATTAGTTTCTATT
GGCTATCCCCAGGAGTTGCTCAGCTTTGCTTATGATTCTACATTCCCTACCAGGGGACTT
GTCTTTGACACACTGTATGGAAATCTTTTGAAAGTCGATGCCTATGGAAACCTCTTGGTC
TGTGCACATGGATTTAACTTTATAAGGGGACCAGAAACTAGAGAACAGTATCCAAATAAA
TTTATCCAGCGAGATGATACTGAAAGATTTTACATTCTGAACACACTATTCAACCTACCA
GAGACCTACCTGTTGGCCTGCCTAGTAGATTTTTTTACTAATTGTCCCAGATATACCAGT
TGTGAAACAGGATTTAAAGATGGGGACCTCTTCATGTCCTACCGGAGTATGTTCCAGGAT
GTAAGAGATGCTGTTGACTGGGTTCATTACAAGGGCTCCCTTAAGGAAAAGACAGTTGAA
AATCTTGAGAAGTATGTAGTCAAAGATGGAAAACTGCCTTTGCTTCTGAGCCGGATGAAG
GAAGTAGGGAAAGTATTTCTTGCTACCAACAGTGACTATAAATATACAGATAAAATTATG
ACTTACCTGTTTGACTTCCCACATGGCCCCAAGCCTGGGAGCTCCCATCGACCATGGCAG
TCCTACTTTGACTTGATCTTGGTGGATGCACGGAAACCACTCTTTTTTGGAGAAGGCACA
GTACTGCGTCAGGTGGATACTAAAACTGGCAAGCTGAAAATTGGTACCTACACAGGGCCC
CTACAGCATGGTATCGTCTACTCAGGAGGTTCTTCTGATACGATCTGTGACCTGTTGGGA
GCCAAGGGAAAAGACATTTTGTATATTGGAGATCACATTTTTGGGGACATTTTAAAATCA
AAGAAACGGCAAGGGTGGCGAACTTTTTTGGTGATTCCTGAACTCGCACAGGAGCTACAT
GTCTGGACTGACAAGAGTTCACTTTTCGAAGAACTTCAGAGCTTGGATATTTTCTTGGCT
GAACTCTACAAGCATCTTGACAGCAGTAGCAATGAGCGTCCAGACATCAGTTCCATCCAG
AGACGTATTAAGAAAGTAACTCATGACATGGACATGTGCTATGGGATGATGGGAAGCCTG
TTTCGCAGTGGCTCCCGGCAGACCCTTTTTGCCAGTCAAGTGATGCGTTATGCTGACCTC
TATGCAGCATCTTTCATCAACCTGCTGTATTACCCTTTCAGCTACCTCTTCAGGGCTGCC
CATGTCTTGATGCCTCATGAATCAACGGTGGAGCACACACACGTAGATATCAATGAGATG
GAGTCTCCTCTTGCCACCCGGAACCGCACATCAGTGGATTTCAAAGACACTGACTACAAG
CGGCACCAGCTGACACGGTCAATTAGTGAGATTAAACCTCCCAACCTCTTCCCACTGGCC
CCCCAGGAAATTACACACTGCCATGACGAAGATGATGATGAAGAGGAGGAGGAGGAGGAA
GAATAA
Enzyme 5 GenBank Gene ID D38524 Link Image
Enzyme 5 GeneCard ID NT5C2 Link Image
Enzyme 5 GenAtlas ID NT5C2 Link Image
Enzyme 5 HGNC ID HGNC:8022 Link Image
Enzyme 5 Chromosome Location 10
Enzyme 5 Locus 10q24.32-q24.33
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Oka J, Matsumoto A, Hosokawa Y, Inoue S: Molecular cloning of human cytosolic purine 5'-nucleotidase. Biochem Biophys Res Commun. 1994 Nov 30;205(1):917-22. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5805
Enzyme 6 Name Purine nucleoside phosphorylase
Enzyme 6 Synonyms
  1. Inosine phosphorylase
  2. PNP
Enzyme 6 Gene Name NP
Enzyme 6 Protein Sequence >Purine nucleoside phosphorylase 
MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRST
VPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGL
NPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQ
MGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSL
ITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
Enzyme 6 Number of Residues 289
Enzyme 6 Molecular Weight 32118
Enzyme 6 Theoretical pI 6.95
Enzyme 6 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 6 General Function Nucleotide transport and metabolism
Enzyme 6 Specific Function Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
Enzyme 6 Pathways
Enzyme 6 Reactions
  • purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 35565 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P00491 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PNPH_HUMAN Link Image
Enzyme 6 PDB ID 1RT9 Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >870 bp 
ATGGAGAACGGATACACCTATGAAGATTATAAGAACACTGCAGAATGGCTTCTGTCTCAT
ACTAAGCACCGACCTCAAGTTGCAATAATCTGTGGTTCTGGATTAGGAGGTCTGACTGAT
AAATTAACTCAGGCCCAGATCTTTGACTACAGTGAAATCCCCAACTTTCCTCGAAGTACA
GTGCCAGGTCATGCTGGCCGACTGGTGTTTGGGTTCCTGAATGGCAGGGCCTGTGTGATG
ATGCAGGGCAGGTTCCACATGTATGAAGGGTACCCACTCTGGAAGGTGACATTCCCAGTG
AGGGTTTTCCACCTTCTGGGTGTGGACACCCTGGTAGTCACCAATGCAGCAGGAGGGCTG
AACCCCAAGTTTGAGGTTGGAGATATCATGCTGATCCGTGACCATATCAACCTACCTGGT
TTCAGTGGTCAGAACCCTCTCAGAGGGCCCAATGATGAAAGGTTTGGAGATCGTTTCCCT
GCCATGTCTGATGCCTACGACCGGACTATGAGGCAGAGGGCTCTCAGTACCTGGAAACAA
ATGGGGGAGCAACGTGAGCTACAGGAAGGCACCTATGTGATGGTGGCAGGCCCCAGCTTT
GAGACTGTGGCAGAATGTCGTGTGCTGCAGAAGCTGGGAGCAGACGCTGTTGGCATGAGT
ACAGTACCAGAAGTTATCGTTGCACGGCACTGTGGACTTCGAGTCTTTGGCTTCTCACTC
ATCACTAACAAGGTCATCATGGATTATGAAAGCCTGGAGAAGGCCAACCATGAAGAAGTC
TTAGCAGCTGGCAAACAAGCTGCACAGAAATTGGAACAGTTTGTCTCCATTCTTATGGCC
AGCATTCCACTCCCTGACAAAGCCAGTTGA
Enzyme 6 GenBank Gene ID X00737 Link Image
Enzyme 6 GeneCard ID NP Link Image
Enzyme 6 GenAtlas ID NP Link Image
Enzyme 6 HGNC ID HGNC:7892 Link Image
Enzyme 6 Chromosome Location 14
Enzyme 6 Locus 14q13.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5806
Enzyme 7 Name Thymidine phosphorylase precursor
Enzyme 7 Synonyms
  1. TdRPase
  2. TP
  3. Platelet-derived endothelial cell growth factor
  4. PD-ECGF
  5. Gliostatin
Enzyme 7 Gene Name ECGF1
Enzyme 7 Protein Sequence >Thymidine phosphorylase precursor 
MAALMTPGTGAPPAPGDFSGEGSQGLPDPSPEPKQLPELIRMKRDGGRLSEADIRGFVAA
VVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQQLVDKHSTGG
VGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQA
GCCIVGQSEQLVPADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAA
VFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKPLGRCVGHALEVEEALLCMDGAGPP
DLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPGLARAL
CSGSPAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVG
AELLVDVGQRLRRGTPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAPSPFAELVLPP
QQ
Enzyme 7 Number of Residues 482
Enzyme 7 Molecular Weight 49956
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 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 7 Pathways
Enzyme 7 Reactions
  • thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 189701 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P19971 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name TYPH_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 >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 7 GenBank Gene ID M63193 Link Image
Enzyme 7 GeneCard ID ECGF1 Link Image
Enzyme 7 GenAtlas ID ECGF1 Link Image
Enzyme 7 HGNC ID HGNC:3148 Link Image
Enzyme 7 Chromosome Location 22
Enzyme 7 Locus 22q13|22q13.33
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6043
Enzyme 8 Name Deoxyguanosine kinase, mitochondrial precursor
Enzyme 8 Synonyms
  1. dGK
Enzyme 8 Gene Name DGUOK
Enzyme 8 Protein Sequence >Deoxyguanosine kinase, mitochondrial precursor 
MAAGRLFLSRLRAPFSSMAKSPLEGVSSSRGLHAGRGPRRLSIEGNIAVGKSTFVKLLTK
TYPEWHVATEPVATWQNIQAAGTQKACTAQSLGNLLDMMYREPARWSYTFQTFSFLSRLK
VQLEPFPEKLLQARKPVQIFERSVYSDRYIFAKNLFENGSLSDIEWHIYQDWHSFLLWEF
ASRITLHGFIYLQASPQVCLKRLYQRAREEEKGIELAYLEQLHGQHEAWLIHKTTKLHFE
ALMNIPVLVLDVNDDFSEEVTKQEDLMREVNTFVKNL
Enzyme 8 Number of Residues 277
Enzyme 8 Molecular Weight 32056
Enzyme 8 Theoretical pI 8.97
Enzyme 8 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
—
Enzyme 8 General Function Nucleotide transport and metabolism
Enzyme 8 Specific Function Required for the phosphorylation of several deoxyribonucleosides and certain nucleoside analogs widely employed as antiviral and chemotherapeutic agents
Enzyme 8 Pathways
Enzyme 8 Reactions
  • ATP + deoxyguanosine = ADP + dGMP
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-19
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 1477482 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q16854 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name DGUOK_HUMAN Link Image
Enzyme 8 PDB ID 1JAG Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >834 bp 
ATGGCCGCGGGCCGCCTCTTTCTAAGTCGGCTTCGAGCACCCTTCAGTTCCATGGCCAAG
AGCCCACTCGAGGGCGTTTCCTCCTCCAGAGGCCTGCACGCGGGGCGCGGGCCCCGAAGG
CTCTCCATCGAAGGCAACATTGCTGTGGGAAAGTCCACGTTTGTGAAGTTACTCACGAAA
ACTTACCCAGAATGGCACGTAGCTACAGAACCTGTAGCAACATGGCAGAATATCCAGGCT
GCTGGCAACCAAAAAGCCTGCACTGCCCAAAGTCTTGGAAACTTGCTGGATATGATGTAC
CGGGAGCCAGCACGATGGTCCTACACATTCCAGACATTTTCCTTTTTGAGCCGCCTGAAA
GTACAGCTGGAGCCCTTCCCTGAGAAACTCTTACAGGCCAGGAAGCCAGTACAGATCTTT
GAGAGGTCTGTGTACAGTGACAGGTATATCTTTGCAAAGAATCTTTTTGAAAATGGTTCC
CTCAGTGACATCGAGTGGCATATCTATCAGGACTGGCATTCTTTTCTCCTGTGGGAGTTT
GCCAGCCGGATCACATTACATGGCTTCATCTACCTCCAGGCTTCTCCCCAGGTTTGTTTG
AAGAGACTGTACCAGAGGGCCAGGGAGGAGGAGAAAGGAATTGAGCTGGCCTATCTAGAG
CAGCTGCATGGCCAACACGAAGCCTGGCTTATTCACAAGACAACGAAGCTCCACTTTGAG
GCTCTGATGAACATTCCAGTGCTGGTGTTGGATGTCAATGATGATTTTTCTGAGGAAGTA
ACCAAACAAGAAGACCTCATGAGAGAGGTAAACACCTTTGTAAAGAATCTGTAA
Enzyme 8 GenBank Gene ID U41668 Link Image
Enzyme 8 GeneCard ID DGUOK Link Image
Enzyme 8 GenAtlas ID DGUOK Link Image
Enzyme 8 HGNC ID HGNC:2858 Link Image
Enzyme 8 Chromosome Location 2
Enzyme 8 Locus 2p13
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Johansson M, Karlsson A: Cloning and expression of human deoxyguanosine kinase cDNA. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):7258-62. [PubMed Link Image]
  2. Wang L, Hellman U, Eriksson S: Cloning and expression of human mitochondrial deoxyguanosine kinase cDNA. FEBS Lett. 1996 Jul 15;390(1):39-43. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 8749
Enzyme 9 Name Cytosolic 5'-nucleotidase III
Enzyme 9 Synonyms
  1. cN-III
  2. Pyrimidine 5'- nucleotidase 1
  3. P5'N-1
  4. P5N-1
  5. PN-I
  6. Uridine 5'-monophosphate hydrolase 1
  7. p36
Enzyme 9 Gene Name NT5C3
Enzyme 9 Protein Sequence >Cytosolic 5'-nucleotidase III 
MRAPSMDRAAVARVGAVASASVCALVAGVVLAQYIFTLKRKTGRKTKIIEMMPEFQKSSV
RIKNPTRVEEIICGLIKGGAAKLQIITDFDMTLSRFSYKGKRCPTCHNIIDNCKLVTDEC
RKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQALPKAKLKEIVAESDVM
LKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLK
GFKGELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYL
NDRVDELLEKYMDSYDIVLVQDESLEVANSILQKIL
Enzyme 9 Number of Residues 336
Enzyme 9 Molecular Weight 37949
Enzyme 9 Theoretical pI 7.15
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate
Enzyme 9 Pathways
Enzyme 9 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-32
Enzyme 9 Transmembrane Regions
  • 13-35
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 11245474 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q9H0P0 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name 5NT3_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >861 bp 
ATGATGCCAGAATTCCAGAAAAGTTCAGTTCGAATCAAGAACCCTACAAGAGTAGAAGAA
ATTATCTGTGGTCTTATCAAAGGAGGAGCTGCCAAACTTCAGATAATAACGGACTTTGAT
ATGACACTCAGTAGATTTTCATATAAAGGGAAAAGATGCCCAACATGTCATAATATCATT
GACAACTGTAAGCTGGTTACAGATGAATGTAGAAAAAAGTTATTGCAACTAAAGGAAAAA
TACTACGCTATTGAAGTTGATCCTGTTCTTACTGTAGAAGAGAAGTACCCTTATATGGTG
GAATGGTATACTAAATCACATGGTTTGCTTGTTCAGCAAGCTTTACCAAAAGCTAAACTT
AAAGAAATTGTGGCAGAATCTGACGTTATGCTCAAAGAAGGATATGAGAATTTCTTTGAT
AAGCTCCAACAACATAGCATCCCCGTGTTCATATTTTCGGCTGGAATCGGCGATGTACTA
GAGGAAGTTATTCGTCAAGCTGGTGTTTATCATCCCAATGTCAAAGTTGTGTCCAATTTT
ATGGATTTTGATGAAACTGGGGTGCTCAAAGGATTTAAAGGAGAACTAATTCATGTATTT
AACAAACATGATGGTGCCTTGAGGAATACAGAATATTTCAATCAACTAAAAGACAATAGT
AACATAATTCTTCTGGGAGACTCCCAAGGAGACTTAAGAATGGCAGATGGAGTGGCCAAT
GTTGAGCACATTCTGAAAATTGGATATCTAAATGATAGAGTGGATGAGCTTTTAGAAAAG
TACATGGACTCTTATGATATTGTTTTAGTACAAGATGAATCATTAGAAGTAGCCAACTCT
ATTTTACAGAAGATTCTATAA
Enzyme 9 GenBank Gene ID AF312735 Link Image
Enzyme 9 GeneCard ID NT5C3 Link Image
Enzyme 9 GenAtlas ID NT5C3 Link Image
Enzyme 9 HGNC ID HGNC:17820 Link Image
Enzyme 9 Chromosome Location 7
Enzyme 9 Locus 7p14.3
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Amici A, Emanuelli M, Raffaelli N, Ruggieri S, Saccucci F, Magni G: Human erythrocyte pyrimidine 5-nucleotidase, PN-I, is identical to p36, a protein associated to lupus inclusion formation in response to alpha-interferon. Blood. 2000 Aug 15;96(4):1596-8. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  3. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
  4. Rich SA, Bose M, Tempst P, Rudofsky UH: Purification, microsequencing, and immunolocalization of p36, a new interferon-alpha-induced protein that is associated with human lupus inclusions. J Biol Chem. 1996 Jan 12;271(2):1118-26. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 15061
Enzyme 10 Name cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name Not Available
Enzyme 10 Protein Sequence >cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA 
MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLV
CAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTS
CETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMK
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLA
SQEITHCHDEDDDEEEEEEEE
Enzyme 10 Number of Residues 561
Enzyme 10 Molecular Weight 64960
Enzyme 10 Theoretical pI 6.05
Enzyme 10 GO Classification Not Available
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function Not Available
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 158256766 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID A8K6K2 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name A8K6K2_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1686 bp 
ATGTCAACCTCCTGGAGTGATCGGTTACAGAATGCAGCAGATATGCCTGCTAACATGGAT
AAGCATGCCCTGAAAAAGTATCGTCGAGAAGCCTATCATCGGGTGTTTGTGAACCGAAGT
TTAGCAATGGAAAAGATAAAGTGTTTTGGTTTTGATATGGATTATACCCTTGCTGTGTAC
AAGTCCCCAGAGTATGAGTCCCTTGGTTTTGAGCTTACTGTGGAGAGATTAGTTTCTATT
GGCTATCCCCAGGAGTTGCTCAGCTTTGCTTATGATTCTACATTCCCTACCAGGGGACTT
GTCTTTGACACACTGTATGGAAATCTTTTGAAAGTCGATGCCTATGGAAACCTCTTGGTC
TGTGCACATGGATTTAACTTTATAAGGGGACCAGAAACTAGAGAACAGTATCCAAATAAA
TTTATCCAGCGAGATGATACTGAAAGATTTTACATTCTGAACACACTATTCAACCTACCA
GAGACCTACCTGTTGGCCTGCCTAGTAGATTTTTTTACTAATTGTCCCAGATATACCAGT
TGTGAAACAGGATTTAAAGATGGGGACCTCTTCATGTCCTACCGGAGTATGTTCCAGGAT
GTAAGAGATGCTGTTGACTGGGTTCATTACAAGGGCTCCCTTAAGGAAAAGACAGTTGAA
AATCTTGAGAAGTATGTAGTCAAAGATGGAAAACTGCCTTTGCTTCTGAGCCGGATGAAG
GAAGTAGGGAAAGTATTTCTTGCTACCAACAGTGACTATAAATATACAGATAAAATTATG
ACTTACCTGTTTGACTTCCCACATGGCCCCAAGCCTGGGAGCTCCCATCGACCATGGCAG
TCCTACTTTGACTTGATCTTGGTGGATGCACGGAAACCACTCTTTTTTGGAGAAGGCACA
GTACTGCGTCAGGTGGATACTAAAACTGGCAAGCTGAAAATTGGTACCTACACAGGGCCC
CTACAGCATGGTATCGTCTACTCAGGAGGTTCTTCTGATACGATCTGTGACCTGTTGGGA
GCCAAGGGAAAAGACATTTTGTATATTGGAGATCACATTTTTGGGGACATTTTAAAATCA
AAGAAACGGCAAGGGTGGCGAACTTTTTTGGTGATTCCTGAACTCGCACAGGAGCTACAT
GTCTGGACTGACAAGAGTTCACTTTTCGAAGAACTTCAGAGCTTGGATATTTTCTTGGCT
GAACTCTACAAGCATCTTGACAGCAGTAGCAATGAGCGTCCAGACATCAGTTCCATCCAG
AGACGTATTAAGAAAGTAACTCATGACATGGACATGTGCTATGGGATGATGGGAAGCCTG
TTTCGCAGTGGCTCCCGGCAGACCCTTTTTGCCAGTCAAGTGATGCGTTATGCTGACCTC
TATGCAGCATCTTTCATCAACCTGCTGTATTACCCTTTCAGCTACCTCTTCAGGGCTGCC
CATGTCTTGATGCCTCATGAATCAACGGTGGAGCACACACACGTAGATATCAATGAGATG
GAGTCTCCTCTTGCCACCCGGAACCGCACATCAGTGGATTTCAAAGACACTGACTACAAG
CGGCACCAGCTGACACGGTCAATTAGTGAGATTAAACCTCCCAACCTCTTCCCACTGGCC
TCCCAGGAAATTACACACTGCCATGATGAAGATGATGATGAAGAGGAGGAGGAGGAGGAA
GAATAA
Enzyme 10 GenBank Gene ID AK291667 Link Image
Enzyme 10 GeneCard ID A8K6K2 Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs Not Available
Enzyme 10 General References Not Available
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 16421
Enzyme 11 Name cDNA, FLJ95575, highly similar to Homo sapiens endothelial cell growth factor 1 (platelet-derived) (ECGF1), mRNA
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name Not Available
Enzyme 11 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 11 Number of Residues 482
Enzyme 11 Molecular Weight 49924
Enzyme 11 Theoretical pI 5.19
Enzyme 11 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 11 General Function Nucleotide transport and metabolism
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein Not Available
Enzyme 11 UniProtKB/Swiss-Prot ID B2RBL3 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name B2RBL3_HUMAN Link Image
Enzyme 11 PDB ID 1UOU Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID AK314716 Link Image
Enzyme 11 GeneCard ID B2RBL3 Link Image
Enzyme 11 GenAtlas ID Not Available
Enzyme 11 HGNC ID Not Available
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs Not Available
Enzyme 11 General References Not Available
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 16422
Enzyme 12 Name cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name Not Available
Enzyme 12 Protein Sequence >cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA 
MCPRAARAPATLLLALGAVLWPAAGAWELTILHTNDVHSRLEQTSEDSSKCVNASRCMGG
VARLFTKVQQIRRAEPNVLLLDAGDQYQGTIWFTVYRGAEVAHFMNALRYDAMALGNHEF
DNGVEGLIEPLLKEAKFPILSANIKAKGPLASQISGLYLPYKVLPVGDEVVGIVGYTSKE
TPFLSNPGTNLVFEDEITALQPEVDKLKTLNVNKIIALGHSGFEMDKLIAQKVRGVDVVV
GGHSNTFLYTGNPPSKEVPAGKYPFIVTSDDGRKVPVVQAYAFGKYLGYLKIEFDERGNV
ISSHGNPILLNSSIPEDPSIKADINKWRIKLDNYSTQELGKTIVYLDGSSQSCRFRECNM
GNLICDAMINNNLRHTDEMFWNHVSMCILNGGGIRSPIDERNNGTITWENLAAVLPFGGT
FDLVQLKGSTLKKAFEHSVHRYGQSTGEFLQVGGIHVVYDLSRKPGDRVVKLDVLCTKCR
VPSYDPLKMDEVYKVILPNFLANGGDGFQMIKDELLRHDSGDQDINVVSTYISKMKVIYP
AVEGRIKFSTGSHCHGSFSLIFLSLWAVIFVLYQ
Enzyme 12 Number of Residues 574
Enzyme 12 Molecular Weight 63396
Enzyme 12 Theoretical pI 7.04
Enzyme 12 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide catabolism
  • nucleotide metabolism
  • physiological process
Component
—
Enzyme 12 General Function Nucleotide transport and metabolism
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID B2RBH2 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name B2RBH2_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID AK314661 Link Image
Enzyme 12 GeneCard ID B2RBH2 Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs Not Available
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available