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Showing drug card for Azathioprine (DB00993)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:07:43
Primary Accession Number DB00993
Secondary Accession Number
  • APRD00811
Name Azathioprine
Drug Type
  • Approved
  • Small Molecule
Description An immunosuppressive agent used in combination with cyclophosphamide and hydroxychloroquine in the treatment of rheumatoid arthritis. According to the Fourth Annual Report on Carcinogens (NTP 85-002, 1985), this substance has been listed as a known carcinogen. (Merck Index, 11th ed)
Synonyms
  1. Azathioprin
  2. Azathioprine Sodium
  3. Azatioprin
  4. Azothioprine
Brand Names
  1. Azamun
  2. Azanin
  3. Azasan
  4. Ccucol
  5. Imuran
  6. Imurek
  7. Imurel
  8. Muran
Brand Mixtures Not Available
Chemical IUPAC Name 6-(3-methyl-5-nitroimidazol-4-yl)sulfanyl-7H-purine
Chemical Formula C9H7N7O2S
Chemical Structure Structure
CAS Registry Number 446-86-6
InChI Identifier InChI=1/C9H7N7O2S/c1-15-4-14-7(16(17)18)9(15)19-8-5-6(11-2-10-5)12-3-13-8/h2-4H,1H3,(H,10,11,12,13)/f/h10H
InChI Key LMEKQMALGUDUQG-KZFATGLACK
KEGG Drug D00238 Link Image
KEGG Compound Not Available
PubChem Compound 2265 Link Image
PubChem Substance 9055 Link Image
ChEBI ID Not Available
PharmGKB ID PA448515 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02242907 Link Image
RxList Link http://www.rxlist.com/cgi/generic/azathioprine.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Azathioprine Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 277.2630
Monoisotopic Molecular Weight 277.0382
State Solid
Melting Point 243.5 oC
Experimental Water Solubility 272 mg/L Source: PhysProp
Predicted Water Solubility 1.07e+00 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 0.7 Source: PhysProp
Predicted LogP 0.84 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -2.41 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Isomeric SMILES CN1C=NC(=C1SC1=NC=NC2=C1NC=N2)[N+]([O-])=O
Canonical SMILES CN1C=NC(=C1SC1=NC=NC2=C1NC=N2)[N+]([O-])=O
Drug Category
  • Antimetabolites
  • Antimetabolites, Antineoplastic
  • Antirheumatic Agents
  • Immunosuppressive Agents
ATC Codes
AHFS Codes
  • 92:00.00
Indication For use as an adjunct in the prevention of rejection in renal homotransplantation. Also for the management of severe, active rheumatoid arthritis unresponsive to rest, aspirin or other nonsteroidal anti-inflammatory drugs, or to agents in the class of which gold is an example.
Pharmacology Azathioprine is a chemotherapy drug, now rarely used for chemotherapy but more for immunosuppression in organ transplantation and autoimmune disease such as rheumatoid arthritis or inflammatory bowel disease or Crohn's disease. It is a pro-drug, converted in the body to the active metabolite 6-mercaptopurine. Azathioprine acts to inhibit purine synthesis necessary for the proliferation of cells, especially leukocytes and lymphocytes. It is a safe and effective drug used alone in certain autoimmune diseases, or in combination with other immunosuppressants in organ transplantation. Its most severe side effect is bone marrow suppression, and it should not be given in conjunction with purine analogues such as allopurinol. The enzyme thiopurine S-methyltransferase (TPMT) deactivates 6-mercaptopurine. Genetic polymorphisms of TPMT can lead to excessive drug toxicity, thus assay of serum TPMT may be useful to prevent this complication.
Mechanism of Action Azathioprine antagonizes purine metabolism and may inhibit synthesis of DNA, RNA, and proteins. It may also interfere with cellular metabolism and inhibit mitosis. The mechanism of action of azathioprine in rheumatoid arthritis is not known but is most likely related to its immunosuppresive action.
Absorption Well absorbed following oral administration.
Toxicity The oral LD50 for single doses of azathioprine in mice and rats are 2500 mg/kg and 400 mg/kg, respectively. Very large doses of this antimetabolite may lead to marrow hypoplasia, bleeding, infection, and death.
Protein Binding Azathioprine and the metabolite mercaptopurine are moderately bound to serum proteins (30%).
Biotransformation Primarily converted to the active metabolites 6-mercaptopurine and 6-thioinosinic acid.
Half Life Approximately 5 hours for the unchanged drug and its metabolites.
Dosage Forms
Form Route
Powder, for solution Intravenous
Tablet Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Acenocoumarol The thiopurine decreases the anticoagulant effect
Allopurinol Allopurinol increases the effect of thiopurine
Anisindione The thiopurine decreases the anticoagulant effect
Atracurium The agent decreases the effect of the muscle relaxant
Dicumarol The thiopurine decreases the anticoagulant effect
Doxacurium The agent decreases the effect of the muscle relaxant
Gallamine Triethiodide The agent decreases the effect of the muscle relaxant
Mesalazine The 5-ASA derivative increases the toxicity of thiopurine
Metocurine The agent decreases the effect of the muscle relaxant
Mivacurium The agent decreases the effect of the muscle relaxant
Olsalazine The 5-ASA derivative increases the toxicity of thiopurine
Pancuronium The agent decreases the effect of the muscle relaxant
Sulfasalazine The 5-ASA derivative increase the toxicity of thiopurine
Tubocurarine The agent decreases the effect of the muscle relaxant
Vecuronium The agent decreases the effect of the muscle relaxant
Warfarin The thiopurine decreases the anticoagulant effect
Food Interactions
  • Take with food to reduce irritation.
Pathways Not Available
General References
  1. Konstantopoulou M, Belgi A, Griffiths KD, Seale JR, Macfarlane AW: Azathioprine-induced pancytopenia in a patient with pompholyx and deficiency of erythrocyte thiopurine methyltransferase. BMJ. 2005 Feb 12;330(7487):350-1. [PubMed Link Image]
  2. Woodroffe R, Yao GL, Meads C, Bayliss S, Ready A, Raftery J, Taylor RS: Clinical and cost-effectiveness of newer immunosuppressive regimens in renal transplantation: a systematic review and modelling study. Health Technol Assess. 2005 May;9(21):1-179, iii-iv. [PubMed Link Image]
  3. Gombar VK, Enslein K, Blake BW: Carcinogenicity of azathioprine: an S-AR investigation. Mutat Res. 1993 May;302(1):7-12. [PubMed Link Image]
  4. Wikipedia Link Image
  5. RxList Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Thiopurine S-methyltransferase
Targets
  1. Hypoxanthine-guanine phosphoribosyltransferase
  2. GMP synthase [glutamine-hydrolyzing]
  3. AMP deaminase 1
  4. Amidophosphoribosyltransferase
  5. Inosine-5'-monophosphate dehydrogenase 2
  6. Inosine-5'-monophosphate dehydrogenase 1
  7. GMP reductase 1
  8. GMP reductase 2
  9. Adenylosuccinate lyase
  10. Adenylosuccinate synthase
  11. AMP deaminase 2
  12. AMP deaminase 3
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Thiopurine S-methyltransferase
Enzyme 1 Gene Name TPMT
Enzyme 1 SwissProt ID P51580 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >P51580|TPMT_HUMAN Thiopurine S-methyltransferase - Homo sapiens (Human) 
MDGTRTSLDIEEYSDTEVQKNQVLTLEEWQDKWVNGKTAFHQEQGHQLLKKHLDTFLKGK
SGLRVFFPLCGKAVEMKWFADRGHSVVGVEISELGIQEFFTEQNLSYSEEPITEIPGTKV
FKSSSGNISLYCCSIFDLPRTNIGKFDMIWDRGALVAINPGDRKCYADTMFSLLGKKFQY
LLCVLSYDPTKHPGPPFYVPHAEIERLFGKICNIRCLEKVDAFEERHKSWGIDCLFEKLY
LLTEK
Drug Target 1 [top]
Target 1 ID 87
Target 1 Name Hypoxanthine-guanine phosphoribosyltransferase
Target 1 Synonyms
  1. EC 2.4.2.8
  2. HGPRT
  3. HGPRTase
Target 1 Gene Name HPRT1
Target 1 Protein Sequence >Hypoxanthine-guanine phosphoribosyltransferase 
ATRSPGVVISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIMDRTERLARDVMKEMGGHH
IVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGDD
LSTLTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKRTPRSVGYKPDFVGF
EIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA
Target 1 Number of Residues 220
Target 1 Molecular Weight 24448
Target 1 Theoretical pI 6.67
Target 1 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring pentosyl groups
hypoxanthine phosphoribosyltransferase activity
Process
nucleoside metabolism
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
purine salvage
purine ribonucleoside salvage
Component
cell
intracellular
cytoplasm
Target 1 General Function Nucleotide transport and metabolism
Target 1 Specific Function Not Available
Target 1 Pathways
Name SMPDB Link KEGG Link
Purine metabolism SMP00050 Link Image map00230 Link Image
Target 1 Reactions
  • IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 306885 Link Image
Target 1 UniProtKB/Swiss-Prot ID P00492 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name HPRT_HUMAN Link Image
Target 1 PDB ID 1BZY Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Cytoplasm
Target 1 Gene Sequence >657 bp 
ATGGCGACCCGCAGCCCTGGCGTCGTGATTAGTGATGATGAACCAGGTTATGACCTTGAT
TTATTTTGCATACCTAATCATTATGCTGAGGATTTGGAAAGGGTGTTTATTCCTCATGGA
CTAATTATGGACAGGACTGAACGTCTTGCTCGAGATGTGATGAAGGAGATGGGAGGCCAT
CACATTGTAGCCCTCTGTGTGCTCAAGGGGGGCTATAAATTCTTTGCTGACCTGCTGGAT
TACATCAAAGCACTGAATAGAAATAGTGATAGATCCATTCCTATGACTGTAGATTTTATC
AGACTGAAGAGCTATTGTAATGACCAGTCAACAGGGGACATAAAAGTAATTGGTGGAGAT
GATCTCTCAACTTTAACTGGAAAGAATGTCTTGATTGTGGAAGATATAATTGACACTGGC
AAAACAATGCAGACTTTGCTTTCCTTGGTCAGGCAGTATAATCCAAAGATGGTCAAGGTC
GCAAGCTTGCTGGTGAAAAGGACCCCACGAAGTGTTGGATATAAGCCAGACTTTGTTGGA
TTTGAAATTCCAGACAAGTTTGTTGTAGGATATGCCCTTGACTATAATGAATACTTCAGG
GATTTGAATCATGTTTGTGTCATTAGTGAAACTGGAAAAGCAAAATACAAAGCCTAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID HPRT1 Link Image
Target 1 GenAtlas ID HPRT1 Link Image
Target 1 HGNC ID HGNC:5157 Link Image
Target 1 Chromosome Location X
Target 1 Locus Xq26.1
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Balendiran GK, Molina JA, Xu Y, Torres-Martinez J, Stevens R, Focia PJ, Eakin AE, Sacchettini JC, Craig SP 3rd: Ternary complex structure of human HGPRTase, PRPP, Mg2+, and the inhibitor HPP reveals the involvement of the flexible loop in substrate binding. Protein Sci. 1999 May;8(5):1023-31. [PubMed Link Image]
  2. Shi W, Li CM, Tyler PC, Furneaux RH, Grubmeyer C, Schramm VL, Almo SC: The 2.0 A structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor. Nat Struct Biol. 1999 Jun;6(6):588-93. [PubMed Link Image]
  3. Sege-Peterson K, Chambers J, Page T, Jones OW, Nyhan WL: Characterization of mutations in phenotypic variants of hypoxanthine phosphoribosyltransferase deficiency. Hum Mol Genet. 1992 Sep;1(6):427-32. [PubMed Link Image]
  4. Sculley DG, Dawson PA, Emmerson BT, Gordon RB: A review of the molecular basis of hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. Hum Genet. 1992 Nov;90(3):195-207. [PubMed Link Image]
  5. Lightfoot T, Joshi R, Nuki G, Snyder FF: The point mutation of hypoxanthine-guanine phosphoribosyltransferase (HPRTEdinburgh) and detection by allele-specific polymerase chain reaction. Hum Genet. 1992 Mar;88(6):695-6. [PubMed Link Image]
  6. Yamada Y, Goto H, Ogasawara N: Identification of two independent Japanese mutant HPRT genes using the PCR technique. Adv Exp Med Biol. 1991;309B:121-4. [PubMed Link Image]
  7. Sculley DG, Dawson PA, Beacham IR, Emmerson BT, Gordon RB: Hypoxanthine-guanine phosphoribosyltransferase deficiency: analysis of HPRT mutations by direct sequencing and allele-specific amplification. Hum Genet. 1991 Oct;87(6):688-92. [PubMed Link Image]
  8. Davidson BL, Tarle SA, Van Antwerp M, Gibbs DA, Watts RW, Kelley WN, Palella TD: Identification of 17 independent mutations responsible for human hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. Am J Hum Genet. 1991 May;48(5):951-8. [PubMed Link Image]
  9. Tarle SA, Davidson BL, Wu VC, Zidar FJ, Seegmiller JE, Kelley WN, Palella TD: Determination of the mutations responsible for the Lesch-Nyhan syndrome in 17 subjects. Genomics. 1991 Jun;10(2):499-501. [PubMed Link Image]
  10. Gordon RB, Sculley DG, Dawson PA, Beacham IR, Emmerson BT: Identification of a single nucleotide substitution in the coding sequence of in vitro amplified cDNA from a patient with partial HPRT deficiency (HPRTBRISBANE). J Inherit Metab Dis. 1990;13(5):692-700. [PubMed Link Image]
  11. 2341149 Edwards A, Voss H, Rice P, Civitello A, Stegemann J, Schwager C, Zimmermann J, Erfle H, Caskey CT, Ansorge W: Automated DNA sequencing of the human HPRT locus. Genomics. 1990 Apr;6(4):593-608.
  12. 2347587 Gibbs RA, Nguyen PN, Edwards A, Civitello AB, Caskey CT: Multiplex DNA deletion detection and exon sequencing of the hypoxanthine phosphoribosyltransferase gene in Lesch-Nyhan families. Genomics. 1990 Jun;7(2):235-44.
  13. 2358296 Skopek TR, Recio L, Simpson D, Dallaire L, Melancon SB, Ogier H, O'Neill JP, Falta MT, Nicklas JA, Albertini RJ: Molecular analyses of a Lesch-Nyhan syndrome mutation (hprtMontreal) by use of T-lymphocyte cultures. Hum Genet. 1990 Jun;85(1):111-6.
  14. 2572141 Igarashi T, Minami M, Nishida Y: Molecular analysis of hypoxanthine-guanine phosphoribosyltransferase mutations in five unrelated Japanese patients. Acta Paediatr Jpn. 1989 Jun;31(3):303-13.
  15. 2738157 Davidson BL, Tarle SA, Palella TD, Kelley WN: Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in ten subjects determined by direct sequencing of amplified transcripts. J Clin Invest. 1989 Jul;84(1):342-6.
  16. 2896620 Fujimori S, Hidaka Y, Davidson BL, Palella TD, Kelley WN: Identification of a single nucleotide change in a mutant gene for hypoxanthine-guanine phosphoribosyltransferase (HPRT Ann Arbor). Hum Genet. 1988 May;79(1):39-43.
  17. 2909537 Davidson BL, Pashmforoush M, Kelley WN, Palella TD: Human hypoxanthine-guanine phosphoribosyltransferase deficiency. The molecular defect in a patient with gout (HPRTAshville). J Biol Chem. 1989 Jan 5;264(1):520-5.
  18. 2910902 Fujimori S, Davidson BL, Kelley WN, Palella TD: Identification of a single nucleotide change in the hypoxanthine-guanine phosphoribosyltransferase gene (HPRTYale) responsible for Lesch-Nyhan syndrome. J Clin Invest. 1989 Jan;83(1):11-3.
  19. 2928313 Gibbs RA, Nguyen PN, McBride LJ, Koepf SM, Caskey CT: Identification of mutations leading to the Lesch-Nyhan syndrome by automated direct DNA sequencing of in vitro amplified cDNA. Proc Natl Acad Sci U S A. 1989 Mar;86(6):1919-23.
  20. 3023844 Patel PI, Framson PE, Caskey CT, Chinault AC: Fine structure of the human hypoxanthine phosphoribosyltransferase gene. Mol Cell Biol. 1986 Feb;6(2):393-403.
  21. 3148064 Keough DT, Gordon RB, de Jersey J, Emmerson BT: Biochemical basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in nine families. J Inherit Metab Dis. 1988;11(3):229-38.
  22. 3198771 Davidson BL, Chin SJ, Wilson JM, Kelley WN, Palella TD: Hypoxanthine-guanine phosphoribosyltransferase. Genetic evidence for identical mutations in two partially deficient subjects. J Clin Invest. 1988 Dec;82(6):2164-7.
  23. 3265398 Davidson BL, Palella TD, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase: a single nucleotide substitution in cDNA clones isolated from a patient with Lesch-Nyhan syndrome (HPRTMidland). Gene. 1988 Aug 15;68(1):85-91.
  24. 3358423 Cariello NF, Scott JK, Kat AG, Thilly WG, Keohavong P: Resolution of a missense mutant in human genomic DNA by denaturing gradient gel electrophoresis and direct sequencing using in vitro DNA amplification: HPRT Munich. Am J Hum Genet. 1988 May;42(5):726-34.
  25. 3384338 Davidson BL, Pashmforoush M, Kelley WN, Palella TD: Genetic basis of hypoxanthine guanine phosphoribosyltransferase deficiency in a patient with the Lesch-Nyhan syndrome (HPRTFlint). Gene. 1988 Mar 31;63(2):331-6.
  26. 6300847 Jolly DJ, Okayama H, Berg P, Esty AC, Filpula D, Bohlen P, Johnson GG, Shively JE, Hunkapillar T, Friedmann T: Isolation and characterization of a full-length expressible cDNA for human hypoxanthine phosphoribosyl transferase. Proc Natl Acad Sci U S A. 1983 Jan;80(2):477-81.
  27. 6572373 Wilson JM, Tarr GE, Kelley WN: Human hypoxanthine (guanine) phosphoribosyltransferase: an amino acid substitution in a mutant form of the enzyme isolated from a patient with gout. Proc Natl Acad Sci U S A. 1983 Feb;80(3):870-3.
  28. 6706936 Wilson JM, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. Structural alteration in a dysfunctional enzyme variant (HPRTMunich) isolated from a patient with gout. J Biol Chem. 1984 Jan 10;259(1):27-30.
  29. 6853490 Wilson JM, Kobayashi R, Fox IH, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. J Biol Chem. 1983 May 25;258(10):6458-60.
  30. 6853716 Wilson JM, Kelley WN: Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in a patient with the Lesch-Nyhan syndrome. J Clin Invest. 1983 May;71(5):1331-5.
  31. 7107641 Wilson JM, Tarr GE, Mahoney WC, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme. J Biol Chem. 1982 Sep 25;257(18):10978-85.
  32. 7627191 Burgemeister R, Rotzer E, Gutensohn W, Gehrke M, Schiel W: Identification of a new missense mutation in exon 2 of the human hypoxanthine phosphoribosyltransferase gene (HPRTIsar): a further example of clinical heterogeneity in HPRT deficiencies. Hum Mutat. 1995;5(4):341-4.
  33. 8044844 Eads JC, Scapin G, Xu Y, Grubmeyer C, Sacchettini JC: The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP. Cell. 1994 Jul 29;78(2):325-34.
  34. 9003484 Fujimori S, Sakuma R, Yamaoka N, Hakoda M, Yamanaka H, Kamatani N: An asymptomatic germline missense base substitution in the hypoxanthine phosphoribosyltransferase (HPRT) gene that reduces the amount of enzyme in humans. Hum Genet. 1997 Jan;99(1):8-10.
  35. 9452051 Liu G, Aral B, Zabot MT, Kamoun P, Ceballos-Picot I: The molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in French families; report of two novel mutations. Hum Mutat. 1998;Suppl 1:S88-90.
Target 1 Drug References Not Available
Drug Target 2 [top]
Target 2 ID 355
Target 2 Name GMP synthase [glutamine-hydrolyzing]
Target 2 Synonyms
  1. EC 6.3.5.2
  2. GMP synthetase
  3. Glutamine amidotransferase
Target 2 Gene Name GMPS
Target 2 Protein Sequence >GMP synthase [glutamine-hydrolyzing] 
MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETP
AFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHK
KSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANE
SKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVL
VLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAA
HSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPE
EVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVR
ILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPH
TLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDW
ESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILR
ESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVE
VVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
Target 2 Number of Residues 704
Target 2 Molecular Weight 76716
Target 2 Theoretical pI 6.86
Target 2 GO Classification
Function
GMP synthase (glutamine-hydrolyzing) activity
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
ligase activity
ligase activity, forming carbon-nitrogen bonds
carbon-nitrogen ligase activity, with glutamine as amido-N-donor
GMP synthase (glutamine-hydrolyzing) activity
molecular function unknown
catalytic activity
Process
purine nucleoside monophosphate biosynthesis
purine ribonucleoside monophosphate biosynthesis
GMP biosynthesis
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleotide metabolism
purine nucleotide metabolism
purine nucleotide biosynthesis
cellular metabolism
amino acid and derivative metabolism
amino acid metabolism
glutamine family amino acid metabolism
glutamine metabolism
physiological process
metabolism
biosynthesis
Component
Not Available
Target 2 General Function Nucleotide transport and metabolism
Target 2 Specific Function Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division
Target 2 Pathways
Name SMPDB Link KEGG Link
Glutamate metabolism SMP00072 Link Image map00251 Link Image
Purine metabolism SMP00050 Link Image map00230 Link Image
Target 2 Reactions
  • ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 595410 Link Image
Target 2 UniProtKB/Swiss-Prot ID P49915 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name GUAA_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Cytoplasm
Target 2 Gene Sequence >2082 bp 
ATGGCTCTGTGCAACGGAGACTCCAAGCTGGAGAATGCTGGAGGAGACCTTAAGGATGGC
CACCACCACTATGAAGGAGCTGTTGTCATTCTGGATGCTGGTGCTCAGTACGGGAAAGTC
ATAGACCGAAGAGTGAGGGAACTGTTCGTGCAGTCTGAAATTTTCCCCTTGGAAACACCA
GCATTTGCTATAAAGGAACAAGGATTCCGTGCTATTATCATCTCTGGAGGACCTAATTCT
GTGTATGCTGAAGATGCTCCCTGGTTTGATCCAGCAATATTCACTATTGGCAAGCCTGTT
CTTGGAATTTGCTATGGTATGCAGATGATGAATAAGGTATTTGGAGGTACTGTGCACAAA
AAAAGTGTCAGAGAAGATGGAGTTTTCAACATTAGTGTGGATAATACATGTTCATTATTC
AGGGGCCTTCAGAAGGAAGAAGTTGTTTTGCTTACACATGGAGATAGTGTAGACAAAGTA
GCTGATGGATTCAAGGTTGTGGCACGTTCTGGAAACATAGTAGCAGGCATAGCAAATGAA
TCTAAAAAGTTATATGGAGCACAGTTCCACCCTGAAGTTGGCCTTACAGAAAATGGAAAA
GTAATACTGAAGAATTTCCTTTATGATATAGCTGGATGCAGTGGAACCTTCACCGTGCAG
AACAGAGAACTTGAGTGTATTCGAGAGATCAAAGAGAGAGTAGGCACGTCAAAAGTTTTG
GTTTTACTCAGTGGTGGAGTAGACTCAACAGTTTGTACAGCTTTGCTAAATCGTGCTTTG
AACCAAGAACAAGTCATTGCTGTGCACATTGATAATGGCTTTATGAGAAAACGAGAAAGC
CAGTCTGTTGAAGAGGCCCTCAAAAAGCTTGGAATTCAGGTCAAAGTGATAAATGCTGCT
CATTCTTTCTACAATGGAACAACAACCCTACCAATATCAGATGAAGATAGAACCCCACGG
AAAAGAATTAGCAAAACGTTAAATATGACCACAAGTCCTGAAGAGAAAAGAAAAATCATT
GGGGATACTTTTGTTAAGATTGCCAATGAAGTAATTGGAGAAATGAACTTGAAACCAGAG
GAGGTTTTCCTTGCCCAAGGTACTTTACGGCCTGATCTAATTGAAAGTGCATCCCTTGTT
GCAAGTGGCAAAGCTGAACTCATCAAAACCCATCACAATGACACAGAGCTCATCAGAAAG
TTGAGAGAGGAGGGAAAAGTAATAGAACCTCTGAAAGATTTTCATAAAGATGAAGTGAGA
ATTTTGGGCAGAGAACTTGGACTTCCAGAAGAGTTAGTTTCCAGGCATCCATTTCCAGGT
CCTGGCCTGGCAATCAGAGTAATATGTGCTGAAGAACCTTATATTTGTAAGGACTTTCCT
GAAACCAACAATATTTTGAAAATAGTAGCTGATTTTTCTGCAAGTGTTAAAAAGCCACAT
ACCCTATTACAGAGAGTCAAAGCCTGCACAACAGAAGAGGATCAGGAGAAGCTGATGCAA
ATTACCAGTCTGCATTCACTGAATGCCTTCTTGCTGCCAATTAAAACTGTAGGTGTGCAG
GGTGACTGTCGTTCCTACAGTTACGTGTGTGGAATCTCCAGTAAAGATGAACCTGACTGG
GAATCACTTATTTTTCTGGCTAGGCTTATACCTCGCATGTGTCACAACGTTAACAGAGTT
GTTTATATATTTGGCCCACCAGTTAAAGAACCTCCTACAGATGTTACTCCCACTTTCTTG
ACAACAGGGGTGCTCAGTACTTTACGCCAAGCTGATTTTGAGGCCCATAACATTCTCAGG
GAGTCTGGGTATGCTGGGAAAATCAGCCAGATGCCGGTGATTTTGACACCATTACATTTT
GATCGGGACCCACTTCAAAAGCAGCCTTCATGCCAGAGATCTGTGGTTATTCGAACCTTT
ATTACTAGTGACTTCATGACTGGTATACCTGCAACACCTGGCAATGAGATCCCTGTAGAG
GTGGTATTAAAGATGGTCACTGAGATTAAGAAGATTCCTGGTATTTCTCGAATTATGTAT
GACTTAACATCAAAGCCCCCAGGAACTACTGAGTGGGAGTAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID GMPS Link Image
Target 2 GenAtlas ID GMPS Link Image
Target 2 HGNC ID HGNC:4378 Link Image
Target 2 Chromosome Location 3
Target 2 Locus 3q24
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Hirst M, Haliday E, Nakamura J, Lou L: Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA. J Biol Chem. 1994 Sep 23;269(38):23830-7. [PubMed Link Image]
Target 2 Drug References Not Available
Drug Target 3 [top]
Target 3 ID 388
Target 3 Name AMP deaminase 1
Target 3 Synonyms
  1. AMP deaminase isoform M
  2. EC 3.5.4.6
  3. Myoadenylate deaminase
Target 3 Gene Name AMPD1
Target 3 Protein Sequence >AMP deaminase 1 
MPLFKLPAEEKQIDDAMRNFAEKVFASEVKDEGGRQEISPFDVDEICPISHHEMQAHIFH
LETLSTSTEARRKKRFQGRKTVNLSIPLSETSSTKLSHIDEYISSSPTYQTVPDFQRVQI
TGDYASGVTVEDFEIVCKGLYRALCIREKYMQKSFQRFPKTPSKYLRNIDGEAWVANESF
YPVFTPPVKKGEDPFRTDNLPENLGYHLKMKDGVVYVYPNEAAVSKDEPKPLPYPNLDTF
LDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKV
DTHIHAAACMNQKHLLRFIKKSYQIDADRVVYSTKEKNLTLKELFAKLKMHPYDLTVDSL
DVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQ
HAEPRLSIYGRSPDEWSKLSSWFVCNRIHCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLE
NIFMPVFEATINPQADPELSVFLKHITGFDSVDDESKHSGHMFSSKSPKPQEWTLEKNPS
YTYYAYYMYANIMVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADDISHGLNLKK
SPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEP
LMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKVKFLGDNYLEEGPAGNDIRRTNV
AQIRMAYRYETWCYELNLIAEGLKSTE
Target 3 Number of Residues 759
Target 3 Molecular Weight 86491
Target 3 Theoretical pI 6.89
Target 3 GO Classification
Function
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
AMP deaminase activity
catalytic activity
deaminase activity
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleotide metabolism
purine nucleotide metabolism
purine nucleotide biosynthesis
purine nucleoside monophosphate biosynthesis
purine ribonucleoside monophosphate biosynthesis
Component
Not Available
Target 3 General Function Involved in deaminase activity
Target 3 Specific Function AMP deaminase plays a critical role in energy metabolism
Target 3 Pathways
Name SMPDB Link KEGG Link
Purine metabolism SMP00050 Link Image map00230 Link Image
Target 3 Reactions
  • AMP + H2O = IMP + NH3
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 10864686 Link Image
Target 3 UniProtKB/Swiss-Prot ID P23109 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name AMPD1_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Cytoplasmic
Target 3 Gene Sequence >2244 bp 
ATGCCTCTGTTCAAACTCCCAGCTGAAGAGAAACAAATTGATGATGCAATGCGCAACTTT
GCTGAAAAAGTGTTTGCCTCTGAAGTCAAAGATGAAGGAGGTCGTCAGGAGATTTCCCCC
TTTGATGTGGATGAGATCTGTCCGATTTCTCATCATGAGATGCAAGCACACATATTCCAT
CTGGAGACTCTGTCCACCTCCACAGAAGCCAGGAGAAAAAAGCGTTTCCAAGGACGGAAG
ACTGTTAATTTGTCCATTCCACTAAGTGAAACATCTTCCACCAAACTGTCCCACATTGAT
GAATACATTTCCTCATCTCCAACCTACCAGACCGTGCCTGATTTTCAGAGAGTGCAGATT
ACTGGTGACTATGCCTCTGGGGTTACAGTTGAAGATTTTGAAATTGTTTGCAAAGGTCTG
TATCGGGCACTATGCATACGTGAGAAATACATGCAGAAGTCGTTTCAGAGGTTCCCTAAA
ACCCCTTCCAAATACTTGCGGAACATTGATGGTGAGGCTTGGGTAGCAAATGAGAGCTTC
TATCCAGTCTTTACTCCTCCTGTGAAGAAGGGAGAGGACCCCTTCCGAACAGACAACCTT
CCTGAAAACCTGGGCTATCACCTCAAAATGAAGGACGGTGTAGTTTACGTCTATCCTAAT
GAAGCAGCAGTCAGCAAAGATGAGCCTAAGCCACTTCCTTACCCAAATCTGGACACCTTC
TTAGACGATATGAATTTTTTACTTGCTTTAATTGCTCAAGGACCTGTTAAGACCTATACC
CACCGGCGCCTGAAGTTCCTCTCCTCGAAGTTCCAGGTCCATCAGATGCTTAACGAGATG
GACGAGTTAAAGGAGCTGAAAAACAACCCCCACCGAGATTTTTATAACTGCAGGAAGGTG
GACACCCATATCCATGCAGCCGCTTGCATGAACCAGAAACATCTGCTGCGTTTTATTAAG
AAATCTTACCAAATTGATGCTGACAGAGTGGTCTATAGCACCAAAGAGAAGAATCTGACC
CTAAAGGAACTTTTTGCTAAATTAAAAATGCATCCTTATGACCTGACTGTTGATTCTCTG
GATGTTCATGCTGGACGCCAGACCTTCCAGCGTTTTGATAAGTTCAATGACAAATATAAT
CCTGTAGGAGCAAGTGAGCTACGGGACCTCTACTTGAAGACAGACAATTACATTAATGGG
GAATATTTTGCCACTATCATCAAGGAGGTAGGTGCGGACCTGGTGGAGGCCAAGTACCAG
CATGCTGAGCCCCGCCTGTCCATCTATGGCCGCAGTCCTGATGAGTGGAGCAAACTCTCC
TCCTGGTTCGTCTGCAATCGCATCCACTGCCCCAACATGACATGGATGATCCAGGTTCCC
AGGATCTATGATGTGTTCCGTTCCAAGAATTTCCTTCCACATTTTGGAAAAATGCTGGAG
AATATTTTCATGCCAGTGTTTGAGGCCACCATCAACCCCCAGGCTGACCCAGAACTCAGT
GTCTTCCTCAAGCATATCACTGGCTTTGACAGTGTGGATGATGAGTCCAAACACAGTGGC
CACATGTTCTCCTCCAAGAGTCCCAAGCCCCAGGAGTGGACATTGGAAAAGAATCCATCT
TACACTTACTATGCCTACTACATGTATGCAAACATCATGGTGCTCAACAGCCTGAGAAAG
GAACGAGGCATGAATACGTTTCTGTTCCGACCTCACTGTGGAGAAGCTGGAGCCCTCACC
CATCTCATGACAGCATTCATGATAGCAGATGATATCTCTCATGGCCTAAATTTAAAAAAG
AGTCCCGTGCTACAGTACTTGTTTTTCTTAGCCCAAATTCCCATCGCCATGTCACCACTA
AGTAACAATAGCCTATTTCTAGAGTATGCCAAAAATCCTTTTTTGGATTTCCTTCAGAAA
GGGCTAATGATCTCACTGTCTACAGATGACCCAATGCAATTCCACTTTACCAAGGAGCCC
CTAATGGAAGAATATGCTATTGCTGCACAAGTCTTCAAGCTGAGCACCTGTGATATGTGC
GAAGTGGCAAGGAACAGTGTCTTGCAGTGTGGAATTTCTCATGAGGAGAAAGTAAAGTTT
CTGGGCGACAATTACCTTGAGGAAGGCCCTGCTGGAAATGATATCCGGAGGACAAATGTA
GCCCAAATCCGCATGGCCTATCGCTATGAAACCTGGTGTTATGAACTCAATTTAATTGCT
GAGGGTCTTAAATCAACAGAATAA
Target 3 GenBank Gene ID
Target 3 GeneCard ID AMPD1 Link Image
Target 3 GenAtlas ID AMPD1 Link Image
Target 3 HGNC ID HGNC:468 Link Image
Target 3 Chromosome Location 1
Target 3 Locus 1p13
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Morisaki H, Higuchi I, Abe M, Osame M, Morisaki T: First missense mutations (R388W and R425H) of AMPD1 accompanied with myopathy found in a Japanese patient. Hum Mutat. 2000 Dec;16(6):467-72. [PubMed Link Image]
  2. Sabina RL, Fishbein WN, Pezeshkpour G, Clarke PR, Holmes EW: Molecular analysis of the myoadenylate deaminase deficiencies. Neurology. 1992 Jan;42(1):170-9. [PubMed Link Image]
  3. Morisaki T, Gross M, Morisaki H, Pongratz D, Zollner N, Holmes EW: Molecular basis of AMP deaminase deficiency in skeletal muscle. Proc Natl Acad Sci U S A. 1992 Jul 15;89(14):6457-61. [PubMed Link Image]
  4. Sabina RL, Morisaki T, Clarke P, Eddy R, Shows TB, Morton CC, Holmes EW: Characterization of the human and rat myoadenylate deaminase genes. J Biol Chem. 1990 Jun 5;265(16):9423-33. [PubMed Link Image]
Target 3 Drug References Not Available
Drug Target 4 [top]
Target 4 ID 413
Target 4 Name Amidophosphoribosyltransferase
Target 4 Synonyms
  1. ATASE
  2. Amidophosphoribosyltransferase precursor
  3. EC 2.4.2.14
  4. GPAT
  5. Glutamine phosphoribosylpyrophosphate amidotransferase
Target 4 Gene Name PPAT
Target 4 Protein Sequence >Amidophosphoribosyltransferase precursor 
MELEELGIREECGVFGCIASGEWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPT
FKSHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVA
HNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEA
PTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLIPVSDINDKEKKTSETEGWVVSSESCSFL
SIGARYYREVLPGEIVEISRHNVQTLDIISRSEGNPVAFCIFEYVYFARPDSMFEDQMVY
TVRYRCGQQLAIEAPVDADLVSTVPESATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQP
NMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRVASP
PIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQEGIKFKKQKE
KKHDIMIQENGNGLECFEKSGHCTACLTGKYPVELEW
Target 4 Number of Residues 525
Target 4 Molecular Weight 57400
Target 4 Theoretical pI 6.74
Target 4 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring pentosyl groups
amidophosphoribosyltransferase activity
Process
nucleoside metabolism
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleobase metabolism
purine base metabolism
purine base biosynthesis
Component
Not Available
Target 4 General Function Nucleotide transport and metabolism
Target 4 Specific Function Not Available
Target 4 Pathways
Name SMPDB Link KEGG Link
Glutamate metabolism SMP00072 Link Image map00251 Link Image
Purine metabolism SMP00050 Link Image map00230 Link Image
Target 4 Reactions
  • 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 219459 Link Image
Target 4 UniProtKB/Swiss-Prot ID Q06203 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name PUR1_HUMAN Link Image
Target 4 PDB ID Not Available
Target 4 Cellular Location Not Available
Target 4 Gene Sequence >1554 bp 
ATGGAGCTGGAGGAGTTGGGGATCCGAGAGGAATGTGGCGTGTTCGGGTGCATCGCCTCA
GGAGAGTGGCCCACGCAGCTGGATGTACCGCATGTGATCACTCTGGGACTCGTGGGGCTG
CAGCACCGGGGTCAGGAGAGTGCTGGTATTGTGACTAGTGATGGGAGTTCGGTGCCAACA
TTCAAATCACACAAGGGAATGGGTCTTGTAAATCACGTCTTTACTGAAGACAATTTGAAA
AAATTATATGTTTCAAATCTTGGAATTGGACACACCAGGTATGCCACCACAGGAAAATGT
GAACTAGAAAATTGTCAGCCCTTCGTTGTTGAAACACTTCATGGGAAGATAGCTGTGGCA
CATAATGGCGAATTGGTAAATGCTGCTCGATTAAGGAAAAAGCTTCTGCGTCATGGTATT
GGTCTGTCTACAAGTTCTGATAGTGAAATGATTACCCAGTTACTGGCGTATACCCCTCCT
CAGGAACAAGATGACACCCCAGACTGGGTAGCCAGGATTAAAAACTTGATGAAGGAAGCA
CCCACAGCATACTCCCTGCTTATAATGCACAGAGATGTTATTTATGCAGTACGAGATCCT
TATGGAAATCGTCCCTTATGCATTGGTCGTCTTATTCCAGTGTCTGATATAAATGACAAA
GAGAAAAAAACATCAGAAACAGAAGGATGGGTGGTGTCTTCAGAATCTTGTAGCTTCTTA
TCTATTGGTGCAAGATATTACCGTGAAGTCTTGCCTGGAGAAATTGTGGAAATATCCAGA
CACAATGTCCAAACTCTTGATATTATATCAAGGTCTGAAGGAAACCCAGTGGCTTTTTGT
ATCTTTGAATATGTTTATTTTGCAAGACCAGACAGTATGTTCGAAGACCAAATGGTTTAT
ACAGTAAGATACCGTTGTGGCCAGCAGCTAGCGATTGAAGCACCTGTGGATGCAGATTTG
GTTAGCACTGTTCCAGAATCTGCTACGCCTGCTGCTCTTGCTTACGCAGGAAAGTGTGGA
CTTCCATATGTGGAGGTGCTGTGTAAAAACCGGTATGTAGGGAGAACCTTCATTCAGCCA
AACATGAGGTTAAGACAACTTGGTGTTGCAAAAAAATTTGGAGTATTGTCAGACAACTTT
AAAGGCAAAAGAATTGTTCTTGTAGATGATTCAATTGTCAGAGGCAATACCATCTCACCT
ATAATAAAACTGCTCAAAGAATCTGGTGCAAAAGAGGTACACATTCGAGTAGCTTCACCA
CCAATTAAATATCCATGCTTCATGGGAATAAACATTCCTACAAAAGAAGAGCTCATTGCC
AATAAACCAGAATTTGATCACCTTGCAGAATATCTAGGAGCAAACAGTGTTGTGTATCTG
TCAGTAGAAGGACTGGTTTCATCTGTACAAGAAGGGATAAAGTTTAAAAAACAGAAAGAG
AAAAAGCACGATATTATGATCCAAGAAAATGGAAATGGTCTGGAATGTTTTGAAAAGAGT
GGTCATTGTACAGCTTGTCTCACTGGAAAATATCCTGTAGAATTAGAATGGTAG
Target 4 GenBank Gene ID
Target 4 GeneCard ID PPAT Link Image
Target 4 GenAtlas ID PPAT Link Image
Target 4 HGNC ID HGNC:9238 Link Image
Target 4 Chromosome Location 4
Target 4 Locus 4q12
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Brayton KA, Chen Z, Zhou G, Nagy PL, Gavalas A, Trent JM, Deaven LL, Dixon JE, Zalkin H: Two genes for de novo purine nucleotide synthesis on human chromosome 4 are closely linked and divergently transcribed. J Biol Chem. 1994 Feb 18;269(7):5313-21. [PubMed Link Image]
  2. Iwahana H, Oka J, Mizusawa N, Kudo E, Ii S, Yoshimoto K, Holmes EW, Itakura M: Molecular cloning of human amidophosphoribosyltransferase. Biochem Biophys Res Commun. 1993 Jan 15;190(1):192-200. [PubMed Link Image]
Target 4 Drug References Not Available
Drug Target 5 [top]
Target 5 ID 796
Target 5 Name Inosine-5'-monophosphate dehydrogenase 2
Target 5 Synonyms
  1. EC 1.1.1.205
  2. IMP dehydrogenase 2
  3. IMPD 2
  4. IMPDH-II
Target 5 Gene Name IMPDH2
Target 5 Protein Sequence >Inosine-5'-monophosphate dehydrogenase 2 
MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKIT
LKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVV
LSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMT
KREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDA
KKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVI
GGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVP
VIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAM
DKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVR
AMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF
Target 5 Number of Residues 522
Target 5 Molecular Weight 55806
Target 5 Theoretical pI 6.90
Target 5 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
IMP dehydrogenase activity
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleotide metabolism
purine nucleotide metabolism
purine nucleotide biosynthesis
purine nucleoside monophosphate biosynthesis
purine ribonucleoside monophosphate biosynthesis
GMP biosynthesis
Component
Not Available
Target 5 General Function Nucleotide transport and metabolism
Target 5 Specific Function Rate limiting enzyme in the de novo synthesis of guanine nucleotides and therefore is involved in the regulation of cell growth. It may also have a role in the development of malignancy and the growth progression of some tumors
Target 5 Pathways
Name SMPDB Link KEGG Link
Purine metabolism SMP00050 Link Image map00230 Link Image
Target 5 Reactions
  • inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH + H+
Target 5 Pfam Domain Function
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • None
Target 5 Essentiality Non-Essential
Target 5 GenBank ID Protein 307066 Link Image
Target 5 UniProtKB/Swiss-Prot ID P12268 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name IMDH2_HUMAN Link Image
Target 5 PDB ID 1NFB Link Image
Target 5 PDB File Show
Target 5 3D Structure
Target 5 Cellular Location Not Available
Target 5 Gene Sequence >1545 bp 
ATGGCCGACTACCTGATTAGTGGGGGCACGTCCTACGTGCCAGACGACGGACTCACAGCA
CAGCAGCTCTTCAACTGCGGAGACGGCCTCACCTACAATGACTTTCTCATTCTCCCTGGG
TACATCGACTTCACTGCAGACCAGGTGGACCTGACTTCTGCTCTGACCAAGAAAATCACT
CTTAAGACCCCACTGGTTTCCTCTCCCATGGACACAGTCACAGAGGCTGGGATGGCCATA
GCAATGGCGCTTACAGGCGGTATTGGCTTCATCCACCACAACTGTACACCTGAATTCCAG
GCCAATGAAGTTCGGAAAGTGAAGAAATATGAACAGGGATTCATCACAGACCCTGTGGTC
CTCAGCCCCAAGGATCGCGTGCGGGATGTTTTTGAGGCCAAGGCCCGGCATGGTTTCTGC
GGTATCCCAATCACAGACACAGGCCGGATGGGGAGCCGCTTGGTGGGCATCATCTCCTCC
AGGGACATTGATTTTCTCAAAGAGGAGGAACATGACTGTTTCTTGGAAGAGATAATGACA
AAGAGGGAAGACTTGGTGGTAGCCCCCCGCAGCATCACACTGAAGGAGGCAAATGAAATT
CTGCAGCGCAGCAAGAAGGGAAAGTTGCCCATTGTAAATGAAGATGATGAGCTTGTGGCC
ATCATTGCCCGGACAGACCTGAAGAAGAATCGGGACTACCCACTAGCCTCCAAAGATGCC
AAGAAACAGCTGCTGTGTGGGGCAGCCATTGGCACTCATGAGGATGACAAGTATAGGCTG
GACTTGCTCGCCCAGGCTGGTGTGGATGTAGTGGTTTTGGACTCTTCCCAGGGAAATTCC
ATCTTCCAGATCAATATGATCAAGTACATCAAAGACAAATACCCTAATCTCCAAGTCATT
GGAGGCAATGTGGTCACTGCTGCCCAGGCCAAGAACCTCATTGATGCAGGTGTGGATGCC
CTGCGGGTGGGCATGGGAAGTGGCTCCATCTGCATTACGCAGGAAGTGCTGGCCTGTGGG
CGGCCCCAAGCAACAGCAGTGTACAAGGTGTCAGAGTATGCACGGCGCTTTGGTGTTCCG
GTCATTGCTGATGGAGGAATCCAAAATGTGGGTCATATTGCGAAAGCCTTGGCCCTTGGG
GCCTCCACAGTCATGATGGGCTCTCTCCTGGCTGCCACCACTGAGGCCCCTGGTGAATAC
TTCTTTTCCGATGGGATCCGGCTAAAGAAATATCGCGGTATGGGTTCTCTCGATGCCATG
GACAAGCACCTCAGCAGCCAGAACAGATATTTCAGTGAAGCTGACAAAATCAAAGTGGCC
CAGGGAGTGTCTGGTGCTGTGCAGGACAAAGGGTCAATCCACAAATTTGTCCCTTACCTG
ATTGCTGGCATCCAACACTCATGCCAGGACATTGGTGCCAAGAGCTTGACCCAAGTCCGA
GCCATGATGTACTCTGGGGAGCTTAAGTTTGAGAAGAGAACGTCCTCAGCCCAGGTGGAA
GGTGGCGTCCATAGCCTCCATTCGTATGAGAAGCGGCTTTTCTGA
Target 5 GenBank Gene ID
Target 5 GeneCard ID IMPDH2 Link Image
Target 5 GenAtlas ID IMPDH2 Link Image
Target 5 HGNC ID HGNC:6053 Link Image
Target 5 Chromosome Location 3
Target 5 Locus 3p21.2
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Colby TD, Vanderveen K, Strickler MD, Markham GD, Goldstein BM: Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design. Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3531-6. [PubMed Link Image]
  2. Natsumeda Y, Ohno S, Kawasaki H, Konno Y, Weber G, Suzuki K: Two distinct cDNAs for human IMP dehydrogenase. J Biol Chem. 1990 Mar 25;265(9):5292-5. [PubMed Link Image]
  3. Collart FR, Huberman E: Cloning and sequence analysis of the human and Chinese hamster inosine-5'-monophosphate dehydrogenase cDNAs. J Biol Chem. 1988 Oct 25;263(30):15769-72. [PubMed Link Image]
  4. Hager PW, Collart FR, Huberman E, Mitchell BS: Recombinant human inosine monophosphate dehydrogenase type I and type II proteins. Purification and characterization of inhibitor binding. Biochem Pharmacol. 1995 May 11;49(9):1323-9. [PubMed Link Image]
  5. Zimmermann AG, Spychala J, Mitchell BS: Characterization of the human inosine-5'-monophosphate dehydrogenase type II gene. J Biol Chem. 1995 Mar 24;270(12):6808-14. [PubMed Link Image]
  6. Glesne DA, Huberman E: Cloning and sequence of the human type II IMP dehydrogenase gene. Biochem Biophys Res Commun. 1994 Nov 30;205(1):537-44. [PubMed Link Image]
  7. Glesne D, Collart F, Varkony T, Drabkin H, Huberman E: Chromosomal localization and structure of the human type II IMP dehydrogenase gene (IMPDH2). Genomics. 1993 Apr;16(1):274-7. [PubMed Link Image]
Target 5 Drug References Not Available
Drug Target 6 [top]
Target 6 ID 838
Target 6 Name Inosine-5'-monophosphate dehydrogenase 1
Target 6 Synonyms
  1. EC 1.1.1.205
  2. IMP dehydrogenase 1
  3. IMPD 1
  4. IMPDH-I
Target 6 Gene Name IMPDH1
Target 6 Protein Sequence >Inosine-5'-monophosphate dehydrogenase 1 
MADYLISGGTGYVPEDGLTAQQLFASADGLTYNDFLILPGFIDFIADEVDLTSALTRKIT
LKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQGFITDPVV
LSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLAEKDHTTLLSEVMT
PRIELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDS
QKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVI
GGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVP
IIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAM
EKSSSSQKRYFSEGDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLR
SMMYSGELKFEKRTMSAQIEGGVHGLHSYEKRLY
Target 6 Number of Residues 522
Target 6 Molecular Weight 55407
Target 6 Theoretical pI 6.90
Target 6 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
IMP dehydrogenase activity
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleotide metabolism
purine nucleotide metabolism
purine nucleotide biosynthesis
purine nucleoside monophosphate biosynthesis
purine ribonucleoside monophosphate biosynthesis
GMP biosynthesis
Component
Not Available
Target 6 General Function Nucleotide transport and metabolism
Target 6 Specific Function Rate limiting enzyme in the de novo synthesis of guanine nucleotides and therefore is involved in the regulation of cell growth. It may also have a role in the development of malignancy and the growth progression of some tumors
Target 6 Pathways
Name SMPDB Link KEGG Link
Purine metabolism SMP00050 Link Image map00230 Link Image
Target 6 Reactions
  • inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH + H+
Target 6 Pfam Domain Function
Target 6 Signals
  • None
Target 6 Transmembrane Regions
  • None
Target 6 Essentiality Non-Essential
Target 6 GenBank ID Protein 307067 Link Image
Target 6 UniProtKB/Swiss-Prot ID P20839 Link Image
Target 6 UniProtKB/Swiss-Prot Entry Name IMDH1_HUMAN Link Image
Target 6 PDB ID 1JCN Link Image
Target 6 PDB File Show
Target 6 3D Structure
Target 6 Cellular Location Not Available
Target 6 Gene Sequence >1545 bp 
ATGGCGGACTACCTGATCAGCGGCGGCACCGGCTACGTGCCCGAGGATGGGCTCACCGCG
CAGCAGCTCTTCGCCAGCGCCGACGACCTCACCTACAACGACTTCCTGATTCTCCCAGGA
TTCATAGACTTCATAGCTGATGAGGTGGACCTGACCTCAGCCCTGACCCGGAAGATCACG
CTGAAGACGCCACTCATCTCCTCCCCCATGGACACTGTGACAGAGGCTGACATGGCCATT
GCCATGGCTCTGATGGGAGGTATTGGGTTCATTCACCACAACTGCACCCCAGAGTTCCAG
GCCAATGAAGTACGCAAGGTCAAGAACTTTGAACAGGGCTTCATCACGGACCCTGTGGTG
CTGAGCCCCTCGCACACTGTGGGCGATGTGCTGGAGGCCAAGATGCGGCATGGCTTCTCT
GGCATCCCCATCACTGAGACGGGCACCATGGGCAGCAAGCTGGTGGGCATCGTCACCTCC
CGAGACATCGACTTTCTTGCTGAGAAGGACCACACCACCCTCCTCAGTGAGGTGATGACG
CCAAGGATTGAACTGGTGGTGGCTCCAGCAGGTGTGACGTTGAAAGAGGCAAATGAGATC
CTGCAGCGTAGCAAGAAAGGGAAGCTGCCTATCGTCAATGATTGCGATGAGCTGGTGGCC
ATCATCGCCCGCACCGACCTGAAGAAGAATCGAGACTACCCTCTGGCCTCCAAGGATTCC
CAGAAGCAGCTGCTCTGTGGGGCAGCTGTGGGCACCCGTGAGGATGACAAATACCGTCTG
GACCTGCTGACCCAGGCGGGGGTCGACGTCATAGTCTTCCACTCGTCCCAAGGGAATTCG
GTGTATCAGATCGCCATGGTGCATTACATCAAACAGAAGTACCCCCACCTCCAGGTGATT
GGGGGGAACGTGGTGACAGCAGCCCAGGCCAAGAACCTGATTGATGCTGGTGTGGACGGG
CTGCGCGTGGGCATGGGCTGCGGCTCCATCTGCATCACCCAGGAAGTGATGGCCTGTGGT
CGGCCCCAGGGCACTGCTGTGTACAAGGTGGCTGAGTATGCCCGGCGCTTTGGTGTGCCC
ATCATAGCCGATGGCGGCATCCAGACCGTGGGACACGTGGTCAAGGCCCTGGCCCTTGGA
GCCTCCACAGTGATGATGGGCTCCCTGCTGGCCGCCACTACGGAGGCCCCTGGCGAGTAC
TTCTTCTCAGACGGGGTGCGGCTCAAGAAGTACCGGGGCATGGGCTCACTGGATCCCATG
GAGAAGAGCAGCAGCAGCCAGAAACGATACTTCAGCGAGGGGGATAAAGTGAAGATCGCA
CAGGGTGTCTCGGGCTCCATCCAGGACAAAGGATCCATTCAGAAGTTCGTGCCCTACCTC
ATAGCAGGCATCCAACACGGCTGCCAGGATATCGGGGCCCGCAGCCTGTCTGTCCTTCGG
TCCATGATGTACTCAGGAGAGCTCAAGTTTGAGAAGCGGACCATGTCGCCCCAGATTGAG
GGTGGTGTCCATGGCCTGCACTCTTACGAAAAGCGGCTGTACTGA
Target 6 GenBank Gene ID
Target 6 GeneCard ID IMPDH1 Link Image
Target 6 GenAtlas ID IMPDH1 Link Image
Target 6 HGNC ID HGNC:6052 Link Image
Target 6 Chromosome Location 7
Target 6 Locus 7q31.3-q32
Target 6 SNPs SNPJam Report Link Image
Target 6 General References
  1. Kennan A, Aherne A, Palfi A, Humphries M, McKee A, Stitt A, Simpson DA, Demtroder K, Orntoft T, Ayuso C, Kenna PF, Farrar GJ, Humphries P: Identification of an IMPDH1 mutation in autosomal dominant retinitis pigmentosa (RP10) revealed following comparative microarray analysis of transcripts derived from retinas of wild-type and Rho(-/-) mice. Hum Mol Genet. 2002 Mar 1;11(5):547-57. [PubMed Link Image]
  2. Bowne SJ, Sullivan LS, Blanton SH, Cepko CL, Blackshaw S, Birch DG, Hughbanks-Wheaton D, Heckenlively JR, Daiger SP: Mutations in the inosine monophosphate dehydrogenase 1 gene (IMPDH1) cause the RP10 form of autosomal dominant retinitis pigmentosa. Hum Mol Genet. 2002 Mar 1;11(5):559-68. [PubMed Link Image]
  3. Natsumeda Y, Ohno S, Kawasaki H, Konno Y, Weber G, Suzuki K: Two distinct cDNAs for human IMP dehydrogenase. J Biol Chem. 1990 Mar 25;265(9):5292-5. [PubMed Link Image]
  4. Hager PW, Collart FR, Huberman E, Mitchell BS: Recombinant human inosine monophosphate dehydrogenase type I and type II proteins. Purification and characterization of inhibitor binding. Biochem Pharmacol. 1995 May 11;49(9):1323-9. [PubMed Link Image]
Target 6 Drug References Not Available
Drug Target 7 [top]
Target 7 ID 2516
Target 7 Name GMP reductase 1
Target 7 Synonyms
  1. EC 1.7.1.7
  2. Guanosine 5'-monophosphate oxidoreductase 1
  3. Guanosine monophosphate reductase 1
Target 7 Gene Name GMPR
Target 7 Protein Sequence >GMP reductase 1 
MPRIDADLKLDFKDVLLRPKRSSLKSRAEVDLERTFTFRNSKQTYSGIPIIVANMDTVGT
FEMAAVMSQHSMFTAIHKHYSLDDWKLFATNHPECLQNVAVSSGSGQNDLEKMTSILEAV
PQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIKVGV
GPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVM
LGGMFSGHTECAGEVFERNGRKLKLFYGMSSDTAMNKHAGGVAEYRASEGKTVEVPYKGD
VENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVTQQHNTVFS
Target 7 Number of Residues 350
Target 7 Molecular Weight 37419
Target 7 Theoretical pI 7.08
Target 7 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on NADH or NADPH
oxidoreductase activity, acting on NADH or NADPH, nitrogenous group as acceptor
GMP reductase activity
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleotide metabolism
Component
Not Available
Target 7 General Function Nucleotide transport and metabolism
Target 7 Specific Function Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides
Target 7 Pathways
Name SMPDB Link KEGG Link
Purine metabolism SMP00050 Link Image map00230 Link Image
Target 7 Reactions
  • inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH + H+
Target 7 Pfam Domain Function
Target 7 Signals
  • None
Target 7 Transmembrane Regions
  • None
Target 7 Essentiality Non-Essential
Target 7 GenBank ID Protein 529232 Link Image
Target 7 UniProtKB/Swiss-Prot ID P36959 Link Image
Target 7 UniProtKB/Swiss-Prot Entry Name GMPR1_HUMAN Link Image
Target 7 PDB ID 2BLE Link Image
Target 7 PDB File Show
Target 7 3D Structure
Target 7 Cellular Location Not Available
Target 7 Gene Sequence >1038 bp 
ATGCCCCGCATAGATGCGGACCTCAAGCTCGACTTCAAGGACGTCCTGCTCCGACCTAAG
CGGAGCAGCCTCAAGAGCCGAGCCGAGGTGGATCTTGAACGCACCTTCACGTTTCGAAAT
TCAAAGCAGACCTACTCAGGGATTCCCATCATCGTGGCCAACATGGACACTGTGGGCACG
TTTGAGATGGCAGCCGTGATGTCACAGCACTCCATGTTTACAGCAATTCATAAGCATTAC
TCCCTGGATGACTGGAAGCTCTTTGCCACAAATCACCCAGAATGCCTGCAGAATGTAGCC
GTGAGTTCAGGCAGTGGGCAGAATGATCTGGAAAAGATGACCAGCATCCTGGAAGCTGTG
CCACAGGTTAAGTTTATTTGCCTGGATGTGGCCAATGGGTATTCAGAACATTTTGTGGAA
TTCGTGAAACTTGTCCGTGCCAAATTTCCTGAACACACCATTATGGCAGGGAACGTGGTG
ACAGGAGAAATGGTAGAAGAGCTTATTCTTTCCGGAGCAGATATCATCAAAGTGGGAGTT
GGACCAGGTTCTGTGTGCACCACCCGCACCAAGACGGGAGTGGGGTACCCCCAGCTGAGT
GCCGTCATTGAGTGTGCCGACTCTGCCCACGGCCTGAAGGGCCACATCATCTCTGATGGA
GGCTGTACGTGTCCAGGGGATGTCGCCAAAGCCTTTGGAACTGGAGCAGATTTTGTCATG
CTGGGAGGAATGTTTTCGGGTCATACGGAGTGTGCTGGAGAAGTGATTGAGAGGAACGGA
CGGAAGCTCAAGCTCTTCTACGGGATGAGCTCTGACACCGCCATGAACAAGCACGCAGGA
GGAGTTGCTGAGTACAGAGCCTCTGAGGGTAAGACTGTGGAAGTTCCTTACAAAGGAGAT
GTGGAAAACACTATCCTGGATATTCTCGGGGGACTGAGGTCCACGTGCACCTACGTGGGG
GCCGCCAAACTCAAGGAGCTCAGCAGGAGGGCAACATTCATCCGGGTGACCCAGCAGCAC
AACACCGTGTTCAGCTAA
Target 7 GenBank Gene ID
Target 7 GeneCard ID GMPR Link Image
Target 7 GenAtlas ID GMPR Link Image
Target 7 HGNC ID HGNC:4376 Link Image
Target 7 Chromosome Location 6
Target 7 Locus 6p23
Target 7 SNPs SNPJam Report Link Image
Target 7 General References
  1. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  2. Kondoh T, Kanno H, Chang L, Yoshida A: Genomic structure and expression of human guanosine monophosphate reductase. Hum Genet. 1991 Dec;88(2):219-24. [PubMed Link Image]
  3. Kondoh T, Kanno H, Chang LF, Yoshida A: Identification of common variant alleles of the human guanosine monophosphate reductase gene. Hum Genet. 1991 Dec;88(2):225-7. [PubMed Link Image]
  4. Kanno H, Huang IY, Kan YW, Yoshida A: Two structural genes on different chromosomes are required for encoding the major subunit of human red cell glucose-6-phosphate dehydrogenase. Cell. 1989 Aug 11;58(3):595-606. [PubMed Link Image]
Target 7 Drug References Not Available
Drug Target 8 [top]
Target 8 ID 5893
Target 8 Name GMP reductase 2
Target 8 Synonyms
  1. EC 1.7.1.7
  2. Guanosine 5'-monophosphate oxidoreductase 2
  3. Guanosine monophosphate reductase 2
Target 8 Gene Name GMPR2
Target 8 Protein Sequence >GMP reductase 2 
MPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQTYSGVPIIAANMDTVGT
FEMAKVLCKFSLFTAVHKHYSLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQLEQILEAI
PQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGI
GPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVM
LGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAGGVAEYRASEGKTVEVPFKGD
VEHTIRDILGGIRSTCTYVGAAKLKELSRRTTFIRVTQQVNPIFSEAC
Target 8 Number of Residues 353
Target 8 Molecular Weight 37875
Target 8 Theoretical pI 7.25
Target 8 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on NADH or NADPH
oxidoreductase activity, acting on NADH or NADPH, nitrogenous group as acceptor
GMP reductase activity
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleotide metabolism
Component
Not Available
Target 8 General Function Nucleotide transport and metabolism
Target 8 Specific Function Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. Plays a role in modulating cellular differentiation
Target 8 Pathways Not Available
Target 8 Reactions Not Available
Target 8 Pfam Domain Function
Target 8 Signals
  • None
Target 8 Transmembrane Regions
  • None
Target 8 Essentiality Non Essential
Target 8 GenBank ID Protein Not Available
Target 8 UniProtKB/Swiss-Prot ID Q9P2T1 Link Image
Target 8 UniProtKB/Swiss-Prot Entry Name GMPR2_HUMAN Link Image
Target 8 PDB ID Not Available
Target 8 Cellular Location Not Available
Target 8 Gene Sequence Not Available
Target 8 GenBank Gene ID
Target 8 GeneCard ID Not Available
Target 8 GenAtlas ID GMPR2 Link Image
Target 8 HGNC ID HGNC:4377 Link Image
Target 8 Chromosome Location Not Available
Target 8 Locus Not Available
Target 8 SNPs SNPJam Report Link Image
Target 8 General References
  1. Deng Y, Wang Z, Ying K, Gu S, Ji C, Huang Y, Gu X, Wang Y, Xu Y, Li Y, Xie Y, Mao Y: NADPH-dependent GMP reductase isoenzyme of human (GMPR2). Expression, purification, and kinetic properties. Int J Biochem Cell Biol. 2002 Sep;34(9):1035-50. [PubMed Link Image]
Target 8 Drug References Not Available
Drug Target 9 [top]
Target 9 ID 5894
Target 9 Name Adenylosuccinate lyase
Target 9 Synonyms
  1. ASASE
  2. ASL
  3. Adenylosuccinase
  4. EC 4.3.2.2
Target 9 Gene Name ADSL
Target 9 Protein Sequence >Adenylosuccinate lyase 
MAAGGDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDE
QIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTD
LIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLC
MDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITG
QTYTRKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMR
SERCCSLARHLMTLVMDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISE
GLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQEGGD
NDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQQVQRFLEEEVYPLLKPYESVMKVKA
ELCL
Target 9 Number of Residues 492
Target 9 Molecular Weight 54890
Target 9 Theoretical pI 7.12
Target 9 GO Classification
Function
lyase activity
carbon-nitrogen lyase activity
amidine-lyase activity
adenylosuccinate lyase activity
catalytic activity
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleotide metabolism
purine nucleotide metabolism
purine nucleotide biosynthesis
purine ribonucleotide biosynthesis
Component
Not Available
Target 9 General Function Nucleotide transport and metabolism
Target 9 Specific Function N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP
Target 9 Pathways Not Available
Target 9 Reactions Not Available
Target 9 Pfam Domain Function
Target 9 Signals
  • None
Target 9 Transmembrane Regions
  • None
Target 9 Essentiality Non Essential
Target 9 GenBank ID Protein Not Available
Target 9 UniProtKB/Swiss-Prot ID P30566 Link Image
Target 9 UniProtKB/Swiss-Prot Entry Name PUR8_HUMAN Link Image
Target 9 PDB ID Not Available
Target 9 Cellular Location Not Available
Target 9 Gene Sequence Not Available
Target 9 GenBank Gene ID
Target 9 GeneCard ID Not Available
Target 9 GenAtlas ID ADSL Link Image
Target 9 HGNC ID HGNC:291 Link Image
Target 9 Chromosome Location Not Available
Target 9 Locus Not Available
Target 9 SNPs SNPJam Report Link Image
Target 9 General References
  1. Marie S, Cuppens H, Heuterspreute M, Jaspers M, Tola EZ, Gu XX, Legius E, Vincent MF, Jaeken J, Cassiman JJ, Van den Berghe G: Mutation analysis in adenylosuccinate lyase deficiency: eight novel mutations in the re-evaluated full ADSL coding sequence. Hum Mutat. 1999;13(3):197-202. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  3. Kmoch S, Hartmannova H, Stiburkova B, Krijt J, Zikanova M, Sebesta I: Human adenylosuccinate lyase (ADSL), cloning and characterization of full-length cDNA and its isoform, gene structure and molecular basis for ADSL deficiency in six patients. Hum Mol Genet. 2000 Jun 12;9(10):1501-13. [PubMed Link Image]
  4. Race V, Marie S, Vincent MF, Van den Berghe G: Clinical, biochemical and molecular genetic correlations in adenylosuccinate lyase deficiency. Hum Mol Genet. 2000 Sep 1;9(14):2159-65. [PubMed Link Image]
  5. Stone RL, Aimi J, Barshop BA, Jaeken J, Van den Berghe G, Zalkin H, Dixon JE: A mutation in adenylosuccinate lyase associated with mental retardation and autistic features. Nat Genet. 1992 Apr;1(1):59-63. [PubMed Link Image]
  6. Verginelli D, Luckow B, Crifo C, Salerno C, Gross M: Identification of new mutations in the adenylosuccinate lyase gene associated with impaired enzyme activity in lymphocytes and red blood cells. Biochim Biophys Acta. 1998 Feb 27;1406(1):81-4. [PubMed Link Image]
Target 9 Drug References Not Available
Drug Target 10 [top]
Target 10 ID 5895
Target 10 Name Adenylosuccinate synthase
Target 10 Synonyms Not Available
Target 10 Gene Name ADSS
Target 10 Protein Sequence Not Available
Target 10 Number of Residues 0
Target 10 Molecular Weight Not Available
Target 10 Theoretical pI Not Available
Target 10 GO Classification Not Available
Target 10 General Function Not Available
Target 10 Specific Function Not Available
Target 10 Pathways Not Available
Target 10 Reactions Not Available
Target 10 Pfam Domain Function Not Available
Target 10 Signals Not Available
Target 10 Transmembrane Regions Not Available
Target 10 Essentiality Not Available
Target 10 GenBank ID Protein Not Available
Target 10 UniProtKB/Swiss-Prot ID B1AQM5 Link Image
Target 10 UniProtKB/Swiss-Prot Entry Name B1AQM5_HUMAN Link Image
Target 10 PDB ID Not Available
Target 10 Cellular Location Not Available
Target 10 Gene Sequence Not Available
Target 10 GenBank Gene ID
Target 10 GeneCard ID Not Available
Target 10 GenAtlas ID Not Available
Target 10 HGNC ID Not Available
Target 10 Chromosome Location Not Available
Target 10 Locus Not Available
Target 10 SNPs SNPJam Report Link Image
Target 10 General References Not Available
Target 10 Drug References Not Available
Drug Target 11 [top]
Target 11 ID 5896
Target 11 Name AMP deaminase 2
Target 11 Synonyms
  1. AMP deaminase isoform L
  2. EC 3.5.4.6
Target 11 Gene Name AMPD2
Target 11 Protein Sequence >AMP deaminase 2 
MRNRGQGLFRLRSRCFLHQSLPLGAGRRKGLDVAEPGPSRCRSDSPAVAAVVPAMASYPS
GSGKPKAKYPFKKRASLQASTAAPEARGGLGAPPLQSARSLPGPAPCLKHFPLDLRTSMD
GKCKEIAEELFTRSLAESELRSAPYEFPEESPIEQLEERRQRLERQISQDVKLEPDILLR
AKQDFLKTDSDSDLQLYKEQGEGQGDRSLRERDVLEREFQRVTISGEEKCGVPFTDLLDA
AKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPP
ALEQHPYEHCEPSTMPGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVN
VLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIH
ASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHAD
RNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELR
LSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLP
LFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYL
YYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQ
YLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEY
SIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRV
GYRYETLCQELALITQAVQSEMLETIPEEAGITMSPGPQ
Target 11 Number of Residues 893
Target 11 Molecular Weight 100689
Target 11 Theoretical pI 6.93
Target 11 GO Classification
Function
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
AMP deaminase activity
catalytic activity
deaminase activity
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleotide metabolism
purine nucleotide metabolism
purine nucleotide biosynthesis
purine nucleoside monophosphate biosynthesis
purine ribonucleoside monophosphate biosynthesis
Component
Not Available
Target 11 General Function Not Available
Target 11 Specific Function AMP deaminase plays a critical role in energy metabolism
Target 11 Pathways Not Available
Target 11 Reactions Not Available
Target 11 Pfam Domain Function
Target 11 Signals
  • None
Target 11 Transmembrane Regions
  • None
Target 11 Essentiality Non Essential
Target 11 GenBank ID Protein Not Available
Target 11 UniProtKB/Swiss-Prot ID Q01433 Link Image
Target 11 UniProtKB/Swiss-Prot Entry Name AMPD2_HUMAN Link Image
Target 11 PDB ID Not Available
Target 11 Cellular Location
  • Cytoplasmic
Target 11 Gene Sequence Not Available
Target 11 GenBank Gene ID
Target 11 GeneCard ID Not Available
Target 11 GenAtlas ID AMPD2 Link Image
Target 11 HGNC ID HGNC:469 Link Image
Target 11 Chromosome Location Not Available
Target 11 Locus Not Available
Target 11 SNPs SNPJam Report Link Image
Target 11 General References
  1. Bausch-Jurken MT, Mahnke-Zizelman DK, Morisaki T, Sabina RL: Molecular cloning of AMP deaminase isoform L. Sequence and bacterial expression of human AMPD2 cDNA. J Biol Chem. 1992 Nov 5;267(31):22407-13. [PubMed Link Image]
  2. Van den Bergh F, Sabina RL: Characterization of human AMP deaminase 2 (AMPD2) gene expression reveals alternative transcripts encoding variable N-terminal extensions of isoform L. Biochem J. 1995 Dec 1;312 ( Pt 2):401-10. [PubMed Link Image]
  3. Mahnke-Zizelman DK, van den Bergh F, Bausch-Jurken MT, Eddy R, Sait S, Shows TB, Sabina RL: Cloning, sequence and characterization of the human AMPD2 gene: evidence for transcriptional regulation by two closely spaced promoters. Biochim Biophys Acta. 1996 Aug 14;1308(2):122-32. [PubMed Link Image]
Target 11 Drug References Not Available
Drug Target 12 [top]
Target 12 ID 5897
Target 12 Name AMP deaminase 3
Target 12 Synonyms
  1. AMP deaminase isoform E
  2. EC 3.5.4.6
  3. Erythrocyte AMP deaminase
Target 12 Gene Name AMPD3
Target 12 Protein Sequence >AMP deaminase 3 
MPRQFPKLNISEVDEQVRLLAEKVFAKVLREEDSKDALSLFTVPEDCPIGQKEAKERELQ
KELAEQKSVETAKRKKSFKMIRSQSLSLQMPPQQDWKGPPAASPAMSPTTPVVTGATSLP
TPAPYAMPEFQRVTISGDYCAGITLEDYEQAAKSLAKALMIREKYARLAYHRFPRITSQY
LGHPRADTAPPEEGLPDFHPPPLPQEDPYCLDDAPPNLDYLVHMQGGILFVYDNKKMLEH
QEPHSLPYPDLETYTVDMSHILALITDGPTKTYCHRRLNFLESKFSLHEMLNEMSEFKEL
KSNPHRDFYNVRKVDTHIHAAACMNQKHLLRFIKHTYQTEPDRTVAEKRGRKITLRQVFD
GLHMDPYDLTVDSLDVHAGRQTFHRFDKFNSKYNPVGASELRDLYLKTENYLGGEYFARM
VKEVARELEESKYQYSEPRLSIYGRSPEEWPNLAYWFIQHKVYSPNMRWIIQVPRIYDIF
RSKKLLPNFGKMLENIFLPLFKATINPQDHRELHLFLKYVTGFDSVDDESKHSDHMFSDK
SPNPDVWTSEQNPPYSYYLYYMYANIMVLNNLRRERGLSTFLFRPHCGEAGSITHLVSAF
LTADNISHGLLLKKSPVLQYLYYLAQIPIAMSPLSNNSLFLEYSKNPLREFLHKGLHVSL
STDDPMQFHYTKEALMEEYAIAAQVWKLSTCDLCEIARNSVLQSGLSHQEKQKFLGQNYY
KEGPEGNDIRKTNVAQIRMAFRYETLCNELSFLSDAMKSEEITALTN
Target 12 Number of Residues 779
Target 12 Molecular Weight 88813
Target 12 Theoretical pI 6.98
Target 12 GO Classification
Function
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
AMP deaminase activity
catalytic activity
deaminase activity
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleotide metabolism
purine nucleotide metabolism
purine nucleotide biosynthesis
purine nucleoside monophosphate biosynthesis
purine ribonucleoside monophosphate biosynthesis
Component
Not Available
Target 12 General Function Not Available
Target 12 Specific Function AMP deaminase plays a critical role in energy metabolism
Target 12 Pathways Not Available
Target 12 Reactions Not Available
Target 12 Pfam Domain Function
Target 12 Signals
  • None
Target 12 Transmembrane Regions
  • None
Target 12 Essentiality Non Essential
Target 12 GenBank ID Protein Not Available
Target 12 UniProtKB/Swiss-Prot ID Q01432 Link Image
Target 12 UniProtKB/Swiss-Prot Entry Name AMPD3_HUMAN Link Image
Target 12 PDB ID Not Available
Target 12 Cellular Location
  • Cytoplasmic
Target 12 Gene Sequence Not Available
Target 12 GenBank Gene ID
Target 12 GeneCard ID Not Available
Target 12 GenAtlas ID AMPD3 Link Image
Target 12 HGNC ID HGNC:470 Link Image
Target 12 Chromosome Location Not Available
Target 12 Locus Not Available
Target 12 SNPs SNPJam Report Link Image
Target 12 General References
  1. Mahnke-Zizelman DK, Sabina RL: Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons. J Biol Chem. 1992 Oct 15;267(29):20866-77. [PubMed Link Image]
  2. Yamada Y, Goto H, Ogasawara N: Cloning and nucleotide sequence of the cDNA encoding human erythrocyte-specific AMP deaminase. Biochim Biophys Acta. 1992 Nov 15;1171(1):125-8. [PubMed Link Image]
  3. Yamada Y, Goto H, Ogasawara N: A point mutation responsible for human erythrocyte AMP deaminase deficiency. Hum Mol Genet. 1994 Feb;3(2):331-4. [PubMed Link Image]
  4. Mahnke-Zizelman DK, Eddy R, Shows TB, Sabina RL: Characterization of the human AMPD3 gene reveals that 5' exon useage is subject to transcriptional control by three tandem promoters and alternative splicing. Biochim Biophys Acta. 1996 Apr 10;1306(1):75-92. [PubMed Link Image]
Target 12 Drug References Not Available

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.