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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:03:54
Primary Accession Number DB00759
Secondary Accession Number
  • APRD00572
Name Tetracycline
Drug Type
  • Approved
  • Small Molecule
Description A naphthacene antibiotic that inhibits amino acyl TRNA binding during protein synthesis. [PubChem]
Synonyms
  1. Anhydrotetracycline
  2. TC
  3. Tetracycline HCl
Brand Names
  1. Abramycin
  2. Abricycline
  3. Achromycin
  4. Achromycin V
  5. Actisite
  6. Agromicina
  7. Ambramicina
  8. Ambramycin
  9. Amycin
  10. Bio-Tetra
  11. Biocycline
  12. Bristaciclin
  13. Bristaciclina
  14. Bristacycline
  15. Cefracycline
  16. Ciclibion
  17. Copharlan
  18. Criseociclina
  19. Cyclopar
  20. Cytome
  21. Democracin
  22. Deschlorobiomycin
  23. Dumocyclin
  24. Enterocycline
  25. Hostacyclin
  26. Lexacycline
  27. Limecycline
  28. Liquamycin
  29. Medocycline
  30. Mericycline
  31. Micycline
  32. Neocycline
  33. Oletetrin
  34. Omegamycin
  35. Orlycycline
  36. Panmycin
  37. Polycycline
  38. Polyotic
  39. Purocyclina
  40. Resteclin
  41. Retet
  42. Robitet
  43. Roviciclina
  44. SK-Tetracycline
  45. Solvocin
  46. Sumycin
  47. TAC
  48. Tetra-CO
  49. Tetrabon
  50. Tetrachel
  51. Tetracycl
  52. Tetracycline II
  53. Tetracyn
  54. Tetradecin
  55. Tetrafil
  56. Tetramed
  57. Tetraverine
  58. Tetrex
  59. Topicycline
  60. Tsiklomistsin
  61. Tsiklomitsin
  62. Veracin
  63. Vetacyclinum
Brand Mixtures
  1. Delta-Albaplex tablets (Novobiocin sodium + Prednisolone + Tetracycline hydrochloride)
  2. Helidac (Metronidazole + Bismuth subsalicylate + tetracycline hydrochloride)
  3. Neo Chlor PWR (Neomycin sulfate + Tetracycline hydrochloride)
  4. Neo-Chlor (Neomycin sulfate + Tetracycline hydrochloride)
  5. Neotetramed PWR (Neomycin sulfate + Tetracycline hydrochloride)
  6. P Onytricin P (Calcium D-pantothenate + Menadione sodium bisulfite + Nicotinamide + Tetracycline hydrochloride + Vitamin A + Vitamin B12 + Vitamin B2 + Vitamin B6 + Vitamin D3 + Vitamin E)
Chemical IUPAC Name (2Z)-2-(amino-hydroxymethylidene)-4-dimethylamino-6,10,11,12a-tetrahydroxy-6-methyl-4,4a,5,5a-tetrahydrotetracene-1,3,12-trione
Chemical Formula C22H24N2O8
Chemical Structure Structure
CAS Registry Number 60-54-8
InChI Identifier InChI=1/C22H24N2O8/c1-21(31)8-5-4-6-11(25)12(8)16(26)13-9(21)7-10-15(24(2)3)17(27)14(20(23)30)19(29)22(10,32)18(13)28/h4-6,9-10,15,25-26,30-32H,7,23H2,1-3H3/b20-14-
InChI Key JYHCQVWYCGHXGP-ZHZULCJRBO
KEGG Drug D00201 Link Image
KEGG Compound C06570 Link Image
PubChem Compound 5353990 Link Image
PubChem Substance 407983 Link Image
ChEBI ID 27902 Link Image
PharmGKB ID PA451640 Link Image
HET ID ATC Link Image
GenBank ID Not Available
Drug ID Number [DIN] 00527777 Link Image
RxList Link http://www.rxlist.com/cgi/generic2/tetcycl2.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Tetracycline Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference J. H. Boothe et al., J. Am. Chem. Soc. 75, 4621 (1953)
Average Molecular Weight 444.4346
Monoisotopic Molecular Weight 444.1533
State Solid
Melting Point 165oC
Experimental Water Solubility 231 mg/L at 25 oC (SRC PhysProp experimental -- YALKOWSKY,SH & DANNENFELSER,RM (1992)) Source: PhysProp
Predicted Water Solubility 8.08e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -0.3 Source: PhysProp
Predicted LogP -0.39 Calculated using ALOGPS
Experimental LogS -3.12 [ADME Research, USCD]
Predicted LogS -2.74 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point 3.3
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 1P87 Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES CN(C)[C@H]1[C@@H]2C[C@@H]3C(C(=O)[C@@]2(O)C(=O)\C(C1=O)=C(\N)O)=C(O)C1=C(C=CC=C1O)[C@@]3(C)O
Canonical SMILES CN(C)C1C2CC3C(C(=O)C2(O)C(=O)C(C1=O)=C(N)O)=C(O)C1=C(C=CC=C1O)C3(C)O
Drug Category
  • Anti-Bacterial Agents
  • Antiprotozoals
  • Protein Synthesis Inhibitors
  • Tetracyclines
ATC Codes
AHFS Codes
  • 08:12.24
  • 52:04.04
Indication Used to treat bacterial infections such as Rocky Mountain spotted fever, typhus fever, and tick fevers; upper respiratory infections; pneumonia; gonorrhea; amoebic infections; and urinary tract infections. It is also used to help treat severe acne and to treat trachoma (a chronic eye infection) and conjunctivitis (pinkeye). Tetracycline is often an alternative drug for people who are allergic to penicillin.
Pharmacology Tetracycline is a short-acting antibiotic semisynthetically produced from chlortetracycline, which is derived from Streptomyces aureofaciens. Tetracycline inhibits cell growth by inhibiting translation. It binds to the 30S ribosomal subunit and prevents the amino-acyl tRNA from binding to the A site of the ribosome. This binding is reversible in nature.
Mechanism of Action Tetracycline passively diffuses through porin channels in the bacterial membrane and reversibly binds to the 30S ribosomal subunit, preventing binding of tRNA to the mRNA-ribosome complex, and thus interfering with protein synthesis.
Absorption Bioavailability is less than 40% when administered via intramuscular injection, 100% intravenously, and 60-80% orally (fasting adults). Food and/or milk reduce GI absorption of oral preparations of tetracycline by 50% or more.
Toxicity LD50=808mg/kg (orally in mice)
Protein Binding Tetracyclines bind to plasma proteins to varying degrees
Biotransformation Not metabolized
Half Life 6-11 hours
Dosage Forms
Form Route
Capsule Oral
Ointment Ophthalmic
Tablet Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Acenocoumarol The tetracycline increases the anticoagulant effect
Acitretin Increased risk of intracranial hypertension
Aluminium Formation of non-absorbable complexes
Amoxicillin Possible antagonism of action
Ampicillin Possible antagonism of action
Anisindione The tetracycline increases the anticoagulant effect
Atovaquone The agent decreases the effect of atovaquone
Attapulgite Formation of non-absorbable complexes
Azlocillin Possible antagonism of action
Aztreonam Possible antagonism of action
Bacampicillin Possible antagonism of action
Bismuth Formation of non-absorbable complexes
Bismuth Subsalicylate Formation of non-absorbable complexes
Calcium Formation of non-absorbable complexes
Carbenicillin Possible antagonism of action
Clavulanate Possible antagonism of action
Cloxacillin Possible antagonism of action
Cyclacillin Possible antagonism of action
Dicloxacillin Possible antagonism of action
Dicumarol The tetracycline increases the anticoagulant effect
Digoxin The tetracycline increases the effect of digoxin in 10% of patients
Dihydroxyaluminium Formation of non-absorbable complexes
Ethinyl Estradiol This anti-infectious agent could decrease the effect of the oral contraceptive
Etretinate Increased risk of intracranial hypertension
Flucloxacillin Possible antagonism of action
Hetacillin Possible antagonism of action
Insulin Tetracycline increases the risk of hypoglycemia
Insulin-aspart Tetracycline increases the risk of hypoglycemia
Insulin-detemir Tetracycline increases the risk of hypoglycemia
Insulin-glargine Tetracycline increases the risk of hypoglycemia
Insulin-glulisine Tetracycline increases the risk of hypoglycemia
Insulin-lispro Tetracycline increases the risk of hypoglycemia
Iron Formation of non-absorbable complexes
Isotretinoin Increased risk of intracranial hypertension
Magnesium Formation of non-absorbable complexes
Mestranol This anti-infectious agent could decrease the effect of the oral contraceptive
Methicillin Acyl-Serine Possible antagonism of action
Methotrexate The tetracycline increases methotrexate toxicity
Methoxyflurane The tetracycline increases the renal toxicity of methoxyflurane
Mezlocillin Possible antagonism of action
Nafcillin Possible antagonism of action
Oxacillin Possible antagonism of action
Penicillin G Possible antagonism of action
Penicillin V Possible antagonism of action
Piperacillin Possible antagonism of action
Pivampicillin Possible antagonism of action
Pivmecillinam Possible antagonism of action
Quinapril Quinapril can reduce the absorption of tetracycline
Salicylate-magnesium Formation of non-absorbable complexes
Tazobactam Possible antagonism of action
Ticarcillin Possible antagonism of action
Trisalicylate-choline Formation of non-absorbable complexes
Warfarin The tetracycline increases the anticoagulant effect
Zinc Formation of non-absorbable complexes
insulin inhaled Tetracycline increases the risk of hypoglycemia
Food Interactions
  • Avoid milk, calcium containing dairy products, iron, antacids, or aluminium salts 2 hours before or 6 hours after using antacids while on this medication.
  • Take on empty stomach: 1 hour before or 2 hours after meals.
  • Take with a full glass of water.
Pathways
Name SMPDB Link KEGG Link
Tetracycline Pathway SMP00294 Link Image
General References
  1. http://en.wikipedia.org/wiki/Tetracycline
  2. Drugs.com Link Image
  3. Wikipedia Link Image
  4. RxList Link Image
Organisms Affected
  • Enteric bacteria and other eubacteria
Targets
  1. 30S ribosomal protein S4
  2. 30S ribosomal protein S9
  3. 16S rRNA
  4. Major prion protein
Drug Target 1 [top]
Target 1 ID 22
Target 1 Name 30S ribosomal protein S4
Target 1 Synonyms Not Available
Target 1 Gene Name rpsD
Target 1 Protein Sequence >30S ribosomal protein S4 
ARYLGPKLKLSRREGTDLFLKSGVRAIDTKCKIEQAPGQHGARKPRLSDYGVQLREKQKV
RRIYGVLERQFRNYYKEAARLKGNTGENLLALLEGRLDNVVYRMGFGATRAEARQLVSHK
AIMVNGRVVNIASYQVSPNDVVSIREKAKKQSRVKAALELAEQREKPTWLEVDAGKMEGT
FKRKPERSDLSADINEHLIVELYSK
Target 1 Number of Residues 208
Target 1 Molecular Weight 23338
Target 1 Theoretical pI 10.66
Target 1 GO Classification
Function
binding
nucleic acid binding
RNA binding
structural molecule activity
structural constituent of ribosome
Process
physiological process
metabolism
macromolecule metabolism
macromolecule biosynthesis
protein biosynthesis
Component
cell
intracellular
protein complex
ribonucleoprotein complex
ribosome
small ribosomal subunit
Target 1 General Function Translation, ribosomal structure and biogenesis
Target 1 Specific Function Also functions as a rho-dependent antiterminator of rRNA transcription, increasing the synthesis of rRNA under conditions of excess protein, allowing a more rapid return to homeostasis. Binds directly to RNA polymerase
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Essential
Target 1 GenBank ID Protein 42798 Link Image
Target 1 UniProtKB/Swiss-Prot ID P0A7V8 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name RS4_ECOLI Link Image
Target 1 PDB ID 1P87 Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Cytoplasmic
Target 1 Gene Sequence >621 bp 
ATGGCAAGATATTTGGGTCCTAAGCTCAAGCTGAGCCGTCGTGAGGGCACCGACTTATTC
CTTAAGTCTGGCGTTCGCGCGATCGATACCAAGTGTAAAATTGAACAAGCTCCTGGCCAG
CACGGTGCGCGTAAACCGCGTCTGTCTGACTATGGTGTGCAGTTGCGTGAAAAGCAAAAA
GTTCGCCGTATCTATGGTGTGCTGGAGCGTCAGTTCCGTAACTACTACAAAGAAGCAGCA
CGTCTGAAAGGCAACACCGGTGAAAACCTGTTGGCTCTGCTGGAAGGTCGTCTGGACAAC
GTTGTATACCGTATGGGCTTCGGTGCCACTCGTGCAGAAGCACGTCAGCTGGTTAGCCAT
AAAGCAATTATGGTAAACGGTCGTGTTGTTAACATCGCTTCTTATCAGGTTAGTCCGAAT
GACGTTGTAAGCATTCGTGAGAAAGCGAAGAAGCAGTCTCGCGTGAAAGCCGCTCTGGAG
CTGGCTGAGCAGCGTGAAAAGCCAACCTGGCTGGAAGTTGATGCTGGCAAGATGGAAGGT
ACGTTTAAGCGTAAGCCGGAGCGTTCTGATCTGTCTGCGGACATTAACGAACACCTGATC
GTCGAGCTTTACTCCAAGTAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID Not Available
Target 1 GenAtlas ID Not Available
Target 1 HGNC ID Not Available
Target 1 Chromosome Location Not Available
Target 1 Locus Not Available
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Arnold RJ, Reilly JP: Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry. Anal Biochem. 1999 Apr 10;269(1):105-12. [PubMed Link Image]
  2. Schiltz E, Reinbolt J: Determination of the complete amino-acid sequence of protein S4 from Escherichia coli ribosomes. Eur J Biochem. 1975 Aug 15;56(2):467-81. [PubMed Link Image]
  3. Dahlgren A, Ryden-Aulin M: A novel mutation in ribosomal protein S4 that affects the function of a mutated RF1. Biochimie. 2000 Aug;82(8):683-91. [PubMed Link Image]
  4. Torres M, Condon C, Balada JM, Squires C, Squires CL: Ribosomal protein S4 is a transcription factor with properties remarkably similar to NusA, a protein involved in both non-ribosomal and ribosomal RNA antitermination. EMBO J. 2001 Jul 16;20(14):3811-20. [PubMed Link Image]
  5. Tung CS, Joseph S, Sanbonmatsu KY: All-atom homology model of the Escherichia coli 30S ribosomal subunit. Nat Struct Biol. 2002 Oct;9(10):750-5. [PubMed Link Image]
  6. Gao H, Sengupta J, Valle M, Korostelev A, Eswar N, Stagg SM, Van Roey P, Agrawal RK, Harvey SC, Sali A, Chapman MS, Frank J: Study of the structural dynamics of the E coli 70S ribosome using real-space refinement. Cell. 2003 Jun 13;113(6):789-801. [PubMed Link Image]
  7. Nowotny V, Nierhaus KH: Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two assembly domains which are initiated by S4 and S7. Biochemistry. 1988 Sep 6;27(18):7051-5. [PubMed Link Image]
  8. Allen PN, Noller HF: Mutations in ribosomal proteins S4 and S12 influence the higher order structure of 16 S ribosomal RNA. J Mol Biol. 1989 Aug 5;208(3):457-68. [PubMed Link Image]
  9. Bedwell D, Davis G, Gosink M, Post L, Nomura M, Kestler H, Zengel JM, Lindahl L: Nucleotide sequence of the alpha ribosomal protein operon of Escherichia coli. Nucleic Acids Res. 1985 Jun 11;13(11):3891-903. [PubMed Link Image]
  10. Thomas MS, Bedwell DM, Nomura M: Regulation of alpha operon gene expression in Escherichia coli. A novel form of translational coupling. J Mol Biol. 1987 Jul 20;196(2):333-45. [PubMed Link Image]
  11. 387752 Post LE, Nomura M: Nucleotide sequence of the intercistronic region preceding the gene for RNA polymerase subunit alpha in Escherichia coli. J Biol Chem. 1979 Nov 10;254(21):10604-6.
  12. 4587210 Reinbolt J, Schiltz E: The primary structure of ribosomal protein S4 from Escherichia coli. FEBS Lett. 1973 Nov 1;36(3):250-2.
  13. 7556101 Urlaub H, Kruft V, Bischof O, Muller EC, Wittmann-Liebold B: Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies. EMBO J. 1995 Sep 15;14(18):4578-88.
  14. 7559430 Baker AM, Draper DE: Messenger RNA recognition by fragments of ribosomal protein S4. J Biol Chem. 1995 Sep 29;270(39):22939-45.
  15. 9278503 Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74.
  16. 9716382 Choi KM, Atkins JF, Gesteland RF, Brimacombe R: Flexibility of the nascent polypeptide chain within the ribosome--contacts from the peptide N-terminus to a specific region of the 30S subunit. Eur J Biochem. 1998 Jul 15;255(2):409-13.
Target 1 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 140
Target 2 Name 30S ribosomal protein S9
Target 2 Synonyms Not Available
Target 2 Gene Name rpsI
Target 2 Protein Sequence >30S ribosomal protein S9 
AENQYYGTGRRKSSAARVFIKPGNGKIVINQRSLEQYFGRETARMVVRQPLELVDMVEKL
DLYITVKGGGISGQAGAIRHGITRALMEYDESLRSELRKAGFVTRDARQVERKKVGLRKA
RRRPQFSKR
Target 2 Number of Residues 131
Target 2 Molecular Weight 14725
Target 2 Theoretical pI 11.52
Target 2 GO Classification
Function
structural molecule activity
structural constituent of ribosome
Process
physiological process
metabolism
macromolecule metabolism
macromolecule biosynthesis
protein biosynthesis
Component
protein complex
ribonucleoprotein complex
ribosome
cell
intracellular
Target 2 General Function Translation, ribosomal structure and biogenesis
Target 2 Specific Function The C-terminal tail plays a role in the affinity of the 30S P site for different tRNAs. Mutations that decrease this affinity are suppressed in the 70S ribosome
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Essential
Target 2 GenBank ID Protein 535073 Link Image
Target 2 UniProtKB/Swiss-Prot ID P0A7X3 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name RS9_ECOLI Link Image
Target 2 PDB ID 1P87 Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location Not Available
Target 2 Gene Sequence >393 bp 
ATGGCTGAAAATCAATACTACGGCACTGGTCGCCGCAAAAGTTCCGCAGCTCGCGTTTTC
ATCAAACCGGGCAACGGTAAAATCGTAATCAACCAACGTTCTCTGGAACAGTACTTCGGT
CGTGAAACTGCCCGCATGGTAGTTCGTCAGCCGCTGGAACTGGTCGACATGGTTGAGAAA
CTGGACCTGTACATCACCGTTAAAGGTGGTGGTATCTCTGGTCAGGCTGGTGCGATCCGT
CACGGTATCACCCGCGCTCTGATGGAATACGACGAGTCCCTGCGTTCTGAACTGCGTAAA
GCTGGCTTCGTTACTCGTGACGCTCGTCAGGTTGAACGTAAGAAAGTCGGTCTGCGTAAA
GCACGTCGTCGTCCGCAGTTCTCCAAACGTTAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID Not Available
Target 2 GenAtlas ID Not Available
Target 2 HGNC ID Not Available
Target 2 Chromosome Location Not Available
Target 2 Locus Not Available
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Arnold RJ, Reilly JP: Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry. Anal Biochem. 1999 Apr 10;269(1):105-12. [PubMed Link Image]
  2. Chen R, Wittmann-Liebold B: The primary structure of protein S9 from the 30S subunit of Escherichia coli ribosomes. FEBS Lett. 1975 Mar 15;52(1):139-40. [PubMed Link Image]
  3. Tung CS, Joseph S, Sanbonmatsu KY: All-atom homology model of the Escherichia coli 30S ribosomal subunit. Nat Struct Biol. 2002 Oct;9(10):750-5. [PubMed Link Image]
  4. Gao H, Sengupta J, Valle M, Korostelev A, Eswar N, Stagg SM, Van Roey P, Agrawal RK, Harvey SC, Sali A, Chapman MS, Frank J: Study of the structural dynamics of the E coli 70S ribosome using real-space refinement. Cell. 2003 Jun 13;113(6):789-801. [PubMed Link Image]
  5. Isono S, Thamm S, Kitakawa M, Isono K: Cloning and nucleotide sequencing of the genes for ribosomal proteins S9 (rpsI) and L13 (rplM) of Escherichia coli. Mol Gen Genet. 1985;198(2):279-82. [PubMed Link Image]
  6. Marsh RC, Parmeggiani A: Requirement of proteins S5 and S9 from 30S subunits for the ribosome-dependent GTPase activity of elongation factor G. Proc Natl Acad Sci U S A. 1973 Jan;70(1):151-5. [PubMed Link Image]
  7. Urlaub H, Kruft V, Bischof O, Muller EC, Wittmann-Liebold B: Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies. EMBO J. 1995 Sep 15;14(18):4578-88. [PubMed Link Image]
  8. Osswald M, Doring T, Brimacombe R: The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site. Nucleic Acids Res. 1995 Nov 25;23(22):4635-41. [PubMed Link Image]
  9. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
Target 2 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 883
Target 3 Name 16S rRNA
Target 3 Synonyms
  1. 16S ribosomal ribonucleic acid
Target 3 Gene Name Not Available
Target 3 Protein Sequence Not Available
Target 3 Number of Residues 0
Target 3 Molecular Weight Not Available
Target 3 Theoretical pI Not Available
Target 3 GO Classification
Function
transferase activity
translation
RNA binding
Process
rRNA processing
RNA processing and modification
Component
cell
Target 3 General Function Translation, ribosomal structure and biogenesis
Target 3 Specific Function In prokaryotes, the 16S rRNA is essential for recognizing the 5' end of mRNA and hence positioning it correctly on the ribosome. The 16S rRNA has a characteristic secondary structure in which half of the nucleotides are base-paired. The 16S rRNA sequence has been highly conserved and is often used for evolutionary and species comparative analysis.
Target 3 Pathways
Name SMPDB Link KEGG Link
Ribosome map03010 Link Image
Target 3 Reactions
  • rRNA + mRNA + Amino Acids = Polypeptide
Target 3 Pfam Domain Function Not Available
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Essential
Target 3 GenBank ID Protein Not Available
Target 3 UniProtKB/Swiss-Prot ID Not Available
Target 3 UniProtKB/Swiss-Prot Entry Name Not Available
Target 3 PDB ID 1EMI Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location
  • Cytoplasmic
Target 3 Gene Sequence >16S rRNA sequence 
AAATTGAAGAGTTTGATCATGGCTCAGATTGAACGCTGGCGGCAGGCCTAACACATGCAA
GTCGAACGGTAACAGGAAACAGCTTGCTGTTTCGCTGACGAGTGGCGGACGGGTGAGTAA
TGTCTGGGAAACTGCCTGATGGAGGGGGATAACTACTGGAAACGGTAGCTAATACCGCAT
AACGTCGCAAGACCAAAGAGGGGGACCCTCGGGCCTCTTGCCATCGGATGTGCCCAGATG
GGATTAGCTTGTTGGTGGGGTAACGGCTCACCAAGGCGACGATCCCTAGCTGGTCTGAGA
GGATGACCAGCCACACTGGAACTGAGACACGGTCCAGACTCCTACGGGAGGCAGCAGTGG
GGAATATTGCACAATGGGCGCAAGCCTGATGCAGCCATGCCGCGTGTATGAAGAAGGCCT
TCGGGTTGTAAAGTACTTTCAGCGGGGAGGAAGGGAGTAAAGTTAATACCTTTGCTCATT
GACGTTACCCGCAGAAGAAGCACCGGCTAACTCCGTGCCAGCAGCCGCGGTAATACGGAG
GGTGCAAGCGTTAATCGGAATTACTGGGCGTAAAGCGCACGCAGGCGGTTTGTTAAGTCA
GATGTGAAATCCCCGGGCTCAACCTGGGAACTGCATCTGATACTGGCAAGCTTGAGTCTC
GTAGAGGGGGGTAGAATTCCAGGTGTAGCGGTGAAATGCGTAGAGATCTGGAGGAATACC
GGTGGCGAAGGCGGCCCCCTGGACGAAGACTGACGCTCAGGTGCGAAAGCGTGGGGAGCA
AACAGGATTAGATACCCTGGTAGTCCACGCCGTAAACGATGTCGACTTGGAGGTTGTGCC
CTTGAGGCGTGGCTTCCGGAGCTAACGCGTTAAGTCGACCGCCTGGGGAGTACGGCCGCA
AGGTTAAAACTCAAATGAATTGACGGGGGCCCGCACAAGCGGTGGAGCATGTGGTTTAAT
TCGATGCAACGCGAAGAACCTTACCTGGTCTTGACATCCACGGAAGTTTTCAGAGATGAG
AATGTGCCTTCGGGAACCGTGAGACAGGTGCTGCATGGCTGTCGTCAGCTCGTGTTGTGA
AATGTTGGGTTAAGTCCCGCAACGAGCGCAACCCTTATCCTTTGTTGCCAGCGGTCCGGC
CGGGAACTCAAAGGAGACTGCCAGTGATAAACTGGAGGAAGGTGGGGATGACGTCAAGTC
ATCATGGCCCTTACGACCAGGGCTACACACGTGCTACAATGGCGCATACAAAGAGAAGCG
ACCTCGCGAGAGCAAGCGGACCTCATAAAGTGCGTCGTAGTCCGGATTGGAGTCTGCAAC
TCGACTCCATGAAGTCGGAATCGCTAGTAATCGTGGATCAGAATGCCACGGTGAATACGT
TCCCGGGCCTTGTACACACCGCCCGTCACACCATGGGAGTGGGTTGCAAAAGAAGTAGGT
AGCTTAACCTTCGGGAGGGCGCTTACCACTTTGTGATTCATGACTGGGGTGAAGTCGTAA
CAAGGTAACCGTAGGGGAACCTGCGGTTGGATCACCTCCTTA
Target 3 GenBank Gene ID
Target 3 GeneCard ID Not Available
Target 3 GenAtlas ID Not Available
Target 3 HGNC ID Not Available
Target 3 Chromosome Location Not Available
Target 3 Locus Not Available
Target 3 SNPs Not Available
Target 3 General References
  1. Gu XR, Gustafsson C, Ku J, Yu M, Santi DV: Identification of the 16S rRNA m5C967 methyltransferase from Escherichia coli. Biochemistry. 1999 Mar 30;38(13):4053-7. [PubMed Link Image]
  2. Martin JF, Barreiro C, Gonzalez-Lavado E, Barriuso M: Ribosomal RNA and ribosomal proteins in corynebacteria. J Biotechnol. 2003 Sep 4;104(1-3):41-53. [PubMed Link Image]
  3. Srivastava AK, Schlessinger D: Structure and organization of ribosomal DNA. Biochimie. 1991 Jun;73(6):631-8. [PubMed Link Image]
  4. Gutell RR, Larsen N, Woese CR: Lessons from an evolving rRNA: 16S and 23S rRNA structures from a comparative perspective. Microbiol Rev. 1994 Mar;58(1):10-26. [PubMed Link Image]
Target 3 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Nawaz M, Sung K, Khan SA, Khan AA, Steele R: Biochemical and molecular characterization of tetracycline-resistant Aeromonas veronii isolates from catfish. Appl Environ Microbiol. 2006 Oct;72(10):6461-6. [PubMed Link Image]
  3. Domingue GJ Sr: Cryptic bacterial infection in chronic prostatitis: diagnostic and therapeutic implications. Curr Opin Urol. 1998 Jan;8(1):45-9. [PubMed Link Image]
  4. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
  5. Pringle M, Fellstrom C, Johansson KE: Decreased susceptibility to doxycycline associated with a 16S rRNA gene mutation in Brachyspira hyodysenteriae. Vet Microbiol. 2007 Jul 20;123(1-3):245-8. Epub 2007 Feb 25. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 1867
Target 4 Name Major prion protein
Target 4 Synonyms
  1. ASCR
  2. CD230 antigen
  3. Major prion protein precursor
  4. PrP
  5. PrP27-30
  6. PrP33-35C
Target 4 Gene Name PRNP
Target 4 Protein Sequence >Major prion protein precursor 
MANLGCWMLVLFVATWSDLGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQP
HGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGA
VVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCV
NITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGSSMVLFSSPPV
ILLISFLIFLIVG
Target 4 Number of Residues 257
Target 4 Molecular Weight 27662
Target 4 Theoretical pI 9.23
Target 4 GO Classification Not Available
Target 4 General Function Carbohydrate transport and metabolism
Target 4 Specific Function The physiological function of PrP is not known
Target 4 Pathways Not Available
Target 4 Reactions Not Available
Target 4 Pfam Domain Function
Target 4 Signals
  • 1-22
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 190468 Link Image
Target 4 UniProtKB/Swiss-Prot ID P04156 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name PRIO_HUMAN Link Image
Target 4 PDB ID 1QLZ Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location
  • Cell membrane
  • GPI-anchor
  • lipid-anchor
Target 4 Gene Sequence >762 bp 
ATGGCGAACCTTGGCTGCTGGATGCTGGTTCTCTTTGTGGCCACATGGAGTGACCTGGGC
CTCTGCAAGAAGCGCCCGAAGCCTGGAGGATGGAACACTGGGGGCAGCCGATACCCGGGG
CAGGGCAGCCCTGGAGGCAACCGCTACCCACCTCAGGGCGGTGGTGGCTGGGGGCAGCCT
CATGGTGGTGGCTGGGGGCAGCCTCATGGTGGTGGCTGGGGGCAGCCCCATGGTGGTGGC
TGGGGACAGCCTCATGGTGGTGGCTGGGGTCAAGGAGGTGGCACCCACAGTCAGTGGAAC
AAGCCGAGTAAGCCAAAAACCAACATGAAGCACATGGCTGGTGCTGCAGCAGCTGGGGCA
GTGGTGGGGGGCCTTGGCGGCTACATGCTGGGAAGTGCCATGAGCAGGCCCATCATACAT
TTCGGCAGTGACTATGAGGACCGTTACTATCGTGAAAACATGCACCGTTACCCCAACCAA
GTGTACTACAGGCCCATGGATGAGTACAGCAACCAGAACAACTTTGTGCACGACTGCGTC
AATATCACAATCAAGCAGCACACGGTCACCACAACCACCAAGGGGGAGAACTTCACCGAG
ACCGACGTTAAGATGATGGAGCGCGTGGTTGAGCAGATGTGTATCACCCAGTACGAGAGG
GAATCTCAGGCCTATTACCAGAGAGGATCGAGCATGGTCCTCTTCTCCTCTCCACCTGTG
ATCCTCCTGATCTCTTTCCTCATCTTCCTGATAGTGGGATGA
Target 4 GenBank Gene ID
Target 4 GeneCard ID PRNP Link Image
Target 4 GenAtlas ID PRNP Link Image
Target 4 HGNC ID HGNC:9449 Link Image
Target 4 Chromosome Location 20
Target 4 Locus 20p13
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Cervenakova L, Buetefisch C, Lee HS, Taller I, Stone G, Gibbs CJ Jr, Brown P, Hallett M, Goldfarb LG: Novel PRNP sequence variant associated with familial encephalopathy. Am J Med Genet. 1999 Dec 15;88(6):653-6. [PubMed Link Image]
  2. Zahn R, Liu A, Luhrs T, Riek R, von Schroetter C, Lopez Garcia F, Billeter M, Calzolai L, Wider G, Wuthrich K: NMR solution structure of the human prion protein. Proc Natl Acad Sci U S A. 2000 Jan 4;97(1):145-50. [PubMed Link Image]
  3. Finckh U, Muller-Thomsen T, Mann U, Eggers C, Marksteiner J, Meins W, Binetti G, Alberici A, Hock C, Nitsch RM, Gal A: High prevalence of pathogenic mutations in patients with early-onset dementia detected by sequence analyses of four different genes. Am J Hum Genet. 2000 Jan;66(1):110-7. [PubMed Link Image]
  4. Calzolai L, Lysek DA, Guntert P, von Schroetter C, Riek R, Zahn R, Wuthrich K: NMR structures of three single-residue variants of the human prion protein. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8340-5. [PubMed Link Image]
  5. Windl O, Giese A, Schulz-Schaeffer W, Zerr I, Skworc K, Arendt S, Oberdieck C, Bodemer M, Poser S, Kretzschmar HA: Molecular genetics of human prion diseases in Germany. Hum Genet. 1999 Sep;105(3):244-52. [PubMed Link Image]
  6. Panegyres PK, Toufexis K, Kakulas BA, Cernevakova L, Brown P, Ghetti B, Piccardo P, Dlouhy SR: A new PRNP mutation (G131V) associated with Gerstmann-Straussler-Scheinker disease. Arch Neurol. 2001 Nov;58(11):1899-902. [PubMed Link Image]
  7. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  8. Medori R, Montagna P, Tritschler HJ, LeBlanc A, Cortelli P, Tinuper P, Lugaresi E, Gambetti P: Fatal familial insomnia: a second kindred with mutation of prion protein gene at codon 178. Neurology. 1992 Mar;42(3 Pt 1):669-70. [PubMed Link Image]
  9. Diedrich JF, Knopman DS, List JF, Olson K, Frey WH 2nd, Emory CR, Sung JH, Haase AT: Deletion in the prion protein gene in a demented patient. Hum Mol Genet. 1992 Sep;1(6):443-4. [PubMed Link Image]
  10. Hsiao K, Dlouhy SR, Farlow MR, Cass C, Da Costa M, Conneally PM, Hodes ME, Ghetti B, Prusiner SB: Mutant prion proteins in Gerstmann-Straussler-Scheinker disease with neurofibrillary tangles. Nat Genet. 1992 Apr;1(1):68-71. [PubMed Link Image]
  11. 1671440 Goldfarb LG, Haltia M, Brown P, Nieto A, Kovanen J, McCombie WR, Trapp S, Gajdusek DC: New mutation in scrapie amyloid precursor gene (at codon 178) in Finnish Creutzfeldt-Jakob kindred. Lancet. 1991 Feb 16;337(8738):425.
  12. 1672107 Tagliavini F, Prelli F, Ghiso J, Bugiani O, Serban D, Prusiner SB, Farlow MR, Ghetti B, Frangione B: Amyloid protein of Gerstmann-Straussler-Scheinker disease (Indiana kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58. EMBO J. 1991 Mar;10(3):513-9.
  13. 1678248 Puckett C, Concannon P, Casey C, Hood L: Genomic structure of the human prion protein gene. Am J Hum Genet. 1991 Aug;49(2):320-9.
  14. 1683708 Goldfarb LG, Brown P, McCombie WR, Goldgaber D, Swergold GD, Wills PR, Cervenakova L, Baron H, Gibbs CJ Jr, Gajdusek DC: Transmissible familial Creutzfeldt-Jakob disease associated with five, seven, and eight extra octapeptide coding repeats in the PRNP gene. Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10926-30.
  15. 1975028 Goldfarb LG, Mitrova E, Brown P, Toh BK, Gajdusek DC: Mutation in codon 200 of scrapie amyloid protein gene in two clusters of Creutzfeldt-Jakob disease in Slovakia. Lancet. 1990 Aug 25;336(8713):514-5.
  16. 2564168 Hsiao K, Baker HF, Crow TJ, Poulter M, Owen F, Terwilliger JD, Westaway D, Ott J, Prusiner SB: Linkage of a prion protein missense variant to Gerstmann-Straussler syndrome. Nature. 1989 Mar 23;338(6213):342-5.
  17. 2783132 Doh-ura K, Tateishi J, Sasaki H, Kitamoto T, Sakaki Y: Pro----leu change at position 102 of prion protein is the most common but not the sole mutation related to Gerstmann-Straussler syndrome. Biochem Biophys Res Commun. 1989 Sep 15;163(2):974-9.
  18. 3014653 Liao YC, Lebo RV, Clawson GA, Smuckler EA: Human prion protein cDNA: molecular cloning, chromosomal mapping, and biological implications. Science. 1986 Jul 18;233(4761):364-7.
  19. 3755672 Kretzschmar HA, Stowring LE, Westaway D, Stubblebine WH, Prusiner SB, Dearmond SJ: Molecular cloning of a human prion protein cDNA. DNA. 1986 Aug;5(4):315-24.
  20. 7485229 Perry RT, Go RC, Harrell LE, Acton RT: SSCP analysis and sequencing of the human prion protein gene (PRNP) detects two different 24 bp deletions in an atypical Alzheimer's disease family. Am J Med Genet. 1995 Feb 27;60(1):12-8.
  21. 7699395 Itoh Y, Yamada M, Hayakawa M, Shozawa T, Tanaka J, Matsushita M, Kitamoto T, Tateishi J, Otomo E: A variant of Gerstmann-Straussler-Scheinker disease carrying codon 105 mutation with codon 129 polymorphism of the prion protein gene: a clinicopathological study. J Neurol Sci. 1994 Dec 1;127(1):77-86.
  22. 7783876 Young K, Jones CK, Piccardo P, Lazzarini A, Golbe LI, Zimmerman TR Jr, Dickson DW, McLachlan DC, St George-Hyslop P, Lennox A, et al.: Gerstmann-Straussler-Scheinker disease with mutation at codon 102 and methionine at codon 129 of PRNP in previously unreported patients. Neurology. 1995 Jun;45(6):1127-34.
  23. 7902693 Pocchiari M, Salvatore M, Cutruzzola F, Genuardi M, Allocatelli CT, Masullo C, Macchi G, Alema G, Galgani S, Xi YG, et al.: A new point mutation of the prion protein gene in Creutzfeldt-Jakob disease. Ann Neurol. 1993 Dec;34(6):802-7.
  24. 7902972 Yamada M, Itoh Y, Fujigasaki H, Naruse S, Kaneko K, Kitamoto T, Tateishi J, Otomo E, Hayakawa M, Tanaka J, et al.: A missense mutation at codon 105 with codon 129 polymorphism of the prion protein gene in a new variant of Gerstmann-Straussler-Scheinker disease. Neurology. 1993 Dec;43(12):2723-4.
  25. 7906019 Inoue I, Kitamoto T, Doh-ura K, Shii H, Goto I, Tateishi J: Japanese family with Creutzfeldt-Jakob disease with codon 200 point mutation of the prion protein gene. Neurology. 1994 Feb;44(2):299-301.
  26. 7913755 Gabizon R, Rosenman H, Meiner Z, Kahana I, Kahana E, Shugart Y, Ott J, Prusiner SB: Mutation in codon 200 and polymorphism in codon 129 of the prion protein gene in Libyan Jews with Creutzfeldt-Jakob disease. Philos Trans R Soc Lond B Biol Sci. 1994 Mar 29;343(1306):385-90.
  27. 8105771 Prusiner SB: Genetic and infectious prion diseases. Arch Neurol. 1993 Nov;50(11):1129-53.
  28. 8364585 Palmer MS, Collinge J: Mutations and polymorphisms in the prion protein gene. Hum Mutat. 1993;2(3):168-73.
  29. 8461023 Kitamoto T, Ohta M, Doh-ura K, Hitoshi S, Terao Y, Tateishi J: Novel missense variants of prion protein in Creutzfeldt-Jakob disease or Gerstmann-Straussler syndrome. Biochem Biophys Res Commun. 1993 Mar 15;191(2):709-14.
  30. 8797472 Barbanti P, Fabbrini G, Salvatore M, Petraroli R, Cardone F, Maras B, Equestre M, Macchi G, Lenzi GL, Pocchiari M: Polymorphism at codon 129 or codon 219 of PRNP and clinical heterogeneity in a previously unreported family with Gerstmann-Straussler-Scheinker disease (PrP-P102L mutation). Neurology. 1996 Sep;47(3):734-41.
  31. 8909447 Mastrianni JA, Iannicola C, Myers RM, DeArmond S, Prusiner SB: Mutation of the prion protein gene at codon 208 in familial Creutzfeldt-Jakob disease. Neurology. 1996 Nov;47(5):1305-12.
  32. 9266722 Nitrini R, Rosemberg S, Passos-Bueno MR, da Silva LS, Iughetti P, Papadopoulos M, Carrilho PM, Caramelli P, Albrecht S, Zatz M, LeBlanc A: Familial spongiform encephalopathy associated with a novel prion protein gene mutation. Ann Neurol. 1997 Aug;42(2):138-46.
  33. 9384372 Samaia HB, Mari JJ, Vallada HP, Moura RP, Simpson AJ, Brentani RR: A prion-linked psychiatric disorder. Nature. 1997 Nov 20;390(6657):241.
  34. 9786248 Piccardo P, Dlouhy SR, Lievens PM, Young K, Bird TD, Nochlin D, Dickson DW, Vinters HV, Zimmerman TR, Mackenzie IR, Kish SJ, Ang LC, De Carli C, Pocchiari M, Brown P, Gibbs CJ Jr, Gajdusek DC, Bugiani O, Ironside J, Tagliavini F, Ghetti B: Phenotypic variability of Gerstmann-Straussler-Scheinker disease is associated with prion protein heterogeneity. J Neuropathol Exp Neurol. 1998 Oct;57(10):979-88.
  35. 9799790 Lee IY, Westaway D, Smit AF, Wang K, Seto J, Chen L, Acharya C, Ankener M, Baskin D, Cooper C, Yao H, Prusiner SB, Hood LE: Complete genomic sequence and analysis of the prion protein gene region from three mammalian species. Genome Res. 1998 Oct;8(10):1022-37.
Target 4 Drug References
  1. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed Link Image]

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.