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Showing drug card for Bacitracin (DB00626)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:03:33
Primary Accession Number DB00626
Secondary Accession Number
  • APRD00816
Name Bacitracin
Drug Type
  • Approved
  • Small Molecule
Description Bacitracin is a mixture of related cyclic polypeptides produced by organisms of the licheniformis group of Bacillus subtilis var Tracy. Its unique name derives from the fact that the bacillus producing it was first isolated in 1943 from a knee scrape from a girl named Margaret Tracy. As a toxic and difficult-to-use antibiotic, bacitracin doesn't work well orally. However, it is very effective topically. Bacitracin is synthesised via the so-called nonribosomal peptide synthetases (NRPSs), which means that ribosomes are not involved in its synthesis.
Synonyms Not Available
Brand Names
  1. Baci-rx
  2. Baciguent
  3. Baciim
  4. Bacitracin Bacillus licheniformis
  5. Ziba-rx
Brand Mixtures
  1. Antibiotic Ointment (Bacitracin + Polymyxin B (Polymyxin B Sulfate))
  2. Aurex Rotenone Drops (Bacitracin + Penicillin + Rotenone + Streptomycin (Streptomycin Sulfate) + Undecylenic Acid)
  3. Baciguent Plus Pain Reliever Ont (Bacitracin + Lidocaine)
  4. Bacitracin-Neomycin Polymyxin Ont (Bacitracin Zinc + Neomycin Sulfate + Polymyxin B Sulfate)
  5. Bacitracin-Neomycin-Polymixin Ont (Bacitracin Zinc + Neomycin Sulfate + Polymyxin B Sulfate)
  6. Bacitracin-Neomycin-Polymyxin Oph Ont (Bacitracin Zinc + Neomycin Sulfate + Polymyxin B Sulfate)
  7. Band-Aid-S-1 (Bacitracin Zinc + Polymyxin B Sulfate)
  8. Cortisporin (Bacitracin (Bacitracin Zinc) + Hydrocortisone + Neomycin (Neomycin Sulfate) + Polymyxin B (Polymyxin B Sulfate))
  9. Cortisporin (Bacitracin Zinc + Hydrocortisone + Neomycin Sulfate + Polymyxin B Sulfate)
  10. Emercreme No4 Ont Efa (Bacitracin + Benzocaine + Cetylpyridinium Chloride + Diphenylpyraline Hydrochloride + Tyrothricin)
  11. First Aid Antibiotic (Bacitracin Zinc + Polymyxin B Sulfate)
  12. First Aid Antibiotic Ointment (Bacitracin Zinc + Polymyxin B Sulfate)
  13. Gercillin (Bacitracin + Benzocaine + Polymyxin B Sulfate + Tyrothricin)
  14. Lanabiotic Ont (Bacitracin + Polymyxin B Sulfate)
  15. Mycitracin Oph Ont (Bacitracin + Neomycin Sulfate + Polymyxin B Sulfate)
  16. Neo Bace Ophthalmic Ointment (Bacitracin + Polymyxin B Sulfate)
  17. Neosporin Ointment (Bacitracin (Bacitracin Zinc) + Neomycin (Neomycin Sulfate) + Polymyxin B (Polymyxin B Sulfate))
  18. Neosporin Ophthalmic Ointment (Bacitracin (Bacitracin Zinc) + Neomycin (Neomycin Sulfate) + Polymyxin B (Polymyxin B Sulfate))
  19. Neotopic Ointment (Bacitracin (Bacitracin Zinc) + Neomycin (Neomycin Sulfate) + Polymyxin B (Polymyxin B Sulfate))
  20. Ozonol Antibiotic Plus - Ointment (Bacitracin + Lidocaine Hydrochloride + Polymyxin B (Polymyxin B Sulfate))
  21. Ozonol Antibiotic Plus Ont (Bacitracin + Lidocaine Hydrochloride + Polymyxin B Sulfate)
  22. Polycidin Ophthalmic Ointment (Bacitracin (Bacitracin Zinc) + Polymyxin B (Polymyxin B Sulfate))
  23. Polyderm Antibiotic Ointment (Bacitracin + Lidocaine Hydrochloride + Polymyxin B Sulfate)
  24. Polysporin Antibiotic Ointment (Bacitracin + Polymyxin B (Polymyxin B Sulfate))
  25. Polysporin Sterile Ophthalmic Ointment (Bacitracin (Bacitracin Zinc) + Polymyxin B (Polymyxin B Sulfate))
  26. Polysporin Topical First Aid Antibiotic Ointment (Bacitracin + Polymyxin B (Polymyxin B Sulfate))
  27. Polysporin Triple Antibiotic Ointment (Bacitracin + Gramicidin + Polymyxin B (Polymyxin B Sulfate))
  28. Polytopic Ont (Bacitracin + Polymyxin B (Polymyxin B Sulfate))
  29. Polytracin Ont (Bacitracin Zinc + Polymyxin B (Polymyxin B Sulfate))
  30. Sandoz Cortimyxin (Bacitracin (Bacitracin Zinc) + Hydrocortisone + Neomycin (Neomycin Sulfate) + Polymyxin B (Polymyxin B Sulfate))
Chemical IUPAC Name (4R)-4-[[(2S)-2-[[2-[(1S)-1-amino-2-methylbutyl]4,5-dihydro-1,3-thiazole-5-carbonyl]amino]-4-methylpentanoyl]amino]-5-[[(2S)-1-[[(3S,6R,9S,12R,15S,18R,21S)-3-(2-amino-2-oxoethyl)-18-(3-aminopropyl)-15-butan-2-yl-6-(carboxymethyl)-9-(3H-imidazol-4-ylmethyl)-2,5,8,11,14,17,20-heptaoxo-12-(phenylmethyl)-1,4,7,10,13,16,19-heptazacyclopentacos-21-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-5-oxopentanoic acid
Chemical Formula C66H103N17O16S
Chemical Structure Structure
CAS Registry Number 1405-87-4
InChI Identifier InChI=1/C66H103N17O16S/c1-9-35(6)52(69)66-72-32-48(100-66)63(97)80-43(26-34(4)5)59(93)75-42(22-23-50(85)86)58(92)83-53(36(7)10-2)64(98)76-40-20-15-16-25-71-55(89)46(29-49(68)84)78-62(96)47(30-51(87)88)79-61(95)45(28-39-31-70-33-73-39)77-60(94)44(27-38-18-13-12-14-19-38)81-65(99)54(37(8)11-3)82-57(91)41(21-17-24-67)74-56(40)90/h12-14,18-19,31,33-37,40-48,52-54H,9-11,15-17,20-30,32,67,69H2,1-8H3,(H2,68,84)(H,70,73)(H,71,89)(H,74,90)(H,75,93)(H,76,98)(H,77,94)(H,78,96)(H,79,95)(H,80,97)(H,81,99)(H,82,91)(H,83,92)(H,85,86)(H,87,88)/t35?,36?,37?,40-,41+,42+,43-,44+,45-,46-,47+,48?,52-,53-,54-/m0/s1/f/h71,73-83,85,87H,68H2
InChI Key MNJKVJAYSVAQLU-PFQTWMIJDA
KEGG Drug D00128 Link Image
KEGG Compound C01667 Link Image
PubChem Compound 439542 Link Image
PubChem Substance 4814 Link Image
ChEBI ID 28669 Link Image
PharmGKB ID PA448531 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02237196 Link Image
RxList Link http://www.rxlist.com/cgi/generic3/bacit.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Bacitracin Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 1422.6930
Monoisotopic Molecular Weight 1421.7489
State Solid
Melting Point 221 - 225 oC
Experimental Water Solubility Freely soluble Source: PhysProp
Predicted Water Solubility 2.52e-02 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -0.8 Source: PhysProp
Predicted LogP -2.98 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -4.75 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 CC[C@@H](C)[C@H](N)C1=NC[C@@H](S1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](CCC(O)=O)C(=O)N[C@@H]([C@H](C)CC)C(=O)N[C@H]1CCCCNC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](CC(O)=O)NC(=O)[C@H](CC2=CN=CN2)NC(=O)[C@@H](CC2=CC=CC=C2)NC(=O)[C@@H](NC(=O)[C@@H](CCCN)NC1=O)[C@H](C)CC
Canonical SMILES CCC(C)C(N)C1=NCC(S1)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(C(C)CC)C(=O)NC1CCCCNC(=O)C(CC(N)=O)NC(=O)C(CC(O)=O)NC(=O)C(CC2=CN=CN2)NC(=O)C(CC2=CC=CC=C2)NC(=O)C(NC(=O)C(CCCN)NC1=O)C(C)CC
Drug Category
  • Anti-Bacterial Agents
  • Anti-Infective Agents, Local
ATC Codes
AHFS Codes
  • 08:12.28.08
  • 84:04.04
Indication For the treatment of infants with pneumonia and empyema caused by staphylococci shown to be susceptible to the drug. Also used in ointment form for topical treatment of a variety of localized skin and eye infections, as well as for the prevention of wound infections.
Pharmacology Bacitracin is a mixture of related cyclic polypeptides produced by organisms of the licheniformis group of Bacillus subtilis var Tracy. As a polypeptide, toxic, and difficult to use chemical, Bacitracin doesn't work well orally, however is very effective topically. Bacitracin exerts pronounced antibacterial action in vitro against a variety of gram-positive and a few gram-negative organisms. However, among systemic diseases, only staphylococcal infections qualify for consideration of bacitracin therapy.
Mechanism of Action Bacitracin intereferes with the dephosphorylation of the 55-carbon, biphosphate lipid transport molecule, which carries the building blocks of the peptidoglycan bacterial cell wall outside the inner membrane for construction.
Absorption Absorption of bacitracin following intramuscular injection is rapid and complete. Absorption from the gastrointestinal tract following oral administration is not appreciable. Absorption following topical application is negligible.
Toxicity Oral, mouse: LD50 = >3750 mg/kg.
Protein Binding Not Available
Biotransformation Not Available
Half Life Not Available
Dosage Forms
Form Route
Ointment Topical
Powder, for solution Intramuscular
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References
  1. Wikipedia Link Image
  2. RxList Link Image
Organisms Affected
  • Enteric bacteria and other eubacteria
Targets
  1. Probable low molecular weight protein-tyrosine-phosphatase epsP
  2. Alpha-2-macroglobulin
  3. Protachykinin 1
  4. Insulin-degrading enzyme
Drug Target 1 [top]
Target 1 ID 560
Target 1 Name Probable low molecular weight protein-tyrosine-phosphatase epsP
Target 1 Synonyms
  1. EC 3.1.3.48
Target 1 Gene Name epsP
Target 1 Protein Sequence >Probable low molecular weight protein-tyrosine-phosphatase epsP 
MIKTILVVCIGNICRSPMAQALLRQSLPGVSVISAGIGALSGYPADPSAVEVMAHHGIDI
SEHRAQQLTGSLVSRADLILVMDGAQKQEIQSRHPAKTGSVFRLGEMEQFDIADPYRKQL
TAFEEALEMIQRGVDAWVPRIRALG
Target 1 Number of Residues 147
Target 1 Molecular Weight 15719
Target 1 Theoretical pI 6.94
Target 1 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
phosphoric ester hydrolase activity
phosphoric monoester hydrolase activity
phosphoprotein phosphatase activity
protein tyrosine phosphatase activity
Process
physiological process
metabolism
macromolecule metabolism
biopolymer metabolism
biopolymer modification
protein modification
protein amino acid dephosphorylation
Component
Not Available
Target 1 General Function Signal transduction mechanisms
Target 1 Specific Function May be involved in assembly or function of the EPS I polymerization/export complex and/or the epsB ATPase. Alternatively it may function in the removal of the terminal phosphate from C55-isoprenyl pyrophosphate in order to recycle the C55-isoprenyl phosphate lipid carrier used in the synthesis of polysaccharide repeat units
Target 1 Pathways Not Available
Target 1 Reactions
  • protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Essential
Target 1 GenBank ID Protein 17431492 Link Image
Target 1 UniProtKB/Swiss-Prot ID P58596 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name EPSP1_RALSO Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Cytoplasmic
Target 1 Gene Sequence >438 bp 
TCAACCGAGTGCCCGTATGCGGGGCACCCAGGCGTCGACACCGCGCTGGATCATTTCGAG
CGCCTCTTCGAAGGCGGTCAGCTGCTTGCGGTACGGGTCCGCGATATCGAACTGCTCCAT
CTCGCCCAACCGGAACACGCTGCCGGTCTTGGCGGGGTGGCGCGATTGGATCTCTTGCTT
CTGCGCACCGTCCATCACCAGGATCAGGTCGGCACGGCTGACCAGCGAACCGGTGAGCTG
CTGCGCGCGGTGCTCGGAGATATCAATGCCGTGGTGGGCCATCACCTCGACGGCGCTCGG
ATCGGCCGGGTAGCCCGACAGCGCGCCGATGCCCGCCGAGATGACGCTCACGCCCGGCAG
CGACTGCCGCAGCAGCGCCTGCGCCATCGGACTGCGGCAGATGTTGCCGATACACACGAC
AAGAATGGTCTTGATCAT
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. Salanoubat M, Genin S, Artiguenave F, Gouzy J, Mangenot S, Arlat M, Billault A, Brottier P, Camus JC, Cattolico L, Chandler M, Choisne N, Claudel-Renard C, Cunnac S, Demange N, Gaspin C, Lavie M, Moisan A, Robert C, Saurin W, Schiex T, Siguier P, Thebault P, Whalen M, Wincker P, Levy M, Weissenbach J, Boucher CA: Genome sequence of the plant pathogen Ralstonia solanacearum. Nature. 2002 Jan 31;415(6871):497-502. [PubMed Link Image]
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 1128
Target 2 Name Alpha-2-macroglobulin
Target 2 Synonyms
  1. Alpha-2-M
  2. Alpha-2-macroglobulin precursor
Target 2 Gene Name A2M
Target 2 Protein Sequence >Alpha-2-macroglobulin precursor 
MGKNKLLHPSLVLLLLVLLPTDASVSGKPQYMVLVPSLLHTETTEKGCVLLSYLNETVTV
SASLESVRGNRSLFTDLEAENDVLHCVAFAVPKSSSNEEVMFLTVQVKGPTQEFKKRTTV
MVKNEDSLVFVQTDKSIYKPGQTVKFRVVSMDENFHPLNELIPLVYIQDPKGNRIAQWQS
FQLEGGLKQFSFPLSSEPFQGSYKVVVQKKSGGRTEHPFTVEEFVLPKFEVQVTVPKIIT
ILEEEMNVSVCGLYTYGKPVPGHVTVSICRKYSDASDCHGEDSQAFCEKFSGQLNSHGCF
YQQVKTKVFQLKRKEYEMKLHTEAQIQEEGTVVELTGRQSSEITRTITKLSFVKVDSHFR
QGIPFFGQVRLVDGKGVPIPNKVIFIRGNEANYYSNATTDEHGLVQFSINTTNVMGTSLT
VRVNYKDRSPCYGYQWVSEEHEEAHHTAYLVFSPSKSFVHLEPMSHELPCGHTQTVQAHY
ILNGGTLLGLKKLSFYYLIMAKGGIVRTGTHGLLVKQEDMKGHFSISIPVKSDIAPVARL
LIYAVLPTGDVIGDSAKYDVENCLANKVDLSFSPSQSLPASHAHLRVTAAPQSVCALRAV
DQSVLLMKPDAELSASSVYNLLPEKDLTGFPGPLNDQDDEDCINRHNVYINGITYTPVSS
TNEKDMYSFLEDMGLKAFTNSKIRKPKMCPQLQQYEMHGPEGLRVGFYESDVMGRGHARL
VHVEEPHTETVRKYFPETWIWDLVVVNSAGVAEVGVTVPDTITEWKAGAFCLSEDAGLGI
SSTASLRAFQPFFVELTMPYSVIRGEAFTLKATVLNYLPKCIRVSVQLEASPAFLAVPVE
KEQAPHCICANGRQTVSWAVTPKSLGNVNFTVSAEALESQELCGTEVPSVPEHGRKDTVI
KPLLVEPEGLEKETTFNSLLCPSGGEVSEELSLKLPPNVVEESARASVSVLGDILGSAMQ
NTQNLLQMPYGCGEQNMVLFAPNIYVLDYLNETQQLTPEVKSKAIGYLNTGYQRQLNYKH
YDGSYSTFGERYGRNQGNTWLTAFVLKTFAQARAYIFIDEAHITQALIWLSQRQKDNGCF
RSSGSLLNNAIKGGVEDEVTLSAYITIALLEIPLTVTHPVVRNALFCLESAWKTAQEGDH
GSHVYTKALLAYAFALAGNQDKRKEVLKSLNEEAVKKDNSVHWERPQKPKAPVGHFYEPQ
APSAEVEMTSYVLLAYLTAQPAPTSEDLTSATNIVKWITKQQNAQGGFSSTQDTVVALHA
LSKYGAATFTRTGKAAQVTIQSSGTFSSKFQVDNNNRLLLQQVSLPELPGEYSMKVTGEG
CVYLQTSLKYNILPEKEEFPFALGVQTLPQTCDEPKAHTSFQISLSVSYTGSRSASNMAI
VDVKMVSGFIPLKPTVKMLERSNHVSRTEVSSNHVLIYLDKVSNQTLSLFFTVLQDVPVR
DLKPAIVKVYDYYETDEFAIAEYNAPCSKDLGNA
Target 2 Number of Residues 1498
Target 2 Molecular Weight 163280
Target 2 Theoretical pI 6.39
Target 2 GO Classification
Function
enzyme regulator activity
enzyme inhibitor activity
protease inhibitor activity
endopeptidase inhibitor activity
Process
Not Available
Component
Not Available
Target 2 General Function Involved in endopeptidase inhibitor activity
Target 2 Specific Function Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-23
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 177870 Link Image
Target 2 UniProtKB/Swiss-Prot ID P01023 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name A2MG_HUMAN Link Image
Target 2 PDB ID 1BV8 Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Secreted protein
Target 2 Gene Sequence >4425 bp 
ATGGGGAAGAACAAACTCCTTCATCCAAGTCTGGTTCTTCTCCTCTTGGTCCTCCTGCCC
ACAGACGCCTCAGTCTCTGGAAAACCGCAGTATATGGTTCTGGTCCCCTCCCTGCTCCAC
ACTGAGACCACTGAGAAGGGCTGTGTCCTTCTGAGCTACCTGAATGAGACAGTGACTGTA
AGTGCTTCCTTGGAGTCTGTCAGGGGAAACAGGAGCCTCTTCACTGACCTGGAGGCGGAG
AATGACGTACTCCACTGTGTCGCCTTCGCTGTCCCAAAGTCTTCATCCAATGAGGAGGTA
ATGTTCCTCACTGTCCAAGTGAAAGGACCAACCCAAGAATTTAAGAAGCGGACCACAGTG
ATGGTTAAGAACGAGGACAGTCTGGTCTTTGTCCAGACAGACAAATCAATCTACAAACCA
GGGCAGACAGTGAAATTTCGTGTTGTCTCCATGGATGAAAACTTTCACCCCCTGAATGAG
TTGATTCCACTAGTATACATTCAGGATCCCAAAGGAAATCGCATCGCACAATGGCAGAGT
TTCCAGTTAGAGGGTGGCCTCAAGCAATTTTCTTTTCCCCTCTCATCAGAGCCCTTCCAG
GGCTCCTACAAGGTGGTGGTACAGAAGAAATCAGGTGGAAGGACAGAGCACCCTTTCACC
GTGGAGGAATTTGTTCTTCCCAAGTTTGAAGTACAAGTAACAGTGCCAAAGATAATCACC
ATCTTGGAAGAAGAGATGAATGTATCAGTGTGTGGCCTATACACATATGGGAAGCCTGTC
CCTGGACATGTGACTGTGAGCATTTGCAGAAAGTATAGTGACGCTTCCGACTGCCACGGT
GAAGATTCACAGGCTTTCTGTGAGAAATTCAGTGGACAGCTAAACAGCCATGGCTGCTTC
TATCAGCAAGTAAAAACCAAGGTCTTCCAGCTGAAGAGGAAGGAGTATGAAATGAAACTT
CACACTGAGGCCCAGATCCAAGAAGAAGGAACAGTGGTGGAATTGACTGGAAGGCAGTCC
AGTGAAATCACAAGAACCATAACCAAACTCTCATTTGTGAAAGTGGACTCACACTTTCGA
CAGGGAATTCCCTTCTTTGGGCAGGTGCGCCTAGTAGATGGGAAAGGCGTCCCTATACCA
AATAAAGTCATATTCATCAGAGGAAATGAAGCAAACTATTACTCCAATGCTACCACGGAT
GAGCATGGCCTTGTACAGTTCTCTATCAACACCACCAACGTTATGGGTACCTCTCTTACT
GTTAGGGTCAATTACAAGGATCGTAGTCCCTGTTACGGCTACCAGTGGGTGTCAGAAGAA
CACGAAGAGGCACATCACACTGCTTATCTTGTGTTCTCCCCAAGCAAGAGCTTTGTCCAC
CTTGAGCCCATGTCTCATGAACTACCCTGTGGCCATACTCAGACAGTCCAGGCACATTAT
ATTCTGAATGGAGGCACCCTGCTGGGGCTGAAGAAGCTCTCCTTTTATTATCTGATAATG
GCAAAGGGAGGCATTGTCCGAACTGGGACTCATGGACTGCTTGTGAAGCAGGAAGACATG
AAGGGCCATTTTTCCATCTCAATCCCTGTGAAGTCAGACATTGCTCCTGTCGCTCGGTTG
CTCATCTATGCTGTTTTACCTACCGGGGACGTGATTGGGGATTCTGCAAAATATGATGTT
GAAAATTGTCTGGCCAACAAGGTGGATTTGAGCTTCAGCCCATCACAAAGTCTCCCAGCC
TCACACGCCCACCTGCGAGTCACAGCGGCTCCTCAGTCCGTCTGCGCCCTCCGTGCTGTG
GACCAAAGCGTGCTGCTCATGAAGCCTGATGCTGAGCTCTCGGCGTCCTCGGTTTACAAC
CTGCTACCAGAAAAGGACCTCACTGGCTTCCCTGGGCCTTTGAATGACCAGGACGATGAA
GACTGCATCAATCGTCATAATGTCTATATTAATGGAATCACATATACTCCAGTATCAAGT
ACAAATGAAAAGGATATGTACAGCTTCCTAGAGGACATGGGCTTAAAGGCATTCACCAAC
TCAAAGATTCGTAAACCCAAAATGTGTCCACAGCTTCAACAGTATGAAATGCATGGACCT
GAAGGTCTACGTGTAGGTTTTTATGAGTCAGATGTAATGGGAAGAGGCCATGCACGCCTG
GTGCATGTTGAAGAGCCTCACACGGAGACCGTACGAAAGTACTTCCCTGAGACATGGATC
TGGGATTTGGTGGTGGTAAACTCAGCAGGGGTGGCTGAGGTAGGAGTAACAGTCCCTGAC
ACCATCACCGAGTGGAAGGCAGGGGCCTTCTGCCTGTCTGAAGATGCTGGACTTGGTATC
TCTTCCACTGCCTCTCTCCGAGCCTTCCAGCCCTTCTTTGTGGAGCTTACAATGCCTTAC
TCTGTGATTCGTGGAGAGGCCTTCACACTCAAGGCCACGGTCCTAAACTACCTTCCCAAA
TGCATCCGGGTCAGTGTGCAGCTGGAAGCCTCTCCCGCCTTCCTTGCTGTCCCAGTGGAG
AAGGAACAAGCGCCTCACTGCATCTGTGCAAACGGGCGGCAAACTGTGTCCTGGGCAGTA
ACCCCAAAGTCATTAGGAAATGTGAATTTCACTGTGAGCGCAGAGGCACTAGAGTCTCAA
GAGCTGTGTGGGACTGAGGTGCCTTCAGTTCCTGAACACGGAAGGAAAGACACAGTCATC
AAGCCTCTGTTGGTTGAACCTGAAGGACTAGAGAAGGAAACAACATTCAACTCCCTACTT
TGTCCATCAGGTGGTGAGGTTTCTGAAGAATTATCCCTGAAACTGCCACCAAATGTGGTA
GAAGAATCTGCCCGAGCTTCTGTCTCAGTTTTGGGAGACATATTAGGCTCTGCCATGCAA
AACACACAAAATCTTCTCCAGATGCCCTATGGCTGTGGAGAGCAGAATATGGTCCTCTTT
GCTCCTAACATCTATGTACTGGATTATCTAAATGAAACACAGCAGCTTACTCCAGAGGTC
AAGTCCAAGGCCATTGGCTATCTCAACACTGGTTACCAGAGACAGTTGAACTACAAACAC
TATGATGGCTCCTACAGCACCTTTGGGGAGCGATATGGCAGGAACCAGGGCAACACCTGG
CTCACAGCCTTTGTTCTGAAGACTTTTGCCCAAGCTCGAGCCTACATCTTCATCGATGAA
GCACACATTACCCAAGCCCTCATATGGCTCTCCCAGAGGCAGAAGGACAATGGCTGTTTC
AGGAGCTCTGGGTCACTGCTCAACAATGCCATAAAGGGAGGAGTAGAAGATGAAGTGACC
CTCTCCGCCTATATCACCATCGCCCTTCTGGAGATTCCTCTCACAGTCACTCACCCTGTT
GTCCGCAATGCCCTGTTTTGCCTGGAGTCAGCCTGGAAGACAGCACAAGAAGGGGACCAT
GGCAGCCATGTATATACCAAAGCACTGCTGGCCTATGCTTTTGCCCTGGCAGGTAACCAG
GACAAGAGGAAGGAAGTACTCAAGTCACTTAATGAGGAAGCTGTGAAGAAAGACAACTCT
GTCCATTGGGAGCGCCCTCAGAAACCCAAGGCACCAGTGGGGCATTTTTACGAACCCCAG
GCTCCCTCTGCTGAGGTGGAGATGACATCCTATGTGCTCCTCGCTTATCTCACGGCCCAG
CCAGCCCCAACCTCGGAGGACCTGACCTCTGCAACCAACATCGTGAAGTGGATCACGAAG
CAGCAGAATGCCCAGGGCGGTTTCTCCTCCACCCAGGACACAGTGGTGGCTCTCCATGCT
CTGTCCAAATATGGAGCCGCCACATTTACCAGGACTGGGAAGGCTGCACAGGTGACTATC
CAGTCTTCAGGGACATTTTCCAGCAAATTCCAAGTGGACAACAACAATCGCCTGTTACTG
CAGCAGGTCTCATTGCCAGAGCTGCCTGGGGAATACAGCATGAAAGTGACAGGAGAAGGA
TGTGTCTACCTCCAGACCTCCTTGAAATACAATATTCTCCCAGAAAAGGAAGAGTTCCCC
TTTGCTTTAGGAGTGCAGACTCTGCCTCAAACTTGTGATGAACCCAAAGCCCACACCAGC
TTCCAAATCTCCCTAAGTGTCAGTTACACAGGGAGCCGCTCTGCCTCCAACATGGCGATC
GTTGATGTGAAGATGGTCTCTGGCTTCATTCCCCTGAAGCCAACAGTGAAAATGCTTGAA
AGATCTAACCATGTGAGCCGGACAGAAGTCAGCAGCAACCATGTCTTGATTTACCTTGAT
AAGGTGTCAAATCAGACACTGAGCTTGTTCTTCACGGTTCTGCAAGATGTCCCAGTAAGA
GATCTCAAACCAGCCATAGTGAAAGTCTATGATTACTACGAGACGGATGAGTTTGCAATC
GCTGAGTACAATGCTCCTTGCAGCAAAGATCTTGGAAATGCTTGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID A2M Link Image
Target 2 GenAtlas ID A2M Link Image
Target 2 HGNC ID HGNC:7 Link Image
Target 2 Chromosome Location 12
Target 2 Locus 12p13.3-p12.3
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed Link Image]
  2. Poller W, Faber JP, Klobeck G, Olek K: Cloning of the human alpha 2-macroglobulin gene and detection of mutations in two functional domains: the bait region and the thiolester site. Hum Genet. 1992 Jan;88(3):313-9. [PubMed Link Image]
  3. Matthijs G, Devriendt K, Cassiman JJ, Van den Berghe H, Marynen P: Structure of the human alpha-2 macroglobulin gene and its promotor. Biochem Biophys Res Commun. 1992 Apr 30;184(2):596-603. [PubMed Link Image]
  4. Marynen P, Devriendt K, Van den Berghe H, Cassiman JJ: A genetic polymorphism in a functional domain of human pregnancy zone protein: the bait region. Genomic structure of the bait domains of human pregnancy zone protein and alpha 2 macroglobulin. FEBS Lett. 1990 Mar 26;262(2):349-52. [PubMed Link Image]
  5. Poller W, Faber JP, Olek K: Sequence polymorphism in the human alpha-2-macroglobulin (A2M) gene. Nucleic Acids Res. 1991 Jan 11;19(1):198. [PubMed Link Image]
  6. Bell GI, Rall LB, Sanchez-Pescador R, Merryweather JP, Scott J, Eddy RL, Shows TB: Human alpha 2-macroglobulin gene is located on chromosome 12. Somat Cell Mol Genet. 1985 May;11(3):285-9. [PubMed Link Image]
  7. Kan CC, Solomon E, Belt KT, Chain AC, Hiorns LR, Fey G: Nucleotide sequence of cDNA encoding human alpha 2-macroglobulin and assignment of the chromosomal locus. Proc Natl Acad Sci U S A. 1985 Apr;82(8):2282-6. [PubMed Link Image]
  8. Sottrup-Jensen L, Lonblad PB, Stepanik TM, Petersen TE, Magnusson S, Jornvall H: Primary structure of the 'bait' region for proteinases in alpha 2-macroglobulin. Nature of the complex. FEBS Lett. 1981 May 18;127(2):167-73. [PubMed Link Image]
  9. Hall PK, Nelles LP, Travis J, Roberts RC: Proteolytic cleavage sites on alpha 2-macroglobulin resulting in proteinase binding are different for trypsin and Staphylococcus aureus V-8 proteinase. Biochem Biophys Res Commun. 1981 May 15;100(1):8-16. [PubMed Link Image]
  10. Mortensen SB, Sottrup-Jensen L, Hansen HF, Petersen TE, Magnusson S: Primary and secondary cleavage sites in the bait region of alpha 2-macroglobulin. FEBS Lett. 1981 Dec 7;135(2):295-300. [PubMed Link Image]
  11. 6195065 Virca GD, Salvesen GS, Travis J: Human neutrophil elastase and cathepsin G cleavage sites in the bait region of alpha 2-macroglobulin. Proposed structural limits of the bait region. Hoppe Seylers Z Physiol Chem. 1983 Sep;364(9):1297-302.
  12. 6203908 Sottrup-Jensen L, Stepanik TM, Kristensen T, Wierzbicki DM, Jones CM, Lonblad PB, Magnusson S, Petersen TE: Primary structure of human alpha 2-macroglobulin. V. The complete structure. J Biol Chem. 1984 Jul 10;259(13):8318-27.
  13. 9865955 Huang W, Dolmer K, Liao X, Gettins PG: Localization of basic residues required for receptor binding to the single alpha-helix of the receptor binding domain of human alpha2-macroglobulin. Protein Sci. 1998 Dec;7(12):2602-12.
Target 2 Drug References
  1. Maxfield FR, Davies PJ, Klempner L, Willingham MC, Pastan I: Epidermal growth factor stimulation of DNA synthesis is potentiated by compounds that inhibit its clustering in coated pits. Proc Natl Acad Sci U S A. 1979 Nov;76(11):5731-5. [PubMed Link Image]
  2. Dickson RB, Willingham MC, Pastan I: Binding and internalization of 125I-alpha 2-macroglobulin by cultured fibroblasts. J Biol Chem. 1981 Apr 10;256(7):3454-9. [PubMed Link Image]
  3. Dickson RB, Willingham MC, Gallo M, Pastan I: Inhibition by bacitracin of high affinity binding of 125I-alpha 2M to plasma membranes. FEBS Lett. 1981 Apr 20;126(2):265-8. [PubMed Link Image]
  4. Hanover JA, Cheng S, Willingham MC, Pastan IH: alpha 2-Macroglobulin binding to cultured fibroblasts. Solubilization and partial purification of binding sites. J Biol Chem. 1983 Jan 10;258(1):370-7. [PubMed Link Image]
  5. Gliemann J, Larsen TR, Sottrup-Jensen L: Cell association and degradation of alpha 2-macroglobulin-trypsin complexes in hepatocytes and adipocytes. Biochim Biophys Acta. 1983 Mar 31;756(2):230-7. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 2046
Target 3 Name Protachykinin 1
Target 3 Synonyms
  1. PPT
  2. Protachykinin 1 precursor
Target 3 Gene Name TAC1
Target 3 Protein Sequence >Protachykinin 1 precursor 
MKILVALAVFFLVSTQLFAEEIGANDDLNYWSDWYDSDQIKEELPEPFEHLLQRIARRPK
PQQFFGLMGKRDADSSIEKQVALLKALYGHGQISHKRHKTDSFVGLMGKRALNSVAYERS
AMQNYERRR
Target 3 Number of Residues 131
Target 3 Molecular Weight 15003
Target 3 Theoretical pI 9.38
Target 3 GO Classification
Function
Not Available
Process
cell-cell signaling
transmission of nerve impulse
synaptic transmission
cellular process
cell communication
signal transduction
cell surface receptor linked signal transduction
G-protein coupled receptor protein signaling pathway
tachykinin signaling pathway
Component
Not Available
Target 3 General Function Not Available
Target 3 Specific Function Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
Target 3 Signals
  • 1-19
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 29483 Link Image
Target 3 UniProtKB/Swiss-Prot ID P20366 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name TKN1_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Secreted protein
Target 3 Gene Sequence >390 bp 
ATGAAAATCCTCGTGGCCTTGGCAGTCTTTTTTCTTGTCTCCACTCAGCTGTTTGCAGAA
GAAATAGGAGCCAATGATGATCTGAATTACTGGTCCGACTGGTACGACAGCGACCAGATC
AAGGAGGAACTGCCGGAGCCCTTTGAGCATCTTCTGCAGAGAATCGCCCGGAGACCCAAG
CCTCAGCAGTTCTTTGGATTAATGGGCAAACGGGATGCTGATTCCTCAATTGAAAAACAA
GTGGCCCTGTTAAAGGCTCTTTATGGACATGGCCAGATCTCTCACAAAAGACATAAAACA
GATTCCTTTGTTGGACTAATGGGCAAAAGAGCTTTAAATTCTGTGGCTTATGAAAGGAGT
GCAATGCAGAATTATGAAAGAAGACGTTAA
Target 3 GenBank Gene ID
Target 3 GeneCard ID TAC1 Link Image
Target 3 GenAtlas ID TAC1 Link Image
Target 3 HGNC ID HGNC:11517 Link Image
Target 3 Chromosome Location Not Available
Target 3 Locus Not Available
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Chiwakata C, Brackmann B, Hunt N, Davidoff M, Schulze W, Ivell R: Tachykinin (substance-P) gene expression in Leydig cells of the human and mouse testis. Endocrinology. 1991 May;128(5):2441-8. [PubMed Link Image]
  2. McGregor GP, Conlon JM: Characterization of the C-terminal flanking peptide of human beta-preprotachykinin. Peptides. 1990 Sep-Oct;11(5):907-10. [PubMed Link Image]
  3. Theodorsson-Norheim E, Jornvall H, Andersson M, Norheim I, Oberg K, Jacobsson G: Isolation and characterization of neurokinin A, neurokinin A(3-10) and neurokinin A(4-10) from a neutral water extract of a metastatic ileal carcinoid tumour. Eur J Biochem. 1987 Aug 3;166(3):693-7. [PubMed Link Image]
  4. Harmar AJ, Armstrong A, Pascall JC, Chapman K, Rosie R, Curtis A, Going J, Edwards CR, Fink G: cDNA sequence of human beta-preprotachykinin, the common precursor to substance P and neurokinin A. FEBS Lett. 1986 Nov 10;208(1):67-72. [PubMed Link Image]
Target 3 Drug References
  1. Seabrook GR, Main M, Bowery B, Wood N, Hill RG: Differences in neurokinin receptor pharmacology between rat and guinea-pig superior cervical ganglia. Br J Pharmacol. 1992 Apr;105(4):925-8. [PubMed Link Image]
  2. Horsthemke B, Schulz M, Bauer K: Degradation of substance P by neurones and glial cells. Biochem Biophys Res Commun. 1984 Dec 14;125(2):728-33. [PubMed Link Image]
  3. Kulakowski EC, Lampson WG, Schaffer SW, Lovenberg W: Action of substance P on the working rat heart. Biochem Pharmacol. 1983 Mar 15;32(6):1097-100. [PubMed Link Image]
  4. Webber SE, Foreman JC: The effect of substance P and related peptides on the guinea-pig lung strip. Agents Actions. 1984 Apr;14(3-4):425-8. [PubMed Link Image]
  5. Morton CR, Chahl LA: Pharmacology of the neurogenic oedema response to electrical stimulation of the saphenous nerve in the rat. Naunyn Schmiedebergs Arch Pharmacol. 1980 Nov;314(3):271-6. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 2155
Target 4 Name Insulin-degrading enzyme
Target 4 Synonyms
  1. EC 3.4.24.56
  2. Insulin protease
  3. Insulinase
  4. Insulysin
Target 4 Gene Name IDE
Target 4 Protein Sequence >Insulin-degrading enzyme 
MRYRLAWLLHPALPSTFRSVLGARLPPPERLCGFQKKTYSKMNNPAIKRIGNHITKSPED
KREYRGLELANGIKVLLMSDPTTDKSSAALDVHIGSLSDPPNIAGLSHFCEHMLFLGTKK
YPKENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFAQFFLCPLFDESCKD
REVNAVDSEHEKNVMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQE
LLKFHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPFQEEHLKQ
LYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLV
GGQKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQEWVFQECKDLNAV
AFRFKDKERPRGYTSKIAGILHYYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAI
VSKSFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPL
EKEATPYPALIKDTVMSKLWFKQDDKKKKPKACLNFEFFSPFAYVDPLHCNMAYLYLELL
KDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIEKMATFEIDEKRFE
IIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLL
SRLHIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQ
QRNEVHNNCGIEIYYQTDMQSTSENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRA
NGIQSLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRRLDKPKKL
SAECAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLA
REMDSCPVVGEFPCQNDINLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPHINFMAAKL
Target 4 Number of Residues 1035
Target 4 Molecular Weight 118023
Target 4 Theoretical pI 6.74
Target 4 GO Classification
Function
catalytic activity
hydrolase activity
peptidase activity
endopeptidase activity
metalloendopeptidase activity
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
proteolysis
Component
Not Available
Target 4 General Function Posttranslational modification, protein turnover, chaperones
Target 4 Specific Function May play a role in the cellular processing of insulin. May be involved in intercellular peptide signaling
Target 4 Pathways Not Available
Target 4 Reactions
  • Degradation of insulin, glucagon and other polypeptides. No action on proteins COFACTOR Zinc INHIBITOR EDTA; 1,10-Phenanthroline; Bacitracin; N-Ethylmaleimide
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 184556 Link Image
Target 4 UniProtKB/Swiss-Prot ID P14735 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name IDE_HUMAN Link Image
Target 4 PDB ID Not Available
Target 4 Cellular Location
  • Cytoplasm
Target 4 Gene Sequence >3060 bp 
ATGCGGTACCGGCTAGCGTGGCTTCTGCACCCCGCACTGCCCAGCACCTTCCGCTCAGTC
CTCGGCGCCCGCCTGCCGCCTCCGGAGCGCCTGTGTGGTTTCCAAAAAAAGACTTACAGC
AAAATGAATAATCCAGCCATCAAGAGAATAGGAAATCACATTACCAAGTCTCCTGAAGAC
AAGCGAGAATATCGAGGGCTAGAGCTGGCCAATGGTATCAAAGTACTTCTTATGAGTGAT
CCCACCACGGATAAGTCATCAGCAGCACTTGATGTGCACATAGGTTCATTGTCGGATCCT
CCAAATATTGCTGGCTTAAGTCATTTTTGTGAACATATGCTTTTTTTGGGAACAAAGAAA
TACCCTAAAGAAAATGAATACAGCCAGTTTCTCAGTGAGCATGCAGGAAGTTCAAATGCC
TTTACTAGTGGAGAGCATACCAATTACTATTTTGATGTTTCTCATGAACACCTAGAAGGT
GCCCTAGACAGGTTTGCACAGTTTTTTCTGTGCCCCTTGTTCGATGAAAGTTGCAAAGAC
AGAGAGGTGAATGCAGTTGATTCAGAACATGAGAAGAATGTGATGAATGATGCCTGGAGA
CTCTTTCAATTGGAAAAAGCTACAGGGAATCCTAAACACCCCTTCAGTAAATTTGGGACA
GGTAACAAATATACTCTGGAGACTAGACCAAACCAAGAAGGCATTGATGTAAGACAAGAG
CTACTGAAATTCCATTCTGCTTACTATTCATCCAACTTAATGGCTGTTTGTGTTTTAGGT
CGAGAATCTTTAGATGACTTGACTAATCTGGTGGTAAAGTTATTTTCTGAAGTAGAGAAC
AAAAATGTTCCATTGCCAGAATTTCCTGAACACCCTTTCCAAGAAGAACATCTTAAACAA
CTTTACAAAATAGTACCCATTAAAGATATTAGGAATCTCTATGTGACATTTCCCATACCT
GACCTTCAGAAATACTACAAATCAAATCCTGGTCATTATCTTGGTCATCTCATTGGGCAT
GAAGGTCCTGGAAGTCTGTTATCAGAACTTAAGTCAAAGGGCTGGGTTAATACTCTTGTT
GGTGGGCAGAAGGAAGGAGCCCGAGGTTTTATGTTTTTTATCATTAATGTGGACTTGACC
GAGGAAGGATTATTACATGTTGAAGATATAATTTTGCACATGTTTCAATACATTCAGAAG
TTACGTGCAGAAGGACCTCAAGAATGGGTTTTCCAAGAGTGCAAGGACTTGAATGCTGTT
GCTTTTAGGTTTAAAGACAAAGAGAGGCCACGGGGCTATACATCTAAGATTGCAGGAATA
TTGCATTATTATCCCCTAGAAGAGGTGCTCACAGCGGAATATTTACTGGAAGAATTTAGA
CCTGACTTAATAGAGATGGTTCTCGATAAACTCAGACCAGAAAATGTCCGGGTTGCCATA
GTTTCTAAATCTTTTGAAGGAAAAACTGATCGCACAGAAGAGTGGTATGGAACCCAGTAC
AAACAAGAAGCTATACCGGATGAAGTCATCAAGAAATGGCAAAATGCTGACCTGAATGGG
AAATTTAAACTTCCTACAAAGAATGAATTTATTCCTACGAATTTTGAGATTTTACCGTTA
GAAAAAGAGGCGACACCATACCCTGCTCTTATTAAGGATACAGTCATGAGCAAACTTTGG
TTCAAACAAGATGATAAGAAAAAAAAGCCGAAGGCTTGTCTCAACTTTGAATTTTTCAGC
CCATTTGCTTATGTGGACCCCTTGCACTGTAACATGGCCTATTTGTACCTTGAGCTCCTC
AAAGACTCACTCAACGAGTATGCATATGCAGCAGAGCTAGCAGGCTTGAGCTATGATCTC
CAAAATACCATCTATGGGATGTATCTTTCAGTGAAAGGTTACAATGACAAGCAGCCAATT
TTACTAAAGAAGATTATTGAGAAAATGGCTACCTTTGAGATTGATGAAAAAAGATTTGAA
ATTATCAAAGAAGCATATATGCGATCTCTTAACAATTTCCGGGCTGAACAGCCTCACCAG
CATGCCATGTACTACCTCCGCTTGCTGATGACTGAAGTGGCCTGGACTAAAGATGAGTTA
AAAGAAGCTCTGGATGATGTAACCCTTCCTCGCCTTAAGGCCTTCATACCTCAGCTCCTG
TCACGGCTGCACATTGAAGCCCTTCTCCATGGAAACATAACAAAGCAGGCTGCATTAGGA
ATTATGCAGATGGTTGAAGACACCCTCATTGAACATGCTCATACCAAACCTCTCCTTCCA
AGTCAGCTGGTTCGGTATAGAGAAGTTCAGCTCCCTGACAGAGGATGGTTTGTTTATCAG
CAGAGAAATGAAGTTCACAATAACTGTGGCATCGAGATATACTACCAAACAGACATGCAA
AGCACCTCAGAGAATATGTTTCTGGAGCTCTTCTGTCAGATTATCTCGGAACCTTGCTTC
AACACCCTGCGCACCAAGGAGCAGTTGGGCTATATCGTCTTCAGCGGGCCACGTCGAGCT
AATGGCATACAGAGCTTGAGATTCATCATCCAGTCAGAAAAGCCACCTCACTACCTAGAA
AGCAGAGTGGAAGCTTTCTTAATTACCATGGAAAAGTCCATAGAGGACATGACAGAAGAG
GCCTTCCAAAAACACATTCAGGCATTAGCAATTCGTCGACTAGACAAACCAAAGAAGCTA
TCTGCTGAGTGTGCTAAATACTGGGGAGAAATCATCTCCCAGCAATATAATTTTGACAGA
GATAACACTGAGGTTGCATATTTAAAGACACTTACCAAGGAAGATATCATCAAATTCTAC
AAGGAAATGTTGGCAGTAGATGCTCCAAGGAGACATAAGGTATCCGTCCATGTTCTTGCC
AGGGAAATGGATTCTTGTCCTGTTGTTGGAGAGTTCCCATGTCAAAATGACATAAATTTG
TCACAAGCACCAGCCTTGCCACAACCTGAAGTGATTCAGAACATGACCGAATTCAAGCGT
GGTCTGCCACTGTTTCCCCTTGTGAAACCACATATTAACTTCATGGCTGCAAAACTCTGA
Target 4 GenBank Gene ID
Target 4 GeneCard ID IDE Link Image
Target 4 GenAtlas ID IDE Link Image
Target 4 HGNC ID HGNC:5381 Link Image
Target 4 Chromosome Location 10
Target 4 Locus 10q23-q25
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Affholter JA, Hsieh CL, Francke U, Roth RA: Insulin-degrading enzyme: stable expression of the human complementary DNA, characterization of its protein product, and chromosomal mapping of the human and mouse genes. Mol Endocrinol. 1990 Aug;4(8):1125-35. [PubMed Link Image]
  2. Affholter JA, Fried VA, Roth RA: Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III. Science. 1988 Dec 9;242(4884):1415-8. [PubMed Link Image]
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]

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