| 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 |
|
| Name |
Bacitracin |
| Drug Type |
|
| 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 |
- Baci-rx
- Baciguent
- Baciim
- Bacitracin Bacillus licheniformis
- Ziba-rx
|
| Brand Mixtures |
- Antibiotic Ointment (Bacitracin + Polymyxin B (Polymyxin B Sulfate))
- Aurex Rotenone Drops (Bacitracin + Penicillin + Rotenone + Streptomycin (Streptomycin Sulfate) + Undecylenic Acid)
- Baciguent Plus Pain Reliever Ont (Bacitracin + Lidocaine)
- Bacitracin-Neomycin Polymyxin Ont (Bacitracin Zinc + Neomycin Sulfate + Polymyxin B Sulfate)
- Bacitracin-Neomycin-Polymixin Ont (Bacitracin Zinc + Neomycin Sulfate + Polymyxin B Sulfate)
- Bacitracin-Neomycin-Polymyxin Oph Ont (Bacitracin Zinc + Neomycin Sulfate + Polymyxin B Sulfate)
- Band-Aid-S-1 (Bacitracin Zinc + Polymyxin B Sulfate)
- Cortisporin (Bacitracin (Bacitracin Zinc) + Hydrocortisone + Neomycin (Neomycin Sulfate) + Polymyxin B (Polymyxin B Sulfate))
- Cortisporin (Bacitracin Zinc + Hydrocortisone + Neomycin Sulfate + Polymyxin B Sulfate)
- Emercreme No4 Ont Efa (Bacitracin + Benzocaine + Cetylpyridinium Chloride + Diphenylpyraline Hydrochloride + Tyrothricin)
- First Aid Antibiotic (Bacitracin Zinc + Polymyxin B Sulfate)
- First Aid Antibiotic Ointment (Bacitracin Zinc + Polymyxin B Sulfate)
- Gercillin (Bacitracin + Benzocaine + Polymyxin B Sulfate + Tyrothricin)
- Lanabiotic Ont (Bacitracin + Polymyxin B Sulfate)
- Mycitracin Oph Ont (Bacitracin + Neomycin Sulfate + Polymyxin B Sulfate)
- Neo Bace Ophthalmic Ointment (Bacitracin + Polymyxin B Sulfate)
- Neosporin Ointment (Bacitracin (Bacitracin Zinc) + Neomycin (Neomycin Sulfate) + Polymyxin B (Polymyxin B Sulfate))
- Neosporin Ophthalmic Ointment (Bacitracin (Bacitracin Zinc) + Neomycin (Neomycin Sulfate) + Polymyxin B (Polymyxin B Sulfate))
- Neotopic Ointment (Bacitracin (Bacitracin Zinc) + Neomycin (Neomycin Sulfate) + Polymyxin B (Polymyxin B Sulfate))
- Ozonol Antibiotic Plus - Ointment (Bacitracin + Lidocaine Hydrochloride + Polymyxin B (Polymyxin B Sulfate))
- Ozonol Antibiotic Plus Ont (Bacitracin + Lidocaine Hydrochloride + Polymyxin B Sulfate)
- Polycidin Ophthalmic Ointment (Bacitracin (Bacitracin Zinc) + Polymyxin B (Polymyxin B Sulfate))
- Polyderm Antibiotic Ointment (Bacitracin + Lidocaine Hydrochloride + Polymyxin B Sulfate)
- Polysporin Antibiotic Ointment (Bacitracin + Polymyxin B (Polymyxin B Sulfate))
- Polysporin Sterile Ophthalmic Ointment (Bacitracin (Bacitracin Zinc) + Polymyxin B (Polymyxin B Sulfate))
- Polysporin Topical First Aid Antibiotic Ointment (Bacitracin + Polymyxin B (Polymyxin B Sulfate))
- Polysporin Triple Antibiotic Ointment (Bacitracin + Gramicidin + Polymyxin B (Polymyxin B Sulfate))
- Polytopic Ont (Bacitracin + Polymyxin B (Polymyxin B Sulfate))
- Polytracin Ont (Bacitracin Zinc + Polymyxin B (Polymyxin B Sulfate))
- 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 |
 |
| 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  |
| KEGG Compound |
C01667  |
| PubChem Compound |
439542  |
| PubChem Substance |
4814  |
| ChEBI ID |
28669  |
| PharmGKB ID |
PA448531  |
| HET ID |
Not Available |
| GenBank ID |
Not Available |
| Drug ID Number [DIN] |
02237196  |
| RxList Link |
http://www.rxlist.com/cgi/generic3/bacit.htm  |
| PDRhealth Link |
Not Available |
| Wikipedia Link |
http://en.wikipedia.org/wiki/Bacitracin  |
| 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 | Download  |
| SDF File |
Show | Download  |
| PDB File |
Show | Download  |
| 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 |
|
| 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  |
| Contraindications |
Show  |
| Interactions |
Show  |
| Drug Interactions |
Not Available
|
| Food Interactions |
Not Available
|
| Pathways |
Not Available
|
| General References |
- Wikipedia

- RxList

|
| Organisms Affected |
- Enteric bacteria and other eubacteria
|
| Targets |
- Probable low molecular weight protein-tyrosine-phosphatase epsP
- Alpha-2-macroglobulin
- Protachykinin 1
- 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 |
- 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 |
|
| Target 1 Transmembrane Regions |
|
| Target 1 Essentiality |
Essential |
| Target 1 GenBank ID Protein |
17431492  |
| Target 1 UniProtKB/Swiss-Prot ID |
P58596  |
| Target 1 UniProtKB/Swiss-Prot Entry Name |
EPSP1_RALSO  |
| Target 1 PDB ID |
Not Available |
| Target 1 Cellular Location |
|
| 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  |
| Target 1 General References |
- 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
]
|
| Target 1 Drug References |
- 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
]
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed
]
|
|
Drug Target 2
[top]
|
| Target 2 ID |
1128 |
| Target 2 Name |
Alpha-2-macroglobulin |
| Target 2 Synonyms |
- Alpha-2-M
- 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 |
|
| Target 2 Transmembrane Regions |
|
| Target 2 Essentiality |
Non-Essential |
| Target 2 GenBank ID Protein |
177870  |
| Target 2 UniProtKB/Swiss-Prot ID |
P01023  |
| Target 2 UniProtKB/Swiss-Prot Entry Name |
A2MG_HUMAN  |
| Target 2 PDB ID |
1BV8  |
| Target 2 PDB File |
Show |
| Target 2 3D Structure |
|
| Target 2 Cellular Location |
|
| 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  |
| Target 2 GenAtlas ID |
A2M  |
| Target 2 HGNC ID |
HGNC:7  |
| Target 2 Chromosome Location |
12 |
| Target 2 Locus |
12p13.3-p12.3 |
| Target 2 SNPs |
SNPJam Report  |
| Target 2 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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.
- 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.
- 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 |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
|
Drug Target 3
[top]
|
| Target 3 ID |
2046 |
| Target 3 Name |
Protachykinin 1 |
| Target 3 Synonyms |
- PPT
- 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 |
|
| Target 3 Transmembrane Regions |
|
| Target 3 Essentiality |
Non-Essential |
| Target 3 GenBank ID Protein |
29483  |
| Target 3 UniProtKB/Swiss-Prot ID |
P20366  |
| Target 3 UniProtKB/Swiss-Prot Entry Name |
TKN1_HUMAN  |
| Target 3 PDB ID |
Not Available |
| Target 3 Cellular Location |
|
| Target 3 Gene Sequence |
>390 bp
ATGAAAATCCTCGTGGCCTTGGCAGTCTTTTTTCTTGTCTCCACTCAGCTGTTTGCAGAA
GAAATAGGAGCCAATGATGATCTGAATTACTGGTCCGACTGGTACGACAGCGACCAGATC
AAGGAGGAACTGCCGGAGCCCTTTGAGCATCTTCTGCAGAGAATCGCCCGGAGACCCAAG
CCTCAGCAGTTCTTTGGATTAATGGGCAAACGGGATGCTGATTCCTCAATTGAAAAACAA
GTGGCCCTGTTAAAGGCTCTTTATGGACATGGCCAGATCTCTCACAAAAGACATAAAACA
GATTCCTTTGTTGGACTAATGGGCAAAAGAGCTTTAAATTCTGTGGCTTATGAAAGGAGT
GCAATGCAGAATTATGAAAGAAGACGTTAA
|
| Target 3 GenBank Gene ID |
|
| Target 3 GeneCard ID |
TAC1  |
| Target 3 GenAtlas ID |
TAC1  |
| Target 3 HGNC ID |
HGNC:11517  |
| Target 3 Chromosome Location |
Not Available |
| Target 3 Locus |
Not Available |
| Target 3 SNPs |
SNPJam Report  |
| Target 3 General References |
- 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
]
- McGregor GP, Conlon JM: Characterization of the C-terminal flanking peptide of human beta-preprotachykinin. Peptides. 1990 Sep-Oct;11(5):907-10. [PubMed
]
- 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
]
- 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
]
|
| Target 3 Drug References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
|
Drug Target 4
[top]
|
| Target 4 ID |
2155 |
| Target 4 Name |
Insulin-degrading enzyme |
| Target 4 Synonyms |
- EC 3.4.24.56
- Insulin protease
- Insulinase
- 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 |
|
| Target 4 Transmembrane Regions |
|
| Target 4 Essentiality |
Non-Essential |
| Target 4 GenBank ID Protein |
184556  |
| Target 4 UniProtKB/Swiss-Prot ID |
P14735  |
| Target 4 UniProtKB/Swiss-Prot Entry Name |
IDE_HUMAN  |
| Target 4 PDB ID |
Not Available |
| Target 4 Cellular Location |
|
| 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  |
| Target 4 GenAtlas ID |
IDE  |
| Target 4 HGNC ID |
HGNC:5381  |
| Target 4 Chromosome Location |
10 |
| Target 4 Locus |
10q23-q25 |
| Target 4 SNPs |
SNPJam Report  |
| Target 4 General References |
- 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
]
- 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
]
|
| Target 4 Drug References |
- Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed
]
|