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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:04:09
Primary Accession Number DB00537
Secondary Accession Number
  • APRD00424
  • EXPT00999
Name Ciprofloxacin
Drug Type
  • Approved
  • Investigational
  • Small Molecule
Description A broad-spectrum antimicrobial carboxyfluoroquinoline. [PubChem]
Synonyms
  1. Ciprofloxacin HCl
  2. Ciprofloxacin dihydrochloride
  3. Ciprofloxacin hydrochloride
  4. Ciprofloxacin monohydrochloride
  5. Ciprofloxacina
  6. ciprofloxacin
Brand Names
  1. Bacquinor
  2. Baycip
  3. Bernoflox
  4. Ciflox
  5. Cifloxin
  6. Ciloxan
  7. Ciprinol
  8. Cipro
  9. Cipro I.V.
  10. Cipro XL
  11. Cipro XR
  12. Ciprobay
  13. Ciprocinol
  14. Ciprodar
  15. Cipromycin
  16. Ciproquinol
  17. Ciproxan
  18. Ciproxin
  19. Flociprin
  20. Floxin
  21. Ocuflox
  22. Proquin XR
  23. Septicide
  24. Velomonit
Brand Mixtures
  1. Cipro HC Otic Suspension (Ciprofloxacin hydrochloride + Hydrocortisone)
  2. Ciprodex (Ciprofloxacin hydrochloride + Dexamethasone)
Chemical IUPAC Name 1-cyclopropyl-6-fluoro-4-oxo-7-piperazin-1-ylquinoline-3-carboxylic acid
Chemical Formula C17H18FN3O3
Chemical Structure Structure
CAS Registry Number 85721-33-1
InChI Identifier InChI=1/C17H18FN3O3/c18-13-7-11-14(8-15(13)20-5-3-19-4-6-20)21(10-1-2-10)9-12(16(11)22)17(23)24/h7-10,19H,1-6H2,(H,23,24)/f/h23H
InChI Key MYSWGUAQZAJSOK-MPIMZMORCO
KEGG Drug D00186 Link Image
KEGG Compound C05349 Link Image
PubChem Compound 2764 Link Image
PubChem Substance 192835 Link Image
ChEBI ID Not Available
PharmGKB ID PA449009 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02248439 Link Image
RxList Link http://www.rxlist.com/cgi/generic/cipro.htm Link Image
PDRhealth Link http://www.pdrhealth.com/drug_info/rxdrugprofiles/drugs/cip1082.shtml Link Image
Wikipedia Link http://en.wikipedia.org/wiki/Ciprofloxacin Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference K. Grohe et al.; U.S. Pat. 4,670,444 (1987)
Average Molecular Weight 331.3415
Monoisotopic Molecular Weight 331.1332
State Solid
Melting Point 255 - 257 oC
Experimental Water Solubility 1.1 mg/L Source: PhysProp
Predicted Water Solubility 1.35e+00 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 2.3 Source: PhysProp
Predicted LogP -0.56 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -2.39 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point 6.09
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 OC(=O)C1=CN(C2CC2)C2=CC(N3CCNCC3)=C(F)C=C2C1=O
Canonical SMILES OC(=O)C1=CN(C2CC2)C2=CC(N3CCNCC3)=C(F)C=C2C1=O
Drug Category
  • Anti-Infective Agents
  • Anti-Infectives
  • Nucleic Acid Synthesis Inhibitors
  • Quinolones
ATC Codes
AHFS Codes
  • 08:12.18
  • 52:04.04
Indication For the treatment of the following infections caused by susceptible organisms: urinary tract infections, acute uncomplicated cystitis, chronic bacterial prostatitis, lower respiratory tract infections, acute sinusitis, skin and skin structure infections, bone and joint infections, complicated intra-abdominal infections (used in combination with metronidazole), infectious diarrhea, typhoid fever (enteric fever), uncomplicated cervical and urethral gonorrhea, and inhalational anthrax (post-exposure).
Pharmacology Ciprofloxacin is a broad-spectrum antiinfective agent of the fluoroquinolone class. Ciprofloxacin has in vitro activity against a wide range of gram-negative and gram-positive microorganisms. The mechanism of action of quinolones, including ciprofloxacin, is different from that of other antimicrobial agents such as beta-lactams, macrolides, tetracyclines, or aminoglycosides; therefore, organisms resistant to these drugs may be susceptible to ciprofloxacin. There is no known cross-resistance between ciprofloxacin and other classes of antimicrobials. Notably the drug has 100 times higher affinity for bacterial DNA gyrase than for mammalian.
Mechanism of Action The bactericidal action of ciprofloxacin results from inhibition of the enzymes topoisomerase II (DNA gyrase) and topoisomerase IV, which are required for bacterial DNA replication, transcription, repair, and recombination.
Absorption Rapidly and well absorbed from the gastrointestinal tract after oral administration. The absolute bioavailability is approximately 70% with no substantial loss by first pass metabolism.
Toxicity The major adverse effect seen with use of is gastrointestinal irritation, common with many antibiotics.
Protein Binding 20 to 40%
Biotransformation Hepatic. Four metabolites have been identified in human urine which together account for approximately 15% of an oral dose. The metabolites have antimicrobial activity, but are less active than unchanged ciprofloxacin.
Half Life 4 hours
Dosage Forms
Form Route
Ointment Ophthalmic
Solution Intravenous
Solution Ophthalmic
Suspension Oral
Tablet Oral
Tablet, extended release Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Acenocoumarol The quinolone increases the anticoagulant effect
Aluminium Formation of non-absorbable complexes
Aminophylline The quinolone increases the effect of theophylline
Anisindione The quinolone increases the anticoagulant effect
Bismuth Formation of non-absorbable complexes
Caffeine The quinolone increases the effect and toxicity of caffeine
Calcium Formation of non-absorbable complexes
Clozapine Ciprofloxacin may increase clozapine serum levels
Cyclosporine The quinolone increases the effect and toxicity of cyclosporine
Dicumarol The quinolone increases the anticoagulant effect
Dihydroxyaluminium Formation of non-absorbable complexes
Duloxetine Increases the effect/toxicity of duloxetine
Dyphylline The quinolone increases the effect of theophylline
Dyphylline The quinolone increases the effect of theophylline
Ethotoin Decreases the hydantoin effect
Foscarnet Increased risk of convulsions
Fosphenytoin Decreases the hydantoin effect
Iron Formation of non-absorbable complexes
Magnesium Formation of non-absorbable complexes
Magnesium oxide Formation of non-absorbable complexes
Mephenytoin Decreases the hydantoin effect
Methotrexate Increases methotrexate toxicity
Oxtriphylline The quinolone increases the effect of theophylline
Phenytoin Decreases the hydantoin effect
Procainamide The quinolone increases the effect of procainamide
Rasagiline Increases effect/toxicity of rasagiline
Ropinirole The quinolone increases the effect and toxicity of ropinirole
Sevelamer Sevelamer decreases ciprofloxacin bioavailability
Sildenafil The quinolone increases sildenafil levels
Sucralfate Formation of non-absorbable complexes
Theophylline The quinolone increases the effect of theophylline
Tizanidine Increases the effect/toxicity of tizanidine
Warfarin The quinolone increases the anticoagulant effect
Zinc Formation of non-absorbable complexes
Food Interactions
  • Avoid excessive quantities of coffee or tea (Caffeine).
  • Avoid milk, calcium containing dairy products, iron, magnesium, zinc, antacids, or aluminum salts 2 hours before or 6 hours after using antacids while on this medication.
  • Take with a full glass of water.
  • Take without regard to meals.
Pathways Not Available
General References
  1. Brouwers JR: Drug interactions with quinolone antibacterials. Drug Saf. 1992 Jul-Aug;7(4):268-81. [PubMed Link Image]
  2. Drusano GL, Standiford HC, Plaisance K, Forrest A, Leslie J, Caldwell J: Absolute oral bioavailability of ciprofloxacin. Antimicrob Agents Chemother. 1986 Sep;30(3):444-6. [PubMed Link Image]
  3. Hilliard JJ, Krause HM, Bernstein JI, Fernandez JA, Nguyen V, Ohemeng KA, Barrett JF: A comparison of active site binding of 4-quinolones and novel flavone gyrase inhibitors to DNA gyrase. Adv Exp Med Biol. 1995;390:59-69. [PubMed Link Image]
  4. Spivey JM, Cummings DM, Pierson NR: Failure of prostatitis treatment secondary to probable ciprofloxacin-sucralfate drug interaction. Pharmacotherapy. 1996 Mar-Apr;16(2):314-6. [PubMed Link Image]
  5. Drugs.com Link Image
  6. Wikipedia Link Image
  7. RxList Link Image
  8. PDRhealth Link Image
Organisms Affected
  • Enteric bacteria and other eubacteria
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 1A2 (CYP1A2)
Targets
  1. DNA gyrase subunit A
  2. DNA topoisomerase 4 subunit A
  3. Serum albumin
  4. DNA topoisomerase 2-alpha
  5. Acriflavine resistance protein B
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 1A2 (CYP1A2)
Enzyme 1 Gene Name CYP1A2
Enzyme 1 SwissProt ID P05177 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >P05177|CP1A2_HUMAN Cytochrome P450 1A2 - Homo sapiens (Human). 
MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKN
PHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDG
QSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELM
AGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFP
ILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGN
LIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLS
DRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPEL
WEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLE
FSVPPGVKVDLTPIYGLTMKHARCEHVQARRFSIN
Drug Target 1 [top]
Target 1 ID 404
Target 1 Name DNA gyrase subunit A
Target 1 Synonyms
  1. EC 5.99.1.3
Target 1 Gene Name gyrA
Target 1 Protein Sequence >DNA gyrase subunit A 
MTDSIQSSITPVNIEEELKSSYLDYAMSVIVGRALPDVRDGLKPVHRRVLFSMDREGNTA
NKKYVKSARVVGDVIGKYHPHGDSAVYDTIVRMAQPFSLRYMLVDGQGNFGSIDGDAPAA
MRYTEVRMQKITQALLTDLDKETVNFSPNYDGELMIPDVLPTRIPALLANGSSGIAVGMA
TNIPPHNLNEVLNGCLAYIDKNEITIDELMQHIPGPDFPTAALINGRKGIEEAYRTGRGK
VYVRARATVETNEKGREQIIVSELPYQVNKAKLVEKIAELIREKKIEGISNITDLSNKEG
IRIEIDIKRDAVGEVVLNHLYSLTQMQVTFGINMVALDHGQPRLFNLKEIIEAFVLHRRE
VVTRRSIFELRKARERTHILEGLAVARSNIDEMIAIIRNSKNREEAATSISSRSWTLHSD
IINLLDASARPDELEENLGIQGEQYYLSPAQVNAILELRLHRLTGIAFEEVIKEYEELLV
KIADLLHILSSAERLMEVIREELEEVKAQFGDDRLTEITAASGDIDLEDLIAQEDVVVTL
SHEGYVKYQPLTDYEAQRRGGKGKSATKMKEEDFIEKLLVANTHDTILCFSSRGRLYWLK
VYQLPQASRGARGRPIVNILPLQENERITAILPVSAYEEDKFVVMATAGGIVKKIALTEF
SRPRSNGIIALNLRDEDELIGVDITDGSNEIMLFSSQGRVVRFAENAVRAMGRLATGVRG
IKLALTNDISDDESAVEIEDISDDNAEASLDLNIDKVVSLVVPKGEGAILTATQNGYGKR
TQLSEYPTKSRNTKGVISIKVSERNGKVVAATQVEETDQIMLITDAGTLVRTRVSEVSIV
GRNTQGVRLIRTADDEHVVSLERVCDADEDDSLEESSSEE
Target 1 Number of Residues 894
Target 1 Molecular Weight 97820
Target 1 Theoretical pI 4.85
Target 1 GO Classification
Function
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
DNA topoisomerase (ATP-hydrolyzing) activity
DNA topoisomerase activity
DNA topoisomerase (ATP-hydrolyzing) activity
binding
nucleic acid binding
DNA binding
Process
DNA replication
DNA-dependent DNA replication
DNA unwinding during replication
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
DNA metabolism
DNA topological change
Component
organelle
non-membrane-bound organelle
intracellular non-membrane-bound organelle
chromosome
Target 1 General Function Replication, recombination and repair
Target 1 Specific Function DNA gyrase negatively supercoils closed circular double- stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings
Target 1 Pathways Not Available
Target 1 Reactions
  • ATP-dependent breakage, passage and rejoining of double-stranded DNA INHIBITOR Coumermycin A1; GRI22222X; Nalidixic acid; Novobiocin; Ciprofloxacin
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Essential
Target 1 GenBank ID Protein 1574722 Link Image
Target 1 UniProtKB/Swiss-Prot ID P43700 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name GYRA_HAEIN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Cytoplasmic
Target 1 Gene Sequence >2643 bp 
TTATTCTTCAGAACTGCTTTCTTCCAAAGAATCATCTTCATCTGCATCACAAACACGTTC
TAAACTTACTACGTGTTCATCATCGGCAGTACGAATTAAGCGAACACCTTGCGTGTTACG
CCCTACAATGCTCACTTCGCTTACGCGTGTGCGAACAAGGGTTCCTGCATCAGTGATCAA
CATAATTTGGTCTGTTTCTTCTACTTGAGTTGCGGCAACGACTTTACCATTGCGTTCACT
CACTTTAATCGAAATCACACCTTTTGTATTACGTGATTTAGTTGGGTATTCACTTAATTG
TGTGCGTTTTCCGTAGCCGTTTTGCGTTGCGGTTAAAATTGCCCCTTCACCTTTTGGCAC
AACGAGCGAGACCACTTTATCGATATTTAAGTCTAATGATGCTTCAGCGTTGTCATCAGA
AATATCTTCAATTTCTACCGCACTTTCATCGTCAGAAATATCGTTTGTTAAAGCCAGTTT
GATACCGCGAACACCTGTTGCTAAACGCCCCATCGCACGCACGGCATTTTCAGCAAAACG
CACCACGCGACCTTGTGATGAGAACAACATAATTTCGTTGCTGCCATCAGTAATATCCAC
GCCGATTAATTCATCTTCGTCACGTAAATTCAATGCGATGATACCGTTTGAACGTGGACG
GCTAAATTCGGTTAAGGCGATTTTCTTCACAATACCGCCAGCAGTTGCCATGACTACGAA
TTTATCTTCTTCGTAAGCAGAAACTGGCAAGATTGCAGTAATACGTTCGTTTTCTTGTAA
CGGAAGAATATTCACAATTGGACGACCGCGTGCGCCACGGCTCGCTTGCGGAAGTTGATA
TACTTTCAACCAATATAAACGACCACGGCTAGAGAAGCAGAGGATGGTATCGTGAGTATT
TGCTACCAGTAATTTTTCGATGAAATCTTCTTCTTTCATCTTCGTTGCAGATTTGCCTTT
ACCGCCACGGCGTTGTGCTTCATAGTCAGTCAGTGGTTGGTATTTCACATAACCTTCGTG
AGAAAGCGTCACAACCACGTCTTCTTGTGCGATTAAATCTTCTAAATCAATATCGCCAGA
AGCAGCGGTAATTTCAGTTAAACGATCATCACCAAATTGTGCTTTTACTTCTTCCAATTC
TTCACGAATTACTTCCATTAAACGTTCTGCACTACTTAAAATATGAAGAAGATCCGCAAT
TTTAACTAATAATTCTTCATATTCTTTTATAACTTCTTCAAACGCAATGCCCGTTAAACG
GTGTAAGCGAAGTTCTAGAATTGCGTTTACTTGCGCTGGCGATAAGTAATATTGTTCGCC
TTGAATACCAAGATTTTCTTCTAACTCATCAGGACGAGCAGAAGCATCAAGAAGATTAAT
AATATCGCTATGTAACGTCCAAGAGCGTGAACTGATTGATGTTGCGGCTTCTTCACGGTT
TTTAGAGTTACGAATGATCGCAATCATTTCATCGATATTAGAACGAGCAACCGCTAAACC
TTCCAAAATATGCGTACGTTCACGTGCTTTGCGAAGCTCAAAGATAGAACGACGTGTAAC
CACTTCACGGCGGTGTAAAACAAAGGCTTCAATAATTTCTTTAAGATTAAATAAACGTGG
CTGACCGTGATCCAATGCCACCATATTGATACCAAAGGTCACTTGCATTTGAGTGAGTGA
GTAAAGATGGTTTAATACCACTTCCCCCACTGCATCACGTTTAATATCAATTTCAATACG
GATCCCTTCTTTATTTGAAAGGTCAGTAATATTGCTGATACCTTCGATTTTTTTCTCGCG
AATTAATTCGGCGATTTTCTCGACTAATTTTGCTTTATTTACTTGGTATGGCAATTCAGA
CACGATAATTTGCTCGCGTCCTTTTTCGTTGGTTTCTACCGTTGCACGAGCACGAACATA
CACTTTACCACGACCAGTGCGATAGGCCTCTTCAATCCCTTTACGACCATTAATTAACGC
AGCCGTTGGGAAGTCAGGCCCTGGAATATGTTGCATTAATTCATCAATGGTAATTTCATT
TTTGTCAATATAAGCCAAACAACCATTTAATACTTCGTTTAAGTTGTGAGGGGGAATGTT
AGTTGCCATCCCCACCGCAATACCAGAAGAACCATTTGCTAACAGTGCTGGAATACGAGT
CGGCAATACATCTGGAATCATTAATTCGCCATCATAGTTTGGCGAGAAATTGACGGTTTC
TTTATCCAAATCCGTGAGCAATGCTTGCGTAATTTTTTGCATACGTACTTCGGTATAACG
CATTGCAGCTGGCGCATCACCATCAATTGAACCAAAGTTACCTTGCCCATCAACCAACAT
ATAGCGAAGTGAGAAGGGTTGTGCCATACGAACGATGGTATCGTACACGGCGGAGTCACC
ATGCGGGTGATATTTACCGATTACATCACCCACAACACGCGCTGATTTTACGTATTTTTT
ATTGGCGGTATTGCCTTCGCGATCCATTGAGAATAGTACGCGGCGGTGAACAGGTTTTAA
ACCATCTCGAACGTCAGGTAATGCACGCCCAACGATAACCGACATCGCGTAGTCAAGGTA
GGAAGATTTAAGTTCTTCTTCGATATTGACAGGGGTGATAGATGATTGGATTGAATCCGT
CAT
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. Fleischmann RD, Adams MD, White O, Clayton RA, Kirkness EF, Kerlavage AR, Bult CJ, Tomb JF, Dougherty BA, Merrick JM, et al.: Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science. 1995 Jul 28;269(5223):496-512. [PubMed Link Image]
Target 1 Drug References
  1. Chaudhry U, Ray K, Bala M, Saluja D: Mutation patterns in gyrA and parC genes of ciprofloxacin resistant isolates of Neisseria gonorrhoeae from India. Sex Transm Infect. 2002 Dec;78(6):440-4. [PubMed Link Image]
  2. 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]
  3. 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]
  4. Abdelbaqi K, Menard A, Prouzet-Mauleon V, Bringaud F, Lehours P, Megraud F: Nucleotide sequence of the gyrA gene of Arcobacter species and characterization of human ciprofloxacin-resistant clinical isolates. FEMS Immunol Med Microbiol. 2007 Apr;49(3):337-45. [PubMed Link Image]
  5. Taylor DE, Chau AS: Cloning and nucleotide sequence of the gyrA gene from Campylobacter fetus subsp. fetus ATCC 27374 and characterization of ciprofloxacin-resistant laboratory and clinical isolates. Antimicrob Agents Chemother. 1997 Mar;41(3):665-71. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 477
Target 2 Name DNA topoisomerase 4 subunit A
Target 2 Synonyms
  1. EC 5.99.1.-
  2. Topoisomerase IV subunit A
Target 2 Gene Name parC
Target 2 Protein Sequence >DNA topoisomerase 4 subunit A 
MTNINYEGIEQMPLRTFTEKAYLNYSMYVIMDRALPFIGDGLKPVQRRIVYAMSELGLNA
TAKYKKSARTVGDVLGKFHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFA
AMRYTESRLSKISEILLNELGQGTVDYQPNFDGTLAEPQYLPARLPHILLNGTTGIAVGM
ATDIPPHNINEIADAAVMLLDNPKAGLDDVLEIVQGPDFPTEAEIISPKSEIRKIYEQGR
GSIKMRATWKKEDGEIIISALPHQSSPSKVIAQIAEQMTAKKLPMLEDIRDEADHENPIR
IVLVPRSNRVDTDALMAHLFATTDLEKSYRVNMNMIGLDHKPAVKGLLEILNEWLDFRRT
TVTRRLQYRLDKVLSRLHILEGLMIAFLNIDEVIEIIRHEDDPKAELMARFNLSDEQADA
ILNLRLRHLAKLEENQLKAEQDELEKERLNLEAILGSERRLNTLIKKEIQEDAKKYANPR
MSQLVEREEAKMISESDMTPAEPVTVILSEMGWVRCAKGHDIDPKSLSYKAGDSYLAHAC
GKSNQAVVFIDSTGRSYALDPLSLPSARSQGEPLTGKLNLPTGATIEYVVMASEQQELLM
ASDAGYGFICKFEDLIARNKAGKALISLPENAKVLKPKTLINSTALVVAITSAGRMLIFP
AQDLPVLSKGKGNKMITIPAANAKDRSELLTKLLLISDQASLEFYSGKRKIVLKPEDLQK
FRAERGRKGSTLPRGLHTNLEIMVIEP
Target 2 Number of Residues 759
Target 2 Molecular Weight 83368
Target 2 Theoretical pI 6.42
Target 2 GO Classification
Function
DNA topoisomerase (ATP-hydrolyzing) activity
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
DNA topoisomerase (ATP-hydrolyzing) activity
DNA topoisomerase activity
binding
nucleic acid binding
DNA binding
Process
DNA replication
DNA-dependent DNA replication
DNA unwinding during replication
DNA topological change
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
DNA metabolism
Component
organelle
non-membrane-bound organelle
intracellular non-membrane-bound organelle
chromosome
Target 2 General Function Replication, recombination and repair
Target 2 Specific Function Topoisomerase IV is essential for chromosome segregation. It has relaxation of supercoiled DNA activity. Performs the decatenation events required during the replication of a circular DNA molecule
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 1574370 Link Image
Target 2 UniProtKB/Swiss-Prot ID P43702 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name PARC_HAEIN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Bacterial cell membrane
  • peripheral membrane protein
Target 2 Gene Sequence >2244 bp 
ATGACAAATATCAACTATGAAGGCATTGAGCAAATGCCTCTACGCACCTTCACTGAAAAG
GCTTATCTCAACTATTCTATGTATGTCATCATGGATCGTGCGTTGCCTTTTATCGGTGAT
GGTTTAAAACCCGTTCAACGTCGTATTGTATATGCGATGTCTGAACTTGGCTTAAATGCC
ACGGCAAAATACAAAAAATCTGCTCGTACCGTCGGTGATGTACTCGGTAAATTCCATCCA
CATGGTGACAGTGCTTGTTATGAAGCTATGGTGTTAATGGCACAACCCTTCTCTTATCGT
TATCCACTTGTAGATGGTCAAGGTAACTGGGGGGCACCAGATGATCCAAAATCCTTCGCA
GCCATGCGTTATACGGAATCTCGCCTATCTAAAATCTCTGAAATCTTGTTGAATGAACTC
GGACAAGGAACAGTAGATTATCAACCAAACTTTGATGGAACCTTGGCTGAACCACAATAT
TTACCTGCTCGTTTACCGCATATTTTATTGAACGGCACAACAGGTATTGCGGTGGGGATG
GCCACAGATATTCCACCACACAATATTAACGAAATTGCTGATGCGGCAGTAATGTTGCTA
GATAATCCTAAAGCGGGATTAGATGATGTACTTGAAATTGTTCAAGGCCCAGATTTTCCA
ACAGAAGCGGAAATTATTTCGCCAAAATCAGAAATTCGTAAAATTTATGAGCAAGGTCGT
GGCTCAATAAAAATGCGTGCAACTTGGAAAAAAGAAGACGGTGAAATTATTATTTCAGCG
CTTCCACATCAATCTTCGCCATCCAAAGTCATTGCACAAATAGCCGAACAAATGACGGCA
AAAAAACTGCCAATGCTAGAAGATATTCGAGATGAAGCCGATCACGAAAATCCAATTCGC
ATTGTGCTAGTTCCTCGCTCAAATCGCGTCGATACTGATGCCTTAATGGCACATTTATTT
GCGACCACAGATCTTGAAAAAAGCTACCGTGTAAATATGAATATGATCGGGCTTGATCAT
AAACCAGCGGTAAAAGGCTTATTAGAAATCTTAAATGAATGGCTTGACTTCCGTCGCACA
ACGGTCACTCGTCGCCTTCAATATCGCCTAGATAAAGTGCTCTCTCGCTTGCATATTTTA
GAAGGCTTGATGATAGCCTTTTTAAATATTGATGAAGTTATCGAAATTATACGCCACGAA
GATGATCCAAAAGCAGAGCTTATGGCACGCTTTAATTTAAGCGATGAACAAGCCGATGCC
ATTTTAAATTTACGCTTACGTCATTTAGCGAAATTAGAAGAAAACCAACTCAAAGCAGAA
CAAGATGAACTTGAAAAAGAGCGGTTAAATTTAGAAGCAATTTTAGGATCAGAACGCCGT
TTGAATACGCTTATCAAAAAAGAAATTCAAGAAGATGCGAAAAAATATGCCAATCCACGT
ATGTCTCAACTGGTCGAACGTGAAGAAGCCAAAATGATCTCTGAAAGTGATATGACACCA
GCAGAACCAGTTACTGTCATCTTATCAGAAATGGGCTGGGTACGTTGTGCAAAAGGACAC
GATATTGATCCTAAATCATTAAGCTACAAAGCTGGTGATAGCTATCTAGCTCACGCTTGT
GGCAAAAGTAATCAAGCCGTTGTATTCATTGATAGCACGGGGCGGAGTTATGCACTCGAT
CCGCTTTCCTTGCCTTCCGCTCGCTCCCAAGGCGAACCACTTACAGGTAAACTCAATTTA
CCCACTGGTGCGACCATTGAATATGTTGTAATGGCCAGCGAACAGCAAGAATTATTGATG
GCTTCTGATGCAGGATATGGTTTTATTTGTAAATTTGAAGATTTAATTGCACGTAACAAG
GCTGGAAAAGCCTTGATTTCTTTACCAGAAAATGCCAAAGTGTTGAAGCCTAAAACATTG
ATAAATTCTACCGCACTTGTTGTCGCAATCACATCAGCAGGCAGAATGTTGATTTTTCCA
GCACAGGATTTACCGGTATTATCAAAAGGTAAAGGCAATAAAATGATCACTATTCCCGCA
GCGAATGCAAAAGATCGTAGCGAACTATTGACAAAATTATTGCTTATTTCAGATCAAGCA
AGTCTTGAATTTTATTCTGGAAAACGAAAAATTGTATTAAAACCAGAAGATCTGCAAAAG
TTCCGCGCAGAACGAGGCAGAAAAGGTTCGACATTACCACGTGGATTACATACCAATCTT
GAAATTATGGTAATCGAGCCGTAA
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. Fleischmann RD, Adams MD, White O, Clayton RA, Kirkness EF, Kerlavage AR, Bult CJ, Tomb JF, Dougherty BA, Merrick JM, et al.: Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science. 1995 Jul 28;269(5223):496-512. [PubMed Link Image]
Target 2 Drug References
  1. Chaudhry U, Ray K, Bala M, Saluja D: Mutation patterns in gyrA and parC genes of ciprofloxacin resistant isolates of Neisseria gonorrhoeae from India. Sex Transm Infect. 2002 Dec;78(6):440-4. [PubMed Link Image]
  2. Lee JK, Lee YS, Park YK, Kim BS: Mutations in the gyrA and parC genes in ciprofloxacin-resistant clinical isolates of Acinetobacter baumannii in Korea. Microbiol Immunol. 2005;49(7):647-53. [PubMed Link Image]
  3. Leavis HL, Willems RJ, Top J, Bonten MJ: High-level ciprofloxacin resistance from point mutations in gyrA and parC confined to global hospital-adapted clonal lineage CC17 of Enterococcus faecium. J Clin Microbiol. 2006 Mar;44(3):1059-64. [PubMed Link Image]
  4. 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]
  5. 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 587
Target 3 Name Serum albumin
Target 3 Synonyms
  1. Serum albumin precursor
Target 3 Gene Name ALB
Target 3 Protein Sequence >Serum albumin precursor 
MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPF
EDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEP
ERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLF
FAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAV
ARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLK
ECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYAR
RHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFE
QLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVV
LNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTL
SEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLV
AASQAALGL
Target 3 Number of Residues 619
Target 3 Molecular Weight 69367
Target 3 Theoretical pI 6.21
Target 3 GO Classification
Function
transporter activity
carrier activity
Process
physiological process
cellular physiological process
transport
Component
extracellular region
extracellular space
Target 3 General Function Involved in antioxidant activity
Target 3 Specific Function Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
Target 3 Signals
  • 1-18
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 28590 Link Image
Target 3 UniProtKB/Swiss-Prot ID P02768 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name ALBU_HUMAN Link Image
Target 3 PDB ID 1HA2 Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location
  • Secreted protein
Target 3 Gene Sequence >1830 bp 
ATGAAGTGGGTAACCTTTATTTCCCTTCTTTTTCTCTTTAGCTCGGCTTATTCCAGGGGT
GTGTTTCGTCGAGATGCACACAAGAGTGAGGTTGCTCATCGGTTTAAAGATTTGGGAGAA
GAAAATTTCAAAGCCTTGGTGTTGATTGCCTTTGCTCAGTATCTTCAGCAGTGTCCATTT
GAAGATCATGTAAAATTAGTGAATGAAGTAACTGAATTTGCAAAAACATGTGTTGCTGAT
GAGTCAGCTGAAAATTGTGACAAATCACTTCATACCCTTTTTGGAGACAAATTATGCACA
GTTGCAACTCTTCGTGAAACCTATGGTGAAATGGCTGACTGCTGTGCAAAACAAGAACCT
GGGAGAAATGAATGCTTCTTGCAACACAAAGATGACAACCCAAACCTCCCCCGATTGGTG
AGACCAGAGGTTGATGTGATGTGCACTGCTTTTCATGACAATGAAGAGACATTTTTGAAA
AAATACTTATATGAAATTGCCAGAAGACATCCTTACTTTTATGCCCCGGAACTCCTTTTC
TTTGCTAAAAGGTATAAAGCTGCTTTTACAGAATGTTGCCAAGCTGCTGATAAAGCTGCC
TGCCTGTTGCCAAAGCTCGATGAACTTCGGGATGAAGGGAAGGCTTCGTCTGCCAAACAG
AGACTCAAGTGTGCCAGTCTCCAAAAATTTGGAGAAAGAGCTTTCAAAGCATGGGCAGTA
GCTCGCCTGAGCCAGAGATTTCCCAAAGCTGAGTTTGCAGAAGTTTCCAAGTTAGTGACA
GATCTTACCAAAGTCCACACGGAATGCTGCCATGGAGATCTGCTTGAATGTGCTGATGAC
AGGGCGGACCTTGCCAAGTATATCTGTGAAAATCAAGATTCGATCTCCAGTAAACTGAAG
GAATGCTGTGAAAAACCTCTGTTGGAAAAATCCCACTGCATTGCCGAAGTGGAAAATGAT
GAGATGCCTGCTGACTTGCCTTCATTAGCTGCTGATTTTGTTGAAAGTAAGGATGTTTGC
AAAAACTATGCTGAGGCAAAGGATGTCTTCTTGGGCATGTTTTTGTATGAATATGCAAGA
AGGCATCCTGATTACTCTGTCGTGCTGCTGCTGAGACTTGCCAAGACATATGAAACCACT
CTAGAGAAGTGCTGTGCCGCTGCAGATCCTCATGAATGCTATGCCAAAGTGTTCGATGAA
TTTAAACCTCTTGTGGAAGAGCCTCAGAATTTAATCAAACAAAATTGTGAGCTTTTTGAG
CAGCTTGGAGAGTACAAATTCCAGAATGCGCTGTTAGTTCGTTACACCAAGAAAGTACCC
GAAGTGTCAACTCCAACTCTTGTAGAGGTCTCAAGAAACCTAGGAAAAGTGGGCAGCAAA
TGTTGTAAACATCCTGAAGCAAAAAGAATGCCCTGTGCAGAAGACTATCTATCCGTGGTC
CTGAACCAGTTATGTGTGTTGCATGAGAAAACGCCAGTAAGTGACAGAGTCACCAAATGC
TGCACAGAATCCTTGGTGAACAGGCGACCATGCTTTTCAGCTCTGGAAGTCGATGAAACA
TACGTTCCCAAAGAGTTTAATGCTGAAACATTCACCTTCCATGCAGATATATGCACACTT
TCTGAGAAGGAGAGACAAATCAAGAAACAAACTGCACTTGTTGAGCTCGTGAAACACAAG
CCCAAGGCAACAAAAGAGCAACTGAAAGCTGTTATGGATGATTTCGCTGCTTTTGTAGAG
AAGTGCTGCAAGGCTGACGATAAGGAGACCTGCTTTGCCGAGGAGGGTAAAAAACTTGTT
GCTGCAAGTCAAGCTGCCTTAGGCTTATAA
Target 3 GenBank Gene ID
Target 3 GeneCard ID ALB Link Image
Target 3 GenAtlas ID ALB Link Image
Target 3 HGNC ID HGNC:399 Link Image
Target 3 Chromosome Location 4
Target 3 Locus 4q11-q13
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K: Crystal structure of human serum albumin at 2.5 A resolution. Protein Eng. 1999 Jun;12(6):439-46. [PubMed Link Image]
  2. Bhattacharya AA, Curry S, Franks NP: Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures. J Biol Chem. 2000 Dec 8;275(49):38731-8. [PubMed Link Image]
  3. Minchiotti L, Campagnoli M, Rossi A, Cosulich ME, Monti M, Pucci P, Kragh-Hansen U, Granel B, Disdier P, Weiller PJ, Galliano M: A nucleotide insertion and frameshift cause albumin Kenitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges. Eur J Biochem. 2001 Jan;268(2):344-52. [PubMed Link Image]
  4. Yu Y, Zhang C, Zhou G, Wu S, Qu X, Wei H, Xing G, Dong C, Zhai Y, Wan J, Ouyang S, Li L, Zhang S, Zhou K, Zhang Y, Wu C, He F: Gene expression profiling in human fetal liver and identification of tissue- and developmental-stage-specific genes through compiled expression profiles and efficient cloning of full-length cDNAs. Genome Res. 2001 Aug;11(8):1392-403. [PubMed Link Image]
  5. Spahr CS, Davis MT, McGinley MD, Robinson JH, Bures EJ, Beierle J, Mort J, Courchesne PL, Chen K, Wahl RC, Yu W, Luethy R, Patterson SD: Towards defining the urinary proteome using liquid chromatography-tandem mass spectrometry. I. Profiling an unfractionated tryptic digest. Proteomics. 2001 Jan;1(1):93-107. [PubMed Link Image]
  6. Petitpas I, Grune T, Bhattacharya AA, Curry S: Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids. J Mol Biol. 2001 Dec 14;314(5):955-60. [PubMed Link Image]
  7. Meloun B, Moravek L, Kostka V: Complete amino acid sequence of human serum albumin. FEBS Lett. 1975 Oct 15;58(1):134-7. [PubMed Link Image]
  8. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  9. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  10. Minchiotti L, Galliano M, Stoppini M, Ferri G, Crespeau H, Rochu D, Porta F: Two alloalbumins with identical electrophoretic mobility are produced by differently charged amino acid substitutions. Biochim Biophys Acta. 1992 Mar 12;1119(3):232-8. [PubMed Link Image]
  11. 1518850 Carlson J, Sakamoto Y, Laurell CB, Madison J, Watkins S, Putnam FW: Alloalbuminemia in Sweden: structural study and phenotypic distribution of nine albumin variants. Proc Natl Acad Sci U S A. 1992 Sep 1;89(17):8225-9.
  12. 1630489 He XM, Carter DC: Atomic structure and chemistry of human serum albumin. Nature. 1992 Jul 16;358(6383):209-15.
  13. 1859851 Peach RJ, Brennan SO: Structural characterization of a glycoprotein variant of human serum albumin: albumin Casebrook (494 Asp----Asn). Biochim Biophys Acta. 1991 Jul 26;1097(1):49-54.
  14. 1946412 Madison J, Arai K, Sakamoto Y, Feld RD, Kyle RA, Watkins S, Davis E, Matsuda Y, Amaki I, Putnam FW: Genetic variants of serum albumin in Americans and Japanese. Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9853-7.
  15. 2068071 Watkins S, Madison J, Davis E, Sakamoto Y, Galliano M, Minchiotti L, Putnam FW: A donor splice mutation and a single-base deletion produce two carboxyl-terminal variants of human serum albumin. Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):5959-63.
  16. 2104980 Brennan SO, Myles T, Peach RJ, Donaldson D, George PM: Albumin Redhill (-1 Arg, 320 Ala----Thr): a glycoprotein variant of human serum albumin whose precursor has an aberrant signal peptidase cleavage site. Proc Natl Acad Sci U S A. 1990 Jan;87(1):26-30.
  17. 2247440 Galliano M, Minchiotti L, Porta F, Rossi A, Ferri G, Madison J, Watkins S, Putnam FW: Mutations in genetic variants of human serum albumin found in Italy. Proc Natl Acad Sci U S A. 1990 Nov;87(22):8721-5.
  18. 2374930 Carter DC, He XM: Structure of human serum albumin. Science. 1990 Jul 20;249(4966):302-3.
  19. 2404284 Arai K, Madison J, Shimizu A, Putnam FW: Point substitutions in albumin genetic variants from Asia. Proc Natl Acad Sci U S A. 1990 Jan;87(1):497-501.
  20. 2419329 Urano Y, Watanabe K, Sakai M, Tamaoki T: The human albumin gene. Characterization of the 5' and 3' flanking regions and the polymorphic gene transcripts. J Biol Chem. 1986 Mar 5;261(7):3244-51.
  21. 2437111 Carraway RE, Mitra SP, Cochrane DE: Structure of a biologically active neurotensin-related peptide obtained from pepsin-treated albumin(s). J Biol Chem. 1987 May 5;262(13):5968-73.
  22. 2727704 Carter DC, He XM, Munson SH, Twigg PD, Gernert KM, Broom MB, Miller TY: Three-dimensional structure of human serum albumin. Science. 1989 Jun 9;244(4909):1195-8.
  23. 2762316 Arai K, Madison J, Huss K, Ishioka N, Satoh C, Fujita M, Neel JV, Sakurabayashi I, Putnam FW: Point substitutions in Japanese alloalbumins. Proc Natl Acad Sci U S A. 1989 Aug;86(16):6092-6.
  24. 2911589 Arai K, Ishioka N, Huss K, Madison J, Putnam FW: Identical structural changes in inherited albumin variants from different populations. Proc Natl Acad Sci U S A. 1989 Jan;86(2):434-8.
  25. 3009475 Minghetti PP, Ruffner DE, Kuang WJ, Dennison OE, Hawkins JW, Beattie WG, Dugaiczyk A: Molecular structure of the human albumin gene is revealed by nucleotide sequence within q11-22 of chromosome 4. J Biol Chem. 1986 May 25;261(15):6747-57.
  26. 3087352 Mogard MH, Kobayashi R, Chen CF, Lee TD, Reeve JR Jr, Shively JE, Walsh JH: The amino acid sequence of kinetensin, a novel peptide isolated from pepsin-treated human plasma: homology with human serum albumin, neurotensin and angiotensin. Biochem Biophys Res Commun. 1986 May 14;136(3):983-8.
  27. 3474609 Takahashi N, Takahashi Y, Blumberg BS, Putnam FW: Amino acid substitutions in genetic variants of human serum albumin and in sequences inferred from molecular cloning. Proc Natl Acad Sci U S A. 1987 Jul;84(13):4413-7.
  28. 3479777 Takahashi N, Takahashi Y, Isobe T, Putnam FW, Fujita M, Satoh C, Neel JV: Amino acid substitutions in inherited albumin variants from Amerindian and Japanese populations. Proc Natl Acad Sci U S A. 1987 Nov;84(22):8001-5.
  29. 3828358 Brennan SO, Herbert P: Albumin Canterbury (313 Lys----Asn). A point mutation in the second domain of serum albumin. Biochim Biophys Acta. 1987 Apr 8;912(2):191-7.
  30. 6171778 Lawn RM, Adelman J, Bock SC, Franke AE, Houck CM, Najarian RC, Seeburg PH, Wion KL: The sequence of human serum albumin cDNA and its expression in E. coli. Nucleic Acids Res. 1981 Nov 25;9(22):6103-114.
  31. 6275391 Dugaiczyk A, Law SW, Dennison OE: Nucleotide sequence and the encoded amino acids of human serum albumin mRNA. Proc Natl Acad Sci U S A. 1982 Jan;79(1):71-5.
  32. 656055 Jacobsen C: Lysine residue 240 of human serum albumin is involved in high-affinity binding of bilirubin. Biochem J. 1978 May 1;171(2):453-9.
  33. 7852505 Rushbrook JI, Becker E, Schussler GC, Divino CM: Identification of a human serum albumin species associated with familial dysalbuminemic hyperthyroxinemia. J Clin Endocrinol Metab. 1995 Feb;80(2):461-7.
  34. 7895732 Corbett JM, Wheeler CH, Baker CS, Yacoub MH, Dunn MJ: The human myocardial two-dimensional gel protein database: update 1994. Electrophoresis. 1994 Nov;15(11):1459-65.
  35. 7902134 Galliano M, Minchiotti L, Iadarola P, Stoppini M, Giagnoni P, Watkins S, Madison J, Putnam FW: Protein and DNA sequence analysis of a 'private' genetic variant: albumin Ortonovo (Glu-505-->Lys). Biochim Biophys Acta. 1993 Nov 25;1225(1):27-32.
  36. 8022807 Madison J, Galliano M, Watkins S, Minchiotti L, Porta F, Rossi A, Putnam FW: Genetic variants of human serum albumin in Italy: point mutants and a carboxyl-terminal variant. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6476-80.
  37. 8048949 Sunthornthepvarakul T, Angkeow P, Weiss RE, Hayashi Y, Refetoff S: An identical missense mutation in the albumin gene results in familial dysalbuminemic hyperthyroxinemia in 8 unrelated families. Biochem Biophys Res Commun. 1994 Jul 29;202(2):781-7.
  38. 8347685 Brennan SO, Fellowes AP: Albumin Hawkes Bay; a low level variant caused by loss of a sulphydryl group at position 177. Biochim Biophys Acta. 1993 Aug 4;1182(1):46-50.
  39. 8513793 Minchiotti L, Galliano M, Zapponi MC, Tenni R: The structural characterization and bilirubin-binding properties of albumin Herborn, a [Lys240-->Glu] albumin mutant. Eur J Biochem. 1993 Jun 1;214(2):437-44.
  40. 9329347 Wada N, Chiba H, Shimizu C, Kijima H, Kubo M, Koike T: A novel missense mutation in codon 218 of the albumin gene in a distinct phenotype of familial dysalbuminemic hyperthyroxinemia in a Japanese kindred. J Clin Endocrinol Metab. 1997 Oct;82(10):3246-50.
  41. 955075 Walker JE: Lysine residue 199 of human serum albumin is modified by acetylsalicyclic acid. FEBS Lett. 1976 Jul 15;66(2):173-5.
  42. 9589637 Sunthornthepvarakul T, Likitmaskul S, Ngowngarmratana S, Angsusingha K, Kitvitayasak S, Scherberg NH, Refetoff S: Familial dysalbuminemic hypertriiodothyroninemia: a new, dominantly inherited albumin defect. J Clin Endocrinol Metab. 1998 May;83(5):1448-54.
  43. 9731778 Curry S, Mandelkow H, Brick P, Franks N: Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat Struct Biol. 1998 Sep;5(9):827-35.
Target 3 Drug References
  1. Fick AC, Reinscheid UM: Characterization of the binding epitope of ciprofloxacin bound to human serum albumin. J Pharm Biomed Anal. 2006 Jun 7;41(3):1025-8. Epub 2006 Feb 21. [PubMed Link Image]
  2. Ahmad B, Parveen S, Khan RH: Effect of albumin conformation on the binding of ciprofloxacin to human serum albumin: a novel approach directly assigning binding site. Biomacromolecules. 2006 Apr;7(4):1350-6. [PubMed Link Image]
  3. Kumar PV, Jain NK: Suppression of agglomeration of ciprofloxacin-loaded human serum albumin nanoparticles. AAPS PharmSciTech. 2007 Mar 2;8(1):17. [PubMed Link Image]
  4. Wang Z, Zhu Y, Ding S, He F, Beier RC, Li J, Jiang H, Feng C, Wan Y, Zhang S, Kai Z, Yang X, Shen J: Development of a monoclonal antibody-based broad-specificity ELISA for fluoroquinolone antibiotics in foods and molecular modeling studies of cross-reactive compounds. Anal Chem. 2007 Jun 15;79(12):4471-83. Epub 2007 May 19. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 817
Target 4 Name DNA topoisomerase 2-alpha
Target 4 Synonyms
  1. DNA topoisomerase II, alpha isozyme
  2. EC 5.99.1.3
Target 4 Gene Name TOP2A
Target 4 Protein Sequence >DNA topoisomerase 2-alpha 
MEVSPLQPVNENMQVNKIKKNEDAKKRLSVERIYQKKTQLEHILLRPDTYIGSVELVTQQ
MWVYDEDVGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCIRVTIDPENNLISIWN
NGKGIPVVEHKVEKMYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVE
TASREYKKMFKQTWMDNMGRAGEMELKPFNGEDYTCITFQPDLSKFKMQSLDKDIVALMV
RRAYDIAGSTKDVKVFLNGNKLPVKGFRSYVDMYLKDKLDETGNSLKVIHEQVNHRWEVC
LTMSEKGFQQISFVNSIATSKGGRHVDYVADQIVTKLVDVVKKKNKGGVAVKAHQVKNHM
WIFVNALIENPTFDSQTKENMTLQPKSFGSTCQLSEKFIKAAIGCGIVESILNWVKFKAQ
VQLNKKCSAVKHNRIKGIPKLDDANDAGGRNSTECTLILTEGDSAKTLAVSGLGVVGRDK
YGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKNYEDEDSLKTLRYGKIMIMT
DQDQDGSHIKGLLINFIHHNWPSLLRHRFLEEFITPIVKVSKNKQEMAFYSLPEFEEWKS
STPNHKKWKVKYYKGLGTSTSKEAKEYFADMKRHRIQFKYSGPEDDAAISLAFSKKQIDD
RKEWLTNFMEDRRQRKLLGLPEDYLYGQTTTYLTYNDFINKELILFSNSDNERSIPSMVD
GLKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSSYHHGEMSLMMTIINLAQNFVGSNN
LNLLQPIGQFGTRLHGGKDSASPRYIFTMLSSLARLLFPPKDDHTLKFLYDDNQRVEPEW
YIPIIPMVLINGAEGIGTGWSCKIPNFDVREIVNNIRRLMDGEEPLPMLPSYKNFKGTIE
ELAPNQYVISGEVAILNSTTIEISELPVRTWTQTYKEQVLEPMLNGTEKTPPLITDYREY
HTDTTVKFVVKMTEEKLAEAERVGLHKVFKLQTSLTCNSMVLFDHVGCLKKYDTVLDILR
DFFELRLKYYGLRKEWLLGMLGAESAKLNNQARFILEKIDGKIIIENKPKKELIKVLIQR
GYDSDPVKAWKEAQQKVPDEEENEESDNEKETEKSDSVTDSGPTFNYLLDMPLWYLTKEK
KDELCRLRNEKEQELDTLKRKSPSDLWKEDLATFIEELEAVEAKEKQDEQVGLPGKGGKA
KGKKTQMAEVLPSPRGQRVIPRITIEMKAEAEKKNKKKIKNENTEGSPQEDGVELEGLKQ
RLEKKQKREPGTKTKKQTTLAFKPIKKGKKRNPWSDSESDRSSDESNFDVPPRETEPRRA
ATKTKFTMDLDSDEDFSDFDEKTDDEDFVPSDASPPKTKTSPKLSNKELKPQKSVVSDLE
ADDVKGSVPLSSSPPATHFPDETEITNPVPKKNVTVKKTAAKSQSSTSTTGAKKRAAPKG
TKRDPALNSGVSQKPDPAKTKNRRKRKPSTSDDSDSNFEKIVSKAVTSKKSKGESDDFHM
DFDSAVAPRAKSVRAKKPIKYLEESDEDDLF
Target 4 Number of Residues 1556
Target 4 Molecular Weight 174387
Target 4 Theoretical pI 9.17
Target 4 GO Classification
Function
DNA topoisomerase (ATP-hydrolyzing) activity
DNA topoisomerase activity
DNA topoisomerase (ATP-hydrolyzing) activity
nucleic acid binding
DNA binding
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
Process
DNA topological change
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
DNA metabolism
Component
Not Available
Target 4 General Function Replication, recombination and repair
Target 4 Specific Function Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks
Target 4 Pathways Not Available
Target 4 Reactions
  • ATP-dependent breakage, passage and rejoining of double-stranded DNA INHIBITOR Coumermycin A1; GRI22222X; Nalidixic acid; Novobiocin; Ciprofloxacin
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 292830 Link Image
Target 4 UniProtKB/Swiss-Prot ID P11388 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name TOP2A_HUMAN Link Image
Target 4 PDB ID Not Available
Target 4 Cellular Location
  • Cytoplasm. Nucleus
  • nucleoplasm. Generally located in the nucleoplasm
Target 4 Gene Sequence >4596 bp 
ATGGAAGTGTCACCATTGCAGCCTGTAAATGAAAATATGCAAGTCAACAAAATAAAGAAA
AATGAAGATGCTAAGAAAAGACTGTCTGTTGAAAGAATCTATCAAAAGAAAACACAATTG
GAACATATTTTGCTCCGCCCAGACACCTACATTGGTTCTGTGGAATTAGTGACCCAGCAA
ATGTGGGTTTACGATGAAGATGTTGGCATTAACTATAGGGAAGTCACTTTTGTTCCTGGT
TTGTACAAAATCTTTGATGAGATTCTAGTTAATGCTGCGGACAACAAACAAAGGGACCCA
AAAATGTCTTGTATTAGAGTCACAATTGATCCGGAAAACAATTTAATTAGTATATGGAAT
AATGGAAAAGGTATTCCTGTTGTTGAACACAAAGTTGAAAAGATGTATGTCCCAGCTCTC
ATATTTGGACAGCTCCTAACTTCTAGTAACTATGATGATGATGAAAAGAAAGTGACAGGT
GGTCGAAATGGCTATGGAGCCAAATTGTGTAACATATTCAGTACCAAATTTACTGTGGAA
ACAGCCAGTAGAGAATACAAGAAAATGTTCAAACAGACATGGATGGATAATATGGGAAGA
GCTGGTGAGATGGAACTCAAGCCCTTCAATGGAGAAGATTATACATGTATCACCTTTCAG
CCTGATTTGTCTAAGTTTAAAATGCAAAGCCTGGACAAAGATATTGTTGCACTAATGGTC
AGAAGAGCATATGATATTGCTGGATCCACCAAAGATGTCAAAGTCTTTCTTAATGGAAAT
AAACTGCCAGTAAAAGGATTTCGTAGTTATGTGGACATGTATTTGAAGGACAAGTTGGAT
GAAACTGGTAACTCCTTGAAAGTAATACATGAACAAGTAAACCACAGGTGGGAAGTGTGT
TTAACTATGAGTGAAAAAGGCTTTCAGCAAATTAGCTTTGTCAACAGCATTGCTACATCC
AAGGGTGGCAGACATGTTGATTATGTAGCTGATCAGATTGTGACTAAACTTGTTGATGTT
GTGAAGAAGAAGAACAAGGGTGGTGTTGCAGTAAAAGCACATCAGGTGAAAAATCACATG
TGGATTTTTGTAAATGCCTTAATTGAAAACCCAACCTTTGACTCTCAGACAAAAGAAAAC
ATGACTTTACAACCCAAGAGCTTTGGATCAACATGCCAATTGAGTGAAAAATTTATCAAA
GCTGCCATTGGCTGTGGTATTGTAGAAAGCATACTAAACTGGGTGAAGTTTAAGGCCCAA
GTCCAGTTAAACAAGAAGTGTTCAGCTGTAAAACATAATAGAATCAAGGGAATTCCCAAA
CTCGATGATGCCAATGATGCAGGGGGCCGAAACTCCACTGAGTGTACGCTTATCCTGACT
GAGGGAGATTCAGCCAAAACTTTGGCTGTTTCAGGCCTTGGTGTGGTTGGGAGAGACAAA
TATGGGGTTTTCCCTCTTAGAGGAAAAATACTCAATGTTCGAGAAGCTTCTCATAAGCAG
ATCATGGAAAATGCTGAGATTAACAATATCATCAAGATTGTGGGTCTTCAGTACAAGAAA
AACTATGAAGATGAAGATTCATTGAAGACGCTTCGTTATGGGAAGATAATGATTATGACA
GATCAGGACCAAGATGGTTCCCACATCAAAGGCTTGCTGATTAATTTTATCCATCACAAC
TGGCCCTCTCTTCTGCGACATCGTTTTCTGGAGGAATTTATCACTCCCATTGTAAAGGTA
TCTAAAAACAAGCAAGAAATGGCATTTTACAGCCTTCCTGAATTTGAAGAGTGGAAGAGT
TCTACTCCAAATCATAAAAAATGGAAAGTCAAATATTACAAAGGTTTGGGCACCAGCACA
TCAAAGGAAGCTAAAGAATACTTTGCAGATATGAAAAGACATCGTATCCAGTTCAAATAT
TCTGGTCCTGAAGATGATGCTGCTATCAGCCTGGCCTTTAGCAAAAAACAGATAGATGAT
CGAAAGGAATGGTTAACTAATTTCATGGAGGATAGAAGACAACGAAAGTTACTTGGGCTT
CCTGAGGATTACTTGTATGGACAAACTACCACATATCTGACATATAATGACTTCATCAAC
AAGGAACTTATCTTGTTCTCAAATTCTGATAACGAGAGATCTATCCCTTCTATGGTGGAT
GGTTTGAAACCAGGTCAGAGAAAGGTTTTGTTTACTTGCTTCAAACGGAATGACAAGCGA
GAAGTAAAGGTTGCCCAATTAGCTGGATCAGTGGCTGAAATGTCTTCTTATCATCATGGT
GAGATGTCACTAATGATGACCATTATCAATTTGGCTCAGAATTTTGTGGGTAGCAATAAT
CTAAACCTCTTGCAGCCCATTGGTCAGTTTGGTACCAGGCTACATGGTGGCAAGGATTCT
GCTAGTCCACGATACATCTTTACAATGCTCAGCTCTTTGGCTCGATTGTTATTTCCACCA
AAAGATGATCACACGTTGAAGTTTTTATATGATGACAACCAGCGTGTTGAGCCTGAATGG
TACATTCCTATTATTCCCATGGTGCTGATAAATGGTGCTGAAGGAATCGGTACTGGGTGG
TCCTGCAAAATCCCCAACTTTGATGTGCGTGAAATTGTAAATAACATCAGGCGTTTGATG
GATGGAGAAGAACCTTTGCCAATGCTTCCAAGTTACAAGAACTTCAAGGGTACTATTGAA
GAACTGGCTCCAAATCAATATGTGATTAGTGGTGAAGTAGCTATTCTTAATTCTACAACC
ATTGAAATCTCAGAGCTTCCCGTCAGAACATGGACCCAGACATACAAAGAACAAGTTCTA
GAACCCATGTTGAATGGCACCGAGAAGACACCTCCTCTCATAACAGACTATAGGGAATAC
CATACAGATACCACTGTGAAATTTGTTGTGAAGATGACTGAAGAAAAACTGGCAGAGGCA
GAGAGAGTTGGACTACACAAAGTCTTCAAACTCCAAACTAGTCTCACATGCAACTCTATG
GTGCTTTTTGACCACGTAGGCTGTTTAAAGAAATATGACACGGTGTTGGATATTCTAAGA
GACTTTTTTGAACTCAGACTTAAATATTATGGATTAAGAAAAGAATGGCTCCTAGGAATG
CTTGGTGCTGAATCTGCTAAACTGAATAATCAGGCTCGCTTTATCTTAGAGAAAATAGAT
GGCAAAATAATCATTGAAAATAAGCCTAAGAAAGAATTAATTAAAGTTCTGATTCAGAGG
GGATATGATTCGGATCCTGTGAAGGCCTGGAAAGAAGCCCAGCAAAAGGTTCCAGATGAA
GAAGAAAATGAAGAGAGTGACAACGAAAAGGAAACTGAAAAGAGTGACTCCGTAACAGAT
TCTGGACCAACCTTCAACTATCTTCTTGATATGCCCCTTTGGTATTTAACCAAGGAAAAG
AAAGATGAACTCTGCAGGCTAAGAAATGAAAAAGAACAAGAGCTGGACACATTAAAAAGA
AAGAGTCCATCAGATTTGTGGAAAGAAGACTTGGCTACATTTATTGAAGAATTGGAGGCT
GTTGAAGCCAAGGAAAAACAAGATGAACAAGTCGGACTTCCTGGGAAAGGGGGGAAGGCC
AAGGGGAAAAAAACACAAATGGCTGAAGTTTTGCCTTCTCCGCGTGGTCAAAGAGTCATT
CCACGAATAACCATAGAAATGAAAGCAGAGGCAGAAAAGAAAAATAAAAAGAAAATTAAG
AATGAAAATACTGAAGGAAGCCCTCAAGAAGATGGTGTGGAACTAGAAGGCCTAAAACAA
AGATTAGAAAAGAAACAGAAAAGAGAACCAGGTACAAAGACAAAGAAACAAACTACATTG
GCATTTAAGCCAATCAAAAAAGGAAAGAAGAGAAATCCCTGGCCTGATTCAGAATCAGAT
AGGAGCAGTGACGAAAGTAATTTTGATGTCCCTCCACGAGAAACAGAGCCACGGAGAGCA
GCAACAAAAACAAAATTCACAATGGATTTGGATTCAGATGAAGATTTCTCAGATTTTGAT
GAAAAAACTGATGATGAAGATTTTGTCCCATCAGATGCTAGTCCACCTAAGACCAAAACT
TCCCCAAAACTTAGTAACAAAGAACTGAAACCACAGAAAAGTGTCGTGTCAGACCTTGAA
GCTGATGATGTTAAGGGCAGTGTACCACTGTCTTCAAGCCCTCCTGCTACACATTTCCCA
GATGAAACTGAAATTACAAACCCAGTTCCTAAAAAGAATGTGACAGTGAAGAAGACAGCA
GCAAAAAGTCAGTCTTCCACCTCCACTACCGGTGCCAAAAAAAGGGCTGCCCCAAAAGGA
ACTAAAAGGGATCCAGCTTTGAATTCTGGTGTCTCTCAAAAGCCTGATCCTGCCAAAACC
AAGAATCGCCGCAAAAGGAAGCCATCCACTTCTGATGATTCTGACTCTAATTTTGAGAAA
ATTGTTTCGAAAGCAGTCACAAGCAAGAAATCCAAGGGGGAGAGTGATGACTTCCATATG
GACTTTGACTCAGCTGTGGCTCCTCGGGCAAAATCTGTACGGGCAAAGAAACCTATAAAG
TACCTGGAAGAGTCAGATGAAGATGATCTGTTTTAA
Target 4 GenBank Gene ID
Target 4 GeneCard ID TOP2A Link Image
Target 4 GenAtlas ID TOP2A Link Image
Target 4 HGNC ID HGNC:11989 Link Image
Target 4 Chromosome Location 17
Target 4 Locus 17q21-q22
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Sng JH, Heaton VJ, Bell M, Maini P, Austin CA, Fisher LM: Molecular cloning and characterization of the human topoisomerase IIalpha and IIbeta genes: evidence for isoform evolution through gene duplication. Biochim Biophys Acta. 1999 Mar 19;1444(3):395-406. [PubMed Link Image]
  2. Escargueil AE, Plisov SY, Filhol O, Cochet C, Larsen AK: Mitotic phosphorylation of DNA topoisomerase II alpha by protein kinase CK2 creates the MPM-2 phosphoepitope on Ser-1469. J Biol Chem. 2000 Nov 3;275(44):34710-8. [PubMed Link Image]
  3. Mirski SE, Bielawski JC, Cole SP: Identification of functional nuclear export sequences in human topoisomerase IIalpha and beta. Biochem Biophys Res Commun. 2003 Jul 11;306(4):905-11. [PubMed Link Image]
  4. Hinds M, Deisseroth K, Mayes J, Altschuler E, Jansen R, Ledley FD, Zwelling LA: Identification of a point mutation in the topoisomerase II gene from a human leukemia cell line containing an amsacrine-resistant form of topoisomerase II. Cancer Res. 1991 Sep 1;51(17):4729-31. [PubMed Link Image]
  5. Bugg BY, Danks MK, Beck WT, Suttle DP: Expression of a mutant DNA topoisomerase II in CCRF-CEM human leukemic cells selected for resistance to teniposide. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7654-8. [PubMed Link Image]
  6. Tsai-Pflugfelder M, Liu LF, Liu AA, Tewey KM, Whang-Peng J, Knutsen T, Huebner K, Croce CM, Wang JC: Cloning and sequencing of cDNA encoding human DNA topoisomerase II and localization of the gene to chromosome region 17q21-22. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7177-81. [PubMed Link Image]
  7. Wasserman RA, Austin CA, Fisher LM, Wang JC: Use of yeast in the study of anticancer drugs targeting DNA topoisomerases: expression of a functional recombinant human DNA topoisomerase II alpha in yeast. Cancer Res. 1993 Aug 1;53(15):3591-6. [PubMed Link Image]
  8. Lang AJ, Mirski SE, Cummings HJ, Yu Q, Gerlach JH, Cole SP: Structural organization of the human TOP2A and TOP2B genes. Gene. 1998 Oct 23;221(2):255-66. [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]
Drug Target 5 [top]
Target 5 ID 3307
Target 5 Name Acriflavine resistance protein B
Target 5 Synonyms Not Available
Target 5 Gene Name acrB
Target 5 Protein Sequence >Acriflavine resistance protein B 
MPNFFIDRPIFAWVIAIIIMLAGGLAILKLPVAQYPTIAPPAVTISASYPGADAKTVQDT
VTQVIEQNMNGIDNLMYMSSNSDSTGTVQITLTFESGTDADIAQVQVQNKLQLAMPLLPQ
EVQQQGVSVEKSSSSFLMVVGVINTDGTMTQEDISDYVAANMKDAISRTSGVGDVQLFGS
QYAMRIWMNPNELNKFQLTPVDVITAIKAQNAQVAAGQLGGTPPVKGQQLNASIIAQTRL
TSTEEFGKILLKVNQDGSRVLLRDVAKIELGGENYDIIAEFNGQPASGLGIKLATGANAL
DTAAAIRAELAKMEPFFPSGLKIVYPYDTTPFVKISIHEVVKTLVEAIILVFLVMYLFLQ
NFRATLIPTIAVPVVLLGTFAVLAAFGFSINTLTMFGMVLAIGLLVDDAIVVVENVERVM
AEEGLPPKEATRKSMGQIQGALVGIAMVLSAVFVPMAFFGGSTGAIYRQFSITIVSAMAL
SVLVALILTPALCATMLKPIAKGDHGEGKKGFFGWFNRMFEKSTHHYTDSVGGILRSTGR
YLVLYLIIVVGMAYLFVRLPSSFLPDEDQGVFMTMVQLPAGATQERTQKVLNEVTHYYLT
KEKNNVESVFAVNGFGFAGRGQNTGIAFVSLKDWADRPGEENKVEAITMRATRAFSQIKD
AMVFAFNLPAIVELGTATGFDFELIDQAGLGHEKLTQARNQLLAEAAKHPDMLTSVRPNG
LEDTPQFKIDIDQEKAQALGVSINDINTTLGAAWGGSYVNDFIDRGRVKKVYVMSEAKYR
MLPDDIGDWYVRAADGQMVPFSAFSSSRWEYGSPRLERYNGLPSMEILGQAAPGKSTGEA
MELMEQLASKLPTGVGYDWTGMSYQERLSGNQAPSLYAISLIVVFLCLAALYESWSIPFS
VMLVVPLGVIGALLAATFRGLTNDVYFQVGLLTTIGLSAKNAILIVEFAKDLMDKEGKGL
IEATLDAVRMRLRPILMTSLAFILGVMPLVISTGAGSGAQNAVGTGVMGGMVTATVLAIF
FVPVFFVVVRRRFSRKNEDIEHSHTVDHH
Target 5 Number of Residues 1066
Target 5 Molecular Weight 113575
Target 5 Theoretical pI 5.23
Target 5 GO Classification
Function
transporter activity
Process
physiological process
cellular physiological process
transport
Component
cell
membrane
intrinsic to membrane
integral to membrane
Target 5 General Function Defense mechanisms and drug export
Target 5 Specific Function AcrAB is a drug efflux protein with a broad substrate specificity
Target 5 Pathways Not Available
Target 5 Reactions Not Available
Target 5 Pfam Domain Function
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • 10-28
  • 337-356
  • 366-385
  • 392-413
  • 439-457
  • 466-490
  • 539-555
  • 872-888
  • 899-918
  • 925-943
  • 973-992
  • 999-1018
Target 5 Essentiality Essential
Target 5 GenBank ID Protein 290406 Link Image
Target 5 UniProtKB/Swiss-Prot ID P31224 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name ACRB_ECOLI Link Image
Target 5 PDB ID 1OYE Link Image
Target 5 PDB File Show
Target 5 3D Structure
Target 5 Cellular Location
  • Cell inner membrane
  • multi-pass membrane protein
Target 5 Gene Sequence >3150 bp 
ATGCCTAATTTCTTTATCGATCGCCCGATTTTTGCGTGGGTGATCGCCATTATCATCATG
TTGGCAGGGGGGCTGGCGATCCTCAAACTGCCGGTGGCGCAATATCCTACGATTGCACCG
CCGGCAGTAACGATCTCCGCCTCCTACCCCGGCGCTGATGCGAAAACAGTGCAGGACACG
GTGACACAGGTTATCGAACAGAATATGAACGGTATCGATAACCTGATGTACATGTCCTCT
AACAGTGACTCCACGGGTACCGTGCAGATCACCCTGACCTTTGAGTCTGGTACTGATGCG
GATATCGCGCAGGTTCAGGTGCAGAACAAACTGCAGCTGGCGATGCCGTTGCTGCCGCAA
GAAGTTCAGCAGCAAGGGGTGAGCGTTGAGAAATCATCCAGCAGCTTCCTGATGGTTGTC
GGCGTTATCAACACCGATGGCACCATGACGCAGGAGGATATCTCCGACTACGTGGCGGCG
AATATGAAAGATGCCATCAGCCGTACGTCGGGCGTGGGTGATGTTCAGTTGTTCGGTTCA
CAGTACGCGATGCGTATCTGGATGAACCCGAATGAGCTGAACAAATTCCAGCTAACGCCG
GTTGATGTCATTACCGCCATCAAAGCGCAGAACGCCCAGGTTGCGGCGGGTCAGCTCGGT
GGTACGCCGCCGGTGAAAGGCCAACAGCTTAACGCCTCTATTATTGCTCAGACGCGTCTG
ACCTCTACTGAAGAGTTCGGCAAAATCCTGCTGAAAGTGAATCAGGATGGTTCCCGCGTG
CTGCTGCGTGACGTCGCGAAGATTGAGCTGGGTGGTGAGAACTACGACATCATCGCAGAG
TTTAACGGCCAACCGGCTTCCGGTCTGGGGATCAAGCTGGCGACCGGTGCAAACGCGCTG
GATACCGCTGCGGCAATCCGTGCTGAACTGGCGAAGATGGAACCGTTCTTCCCGTCGGGT
CTGAAAATTGTTTACCCATACGACACCACGCCGTTCGTGAAAATCTCTATTCACGAAGTG
GTTAAAACGCTGGTCGAAGCGATCATCCTCGTGTTCCTGGTTATGTATCTGTTCCTGCAG
AACTTCCGCGCGACGTTGATTCCGACCATTGCCGTACCGGTGGTATTGCTCGGGACCTTT
GCCGTCCTTGCCGCCTTTGGCTTCTCGATAAACACGCTAACAATGTTCGGGATGGTGCTC
GCCATCGGCCTGTTGGTGGATGACGCCATCGTTGTGGTAGAAAACGTTGAGCGTGTTATG
GCGGAAGAAGGTTTGCCGCCAAAAGAAGCTACCCGTAAGTCGATGGGGCAGATTCAGGGC
GCTCTGGTCGGTATCGCGATGGTACTGTCGGCGGTATTCGTACCGATGGCCTTCTTTGGC
GGTTCTACTGGTGCTATCTATCGTCAGTTCTCTATTACCATTGTTTCAGCAATGGCGCTG
TCGGTACTGGTGGCGTTGATCCTGACTCCAGCTCTTTGTGCCACCATGCTGAAACCGATT
GCCAAAGGCGATCACGGGGAAGGTAAAAAAGGCTTCTTCGGCTGGTTTAACCGCATGTTC
GAGAAGAGCACGCACCACTACACCGACAGCGTAGGCGGTATTCTGCGCAGTACGGGGCGT
TACCTGGTGCTGTATCTGATCATCGTGGTCGGCATGGCCTATCTGTTCGTGCGTCTGCCA
AGCTCCTTCTTGCCAGATGAGGACCAGGGCGTGTTTATGACCATGGTTCAGCTGCCAGCA
GGTGCAACGCAGGAACGTACACAGAAAGTGCTCAATGAGGTAACGCATTACTATCTGACC
AAAGAAAAGAACAACGTTGAGTCGGTGTTCGCCGTTAACGGCTTCGGCTTTGCGGGACGT
GGTCAGAATACCGGTATTGCGTTCGTTTCCTTGAAGGACTGGGCCGATCGTCCGGGCGAA
GAAAACAAAGTTGAAGCGATTACCATGCGTGCAACACGCGCTTTCTCGCAAATCAAAGAT
GCGATGGTTTTCGCCTTTAACCTGCCCGCAATCGTGGAACTGGGTACTGCAACCGGCTTT
GACTTTGAGCTGATTGACCAGGCTGGCCTTGGTCACGAAAAACTGACTCAGGCGCGTAAC
CAGTTGCTTGCAGAAGCAGCGAAGCACCCTGATATGTTGACCAGCGTACGTCCAAACGGT
CTGGAAGATACCCCGCAGTTTAAGATTGATATCGACCAGGAAAAAGCGCAGGCGCTGGGT
GTTTCTATCAACGACATTAACACCACTCTGGGCGCTGCATGGGGCGGCAGCTATGTGAAC
GACTTTATCGACCGCGGTCGTGTGAAGAAAGTTTATGTCATGTCAGAAGCGAAATACCGT
ATGCTGCCGGATGATATCGGCGACTGGTATGTTCGTGCTGCTGATGGTCAGATGGTGCCA
TTCTCGGCGTTCTCCTCTTCTCGTTGGGAGTACGGTTCGCCGCGTCTGGAACGTTACAAC
GGCCTGCCATCCATGGAAATCTTAGGCCAGGCGGCACCGGGTAAAAGTACCGGTGAAGCA
ATGGAGCTGATGGAACAACTGGCGAGCAAACTGCCTACCGGTGTTGGCTATGACTGGACG
GGGATGTCCTATCAGGAACGTCTCTCCGGCAACCAGGCACCTTCACTGTACGCGATTTCG
TTGATTGTCGTGTTCCTGTGTCTGGCGGCGCTGTACGAGAGCTGGTCGATTCCGTTCTCC
GTTATGCTGGTCGTTCCGCTGGGGGTTATCGGTGCGTTGCTGGCTGCCACCTTCCGTGGC
CTGACCAATGACGTTTACTTCCAGGTAGGCCTGCTCACAACCATTGGGTTGTCGGCGAAG
AACGCGATCCTTATCGTCGAATTCGCCAAAGACTTGATGGATAAAGAAGGTAAAGGTCTG
ATTGAAGCGACGCTTGATGCGGTGCGGATGCGTTTACGTCCGATCCTGATGACCTCGCTG
GCGTTTATCCTCGGCGTTATGCCGCTGGTTATCAGTACTGGTGCTGGTTCCGGCGCGCAG
AACGCAGTAGGTACCGGTGTAATGGGCGGGATGGTGACCGCAACGGTACTGGCAATCTTC
TTCGTTCCGGTATTCTTTGTGGTGGTTCGCCGCCGCTTTAGCCGCAAGAATGAAGATATC
GAGCACAGCCATACTGTCGATCATCATTGA
Target 5 GenBank Gene ID
Target 5 GeneCard ID Not Available
Target 5 GenAtlas ID Not Available
Target 5 HGNC ID Not Available
Target 5 Chromosome Location Not Available
Target 5 Locus Not Available
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Kawabe T, Fujihira E, Yamaguchi A: Molecular construction of a multidrug exporter system, AcrAB: molecular interaction between AcrA and AcrB, and cleavage of the N-terminal signal sequence of AcrA. J Biochem (Tokyo). 2000 Aug;128(2):195-200. [PubMed Link Image]
  2. Ma D, Cook DN, Alberti M, Pon NG, Nikaido H, Hearst JE: Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli. Mol Microbiol. 1995 Apr;16(1):45-55. [PubMed Link Image]
  3. Ma D, Cook DN, Alberti M, Pon NG, Nikaido H, Hearst JE: Molecular cloning and characterization of acrA and acrE genes of Escherichia coli. J Bacteriol. 1993 Oct;175(19):6299-313. [PubMed Link Image]
  4. 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 5 Drug References Not Available

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