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Showing drug card for Bismuth (DB01402)

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Version 2.5
Creation Date 2007-07-10 16:33:24
Update Date 2009-06-23 18:07:37
Primary Accession Number DB01402
Secondary Accession Number Not Available
Name Bismuth
Drug Type
  • Approved
  • Small Molecule
Description Bismuth compounds are widely used for the treatment of peptic ulcers and Helicobacter pylori infections. It has been suggested that enzyme inhibition plays an important role in the antibacterial activity of bismuth towards this bacterium. Bismuth thiols appear to act on bacterial ureases.
Synonyms Not Available
Brand Names Not Available
Brand Mixtures Not Available
Chemical IUPAC Name 3,5-dioxa-4$l^{2}-bismabicyclo[4.4.0]deca-1(10),6,8-trien-2-one hydrate
Chemical Formula C7H6BiO4
Chemical Structure Structure
CAS Registry Number 7440-69-9
InChI Identifier InChI=1/C7H6O3.Bi.H2O/c8-6-4-2-1-3-5(6)7(9)10;;/h1-4,8H,(H,9,10);;1H2/q;+2;/p-2/fC7H4O3.Bi.H2O/h8h;;/q-2;m;/rC7H4BiO3.H2O/c9-7-5-3-1-2-4-6(5)10-8-11-7;/h1-4H;1H2
InChI Key QBWLKDFBINPHFT-HLFHKPLUCZ
KEGG Drug Not Available
KEGG Compound C15471 Link Image
PubChem Compound 16682734 Link Image
PubChem Substance 10072 Link Image
ChEBI ID 33301 Link Image
PharmGKB ID Not Available
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 00065927 Link Image
RxList Link http://www.rxlist.com/cgi/generic/pylera.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Bismuth Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 363.1005
Monoisotopic Molecular Weight 363.0070
State Solid
Melting Point 271 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility Not Available Calculated using ALOGPS
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP Not Available Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS Not Available 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 O.O=C1O[Bi]OC2=CC=CC=C12
Canonical SMILES O.O=C1O[Bi]OC2=CC=CC=C12
Drug Category
  • Antidiarrheals
ATC Codes
AHFS Codes
  • 52:92.00
  • 56:04.00
  • 56:08.00
  • 84:92.00
  • 92:02.00*
Indication Not Available
Pharmacology Not Available
Mechanism of Action Not Available
Absorption Not Available
Toxicity Not Available
Protein Binding Not Available
Biotransformation Not Available
Half Life Not Available
Dosage Forms
Form Route
Dressing Topical
Liquid Oral
Liquid Sublingual
Solution / drops Oral
Suppository Rectal
Suspension Oral
Tablet Oral
Patient Information Not Available
Contraindications Not Available
Interactions Not Available
Drug Interactions
Drug Interaction
Acenocoumarol The salicylate increases effect of anticoagulant
Acetazolamide The salicylate at high dose increases the effect of the carbonic anhydrase inhibitors
Acetohexamide The salicylate increase the effect of sulfonylurea
Anisindione The salicylate increase effect of anticoagulant
Betamethasone The corticosteroid decreases the effect of salicylates
Chlorpropamide The salicylate increase the effect of sulfonylurea
Cortisone acetate The corticosteroid decreases the effect of salicylates
Demeclocycline Formation of non-absorbable complexes
Dexamethasone The corticosteroid decreases the effect of salicylates
Dichlorphenamide The salicylate at high dose increases the effect of the carbonic anyhydrase inhibitors
Dicumarol The salicylate increase effect of anticoagulant
Doxycycline Formation of non absorbable complexes
Fludrocortisone The corticosteroid decreases the effect of salicylates
Glibenclamide The salicylate increase the effect of sulfonylurea
Gliclazide The salicylate increase the effect of sulfonylurea
Glipizide The salicylate increase the effect of sulfonylurea
Glisoxepide The salicylate increase the effect of sulfonylurea
Glycodiazine The salicylate increase the effect of sulfonylurea
Hydrocortisone The corticosteroid decreases the effect of salicylates
Insulin The salicylate increase the effect of insulin
Insulin-aspart The salicylate increase the effect of insulin
Insulin-detemir The salicylate increase the effect of insulin
Insulin-glargine The salicylate increase the effect of insulin
Insulin-glulisine The salicylate increase the effect of insulin
Insulin-lispro The salicylate increase the effect of insulin
Methacycline Formation of non absorbable complexes
Methazolamide The salicylate at high dose increases the effect of the carbonic anhydrase inhibitors
Methotrexate The salicylate increase the effect and toxicity of methotrexate
Methylprednisolone The corticosteroid decreases the effect of salicylates
Minocycline Formation of non-absorbable complexes
Oxytetracycline Formation of non-absorbable complexes
Paramethasone The corticosteroid decreases the effect of salicylates
Prednisolone The corticosteroid decreases the effect of salicylates
Prednisone The corticosteroid decreases the effect of salicylates
Probenecid The salicylate decreases the uricosuric effect of probenecid
Sulfinpyrazone The salicylate antagonizes the uricosuric effect of sulfinpyrazone
Tetracycline Formation of non-absorbable complexes
Tolazamide The salicylate increase the effect of sulfonylurea
Tolbutamide The salicylate increase the effect of sulfonylurea
Triamcinolone The corticosteroid decreases the effect of salicylates
Valproic Acid The salicylate increase the effect of valproic acid
Warfarin The salicylate increases effect of anticoagulant
Food Interactions
  • Take without regard to meals.
Pathways Not Available
General References
  1. Wikipedia Link Image
  2. RxList Link Image
Organisms Affected Not Available
Targets
  1. Serotransferrin
  2. Serum albumin
Drug Target 1 [top]
Target 1 ID 566
Target 1 Name Serotransferrin
Target 1 Synonyms
  1. Beta-1-metal- binding globulin
  2. Serotransferrin precursor
  3. Siderophilin
  4. Transferrin
Target 1 Gene Name TF
Target 1 Protein Sequence >Serotransferrin precursor 
MRLAVGALLVCAVLGLCLAVPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVK
KASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVV
KKDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPC
ADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRD
QYELLCLDNTRKPVDEYKDCHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKE
FQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEAPTDECKP
VKWCALSHHERLKCDEWSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGK
CGLVPVLAENYNKSDNCEDTPEAGYFAVAVVKKSASDLTWDNLKGKKSCHTAVGRTAGWN
IPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYTGAF
RCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTRKPVEEYANCHLAR
APNHAVVTRKDKEACVHKILRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAKL
HDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP
Target 1 Number of Residues 709
Target 1 Molecular Weight 77050
Target 1 Theoretical pI 7.13
Target 1 GO Classification
Function
binding
ion binding
cation binding
transition metal ion binding
iron ion binding
ferric iron binding
Process
homeostasis
cell homeostasis
cell ion homeostasis
cation homeostasis
di-, tri-valent inorganic cation homeostasis
iron ion homeostasis
physiological process
cellular physiological process
transport
ion transport
cation transport
di-, tri-valent inorganic cation transport
transition metal ion transport
iron ion transport
Component
extracellular region
Target 1 General Function Involved in ferric iron binding
Target 1 Specific Function Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • 1-19
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 339453 Link Image
Target 1 UniProtKB/Swiss-Prot ID P02787 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name TRFE_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Secreted protein
Target 1 Gene Sequence >2097 bp 
ATGAGGCTCGCCGTGGGAGCCCTGCTGGTCTGCGCCGTCCTGGGGCTGTGTCTGGCTGTC
CCTGATAAAACTGTGAGATGGTGTGCAGTGTCGGAGCATGAGGCCACTAAGTGCCAGAGT
TTCCGCGACCATATGAAAAGCGTCATTCCATCCGATGGTCCCAGTGTTGCTTGTGTGAAG
AAAGCCTCCTACCTTGATTGCATCAGGGCCATTGCGGCAAACGAAGCGGATGCTGTGACA
CTGGATGCAGGTTTGGTGTATGATGCTTACTTGGCTCCCAATAACCTGAAGCCTGTGGTG
GCAGAGTTCTATGGGTCAAAAGAGGATCCACAGACTTTCTATTATGCTGTTGCTGTGGTG
AAGAAGGATAGTGGCTTCCAGATGAACCAGCTTCGAGGCAAGAAGTCCTGCCACACGGGT
CTAGGCAGGTCCGCTGGGTGGAACATCCCCATAGGCTTACTTTACTGTGACTTACCTGAG
CCACGTAAACCTCTTGAGAAAGCAGTGGCCAATTTCTTCTCGGGCAGCTGTGCCCCTTGT
GCGGATGGGACGGACTTCCCCCAGCTGTGTCAACTGTGTCCAGGGTGTGGCTGCTCCACC
CTTAACCAATACTTCGGCTACTCGGGAGCCTTCAAGTGTCTGAAGGATGGTGCTGGGGAT
GTGGCCTTTGTCAAGCACTCGACTATATTTGAGAACTTGGCAAACAAGGCTGACAGGGAC
CAGTATGAGCTGCTTTGCCTAGACAACACCCGGAAGCCGGTAGATGAATACAAGGACTGC
CACTTGGCCCAGGTCCCTTCTCATACCGTCGTGGCCCGAAGTATGGGCGGCAAGGAGGAC
TTGATCTGGGAGCTTCTCAACCAGGCCCAGGAACATTTTGGCAAAGACAAATCAAAAGAA
TTCCAACTATTCAGCTCTCCTCATGGGAAGGACCTGCTGTTTAAGGACTCTGCCCACGGG
TTTTTAAAAGTCCCCCCAAGGATGGATGCCAAGATGTACCTGGGCTATGAGTATGTCACT
GCCATCCGGAATCTACGGGAAGGCACATGCCCAGAAGCCCCAACAGATGAATGCAAGCCT
GTGAAGTGGTGTGCGCTGAGCCACCACGAGAGGCTCAAGTGTGATGAGTGGAGTGTTAAC
AGTGTAGGGAAAATAGAGTGTGTATCAGCAGAGACCACCGAAGACTGCATCGCCAAGATC
ATGAATGGAGAAGCTGATGCCATGAGCTTGGATGGAGGGTTTGTCTACATAGCGGGCAAG
TGTGGTCTGGTGCCTGTCTTGGCAGAAAACTACAATAAGAGCGATAATTGTGAGGATACA
CCAGAGGCAGGGTATTTTGCTGTAGCAGTGGTGAAGAAATCAGCTTCTGACCTCACCTGG
GACAATCTGAAAGGCAAGAAGTCCTGCCATACGGCAGTTGGCAGAACCGCTGGCTGGAAC
ATCCCCATGGGCCTGCTCTACAATAAGATCAACCACTGCAGATTTGATGAATTTTTCAGT
GAAGGTTGTGCCCCTGGGTCTAAGAAAGACTCCAGTCTCTGTAAGCTGTGTATGGGCTCA
GGCCTAAACCTGTGTGAACCCAACAACAAAGAGGGATACTACGGCTACACAGGCGCTTTC
AGGTGTCTGGTTGAGAAGGGAGATGTGGCCTTTGTGAAACACCAGACTGTCCCACAGAAC
ACTGGGGGAAAAAACCCTGATCCATGGGCTAAGAATCTGAATGAAAAAGACTATGAGTTG
CTGTGCCTTGATGGTACCAGGAAACCTGTGGAGGAGTATGCGAACTGCCACCTGGCCAGA
GCCCCGAATCACGCTGTGGTCACACGGAAAGATAAGGAAGCTTGCGTCCACAAGATATTA
CGTCAACAGCAGCACCTATTTGGAAGCAACGTAACTGACTGCTCGGGCAACTTTTGTTTG
TTCCGGTCGGAAACCAAGGACCTTCTGTTCAGAGATGACACAGTATGTTTGGCCAAACTT
CATGACAGAAACACATATGAAAAATACTTAGGAGAAGAATATGTCAAGGCTGTTGGTAAC
CTGAGAAAATGCTCCACCTCATCACTCCTGGAAGCCTGCACTTTCCGTAGACCTTAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID TF Link Image
Target 1 GenAtlas ID TF Link Image
Target 1 HGNC ID HGNC:11740 Link Image
Target 1 Chromosome Location 3
Target 1 Locus 3q22.1
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Bewley MC, Tam BM, Grewal J, He S, Shewry S, Murphy ME, Mason AB, Woodworth RC, Baker EN, MacGillivray RT: X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32. Biochemistry. 1999 Feb 23;38(8):2535-41. [PubMed Link Image]
  2. de Arriba Zerpa GA, Saleh MC, Fernandez PM, Guillou F, Espinosa de los Monteros A, de Vellis J, Zakin MM, Baron B: Alternative splicing prevents transferrin secretion during differentiation of a human oligodendrocyte cell line. J Neurosci Res. 2000 Aug 15;61(4):388-95. [PubMed Link Image]
  3. Beutler E, Gelbart T, Lee P, Trevino R, Fernandez MA, Fairbanks VF: Molecular characterization of a case of atransferrinemia. Blood. 2000 Dec 15;96(13):4071-4. [PubMed Link Image]
  4. Douabin-Gicquel V, Soriano N, Ferran H, Wojcik F, Palierne E, Tamim S, Jovelin T, McKie AT, Le Gall JY, David V, Mosser J: Identification of 96 single nucleotide polymorphisms in eight genes involved in iron metabolism: efficiency of bioinformatic extraction compared with a systematic sequencing approach. Hum Genet. 2001 Oct;109(4):393-401. [PubMed Link Image]
  5. Lee PL, Halloran C, Trevino R, Felitti V, Beutler E: Human transferrin G277S mutation: a risk factor for iron deficiency anaemia. Br J Haematol. 2001 Nov;115(2):329-33. [PubMed Link Image]
  6. Hershberger CL, Larson JL, Arnold B, Rosteck PR Jr, Williams P, DeHoff B, Dunn P, O'Neal KL, Riemen MW, Tice PA, et al.: A cloned gene for human transferrin. Ann N Y Acad Sci. 1991 Dec 27;646:140-54. [PubMed Link Image]
  7. Woodworth RC, Mason AB, Funk WD, MacGillivray RT: Expression and initial characterization of five site-directed mutants of the N-terminal half-molecule of human transferrin. Biochemistry. 1991 Nov 12;30(45):10824-9. [PubMed Link Image]
  8. Duguid JR, Bohmont CW, Liu NG, Tourtellotte WW: Changes in brain gene expression shared by scrapie and Alzheimer disease. Proc Natl Acad Sci U S A. 1989 Sep;86(18):7260-4. [PubMed Link Image]
  9. Adrian GS, Korinek BW, Bowman BH, Yang F: The human transferrin gene: 5' region contains conserved sequences which match the control elements regulated by heavy metals, glucocorticoids and acute phase reaction. Gene. 1986;49(2):167-75. [PubMed Link Image]
  10. Schaeffer E, Lucero MA, Jeltsch JM, Py MC, Levin MJ, Chambon P, Cohen GN, Zakin MM: Complete structure of the human transferrin gene. Comparison with analogous chicken gene and human pseudogene. Gene. 1987;56(1):109-16. [PubMed Link Image]
  11. 3786138 Lucero MA, Schaeffer E, Cohen GN, Zakin MM: The 5' region of the human transferrin gene: structure and potential regulatory sites. Nucleic Acids Res. 1986 Nov 11;14(21):8692.
  12. 3858812 Park I, Schaeffer E, Sidoli A, Baralle FE, Cohen GN, Zakin MM: Organization of the human transferrin gene: direct evidence that it originated by gene duplication. Proc Natl Acad Sci U S A. 1985 May;82(10):3149-53.
  13. 6322780 Uzan G, Frain M, Park I, Besmond C, Maessen G, Trepat JS, Zakin MM, Kahn A: Molecular cloning and sequence analysis of cDNA for human transferrin. Biochem Biophys Res Commun. 1984 Feb 29;119(1):273-81.
  14. 6585826 Yang F, Lum JB, McGill JR, Moore CM, Naylor SL, van Bragt PH, Baldwin WD, Bowman BH: Human transferrin: cDNA characterization and chromosomal localization. Proc Natl Acad Sci U S A. 1984 May;81(9):2752-6.
  15. 6833213 MacGillivray RT, Mendez E, Shewale JG, Sinha SK, Lineback-Zins J, Brew K: The primary structure of human serum transferrin. The structures of seven cyanogen bromide fragments and the assembly of the complete structure. J Biol Chem. 1983 Mar 25;258(6):3543-53.
  16. 6953407 MacGillivray RT, Mendez E, Sinha SK, Sutton MR, Lineback-Zins J, Brew K: The complete amino acid sequence of human serum transferrin. Proc Natl Acad Sci U S A. 1982 Apr;79(8):2504-8.
  17. 7498159 Kovalyov LI, Shishkin SS, Efimochkin AS, Kovalyova MA, Ershova ES, Egorov TA, Musalyamov AK: The major protein expression profile and two-dimensional protein database of human heart. Electrophoresis. 1995 Jul;16(7):1160-9.
  18. 9272172 Namekata K, Oyama F, Imagawa M, Ihara Y: Human transferrin (Tf): a single mutation at codon 570 determines Tf C1 or Tf C2 variant. Hum Genet. 1997 Sep;100(3-4):457-8.
  19. 9358047 Evans P, Kemp J: Exon/intron structure of the human transferrin receptor gene. Gene. 1997 Oct 15;199(1-2):123-31.
  20. 9609685 MacGillivray RT, Moore SA, Chen J, Anderson BF, Baker H, Luo Y, Bewley M, Smith CA, Murphy ME, Wang Y, Mason AB, Woodworth RC, Brayer GD, Baker EN: Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release. Biochemistry. 1998 Jun 2;37(22):7919-28.
  21. 9760232 Jeffrey PD, Bewley MC, MacGillivray RT, Mason AB, Woodworth RC, Baker EN: Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin. Biochemistry. 1998 Oct 6;37(40):13978-86.
  22. 9803271 Pang H, Koda Y, Soejima M, Kimura H: Identification of a mutation (A1879G) of transferrin from cDNA prepared from peripheral blood cells. Ann Hum Genet. 1998 May;62(Pt 3):271-4.
Target 1 Drug References
  1. Sun H, Li H, Mason AB, Woodworth RC, Sadler PJ: Competitive binding of bismuth to transferrin and albumin in aqueous solution and in blood plasma. J Biol Chem. 2001 Mar 23;276(12):8829-35. Epub 2000 Dec 7. [PubMed Link Image]
  2. Sun H, Szeto KY: Binding of bismuth to serum proteins: implication for targets of Bi(III) in blood plasma. J Inorg Biochem. 2003 Feb 1;94(1-2):114-20. [PubMed Link Image]
  3. Zhang M, Gumerov DR, Kaltashov IA, Mason AB: Indirect detection of protein-metal binding: interaction of serum transferrin with In3+ and Bi3+. J Am Soc Mass Spectrom. 2004 Nov;15(11):1658-64. [PubMed Link Image]
  4. Miquel G, Nekaa T, Kahn PH, Hemadi M, El Hage Chahine JM: Mechanism of formation of the complex between transferrin and bismuth, and interaction with transferrin receptor 1. Biochemistry. 2004 Nov 23;43(46):14722-31. [PubMed Link Image]
  5. Ge R, Sun H: Bioinorganic chemistry of bismuth and antimony: target sites of metallodrugs. Acc Chem Res. 2007 Apr;40(4):267-74. Epub 2007 Mar 2. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 587
Target 2 Name Serum albumin
Target 2 Synonyms
  1. Serum albumin precursor
Target 2 Gene Name ALB
Target 2 Protein Sequence >Serum albumin precursor 
MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPF
EDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEP
ERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLF
FAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAV
ARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLK
ECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYAR
RHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFE
QLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVV
LNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTL
SEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLV
AASQAALGL
Target 2 Number of Residues 619
Target 2 Molecular Weight 69367
Target 2 Theoretical pI 6.21
Target 2 GO Classification
Function
transporter activity
carrier activity
Process
physiological process
cellular physiological process
transport
Component
extracellular region
extracellular space
Target 2 General Function Involved in antioxidant activity
Target 2 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 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-18
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 28590 Link Image
Target 2 UniProtKB/Swiss-Prot ID P02768 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name ALBU_HUMAN Link Image
Target 2 PDB ID 1HA2 Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Secreted protein
Target 2 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 2 GenBank Gene ID
Target 2 GeneCard ID ALB Link Image
Target 2 GenAtlas ID ALB Link Image
Target 2 HGNC ID HGNC:399 Link Image
Target 2 Chromosome Location 4
Target 2 Locus 4q11-q13
Target 2 SNPs SNPJam Report Link Image
Target 2 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 2 Drug References
  1. Sun H, Li H, Mason AB, Woodworth RC, Sadler PJ: Competitive binding of bismuth to transferrin and albumin in aqueous solution and in blood plasma. J Biol Chem. 2001 Mar 23;276(12):8829-35. Epub 2000 Dec 7. [PubMed Link Image]
  2. Sun H, Szeto KY: Binding of bismuth to serum proteins: implication for targets of Bi(III) in blood plasma. J Inorg Biochem. 2003 Feb 1;94(1-2):114-20. [PubMed Link Image]

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