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Showing drug card for Iron Dextran (DB00893)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:08:05
Primary Accession Number DB00893
Secondary Accession Number
  • APRD01053
Name Iron Dextran
Drug Type
  • Approved
  • Small Molecule
Description Iron dextran is a dark brown, slightly viscous liquid complex of ferric hydroxide and dextran for intravenous or intramuscular use. Iron Dextran is used for the treatment of patients with documented iron deficiency in which oral administration is unsatisfactory or impossible.
Synonyms
  1. Dexferrum
  2. Dextran iron
Brand Names
  1. Imferon
  2. Infed
  3. Proferdex
Brand Mixtures
  1. Omni 2000tab (Beta-Carotene + Biotin + Calcium (Bone Meal) + Choline + Chromium (Yeast) + D-Pantothenic Acid + Folic Acid + Inositol + Iodine (Kelp) + Iron (Iron Dextran Complex) + Magnesium (Magnesium Oxide) + Manganese (Manganese Gluconate) + Molybdenum (Yeast) + Nicotinamide + Potassium (Potassium Gluconate) + Selenium (Yeast) + Vitamin a (Fish Liver Oil) + Vitamin B1 + Vitamin B12 + Vitamin B2 + Vitamin B6 (Pyridoxine Hydrochloride) + Vitamin C (Calcium Ascorbate) + Vitamin C (Vitamin C) + Vitamin D3 + Vitamin E (D-Alpha Tocopheryl Acetate) + Zinc (Zinc Gluconate))
Chemical IUPAC Name Iron dextran
Chemical Formula (FeO.OH.2H2O)478 (Dx.COOH)9
Chemical Structure Structure
CAS Registry Number 9004-66-4
InChI Identifier Not Available
InChI Key Not Available
KEGG Drug D02141 Link Image
KEGG Compound Not Available
PubChem Compound Not Available
PubChem Substance 7849202 Link Image
ChEBI ID Not Available
PharmGKB ID PA450093 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 00611891 Link Image
RxList Link http://www.rxlist.com/cgi/generic3/fedex.htm Link Image
PDRhealth Link Not Available
Wikipedia Link Not Available
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 105000.0000
Monoisotopic Molecular Weight Not Available
State Solid
Melting Point Not Available
Experimental Water Solubility Soluble 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 Not Available
SDF File Not Available
PDB File Not Available
Experimental PDB ID Not Available
Isomeric SMILES Not Available
Canonical SMILES Not Available
Drug Category
  • Anti-anemic Agents
  • Iron Supplement
ATC Codes Not Available
AHFS Codes Not Available
Indication For treatment of patients with documented iron deficiency in whom oral administration is unsatisfactory or impossible. Also used to replenish body iron stores in Non-Dialysis Dependent-Chronic Kidney Disease (NDD-CKD) patients receiving or not receiving erythropoietin and in Hemodialysis Dependent (HDD-CKD) and Peritoneal Dialysis Dependent (PDD-CKD) - Chronic Kidney Disease patients receiving an erythropoietin.
Pharmacology Iron dextran is a dark brown, slightly viscous sterile liquid complex of ferric hydroxide and dextran for intravenous or intramuscular use. It is for treatment of patients with documented iron deficiency in whom oral administration is unsatisfactory or impossible. Iron is essential to the formation of hemoglobin and to the function and formation of other heme and nonheme compounds. Untreated depletion of iron stores leads to iron-deficient erythropoiesis and, in turn, to iron deficiency anemia.
Mechanism of Action After iron dextran is injected, the circulating iron dextran is removed from the plasma by cells of the reticuloendothelial system, which split the complex into its components of iron and dextran. The iron is immediately bound to the available protein moieties to form hemosiderin or ferritin, the physiological forms of iron, or to a lesser extent to transferrin. This iron which is subject to physiological control replenishes hemoglobin and depleted iron stores.
Absorption The major portion of intramuscular injections of iron dextran is absorbed within 72 hours; most of the remaining iron is absorbed over the ensuing 3 to 4 weeks.
Toxicity LD50 = 500 mg/kg (mouse, IV). Dosages of iron dextran in excess of the requirements for restoration of hemoglobin and replenishment of iron stores may lead to hemosiderosis. Cases of severe, sometimes fatal, allergic reactions (loss of consciousness, collapse, difficulty breathing, hives, swelling, or convulsions) and severe low blood pressure (hypotension) have been reported with the use of iron dextran.
Protein Binding 100% (after release from dextran)
Biotransformation Dextran, a polyglucose, is either metabolized or excreted.
Half Life 5 hours (some indications that it can be as long as 10 hours)
Dosage Forms
Form Route
Injection, solution Intramuscular
Injection, solution Intravenous
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Not Available
Drug Interactions
Drug Interaction
Alendronate Formation of non-absorbable complexes
Ciprofloxacin Formation of non-absorbable complexes
Clodronate Formation of non-absorbable complexes
Demeclocycline Formation of non-absorbable complexes
Doxycycline Formation of non-absorbable complexes
Enoxacin Formation of non-absorbable complexes
Etidronic acid Formation of non-absorbable complexes
Gatifloxacin Formation of non-absorbable complexes
Gemifloxacin Formation of non-absorbable complexes
Grepafloxacin Formation of non-absorbable complexes
Ibandronate Formation of non-absorbable complexes
Levodopa Iron decreases the absorption of dopa derivatives
Levofloxacin Formation of non-absorbable complexes
Levothyroxine Iron decreases the absorption of levothyroxine
Lomefloxacin Formation of non-absorbable complexes
Methacycline Formation of non-absorbable complexes
Methyldopa Iron decreases the absorption of dopa derivatives
Minocycline Formation of non-absorbable complexes
Moxifloxacin Formation of non-absorbable complexes
Mycophenolate mofetil Oral iron decreases the absorption of mycophenolate-mofetil
Norfloxacin Formation of non-absorbable complexes
Ofloxacin Formation of non-absorbable complexes
Oxytetracycline Formation of non-absorbable complexes
Pefloxacin Formation of non-absorbable complexes
Penicillamine The multivalent agent decreases the effect of penicillamine
Risedronate Formation of non-absorbable complexes
Temafloxacin Formation of non-absorbable complexes
Tetracycline Formation of non-absorbable complexes
Trovafloxacin Formation of non-absorbable complexes
Food Interactions Not Available
Pathways Not Available
General References
  1. RxList Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Ferritin light chain
  2. Hemoglobin subunit alpha
  3. Ferritin heavy chain
  4. Serotransferrin
  5. Hemoglobin subunit beta
Drug Target 1 [top]
Target 1 ID 95
Target 1 Name Ferritin light chain
Target 1 Synonyms
  1. Ferritin L subunit
Target 1 Gene Name FTL
Target 1 Protein Sequence >Ferritin light chain 
SSQIRQNYSTDVEAAVNSLVNLYLQASYTYLSLGFYFDRDDVALEGVSHFFRELAEEKRE
GYERLLKMQNQRGGRALFQDIKKPAEDEWGKTPDAMKAAMALEKKLNQALLDLHALGSAR
TDPHLCDFLETHFLDEEVKLIKKMGDHLTNLHRLGGPEAGLGEYLFERLTLKHD
Target 1 Number of Residues 176
Target 1 Molecular Weight 19889
Target 1 Theoretical pI 5.59
Target 1 GO Classification
Function
ion binding
cation binding
transition metal ion binding
iron ion binding
ferric iron binding
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
Not Available
Target 1 General Function Inorganic ion transport and metabolism
Target 1 Specific Function Stores iron in a soluble, nontoxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 182514 Link Image
Target 1 UniProtKB/Swiss-Prot ID P02792 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name FRIL_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location Not Available
Target 1 Gene Sequence >528 bp 
ATGAGCTCCCAGATTCGTCAGAATTATTCCACCGACGTGGAGGCAGCCGTCAACAGCCTG
GTCAATTTGTACCTGCAGGCCTCCTACACCTACCTCTCTCTGGGCTTCTATTTCGACCGC
GATGATGTGGCTCTGGAAGGCGTGAGCCACTTCTTCCGCGAACTGGCCGAGGAGAAGCGC
GAGGGCTACGAGCGTCTCCTGAAGATGCAAAACCAGCGTGGCGGCCGCGCTCTCTTCCAG
GACATCAAGAAGCCAGCTGAAGATGAGTGGGGTAAAACCCCAGACGCCATGAAAGCTGCC
ATGGCCCTGGAGAAAAAGCTGAACCAGGCCCTTTTGGATCTTCATGCCCTGGGTTCTGCC
CGCACGGACCCCCATCTCTGTGACTTCCTGGAGACTCACTTCCTAGATGAGGAAGTGAAG
CTTATCAAGAAGATGGGTGACCACCTGACCAACCTCCACAGGCTGGGTGGCCCGGAGGCT
GGGCTGGGCGAGTATCTCTTCGAAAGGCTCACTCTCAAGCACGACTAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID FTL Link Image
Target 1 GenAtlas ID FTL Link Image
Target 1 HGNC ID HGNC:3999 Link Image
Target 1 Chromosome Location 19
Target 1 Locus 19q13.3-q13.4
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Chou CC, Gatti RA, Fuller ML, Concannon P, Wong A, Chada S, Davis RC, Salser WA: Structure and expression of ferritin genes in a human promyelocytic cell line that differentiates in vitro. Mol Cell Biol. 1986 Feb;6(2):566-73. [PubMed Link Image]
  2. Santoro C, Marone M, Ferrone M, Costanzo F, Colombo M, Minganti C, Cortese R, Silengo L: Cloning of the gene coding for human L apoferritin. Nucleic Acids Res. 1986 Apr 11;14(7):2863-76. [PubMed Link Image]
  3. Boyd D, Vecoli C, Belcher DM, Jain SK, Drysdale JW: Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones. J Biol Chem. 1985 Sep 25;260(21):11755-61. [PubMed Link Image]
  4. Dorner MH, Salfeld J, Will H, Leibold EA, Vass JK, Munro HN: Structure of human ferritin light subunit messenger RNA: comparison with heavy subunit message and functional implications. Proc Natl Acad Sci U S A. 1985 May;82(10):3139-43. [PubMed Link Image]
  5. Addison JM, Fitton JE, Lewis WG, May K, Harrison PM: The amino acid sequence of human liver apoferritin. FEBS Lett. 1983 Nov 28;164(1):139-44. [PubMed Link Image]
  6. Vladimirov SN, Ivanov AV, Karpova GG, Musolyamov AK, Egorov TA, Thiede B, Wittmann-Liebold B, Otto A: Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry. Eur J Biochem. 1996 Jul 1;239(1):144-9. [PubMed Link Image]
Target 1 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 144
Target 2 Name Hemoglobin subunit alpha
Target 2 Synonyms
  1. Alpha-globin
  2. Hemoglobin alpha chain
Target 2 Gene Name HBA1
Target 2 Protein Sequence >Hemoglobin subunit alpha 
VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGK
KVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPA
VHASLDKFLASVSTVLTSKYR
Target 2 Number of Residues 143
Target 2 Molecular Weight 15126
Target 2 Theoretical pI 9.09
Target 2 GO Classification
Function
tetrapyrrole binding
heme binding
binding
oxygen binding
Process
physiological process
cellular physiological process
transport
gas transport
oxygen transport
Component
protein complex
hemoglobin complex
Target 2 General Function Involved in iron ion binding
Target 2 Specific Function Involved in oxygen transport from the lung to the various peripheral tissues
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 Non-Essential
Target 2 GenBank ID Protein 386764 Link Image
Target 2 UniProtKB/Swiss-Prot ID P69905 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name HBA_HUMAN Link Image
Target 2 PDB ID 1Y01 Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location Not Available
Target 2 Gene Sequence >429 bp 
ATGGTGCTGTCTCCTGCCGACAAGACCAACGTCAAGGCCGCCTGGGGTAAGGTCGGCGCG
CACGCTGGCGAGTATGGTGCGGAGGCCCTGGAGAGGATGTTCCTGTCCTTCCCCACCACC
AAGACCTACTTCCCGCACTTCGACCTGAGCCACGGCTCTGCCCAGGTTAAGGGCCACGGC
AAGAAGGTGGCCGACGCCCTGACCAACGCCGTGGCGCACGTGGACGACATGCCCAACGCG
CTGTCCGCCCTGAGCGACCTGCACGCGCACAAGCTTCGGGTGGACCCGGTCAACTTCAAG
CTCCTAAGCCACTGCCTGCTGGTGACCCTGGCCGCCCACCTCCCCGCCGAGTTCACCCCT
GCGGTGCACGCCTCCCTGGACAAGTTCCTGGCTTCTGTGAGCACCGTGCTGACCTCCAAA
TACCGTTAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID HBA1 Link Image
Target 2 GenAtlas ID HBA1 Link Image
Target 2 HGNC ID HGNC:4823 Link Image
Target 2 Chromosome Location 16
Target 2 Locus 16p13.3
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  2. Brimhall B, Jones RT, Schneider RG, Hosty TS, Tomlin G, Atkins R: Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys) and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg). Biochim Biophys Acta. 1975 Jan 30;379(1):28-32. [PubMed Link Image]
  3. Zhao Y, Zhong M, Liu Z, Xu X: [Rapid detection of the common alpha-thalassemia-2 determinants by PCR assay] Zhonghua Yi Xue Yi Chuan Xue Za Zhi. 2001 Jun;18(3):216-8. [PubMed Link Image]
  4. Zhao Y, Xu X: Alpha2(CD31 AGG-->AAG, Arg-->Lys) causing non-deletional alpha-thalassemia in a Chinese family with HbH disease. Haematologica. 2001 May;86(5):541-2. [PubMed Link Image]
  5. Fermi G: Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2-5 A resolution: refinement of the atomic model. J Mol Biol. 1975 Sep 15;97(2):237-56. [PubMed Link Image]
  6. 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]
  7. Abbes S, M'Rad A, Fitzgerald PA, Dormer P, Blouquit Y, Kister J, Galacteros F, Wajcman H: HB Al-Ain Abu Dhabi [alpha 18(A16)Gly----Asp]: a new hemoglobin variant discovered in an Emiratee family. Hemoglobin. 1992;16(5):355-62. [PubMed Link Image]
  8. Fujisawa K, Hattori Y, Ohba Y, Ando S: Hb Yuda or alpha 130(H13)Ala----Asp; a new alpha chain variant with low oxygen affinity. Hemoglobin. 1992;16(5):435-9. [PubMed Link Image]
  9. Wajcman H, Blouquit Y, Vasseur C, Le Querrec A, Laniece M, Melevendi C, Rasore A, Galacteros F: Two new human hemoglobin variants caused by unusual mutational events: Hb Zaire contains a five residue repetition within the alpha-chain and Hb Duino has two residues substituted in the beta-chain. Hum Genet. 1992 Aug;89(6):676-80. [PubMed Link Image]
  10. Silva MM, Rogers PH, Arnone A: A third quaternary structure of human hemoglobin A at 1.7-A resolution. J Biol Chem. 1992 Aug 25;267(24):17248-56. [PubMed Link Image]
  11. 1618774 Vasseur C, Blouquit Y, Kister J, Prome D, Kavanaugh JS, Rogers PH, Guillemin C, Arnone A, Galacteros F, Poyart C, et al.: Hemoglobin Thionville. An alpha-chain variant with a substitution of a glutamate for valine at NA-1 and having an acetylated methionine NH2 terminus. J Biol Chem. 1992 Jun 25;267(18):12682-91.
  12. 1634355 Miyashita H, Hashimoto K, Mohri H, Ohokubo T, Harano T, Harano K, Imai K: Hb Kanagawa [alpha 40(C5)Lys----Met]: a new alpha chain variant with an increased oxygen affinity. Hemoglobin. 1992;16(1-2):1-10.
  13. 1634357 Langdown JV, Davidson RJ, Williamson D: A new alpha chain variant, Hb Turriff [alpha 99(G6)Lys----Glu]: the interference of abnormal hemoglobins in Hb A1c determination. Hemoglobin. 1992;16(1-2):11-7.
  14. 1634363 Orisaka M, Tajima T, Harano T, Harano K, Kushida Y, Imai K: A new alpha chain variant, Hb Hanamaki or alpha 2(139)(HC1)Lys----Glu beta 2, found in a Japanese family. Hemoglobin. 1992;16(1-2):67-71.
  15. 1686260 Jiang NH, Liang S, Wen XJ, Liang R, Su C, Tang Z: Hb Westmead: an alpha 2-globin gene mutation detected by polymerase chain reaction and Stu I cleavage. Hemoglobin. 1991;15(4):291-5.
  16. 1802882 Zwerdling T, Williams S, Nasr SA, Rucknagel DL: Hb Port Huron [alpha 56 (E5)Lys----ARG]: a new alpha chain variant. Hemoglobin. 1991;15(5):381-91.
  17. 2079430 Harkness M, Harkness DR, Kutlar F, Kutlar A, Wilson JB, Webber BB, Codrington JF, Huisman TH: Hb Sun Prairie or alpha(2)130(H13)Ala----Pro beta 2, a new unstable variant occurring in low quantities. Hemoglobin. 1990;14(5):479-89.
  18. 2101836 Wilson JB, Webber BB, Plaseska D, de Alarcon PA, McMillan SK, Huisman TH: Hb Davenport or alpha 2(78)(EF7)Asn----His beta 2. Hemoglobin. 1990;14(6):599-605.
  19. 2606724 Wilson JB, Webber BB, Kutlar A, Reese AL, McKie VC, Lutcher CL, Felice AE, Huisman TH: Hb Evans or alpha 262(E11)Val----Met beta 2; an unstable hemoglobin causing a mild hemolytic anemia. Hemoglobin. 1989;13(6):557-66.
  20. 2752146 Cash FE, Monplaisir N, Goossens M, Liebhaber SA: Locus assignment of two alpha-globin structural mutants from the Caribbean basin: alpha Fort de France (alpha 45 Arg) and alpha Spanish Town (alpha 27 Val). Blood. 1989 Aug 1;74(2):833-5.
  21. 3654264 Fleming PJ, Sumner DR, Wyatt K, Hughes WG, Melrose WD, Jupe DM, Baikie MJ: Hemoglobin Hobart or alpha 20(Bl)His----Arg: a new alpha chain hemoglobin variant. Hemoglobin. 1987;11(3):211-20.
  22. 3754246 Como PF, Barber S, Sage RE, Trent RJ, Kronenberg H: Hemoglobin Woodville: alpha (2)6(A4) aspartic acid----tyrosine. Hemoglobin. 1986;10(2):135-41.
  23. 4212045 Reed RE, Winter WP, Rucknagel DL: Haemoglobin inkster (alpha2 85aspartic acid leads to valine beta2) coexisting with beta-thalassaemia in a Caucasian family. Br J Haematol. 1974 Mar;26(3):475-84.
  24. 4528583 Huisman TH, Wilson JB, Gravely M, Hubbard M: Hemoglobin Grady: the first example of a variant with elongated chains due to an insertion of residues. Proc Natl Acad Sci U S A. 1974 Aug;71(8):3270-3.
  25. 4744335 Sumida I, Ota Y, Imamura T, Yanase T: Hemoglobin Sawara: alpha 6(A4) aspartic acid leads to alanine. Biochim Biophys Acta. 1973 Sep 21;322(1):23-6.
  26. 478977 Sanguansermsri T, Matragoon S, Changloah L, Flatz G: Hemoglobin Suan-Dok (alpha 2 109 (G16) Leu replaced by Arg beta 2): an unstable variant associated with alpha-thalassemia. Hemoglobin. 1979;3(2-3):161-74.
  27. 5115619 Fujiwara N, Maekawa T, Matsuda G: Hemoglobin Atago (alpha2-85Tyr beta-2) a new abnormal human hemoglobin found in Nagasaki. Biochemical studies on hemoglobins and myoglobins. VI. Int J Protein Res. 1971;3(1):35-9.
  28. 5780195 Charache S, Mondzac AM, Gessner U: Hemoglobin Hasharon (alpha-2-47 his(CD5)beta-2): a hemoglobin found in low concentration. J Clin Invest. 1969 May;48(5):834-47.
  29. 6244294 Wilson JT, Wilson LB, Reddy VB, Cavallesco C, Ghosh PK, deRiel JK, Forget BG, Weissman SM: Nucleotide sequence of the coding portion of human alpha globin messenger RNA. J Biol Chem. 1980 Apr 10;255(7):2807-15.
  30. 6452630 Liebhaber SA, Goossens MJ, Kan YW: Cloning and complete nucleotide sequence of human 5'-alpha-globin gene. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7054-8.
  31. 6526652 Zeng YT, Huang SZ, Qiu XK, Cheng GC, Ren ZR, Jin QC, Chen CY, Jiao CT, Tang ZG, Liu RH, et al.: Hemoglobin Chongqing [alpha 2(NA2)Leu----Arg] and hemoglobin Harbin [alpha 16(A14)Lys----Met] found in China. Hemoglobin. 1984;8(6):569-81.
  32. 6815131 Harano T, Harano K, Shibata S, Ueda S, Imai K, Seki M: HB Handa [alpha 90 (FG 2) Lys replaced by Met]: structure and biosynthesis of a new slightly higher oxygen affinity variant. Hemoglobin. 1982;6(4):379-89.
  33. 7161109 Zeng YT, Huang SZ, Zhou XD, Qiu XK, Dong QY, Li MY, Bai JH: Hb Shenyang (alpha 26 (B7) Ala replaced by Glu): a new unstable variant found in China. Hemoglobin. 1982;6(6):625-8.
  34. 7448866 Michelson AM, Orkin SH: The 3' untranslated regions of the duplicated human alpha-globin genes are unexpectedly divergent. Cell. 1980 Nov;22(2 Pt 2):371-7.
  35. 7470621 Honig GR, Shamsuddin M, Zaizov R, Steinherz M, Solar I, Kirschmann C: Hemoglobin Petah Tikva (alpha 110 ala replaced by asp): a new unstable variant with alpha-thalassemia-like expression. Blood. 1981 Apr;57(4):705-11.
  36. 7558876 Harano T, Harano K, Imai K, Murakami T, Matsubara H: Hb Kurosaki [alpha 7(A5)Lys-->Glu]: a new alpha chain variant found in a Japanese woman. Hemoglobin. 1995 May-Jul;19(3-4):197-201.
  37. 7713747 Yalcin A, Avcu F, Beyan C, Gurgey A, Ural AU: A case of HB J-Meerut (or Hb J-Birmingham) [alpha 120(H3)Ala-->Glu] Hemoglobin. 1994 Nov;18(6):433-5.
  38. 7786798 Darbellay R, Mach-Pascual S, Rose K, Graf J, Beris P: Haemoglobin Tunis-Bizerte: a new alpha 1 globin 129 Leu-->Pro unstable variant with thalassaemic phenotype. Br J Haematol. 1995 May;90(1):71-6.
  39. 8195005 Giordano PC, Harteveld CL, Streng H, Oosterwijk JC, Heister JG, Amons R, Bernini LF: Hb Kurdistan [alpha 47(CE5)Asp-->Tyr], a new alpha chain variant in combination with beta (0)-thalassemia. Hemoglobin. 1994 Jan;18(1):11-8.
  40. 8294199 Wajcman H, Kalmes G, Groff P, Prome D, Riou J, Galacteros F: Hb Melusine [alpha 114(GH2)Pro-->Ser]: a new neutral hemoglobin variant. Hemoglobin. 1993 Oct;17(5):397-405.
  41. 8294200 Wajcman H, Kister J, M'Rad A, Marden MC, Riou J, Galacteros F: Hb Val de Marne [alpha 133(H16)Ser-->Arg]: a new hemoglobin variant with moderate increase in oxygen affinity. Hemoglobin. 1993 Oct;17(5):407-17.
  42. 8448109 Kavanaugh JS, Moo-Penn WF, Arnone A: Accommodation of insertions in helices: the mutation in hemoglobin Catonsville (Pro 37 alpha-Glu-Thr 38 alpha) generates a 3(10)-->alpha bulge. Biochemistry. 1993 Mar 16;32(10):2509-13.
  43. 8745434 Harano T, Harano K, Imai K, Terunuma S: HB Swan River [alpha 6(A4)ASP-->Gly] observed in a Japanese man. Hemoglobin. 1996 Feb;20(1):75-8.
  44. 9322075 Brennan SO, Matthews JR: Hb Auckland [alpha 87(F8) His-->Asn]: a new mutation of the proximal histidine identified by electrospray mass spectrometry. Hemoglobin. 1997 Sep;21(5):393-403.
  45. 9452028 Wajcman H, Prehu MO, Prehu C, Blouquit Y, Prome D, Galacteros F: Hemoglobin Phnom Penh [alpha117Phe(H1)-Ile-alpha118Thr(H2)]; evidence for a hotspot for insertion of residues in the third exon of the alpha1-globin gene. Hum Mutat. 1998;Suppl 1:S20-2.
  46. 9494044 Wajcman H, Kister J, Riou J, Galacteros F, Girot R, Maier-Redelsperger M, Nayudu NV, Giordano PC: Hb Godavari [alpha 95(G2)Pro-->Thr]: a neutral amino acid substitution in the alpha 1 beta 2 interface that modifies the electrophoretic mobility of hemoglobin. Hemoglobin. 1998 Jan;22(1):11-22.
  47. 9665850 Sutherland-Smith AJ, Baker HM, Hofmann OM, Brittain T, Baker EN: Crystal structure of a human embryonic haemoglobin: the carbonmonoxy form of gower II (alpha2 epsilon2) haemoglobin at 2.9 A resolution. J Mol Biol. 1998 Jul 17;280(3):475-84.
Target 2 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 443
Target 3 Name Ferritin heavy chain
Target 3 Synonyms
  1. EC 1.16.3.1
  2. Ferritin H subunit
  3. Proliferation-inducing gene 15 protein
Target 3 Gene Name FTH1
Target 3 Protein Sequence >Ferritin heavy chain 
TTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSH
EEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKL
ATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDN
ES
Target 3 Number of Residues 185
Target 3 Molecular Weight 21095
Target 3 Theoretical pI 5.29
Target 3 GO Classification
Function
ion binding
cation binding
transition metal ion binding
iron ion binding
ferric iron binding
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
Not Available
Target 3 General Function Inorganic ion transport and metabolism
Target 3 Specific Function Stores iron in a soluble, nontoxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation
Target 3 Pathways
Name SMPDB Link KEGG Link
Porphyrin and chlorophyll metabolism map00860 Link Image
Target 3 Reactions
  • 4 Fe(II) + 4 H+ + O2 = 4 Fe(III) + 2 H2O
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 28435 Link Image
Target 3 UniProtKB/Swiss-Prot ID P02794 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name FRIH_HUMAN Link Image
Target 3 PDB ID 2FHA Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location Not Available
Target 3 Gene Sequence >573 bp 
ATGACGACCGCGTCCACCTCGCAGGTGCGCCAGAACTACCACCAGGACTCAGAGGCCGCC
ATCAACCGCCAGATCAACCTGGAGCTCTACGCCTCCTACGTTTACCTGTCCATGTCTTAC
TACTTTGACCGCGATGATGTGGCTTTGAAGAACTTTGCCAAATACTTTCTTCACCAATCT
CATGAGGAGAGGGAACATGCTGAGAAACTGATGAAGCTGCAGAACCAACGAGGTGGCCGA
ATCTTCCTTCAGGATATCAAGAAACCAGACTGTGATGACTGGGAGAGCGGGCTGAATGCA
ATGGAGTGTGCATTACATTTGGAAAAAAATGTGAATCAGTCACTACTGGAACTGCACAAA
CTGGCCACTGACAAAAATGACCCCCATTTGTGTGACTTCATTGAGACACATTACCTGAAT
GAGCAGGTGAAAGCCATCAAAGAATTGGGTGACCACGTGACCAACTTGCGCAAGATGGGA
GCGCCCGAATCTGGCTTGGCGGAATATCTCTTTGACAAGCACACCTGGGAGACAGTGATA
ATGAAAGCTAAGCCTCGGGCTAATTTCCCATAG
Target 3 GenBank Gene ID
Target 3 GeneCard ID FTH1 Link Image
Target 3 GenAtlas ID FTH1 Link Image
Target 3 HGNC ID HGNC:3976 Link Image
Target 3 Chromosome Location 11
Target 3 Locus 11q13
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Lawson DM, Artymiuk PJ, Yewdall SJ, Smith JM, Livingstone JC, Treffry A, Luzzago A, Levi S, Arosio P, Cesareni G, et al.: Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts. Nature. 1991 Feb 7;349(6309):541-4. [PubMed Link Image]
  2. Costanzo F, Colombo M, Staempfli S, Santoro C, Marone M, Frank R, Delius H, Cortese R: Structure of gene and pseudogenes of human apoferritin H. Nucleic Acids Res. 1986 Jan 24;14(2):721-36. [PubMed Link Image]
  3. Hentze MW, Keim S, Papadopoulos P, O'Brien S, Modi W, Drysdale J, Leonard WJ, Harford JB, Klausner RD: Cloning, characterization, expression, and chromosomal localization of a human ferritin heavy-chain gene. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7226-30. [PubMed Link Image]
  4. Chou CC, Gatti RA, Fuller ML, Concannon P, Wong A, Chada S, Davis RC, Salser WA: Structure and expression of ferritin genes in a human promyelocytic cell line that differentiates in vitro. Mol Cell Biol. 1986 Feb;6(2):566-73. [PubMed Link Image]
  5. Boyd D, Vecoli C, Belcher DM, Jain SK, Drysdale JW: Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones. J Biol Chem. 1985 Sep 25;260(21):11755-61. [PubMed Link Image]
  6. Costanzo F, Santoro C, Colantuoni V, Bensi G, Raugei G, Romano V, Cortese R: Cloning and sequencing of a full length cDNA coding for a human apoferritin H chain: evidence for a multigene family. EMBO J. 1984 Jan;3(1):23-7. [PubMed Link Image]
  7. Boyd D, Jain SK, Crampton J, Barrett KJ, Drysdale J: Isolation and characterization of a cDNA clone for human ferritin heavy chain. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4751-5. [PubMed Link Image]
  8. Dhar M, Chauthaiwale V, Joshi JG: Sequence of a cDNA encoding the ferritin H-chain from an 11-week-old human fetal brain. Gene. 1993 Apr 30;126(2):275-8. [PubMed Link Image]
  9. Hempstead PD, Yewdall SJ, Fernie AR, Lawson DM, Artymiuk PJ, Rice DW, Ford GC, Harrison PM: Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution. J Mol Biol. 1997 May 2;268(2):424-48. [PubMed Link Image]
Target 3 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. 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 4 [top]
Target 4 ID 566
Target 4 Name Serotransferrin
Target 4 Synonyms
  1. Beta-1-metal- binding globulin
  2. Serotransferrin precursor
  3. Siderophilin
  4. Transferrin
Target 4 Gene Name TF
Target 4 Protein Sequence >Serotransferrin precursor 
MRLAVGALLVCAVLGLCLAVPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVK
KASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVV
KKDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPC
ADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRD
QYELLCLDNTRKPVDEYKDCHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKE
FQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEAPTDECKP
VKWCALSHHERLKCDEWSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGK
CGLVPVLAENYNKSDNCEDTPEAGYFAVAVVKKSASDLTWDNLKGKKSCHTAVGRTAGWN
IPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYTGAF
RCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTRKPVEEYANCHLAR
APNHAVVTRKDKEACVHKILRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAKL
HDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP
Target 4 Number of Residues 709
Target 4 Molecular Weight 77050
Target 4 Theoretical pI 7.13
Target 4 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 4 General Function Involved in ferric iron binding
Target 4 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 4 Pathways Not Available
Target 4 Reactions Not Available
Target 4 Pfam Domain Function
Target 4 Signals
  • 1-19
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 339453 Link Image
Target 4 UniProtKB/Swiss-Prot ID P02787 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name TRFE_HUMAN Link Image
Target 4 PDB ID Not Available
Target 4 Cellular Location
  • Secreted protein
Target 4 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 4 GenBank Gene ID
Target 4 GeneCard ID TF Link Image
Target 4 GenAtlas ID TF Link Image
Target 4 HGNC ID HGNC:11740 Link Image
Target 4 Chromosome Location 3
Target 4 Locus 3q22.1
Target 4 SNPs SNPJam Report Link Image
Target 4 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 4 Drug References
  1. Macdougall IC: Strategies for iron supplementation: oral versus intravenous. Kidney Int Suppl. 1999 Mar;69:S61-6. [PubMed Link Image]
  2. Salahudeen AK, Oliver B, Bower JD, Roberts LJ 2nd: Increase in plasma esterified F2-isoprostanes following intravenous iron infusion in patients on hemodialysis. Kidney Int. 2001 Oct;60(4):1525-31. [PubMed Link Image]
  3. Pai AB, Boyd AV, McQuade CR, Harford A, Norenberg JP, Zager PG: Comparison of oxidative stress markers after intravenous administration of iron dextran, sodium ferric gluconate, and iron sucrose in patients undergoing hemodialysis. Pharmacotherapy. 2007 Mar;27(3):343-50. [PubMed Link Image]
  4. Jacobs JC, Alexander NM: Colorimetry and constant-potential coulometry determinations of transferrin-bound iron, total iron-binding capacity, and total iron in serum containing iron-dextran, with use of sodium dithionite and alumina columns. Clin Chem. 1990 Oct;36(10):1803-7. [PubMed Link Image]
  5. Speyer BE, Doney VJ, Fielding J: Transfer of iron from Ferastral and other organic complexes to transferrin as measured by reticulocyte uptake. Scand J Haematol Suppl. 1977;32:215-21. [PubMed Link Image]
Drug Target 5 [top]
Target 5 ID 693
Target 5 Name Hemoglobin subunit beta
Target 5 Synonyms
  1. Beta-globin
  2. Hemoglobin beta chain
Target 5 Gene Name HBB
Target 5 Protein Sequence >Hemoglobin subunit beta 
VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKV
KAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGK
EFTPPVQAAYQKVVAGVANALAHKYH
Target 5 Number of Residues 148
Target 5 Molecular Weight 15867
Target 5 Theoretical pI 7.32
Target 5 GO Classification
Function
tetrapyrrole binding
heme binding
binding
oxygen binding
Process
physiological process
cellular physiological process
transport
gas transport
oxygen transport
Component
protein complex
hemoglobin complex
Target 5 General Function Involved in iron ion binding
Target 5 Specific Function Involved in oxygen transport from the lung to the various peripheral tissues
Target 5 Pathways Not Available
Target 5 Reactions Not Available
Target 5 Pfam Domain Function
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • None
Target 5 Essentiality Non-Essential
Target 5 GenBank ID Protein 455997 Link Image
Target 5 UniProtKB/Swiss-Prot ID P68871 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name HBB_HUMAN Link Image
Target 5 PDB ID 1DXT Link Image
Target 5 PDB File Show
Target 5 3D Structure
Target 5 Cellular Location Not Available
Target 5 Gene Sequence >444 bp 
ATGGTGCACCTGACTCCTGAGGAGAAGTCTGCCGTTACTGCCCTGTGGGGCAAGGTGAAC
GTGGATGAAGTTGGTGGTGAGGCCCTGGGCAGGCTGCTGGTGGTCTACCCTTGGACCCAG
AGGTTCTTTGAGTCCTTTGGGGATCTGTCCACTCCTGATGCTGTTATGGGCAACCCTAAG
GTGAAGGCTCATGGCAAGAAAGTGCTCGGTGCCTTTAGTGATGGCCTGGCTCACCTGGAC
AACCTCAAGGGCACCTTTGCCACACTGAGTGAGCTGCACTGTGACAAGCTGCACGTGGAT
CCTGAGAACTTCAGGCTCCTGGGCAACGTGCTGGTCTGTGTGCTGGCCCATCACTTTGGC
AAAGAATTCACCCCACCAGTGCAGGCTGCCTATCAGAAAGTGGTGGCTGGTGTGGCTAAT
GCCCTGGCCCACAAGTATCACTAA
Target 5 GenBank Gene ID
Target 5 GeneCard ID HBB Link Image
Target 5 GenAtlas ID HBB Link Image
Target 5 HGNC ID HGNC:4827 Link Image
Target 5 Chromosome Location 11
Target 5 Locus 11p15.5
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Marotta CA, Forget BG, Cohen-Solal M, Weissman SM: Nucleotide sequence analysis of coding and noncoding regions of human beta-globin mRNA. Prog Nucleic Acid Res Mol Biol. 1976;19:165-75. [PubMed Link Image]
  2. Durner J, Gow AJ, Stamler JS, Glazebrook J: Ancient origins of nitric oxide signaling in biological systems. Proc Natl Acad Sci U S A. 1999 Dec 7;96(25):14206-7. [PubMed Link Image]
  3. Brimhall B, Jones RT, Schneider RG, Hosty TS, Tomlin G, Atkins R: Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys) and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg). Biochim Biophys Acta. 1975 Jan 30;379(1):28-32. [PubMed Link Image]
  4. Wilkinson T, Chua CG, Carrell RW, Robin H, Exner T, Lee KM, Kronenberg H: Haemoglobin Camperdown beta104(G6) arginine leads to serine. Biochim Biophys Acta. 1975 May 30;393(1):195-200. [PubMed Link Image]
  5. Fermi G: Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2-5 A resolution: refinement of the atomic model. J Mol Biol. 1975 Sep 15;97(2):237-56. [PubMed Link Image]
  6. Garel MC, Hassan W, Coquelet MT, Goossens M, Rosa J, Arous N: Hemoglobin J Cairo: beta 65 (E9) Lys leads to Gln, A new hemoglobin variant discovered in an Egyptian family. Biochim Biophys Acta. 1976 Jan 20;420(1):97-104. [PubMed Link Image]
  7. Murru S, Poddie D, Sciarratta GV, Agosti S, Baffico M, Melevendi C, Pirastu M, Cao A: A novel beta-globin structural mutant, Hb Brescia (beta 114 Leu-Pro), causing a severe beta-thalassemia intermedia phenotype. Hum Mutat. 1992;1(2):124-8. [PubMed Link Image]
  8. Liu JS, Molchanova TP, Gu LH, Wilson JB, Hopmeier P, Schnedl W, Balaun E, Krejs GJ, Huisman TH: Hb Graz or alpha 2 beta 2(2)(NA2)His-->Leu; a new beta chain variant observed in four families from southern Austria. Hemoglobin. 1992;16(6):493-501. [PubMed Link Image]
  9. Wajcman H, Blouquit Y, Vasseur C, Le Querrec A, Laniece M, Melevendi C, Rasore A, Galacteros F: Two new human hemoglobin variants caused by unusual mutational events: Hb Zaire contains a five residue repetition within the alpha-chain and Hb Duino has two residues substituted in the beta-chain. Hum Genet. 1992 Aug;89(6):676-80. [PubMed Link Image]
  10. Ramachandran M, Gu LH, Wilson JB, Kitundu MN, Adekile AD, Liu JC, McKie KM, Huisman TH: A new variant, HB Muscat [alpha 2 beta (2)32(B14)Leu----Val] observed in association with HB S in an Arabian family. Hemoglobin. 1992;16(4):259-66. [PubMed Link Image]
  11. 1540659 Wajcman H, Kister J, Vasseur C, Blouquit Y, Trastour JC, Cottenceau D, Galacteros F: Structure of the EF corner favors deamidation of asparaginyl residues in hemoglobin: the example of Hb La Roche-sur-Yon [beta 81 (EF5) Leu----His] Biochim Biophys Acta. 1992 Feb 14;1138(2):127-32.
  12. 1567857 Kavanaugh JS, Rogers PH, Case DA, Arnone A: High-resolution X-ray study of deoxyhemoglobin Rothschild 37 beta Trp----Arg: a mutation that creates an intersubunit chloride-binding site. Biochemistry. 1992 Apr 28;31(16):4111-21.
  13. 1634367 Harano T, Harano K, Kushida Y, Imai K, Nishinakamura R, Matsunaga T: Hb Kodaira [beta 146(HC3)His----Gln]: a new beta chain variant with an amino acid substitution at the C-terminus. Hemoglobin. 1992;16(1-2):85-91.
  14. 1787097 Harano T, Harano K, Kushida Y, Ueda S, Yoshii A, Nishinarita M: Hb Isehara (or Hb Redondo) [beta 92 (F8) His----Asn]: an unstable variant with a proximal histidine substitution at the heme contact. Hemoglobin. 1991;15(4):279-90.
  15. 1814856 Tamagnini GP, Ribeiro ML, Valente V, Ramachandran M, Wilson JB, Baysal E, Gu LH, Huisman TH: Hb Coimbra or alpha 2 beta (2)99(G1)Asp----Glu, a newly discovered highoxygen affinity variant. Hemoglobin. 1991;15(6):487-96.
  16. 1917530 Harano T, Harano K, Kushida Y, Ueda S: A new abnormal variant, Hb Yahata or beta 112(G14)Cys----Tyr, found in a Japanese: structural confirmation by DNA sequencing of the beta-globin gene. Hemoglobin. 1991;15(1-2):109-13.
  17. 1917537 Como PF, Wylie BR, Trent RJ, Bruce D, Volpato F, Wilkinson T, Kronenberg H, Holland RA, Tibben EA: A new unstable and low oxygen affinity hemoglobin variant: Hb Stanmore [beta 111(G13)Val----Ala] Hemoglobin. 1991;15(1-2):53-65.
  18. 1917539 Como PF, Hocking DR, Swinton GW, Trent RJ, Holland RA, Tibben EA, Wilkinson T, Kronenberg H: Hb Geelong [beta 139(H17)Asn----Asp] Hemoglobin. 1991;15(1-2):85-95.
  19. 2079435 Plaseska D, Wilson JB, Gu LH, Kutlar F, Huisman TH, Zeng YT, Shen M: Hb Zengcheng or alpha 2 beta(2)114(G16)Leu----Met. Hemoglobin. 1990;14(5):555-7.
  20. 2101840 Gaudry CL Jr, Pitel PA, Jue DL, Hine TK, Johnson MH, Moo-Penn WF: Hb Jacksonville [alpha 2 beta 2(54)(D5)Val----Asp]: a new unstable variant found in a patient with hemolytic anemia. Hemoglobin. 1990;14(6):653-9.
  21. 2384314 Sciarratta GV, Ivaldi G: Hb Matera [beta 55(D6)Met----Lys]: a new unstable hemoglobin variant in an Italian family. Hemoglobin. 1990;14(1):79-85.
  22. 2399911 Bardakdjian-Michau J, Fucharoen S, Delanoe-Garin J, Kister J, Lacombe C, Winichagoon P, Blouquit Y, Riou J, Wasi P, Galacteros F: Hemoglobin Dhonburi alpha 2 beta 2 126 (H4) Val----Gly: a new unstable beta variant producing a beta-thalassemia intermedia phenotype in association with beta zero-thalassemia. Am J Hematol. 1990 Oct;35(2):96-9.
  23. 2513289 Moo-Penn WF, Johnson MH, Jue DL, Lonser R: Hb Hinsdale [beta 139 (H17)Asn----Lys]: a variant in the central cavity showing reduced affinity for oxygen and 2,3-diphosphoglycerate. Hemoglobin. 1989;13(5):455-64.
  24. 2581851 Lang KM, Spritz RA: Cloning specific complete polyadenylylated 3'-terminal cDNA segments. Gene. 1985;33(2):191-6.
  25. 2599880 Gilbert AT, Fleming PJ, Sumner DR, Hughes WG, Holland RA, Tibben EA: Hemoglobin Windsor or beta 11 (A8)Val----Asp: a new unstable beta-chain hemoglobin variant producing a hemolytic anemia. Hemoglobin. 1989;13(5):437-53.
  26. 2634671 Lena-Russo D, Orsini A, Vovan L, Bardakdjian-Michau J, Lacombe C, Blouquit Y, Craescu CT, Galacteros F: Hb N-Timone [alpha 2 beta 2(8)(A5)Lys----Glu]: a new fast-moving variant with normal stability and oxygen affinity. Hemoglobin. 1989;13(7-8):743-7.
  27. 3384707 Gilbert AT, Fleming PJ, Sumner DR, Hughes WG, Ip F, Kwan YL, Holland RA: Hemoglobin Randwick or beta 15 (A12)Trp----Gly: a new unstable beta-chain hemoglobin variant. Hemoglobin. 1988;12(2):149-61.
  28. 3384708 Malcorra-Azpiazu JJ, Balda-Aguirre MI, Diaz-Chico JC, Hu H, Wilson JB, Webber BB, Kutlar F, Kutlar A, Huisman TH: Hb Las Palmas or alpha 2 beta 2(49)(CD8)Ser----Phe, a mildly unstable hemoglobin variant. Hemoglobin. 1988;12(2):163-70.
  29. 3384709 Baklouti F, Giraud Y, Francina A, Richard G, Favre-Gilly J, Delaunay J: Hemoglobin Pierre-Benite [beta 90(F6)Glu----Asp], a new high affinity variant found in a French family. Hemoglobin. 1988;12(2):171-7.
  30. 3384710 Baudin-Chich V, Wajcman H, Gombaud-Saintonge G, Arous N, Riou J, Briere J, Galacteros F: Hemoglobin Brest [beta 127 (H5)Gln----Lys] a new unstable human hemoglobin variant located at the alpha 1 beta 1 interface with specific electrophoretic behavior. Hemoglobin. 1988;12(2):179-88.
  31. 3557994 Merault G, Keclard L, Garin J, Poyart C, Blouquit Y, Arous N, Galacteros F, Feingold J, Rosa J: Hemoglobin La Desirade alpha A2 beta 2 129 (H7) Ala----Val: a new unstable hemoglobin. Hemoglobin. 1986;10(6):593-605.
  32. 3623975 Indrak K, Wiedermann BF, Batek F, Wilson JB, Webber BB, Kutlar A, Huisman TH: Hb Olomouc or alpha 2 beta 2(86)(F2)Ala----Asp, a new high oxygen affinity variant. Hemoglobin. 1987;11(2):151-5.
  33. 3654265 Williamson D, Wells RM, Anderson R, Matthews J: A new unstable and low oxygen affinity hemoglobin variant: Hb J-Auckland [beta 25(B7)Gly----Asp]. Hemoglobin. 1987;11(3):221-30.
  34. 3666141 Baklouti F, Giraud Y, Francina A, Richard G, Perier C, Geyssant A, Jaubert J, Brizard C, Delaunay J: Hemoglobin Grange-Blanche [beta 27(B9) Ala----Val], a new variant with normal expression and increased affinity for oxygen. FEBS Lett. 1987 Oct 19;223(1):59-62.
  35. 3691763 Berlin G, Wranne B, Jeppsson JO: Hb Linkoping (beta 36 Pro----Thr): a new high oxygen affinity hemoglobin variant found in two families of Finnish origin. Eur J Haematol. 1987 Nov;39(5):452-6.
  36. 3707969 Huisman TH, Wilson JB, Kutlar A, Yang KG, Chen SS, Webber BB, Altay C, Martinez AV: Hb J-Antakya or alpha 2 beta (2)65(E9)Lys----Met in a Turkish family and Hb complutense or alpha 2 beta (2)127(H5)Gln----Glu in a Spanish family; correction of a previously published identification. Biochim Biophys Acta. 1986 Jun 5;871(2):229-31.
  37. 3718478 Yoshioka N, Atassi MZ: Haemoglobin binding with haptoglobin. Localization of the haptoglobin-binding sites on the beta-chain of human haemoglobin by synthetic overlapping peptides encompassing the entire chain. Biochem J. 1986 Mar 1;234(2):453-6.
  38. 3744871 Harano T, Harano K, Ueda S, Imai N, Kitazumi T: A new electrophoretically-silent hemoglobin variant: hemoglobin Kofu or alpha 2 beta 2 84 (EF8) Thr----Ile. Hemoglobin. 1986;10(4):417-20.
  39. 3754244 Ohba Y, Miyaji T, Murakami M, Kadowaki S, Fujita T, Oimomi M, Hatanaka H, Ishikawa K, Baba S, Hitaka K, et al.: Hb Himeji or beta 140 (H18) Ala----Asp. A slightly unstable hemoglobin with increased beta N-terminal glycation. Hemoglobin. 1986;10(2):109-25.
  40. 3838976 Ohba Y, Imanaka M, Matsuoka M, Hattori Y, Miyaji T, Funaki C, Shibata K, Shimokata H, Kuzuya F, Miwa S: A new unstable, high oxygen affinity hemoglobin: Hb Nagoya or beta 97 (FG4) His----Pro. Hemoglobin. 1985;9(1):11-24.
  41. 3937824 Rahbar S, Louis J, Lee T, Asmerom Y: Hemoglobin North Chicago (beta 36 [C2] proline----serine): a new high affinity hemoglobin. Hemoglobin. 1985;9(6):559-76.
  42. 4129558 Adams JG 3rd, Winter WP, Tausk K, Heller P: Hemoglobin Rush (beta 101 (g3) glutamine): a new unstable hemoglobin causing mild hemolytic anemia. Blood. 1974 Feb;43(2):261-9.
  43. 429365 Adams JG, Steinberg MH, Boxer LA, Baehner RL, Forget BG, Tsistrakis GA: The structure of hemoglobin Indianapolis [beta112(G14) arginine]. An unstable variant detectable only by isotopic labeling. J Biol Chem. 1979 May 10;254(9):3479-82.
  44. 4639022 Aksoy M, Erdem S, Efremov GD, Wilson JB, Huisman TH, Schroeder WA, Shelton JR, Shelton JB, Ulitin ON, Muftuoglu A: Hemoglobin Istanbul: substitution of glutamine for histidine in a proximal histidine (F8(92) ). J Clin Invest. 1972 Sep;51(9):2380-7.
  45. 4850241 Arcasoy A, Casey R, Lehmann H, Cavdar AO, Berki A: A new haemoglobin J from Turkey--Hb Ankara (beta10 (A7) Ala-Asp). FEBS Lett. 1974 Jun 1;42(2):121-3.
  46. 4852224 Ricco G, Pich PG, Mazza U, Rossi G, Ajmar F, Arese P, Gallo E: Hb J Sicilia: beta 65 (E9) Lys-Asn, a beta homologue of Hb Zambia. FEBS Lett. 1974 Feb 15;39(2):200-4.
  47. 6166590 Brennan SO, Wells RM, Smith H, Carrell RW: Hemoglobin Brisbane: beta68 Leu replaced by His. A new high oxygen affinity variant. Hemoglobin. 1981;5(4):325-35.
  48. 6254664 Lawn RM, Efstratiadis A, O'Connell C, Maniatis T: The nucleotide sequence of the human beta-globin gene. Cell. 1980 Oct;21(3):647-51.
  49. 635569 Bunn HF, Gabbay KH, Gallop PM: The glycosylation of hemoglobin: relevance to diabetes mellitus. Science. 1978 Apr 7;200(4337):21-7.
  50. 6434492 Rahbar S, Asmerom Y, Blume KG: A silent hemoglobin variant detected by HPLC: hemoglobin City of Hope beta 69 (E13) Gly----Ser. Hemoglobin. 1984;8(4):333-42.
  51. 6526653 Moo-Penn WF, Johnson MH, McGuffey JE, Jue DL: Hemoglobin Shelby [beta 131(H9) Gln----Lys] a correction to the structure of hemoglobin Deaconess and hemoglobin Leslie. Hemoglobin. 1984;8(6):583-93.
  52. 6618888 Lu YQ, Fan JL, Liu JF, Hu HL, Peng XH, Huang CH, Huang PY, Chen SS, Jai PC, Yang KG, et al.: Hemoglobin Jianghua [beta 120(GH3) LYS leads to ILE]: a new fast-moving variant found in China. Hemoglobin. 1983;7(4):321-6.
  53. 6629822 Jen PC, Chen LC, Chen PF, Wong Y, Chen LF, Guo YY, Chang FQ, Chow YC, Chiu Y: Hemoglobin Quin-Hai, beta 78 (EF2) Leu replaced by Arg, a new abnormal hemoglobin found in Guangdong, China. Hemoglobin. 1983;7(5):407-12.
  54. 6629823 Como PF, Kennett D, Wilkinson T, Kronenberg H: A new hemoglobin with high oxygen affinity--hemoglobin bunbury: alpha 2 beta 2 [94 (FG1) Asp replaced by Asn] Hemoglobin. 1983;7(5):413-21.
  55. 6629824 Marinucci M, Boissel JP, Massa A, Wajcman H, Tentori L, Labie D: Hemoglobin Maputo: a new beta-chain variant (alpha 2 beta 2 47 (CD6) Asp replaced by Tyr) in combination with hemoglobin S, identified by high performance liquid chromatography (HPLC). Hemoglobin. 1983;7(5):423-33.
  56. 6687721 Ohba Y, Hasegawa Y, Amino H, Miwa S, Nakatsuji T, Hattori Y, Miyaji T: Hemoglobin saitama or beta 117 (G19) His leads to Pro, a new variant causing hemolytic disease. Hemoglobin. 1983;7(1):47-56.
  57. 668922 Moo-Penn WF, Wolff JA, Simon G, Vacek M, Jue DL, Johnson MH: Hemoglobin Presbyterian: beta108 (G10) asparagine leads to lysine, A hemoglobin variant with low oxygen affinity. FEBS Lett. 1978 Aug 1;92(1):53-6.
  58. 6857757 Moo-Penn WF, Johnson MH, McGuffey JE, Jue DL, Therrell BL Jr: Hemoglobin Rio Grande [beta 8 (A5) Lys leads to Thr] a new variant found in a Mexican-American family. Hemoglobin. 1983;7(1):91-5.
  59. 7161106 Brennan SO, Williamson D, Whisson ME, Carrell RW: Hemoglobin Palmerston North beta 23 (B5) Val replaced by Phe. A new variant identified in a patient with polycythemia. Hemoglobin. 1982;6(6):569-75.
  60. 7173395 Arous N, Galacteros F, Fessas P, Loukopoulos D, Blouquit Y, Komis G, Sellaye M, Boussiou M, Rosa J: Structural study of hemoglobin Knossos, beta 27 (B9) Ala leads to Ser. A new abnormal hemoglobin present as a silent beta-thalassemia. FEBS Lett. 1982 Oct 18;147(2):247-50.
  61. 721609 Adams JG 3rd, Przywara KP, Heller P, Shamsuddin M: Hemoglobin J Altgeld Gardens. A hemoglobin variant with a substitution of the proximal histidine of the beta-chain. Hemoglobin. 1978;2(5):403-15.
  62. 7238856 Arous N, Braconnier F, Thillet J, Blouquit Y, Galacteros F, Chevrier M, Bordahandy C, Rosa J: Hemoglobin Saint Mande beta 102 (G4) asn replaced by tyr: a new low oxygen affinity variant. FEBS Lett. 1981 Apr 6;126(1):114-6.
  63. 7338468 Nakatsuji T, Miwa S, Ohba Y, Hattori Y, Miyaji T, Miyata H, Shinohara T, Hori T, Takayama J: Hemoglobin Miyashiro (beta 23[B5] val substituting for gly) an electrophoretically silent variant discovered by the isopropanol test. Hemoglobin. 1981;5(7-8):653-66.
  64. 7338469 Nakatsuji T, Miwa S, Ohba Y, Hattori Y, Miyaji T, Hino S, Matsumoto N: A new unstable hemoglobin, Hb Yokohama beta 31 (B13)Leu substituting for Pro, causing hemolytic anemia. Hemoglobin. 1981;5(7-8):667-78.
  65. 7693620 Divoky V, Svobodova M, Indrak K, Chrobak L, Molchanova TP, Huisman TH: Hb Hradec Kralove (Hb HK) or alpha 2 beta 2 115(G17)Ala-->Asp, a severely unstable hemoglobin variant resulting in a dominant beta-thalassemia trait in a Czech family. Hemoglobin. 1993 Aug;17(4):319-28.
  66. 8111050 de Castro CM, Devlin B, Fleenor DE, Lee ME, Kaufman RE: A novel beta-globin mutation, beta Durham-NC [beta 114 Leu-->Pro], produces a dominant thalassemia-like phenotype. Blood. 1994 Feb 15;83(4):1109-16.
  67. 8144352 Owen MC, Ockelford PA, Wells RM: Hb Howick [beta 37(C3)Trp-->Gly]: a new high oxygen affinity variant of the alpha 1 beta 2 contact. Hemoglobin. 1993 Dec;17(6):513-21.
  68. 826083 Ikkala E, Koskela J, Pikkarainen P, Rahiala EL, El-Hazmi MA, Nagai K, Lang A, Lehmann H: Hb Helsinki: a variant with a high oxygen affinity and a substitution at a 2,3-DPG binding site (beta82[EF6] Lys replaced by Met). Acta Haematol. 1976;56(5):257-75.
  69. 8330972 Landin B: Hb Karlskoga or alpha 2 beta (2)21(B3) Asp-->His: a new slow-moving variant found in Sweden. Hemoglobin. 1993 Jun;17(3):201-8.
  70. 8330974 Molchanova TP, Postnikov YuV, Pobedimskaya DD, Smetanina NS, Moschan AA, Kazanetz EG, Tokarev YuN, Huisman TH: Hb Alesha or alpha 2 beta (2)67(E11)Val-->Met: a new unstable hemoglobin variant identified through sequencing of amplified DNA. Hemoglobin. 1993 Jun;17(3):217-25.
  71. 8330979 Welch SG, Bateman C: Hb D-Neath or beta 121 (GH4) Glu-->Ala: a new member of the Hb D family. Hemoglobin. 1993 Jun;17(3):255-9.
  72. 8522332 Wajcman H, Girodon E, Prome D, North ML, Plassa F, Duwig I, Kister J, Bergerat JP, Oberling F, Lampert E, et al.: Germline mosaicism for an alanine to valine substitution at residue beta 140 in hemoglobin Puttelange, a new variant with high oxygen affinity. Hum Genet. 1995 Dec;96(6):711-6.
  73. 8602627 Lacan P, Kister J, Francina A, Souillet G, Galacteros F, Delaunay J, Wajcman H: Hemoglobin Debrousse (beta 96[FG3]Leu-->Pro): a new unstable hemoglobin with twofold increased oxygen affinity. Am J Hematol. 1996 Apr;51(4):276-81.
  74. 8641705 Rodriguez Romero WE, Castillo M, Chaves MA, Saenz GF, Gu LH, Wilson JB, Baysal E, Smetanina NS, Leonova JY, Huisman TH: Hb Costa Rica or alpha 2 beta 2 77(EF1)His --> Arg: the first example of a somatic cell mutation in a globin gene. Hum Genet. 1996 Jun;97(6):829-33.
  75. 8718692 Lafferty J, Ali M, Matthew K, Eng B, Patterson M, Waye JS: Identification of a new high oxygen affinity hemoglobin variant: Hb Aurora [beta 139(H17) Asn-->Tyr] Hemoglobin. 1995;19(6):335-41.
  76. 8745430 Frischknecht H, Ventruto M, Hess D, Hunziker P, Rosatelli MC, Cao A, Breitenstein U, Fehr J, Tuchschmid P: HB Hinwil or beta 38(C4)Thr-->Asn: a new beta chain variant detected in a Swiss family. Hemoglobin. 1996 Feb;20(1):31-40.
  77. 8811317 Kiger L, Kister J, Groff P, Kalmes G, Prome D, Galacteros F, Wajcman H: Hb J-Europa [beta 62(E6)Ala-->Asp]: normal oxygen binding properties in a new variant involving a residue located distal to the heme. Hemoglobin. 1996 May;20(2):135-40.
  78. 891976 Arends T, Lehmann H, Plowman D, Stathopoulou R: Haemoglobin North Shore-Caracas beta 134 (H12) valine replaced by glutamic acid. FEBS Lett. 1977 Aug 15;80(2):261-5.
  79. 893142 Ohba Y, Miyaji T, Matsuoka M, Sugiyama K, Suzuki T, Sugiura T: Hemoglobin Mizuho or beta 68 (E 12) leucine leads to proline, a new unstable variant associated with severe hemolytic anemia. Hemoglobin. 1977;1(5):467-77.
  80. 9761252 Bisse E, Zorn N, Eigel A, Lizama M, Huaman-Guillen P, Marz W, Van Dorsselaer A, Wieland H: Hemoglobin Rambam (beta69[E13]Gly-->Asp), a pitfall in the assessment of diabetic control: characterization by electrospray mass spectrometry and HPLC. Clin Chem. 1998 Oct;44(10):2172-7.
  81. 9843411 Chan NL, Rogers PH, Arnone A: Crystal structure of the S-nitroso form of liganded human hemoglobin. Biochemistry. 1998 Nov 24;37(47):16459-64.
  82. 992050 Ahern E, Ahern V, Hilton T, Serjeant GR, Serjeant BE, Seakins M, Lang A, Middleton A, Lehmann H: Haemoglobin caribbean beta91 (F7) Leu replaced by Arg: a mildly haemoglobin with a low oxygen affinity. FEBS Lett. 1976 Oct 15;69(1):99-102.
Target 5 Drug References
  1. Zaric J, Lazic D, Markovic S, Glisin V, Ivanovic Z, Milenkovic P, Popovic Z: Alpha- and beta-globins of the anemic Belgrade laboratory rat. II. The effect of hemin and iron-dextran treatment. Hemoglobin. 1998 May;22(3):231-44. [PubMed Link Image]

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