IthaID: 669

Names and Sequences

Functionality: Globin gene causative mutation Pathogenicity: Pathogenic / Likely Pathogenic
Common Name: CD 92 CGG>CTG [Arg>Leu] HGVS Name: HBA2:c.278G>T
Hb Name: Hb Chesapeake Protein Info: α2 92(FG4) Arg>Leu

Context nucleotide sequence:

Protein sequence:

Also known as:

Comments: Hb Chesapeake displays high oxygen affinity and presents with erythrocytosis in heterozygous individuals. It affects the amino acids involved in the α1-β2 chains’ contact, and impairs the normal rotational transition from the deoxygenated low-affinity state to the oxygenated high-affinity state, tending to lock the hemoglobin into the high-affinity relaxed state. It has been described in

We follow the HGVS sequence variant nomenclature and IUPAC standards.


Hemoglobinopathy Group: Structural Haemoglobinopathy
Hemoglobinopathy Subgroup: α-chain variant
Allele Phenotype:N/A
Stability: Unstable
Oxygen Affinity: Increased Oxygen Affinity
Associated Phenotypes: N/A


Chromosome: 16
Locus: NG_000006.1
Locus Location: 34170
Size: 1 bp
Located at: α2
Specific Location: Exon 2

Other details

Type of Mutation: Point-Mutation(Substitution)
Effect on Gene/Protein Function: Missense codons (Protein Structure)
Ethnic Origin: German, Irish, Japanese, French
Molecular mechanism: N/A
Inheritance: Recessive
DNA Sequence Determined: Yes

In silico pathogenicity prediction

Sequence Viewer

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Publications / Origin

  1. Clegg JB, Naughton MA, Weatherball DJ, Abnormal human haemoglobins. Separation and characterization of the alpha and beta chains by chromatography, and the determination of two new variants, hb Chesapeak and hb J (Bangkok)., Journal of molecular biology, 19(1), 91-108, 1966 PubMed
  2. Charache S, Weatherall DJ, Clegg JB, Polycythemia associated with a hemoglobinopathy., J. Clin. Invest. , 45(6), 813-22, 1966 PubMed
  3. Greer J, Three-dimensional structure of abnormal human haemoglobins Chesapeake and J Capetown., J. Mol. Biol. , 62(1), 241-9, 1971 PubMed
  4. Gibson QH, Nagel RL, Allosteric transition and ligand binding in hemoglobin Chesapeake., J. Biol. Chem. , 249(22), 7255-9, 1974 PubMed
  5. Imai K, Hemoglobin Chesapeake (92 alpha, arginine--leucine). Precise measurements and analyses of oxygen equilibrium., J. Biol. Chem. , 249(23), 7607-12, 1974 PubMed
  6. Jones CM, Charache S, Hathaway PJ, The effect of hemoglobin F-Chesapeake (alpha 2 92 Arg. leads to Leu gamma 2) on fetal oxygen affinity and erythropoiesis., Pediatr. Res. , 13(7), 851-3, 1979 PubMed
  7. Harano T, Harano K, Shibata S, Ueda S, Mori H, Imai K, Hb Chesapeake [alpha 92 (FG 4) Arg replaced by Leu] and Hb J Cape Town [alpha 92 (FG 4) Arg leads to Gln] first discovered in Japanese., Hemoglobin , 7(5), 461-5, 1983 PubMed
  8. Granel B, Serratrice J, Badens C, Lena-Russo D, Disdier P, Weiller PJ, A new case of hemoglobin Chesapeake., Haematologica , 86(1), 105, 2001 PubMed
Created on 2010-06-16 16:13:16, Last reviewed on 2023-11-08 15:23:11 (Show full history)

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