Biology:HBE1

Generic protein structure example

Hemoglobin subunit epsilon is a protein that in humans is encoded by the HBE1 gene.

Function

The epsilon globin gene (HBE) is normally expressed in the embryonic yolk sac: two epsilon chains together with two zeta chains (an alpha-like globin) constitute the embryonic hemoglobin Hb Gower I; two epsilon chains together with two alpha chains form the embryonic Hb Gower II. Both of these embryonic hemoglobins are normally supplanted by fetal, and later, adult hemoglobin. The five beta-like globin genes are found within a 45 kb cluster on chromosome 11 in the following order: 5' - epsilon – gamma-G – gamma-A – delta – beta - 3'.

See also

• Hemoglobin
• Human β-globin locus
• Hemoglobin alpha chains (two genes, same sequence):
  • HBA1
  • HBA2

Further reading

• Clegg JB (1982). "Embryonic hemoglobin: sequence of the epsilon and zeta chains.". Tex. Rep. Biol. Med. 40: 23–8. PMID 6172865. 
• "The multiple functions of hemoglobin.". Crit. Rev. Biochem. Mol. Biol. 30 (3): 165–96. 1995. doi:10.3109/10409239509085142. PMID 7555018. 
• "beta 0 thalassemia, a nonsense mutation in man.". Proc. Natl. Acad. Sci. U.S.A. 76 (6): 2886–9. 1979. doi:10.1073/pnas.76.6.2886. PMID 88735. Bibcode: 1979PNAS...76.2886C. 
• "Molecular cloning of human epsilon-globin gene.". Proc. Natl. Acad. Sci. U.S.A. 76 (11): 5435–9. 1980. doi:10.1073/pnas.76.11.5435. PMID 160554. 
• "3' non-coding region sequences in eukaryotic messenger RNA.". Nature 263 (5574): 211–4. 1976. doi:10.1038/263211a0. PMID 822353. Bibcode: 1976Natur.263..211P. 
• "Human beta-globin messenger RNA. I. Nucleotide sequences derived from complementary RNA.". J. Biol. Chem. 252 (14): 5019–31. 1977. doi:10.1016/S0021-9258(17)40154-2. PMID 873928. 
• "G to A substitution in the distal CCAAT box of the A gamma-globin gene in Greek hereditary persistence of fetal haemoglobin.". Nature 313 (6000): 323–5. 1985. doi:10.1038/313323a0. PMID 2578619. Bibcode: 1985Natur.313..323G. 
• "A point mutation in the A gamma-globin gene promoter in Greek hereditary persistence of fetal haemoglobin.". Nature 313 (6000): 325–6. 1985. doi:10.1038/313325a0. PMID 2578620. Bibcode: 1985Natur.313..325C. 
• "Cloning specific complete polyadenylylated 3'-terminal cDNA segments.". Gene 33 (2): 191–6. 1985. doi:10.1016/0378-1119(85)90093-9. PMID 2581851. 
• "Globin gene expression in erythroid human fetal liver cells.". J. Clin. Invest. 83 (3): 1032–8. 1989. doi:10.1172/JCI113944. PMID 2921315. 
• "The 3' splice site of pre-messenger RNA is recognized by a small nuclear ribonucleoprotein.". Science 230 (4732): 1344–9. 1986. doi:10.1126/science.2933810. PMID 2933810. 
• "Direct sequencing of enzymatically amplified human genomic DNA.". Proc. Natl. Acad. Sci. U.S.A. 85 (2): 544–8. 1988. doi:10.1073/pnas.85.2.544. PMID 3267215. Bibcode: 1988PNAS...85..544E. 
• "Beta-thalassemia due to a T----A mutation within the ATA box.". Biochem. Biophys. Res. Commun. 153 (2): 741–7. 1988. doi:10.1016/S0006-291X(88)81157-4. PMID 3382401. 
• "Hemoglobin Long Island is caused by a single mutation (adenine to cytosine) resulting in a failure to cleave amino-terminal methionine.". Proc. Natl. Acad. Sci. U.S.A. 83 (1): 24–7. 1986. doi:10.1073/pnas.83.1.24. PMID 3455755. Bibcode: 1986PNAS...83...24P. 
• "mRNA precursor splicing in vivo: sequence requirements determined by deletion analysis of an intervening sequence.". Proc. Natl. Acad. Sci. U.S.A. 82 (9): 2885–9. 1985. doi:10.1073/pnas.82.9.2885. PMID 3857622. Bibcode: 1985PNAS...82.2885V. 
• "Cryptic branch point activation allows accurate in vitro splicing of human beta-globin intron mutants.". Cell 41 (3): 833–44. 1985. doi:10.1016/S0092-8674(85)80064-7. PMID 3879973. 
• "The "beta-like-globin" gene domain in human erythroid cells.". Proc. Natl. Acad. Sci. U.S.A. 82 (19): 6384–8. 1985. doi:10.1073/pnas.82.19.6384. PMID 3879975. Bibcode: 1985PNAS...82.6384T. 
• "Base substitution at position -88 in a beta-thalassemic globin gene. Further evidence for the role of distal promoter element ACACCC.". J. Biol. Chem. 259 (14): 8679–81. 1984. doi:10.1016/S0021-9258(17)47203-6. PMID 6086605. 

This article incorporates text from the United States National Library of Medicine, which is in the public domain.