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Associate Editor(s)-in-Chief: Henry A. Hoff

Hemoglobin, alpha 1
PBB Protein HBA1 image.jpg
PDB rendering based on 1a00.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Symbols HBA1 ; CD31; MGC126895; MGC126897; HBA1
External IDs Template:OMIM5 Template:MGI HomoloGene469
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Hemoglobin, alpha 1, also known as HBA1, is a human gene encoding the hemoglobin protein.

"The human alpha globin gene cluster located on chromosome 16 spans about 30 kb and includes seven loci: 5'- zeta - pseudozeta - mu - pseudoalpha-1 - alpha-2 - alpha-1 - theta - 3'. The alpha-2 (HBA2) and alpha-1 (HBA1) coding sequences are identical. These genes differ slightly over the 5' untranslated regions and the introns, but they differ significantly over the 3' untranslated regions. Two alpha chains plus two beta chains constitute HbA, which in normal adult life comprises about 97% of the total hemoglobin; alpha chains combine with delta chains to constitute HbA-2, which with HbF (fetal hemoglobin) makes up the remaining 3% of adult hemoglobin. Alpha thalassemias result from deletions of each of the alpha genes as well as deletions of both HBA2 and HBA1; some nondeletion alpha thalassemias have also been reported."[1]



"The 3' flanking area contained the highly conserved hexanucleotide sequence A-A-T-A-A-A found in eukaryotic messages between the terminator codon and the polyadenylylation site (44)."[2]


  1. RefSeq (July 2008). HBA1 hemoglobin subunit alpha 1 [ Homo sapiens (human) ]. 8600 Rockville Pike, Bethesda MD, 20894 USA: National Center for Biotechnology Information, U.S. National Library of Medicine. Retrieved 2017-02-04.
  2. Stephen A. Liebhaber, Michel J. Goossens, and Yuet Wai Kan (December 1980). "Cloning and complete nucleotide sequence of human 5'-α-globin gene" (PDF). Proceedings of the National Academy of Science USA. 77 (12): 7054–8. Retrieved 2013-06-28.

Further reading

  • Schillirò G, Russo-Mancuso G, Dibenedetto SP; et al. (1992). "Six rare hemoglobin variants found in Sicily". Hemoglobin. 15 (5): 431–7. PMID 1802885.
  • Higgs DR, Vickers MA, Wilkie AO; et al. (1989). "A review of the molecular genetics of the human alpha-globin gene cluster". Blood. 73 (5): 1081–104. PMID 2649166.
  • Giardina B, Messana I, Scatena R, Castagnola M (1995). "The multiple functions of hemoglobin". Crit. Rev. Biochem. Mol. Biol. 30 (3): 165–96. PMID 7555018.
  • Yalçin A, Avcu F, Beyan C; et al. (1995). "A case of HB J-Meerut (or Hb J-Birmingham) [alpha 120(H3)Ala-->Glu]". Hemoglobin. 18 (6): 433–5. PMID 7713747.
  • Turbpaiboon C, Svasti S, Sawangareetakul P; et al. (2002). "Hb Siam [alpha15(A13)Gly-->Arg (alpha1) (GGT-->CGT)] is a typical alpha chain hemoglobinopathy without an alpha-thalassemic effect". Hemoglobin. 26 (1): 77–81. PMID 11939517.


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