Hemoglobin, alpha 1

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Hemoglobin, alpha 1
Protein HBA1 PDB 1a00.png
PDB rendering based on 1a00.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols HBA1 ; HBA-T3; HBH
External IDs OMIM141800 MGI96015 HomoloGene469 ChEMBL: 2887 GeneCards: HBA1 Gene
Species Human Mouse
Entrez 3039 15122
Ensembl ENSG00000206172 ENSMUSG00000069919
UniProt P69905 Q91VB8
RefSeq (mRNA) NM_000558 NM_008218
RefSeq (protein) NP_000549 NP_032244
Location (UCSC) Chr 16:
0.18 – 0.18 Mb
Chr 11:
32.28 – 32.28 Mb
PubMed search [1] [2]

Hemoglobin, alpha 1, also known as HBA1, is a hemoglobin protein that in humans is encoded by the HBA1 gene.[1]


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; this gene) 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.[1]


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.[1]

Clinical significance[edit]

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]


Hemoglobin, alpha 1 has been shown to interact with HBB.[2][3]


  1. ^ a b c d "Entrez Gene: HBA1 hemoglobin, alpha 1". 
  2. ^ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070. 
  3. ^ Shaanan B (November 1983). "Structure of human oxyhaemoglobin at 2.1 A resolution". J. Mol. Biol. 171 (1): 31–59. doi:10.1016/S0022-2836(83)80313-1. PMID 6644819. 

Further reading[edit]

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