Hemoglobin subunit alpha

HBA1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1A00, 1A01, 1A0U, 1A0Z, 1A3N, 1A3O, 1A9W, 1ABW, 1ABY, 1AJ9, 1B86, 1BAB, 1BBB, 1BIJ, 1BUW, 1BZ0, 1BZ1, 1BZZ, 1C7B, 1C7C, 1C7D, 1CLS, 1CMY, 1COH, 1DKE, 1DXT, 1DXU, 1DXV, 1FDH, 1FN3, 1G9V, 1GBU, 1GBV, 1GLI, 1GZX, 1HAB, 1HAC, 1HBA, 1HBB, 1HBS, 1HCO, 1HDB, 1HGA, 1HGB, 1HGC, 1HHO, 1IRD, 1J3Y, 1J3Z, 1J40, 1J41, 1J7S, 1J7W, 1J7Y, 1JY7, 1K0Y, 1K1K, 1KD2, 1LFL, 1LFQ, 1LFT, 1LFV, 1LFY, 1LFZ, 1LJW, 1M9P, 1MKO, 1NEJ, 1NIH, 1NQP, 1O1I, 1O1J, 1O1K, 1O1L, 1O1M, 1O1N, 1O1O, 1O1P, 1QI8, 1QSH, 1QSI, 1QXD, 1QXE, 1R1X, 1R1Y, 1RPS, 1RQ3, 1RQ4, 1RQA, 1RVW, 1SDK, 1SDL, 1SHR, 1SI4, 1THB, 1UIW, 1VWT, 1XXT, 1XY0, 1XYE, 1XZ2, 1XZ4, 1XZ5, 1XZ7, 1XZU, 1XZV, 1Y01, 1Y09, 1Y0A, 1Y0C, 1Y0D, 1Y0T, 1Y0W, 1Y22, 1Y2Z, 1Y31, 1Y35, 1Y45, 1Y46, 1Y4B, 1Y4F, 1Y4G, 1Y4P, 1Y4Q, 1Y4R, 1Y4V, 1Y5F, 1Y5J, 1Y5K, 1Y7C, 1Y7D, 1Y7G, 1Y7Z, 1Y83, 1Y85, 1Y8W, 1YDZ, 1YE0, 1YE1, 1YE2, 1YEN, 1YEO, 1YEQ, 1YEU, 1YEV, 1YFF, 1YG5, 1YGD, 1YGF, 1YH9, 1YHE, 1YHR, 1YIE, 1YIH, 1YVQ, 1YVT, 1YZI, 1Z8U, 2D5Z, 2D60, 2DN1, 2DN2, 2DN3, 2DXM, 2H35, 2HBC, 2HBD, 2HBE, 2HBF, 2HBS, 2HCO, 2HHD, 2HHE, 2M6Z, 2W6V, 2W72, 2YRS, 3B75, 3D17, 3D7O, 3DUT, 3HXN, 3IA3, 3IC0, 3IC2, 3KMF, 3NL7, 3NMM, 3ODQ, 3ONZ, 3OO4, 3OO5, 3OVU, 3P5Q, 3QJB, 3QJC, 3QJD, 3QJE, 3R5I, 3S48, 3S65, 3S66, 3SZK, 3WCP, 3WHM, 4FC3, 4HHB, 4IJ2, 4L7Y, 4M4A, 4M4B, 4MQC, 4MQG, 4MQH, 4MQI, 4MQJ, 4MQK, 4N7N, 4N7O, 4N7P, 4N8T, 4NI0, 4NI1, 4ROL, 4ROM, 4WJG, 4X0L, 4XS0, 6HBW, 5E29, 5E6E, 5EE4, 5HU6, 5JDO, 5KDQ, 5E83,%%s1Y01, 1Z8U, 1BZ1
Identifiers
Aliases	HBA1, HBA-T3, HBH, hemoglobin subunit alpha 1, METHBA, ECYT7
External IDs	OMIM: 141800; MGI: 96015; HomoloGene: 469; GeneCards: HBA1; OMA:HBA1 - orthologs
Gene location (Human) Chr. Chromosome 16 (human) Band 16p13.3 Start 176,680 bp End 177,522 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11 A4|11 18.86 cM Start 32,233,511 bp End 32,234,465 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte blood bone marrow bone marrow cells placenta spleen ganglionic eminence muscle of thigh olfactory zone of nasal mucosa apex of heart Top expressed in bone marrow spleen lung yolk sac neural tube mesencephalon heart cerebellar cortex genital tubercle zone of skin More reference expression data BioGPS n/a
Gene ontology Molecular function iron ion binding oxygen binding peroxidase activity oxygen carrier activity metal ion binding protein binding heme binding haptoglobin binding organic acid binding Cellular component cytosol endocytic vesicle lumen blood microparticle membrane extracellular region cytosolic small ribosomal subunit hemoglobin complex extracellular exosome haptoglobin-hemoglobin complex extracellular space Biological process positive regulation of cell death protein heterooligomerization oxygen transport receptor-mediated endocytosis bicarbonate transport hydrogen peroxide catabolic process response to hydrogen peroxide cellular oxidant detoxification transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3039 15122 Ensembl ENSG00000206172 ENSMUSG00000069919 UniProt P69905 Q91VB8 RefSeq (mRNA) NM_000558 NM_008218 RefSeq (protein) NP_000508 NP_000508.1 NP_000549.1 NP_001077424 Location (UCSC) Chr 16: 0.18 – 0.18 Mb Chr 11: 32.23 – 32.23 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Hemoglobin subunit alpha, Hemoglobin, alpha 1, is a hemoglobin protein that in humans is encoded by the HBA1 gene.

Gene

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.

Protein

Two alpha chains plus two beta chains constitute HbA, which in normal adult life accounts for about 97% of the total hemoglobin; alpha chains combine with delta chains to constitute HbA-2, which with fetal hemoglobin (HbF), composed of alpha and gamma chains, make up the remaining 3% of adult hemoglobin.

Clinical significance

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.

Interactions

Hemoglobin subunit alpha has been shown to interact with hemoglobin subunit beta (HBB).

See also

• Hemoglobin subunit beta
• Human β-globin locus

Further reading

• 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. doi:10.1081/HEM-120002944. PMID 11939517. S2CID 85035930.
• 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. doi:10.3109/03630269409045775. PMID 7713747.
• Giardina B, Messana I, Scatena R, Castagnola M (1995). "The multiple functions of hemoglobin". Crit. Rev. Biochem. Mol. Biol. 30 (3): 165–96. doi:10.3109/10409239509085142. PMID 7555018.
• 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. doi:10.1182/blood.V73.5.1081.1081. PMID 2649166.
• Schillirò G, Russo-Mancuso G, Dibenedetto SP, et al. (1992). "Six rare hemoglobin variants found in Sicily". Hemoglobin. 15 (5): 431–7. doi:10.3109/03630269108998862. PMID 1802885.
• Vafa M, Troye-Blomberg M, Anchang J, et al. (2008). "Multiplicity of Plasmodium falciparum infection in asymptomatic children in Senegal: relation to transmission, age and erythrocyte variants". Malar. J. 7: 17. doi:10.1186/1475-2875-7-17. PMC 2267475. PMID 18215251.
• Datta P, Chakrabarty S, Chakrabarty A, Chakrabarti A (2008). "Membrane interactions of hemoglobin variants, HbA, HbE, HbF and globin subunits of HbA: effects of aminophospholipids and cholesterol". Biochim. Biophys. Acta. 1778 (1): 1–9. doi:10.1016/j.bbamem.2007.08.019. PMID 17916326.
• Taylor JG, Ackah D, Cobb C, et al. (2008). "Mutations and polymorphisms in hemoglobin genes and the risk of pulmonary hypertension and death in sickle cell disease". Am. J. Hematol. 83 (1): 6–14. doi:10.1002/ajh.21035. PMC 3509176. PMID 17724704.
• Sahu SC, Simplaceanu V, Gong Q, et al. (2007). "Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector". Biochemistry. 46 (35): 9973–80. doi:10.1021/bi700935z. PMC 2532491. PMID 17691822.
• Sorour Y, Heppinstall S, Porter N, et al. (2007). "Is routine molecular screening for common alpha-thalassaemia deletions necessary as part of an antenatal screening programme?". Journal of Medical Screening. 14 (2): 60–1. doi:10.1258/096914107781261981. PMID 17626702. S2CID 24823660.
• Hung CC, Lee CN, Chen CP, et al. (2007). "Molecular assay of -alpha(3.7) and -alpha(4.2) deletions causing alpha-thalassemia by denaturing high-performance liquid chromatography". Clin. Biochem. 40 (11): 817–21. doi:10.1016/j.clinbiochem.2007.03.018. PMID 17512924.
• Ye BC, Zhang Z, Lei Z (2007). "Molecular analysis of alpha/beta-thalassemia in a southern Chinese population". Genet. Test. 11 (1): 75–83. doi:10.1089/gte.2006.0502. PMID 17394396.
• Dilley J, Ganesan A, Deepa R, et al. (2007). "Association of A1C with cardiovascular disease and metabolic syndrome in Asian Indians with normal glucose tolerance". Diabetes Care. 30 (6): 1527–32. doi:10.2337/dc06-2414. PMID 17351274.
• Fonseka PV, Vasudevan G, Clarizia LJ, McDonald MJ (2007). "Temperature dependent soret spectral band shifts accompany human CN-mesohemoglobin assembly". Protein J. 26 (4): 257–63. doi:10.1007/s10930-006-9067-7. PMID 17191128. S2CID 24601675.
• Sankar VH, Arya V, Tewari D, et al. (2007). "Genotyping of alpha-thalassemia in microcytic hypochromic anemia patients from North India". J. Appl. Genet. 47 (4): 391–5. doi:10.1007/BF03194650. PMID 17132905. S2CID 19194610.
• Origa R, Sollaino MC, Giagu N, et al. (2007). "Clinical and molecular analysis of haemoglobin H disease in Sardinia: haematological, obstetric and cardiac aspects in patients with different genotypes". Br. J. Haematol. 136 (2): 326–32. doi:10.1111/j.1365-2141.2006.06423.x. PMID 17129226. S2CID 23265827.
• Hussein OA, Gefen Y, Zidan JM, et al. (2007). "LDL oxidation is associated with increased blood hemoglobin A1c levels in diabetic patients". Clin. Chim. Acta. 377 (1–2): 114–8. doi:10.1016/j.cca.2006.09.002. PMID 17070510.
• Pan W, Galkin O, Filobelo L, et al. (2007). "Metastable mesoscopic clusters in solutions of sickle-cell hemoglobin". Biophys. J. 92 (1): 267–77. Bibcode:2007BpJ....92..267P. doi:10.1529/biophysj.106.094854. PMC 1697867. PMID 17040989.
• Pistrosch F, Koehler C, Wildbrett J, Hanefeld M (2006). "Relationship between diurnal glucose levels and HbA1c in type 2 diabetes". Horm. Metab. Res. 38 (7): 455–9. doi:10.1055/s-2006-947838. PMID 16933182. S2CID 260166156.
• Chong YM, Tan JA, Zubaidah Z, et al. (2006). "Screening of concurrent alpha-thalassaemia 1 in beta-thalassaemia carriers". Med. J. Malaysia. 61 (2): 217–20. PMID 16898315.

External links

• GeneReviews/NCBI/NIH/UW entry on Alpha-Thalassemia
• OMIM entries on Alpha-Thalassemia
• Overview of all the structural information available in the PDB for UniProt: P69905 (Hemoglobin subunit alpha) at the PDBe-KB.