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Hemoglobin, alpha 1

 
Wikipedia: Hemoglobin, alpha 1
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Hemoglobin, alpha 1
PBB Protein HBA1 image.jpg
PDB rendering based on 1a00.
Available structures
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, 2h35, 2hbc, 2hbd, 2hbe, 2hbf, 2hbs, 2hco, 2hhb, 2hhd, 2hhe, 3hhb, 4hhb, 6hbw
Identifiers
Symbols HBA1; CD31; MGC126895; MGC126897; HBA1
External IDs OMIM: 141800 MGI: 96015 HomoloGene: 469
Orthologs
Species Human Mouse
Entrez 3039 15122
Ensembl n/a ENSMUSG00000069917
UniProt n/a Q61287
RefSeq NM_000558 (mRNA) NM_008218 (mRNA)
NP_000549 (protein) NP_032244 (protein)
Location n/a Chr 11:
32.2 - 32.2 Mb
PubMed search [1] [2]

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]

Interactions

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

References

  1. ^ "Entrez Gene: HBA1 hemoglobin, alpha 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3039. 
  2. ^ Stelzl, Ulrich; Worm Uwe, Lalowski Maciej, Haenig Christian, Brembeck Felix H, Goehler Heike, Stroedicke Martin, Zenkner Martina, Schoenherr Anke, Koeppen Susanne, Timm Jan, Mintzlaff Sascha, Abraham Claudia, Bock Nicole, Kietzmann Silvia, Goedde Astrid, Toksöz Engin, Droege Anja, Krobitsch Sylvia, Korn Bernhard, Birchmeier Walter, Lehrach Hans, Wanker Erich E (Sep. 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell (United States) 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. ISSN 0092-8674. PMID 16179252. 
  3. ^ Shaanan, B (Nov. 1983). "Structure of human oxyhaemoglobin at 2.1 A resolution". J. Mol. Biol. (ENGLAND) 171 (1): 31–59. ISSN 0022-2836. PMID 6644819. 

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. PMID 11939517. 
  • 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. 
  • 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. 
  • 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. 
  • Schillirò G, Russo-Mancuso G, Dibenedetto SP, et al. (1992). "Six rare hemoglobin variants found in Sicily.". Hemoglobin 15 (5): 431–7. 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. 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. 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. 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. 
  • 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. 
  • 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. PMID 17132905. 
  • 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. 
  • 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. doi:10.1529/biophysj.106.094854. 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. 
  • 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. 
Stub icon This protein-related article is a stub. You can help Wikipedia by expanding it.


v • d • e
Proteins: hemeproteins
Globins
Subunits

Alpha locus on 16: α (HBA1, HBA2) · ζ (HBZ) · θ (HBQ1) · μ (HBM)

Beta locus on 11: β (HBB) · δ (HBD) · γ (HBG1, HBG2) · ε (HBE1)

stages of development: HbA (α2β2) · HbA2 (α2δ2) · HbF/Fetal (α2γ2) · HbE Gower 2 (α2ε2) · HbE Gower 1 (ζ2ε2)

pathology: HbH (β4) · HbS (α2βS2) · HbC (α2βC2) · HbE (α2βE2)
Compounds
Other human
Nonhuman
Other
Other

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