Hemoglobin, alpha 1

Hemoglobin, alpha 1, also known as HBA1, is a hemoglobin protein that in humans is encoded by the HBA1 gene.[5]

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
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16p13.3 Start 176,680 bp[1] End 177,522 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11 A4|11 18.86 cM Start 32,283,511 bp[2] End 32,284,465 bp[2]
Gene ontology Molecular function • iron ion binding • oxygen binding • peroxidase activity • oxygen carrier activity • metal ion binding • GO:0001948 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 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 NP_032244
Location (UCSC)	Chr 16: 0.18 – 0.18 Mb	Chr 11: 32.28 – 32.28 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[5]

Protein

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 fetal hemoglobin (HbF) makes up the remaining 3% of adult hemoglobin.[5]

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.[5]

Interactions

Hemoglobin, alpha 1 has been shown to interact with HBB.[6][7]

References

1. GRCh38: Ensembl release 89: ENSG00000206172 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000069919 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: HBA1 hemoglobin, alpha 1".
6. 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. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070.
7. 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

• 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.
• 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.
• 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. doi:10.1007/BF03194650. 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. 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.
• 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 etries on Alpha-Thalassemia
• Overview of all the structural information available in the PDB for UniProt: P69905 (Hemoglobin subunit alpha) at the PDBe-KB.