Beta-globin

Hemoglobin, beta

PDB rendering based on 1a00.
Identifiers
Symbols HBB; CD113t-C; HBD
External IDs OMIM: 141900 MGI: 96022 HomoloGene: 68066 GeneCards: HBB Gene
Orthologs
Species Human Mouse
Entrez 3043 15130
Ensembl ENSG00000223609 ENSMUSG00000052305
UniProt P68871 P02089
RefSeq (mRNA) NM_000518 NM_016956
RefSeq (protein) NP_000509 NP_058652
Location (UCSC) Chr 11:
5.2 - 5.2 Mb		 Chr 7:
110.98 - 110.98 Mb
PubMed search [1] [2]

Beta globin (HBB, β-globin) is a protein that, along with alpha globin (HBA), makes up the most common form of hemoglobin in adult humans.[1] The normal adult hemoglobin tetramer consists of two alpha chains and two beta chains.

Contents

Gene locus

The gene is located in the β-globin locus. Expression of beta globin and the neighboring globins in the β-globin locus is controlled by single locus control region (LCR).[2] The order of the genes in the beta-globin cluster is 5' - epsilon – gamma-G – gamma-A – delta – beta - 3'.[1]

Disease linkage

Mutant beta globin is responsible for the sickling of red blood cells seen in sickle cell anemia. Absence of beta chain causes beta-zero-thalassemia. Reduced amounts of detectable beta globin causes beta-plus-thalassemia.[1]

See also

Human β-globin locus

Interactions

HBB has been shown to interact with Hemoglobin, alpha 1.[3][4]

References

  1. ^ a b c "Entrez Gene: HBB hemoglobin, beta". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3043. 
  2. ^ Levings PP, Bungert J (March 2002). "The human beta-globin locus control region". Eur. J. Biochem. 269 (6): 1589–99. doi:10.1046/j.1432-1327.2002.02797.x. PMID 11895428. 
  3. ^ 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 16169070. 
  4. ^ Shaanan, B (Nov. 1983). "Structure of human oxyhaemoglobin at 2.1 A resolution". J. Mol. Biol. (ENGLAND) 171 (1): 31–59. doi:10.1016/S0022-2836(83)80313-1. ISSN 0022-2836. PMID 6644819. 

Further reading

  • 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. doi:10.3109/10409239509085142. PMID 7555018. 
  • Salzano AM, Carbone V, Pagano L, et al. (2002). "Hb Vila Real [beta36(C2)Pro-->His] in Italy: characterization of the amino acid substitution and the DNA mutation.". Hemoglobin 26 (1): 21–31. doi:10.1081/HEM-120002937. PMID 11939509. 
  • Frischknecht H, Dutly F (2007). "A 65 bp duplication/insertion in exon II of the beta globin gene causing beta0-thalassemia.". Haematologica 92 (3): 423–4. doi:10.3324/haematol.10785. PMID 17339197. 


Open source encyclopedia content modification information:

Authorship and Review

Open source encyclopedia content provided here is not reviewed directly by PediaView.com. Content is authored by an open community of volunteers and is not produced by or in any way affiliated with PediaView.com.

Usage Guidelines

This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article on "Beta-globin", which is available in its original form here:

http://en.wikipedia.org/w/index.php?title=Beta-globin

All Wikipedia text is available under the terms of the GNU Free Documentation License. Wikipedia® itself is a registered trademark of the Wikimedia Foundation, Inc.