HBB: Information from Answers.com

"HBB" redirects here. For other uses, see HBB (disambiguation).

Hemoglobin, beta

PDB rendering based on 1a00.

Available structures

1a00, 1a01, 1a0u, 1a0z, 1a3n, 1a3o, 1abw, 1aby, 1aj9, 1b86, 1bab, 1bbb, 1bij, 1buw, 1bz0, 1bz1, 1bzz, 1c7b, 1c7c, 1c7d, 1cbl, 1cbm, 1cls, 1cmy, 1coh, 1dke, 1dxt, 1dxu, 1dxv, 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, 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, 2d5z, 2d60, 2dn1, 2dn2, 2dn3, 2h35, 2hbc, 2hbd, 2hbe, 2hbf, 2hbs, 2hco, 2hhb, 2hhd, 2hhe, 3hhb, 4hhb, 6hbw

Identifiers

Symbols

HBB; CD113t-C; HBD

External IDs

OMIM: 141900 MGI: 96022 HomoloGene: 68066

Gene ontology
Molecular function	• oxygen transporter activity • iron ion binding • selenium binding • oxygen binding • heme binding • hemoglobin binding • metal ion binding
Cellular component	• hemoglobin complex
Biological process	• transport • biological_process • oxygen transport • nitric oxide transport • positive regulation of nitric oxide biosynthetic process

Orthologs

Species

Human

Mouse

Entrez

3043

15130

RefSeq

NM_000518 (mRNA)

NM_016956 (mRNA)

NP_000509 (protein)

NP_058652 (protein)

Location

Chr 11:
5.2 - 5.2 Mb

n/a

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.

1 Gene locus
2 Disease linkage
3 See also
4 Interactions
5 References
6 Further reading

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]

Interactions

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

References

^ ^a ^b ^c "Entrez Gene: HBB hemoglobin, beta". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3043.
^ 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.
^ 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.
^ 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.

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.

PDB Gallery

1a00: HEMOGLOBIN (VAL BETA1 MET, TRP BETA37 TYR) MUTANT

1a01: HEMOGLOBIN (VAL BETA1 MET, TRP BETA37 ALA) MUTANT

1a0u: HEMOGLOBIN (VAL BETA1 MET) MUTANT

1a0z: HEMOGLOBIN (VAL BETA1 MET) MUTANT

1a3n: DEOXY HUMAN HEMOGLOBIN

1a3o: ARTIFICIAL MUTANT (ALPHA Y42H) OF DEOXY HEMOGLOBIN

1abw: DEOXY RHB1.1 (RECOMBINANT HEMOGLOBIN)

1aby: CYANOMET RHB1.1 (RECOMBINANT HEMOGLOBIN)

1aj9: R-STATE HUMAN CARBONMONOXYHEMOGLOBIN ALPHA-A53S

1b86: HUMAN DEOXYHAEMOGLOBIN-2,3-DIPHOSPHOGLYCERATE COMPLEX

1bab: HEMOGLOBIN THIONVILLE: AN ALPHA-CHAIN VARIANT WITH A SUBSTITUTION OF A GLUTAMATE FOR VALINE AT NA-1 AND HAVING AN ACETYLATED METHIONINE NH2 TERMINUS

1bbb: A THIRD QUATERNARY STRUCTURE OF HUMAN HEMOGLOBIN A AT 1.7-ANGSTROMS RESOLUTION

1bij: CROSSLINKED, DEOXY HUMAN HEMOGLOBIN A

1buw: CRYSTAL STRUCTURE OF S-NITROSO-NITROSYL HUMAN HEMOGLOBIN A

1bz0: HEMOGLOBIN A (HUMAN, DEOXY, HIGH SALT)

1bz1: HEMOGLOBIN (ALPHA + MET) VARIANT

1bzz: HEMOGLOBIN (ALPHA V1M) MUTANT

1c7b: DEOXY RHB1.0 (RECOMBINANT HEMOGLOBIN)

1c7c: DEOXY RHB1.1 (RECOMBINANT HEMOGLOBIN)

1c7d: DEOXY RHB1.2 (RECOMBINANT HEMOGLOBIN)

1cbl: THE 1.9 ANGSTROM STRUCTURE OF DEOXY-BETA4 HEMOGLOBIN: ANALYSIS OF THE PARTITIONING OF QUATERNARY-ASSOCIATED AND LIGAND-INDUCED CHANGES IN TERTIARY STRUCTURE

1cbm: THE 1.8 ANGSTROM STRUCTURE OF CARBONMONOXY-BETA4 HEMOGLOBIN: ANALYSIS OF A HOMOTETRAMER WITH THE R QUATERNARY STRUCTURE OF LIGANDED ALPHA2BETA2 HEMOGLOBIN

1cls: CROSS-LINKED HUMAN HEMOGLOBIN DEOXY

1cmy: THE MUTATION BETA99 ASP-TYR STABILIZES Y-A NEW, COMPOSITE QUATERNARY STATE OF HUMAN HEMOGLOBIN

1coh: STRUCTURE OF HAEMOGLOBIN IN THE DEOXY QUATERNARY STATE WITH LIGAND BOUND AT THE ALPHA HAEMS

1dke: NI BETA HEME HUMAN HEMOGLOBIN

1dxt: HIGH-RESOLUTION X-RAY STUDY OF DEOXY RECOMBINANT HUMAN HEMOGLOBINS SYNTHESIZED FROM BETA-GLOBINS HAVING MUTATED AMINO TERMINI

1dxu: HIGH-RESOLUTION X-RAY STUDY OF DEOXY RECOMBINANT HUMAN HEMOGLOBINS SYNTHESIZED FROM BETA-GLOBINS HAVING MUTATED AMINO TERMINI

1dxv: HIGH-RESOLUTION X-RAY STUDY OF DEOXY RECOMBINANT HUMAN HEMOGLOBINS SYNTHESIZED FROM BETA-GLOBINS HAVING MUTATED AMINO TERMINI

1fn3: CRYSTAL STRUCTURE OF NICKEL RECONSTITUTED HEMOGLOBIN-A CASE FOR PERMANENT, T-STATE HEMOGLOBIN

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Proteins: hemeproteins

Globins

Hemoglobin

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)

Tetramers	stages of development: HbA (α₂β₂) · HbA2 (α₂δ₂) · HbF/Fetal (α₂γ₂) · HbE Gower 2 (α₂ε₂) · HbE Gower 1 (ζ₂ε₂) pathology: HbH (β₄) · HbS (α₂β^S₂) · HbC (α₂β^C₂)

Compounds	Carboxyhemoglobin · Carbaminohemoglobin · Oxyhemoglobin/Deoxyhemoglobin · Sulfhemoglobin

Other human	Glycosylated hemoglobin · Methemoglobin

Nonhuman	Chlorocruorin · Erythrocruorin