HBB

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, 1CH4, 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, 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, 2DXM, 2H35, 2HBC, 2HBD, 2HBE, 2HBF, 2HBS, 2HCO, 2HHB, 2HHD, 2HHE, 2W6V, 2W72, 2YRS, 3B75, 3D17, 3D7O, 3DUT, 3HHB, 3HXN, 3IC0, 3IC2, 3KMF, 3NL7, 3NMM, 4HHB, 6HBW

Identifiers

Symbols

HBB; CD113t-C; beta-globin

External IDs

OMIM: 141900 MGI: 96022 HomoloGene: 68066 GeneCards: HBB Gene

Gene Ontology
Molecular function	• peroxidase activity • oxygen transporter activity • protein binding • oxygen binding • heme binding • hemoglobin binding • haptoglobin binding • metal ion binding
Cellular component	• hemoglobin complex • hemoglobin complex • hemoglobin complex • haptoglobin-hemoglobin complex
Biological process	• transport • blood coagulation • regulation of blood pressure • positive regulation of cell death • oxygen transport • oxygen transport • nitric oxide transport • response to hydrogen peroxide • hydrogen peroxide catabolic process • positive regulation of nitric oxide biosynthetic process • regulation of blood vessel size • protein heterooligomerization
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 11:
5.25 – 5.25 Mb

Chr 7:
110.98 – 110.98 Mb

PubMed search

[1]

[2]

Beta globin (HBB, β-globinprotin 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 16169070.
^ 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.

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

1g9v: HIGH RESOLUTION CRYSTAL STRUCTURE OF DEOXY HEMOGLOBIN COMPLEXED WITH A POTENT ALLOSTERIC EFFECTOR

1gbu: DEOXY (BETA-(C93A,C112G)) HUMAN HEMOGLOBIN

1gbv: (ALPHA-OXY, BETA-(C112G)DEOXY) T-STATE HUMAN HEMOGLOBIN

1gli: DEOXYHEMOGLOBIN T38W (ALPHA CHAINS), V1G (ALPHA AND BETA CHAINS)

1gzx: OXY T STATE HAEMOGLOBIN: OXYGEN BOUND AT ALL FOUR HAEMS

1hab: CROSSLINKED HAEMOGLOBIN

1hac: CROSSLINKED HAEMOGLOBIN

1hba: HIGH-RESOLUTION X-RAY STUDY OF DEOXYHEMOGLOBIN ROTHSCHILD 37BETA TRP-> ARG: A MUTATION THAT CREATES AN INTERSUBUNIT CHLORIDE-BINDING SITE

1hbb: HIGH-RESOLUTION X-RAY STUDY OF DEOXYHEMOGLOBIN ROTHSCHILD 37BETA TRP-> ARG: A MUTATION THAT CREATES AN INTERSUBUNIT CHLORIDE-BINDING SITE

1hbs: REFINED CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S. I. RESTRAINED LEAST-SQUARES REFINEMENT AT 3.0-ANGSTROMS RESOLUTION

1hco: THE STRUCTURE OF HUMAN CARBONMONOXY HAEMOGLOBIN AT 2.7 ANGSTROMS RESOLUTION

1hdb: ANALYSIS OF THE CRYSTAL STRUCTURE, MOLECULAR MODELING AND INFRARED SPECTROSCOPY OF THE DISTAL BETA-HEME POCKET VALINE67(E11)-THREONINE MUTATION OF HEMOGLOBIN

1hga: HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN

1hgb: HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN

1hgc: HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN

1hho: STRUCTURE OF HUMAN OXYHAEMOGLOBIN AT 2.1 ANGSTROMS RESOLUTION

1ird: Crystal Structure of Human Carbonmonoxy-Haemoglobin at 1.25 A Resolution

1j3y: Direct observation of photolysis-induced tertiary structural changes in human hemoglobin; Crystal structure of alpha(Fe)-beta(Ni) hemoglobin (laser photolysed)

1j3z: Direct observation of photolysis-induced tertiary structural changes in human haemoglobin; Crystal structure of alpha(Fe-CO)-beta(Ni) hemoglobin (laser unphotolysed)

1j40: Direct observation of photolysis-induced tertiary structural changes in human haemoglobin; Crystal structure of alpha(Ni)-beta(Fe-CO) hemoglobin (laser unphotolysed)

1j41: Direct observation of photolysis-induced tertiary structural changes in human haemoglobin; Crystal structure of alpha(Ni)-beta(Fe) hemoglobin (laser photolysed)

1j7s: Crystal Structure of deoxy HbalphaYQ, a mutant of HbA

1j7w: Crystal structure of deoxy HbbetaYQ, a site directed mutant of HbA

1j7y: Crystal structure of partially ligated mutant of HbA

1jy7: THE STRUCTURE OF HUMAN METHEMOGLOBIN. THE VARIATION OF A THEME

1k0y: X-ray Crystallographic Analyses of Symmetrical Allosteric Effectors of Hemoglobin. Compounds Designed to Link Primary and Secondary Binding Sites

1k1k: Structure of Mutant Human Carbonmonoxyhemoglobin C (beta E6K) at 2.0 Angstrom Resolution in Phosphate Buffer.

1kd2: Crystal Structure of Human Deoxyhemoglobin in Absence of Any Anions

1lfl: DEOXY HEMOGLOBIN (90% RELATIVE HUMIDITY)

1lfq: OXY HEMOGLOBIN (93% RELATIVE HUMIDITY)

1lft: OXY HEMOGLOBIN (90% RELATIVE HUMIDITY)

1lfv: OXY HEMOGLOBIN (88% RELATIVE HUMIDITY)

1lfy: OXY HEMOGLOBIN (84% RELATIVE HUMIDITY)

1lfz: OXY HEMOGLOBIN (25% METHANOL)

1ljw: Crystal Structure of Human Carbonmonoxy Hemoglobin at 2.16 A: A Snapshot of the Allosteric Transition

1m9p: Crystalline Human Carbonmonoxy Hemoglobin C Exhibits The R2 Quaternary State at Neutral pH In The Presence of Polyethylene Glycol: The 2.1 Angstrom Resolution Crystal Structure

1mko: A Fourth Quaternary Structure of Human Hemoglobin A at 2.18 A Resolution

1nej: Crystalline Human Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Exhibits The R2 Quaternary State At Neutral pH In The Presence Of Polyethylene Glycol: The 2.1 Angstrom Resolution Crystal Structure

1nih: Structure of deoxy-quaternary haemoglobin with liganded beta subunits

1nqp: Crystal structure of Human hemoglobin E at 1.73 A resolution

1o1i: Cyanomet hemoglobin (A-GLY-C:V1M,L29F,H58Q; B,D:V1M,L106W)

1o1j: Deoxy hemoglobin (A-GLY-C:V1M,L29F,H58Q; B,D:V1M,L106W)

1o1k: Deoxy hemoglobin (A,C:V1M; B,D:V1M,V67W)

1o1l: Deoxy hemoglobin (A-GLY-C:V1M,L29W,H58Q; B,D:V1M)

1o1m: Deoxy hemoglobin (A-GLYGLYGLY-C:V1M,L29F,H58Q B,D:V1M,V67W)

1o1n: Deoxy hemoglobin (A-GLYGLYGLY-C:V1M,L29W; B,D:V1M)

1o1o: Deoxy hemoglobin (A,C:V1M,V62L; B,D:V1M,V67L)

1o1p: Deoxy hemoglobin (A-GLY-C:V1M; B,D:V1M,C93A,N108K)

1qi8: DEOXYGENATED STRUCTURE OF A DISTAL POCKET HEMOGLOBIN MUTANT

1qsh: MAGNESIUM(II)-AND ZINC(II)-PROTOPORPHYRIN IX'S STABILIZE THE LOWEST OXYGEN AFFINITY STATE OF HUMAN HEMOGLOBIN EVEN MORE STRONGLY THAN DEOXYHEME

1qsi: MAGNESIUM(II)-AND ZINC(II)-PROTOPORPHYRIN IX'S STABILIZE THE LOWEST OXYGEN AFFINITY STATE OF HUMAN HEMOGLOBIN EVEN MORE STRONGLY THAN DEOXYHEME

1qxd: Structural Basis for the Potent Antisickling Effect of a Novel Class of 5-Membered Heterocyclic Aldehydic Compounds

1qxe: Structural Basis for the Potent Antisickling Effect of a Novel Class of 5-Membered Heterocyclic Aldehydic Compounds

1r1x: Crystal structure of oxy-human hemoglobin Bassett at 2.15 angstrom

1r1y: Crystal structure of deoxy-human hemoglobin Bassett at 1.8 angstrom

1rps: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Hemoglobin exposed to NO under anerobic conditions

1rq3: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Deoxyhemoglobin, Deoxyhemoglobin

1rq4: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin, HEMOGLOBIN EXPOSED TO NO UNDER AEROBIC CONDITIONS

1rqa: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Beta W73E hemoglobin exposed to NO under anaerobic conditions

1rvw: R STATE HUMAN HEMOGLOBIN [ALPHA V96W], CARBONMONOXY

1sdk: CROSS-LINKED, CARBONMONOXY HEMOGLOBIN A

1sdl: CROSS-LINKED, CARBONMONOXY HEMOGLOBIN A

1shr: Crystal structure of ferrocyanide bound human hemoglobin A2 at 1.88A resolution

1si4: Crystal structure of Human hemoglobin A2 (in R2 state) at 2.2 A resolution

1thb: REFINEMENT OF A PARTIALLY OXYGENATED T STATE HAEMOGLOBIN AT 1.5 ANGSTROMS RESOLUTION

1uiw: Crystal Structures of Unliganded and Half-Liganded Human Hemoglobin Derivatives Cross-Linked between Lys 82beta1 and Lys 82beta2

1vwt: T STATE HUMAN HEMOGLOBIN [ALPHA V96W], ALPHA AQUOMET, BETA DEOXY

1xxt: The T-to-T High Transitions in Human Hemoglobin: wild-type deoxy Hb A (low salt, one test set)

1xy0: T-to-THigh Transitions in Human Hemoglobin: alphaK40G deoxy low-salt

1xye: T-to-THigh Transitions in Human Hemoglobin: alpha Y42A deoxy low salt

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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) · Barts (γ₄) · HbS (α₂β^S₂) · HbC (α₂β^C₂) · HbE (α₂β^E₂)

Compounds	Carboxyhemoglobin · Carbaminohemoglobin · Oxyhemoglobin/Deoxyhemoglobin · Sulfhemoglobin

Other human	Glycosylated hemoglobin · Methemoglobin

Nonhuman	Chlorocruorin · Erythrocruorin

Other

human: Myoglobin (Metmyoglobin) · Neuroglobin · Cytoglobin

plant: Leghemoglobin

Other

Cytochrome (Cytochrome b, Cytochrome P450) · Hemocyanin · Methemalbumin

see also disorders of globin and globulin proteins

M: MYL

cell/phys (coag, heme, immu, gran), csfs

rbmg/mogr/tumr/hist, sysi/epon, btst

drug (B1/2/3+5+6), btst, trns

HBB

Contents

Gene locus

Disease linkage

See also

Interactions

References

Further reading