- HBD
-
Hemoglobin, delta
PDB rendering based on 1a00.Available structures PDB 1SHR, 1SI4 Identifiers Symbols HBD; External IDs OMIM: 142000 MGI: 96021 HomoloGene: 73881 GeneCards: HBD Gene Gene Ontology Molecular function • oxygen transporter activity
• oxygen binding
• heme binding
• metal ion bindingCellular component • hemoglobin complex Biological process • transport
• blood coagulationSources: Amigo / QuickGO Orthologs Species Human Mouse Entrez 3045 15129 Ensembl ENSG00000223609 ENSMUSG00000073940 UniProt P02042 P02088 RefSeq (mRNA) NM_000519 XM_973056 RefSeq (protein) NP_000510 XP_978150 Location (UCSC) Chr 11:
5.25 – 5.26 MbChr 7:
110.96 – 110.96 MbPubMed search [1] [2] Hemoglobin subunit delta is a protein that in humans is encoded by the HBD gene.[1]
The delta (HBD) and beta (HBB) genes are normally expressed in the adult: two alpha chains plus two beta chains constitute HbA, which in normal adult life comprises about 97% of the total hemoglobin. Two alpha chains plus two delta chains constitute HbA-2, which with HbF comprises the remaining 3% of adult hemoglobin. Five beta-like globin genes are found within a 45 kb cluster on chromosome 11 in the following order: 5'-epsilon--Ggamma--Agamma--delta--beta-3'. Mutations in the delta-globin gene are associated with beta-thalassemia.[2]
See also
References
- ^ Higgs DR, Vickers MA, Wilkie AO, Pretorius IM, Jarman AP, Weatherall DJ (May 1989). "A review of the molecular genetics of the human alpha-globin gene cluster". Blood 73 (5): 1081–104. PMID 2649166.
- ^ "Entrez Gene: HBD hemoglobin, delta". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3045.
Further reading
- 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.
- Collins FS, Weissman SM (1985). "The molecular genetics of human hemoglobin.". Prog. Nucleic Acid Res. Mol. Biol. 31: 315–462. PMID 6397774.
- 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.
PDB gallery 1a00: HEMOGLOBIN (VAL BETA1 MET, TRP BETA37 TYR) MUTANT1a01: HEMOGLOBIN (VAL BETA1 MET, TRP BETA37 ALA) MUTANT1a0u: HEMOGLOBIN (VAL BETA1 MET) MUTANT1a0z: HEMOGLOBIN (VAL BETA1 MET) MUTANT1a3n: DEOXY HUMAN HEMOGLOBIN1a3o: ARTIFICIAL MUTANT (ALPHA Y42H) OF DEOXY HEMOGLOBIN1abw: DEOXY RHB1.1 (RECOMBINANT HEMOGLOBIN)1aby: CYANOMET RHB1.1 (RECOMBINANT HEMOGLOBIN)1aj9: R-STATE HUMAN CARBONMONOXYHEMOGLOBIN ALPHA-A53S1b86: HUMAN DEOXYHAEMOGLOBIN-2,3-DIPHOSPHOGLYCERATE COMPLEX1bab: HEMOGLOBIN THIONVILLE: AN ALPHA-CHAIN VARIANT WITH A SUBSTITUTION OF A GLUTAMATE FOR VALINE AT NA-1 AND HAVING AN ACETYLATED METHIONINE NH2 TERMINUS1bbb: A THIRD QUATERNARY STRUCTURE OF HUMAN HEMOGLOBIN A AT 1.7-ANGSTROMS RESOLUTION1bij: CROSSLINKED, DEOXY HUMAN HEMOGLOBIN A1buw: CRYSTAL STRUCTURE OF S-NITROSO-NITROSYL HUMAN HEMOGLOBIN A1bz0: HEMOGLOBIN A (HUMAN, DEOXY, HIGH SALT)1bz1: HEMOGLOBIN (ALPHA + MET) VARIANT1bzz: HEMOGLOBIN (ALPHA V1M) MUTANT1c7b: 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 STRUCTURE1cbm: THE 1.8 ANGSTROM STRUCTURE OF CARBONMONOXY-BETA4 HEMOGLOBIN: ANALYSIS OF A HOMOTETRAMER WITH THE R QUATERNARY STRUCTURE OF LIGANDED ALPHA2BETA2 HEMOGLOBIN1cls: CROSS-LINKED HUMAN HEMOGLOBIN DEOXY1cmy: THE MUTATION BETA99 ASP-TYR STABILIZES Y-A NEW, COMPOSITE QUATERNARY STATE OF HUMAN HEMOGLOBIN1coh: STRUCTURE OF HAEMOGLOBIN IN THE DEOXY QUATERNARY STATE WITH LIGAND BOUND AT THE ALPHA HAEMS1dke: NI BETA HEME HUMAN HEMOGLOBIN1dxt: HIGH-RESOLUTION X-RAY STUDY OF DEOXY RECOMBINANT HUMAN HEMOGLOBINS SYNTHESIZED FROM BETA-GLOBINS HAVING MUTATED AMINO TERMINI1dxu: HIGH-RESOLUTION X-RAY STUDY OF DEOXY RECOMBINANT HUMAN HEMOGLOBINS SYNTHESIZED FROM BETA-GLOBINS HAVING MUTATED AMINO TERMINI1dxv: HIGH-RESOLUTION X-RAY STUDY OF DEOXY RECOMBINANT HUMAN HEMOGLOBINS SYNTHESIZED FROM BETA-GLOBINS HAVING MUTATED AMINO TERMINI1fn3: CRYSTAL STRUCTURE OF NICKEL RECONSTITUTED HEMOGLOBIN-A CASE FOR PERMANENT, T-STATE HEMOGLOBIN1g9v: HIGH RESOLUTION CRYSTAL STRUCTURE OF DEOXY HEMOGLOBIN COMPLEXED WITH A POTENT ALLOSTERIC EFFECTOR1gbu: DEOXY (BETA-(C93A,C112G)) HUMAN HEMOGLOBIN1gbv: (ALPHA-OXY, BETA-(C112G)DEOXY) T-STATE HUMAN HEMOGLOBIN1gli: DEOXYHEMOGLOBIN T38W (ALPHA CHAINS), V1G (ALPHA AND BETA CHAINS)1gzx: OXY T STATE HAEMOGLOBIN: OXYGEN BOUND AT ALL FOUR HAEMS1hab: CROSSLINKED HAEMOGLOBIN1hac: CROSSLINKED HAEMOGLOBIN1hba: HIGH-RESOLUTION X-RAY STUDY OF DEOXYHEMOGLOBIN ROTHSCHILD 37BETA TRP-> ARG: A MUTATION THAT CREATES AN INTERSUBUNIT CHLORIDE-BINDING SITE1hbb: HIGH-RESOLUTION X-RAY STUDY OF DEOXYHEMOGLOBIN ROTHSCHILD 37BETA TRP-> ARG: A MUTATION THAT CREATES AN INTERSUBUNIT CHLORIDE-BINDING SITE1hbs: REFINED CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S. I. RESTRAINED LEAST-SQUARES REFINEMENT AT 3.0-ANGSTROMS RESOLUTION1hco: THE STRUCTURE OF HUMAN CARBONMONOXY HAEMOGLOBIN AT 2.7 ANGSTROMS RESOLUTION1hdb: ANALYSIS OF THE CRYSTAL STRUCTURE, MOLECULAR MODELING AND INFRARED SPECTROSCOPY OF THE DISTAL BETA-HEME POCKET VALINE67(E11)-THREONINE MUTATION OF HEMOGLOBIN1hga: HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN1hgb: HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN1hgc: HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN1hho: STRUCTURE OF HUMAN OXYHAEMOGLOBIN AT 2.1 ANGSTROMS RESOLUTION1ird: Crystal Structure of Human Carbonmonoxy-Haemoglobin at 1.25 A Resolution1j3y: 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 HbA1j7w: Crystal structure of deoxy HbbetaYQ, a site directed mutant of HbA1j7y: Crystal structure of partially ligated mutant of HbA1jy7: THE STRUCTURE OF HUMAN METHEMOGLOBIN. THE VARIATION OF A THEME1k0y: X-ray Crystallographic Analyses of Symmetrical Allosteric Effectors of Hemoglobin. Compounds Designed to Link Primary and Secondary Binding Sites1k1k: 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 Anions1lfl: 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 Transition1m9p: 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 Structure1mko: A Fourth Quaternary Structure of Human Hemoglobin A at 2.18 A Resolution1nej: 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 Structure1nih: Structure of deoxy-quaternary haemoglobin with liganded beta subunits1nqp: Crystal structure of Human hemoglobin E at 1.73 A resolution1o1i: 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 MUTANT1qsh: MAGNESIUM(II)-AND ZINC(II)-PROTOPORPHYRIN IX'S STABILIZE THE LOWEST OXYGEN AFFINITY STATE OF HUMAN HEMOGLOBIN EVEN MORE STRONGLY THAN DEOXYHEME1qsi: MAGNESIUM(II)-AND ZINC(II)-PROTOPORPHYRIN IX'S STABILIZE THE LOWEST OXYGEN AFFINITY STATE OF HUMAN HEMOGLOBIN EVEN MORE STRONGLY THAN DEOXYHEME1qxd: Structural Basis for the Potent Antisickling Effect of a Novel Class of 5-Membered Heterocyclic Aldehydic Compounds1qxe: Structural Basis for the Potent Antisickling Effect of a Novel Class of 5-Membered Heterocyclic Aldehydic Compounds1r1x: Crystal structure of oxy-human hemoglobin Bassett at 2.15 angstrom1r1y: Crystal structure of deoxy-human hemoglobin Bassett at 1.8 angstrom1rps: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Hemoglobin exposed to NO under anerobic conditions1rq3: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Deoxyhemoglobin, Deoxyhemoglobin1rq4: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin, HEMOGLOBIN EXPOSED TO NO UNDER AEROBIC CONDITIONS1rqa: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Beta W73E hemoglobin exposed to NO under anaerobic conditions1rvw: R STATE HUMAN HEMOGLOBIN [ALPHA V96W], CARBONMONOXY1sdk: CROSS-LINKED, CARBONMONOXY HEMOGLOBIN A1sdl: CROSS-LINKED, CARBONMONOXY HEMOGLOBIN A1shr: Crystal structure of ferrocyanide bound human hemoglobin A2 at 1.88A resolution1si4: Crystal structure of Human hemoglobin A2 (in R2 state) at 2.2 A resolution1thb: REFINEMENT OF A PARTIALLY OXYGENATED T STATE HAEMOGLOBIN AT 1.5 ANGSTROMS RESOLUTION1uiw: Crystal Structures of Unliganded and Half-Liganded Human Hemoglobin Derivatives Cross-Linked between Lys 82beta1 and Lys 82beta21vwt: T STATE HUMAN HEMOGLOBIN [ALPHA V96W], ALPHA AQUOMET, BETA DEOXY1xxt: 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-salt1xye: T-to-THigh Transitions in Human Hemoglobin: alpha Y42A deoxy low saltThe maximum number of images (100) is exceeded ! Otherhuman: Myoglobin (Metmyoglobin) · Neuroglobin · Cytoglobin
plant: LeghemoglobinOther see also disorders of globin and globulin proteinsCategories:- Human proteins
- Protein stubs
- Hemoglobins
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