Hemoglobin subunit alpha

HBA1
	Gene ontology
Molecular function	iron ion binding; oxygen binding; peroxidase activity; oxygen carrier activity; metal ion binding; 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 space;
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

Ensembl


ENSG00000206172


ENSMUSG00000069919

UniProt


P69905


Q91VB8

RefSeq (mRNA)


NM_000558


NM_008218

RefSeq (protein)


NP_000508 NP_000508.1 NP_000549.1


NP_001077424

Location (UCSC)

Chr 16: 0.18 – 0.18 Mb

Chr 11: 32.23 – 32.23 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Hemoglobin subunit alpha, Hemoglobin, alpha 1,^[5] is a hemoglobin protein that in humans is encoded by the HBA1 gene.^[6]

Gene

The human alpha globin

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.^[6]

Protein

Two alpha chains plus two beta chains constitute HbA, which in normal adult life accounts for about 97% of the total hemoglobin; alpha chains combine with delta chains to constitute HbA-2, which with fetal hemoglobin (HbF), composed of alpha and gamma chains, make up the remaining 3% of adult hemoglobin.^[6]

Clinical significance

Alpha

HBA1; some nondeletion alpha thalassemias have also been reported.^[6]

Interactions

Hemoglobin subunit alpha has been shown to

interact with hemoglobin subunit beta (HBB).^[7]^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000206172 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000069919 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "HBA1 gene: MedlinePlus Genetics".
^ ^a ^b ^c ^d "Entrez Gene: HBA1 hemoglobin, alpha 1".
S2CID 8235923
.

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.
S2CID 85035930
.

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.
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.
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.
PMID 2649166
.

Schillirò G, Russo-Mancuso G, Dibenedetto SP, et al. (1992). "Six rare hemoglobin variants found in Sicily". Hemoglobin. 15 (5): 431–7.
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.
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.
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.
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.
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?". S2CID 24823660
.

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.
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.
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.
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.
S2CID 24601675
.

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.
S2CID 19194610
.

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.
S2CID 23265827
.

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.
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.
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.
S2CID 260166156
.

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 entries on Alpha-Thalassemia

Overview of all the structural information available in the PDB for UniProt: P69905 (Hemoglobin subunit alpha) at the PDBe-KB.

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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

1a9w: HUMAN EMBRYONIC GOWER II CARBONMONOXY 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)

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

1fdh: STRUCTURE OF HUMAN FOETAL DEOXYHAEMOGLOBIN

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

1xz2: wild-type hemoglobin deoxy no-salt

1xz4: Intersubunit Interactions Associated with Tyr42alpha Stabilize the Quaternary-T Tetramer but are not Major Quaternary Constraints in Deoxyhemoglobin: alphaY42A deoxyhemoglobin no-salt

1xz5: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaL91A deoxy low-salt

1xz7: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaR92A deoxy low-salt

1xzu: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaD94G deoxy low-salt

1xzv: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaP95A deoxy low-salt

1y01: Crystal structure of AHSP bound to Fe(II) alpha-hemoglobin

1y09: T-to-T(High) Quaternary Transitions in Human Hemoglobin: alphaN97A deoxy low-salt

1y0a: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaY140A deoxy low-salt

1y0c: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaY140F deoxy low-salt

1y0d: T-to-THigh Quaternary Transitions in Human Hemoglobin: desArg141alpha deoxy low-salt

1y0t: T-to-T(High) Quaternary Transitions in Human Hemoglobin: betaV1M deoxy low-salt (1 test set)

1y0w: T-to-THigh quaternary Transitions in Human Hemoglobin: betaV1M deoxy low-salt (10 test sets)

1y22: T-To-T(High) quaternary transitions in human hemoglobin: betaV33A deoxy low-salt (1 test set)

1y2z: T-To-T(High) quaternary transitions in human hemoglobin: betaV34G deoxy low-salt (1 test set)

1y31: T-To-T(High) quaternary transitions in human hemoglobin: betaY35A deoxy low-salt (1 test set)

1y35: T-To-T(High) quaternary transitions in human hemoglobin: betaY35F deoxy low-salt (1 test set)

1y45: T-To-T(high) quaternary transitions in human hemoglobin: betaP36A deoxy low-salt (10 test sets)

1y46: T-To-T(High) quaternary transitions in human hemoglobin: betaW37Y deoxy low-salt (10 test sets)

1y4b: T-To-T(High) quaternary transitions in human hemoglobin: betaW37H deoxy low-salt (10 test sets)

1y4f: T-To-T(High) quaternary transitions in human hemoglobin: betaW37A deoxy low-salt (10 test sets)

1y4g: T-To-T(High) quaternary transitions in human hemoglobin: betaW37G deoxy low-salt (10 test sets)

1y4p: T-To-T(high) quaternary transitions in human hemoglobin: betaW37E deoxy low-salt (10 test sets)

1y4q: T-To-T(High) quaternary transitions in human hemoglobin: betaF42A deoxy low-salt (1 test set)

1y4r: T-To-T(High) quaternary transitions in human hemoglobin: betaF45A deoxy low-salt (1 test set)

1y4v: T-To-T(High) quaternary transitions in human hemoglobin: betaC93A deoxy low-salt (1 test set)

1y5f: T-To-T(High) quaternary transitions in human hemoglobin: betaL96A deoxy low-salt (1 test set)

1y5j: T-To-T(High) quaternary transitions in human hemoglobin: betaH97A deoxy low-salt (1 test set)

1y5k: T-To-T(High) quaternary transitions in human hemoglobin: betaD99A deoxy low-salt (10 test sets)

1y7c: T-To-T(High) quaternary transitions in human hemoglobin: betaP100A deoxy low-salt (1 test set)

1y7d: T-To-T(High) quaternary transitions in human hemoglobin: betaP100G deoxy low-salt (1 test set)

1y7g: T-To-T(high) quaternary transitions in human hemoglobin: betaN102A deoxy low-salt (1 test set)

1y7z: T-To-T(High) quaternary transitions in human hemoglobin: betaN108A deoxy low-salt (1 test set)

1y83: T-To-T(High) quaternary transitions in human hemoglobin: betaY145G deoxy low-salt (1 test set)

1y85: T-To-T(High) quaternary transitions in human hemoglobin: desHIS146beta deoxy low-salt

1y8w: T-To-T(High) quaternary transitions in human hemoglobin: alphaR92A oxy (2mM IHP, 20% PEG) (10 test sets)

1ydz: T-To-T(High) quaternary transitions in human hemoglobin: alphaY140F oxy (2MM IHP, 20% PEG) (1 test set)

1ye0: T-To-T(High) quaternary transitions in human hemoglobin: betaV33A oxy (2MM IHP, 20% PEG) (1 test set)

1ye1: T-To-T(High) quaternary transitions in human hemoglobin: betaY35A oxy (2MM IHP, 20% PEG) (1 test set)

1ye2: T-To-T(High) quaternary transitions in human hemoglobin: betaY35F oxy (2MM IHP, 20% PEG) (1 test set)

1yen: T-To-T(High) quaternary transitions in human hemoglobin: betaP36A oxy (2MM IHP, 20% PEG) (10 test sets)

1yeo: T-To-T(High) quaternary transitions in human hemoglobin: betaW37A OXY (10 test sets)

1yeq: T-To-T(High) quaternary transitions in human hemoglobin: betaW37Y OXY (10 test sets)

1yeu: T-To-T(High) quaternary transitions in human hemoglobin: betaW37G OXY (10 test sets)

1yev: T-To-T(High) quaternary transitions in human hemoglobin: betaW37E OXY (10 test sets)

1yff: STRUCTURE OF HUMAN CARBONMONOXYHEMOGLOBIN C (BETA E6K): TWO QUATERNARY STATES (R2 and R3) IN ONE CRYSTAL

1yg5: T-To-T(High) quaternary transitions in human hemoglobin: betaW37H OXY (2MM IHP, 20% PEG) (10 test sets)

1ygd: T-To-T(High) quaternary transitions in human hemoglobin: betaW37E alpha zinc beta oxy (10 TEST SETS)

1ygf: T-to-T(high) quaternary transitions in human hemoglobin: betaH97A oxy (2MM IHP, 20% PEG) (1 test set)

1yh9: T-to-T(High) quaternary transitions in human hemoglobin: HbA OXY (2MM IHP, 20% PEG) (10 test sets)

1yhe: T-To-T(High) quaternary transitions in human hemoglobin: HbA OXY (5.0MM IHP, 20% PEG) (10 test sets)

1yhr: T-To-T(High) quaternary transitions in human hemoglobin: HbA OXY (10.0MM IHP, 20% PEG) (10 test sets)

1yie: T-to-thigh quaternary transitions in human hemoglobin: betaW37A oxy (2.2MM IHP, 13% PEG) (1 test set)

1yih: T-to-T(High) quaternary transitions in human hemoglobin: betaP100A oxy (2.2MM IHP, 20% PEG) (1 test set)

1yvq: The low salt (PEG) crystal structure of CO Hemoglobin E (betaE26K) approaching physiological pH (pH 7.5)

1yvt: The high salt (phosphate) crystal structure of CO Hemoglobin E (Glu26Lys) at physiological pH (pH 7.35)

1yzi: A novel quaternary structure of human carbonmonoxy hemoglobin

1z8u: Crystal structure of oxidized alpha hemoglobin bound to AHSP

2d5z: Crystal structure of T-state human hemoglobin complexed with three L35 molecules

2d60: Crystal structure of deoxy human hemoglobin complexed with two L35 molecules

2dn1: 1.25A resolution crystal structure of human hemoglobin in the oxy form

2dn2: 1.25A resolution crystal structure of human hemoglobin in the deoxy form

2dn3: 1.25A resolution crystal structure of human hemoglobin in the carbonmonoxy form

2h35: Solution structure of Human normal adult hemoglobin

2hbc: HIGH RESOLUTION X-RAY STRUCTURES OF MYOGLOBIN-AND HEMOGLOBIN-ALKYL ISOCYANIDE COMPLEXES

2hbd: HIGH RESOLUTION X-RAY STRUCTURES OF MYOGLOBIN-AND HEMOGLOBIN-ALKYL ISOCYANIDE COMPLEXES

2hbe: HIGH RESOLUTION X-RAY STRUCTURES OF MYOGLOBIN-AND HEMOGLOBIN-ALKYL ISOCYANIDE COMPLEXES

2hbf: HIGH RESOLUTION X-RAY STRUCTURES OF MYOGLOBIN-AND HEMOGLOBIN-ALKYL ISOCYANIDE COMPLEXES

2hbs: THE HIGH RESOLUTION CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S

2hco: THE STRUCTURE OF HUMAN CARBONMONOXY HAEMOGLOBIN AT 2.7 ANGSTROMS RESOLUTION

2hhb: THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT 1.74 ANGSTROMS RESOLUTION

2hhd: OXYGEN AFFINITY MODULATION BY THE N-TERMINI OF THE BETA-CHAINS IN HUMAN AND BOVINE HEMOGLOBIN

2hhe: OXYGEN AFFINITY MODULATION BY THE N-TERMINI OF THE BETA CHAINS IN HUMAN AND BOVINE HEMOGLOBIN

3hhb: THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT 1.74 ANGSTROMS RESOLUTION

4hhb: THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT 1.74 ANGSTROMS RESOLUTION

6hbw: Crystal structure of deoxy-human hemoglobin beta6 glu->trp

v
t
e
Proteins that contain heme (hemoproteins)
Globins
Hemoglobin
Subunits
Alpha locus on 16:

α
HBA1

HBA2

pseudo

ζ
HBZ

θ
HBQ1

μ
HBM

Beta locus on 11:

β
HBB

δ
HBD

γ
HBG1

HBG2

ε
HBE1

Tetramers
stages of
development:
Embryonic

HbE Gower 1 (ζ₂ε₂)

HbE Gower 2 (α₂ε₂)

HbE Portland I (ζ₂γ₂)

HbE Portland II (ζ₂β₂)

Fetal

HbF/Fetal (α₂γ₂)

HbA (α₂β₂)

Adult

HbA (α₂β₂)

HbA₂ (α₂δ₂)

HbF/Fetal (α₂γ₂)

pathology:

HbH (β₄)

Barts (γ₄)

HbD
(α₂β^D₂)

HbS (α₂β^S₂)

HbC (α₂β^C₂)

HbE (α₂β^E₂)

HbO (α₂β^O₂)

Compounds

Carboxyhemoglobin

Carbaminohemoglobin

Deoxyhemoglobin

Sulfhemoglobin

Other human

Glycated hemoglobin

Methemoglobin

Nonhuman

Chlorocruorin

Erythrocruorin

Other
human:

Myoglobin
Metmyoglobin

Neuroglobin

Cytoglobin

plant:

Leghemoglobin

Other

Cytochrome
Cytochrome b

Cytochrome P450

Methemalbumin

see also disorders of globin and globulin proteins

Retrieved from "https://en.wikipedia.org/w/index.php?title=Hemoglobin_subunit_alpha&oldid=1191239454"

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000206172 – Ensembl, May 2017

[refGRCm38Ensembl-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] "HBA1 gene: MedlinePlus Genetics".

[entrez-6] "Entrez Gene: HBA1 hemoglobin, alpha 1".

[pmid16169070-7] S2CID 8235923
.

[pmid6644819-8] PMID 6644819
.

[3]

[4]

[5]

[6]

[7]

[8]

Gene

Protein

Clinical significance

Interactions

See also

References

Further reading

External links