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P69905

- HBA_HUMAN

UniProt

P69905 - HBA_HUMAN

Protein

Hemoglobin subunit alpha

Gene

HBA1

more
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Involved in oxygen transport from the lung to the various peripheral tissues.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei12 – 121Not glycated
    Sitei57 – 571Not glycated
    Metal bindingi59 – 591Iron (heme distal ligand)
    Sitei61 – 611Not glycated
    Metal bindingi88 – 881Iron (heme proximal ligand)
    Sitei91 – 911Not glycated
    Sitei100 – 1001Not glycated

    GO - Molecular functioni

    1. heme binding Source: InterPro
    2. iron ion binding Source: InterPro
    3. oxygen binding Source: InterPro
    4. oxygen transporter activity Source: UniProtKB-KW
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. bicarbonate transport Source: Reactome
    2. hydrogen peroxide catabolic process Source: BHF-UCL
    3. oxidation-reduction process Source: GOC
    4. oxygen transport Source: UniProtKB
    5. positive regulation of cell death Source: BHF-UCL
    6. protein heterooligomerization Source: BHF-UCL
    7. response to hydrogen peroxide Source: BHF-UCL
    8. small molecule metabolic process Source: Reactome

    Keywords - Biological processi

    Oxygen transport, Transport

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
    REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
    REACT_160163. Scavenging of heme from plasma.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hemoglobin subunit alpha
    Alternative name(s):
    Alpha-globin
    Hemoglobin alpha chain
    Gene namesi
    Name:HBA1
    AND
    Name:HBA2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:4823. HBA1.
    HGNC:4824. HBA2.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cytosol Source: Reactome
    3. cytosolic small ribosomal subunit Source: UniProtKB
    4. endocytic vesicle lumen Source: Reactome
    5. extracellular region Source: Reactome
    6. extracellular vesicular exosome Source: UniProt
    7. haptoglobin-hemoglobin complex Source: BHF-UCL
    8. hemoglobin complex Source: UniProtKB
    9. membrane Source: UniProtKB

    Pathology & Biotechi

    Involvement in diseasei

    Heinz body anemias (HEIBAN) [MIM:140700]: Form of non-spherocytic hemolytic anemia of Dacie type 1. After splenectomy, which has little benefit, basophilic inclusions called Heinz bodies are demonstrable in the erythrocytes. Before splenectomy, diffuse or punctate basophilia may be evident. Most of these cases are probably instances of hemoglobinopathy. The hemoglobin demonstrates heat lability. Heinz bodies are observed also with the Ivemark syndrome (asplenia with cardiovascular anomalies) and with glutathione peroxidase deficiency.1 Publication
    Note: The disease may be caused by mutations affecting the gene represented in this entry.
    Alpha-thalassemia (A-THAL) [MIM:604131]: A form of thalassemia. Thalassemias are common monogenic diseases occurring mostly in Mediterranean and Southeast Asian populations. The hallmark of alpha-thalassemia is an imbalance in globin-chain production in the adult HbA molecule. The level of alpha chain production can range from none to very nearly normal levels. Deletion of both copies of each of the two alpha-globin genes causes alpha(0)-thalassemia, also known as homozygous alpha thalassemia. Due to the complete absence of alpha chains, the predominant fetal hemoglobin is a tetramer of gamma-chains (Bart hemoglobin) that has essentially no oxygen carrying capacity. This causes oxygen starvation in the fetal tissues leading to prenatal lethality or early neonatal death. The loss of two alpha genes results in mild alpha-thalassemia, also known as heterozygous alpha-thalassemia. Affected individuals have small red cells and a mild anemia (microcytosis). If three of the four alpha-globin genes are functional, individuals are completely asymptomatic. Some rare forms of alpha-thalassemia are due to point mutations (non-deletional alpha-thalassemia).
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Alpha(0)-thalassemia is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders.
    Hemoglobin H disease (HBH) [MIM:613978]: A form of alpha-thalassemia due to the loss of three alpha genes. This results in high levels of a tetramer of four beta chains (hemoglobin H), causing a severe and life-threatening anemia. Untreated, most patients die in childhood or early adolescence.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti63 – 631Missing in HBH; hemoglobin Aghia Sophia. 1 Publication
    VAR_066401

    Keywords - Diseasei

    Disease mutation, Hereditary hemolytic anemia

    Organism-specific databases

    MIMi140700. phenotype.
    141800. gene+phenotype.
    604131. phenotype.
    613978. phenotype.
    Orphaneti98791. Alpha-thalassemia - intellectual disability syndrome linked to chromosome 16.
    330041. Autosomal dominant methemoglobinemia.
    163596. Hb Bart's hydrops fetalis.
    93616. Hemoglobin H disease.
    PharmGKBiPA29199.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 142141Hemoglobin subunit alphaPRO_0000052653Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei8 – 81N6-succinyllysine; alternateBy similarity
    Glycosylationi8 – 81N-linked (Glc) (glycation); alternate
    Modified residuei17 – 171N6-acetyllysine; alternate1 Publication
    Modified residuei17 – 171N6-succinyllysine; alternateBy similarity
    Glycosylationi17 – 171N-linked (Glc) (glycation); alternate
    Modified residuei41 – 411N6-succinyllysine; alternateBy similarity
    Glycosylationi41 – 411N-linked (Glc) (glycation); alternate
    Glycosylationi62 – 621N-linked (Glc) (glycation)

    Post-translational modificationi

    The initiator Met is not cleaved in variant Thionville and is acetylated.1 Publication

    Keywords - PTMi

    Acetylation, Glycation, Glycoprotein

    Proteomic databases

    MaxQBiP69905.
    PaxDbiP69905.
    PeptideAtlasiP69905.
    PRIDEiP69905.

    2D gel databases

    DOSAC-COBS-2DPAGEP69905.
    REPRODUCTION-2DPAGEIPI00410714.
    SWISS-2DPAGEP69905.
    UCD-2DPAGEP01922.
    P69905.

    PTM databases

    PhosphoSiteiP69905.

    Miscellaneous databases

    PMAP-CutDBP69905.

    Expressioni

    Tissue specificityi

    Red blood cells.

    Gene expression databases

    BgeeiP69905.
    CleanExiHS_HBA1.
    HS_HBA2.
    GenevestigatoriP69905.

    Organism-specific databases

    HPAiCAB032534.
    CAB038417.
    HPA043780.

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha chains and two beta chains in adult hemoglobin A (HbA); two alpha chains and two delta chains in adult hemoglobin A2 (HbA2); two alpha chains and two epsilon chains in early embryonic hemoglobin Gower-2; two alpha chains and two gamma chains in fetal hemoglobin F (HbF).

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HBBP6887120EBI-714680,EBI-715554

    Protein-protein interaction databases

    BioGridi109289. 15 interactions.
    109290. 7 interactions.
    DIPiDIP-35199N.
    IntActiP69905. 20 interactions.
    MINTiMINT-1519936.
    STRINGi9606.ENSP00000251595.

    Structurei

    Secondary structure

    1
    142
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 1814
    Helixi19 – 213
    Helixi22 – 3615
    Helixi38 – 436
    Beta strandi45 – 473
    Beta strandi50 – 523
    Helixi54 – 7219
    Turni73 – 753
    Helixi77 – 804
    Helixi82 – 909
    Turni91 – 933
    Helixi97 – 11317
    Turni115 – 1173
    Helixi120 – 13819
    Helixi139 – 1413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A00X-ray2.00A/C2-142[»]
    1A01X-ray1.80A/C2-142[»]
    1A0UX-ray2.14A/C2-142[»]
    1A0ZX-ray2.00A/C2-142[»]
    1A3NX-ray1.80A/C2-142[»]
    1A3OX-ray1.80A/C2-142[»]
    1A9WX-ray2.90A/C2-142[»]
    1ABWX-ray2.00A1-142[»]
    1ABYX-ray2.60A1-142[»]
    1AJ9X-ray2.20A2-142[»]
    1B86X-ray2.50A/C2-142[»]
    1BABX-ray1.50A/C1-142[»]
    1BBBX-ray1.70A/C2-142[»]
    1BIJX-ray2.30A/C2-142[»]
    1BUWX-ray1.90A/C2-142[»]
    1BZ0X-ray1.50A/C2-142[»]
    1BZ1X-ray1.59A/C1-142[»]
    1BZZX-ray1.59A/C2-142[»]
    1C7BX-ray1.80A/C2-142[»]
    1C7CX-ray1.80A2-142[»]
    1C7DX-ray1.80A2-142[»]
    1CLSX-ray1.90A/C2-142[»]
    1CMYX-ray3.00A/C2-142[»]
    1COHX-ray2.90A/C2-142[»]
    1DKEX-ray2.10A/C2-142[»]
    1DXTX-ray1.70A/C2-142[»]
    1DXUX-ray1.70A/C2-142[»]
    1DXVX-ray1.70A/C2-142[»]
    1FDHX-ray2.50A/B2-142[»]
    1FN3X-ray2.48A/C2-142[»]
    1G9VX-ray1.85A/C2-142[»]
    1GBUX-ray1.80A/C2-142[»]
    1GBVX-ray2.00A/C2-142[»]
    1GLIX-ray2.50A/C3-142[»]
    1GZXX-ray2.10A/C2-142[»]
    1HABX-ray2.30A/C2-142[»]
    1HACX-ray2.60A/C2-142[»]
    1HBAX-ray2.10A/C2-142[»]
    1HBBX-ray1.90A/C2-142[»]
    1HBSX-ray3.00A/C/E/G2-142[»]
    1HCOX-ray2.70A2-142[»]
    1HDBX-ray2.20A/C2-142[»]
    1HGAX-ray2.10A/C2-142[»]
    1HGBX-ray2.10A/C2-142[»]
    1HGCX-ray2.10A/C2-142[»]
    1HHOX-ray2.10A2-142[»]
    1IRDX-ray1.25A2-142[»]
    1J3YX-ray1.55A/C/E/G2-142[»]
    1J3ZX-ray1.60A/C/E/G2-142[»]
    1J40X-ray1.45A/C/E/G2-142[»]
    1J41X-ray1.45A/C/E/G2-142[»]
    1J7SX-ray2.20A/C2-142[»]
    1J7WX-ray2.00A/C2-142[»]
    1J7YX-ray1.70A/C2-142[»]
    1JY7X-ray3.20A/C/P/R/U/W2-142[»]
    1K0YX-ray1.87A/C2-142[»]
    1K1KX-ray2.00A2-142[»]
    1KD2X-ray1.87A/C2-142[»]
    1LFLX-ray2.70A/C/P/R2-142[»]
    1LFQX-ray2.60A2-142[»]
    1LFTX-ray2.60A2-142[»]
    1LFVX-ray2.80A2-142[»]
    1LFYX-ray3.30A2-142[»]
    1LFZX-ray3.10A2-142[»]
    1LJWX-ray2.16A2-142[»]
    1M9PX-ray2.10A/C2-142[»]
    1MKOX-ray2.18A/C2-142[»]
    1NEJX-ray2.10A/C2-142[»]
    1NIHX-ray2.60A/C2-142[»]
    1NQPX-ray1.73A/C2-142[»]
    1O1IX-ray2.30A2-142[»]
    1O1JX-ray1.90A2-142[»]
    1O1KX-ray2.00A/C3-142[»]
    1O1LX-ray1.80A2-142[»]
    1O1MX-ray1.85A2-142[»]
    1O1NX-ray1.80A2-142[»]
    1O1OX-ray1.80A/C2-142[»]
    1O1PX-ray1.80A2-142[»]
    1QI8X-ray1.80A/C3-142[»]
    1QSHX-ray1.70A/C2-142[»]
    1QSIX-ray1.70A/C2-142[»]
    1QXDX-ray2.25A/C2-142[»]
    1QXEX-ray1.85A/C2-142[»]
    1R1XX-ray2.15A2-142[»]
    1R1YX-ray1.80A/C2-142[»]
    1RPSX-ray2.11A/C2-142[»]
    1RQ3X-ray1.91A/C2-142[»]
    1RQ4X-ray2.11A/C2-142[»]
    1RQAX-ray2.11A/C2-142[»]
    1RVWX-ray2.50A2-142[»]
    1SDKX-ray1.80A/C2-142[»]
    1SDLX-ray1.80A/C2-142[»]
    1SHRX-ray1.88A/C2-142[»]
    1SI4X-ray2.20A/C2-142[»]
    1THBX-ray1.50A/C2-142[»]
    1UIWX-ray1.50A/C/E/G2-142[»]
    1VWTX-ray1.90A/C2-142[»]
    1XXTX-ray1.91A/C2-142[»]
    1XY0X-ray1.99A/C2-142[»]
    1XYEX-ray2.13A/C3-142[»]
    1XZ2X-ray1.90A/C2-142[»]
    1XZ4X-ray2.00A/C3-142[»]
    1XZ5X-ray2.11A/C2-142[»]
    1XZ7X-ray1.90A/C2-142[»]
    1XZUX-ray2.16A/C2-142[»]
    1XZVX-ray2.11A/C2-142[»]
    1Y01X-ray2.80B1-142[»]
    1Y09X-ray2.25A/C2-142[»]
    1Y0AX-ray2.22A/C2-140[»]
    1Y0CX-ray2.30A/C2-140[»]
    1Y0DX-ray2.10A/C2-141[»]
    1Y0TX-ray2.14A/C2-142[»]
    1Y0WX-ray2.14A/C2-142[»]
    1Y22X-ray2.16A/C2-142[»]
    1Y2ZX-ray2.07A/C2-142[»]
    1Y31X-ray2.13A/C2-142[»]
    1Y35X-ray2.12A/C2-142[»]
    1Y45X-ray2.00A/C2-142[»]
    1Y46X-ray2.22A/C2-142[»]
    1Y4BX-ray2.10A/C2-142[»]
    1Y4FX-ray2.00A/C2-142[»]
    1Y4GX-ray1.91A/C2-142[»]
    1Y4PX-ray1.98A/C2-142[»]
    1Y4QX-ray2.11A/C2-142[»]
    1Y4RX-ray2.22A/C2-142[»]
    1Y4VX-ray1.84A/C2-142[»]
    1Y5FX-ray2.14A/C2-142[»]
    1Y5JX-ray2.03A/C2-142[»]
    1Y5KX-ray2.20A/C2-142[»]
    1Y7CX-ray2.10A/C2-142[»]
    1Y7DX-ray1.90A/C2-142[»]
    1Y7GX-ray2.10A/C2-142[»]
    1Y7ZX-ray1.98A/C2-142[»]
    1Y83X-ray1.90A/C2-142[»]
    1Y85X-ray2.13A/C2-142[»]
    1Y8WX-ray2.90A/C2-142[»]
    1YDZX-ray3.30A/C2-140[»]
    1YE0X-ray2.50A/C2-142[»]
    1YE1X-ray4.50A/C2-142[»]
    1YE2X-ray1.80A/C2-142[»]
    1YENX-ray2.80A/C2-142[»]
    1YEOX-ray2.22A/C2-142[»]
    1YEQX-ray2.75A/C2-142[»]
    1YEUX-ray2.12A/C2-142[»]
    1YEVX-ray2.11A/C2-142[»]
    1YFFX-ray2.40A/C/E/G2-142[»]
    1YG5X-ray2.70A/C2-142[»]
    1YGDX-ray2.73A/C2-142[»]
    1YGFX-ray2.70A/C2-142[»]
    1YH9X-ray2.20A/C2-142[»]
    1YHEX-ray2.10A/C2-142[»]
    1YHRX-ray2.60A/C2-142[»]
    1YIEX-ray2.40A/C2-142[»]
    1YIHX-ray2.00A/C2-142[»]
    1YVQX-ray1.80A/C2-142[»]
    1YVTX-ray1.80A2-142[»]
    1YZIX-ray2.07A2-142[»]
    1Z8UX-ray2.40B/D1-142[»]
    2D5ZX-ray1.45A/C2-142[»]
    2D60X-ray1.70A/C2-142[»]
    2DN1X-ray1.25A2-142[»]
    2DN2X-ray1.25A/C2-142[»]
    2DN3X-ray1.25A2-142[»]
    2DXMneutron diffraction2.10A/C2-142[»]
    2H35NMR-A/C2-142[»]
    2HBCX-ray2.10A2-142[»]
    2HBDX-ray2.20A2-142[»]
    2HBEX-ray2.00A2-142[»]
    2HBFX-ray2.20A2-142[»]
    2HBSX-ray2.05A/C/E/G2-142[»]
    2HCOX-ray2.70A2-142[»]
    2HHBX-ray1.74A/C2-142[»]
    2HHDX-ray2.20A/C2-142[»]
    2HHEX-ray2.20A/C2-142[»]
    2M6ZNMR-A/C2-142[»]
    2W6VX-ray1.80A/C2-142[»]
    2W72X-ray1.07A2-142[»]
    C3-142[»]
    2YRSX-ray2.30A/C/I/M2-142[»]
    3B75X-ray2.30A/C/E/G/S2-142[»]
    3D17X-ray2.80A/C2-142[»]
    3D7OX-ray1.80A2-142[»]
    3DUTX-ray1.55A/C2-142[»]
    3HHBX-ray1.74A/C2-142[»]
    3HXNX-ray2.00A/C2-142[»]
    3IA3X-ray3.20B/D1-142[»]
    3IC0X-ray1.80A/C2-142[»]
    3IC2X-ray2.40A/C2-142[»]
    3KMFneutron diffraction2.00A/E2-142[»]
    3NL7X-ray1.80A2-142[»]
    3NMMX-ray1.60A/C2-142[»]
    3ODQX-ray3.10A/C2-142[»]
    3ONZX-ray2.09A2-142[»]
    3OO4X-ray1.90A2-142[»]
    3OO5X-ray2.10A2-142[»]
    3OVUX-ray2.83C2-142[»]
    3P5QX-ray2.00A2-142[»]
    3QJBX-ray1.80A2-142[»]
    3QJCX-ray2.00A2-142[»]
    3QJDX-ray1.56A/C2-142[»]
    3QJEX-ray1.80A/C2-142[»]
    3R5IX-ray2.20A/C2-142[»]
    3S48X-ray3.05C/D2-142[»]
    3S65X-ray1.80A/C2-142[»]
    3S66X-ray1.40A2-142[»]
    3SZKX-ray3.01A/D2-142[»]
    3WCPX-ray1.94A/C2-142[»]
    4FC3X-ray2.26A2-142[»]
    4HHBX-ray1.74A/C2-142[»]
    4IJ2X-ray4.24A/C2-142[»]
    4L7YX-ray1.80A/C2-142[»]
    4MQCX-ray2.20A2-142[»]
    4MQGX-ray1.68A2-142[»]
    4MQHX-ray2.50A2-140[»]
    4MQIX-ray1.92A2-141[»]
    4MQJX-ray1.80A/C/E/G2-142[»]
    4MQKX-ray2.24A/C/E/G2-142[»]
    4N7NX-ray2.75A/C/E/G/I/K2-142[»]
    4N7OX-ray2.50A/C/E/G/I/K2-142[»]
    4N7PX-ray2.81A/C/E/G/I/K2-142[»]
    6HBWX-ray2.00A/C2-142[»]
    ProteinModelPortaliP69905.
    SMRiP69905. Positions 2-142.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP69905.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the globin family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG283543.
    HOVERGENiHBG009709.
    InParanoidiP69905.
    KOiK13822.
    OMAiDKFLCAV.
    OrthoDBiEOG7KH9MP.
    PhylomeDBiP69905.
    TreeFamiTF332328.

    Family and domain databases

    Gene3Di1.10.490.10. 1 hit.
    InterProiIPR000971. Globin.
    IPR009050. Globin-like.
    IPR012292. Globin_dom.
    IPR002338. Haemoglobin_a.
    IPR002339. Haemoglobin_pi.
    [Graphical view]
    PfamiPF00042. Globin. 1 hit.
    [Graphical view]
    PRINTSiPR00612. ALPHAHAEM.
    PR00815. PIHAEM.
    SUPFAMiSSF46458. SSF46458. 1 hit.
    PROSITEiPS01033. GLOBIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P69905-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLSPADKTN VKAAWGKVGA HAGEYGAEAL ERMFLSFPTT KTYFPHFDLS    50
    HGSAQVKGHG KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK 100
    LLSHCLLVTL AAHLPAEFTP AVHASLDKFL ASVSTVLTSK YR 142
    Length:142
    Mass (Da):15,258
    Last modified:January 23, 2007 - v2
    Checksum:i15E13666573BBBAE
    GO

    Sequence cautioni

    The sequence BAD97112.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101N → H in BAD97112. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21V → E in Thionville; O(2) affinity down. 1 Publication
    VAR_002719
    Natural varianti3 – 31L → R in ChongQing; O(2) affinity up. 1 Publication
    Corresponds to variant rs36030576 [ dbSNP | Ensembl ].
    VAR_002720
    Natural varianti6 – 61A → D in J-Toronto.
    Corresponds to variant rs34090856 [ dbSNP | Ensembl ].
    VAR_002721
    Natural varianti6 – 61A → P in Karachi.
    Corresponds to variant rs34751764 [ dbSNP | Ensembl ].
    VAR_002722
    Natural varianti7 – 71D → A in Sawara; O(2) affinity up. 1 Publication
    Corresponds to variant rs33986902 [ dbSNP | Ensembl ].
    VAR_002723
    Natural varianti7 – 71D → G in Swan River. 1 Publication
    VAR_002724
    Natural varianti7 – 71D → N in Dunn; O(2) affinity up.
    Corresponds to variant rs33961916 [ dbSNP | Ensembl ].
    VAR_002725
    Natural varianti7 – 71D → V in Ferndown; O(2) affinity up.
    VAR_002726
    Natural varianti7 – 71D → Y in Woodville; O(2) affinity up. 1 Publication
    VAR_002727
    Natural varianti8 – 81K → E in Kurosaki. 1 Publication
    Corresponds to variant rs34817956 [ dbSNP | Ensembl ].
    VAR_002728
    Natural varianti10 – 101N → T in Broomfield.
    VAR_038149
    Natural varianti11 – 111V → F.
    Corresponds to variant rs1799896 [ dbSNP | Ensembl ].
    VAR_014605
    Natural varianti12 – 121K → E in Anantharaj.
    VAR_002729
    Natural varianti13 – 131A → D in J-Paris 1/J-Aljezur.
    Corresponds to variant rs35615982 [ dbSNP | Ensembl ].
    VAR_002730
    Natural varianti14 – 141A → P in Ravenscourt Park; causes alpha-thalassemia.
    Corresponds to variant rs35331909 [ dbSNP | Ensembl ].
    VAR_038150
    Natural varianti15 – 151W → R in Evanston; O(2) affinity up.
    Corresponds to variant rs33964317 [ dbSNP | Ensembl ].
    VAR_002731
    Natural varianti16 – 161G → R in Ottawa/Siam.
    Corresponds to variant rs35816645 [ dbSNP | Ensembl ].
    VAR_002732
    Natural varianti17 – 171K → M in Harbin; slightly unstable. 1 Publication
    Corresponds to variant rs35210126 [ dbSNP | Ensembl ].
    VAR_002733
    Natural varianti17 – 171K → N in Beijing.
    Corresponds to variant rs33923844 [ dbSNP | Ensembl ].
    VAR_002734
    Natural varianti19 – 191G → D in Al-Ain Abu Dhabi. 1 Publication
    Corresponds to variant rs35993097 [ dbSNP | Ensembl ].
    VAR_002735
    Natural varianti19 – 191G → R in Handsworth.
    Corresponds to variant rs34504387 [ dbSNP | Ensembl ].
    VAR_002736
    Natural varianti20 – 201A → D in J-Kurosh.
    VAR_002737
    Natural varianti20 – 201A → E in J-Tashikuergan.
    Corresponds to variant rs35628685 [ dbSNP | Ensembl ].
    VAR_002738
    Natural varianti21 – 211H → Q in Le Lamentin.
    Corresponds to variant rs41525149 [ dbSNP | Ensembl ].
    VAR_002739
    Natural varianti21 – 211H → R in Hobart. 1 Publication
    Corresponds to variant rs33943087 [ dbSNP | Ensembl ].
    VAR_002740
    Natural varianti22 – 221A → D in J-Nyanza.
    Corresponds to variant rs11548605 [ dbSNP | Ensembl ].
    VAR_002741
    Natural varianti22 – 221A → P in Fontainebleau.
    Corresponds to variant rs34324664 [ dbSNP | Ensembl ].
    VAR_002742
    Natural varianti23 – 231G → D in J-Medellin.
    Corresponds to variant rs34608326 [ dbSNP | Ensembl ].
    VAR_002743
    Natural varianti24 – 241E → G in Reims; slightly unstable.
    Corresponds to variant rs33939421 [ dbSNP | Ensembl ].
    VAR_002744
    Natural varianti24 – 241E → K in Chad.
    VAR_002745
    Natural varianti25 – 251Y → H in Luxembourg; unstable.
    VAR_002746
    Natural varianti27 – 271A → E in Shenyang; unstable. 1 Publication
    VAR_002747
    Natural varianti27 – 271A → V in Campinas. 1 Publication
    VAR_025387
    Natural varianti28 – 281E → D in Hekinan.
    VAR_002748
    Natural varianti28 – 281E → G in Fort Worth.
    VAR_002749
    Natural varianti28 – 281E → V in Spanish town. 1 Publication
    VAR_002750
    Natural varianti31 – 311E → K in O-Padova.
    VAR_002751
    Natural varianti32 – 321R → K Causes alpha-thalassemia. 1 Publication
    VAR_025002
    Natural varianti32 – 321R → S in Prato; unstable.
    VAR_002752
    Natural varianti35 – 351L → R in Queens/Ogi.
    VAR_002753
    Natural varianti38 – 381P → PE in Catonsville.
    VAR_002755
    Natural varianti38 – 381P → R in Bourmedes.
    VAR_002754
    Natural varianti41 – 411K → M in Kanagawa; O(2) affinity up. 1 Publication
    VAR_002756
    Natural varianti42 – 421T → S in Miyano; O(2) affinity up.
    VAR_002757
    Natural varianti44 – 441F → L in Hirosaki; unstable.
    VAR_002758
    Natural varianti45 – 451P → L in Milledgeville; O(2) affinity up.
    Corresponds to variant rs41514946 [ dbSNP | Ensembl ].
    VAR_002759
    Natural varianti45 – 451P → R in Kawachi; O(2) affinity up.
    VAR_002760
    Natural varianti46 – 461H → Q in Bari.
    VAR_002761
    Natural varianti46 – 461H → R in Fort de France; O(2) affinity up. 1 Publication
    VAR_002762
    Natural varianti48 – 481D → A in Cordele; unstable.
    VAR_002763
    Natural varianti48 – 481D → G in Umi/Michigan; unstable.
    VAR_002764
    Natural varianti48 – 481D → H in Hasharon/Sinai; unstable. 1 Publication
    VAR_002765
    Natural varianti48 – 481D → Y in Kurdistan. 1 Publication
    VAR_002766
    Natural varianti49 – 491L → R in Montgomery. 1 Publication
    VAR_002767
    Natural varianti50 – 501S → R in Savaria.
    VAR_002768
    Natural varianti51 – 511H → R in Aichi; slightly unstable.
    VAR_002769
    Natural varianti52 – 521G → D in J-Abidjan.
    VAR_002770
    Natural varianti52 – 521G → R in Russ.
    VAR_002771
    Natural varianti54 – 541A → D in J-Rovigo; unstable.
    VAR_002772
    Natural varianti55 – 551Q → R in Hikoshima/Shimonoseki.
    VAR_002773
    Natural varianti57 – 571K → R in Port Huron. 1 Publication
    VAR_002774
    Natural varianti57 – 571K → T in Thailand.
    VAR_002775
    Natural varianti58 – 581G → R in L-Persian Gulf.
    VAR_002776
    Natural varianti59 – 591H → Q in Boghe. 1 Publication
    VAR_025388
    Natural varianti59 – 591H → Y in M-Boston/M-Osaka; O(2) affinity down.
    VAR_002777
    Natural varianti60 – 601G → D in Adana; unstable; causes alpha-thalassemia.
    Corresponds to variant rs28928878 [ dbSNP | Ensembl ].
    VAR_002778
    Natural varianti60 – 601G → V in Tottori; unstable.
    VAR_002779
    Natural varianti61 – 611K → N in Zambia.
    Corresponds to variant rs28928887 [ dbSNP | Ensembl ].
    VAR_002780
    Natural varianti61 – 611Missing in Clinic; unstable; causes alpha-thalassemia. 1 Publication
    VAR_002781
    Natural varianti62 – 621K → N in J-Buda. 1 Publication
    VAR_002782
    Natural varianti62 – 621K → T in J-Anatolia.
    VAR_002783
    Natural varianti63 – 631V → M in Evans; unstable. 2 Publications
    VAR_002784
    Natural varianti63 – 631Missing in HBH; hemoglobin Aghia Sophia. 1 Publication
    VAR_066401
    Natural varianti64 – 641A → D in Pontoise; unstable.
    VAR_002785
    Natural varianti65 – 651D → Y in Persepolis.
    VAR_002786
    Natural varianti69 – 691N → K in G-Philadelphia. 1 Publication
    Corresponds to variant rs1060339 [ dbSNP | Ensembl ].
    VAR_002787
    Natural varianti72 – 721A → E in J-Habana.
    VAR_002788
    Natural varianti72 – 721A → V in Ozieri.
    VAR_002789
    Natural varianti73 – 731H → R in Daneskgah-Teheran.
    VAR_002790
    Natural varianti75 – 751D → A in Lille.
    VAR_002791
    Natural varianti75 – 751D → G in Chapel Hill.
    VAR_002792
    Natural varianti75 – 751D → N in G-Pest. 1 Publication
    VAR_002793
    Natural varianti76 – 761D → A in Duan.
    VAR_002794
    Natural varianti76 – 761D → H in Q-Iran.
    VAR_002795
    Natural varianti77 – 771M → K in Noko.
    VAR_002796
    Natural varianti77 – 771M → T in Aztec.
    VAR_002797
    Natural varianti78 – 781P → R in Guizhou.
    VAR_002798
    Natural varianti79 – 791N → H in Davenport. 1 Publication
    VAR_002799
    Natural varianti79 – 791N → K in Stanleyville-2.
    VAR_002800
    Natural varianti80 – 801A → G in Singapore.
    VAR_012662
    Natural varianti81 – 811L → R in Ann Arbor; unstable.
    VAR_002801
    Natural varianti82 – 821S → C in Nigeria.
    VAR_002802
    Natural varianti83 – 831A → D in Garden State.
    VAR_002803
    Natural varianti85 – 851S → R in Etobicoke; O(2) affinity up.
    VAR_002804
    Natural varianti86 – 861D → V in Inkster; O(2) affinity up. 1 Publication
    VAR_002805
    Natural varianti86 – 861D → Y in Atago; O(2) affinity up. 1 Publication
    VAR_002806
    Natural varianti87 – 871L → R in Moabit; unstable.
    VAR_002807
    Natural varianti88 – 881H → N in Auckland; unstable. 1 Publication
    VAR_002808
    Natural varianti88 – 881H → R in Iwata; unstable.
    VAR_002809
    Natural varianti89 – 891A → S in Loire; O(2) affinity up.
    VAR_002810
    Natural varianti91 – 911K → M in Handa; O(2) affinity up. 1 Publication
    VAR_002811
    Natural varianti92 – 921L → F.
    Corresponds to variant rs17407508 [ dbSNP | Ensembl ].
    VAR_049272
    Natural varianti92 – 921L → P in Port Phillip; unstable.
    Corresponds to variant rs17407508 [ dbSNP | Ensembl ].
    VAR_002812
    Natural varianti93 – 931R → Q in J-Cape Town; O(2) affinity up.
    VAR_002813
    Natural varianti93 – 931R → W in Cemenelum; O(2) affinity up. 1 Publication
    VAR_020775
    Natural varianti95 – 951D → A in Bassett; markedly reduced oxygen affinity. 1 Publication
    VAR_025389
    Natural varianti95 – 951D → Y in Setif; unstable.
    VAR_002814
    Natural varianti96 – 961P → A in Denmark Hill; O(2) affinity up.
    VAR_002815
    Natural varianti96 – 961P → T in Godavari; O(2) affinity up. 1 Publication
    VAR_002816
    Natural varianti98 – 981N → K in Dallas; O(2) affinity up.
    VAR_002817
    Natural varianti100 – 1001K → E in Turriff. 1 Publication
    VAR_002818
    Natural varianti103 – 1031S → R in Manitoba; slightly unstable.
    Corresponds to variant rs41344646 [ dbSNP | Ensembl ].
    VAR_002819
    Natural varianti104 – 1041H → R in Contaldo; unstable.
    VAR_002820
    Natural varianti104 – 1041H → Y in Charolles. 1 Publication
    VAR_025390
    Natural varianti110 – 1101L → R in Suan-Dok; unstable; causes alpha-thalassemia. 1 Publication
    VAR_002821
    Natural varianti111 – 1111A → D in Petah Tikva; unstable; causes alpha-thalassemia. 1 Publication
    VAR_002822
    Natural varianti113 – 1131H → D in Hopkins-II; unstable.
    VAR_002823
    Natural varianti114 – 1141L → H in Twin Peaks.
    VAR_002824
    Natural varianti115 – 1151P → L in Nouakchott.
    VAR_002825
    Natural varianti115 – 1151P → R in Chiapas.
    VAR_002826
    Natural varianti115 – 1151P → S in Melusine. 1 Publication
    VAR_002827
    Natural varianti116 – 1161A → D in J-Tongariki.
    VAR_002828
    Natural varianti117 – 1171E → A in Ube-4.
    VAR_002829
    Natural varianti117 – 1171E → EHLPAE in Zaire. 1 Publication
    VAR_002830
    Natural varianti118 – 1181F → FI in Phnom Penh. 1 Publication
    VAR_002831
    Natural varianti119 – 1191T → TEFT in Grady. 1 Publication
    VAR_002832
    Natural varianti121 – 1211A → E in J-Meerut/J-Birmingham. 1 Publication
    VAR_002833
    Natural varianti122 – 1221V → M in Owari.
    VAR_002834
    Natural varianti123 – 1231H → Q in Westmead. 1 Publication
    VAR_002835
    Natural varianti126 – 1261L → P in Quong Sze; causes alpha-thalassemia.
    VAR_002836
    Natural varianti126 – 1261L → R in Plasencia; family with moderate microcytosis and hypochromia. 1 Publication
    VAR_025391
    Natural varianti127 – 1271D → G in West One. 1 Publication
    VAR_025392
    Natural varianti127 – 1271D → V in Fukutomi; O(2) affinity up.
    VAR_002837
    Natural varianti127 – 1271D → Y in Monteriore; O(2) affinity up.
    VAR_002838
    Natural varianti128 – 1281K → N in Jackson.
    VAR_002839
    Natural varianti130 – 1301L → P in Tunis-Bizerte; unstable; causes alpha-thalassemia. 1 Publication
    VAR_002840
    Natural varianti131 – 1311A → D in Yuda; O(2) affinity down. 1 Publication
    VAR_002842
    Natural varianti131 – 1311A → P in Sun Prairie; unstable. 1 Publication
    VAR_002841
    Natural varianti132 – 1321S → P in Questembert; highly unstable; causes alpha-thalassemia.
    VAR_002843
    Natural varianti134 – 1341S → R in Val de Marne; O(2) affinity up. 1 Publication
    VAR_002844
    Natural varianti136 – 1361V → E in Pavie.
    VAR_002845
    Natural varianti137 – 1371L → M in Chicago.
    VAR_002846
    Natural varianti137 – 1371L → P in Bibba; unstable; causes alpha-thalassemia.
    VAR_002847
    Natural varianti137 – 1371L → R in Toyama. 1 Publication
    VAR_035242
    Natural varianti139 – 1391S → P in Attleboro; O(2) affinity up.
    VAR_002848
    Natural varianti140 – 1401K → E in Hanamaki; O(2) affinity up. 1 Publication
    VAR_002849
    Natural varianti140 – 1401K → T in Tokoname; O(2) affinity up.
    VAR_002850
    Natural varianti141 – 1411Y → H in Rouen/Ethiopia; O(2) affinity up. 1 Publication
    VAR_002851
    Natural varianti142 – 1421R → C in Nunobiki; O(2) affinity up.
    VAR_002852
    Natural varianti142 – 1421R → H in Suresnes; O(2) affinity up.
    VAR_002854
    Natural varianti142 – 1421R → L in Legnano; O(2) affinity up.
    VAR_002853
    Natural varianti142 – 1421R → P in Singapore.
    VAR_002855

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00153 Genomic DNA. Translation: AAB59407.1.
    J00153 Genomic DNA. Translation: AAB59408.1.
    V00491 Genomic DNA. Translation: CAA23750.1.
    V00493 mRNA. Translation: CAA23752.1.
    V00488 Genomic DNA. Translation: CAA23748.1.
    V00516 Genomic DNA. Translation: CAA23774.1.
    AF230076 Genomic DNA. Translation: AAF72612.1.
    AF525460 Genomic DNA. Translation: AAM83102.1.
    DQ431198 Genomic DNA. Translation: ABD95910.1.
    DQ431198 Genomic DNA. Translation: ABD95911.1.
    AF097635 mRNA. Translation: AAC72839.1.
    AF105974 mRNA. Translation: AAC97373.1.
    AF349571 mRNA. Translation: AAK37554.1.
    AF536204 Genomic DNA. Translation: AAN04486.1.
    DQ499017 Genomic DNA. Translation: ABF56144.1.
    DQ499018 Genomic DNA. Translation: ABF56145.1.
    AK223392 mRNA. Translation: BAD97112.1. Different initiation.
    AE006462 Genomic DNA. Translation: AAK61215.1.
    AE006462 Genomic DNA. Translation: AAK61216.1.
    Z84721 Genomic DNA. Translation: CAB06554.1.
    Z84721 Genomic DNA. Translation: CAB06555.1.
    BC005931 mRNA. Translation: AAH05931.1.
    BC008572 mRNA. Translation: AAH08572.1.
    BC032122 mRNA. Translation: AAH32122.1.
    BC050661 mRNA. Translation: AAH50661.1.
    BC101846 mRNA. Translation: AAI01847.1.
    BC101848 mRNA. Translation: AAI01849.1.
    CCDSiCCDS10398.1.
    CCDS10399.1.
    PIRiA90807. HAHU.
    C93303. HACZP.
    I58217. HACZ.
    RefSeqiNP_000508.1. NM_000517.4.
    NP_000549.1. NM_000558.3.
    UniGeneiHs.449630.
    Hs.654744.

    Genome annotation databases

    EnsembliENST00000251595; ENSP00000251595; ENSG00000188536.
    ENST00000320868; ENSP00000322421; ENSG00000206172.
    GeneIDi3039.
    3040.
    KEGGihsa:3039.
    hsa:3040.
    UCSCiuc002cfv.4. human.

    Polymorphism databases

    DMDMi57013850.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    HbVar

    Human hemoglobin variants and thalassemias

    HbVar

    Human hemoglobin variants and thalassemias

    SHMPD

    The Singapore human mutation and polymorphism database

    Wikipedia

    Hemoglobin entry

    Protein Spotlight

    Journey into a tiny world - Issue 84 of July 2007

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00153 Genomic DNA. Translation: AAB59407.1 .
    J00153 Genomic DNA. Translation: AAB59408.1 .
    V00491 Genomic DNA. Translation: CAA23750.1 .
    V00493 mRNA. Translation: CAA23752.1 .
    V00488 Genomic DNA. Translation: CAA23748.1 .
    V00516 Genomic DNA. Translation: CAA23774.1 .
    AF230076 Genomic DNA. Translation: AAF72612.1 .
    AF525460 Genomic DNA. Translation: AAM83102.1 .
    DQ431198 Genomic DNA. Translation: ABD95910.1 .
    DQ431198 Genomic DNA. Translation: ABD95911.1 .
    AF097635 mRNA. Translation: AAC72839.1 .
    AF105974 mRNA. Translation: AAC97373.1 .
    AF349571 mRNA. Translation: AAK37554.1 .
    AF536204 Genomic DNA. Translation: AAN04486.1 .
    DQ499017 Genomic DNA. Translation: ABF56144.1 .
    DQ499018 Genomic DNA. Translation: ABF56145.1 .
    AK223392 mRNA. Translation: BAD97112.1 . Different initiation.
    AE006462 Genomic DNA. Translation: AAK61215.1 .
    AE006462 Genomic DNA. Translation: AAK61216.1 .
    Z84721 Genomic DNA. Translation: CAB06554.1 .
    Z84721 Genomic DNA. Translation: CAB06555.1 .
    BC005931 mRNA. Translation: AAH05931.1 .
    BC008572 mRNA. Translation: AAH08572.1 .
    BC032122 mRNA. Translation: AAH32122.1 .
    BC050661 mRNA. Translation: AAH50661.1 .
    BC101846 mRNA. Translation: AAI01847.1 .
    BC101848 mRNA. Translation: AAI01849.1 .
    CCDSi CCDS10398.1.
    CCDS10399.1.
    PIRi A90807. HAHU.
    C93303. HACZP.
    I58217. HACZ.
    RefSeqi NP_000508.1. NM_000517.4.
    NP_000549.1. NM_000558.3.
    UniGenei Hs.449630.
    Hs.654744.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A00 X-ray 2.00 A/C 2-142 [» ]
    1A01 X-ray 1.80 A/C 2-142 [» ]
    1A0U X-ray 2.14 A/C 2-142 [» ]
    1A0Z X-ray 2.00 A/C 2-142 [» ]
    1A3N X-ray 1.80 A/C 2-142 [» ]
    1A3O X-ray 1.80 A/C 2-142 [» ]
    1A9W X-ray 2.90 A/C 2-142 [» ]
    1ABW X-ray 2.00 A 1-142 [» ]
    1ABY X-ray 2.60 A 1-142 [» ]
    1AJ9 X-ray 2.20 A 2-142 [» ]
    1B86 X-ray 2.50 A/C 2-142 [» ]
    1BAB X-ray 1.50 A/C 1-142 [» ]
    1BBB X-ray 1.70 A/C 2-142 [» ]
    1BIJ X-ray 2.30 A/C 2-142 [» ]
    1BUW X-ray 1.90 A/C 2-142 [» ]
    1BZ0 X-ray 1.50 A/C 2-142 [» ]
    1BZ1 X-ray 1.59 A/C 1-142 [» ]
    1BZZ X-ray 1.59 A/C 2-142 [» ]
    1C7B X-ray 1.80 A/C 2-142 [» ]
    1C7C X-ray 1.80 A 2-142 [» ]
    1C7D X-ray 1.80 A 2-142 [» ]
    1CLS X-ray 1.90 A/C 2-142 [» ]
    1CMY X-ray 3.00 A/C 2-142 [» ]
    1COH X-ray 2.90 A/C 2-142 [» ]
    1DKE X-ray 2.10 A/C 2-142 [» ]
    1DXT X-ray 1.70 A/C 2-142 [» ]
    1DXU X-ray 1.70 A/C 2-142 [» ]
    1DXV X-ray 1.70 A/C 2-142 [» ]
    1FDH X-ray 2.50 A/B 2-142 [» ]
    1FN3 X-ray 2.48 A/C 2-142 [» ]
    1G9V X-ray 1.85 A/C 2-142 [» ]
    1GBU X-ray 1.80 A/C 2-142 [» ]
    1GBV X-ray 2.00 A/C 2-142 [» ]
    1GLI X-ray 2.50 A/C 3-142 [» ]
    1GZX X-ray 2.10 A/C 2-142 [» ]
    1HAB X-ray 2.30 A/C 2-142 [» ]
    1HAC X-ray 2.60 A/C 2-142 [» ]
    1HBA X-ray 2.10 A/C 2-142 [» ]
    1HBB X-ray 1.90 A/C 2-142 [» ]
    1HBS X-ray 3.00 A/C/E/G 2-142 [» ]
    1HCO X-ray 2.70 A 2-142 [» ]
    1HDB X-ray 2.20 A/C 2-142 [» ]
    1HGA X-ray 2.10 A/C 2-142 [» ]
    1HGB X-ray 2.10 A/C 2-142 [» ]
    1HGC X-ray 2.10 A/C 2-142 [» ]
    1HHO X-ray 2.10 A 2-142 [» ]
    1IRD X-ray 1.25 A 2-142 [» ]
    1J3Y X-ray 1.55 A/C/E/G 2-142 [» ]
    1J3Z X-ray 1.60 A/C/E/G 2-142 [» ]
    1J40 X-ray 1.45 A/C/E/G 2-142 [» ]
    1J41 X-ray 1.45 A/C/E/G 2-142 [» ]
    1J7S X-ray 2.20 A/C 2-142 [» ]
    1J7W X-ray 2.00 A/C 2-142 [» ]
    1J7Y X-ray 1.70 A/C 2-142 [» ]
    1JY7 X-ray 3.20 A/C/P/R/U/W 2-142 [» ]
    1K0Y X-ray 1.87 A/C 2-142 [» ]
    1K1K X-ray 2.00 A 2-142 [» ]
    1KD2 X-ray 1.87 A/C 2-142 [» ]
    1LFL X-ray 2.70 A/C/P/R 2-142 [» ]
    1LFQ X-ray 2.60 A 2-142 [» ]
    1LFT X-ray 2.60 A 2-142 [» ]
    1LFV X-ray 2.80 A 2-142 [» ]
    1LFY X-ray 3.30 A 2-142 [» ]
    1LFZ X-ray 3.10 A 2-142 [» ]
    1LJW X-ray 2.16 A 2-142 [» ]
    1M9P X-ray 2.10 A/C 2-142 [» ]
    1MKO X-ray 2.18 A/C 2-142 [» ]
    1NEJ X-ray 2.10 A/C 2-142 [» ]
    1NIH X-ray 2.60 A/C 2-142 [» ]
    1NQP X-ray 1.73 A/C 2-142 [» ]
    1O1I X-ray 2.30 A 2-142 [» ]
    1O1J X-ray 1.90 A 2-142 [» ]
    1O1K X-ray 2.00 A/C 3-142 [» ]
    1O1L X-ray 1.80 A 2-142 [» ]
    1O1M X-ray 1.85 A 2-142 [» ]
    1O1N X-ray 1.80 A 2-142 [» ]
    1O1O X-ray 1.80 A/C 2-142 [» ]
    1O1P X-ray 1.80 A 2-142 [» ]
    1QI8 X-ray 1.80 A/C 3-142 [» ]
    1QSH X-ray 1.70 A/C 2-142 [» ]
    1QSI X-ray 1.70 A/C 2-142 [» ]
    1QXD X-ray 2.25 A/C 2-142 [» ]
    1QXE X-ray 1.85 A/C 2-142 [» ]
    1R1X X-ray 2.15 A 2-142 [» ]
    1R1Y X-ray 1.80 A/C 2-142 [» ]
    1RPS X-ray 2.11 A/C 2-142 [» ]
    1RQ3 X-ray 1.91 A/C 2-142 [» ]
    1RQ4 X-ray 2.11 A/C 2-142 [» ]
    1RQA X-ray 2.11 A/C 2-142 [» ]
    1RVW X-ray 2.50 A 2-142 [» ]
    1SDK X-ray 1.80 A/C 2-142 [» ]
    1SDL X-ray 1.80 A/C 2-142 [» ]
    1SHR X-ray 1.88 A/C 2-142 [» ]
    1SI4 X-ray 2.20 A/C 2-142 [» ]
    1THB X-ray 1.50 A/C 2-142 [» ]
    1UIW X-ray 1.50 A/C/E/G 2-142 [» ]
    1VWT X-ray 1.90 A/C 2-142 [» ]
    1XXT X-ray 1.91 A/C 2-142 [» ]
    1XY0 X-ray 1.99 A/C 2-142 [» ]
    1XYE X-ray 2.13 A/C 3-142 [» ]
    1XZ2 X-ray 1.90 A/C 2-142 [» ]
    1XZ4 X-ray 2.00 A/C 3-142 [» ]
    1XZ5 X-ray 2.11 A/C 2-142 [» ]
    1XZ7 X-ray 1.90 A/C 2-142 [» ]
    1XZU X-ray 2.16 A/C 2-142 [» ]
    1XZV X-ray 2.11 A/C 2-142 [» ]
    1Y01 X-ray 2.80 B 1-142 [» ]
    1Y09 X-ray 2.25 A/C 2-142 [» ]
    1Y0A X-ray 2.22 A/C 2-140 [» ]
    1Y0C X-ray 2.30 A/C 2-140 [» ]
    1Y0D X-ray 2.10 A/C 2-141 [» ]
    1Y0T X-ray 2.14 A/C 2-142 [» ]
    1Y0W X-ray 2.14 A/C 2-142 [» ]
    1Y22 X-ray 2.16 A/C 2-142 [» ]
    1Y2Z X-ray 2.07 A/C 2-142 [» ]
    1Y31 X-ray 2.13 A/C 2-142 [» ]
    1Y35 X-ray 2.12 A/C 2-142 [» ]
    1Y45 X-ray 2.00 A/C 2-142 [» ]
    1Y46 X-ray 2.22 A/C 2-142 [» ]
    1Y4B X-ray 2.10 A/C 2-142 [» ]
    1Y4F X-ray 2.00 A/C 2-142 [» ]
    1Y4G X-ray 1.91 A/C 2-142 [» ]
    1Y4P X-ray 1.98 A/C 2-142 [» ]
    1Y4Q X-ray 2.11 A/C 2-142 [» ]
    1Y4R X-ray 2.22 A/C 2-142 [» ]
    1Y4V X-ray 1.84 A/C 2-142 [» ]
    1Y5F X-ray 2.14 A/C 2-142 [» ]
    1Y5J X-ray 2.03 A/C 2-142 [» ]
    1Y5K X-ray 2.20 A/C 2-142 [» ]
    1Y7C X-ray 2.10 A/C 2-142 [» ]
    1Y7D X-ray 1.90 A/C 2-142 [» ]
    1Y7G X-ray 2.10 A/C 2-142 [» ]
    1Y7Z X-ray 1.98 A/C 2-142 [» ]
    1Y83 X-ray 1.90 A/C 2-142 [» ]
    1Y85 X-ray 2.13 A/C 2-142 [» ]
    1Y8W X-ray 2.90 A/C 2-142 [» ]
    1YDZ X-ray 3.30 A/C 2-140 [» ]
    1YE0 X-ray 2.50 A/C 2-142 [» ]
    1YE1 X-ray 4.50 A/C 2-142 [» ]
    1YE2 X-ray 1.80 A/C 2-142 [» ]
    1YEN X-ray 2.80 A/C 2-142 [» ]
    1YEO X-ray 2.22 A/C 2-142 [» ]
    1YEQ X-ray 2.75 A/C 2-142 [» ]
    1YEU X-ray 2.12 A/C 2-142 [» ]
    1YEV X-ray 2.11 A/C 2-142 [» ]
    1YFF X-ray 2.40 A/C/E/G 2-142 [» ]
    1YG5 X-ray 2.70 A/C 2-142 [» ]
    1YGD X-ray 2.73 A/C 2-142 [» ]
    1YGF X-ray 2.70 A/C 2-142 [» ]
    1YH9 X-ray 2.20 A/C 2-142 [» ]
    1YHE X-ray 2.10 A/C 2-142 [» ]
    1YHR X-ray 2.60 A/C 2-142 [» ]
    1YIE X-ray 2.40 A/C 2-142 [» ]
    1YIH X-ray 2.00 A/C 2-142 [» ]
    1YVQ X-ray 1.80 A/C 2-142 [» ]
    1YVT X-ray 1.80 A 2-142 [» ]
    1YZI X-ray 2.07 A 2-142 [» ]
    1Z8U X-ray 2.40 B/D 1-142 [» ]
    2D5Z X-ray 1.45 A/C 2-142 [» ]
    2D60 X-ray 1.70 A/C 2-142 [» ]
    2DN1 X-ray 1.25 A 2-142 [» ]
    2DN2 X-ray 1.25 A/C 2-142 [» ]
    2DN3 X-ray 1.25 A 2-142 [» ]
    2DXM neutron diffraction 2.10 A/C 2-142 [» ]
    2H35 NMR - A/C 2-142 [» ]
    2HBC X-ray 2.10 A 2-142 [» ]
    2HBD X-ray 2.20 A 2-142 [» ]
    2HBE X-ray 2.00 A 2-142 [» ]
    2HBF X-ray 2.20 A 2-142 [» ]
    2HBS X-ray 2.05 A/C/E/G 2-142 [» ]
    2HCO X-ray 2.70 A 2-142 [» ]
    2HHB X-ray 1.74 A/C 2-142 [» ]
    2HHD X-ray 2.20 A/C 2-142 [» ]
    2HHE X-ray 2.20 A/C 2-142 [» ]
    2M6Z NMR - A/C 2-142 [» ]
    2W6V X-ray 1.80 A/C 2-142 [» ]
    2W72 X-ray 1.07 A 2-142 [» ]
    C 3-142 [» ]
    2YRS X-ray 2.30 A/C/I/M 2-142 [» ]
    3B75 X-ray 2.30 A/C/E/G/S 2-142 [» ]
    3D17 X-ray 2.80 A/C 2-142 [» ]
    3D7O X-ray 1.80 A 2-142 [» ]
    3DUT X-ray 1.55 A/C 2-142 [» ]
    3HHB X-ray 1.74 A/C 2-142 [» ]
    3HXN X-ray 2.00 A/C 2-142 [» ]
    3IA3 X-ray 3.20 B/D 1-142 [» ]
    3IC0 X-ray 1.80 A/C 2-142 [» ]
    3IC2 X-ray 2.40 A/C 2-142 [» ]
    3KMF neutron diffraction 2.00 A/E 2-142 [» ]
    3NL7 X-ray 1.80 A 2-142 [» ]
    3NMM X-ray 1.60 A/C 2-142 [» ]
    3ODQ X-ray 3.10 A/C 2-142 [» ]
    3ONZ X-ray 2.09 A 2-142 [» ]
    3OO4 X-ray 1.90 A 2-142 [» ]
    3OO5 X-ray 2.10 A 2-142 [» ]
    3OVU X-ray 2.83 C 2-142 [» ]
    3P5Q X-ray 2.00 A 2-142 [» ]
    3QJB X-ray 1.80 A 2-142 [» ]
    3QJC X-ray 2.00 A 2-142 [» ]
    3QJD X-ray 1.56 A/C 2-142 [» ]
    3QJE X-ray 1.80 A/C 2-142 [» ]
    3R5I X-ray 2.20 A/C 2-142 [» ]
    3S48 X-ray 3.05 C/D 2-142 [» ]
    3S65 X-ray 1.80 A/C 2-142 [» ]
    3S66 X-ray 1.40 A 2-142 [» ]
    3SZK X-ray 3.01 A/D 2-142 [» ]
    3WCP X-ray 1.94 A/C 2-142 [» ]
    4FC3 X-ray 2.26 A 2-142 [» ]
    4HHB X-ray 1.74 A/C 2-142 [» ]
    4IJ2 X-ray 4.24 A/C 2-142 [» ]
    4L7Y X-ray 1.80 A/C 2-142 [» ]
    4MQC X-ray 2.20 A 2-142 [» ]
    4MQG X-ray 1.68 A 2-142 [» ]
    4MQH X-ray 2.50 A 2-140 [» ]
    4MQI X-ray 1.92 A 2-141 [» ]
    4MQJ X-ray 1.80 A/C/E/G 2-142 [» ]
    4MQK X-ray 2.24 A/C/E/G 2-142 [» ]
    4N7N X-ray 2.75 A/C/E/G/I/K 2-142 [» ]
    4N7O X-ray 2.50 A/C/E/G/I/K 2-142 [» ]
    4N7P X-ray 2.81 A/C/E/G/I/K 2-142 [» ]
    6HBW X-ray 2.00 A/C 2-142 [» ]
    ProteinModelPortali P69905.
    SMRi P69905. Positions 2-142.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109289. 15 interactions.
    109290. 7 interactions.
    DIPi DIP-35199N.
    IntActi P69905. 20 interactions.
    MINTi MINT-1519936.
    STRINGi 9606.ENSP00000251595.

    Chemistry

    ChEMBLi CHEMBL2095168.
    DrugBanki DB00613. Amodiaquine.
    DB00608. Chloroquine.
    DB00893. Iron Dextran.
    DB00358. Mefloquine.
    DB01087. Primaquine.
    DB00468. Quinine.

    PTM databases

    PhosphoSitei P69905.

    Polymorphism databases

    DMDMi 57013850.

    2D gel databases

    DOSAC-COBS-2DPAGE P69905.
    REPRODUCTION-2DPAGE IPI00410714.
    SWISS-2DPAGE P69905.
    UCD-2DPAGE P01922.
    P69905.

    Proteomic databases

    MaxQBi P69905.
    PaxDbi P69905.
    PeptideAtlasi P69905.
    PRIDEi P69905.

    Protocols and materials databases

    DNASUi 3039.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000251595 ; ENSP00000251595 ; ENSG00000188536 .
    ENST00000320868 ; ENSP00000322421 ; ENSG00000206172 .
    GeneIDi 3039.
    3040.
    KEGGi hsa:3039.
    hsa:3040.
    UCSCi uc002cfv.4. human.

    Organism-specific databases

    CTDi 3039.
    3040.
    GeneCardsi GC16P000291.
    GC16P000292.
    GeneReviewsi HBA1.
    HBA2.
    HGNCi HGNC:4823. HBA1.
    HGNC:4824. HBA2.
    HPAi CAB032534.
    CAB038417.
    HPA043780.
    MIMi 140700. phenotype.
    141800. gene+phenotype.
    141850. gene.
    141860. gene.
    604131. phenotype.
    613978. phenotype.
    neXtProti NX_P69905.
    Orphaneti 98791. Alpha-thalassemia - intellectual disability syndrome linked to chromosome 16.
    330041. Autosomal dominant methemoglobinemia.
    163596. Hb Bart's hydrops fetalis.
    93616. Hemoglobin H disease.
    PharmGKBi PA29199.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG283543.
    HOVERGENi HBG009709.
    InParanoidi P69905.
    KOi K13822.
    OMAi DKFLCAV.
    OrthoDBi EOG7KH9MP.
    PhylomeDBi P69905.
    TreeFami TF332328.

    Enzyme and pathway databases

    Reactomei REACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
    REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
    REACT_160163. Scavenging of heme from plasma.

    Miscellaneous databases

    ChiTaRSi HBA2. human.
    EvolutionaryTracei P69905.
    GeneWikii HBA2.
    Hemoglobin,_alpha_1.
    Hemoglobin,_alpha_2.
    NextBioi 12034.
    PMAP-CutDB P69905.
    PROi P69905.
    SOURCEi Search...

    Gene expression databases

    Bgeei P69905.
    CleanExi HS_HBA1.
    HS_HBA2.
    Genevestigatori P69905.

    Family and domain databases

    Gene3Di 1.10.490.10. 1 hit.
    InterProi IPR000971. Globin.
    IPR009050. Globin-like.
    IPR012292. Globin_dom.
    IPR002338. Haemoglobin_a.
    IPR002339. Haemoglobin_pi.
    [Graphical view ]
    Pfami PF00042. Globin. 1 hit.
    [Graphical view ]
    PRINTSi PR00612. ALPHAHAEM.
    PR00815. PIHAEM.
    SUPFAMi SSF46458. SSF46458. 1 hit.
    PROSITEi PS01033. GLOBIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The 3' untranslated regions of the duplicated human alpha-globin genes are unexpectedly divergent."
      Michelson A.M., Orkin S.H.
      Cell 22:371-377(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1).
    2. "Nucleotide sequence of the coding portion of human alpha globin messenger RNA."
      Wilson J.T., Wilson L.B., Reddy V.B., Cavallesco C., Ghosh P.K., Deriel J.K., Forget B.G., Weissman S.M.
      J. Biol. Chem. 255:2807-2815(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (HBA2).
    3. "Cloning and complete nucleotide sequence of human 5'-alpha-globin gene."
      Liebhaber S.A., Goossens M.J., Kan Y.W.
      Proc. Natl. Acad. Sci. U.S.A. 77:7054-7058(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2).
    4. "Mutation in an intervening sequence splice junction in man."
      Orkin S.H., Goff S.C., Hechtman R.L.
      Proc. Natl. Acad. Sci. U.S.A. 78:5041-5045(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Alpha2(CD31 AGG-->AAG, Arg-->Lys) causing non-deletional alpha-thalassemia in a Chinese family with HbH disease."
      Zhao Y., Xu X.
      Haematologica 86:541-542(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-32.
    6. "Rapid detection of the common alpha-thalassemia-2 determinants by PCR assay."
      Zhao Y., Zhong M., Liu Z., Xu X.
      Zhonghua Yi Xue Yi Chuan Xue Za Zhi 18:216-218(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1).
    7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALPHA-1 AND ALPHA-2).
    8. "Rapid sequencing of mRNA of the human alpha two globin, directly isolated from reticulocytes in whole blood."
      Kutlar F., Leithner C., Kutlar A.
      Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (HBA2).
      Tissue: Blood.
    9. "cDNA sequencing of human alpha one globin mRNA, the 3'untranslated region is different than alpha two globin."
      Kutlar F., Leithner C., Kutlar A.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (HBA1).
      Tissue: Blood.
    10. "An alpha chain variant 'Hemoglobin J-Toronto (Cd.5 /Ala to Asp)' mutation was detected on the alpha-1 globin mRNA by sequencing of cDNA."
      Kutlar F., Holley L., Leithner C., Kutlar A.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Blood.
    11. "Unstable Hb 'Evans' (GTG->ATG/Val 62 Met) was detected on the alpha-2 globin gene of an Hispanic girl."
      Kutlar F., Elam D., Hoff J.V., Holley L., Kutlar A.
      Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2), VARIANT EVANS MET-63.
      Tissue: Blood.
    12. "Hb G-Philadelphia (Alpha,Codon 68;AAC>AAG/Asn>Lys)in black is detected on a chromosome that carries alpha 3.7 kb deletion showed completely normal alpha-2 globin gene sequence."
      Kutlar F., Davis D.H., Nechtman J., Elam D.
      Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2), VARIANT G-PHILADELPHIA LYS-69.
    13. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Thymus.
    14. "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
      Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
      Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HBA1 AND HBA2).
    15. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HBA1 AND HBA2).
    16. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HBA1 AND HBA2).
      Tissue: Bone marrow, Brain, Lung and Spleen.
    17. "The constitution of normal adult human haemoglobin."
      Braunitzer G., Gehring-Muller R., Hilschmann N., Hilse K., Hobom G., Rudloff V., Wittmann-Liebold B.
      Hoppe-Seyler's Z. Physiol. Chem. 325:283-286(1961) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-142.
    18. "The structure of human hemoglobin: IV. The chymotryptic digestion of the alpha chain of human hemoglobin."
      Hill R.J., Konigsberg W.
      J. Biol. Chem. 237:3151-3156(1962) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-142.
    19. "The amino acid sequence of the alpha chain of human fetal hemoglobin."
      Schroeder W.A., Shelton J.R., Shelton J.B., Cormick J.
      Biochemistry 2:1353-1357(1963) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-142.
    20. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-32.
      Tissue: Platelet.
    21. "Hb Ethiopia or alpha 2(140)(HC2)Tyr----His beta 2."
      Webber B.B., Wilson J.B., Gu L.-H., Huisman T.H.J.
      Hemoglobin 16:441-443(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 128-142, VARIANT ETHIOPIA HIS-141.
      Tissue: Umbilical cord blood.
    22. "Sites of nonenzymatic glycosylation of human hemoglobin A."
      Shapiro R., McManus M.J., Zalut C., Bunn H.F.
      J. Biol. Chem. 255:3120-3127(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCATION AT LYS-8; LYS-17; LYS-41 AND LYS-62, LACK OF GLYCATION AT LYS-12; LYS-57; LYS-61; LYS-91 AND LYS-100.
    23. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Three-dimensional Fourier synthesis of human deoxyhaemoglobin at 2.5-A resolution: refinement of the atomic model."
      Fermi G.
      J. Mol. Biol. 97:237-256(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN.
    26. "The structure of human carbonmonoxy haemoglobin at 2.7-A resolution."
      Baldwin J.M.
      J. Mol. Biol. 136:103-128(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    27. "A third quaternary structure of human hemoglobin A at 1.7-A resolution."
      Silva M.M., Rogers P.H., Arnone A.
      J. Biol. Chem. 267:17248-17256(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF LIGANDED R2 STATE.
    28. "Crystal structure of a human embryonic haemoglobin: the carbonmonoxy form of Gower II (alpha2 epsilon2) haemoglobin at 2.9-A resolution."
      Sutherland-Smith A.J., Baker H.M., Hofmann O.M., Brittain T., Baker E.N.
      J. Mol. Biol. 280:475-484(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF HB GOWER-2.
    29. "Accommodation of insertions in helices: the mutation in hemoglobin Catonsville (Pro 37 alpha-Glu-Thr 38 alpha) generates a 3(10)-->alpha bulge."
      Kavanaugh J.S., Moo-Penn W.F., Arnone A.
      Biochemistry 32:2509-2513(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF VARIANT HB CATONSVILLE GLU-38 INS.
    30. "HB Al-Ain Abu Dhabi [alpha 18(A16)Gly-->Asp]: a new hemoglobin variant discovered in an Emiratee family."
      Abbes S., M'Rad A., Fitzgerald P.A., Dormer P., Blouquit Y., Kister J., Galacteros F., Wajcman H.
      Hemoglobin 16:355-362(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AL-AIN ABU DHABI ASP-19.
    31. "Hemoglobin Atago (alpha2-85 Tyr beta-2) a new abnormal human hemoglobin found in Nagasaki. Biochemical studies on hemoglobins and myoglobins. VI."
      Fujiwara N., Maekawa T., Matsuda G.
      Int. J. Protein Res. 3:35-39(1971) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ATAGO TYR-86.
    32. "Hb Auckland [alpha 87(F8) His-->Asn]: a new mutation of the proximal histidine identified by electrospray mass spectrometry."
      Brennan S.O., Matthews J.R.
      Hemoglobin 21:393-403(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AUCKLAND ASN-88.
    33. "Structural characterizations of hemoglobins J-Buda (alpha 61 (E10) Lys-to-Asn) and G-Pest (alpha 74 (EF3) Asp-to-Asn)."
      Brimhall B.J., Duerst M., Hollan S.R., Stenzel P., Szelenyi J., Jones R.T.
      Biochim. Biophys. Acta 336:344-360(1974)
      Cited for: VARIANTS J-BUDA ASN-62 AND G-PEST ASN-75.
    34. "Hb Cemenelum [alpha 92 (FG4) Arg-->Trp]: a hemoglobin variant of the alpha 1/beta 2 interface that displays a moderate increase in oxygen affinity."
      Wajcman H., Kister J., M'Rad A., Soummer A.M., Galacteros F.
      Ann. Hematol. 68:73-76(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CEMENELUM TRP-93.
    35. "Hemoglobin Chongqing [alpha 2(NA2)Leu-->Arg] and hemoglobin Harbin [alpha 16(A14)Lys-->Met] found in China."
      Zeng Y.-T., Huang S.-Z., Qiu X.-K., Cheng G.-C., Ren Z.-R., Jin Q.-C., Chen C.-Y., Jiao C.-T., Tang Z.-G., Liu R.-H., Bao X.-H., Zeng L.-Z., Duan Y.-Q., Zhang G.-Y.
      Hemoglobin 8:569-581(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CHONGQING ARG-3 AND HARBIN MET-17.
    36. "Alpha-thalassaemia due to a single codon deletion in the alpha 1-globin gene. Computational structural analysis of the new alpha-chain variant."
      Ayala S., Colomer D., Gelpi J.L., Corron J.L.V.
      Hum. Mutat. 11:412-412(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CLINIC LYS-61 DEL.
    37. "Hb Davenport or alpha 2(78)(EF7)Asn-->His beta 2."
      Wilson J.B., Webber B.B., Plaseska D., de Alarcon P.A., McMillan S.K., Huisman T.H.J.
      Hemoglobin 14:599-605(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DAVENPORT HIS-79.
    38. "Hb Evans or alpha 262(E11)Val-->Met beta 2; an unstable hemoglobin causing a mild hemolytic anemia."
      Wilson J.B., Webber B.B., Kutlar A., Reese A.L., McKie V.C., Lutcher C.L., Felice A.E., Huisman T.H.J.
      Hemoglobin 13:557-566(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EVANS MET-63.
    39. "Locus assignment of two alpha-globin structural mutants from the Caribbean basin: alpha Fort de France (alpha 45 Arg) and alpha Spanish Town (alpha 27 Val)."
      Cash F.E., Monplaisir N., Goossens M., Liebhaber S.A.
      Blood 74:833-835(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SPANISH TOWN VAL-28 AND FORT DE FRANCE ARG-46.
    40. "Hb Godavari [alpha 95(G2)Pro-->Thr]: a neutral amino acid substitution in the alpha 1 beta 2 interface that modifies the electrophoretic mobility of hemoglobin."
      Wajcman H., Kister J., Riou J., Galacteros F., Girot R., Maier-Redelsperger M., Nayudu N.V.S., Giordano P.C.
      Hemoglobin 22:11-22(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GODAVARI THR-96.
    41. "Hemoglobin Grady: the first example of a variant with elongated chains due to an insertion of residues."
      Huisman T.H.J., Wilson J.B., Gravely M., Hubbard M.
      Proc. Natl. Acad. Sci. U.S.A. 71:3270-3273(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GRADY GLU-PHE-THR-119 INS.
    42. "A new alpha chain variant, Hb Hanamaki or alpha 2(139)(HC1)Lys-->Glu beta 2, found in a Japanese family."
      Orisaka M., Tajima T., Harano T., Harano K., Kushida Y., Imai K.
      Hemoglobin 16:67-71(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HANAMAKI GLU-140.
    43. "HB Handa [alpha 90 (FG 2) Lys replaced by Met]: structure and biosynthesis of a new slightly higher oxygen affinity variant."
      Harano T., Harano K., Shibata S., Ueda S., Imai K., Seki M.
      Hemoglobin 6:379-389(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HANDA MET-91.
    44. "Hemoglobin Hasharon (alpha-2-47 his(CD5)beta-2): a hemoglobin found in low concentration."
      Charache S., Mondzac A.M., Gessner U.
      J. Clin. Invest. 48:834-847(1969) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HASHARON HIS-48.
    45. "Hemoglobin Hobart or alpha 20(Bl)His-->Arg: a new alpha chain hemoglobin variant."
      Fleming P.J., Sumner D.R., Wyatt K., Hughes W.G., Melrose W.D., Jupe D.M.D., Baikie M.J.
      Hemoglobin 11:211-220(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HOBART ARG-21.
    46. "Haemoglobin Inkster (alpha2 85aspartic acid leads to valine beta2) coexisting with beta-thalassaemia in a Caucasian family."
      Reed R.E., Winter W.P., Rucknagel D.L.
      Br. J. Haematol. 26:475-484(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT INKSTER VAL-86.
    47. "Hb Kanagawa [alpha 40(C5)Lys-->Met]: a new alpha chain variant with an increased oxygen affinity."
      Miyashita H., Hashimoto K., Mohri H., Ohokubo T., Harano T., Harano K., Imai K.
      Hemoglobin 16:1-10(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT KANAGAWA MET-41.
    48. "Hb Kurdistan [alpha 47(CE5)Asp-->Tyr], a new alpha chain variant in combination with beta (0)-thalassemia."
      Giordano P.C., Harteveld C.L., Streng H., Oosterwijk J.C., Heister J.G.A.M., Amons R., Bernini L.F.
      Hemoglobin 18:11-18(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT KURDISTAN TYR-48.
    49. "Hb Kurosaki [alpha 7(A5)Lys-->Glu]: a new alpha chain variant found in a Japanese woman."
      Harano T., Harano K., Imai K., Murakami T., Matsubara H.
      Hemoglobin 19:197-201(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT KUROSAKI GLU-8.
    50. "A case of HB J-Meerut (or Hb J-Birmingham) [alpha 120(H3)Ala-->Glu]."
      Yalcin A., Avcu F., Beyan C., Guergey A., Ural A.U.
      Hemoglobin 18:433-435(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT J-MEERUT/J-BIRMINGHAM GLU-121.
    51. "Hb Melusine [alpha 114(GH2)Pro-->Ser]: a new neutral hemoglobin variant."
      Wacjman H., Klames G., Groff P., Prome D., Riou J., Galacteros F.
      Hemoglobin 17:397-405(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MELUSINE SER-115.
    52. "Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys) and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg)."
      Brimhall B., Jones R.T., Schneider R.G., Hosty T.S., Tomlin G., Atkins R.
      Biochim. Biophys. Acta 379:28-32(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MONTGOMERY ARG-49.
    53. "Hemoglobin Petah Tikva (alpha 110 Ala replaced by Asp): a new unstable variant with alpha-thalassemia-like expression."
      Honig G.R., Shamsuddin M., Zaizov R., Steinherz M., Solar I., Kirschman C.
      Blood 57:705-711(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PETAH TIKVA ASP-111.
    54. "Hemoglobin Phnom Penh [alpha117Phe(H1)-Ile-alpha118Thr(H2)]; evidence for a hotspot for insertion of residues in the third exon of the alpha1-globin gene."
      Wajcman H., Prehu M.O., Prehu C., Blouquit Y., Prome D., Galacteros F.
      Hum. Mutat. Suppl. 1:S20-S22(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PHNOM PENH ILE-118 INS.
    55. "Hb Port Huron [alpha 56 (E5)Lys-->Arg]: a new alpha chain variant."
      Zwerdling T., Williams S., Nasr S.A., Rucknagel D.L.
      Hemoglobin 15:381-391(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PORT HURON ARG-57.
    56. "Hemoglobin Sawara: alpha 6(A4) aspartic acid leads to alanine."
      Sumida I., Ohta Y., Imamura T., Yanase T.
      Biochim. Biophys. Acta 322:23-26(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SAWARA ALA-7.
    57. "Hb Shenyang (alpha 26 (B7) Ala replaced by Glu): a new unstable variant found in China."
      Zeng Y.-T., Huang S.-Z., Zhou X., Qiu X.-K., Dong Q., Li M., Bai J.
      Hemoglobin 6:625-628(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SHENYANG GLU-27.
    58. "Hemoglobin Suan-Dok (alpha 2 109 (G16) Leu replaced by Arg beta 2): an unstable variant associated with alpha-thalassemia."
      Sanguansermsri T., Matragoon S., Changloah L., Flatz G.
      Hemoglobin 3:161-174(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SUAN-DOK ARG-110.
    59. "Hyperunstable hemoglobin Toyama [alpha 2 136(H19)Leu----Arg beta 2]: detection and identification by in vitro biosynthesis with radioactive amino acids."
      Ohba Y., Yamamoto K., Hattori Y., Kawata R., Miyaji T.
      Hemoglobin 11:539-556(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN HEIBAN, VARIANT TOYAMA ARG-137.
    60. "Hb Sun Prairie or alpha(2)130(H13)Ala-->Pro beta 2, a new unstable variant occurring in low quantities."
      Harkness M., Harkness D.R., Kutlar F., Kutlar A., Wilson J.B., Webber B.B., Codrington J.F., Huisman T.H.J.
      Hemoglobin 14:479-489(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SUN PRAIRIE PRO-131.
    61. "HB Swan River [alpha 6(A4)Asp-->Gly] observed in a Japanese man."
      Harano T., Harano K., Imai K., Terunuma S.
      Hemoglobin 20:75-78(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SWAN RIVER GLY-7.
    62. "Hemoglobin Thionville. An alpha-chain variant with a substitution of a glutamate for valine at NA-1 and having an acetylated methionine NH2 terminus."
      Vasseur C., Blouquit Y., Kister J., Prome D., Kavanaugh J.S., Rogers P.H., Guillemin C., Arnone A., Galacteros F., Poyart C., Rosa J., Wajcman H.
      J. Biol. Chem. 267:12682-12691(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT THIONVILLE GLU-2.
    63. "Haemoglobin Tunis-Bizerte: a new alpha 1 globin 129 Leu-->Pro unstable variant with thalassaemic phenotype."
      Darbellay R., Mach-Pascual S., Rose K., Graf J., Beris P.
      Br. J. Haematol. 90:71-76(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TUNIS-BIZERTE PRO-130.
    64. "A new alpha chain variant, Hb Turriff [alpha 99(G6)Lys-->Glu]: the interference of abnormal hemoglobins in Hb A1c determination."
      Langdown J.V., Davidson R.J., Williamson D.
      Hemoglobin 16:11-17(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TURRIFF GLU-100.
    65. "Hb Val de Marne [alpha 133(H16)Ser-->Arg]: a new hemoglobin variant with moderate increase in oxygen affinity."
      Wacjman H., Kister J., M'Rad A., Marden M.C., Riou J., Galacteros F.
      Hemoglobin 17:407-417(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VAL DE MARNE ARG-134.
    66. "Hb Westmead: an alpha 2-globin gene mutation detected by polymerase chain reaction and Stu I cleavage."
      Jiang N.H., Liang S., Wen X.J., Liang R., Su C., Tang Z.
      Hemoglobin 15:291-295(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT WESTMEAD GLN-123.
    67. "Hemoglobin Woodville: alpha (2)6(A4) aspartic acid-->tyrosine."
      Como P.F., Barber S., Sage R.E., Kronenberg H.
      Hemoglobin 10:135-141(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT WOODVILLE TYR-7.
    68. "Hb Yuda or alpha 130(H13)Ala-->Asp; a new alpha chain variant with low oxygen affinity."
      Fujisawa K., Hattori Y., Ohba Y., Ando S.
      Hemoglobin 16:435-439(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT YUDA ASP-131.
    69. "Two new human hemoglobin variants caused by unusual mutational events: Hb Zaire contains a five residue repetition within the alpha-chain and Hb Duino has two residues substituted in the beta-chain."
      Wajcman H., Blouquit Y., Vasseur C., le Querrec A., Laniece M., Melevendi C., Rasore A., Galacteros F.
      Hum. Genet. 89:676-680(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ZAIRE HIS-LEU-PRO-ALA-GLU-117 INS.
    70. "Hb Aghia Sophia [alpha62(E11)Val-->0 (alpha1)], an 'in-frame' deletion causing alpha-thalassemia."
      Traeger-Synodinos J., Harteveld C.L., Kanavakis E., Giordano P.C., Kattamis C., Bernini L.F.
      Hemoglobin 23:317-324(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HBH VAL-63 DEL.
    71. "Two new alpha chain variants: Hb Boghe [alpha58(E7)His-->Gln, alpha2], a variant on the distal histidine, and Hb Charolles [alpha103(G10)His-Tyr, alpha1]."
      Lacan P., Francina A., Souillet G., Aubry M., Couprie N., Dementhon L., Becchi M.
      Hemoglobin 23:345-352(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BOGHE GLN-59, VARIANT CHAROLLES TYR-104.
    72. "Screening for mutations in human alpha-globin genes by nonradioactive single-strand conformation polymorphism."
      Jorge S.B., Melo M.B., Costa F.F., Sonati M.F.
      Braz. J. Med. Biol. Res. 36:1471-1474(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CAMPINAS VAL-27, VARIANT WEST ONE GLY-127.
    73. "Characterization of hemoglobin Bassett (alpha94Asp-->Ala), a variant with very low oxygen affinity."
      Abdulmalik O., Safo M.K., Lerner N.B., Ochotorena J., Daikhin E., Lakka V., Santacroce R., Abraham D.J., Asakura T.
      Am. J. Hematol. 77:268-276(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BASSETT ALA-95, CHARACTERIZATION OF VARIANT BASSETT ALA-95.
    74. "A novel mutation of the alpha2-globin causing alpha(+)-thalassemia: Hb Plasencia [alpha125(H8)Leu-->Arg (alpha2)."
      Martin G., Villegas A., Gonzalez F.A., Ropero P., Hojas R., Polo M., Mateo M., Salvador M., Benavente C.
      Hemoglobin 29:113-117(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PLASENCIA ARG-126.

    Entry informationi

    Entry nameiHBA_HUMAN
    AccessioniPrimary (citable) accession number: P69905
    Secondary accession number(s): P01922
    , Q1HDT5, Q3MIF5, Q53F97, Q96KF1, Q9NYR7, Q9UCM0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Gives blood its red color.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

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