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P68871

- HBB_HUMAN

UniProt

P68871 - HBB_HUMAN

Protein

Hemoglobin subunit beta

Gene

HBB

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.
    LVV-hemorphin-7 potentiates the activity of bradykinin, causing a decrease in blood pressure.
    Spinorphin: functions as an endogenous inhibitor of enkephalin-degrading enzymes such as DPP3, and as a selective antagonist of the P2RX3 receptor which is involved in pain signaling, these properties implicate it as a regulator of pain and inflammation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei2 – 212,3-bisphosphoglycerate; via amino nitrogen
    Binding sitei3 – 312,3-bisphosphoglycerate
    Sitei60 – 601Not glycated
    Metal bindingi64 – 641Iron (heme distal ligand)
    Binding sitei83 – 8312,3-bisphosphoglycerate
    Sitei83 – 831Not glycated
    Metal bindingi93 – 931Iron (heme proximal ligand)
    Sitei96 – 961Not glycated
    Sitei142 – 1421Susceptible to oxidation; associated with variant Atlanta, variant non-spherocytic haemolytic anemia and variant Christchurch
    Binding sitei144 – 14412,3-bisphosphoglycerate

    GO - Molecular functioni

    1. heme binding Source: InterPro
    2. hemoglobin binding Source: UniProtKB
    3. iron ion binding Source: InterPro
    4. oxygen binding Source: UniProtKB
    5. oxygen transporter activity Source: UniProtKB
    6. protein binding Source: IntAct

    GO - Biological processi

    1. bicarbonate transport Source: Reactome
    2. blood coagulation Source: Reactome
    3. hydrogen peroxide catabolic process Source: BHF-UCL
    4. nitric oxide transport Source: UniProtKB
    5. oxidation-reduction process Source: GOC
    6. oxygen transport Source: UniProtKB
    7. positive regulation of cell death Source: BHF-UCL
    8. positive regulation of nitric oxide biosynthetic process Source: UniProtKB
    9. protein heterooligomerization Source: BHF-UCL
    10. regulation of blood pressure Source: UniProtKB-KW
    11. regulation of blood vessel size Source: UniProtKB-KW
    12. renal absorption Source: UniProtKB
    13. response to hydrogen peroxide Source: BHF-UCL
    14. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hypotensive agent, Vasoactive

    Keywords - Biological processi

    Oxygen transport, Transport

    Keywords - Ligandi

    Heme, Iron, Metal-binding, Pyruvate

    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.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hemoglobin subunit beta
    Alternative name(s):
    Beta-globin
    Hemoglobin beta chain
    Cleaved into the following 2 chains:
    Gene namesi
    Name:HBB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:4827. HBB.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cytosol Source: Reactome
    3. endocytic vesicle lumen Source: Reactome
    4. extracellular region Source: Reactome
    5. extracellular vesicular exosome Source: UniProt
    6. haptoglobin-hemoglobin complex Source: BHF-UCL
    7. hemoglobin complex 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.4 Publications
    Note: The disease may be caused by mutations affecting the gene represented in this entry.
    Beta-thalassemia (B-THAL) [MIM:613985]: A form of thalassemia. Thalassemias are common monogenic diseases occurring mostly in Mediterranean and Southeast Asian populations. The hallmark of beta-thalassemia is an imbalance in globin-chain production in the adult HbA molecule. Absence of beta chain causes beta(0)-thalassemia, while reduced amounts of detectable beta globin causes beta(+)-thalassemia. In the severe forms of beta-thalassemia, the excess alpha globin chains accumulate in the developing erythroid precursors in the marrow. Their deposition leads to a vast increase in erythroid apoptosis that in turn causes ineffective erythropoiesis and severe microcytic hypochromic anemia. Clinically, beta-thalassemia is divided into thalassemia major which is transfusion dependent, thalassemia intermedia (of intermediate severity), and thalassemia minor that is asymptomatic.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Sickle cell anemia (SKCA) [MIM:603903]: Characterized by abnormally shaped red cells resulting in chronic anemia and periodic episodes of pain, serious infections and damage to vital organs. Normal red blood cells are round and flexible and flow easily through blood vessels, but in sickle cell anemia, the abnormal hemoglobin (called Hb S) causes red blood cells to become stiff. They are C-shaped and resembles a sickle. These stiffer red blood cells can led to microvascular occlusion thus cutting off the blood supply to nearby tissues.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Beta-thalassemia, dominant, inclusion body type (B-THALIB) [MIM:603902]: An autosomal dominant form of beta thalassemia characterized by moderate anemia, lifelong jaundice, cholelithiasis and splenomegaly, marked morphologic changes in the red cells, erythroid hyperplasia of the bone marrow with increased numbers of multinucleate red cell precursors, and the presence of large inclusion bodies in the normoblasts, both in the marrow and in the peripheral blood after splenectomy.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Congenital dyserythropoietic anemia, Disease mutation, Hereditary hemolytic anemia

    Organism-specific databases

    MIMi140700. phenotype.
    141900. gene+phenotype.
    603902. phenotype.
    603903. phenotype.
    613985. phenotype.
    Orphaneti330041. Autosomal dominant methemoglobinemia.
    231222. Beta-thalassemia intermedia.
    231214. Beta-thalassemia major.
    231237. Delta-beta-thalassemia.
    231226. Dominant beta-thalassemia.
    178330. Heinz body anemia.
    231242. Hemoglobin C - beta-thalassemia.
    2132. Hemoglobin C disease.
    90039. Hemoglobin D disease.
    231249. Hemoglobin E - beta-thalassemia.
    2133. Hemoglobin E disease.
    330032. Hemoglobin Lepore - beta-thalassemia.
    46532. Hereditary persistence of fetal hemoglobin - beta-thalassemia.
    251380. Hereditary persistence of fetal hemoglobin - sickle cell disease.
    251359. Sickle cell - beta-thalassemia disease.
    251365. Sickle cell - hemoglobin C disease.
    251370. Sickle cell - hemoglobin D disease.
    251375. Sickle cell - hemoglobin E disease.
    232. Sickle cell anemia.
    PharmGKBiPA29202.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 147146Hemoglobin subunit betaPRO_0000052976Add
    BLAST
    Peptidei33 – 4210LVV-hemorphin-7PRO_0000296641
    Peptidei33 – 397SpinorphinPRO_0000424226

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylvalineBy similarity
    Modified residuei2 – 21N-pyruvate 2-iminyl-valine; in Hb A1b
    Glycosylationi2 – 21N-linked (Glc) (glycation); in Hb A1c
    Glycosylationi9 – 91N-linked (Glc) (glycation)
    Glycosylationi18 – 181N-linked (Glc) (glycation)
    Modified residuei60 – 601N6-acetyllysine1 Publication
    Glycosylationi67 – 671N-linked (Glc) (glycation)
    Modified residuei83 – 831N6-acetyllysine1 Publication
    Modified residuei94 – 941S-nitrosocysteine2 Publications
    Glycosylationi121 – 1211N-linked (Glc) (glycation)
    Modified residuei145 – 1451N6-acetyllysine; alternate1 Publication
    Glycosylationi145 – 1451N-linked (Glc) (glycation); alternate

    Post-translational modificationi

    Glucose reacts non-enzymatically with the N-terminus of the beta chain to form a stable ketoamine linkage. This takes place slowly and continuously throughout the 120-day life span of the red blood cell. The rate of glycation is increased in patients with diabetes mellitus.
    S-nitrosylated; a nitric oxide group is first bound to Fe2+ and then transferred to Cys-94 to allow capture of O2.3 Publications
    Acetylated on Lys-60, Lys-83 and Lys-145 upon aspirin exposure.1 Publication

    Keywords - PTMi

    Acetylation, Glycation, Glycoprotein, S-nitrosylation

    Proteomic databases

    MaxQBiP68871.
    PaxDbiP68871.
    PeptideAtlasiP68871.
    PRIDEiP68871.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00654755.
    P68871.
    SWISS-2DPAGEP68871.
    UCD-2DPAGEP02023.
    P68871.

    PTM databases

    PhosphoSiteiP68871.

    Miscellaneous databases

    PMAP-CutDBP68871.

    Expressioni

    Tissue specificityi

    Red blood cells.1 Publication

    Gene expression databases

    ArrayExpressiP68871.
    BgeeiP68871.
    GenevestigatoriP68871.

    Organism-specific databases

    HPAiCAB009526.
    HPA043234.

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha chains and two beta chains in adult hemoglobin A (HbA). Heterotetramer of two zeta chains and two beta chains in hemoglobin Portland-2, detected in fetuses and neonates with homozygous alpha-thalassemia.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HBA2P6990520EBI-715554,EBI-714680
    HBZP020082EBI-715554,EBI-719843

    Protein-protein interaction databases

    BioGridi109293. 19 interactions.
    IntActiP68871. 8 interactions.
    MINTiMINT-5000306.

    Structurei

    Secondary structure

    1
    147
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 1712
    Helixi21 – 3515
    Helixi37 – 426
    Helixi44 – 463
    Helixi52 – 576
    Helixi59 – 7517
    Turni78 – 803
    Helixi82 – 9514
    Helixi102 – 11918
    Helixi120 – 1223
    Helixi125 – 14319
    Helixi144 – 1463

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A00X-ray2.00B/D3-147[»]
    1A01X-ray1.80B/D3-147[»]
    1A0UX-ray2.14B/D3-147[»]
    1A0ZX-ray2.00B/D3-147[»]
    1A3NX-ray1.80B/D2-147[»]
    1A3OX-ray1.80B/D2-147[»]
    1ABWX-ray2.00B/D3-147[»]
    1ABYX-ray2.60B/D3-147[»]
    1AJ9X-ray2.20B2-147[»]
    1B86X-ray2.50B/D2-147[»]
    1BABX-ray1.50B/D2-147[»]
    1BBBX-ray1.70B/D2-147[»]
    1BIJX-ray2.30B/D2-147[»]
    1BUWX-ray1.90B/D2-147[»]
    1BZ0X-ray1.50B/D2-147[»]
    1BZ1X-ray1.59B/D2-147[»]
    1BZZX-ray1.59B/D2-147[»]
    1C7BX-ray1.80B/D2-147[»]
    1C7CX-ray1.80B/D2-147[»]
    1C7DX-ray1.80B/D2-147[»]
    1CBLX-ray1.80A/B/C/D2-147[»]
    1CBMX-ray1.74A/B/C/D2-147[»]
    1CH4X-ray2.50A/B/C/D2-146[»]
    1CLSX-ray1.90B/D2-147[»]
    1CMYX-ray3.00B/D2-147[»]
    1COHX-ray2.90B/D2-147[»]
    1DKEX-ray2.10B/D2-147[»]
    1DXTX-ray1.70B/D1-147[»]
    1DXUX-ray1.70B/D3-147[»]
    1DXVX-ray1.70B/D3-147[»]
    1FN3X-ray2.48B/D2-147[»]
    1G9VX-ray1.85B/D2-147[»]
    1GBUX-ray1.80B/D2-147[»]
    1GBVX-ray2.00B/D2-147[»]
    1GLIX-ray2.50B/D3-147[»]
    1GZXX-ray2.10B/D2-147[»]
    1HABX-ray2.30B/D2-147[»]
    1HACX-ray2.60B/D2-147[»]
    1HBAX-ray2.10B/D2-147[»]
    1HBBX-ray1.90B/D2-147[»]
    1HBSX-ray3.00B/D/F/H2-147[»]
    1HCOX-ray2.70B2-147[»]
    1HDBX-ray2.20B/D2-147[»]
    1HGAX-ray2.10B/D2-147[»]
    1HGBX-ray2.10B/D2-147[»]
    1HGCX-ray2.10B/D2-147[»]
    1HHOX-ray2.10B2-147[»]
    1IRDX-ray1.25B2-147[»]
    1J3YX-ray1.55B/D/F/H2-147[»]
    1J3ZX-ray1.60B/D/F/H2-147[»]
    1J40X-ray1.45B/D/F/H2-147[»]
    1J41X-ray1.45B/D/F/H2-147[»]
    1J7SX-ray2.20B/D2-147[»]
    1J7WX-ray2.00B/D2-147[»]
    1J7YX-ray1.70B/D2-147[»]
    1JY7X-ray3.20B/D/Q/S/V/X2-147[»]
    1K0YX-ray1.87B/D2-147[»]
    1K1KX-ray2.00B2-147[»]
    1KD2X-ray1.87B/D2-147[»]
    1LFLX-ray2.70B/D/Q/S2-147[»]
    1LFQX-ray2.60B2-147[»]
    1LFTX-ray2.60B2-147[»]
    1LFVX-ray2.80B2-147[»]
    1LFYX-ray3.30B2-147[»]
    1LFZX-ray3.10B2-147[»]
    1LJWX-ray2.16B2-147[»]
    1M9PX-ray2.10B/D2-147[»]
    1MKOX-ray2.18B/D2-147[»]
    1NEJX-ray2.10B/D2-147[»]
    1NIHX-ray2.60B/D2-147[»]
    1NQPX-ray1.73B/D2-147[»]
    1O1IX-ray2.30B1-147[»]
    1O1JX-ray1.90B/D1-147[»]
    1O1KX-ray2.00B/D1-147[»]
    1O1LX-ray1.80B/D1-147[»]
    1O1MX-ray1.85B/D1-147[»]
    1O1NX-ray1.80B/D1-147[»]
    1O1OX-ray1.80B/D1-147[»]
    1O1PX-ray1.80B/D1-147[»]
    1QI8X-ray1.80B/D3-147[»]
    1QSHX-ray1.70B/D2-147[»]
    1QSIX-ray1.70B/D2-147[»]
    1QXDX-ray2.25B/D2-147[»]
    1QXEX-ray1.85B/D2-147[»]
    1R1XX-ray2.15B2-147[»]
    1R1YX-ray1.80B/D2-147[»]
    1RPSX-ray2.11B/D2-147[»]
    1RQ3X-ray1.91B/D2-147[»]
    1RQ4X-ray2.11B/D2-147[»]
    1RQAX-ray2.11B/D2-147[»]
    1RVWX-ray2.50B2-147[»]
    1SDKX-ray1.80B/D2-147[»]
    1SDLX-ray1.80B/D2-147[»]
    1THBX-ray1.50B/D2-147[»]
    1UIWX-ray1.50B/D/F/H2-147[»]
    1VWTX-ray1.90B/D2-147[»]
    1XXTX-ray1.91B/D2-147[»]
    1XY0X-ray1.99B/D2-147[»]
    1XYEX-ray2.13B/D2-147[»]
    1XZ2X-ray1.90B/D2-147[»]
    1XZ4X-ray2.00B/D2-147[»]
    1XZ5X-ray2.11B/D2-147[»]
    1XZ7X-ray1.90B/D2-147[»]
    1XZUX-ray2.16B/D2-147[»]
    1XZVX-ray2.11B/D2-147[»]
    1Y09X-ray2.25B/D2-147[»]
    1Y0AX-ray2.22B/D2-147[»]
    1Y0CX-ray2.30B/D2-147[»]
    1Y0DX-ray2.10B/D2-147[»]
    1Y0TX-ray2.14B/D2-147[»]
    1Y0WX-ray2.14B/D2-147[»]
    1Y22X-ray2.16B/D2-147[»]
    1Y2ZX-ray2.07B/D2-147[»]
    1Y31X-ray2.13B/D2-147[»]
    1Y35X-ray2.12B/D2-147[»]
    1Y45X-ray2.00B/D2-147[»]
    1Y46X-ray2.22B/D2-147[»]
    1Y4BX-ray2.10B/D2-147[»]
    1Y4FX-ray2.00B/D2-147[»]
    1Y4GX-ray1.91B/D2-147[»]
    1Y4PX-ray1.98B/D2-147[»]
    1Y4QX-ray2.11B/D2-147[»]
    1Y4RX-ray2.22B/D2-147[»]
    1Y4VX-ray1.84B/D2-147[»]
    1Y5FX-ray2.14B/D2-147[»]
    1Y5JX-ray2.03B/D2-147[»]
    1Y5KX-ray2.20B/D2-147[»]
    1Y7CX-ray2.10B/D2-147[»]
    1Y7DX-ray1.90B/D2-147[»]
    1Y7GX-ray2.10B/D2-147[»]
    1Y7ZX-ray1.98B/D2-147[»]
    1Y83X-ray1.90B/D2-145[»]
    1Y85X-ray2.13B/D2-146[»]
    1Y8WX-ray2.90B/D2-147[»]
    1YDZX-ray3.30B/D2-147[»]
    1YE0X-ray2.50B/D2-147[»]
    1YE1X-ray4.50B/D2-147[»]
    1YE2X-ray1.80B/D2-147[»]
    1YENX-ray2.80B/D2-147[»]
    1YEOX-ray2.22B/D2-147[»]
    1YEQX-ray2.75B/D2-147[»]
    1YEUX-ray2.12B/D2-147[»]
    1YEVX-ray2.11B/D2-147[»]
    1YFFX-ray2.40B/D/F/H2-147[»]
    1YG5X-ray2.70B/D2-147[»]
    1YGDX-ray2.73B/D2-147[»]
    1YGFX-ray2.70B/D2-147[»]
    1YH9X-ray2.20B/D2-147[»]
    1YHEX-ray2.10B/D2-147[»]
    1YHRX-ray2.60B/D2-147[»]
    1YIEX-ray2.40B/D2-147[»]
    1YIHX-ray2.00B/D2-147[»]
    1YVQX-ray1.80B/D2-147[»]
    1YVTX-ray1.80B2-147[»]
    1YZIX-ray2.07B2-147[»]
    2D5ZX-ray1.45B/D2-147[»]
    2D60X-ray1.70B/D2-147[»]
    2DN1X-ray1.25B2-147[»]
    2DN2X-ray1.25B/D2-147[»]
    2DN3X-ray1.25B2-147[»]
    2DXMneutron diffraction2.10B/D2-147[»]
    2H35NMR-B/D2-147[»]
    2HBCX-ray2.10B2-147[»]
    2HBDX-ray2.20B2-147[»]
    2HBEX-ray2.00B2-147[»]
    2HBFX-ray2.20B2-147[»]
    2HBSX-ray2.05B/D/F/H2-147[»]
    2HCOX-ray2.70B2-147[»]
    2HHBX-ray1.74B/D2-147[»]
    2HHDX-ray2.20B/D2-147[»]
    2HHEX-ray2.20B/D4-147[»]
    2M6ZNMR-B/D2-147[»]
    2W6VX-ray1.80B/D2-147[»]
    2W72X-ray1.07B/D3-147[»]
    2YRSX-ray2.30B/D/K/O2-147[»]
    3B75X-ray2.30B/D/F/H/T2-147[»]
    3D17X-ray2.80B/D2-147[»]
    3D7OX-ray1.80B2-147[»]
    3DUTX-ray1.55B/D2-147[»]
    3HHBX-ray1.74B/D2-147[»]
    3HXNX-ray2.00B/D2-147[»]
    3IC0X-ray1.80B/D2-147[»]
    3IC2X-ray2.40B/D2-147[»]
    3KMFneutron diffraction2.00C/G2-147[»]
    3NL7X-ray1.80B2-147[»]
    3NMMX-ray1.60B/D2-147[»]
    3ODQX-ray3.10B/D2-147[»]
    3ONZX-ray2.09B2-147[»]
    3OO4X-ray1.90B2-147[»]
    3OO5X-ray2.10B2-147[»]
    3P5QX-ray2.00B2-147[»]
    3QJBX-ray1.80B2-147[»]
    3QJCX-ray2.00B2-147[»]
    3QJDX-ray1.56B/D2-147[»]
    3QJEX-ray1.80B/D2-147[»]
    3R5IX-ray2.20B/D2-147[»]
    3S65X-ray1.80B/D2-147[»]
    3S66X-ray1.40B2-147[»]
    3SZKX-ray3.01B/E2-147[»]
    3W4UX-ray1.95B/D/F2-147[»]
    3WCPX-ray1.94B/D2-147[»]
    4FC3X-ray2.26B2-147[»]
    4HHBX-ray1.74B/D2-147[»]
    4IJ2X-ray4.24B/D2-147[»]
    4L7YX-ray1.80B/D2-147[»]
    4MQCX-ray2.20B2-147[»]
    4MQGX-ray1.68B2-147[»]
    4MQHX-ray2.50B2-147[»]
    4MQIX-ray1.92B2-147[»]
    4N7NX-ray2.75B/D/F/H/J/L2-147[»]
    4N7OX-ray2.50B/D/F/H/J/L2-147[»]
    4N7PX-ray2.81B/D/F/H/J/L2-147[»]
    6HBWX-ray2.00B/D2-147[»]
    ProteinModelPortaliP68871.
    SMRiP68871. Positions 2-147.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP68871.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the globin family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG269316.
    HOVERGENiHBG009709.
    InParanoidiP68871.
    KOiK13823.
    OrthoDBiEOG7B8S5H.
    PhylomeDBiP68871.
    TreeFamiTF333268.

    Family and domain databases

    Gene3Di1.10.490.10. 1 hit.
    InterProiIPR000971. Globin.
    IPR009050. Globin-like.
    IPR012292. Globin_dom.
    IPR002337. Haemoglobin_b.
    [Graphical view]
    PfamiPF00042. Globin. 1 hit.
    [Graphical view]
    PRINTSiPR00814. BETAHAEM.
    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.

    P68871-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS    50
    TPDAVMGNPK VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD 100
    PENFRLLGNV LVCVLAHHFG KEFTPPVQAA YQKVVAGVAN ALAHKYH 147
    Length:147
    Mass (Da):15,998
    Last modified:January 23, 2007 - v2
    Checksum:iA31F6D621C6556A1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261Missing in ACD39349. 1 PublicationCurated
    Sequence conflicti42 – 421F → L in AAR96398. 1 PublicationCurated

    Mass spectrometryi

    Molecular mass is 1310 Da from positions 33 - 42. Determined by FAB. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21V → A in Raleigh; O(2) affinity down.
    Corresponds to variant rs33949930 [ dbSNP | Ensembl ].
    VAR_002856
    Natural varianti3 – 31H → L in Graz. 1 Publication
    Corresponds to variant rs35906307 [ dbSNP | Ensembl ].
    VAR_002857
    Natural varianti3 – 31H → Q in Okayama; O(2) affinity up.
    Corresponds to variant rs713040 [ dbSNP | Ensembl ].
    VAR_002858
    Natural varianti3 – 31H → R in Deer Lodge; O(2) affinity up.
    Corresponds to variant rs33983205 [ dbSNP | Ensembl ].
    VAR_002859
    Natural varianti3 – 31H → Y in Fukuoka.
    Corresponds to variant rs35906307 [ dbSNP | Ensembl ].
    VAR_002860
    Natural varianti6 – 61P → R in Warwickshire.
    Corresponds to variant rs34769005 [ dbSNP | Ensembl ].
    VAR_002861
    Natural varianti7 – 71E → A in G-Makassar.
    Corresponds to variant rs334 [ dbSNP | Ensembl ].
    VAR_002862
    Natural varianti7 – 71E → K in C. 1 Publication
    Corresponds to variant rs33930165 [ dbSNP | Ensembl ].
    VAR_002864
    Natural varianti7 – 71E → Q in Machida.
    Corresponds to variant rs33930165 [ dbSNP | Ensembl ].
    VAR_002865
    Natural varianti7 – 71E → V in S; sickle cell anemia. 1 Publication
    Corresponds to variant rs334 [ dbSNP | Ensembl ].
    VAR_002863
    Natural varianti8 – 81E → G in G-San Jose; mildly unstable.
    Corresponds to variant rs34948328 [ dbSNP | Ensembl ].
    VAR_002866
    Natural varianti8 – 81E → K in G-Siriraj.
    Corresponds to variant rs34948328 [ dbSNP | Ensembl ].
    VAR_002867
    Natural varianti9 – 91K → E in N-Timone. 1 Publication
    Corresponds to variant rs33932981 [ dbSNP | Ensembl ].
    VAR_002868
    Natural varianti9 – 91K → Q in J-Luhe.
    Corresponds to variant rs33926764 [ dbSNP | Ensembl ].
    VAR_002869
    Natural varianti9 – 91K → T in Rio Grande. 1 Publication
    VAR_002870
    Natural varianti10 – 101S → C in Porto Alegre; O(2) affinity up.
    Corresponds to variant rs33918131 [ dbSNP | Ensembl ].
    VAR_002871
    Natural varianti11 – 111A → D in Ankara. 1 Publication
    Corresponds to variant rs33947457 [ dbSNP | Ensembl ].
    VAR_002872
    Natural varianti11 – 111A → V in Iraq-Halabja. 1 Publication
    VAR_025393
    Natural varianti12 – 121V → D in Windsor; O(2) affinity up; unstable. 1 Publication
    Corresponds to variant rs33974228 [ dbSNP | Ensembl ].
    VAR_002873
    Natural varianti12 – 121V → I in Hamilton.
    VAR_002874
    Natural varianti14 – 141A → D in J-Lens.
    Corresponds to variant rs35203747 [ dbSNP | Ensembl ].
    VAR_002875
    Natural varianti15 – 151L → P in Saki; unstable.
    VAR_002876
    Natural varianti15 – 151L → R in Soegn; unstable.
    Corresponds to variant rs33935445 [ dbSNP | Ensembl ].
    VAR_002877
    Natural varianti16 – 161W → G in Randwick; unstable. 1 Publication
    Corresponds to variant rs33946157 [ dbSNP | Ensembl ].
    VAR_002878
    Natural varianti16 – 161W → R in Belfast; O(2) affinity up; unstable.
    Corresponds to variant rs33946157 [ dbSNP | Ensembl ].
    VAR_002879
    Natural varianti17 – 171G → D in J-Baltimore/J-Trinidad/J-Ireland/J-Georgia/N-New Haven.
    VAR_002880
    Natural varianti17 – 171G → R in D-Bushman.
    VAR_002881
    Natural varianti18 – 181K → E in Nagasaki.
    Corresponds to variant rs33986703 [ dbSNP | Ensembl ].
    VAR_002882
    Natural varianti18 – 181K → N in J-Amiens.
    Corresponds to variant rs36006214 [ dbSNP | Ensembl ].
    VAR_002883
    Natural varianti18 – 181K → Q in Nikosia.
    Corresponds to variant rs33986703 [ dbSNP | Ensembl ].
    VAR_002884
    Natural varianti19 – 191V → M in Baden; slightly unstable.
    Corresponds to variant rs35802118 [ dbSNP | Ensembl ].
    VAR_002885
    Natural varianti20 – 201N → D in Alamo.
    Corresponds to variant rs34866629 [ dbSNP | Ensembl ].
    VAR_002886
    Natural varianti20 – 201N → K in D-Ouleh RABAH.
    VAR_002887
    Natural varianti20 – 201N → S in Malay.
    Corresponds to variant rs33972047 [ dbSNP | Ensembl ].
    VAR_002888
    Natural varianti21 – 211V → M in Olympia; O(2) affinity up.
    Corresponds to variant rs35890959 [ dbSNP | Ensembl ].
    VAR_002889
    Natural varianti22 – 221D → G in Connecticut; O(2) affinity down.
    Corresponds to variant rs33977536 [ dbSNP | Ensembl ].
    VAR_002890
    Natural varianti22 – 221D → H in Karlskoga. 1 Publication
    Corresponds to variant rs33950093 [ dbSNP | Ensembl ].
    VAR_002892
    Natural varianti22 – 221D → N in Cocody.
    VAR_002891
    Natural varianti22 – 221D → Y in Yusa.
    VAR_002893
    Natural varianti23 – 231E → A in G-Coushatta/G-Saskatoon/G-Taegu/Hsin Chu.
    Corresponds to variant rs33936254 [ dbSNP | Ensembl ].
    VAR_002894
    Natural varianti23 – 231E → G in G-Taipei.
    VAR_002895
    Natural varianti23 – 231E → K in E-Saskatoon; unstable.
    VAR_002896
    Natural varianti23 – 231E → Q in D-Iran.
    VAR_002897
    Natural varianti23 – 231E → V in D-Granada.
    VAR_002898
    Natural varianti24 – 241V → D in Strasbourg; O(2) affinity up.
    VAR_002899
    Natural varianti24 – 241V → F in Palmerston North; O(2) affinity up; unstable. 1 Publication
    VAR_002900
    Natural varianti24 – 241V → G in Miyashiro; O(2) affinity up; unstable. 1 Publication
    VAR_002901
    Natural varianti24 – 241Missing in Freiburg. 1 Publication
    Corresponds to variant rs34160180 [ dbSNP | Ensembl ].
    VAR_069169
    Natural varianti25 – 251G → D in Moscva; O(2) affinity down; unstable.
    VAR_002902
    Natural varianti25 – 251G → R in Riverdale-Bronx; O(2) affinity up; unstable.
    VAR_002903
    Natural varianti25 – 251G → V in Savannah; unstable.
    VAR_002904
    Natural varianti26 – 261G → D in J-Auckland; unstable; O(2) affinity down. 1 Publication
    VAR_002905
    Natural varianti26 – 261G → R in G-Taiwan Ami.
    VAR_002906
    Natural varianti27 – 271E → K in E. 2 Publications
    VAR_002907
    Natural varianti27 – 271E → V in Henri Mondor; slightly unstable.
    VAR_002908
    Natural varianti28 – 281A → D in Volga/Drenthe; unstable.
    VAR_002909
    Natural varianti28 – 281A → S in Knossos. 1 Publication
    VAR_002910
    Natural varianti28 – 281A → V in Grange-blanche; O(2) affinity up. 1 Publication
    VAR_002911
    Natural varianti29 – 291L → P in Genova/Hyogo; unstable.
    VAR_002912
    Natural varianti29 – 291L → Q in St Louis. 1 Publication
    VAR_035236
    Natural varianti30 – 301G → D in Lufkin; unstable.
    VAR_002913
    Natural varianti31 – 311R → S in Tacoma; unstable.
    Corresponds to variant rs1135071 [ dbSNP | Ensembl ].
    VAR_002914
    Natural varianti32 – 321L → P in Yokohama; unstable. 1 Publication
    VAR_002915
    Natural varianti33 – 331L → R in Castilla; unstable.
    VAR_002916
    Natural varianti33 – 331L → V in Muscat; slightly unstable. 1 Publication
    VAR_002917
    Natural varianti35 – 351V → D in Santander; unstable. 1 Publication
    VAR_025394
    Natural varianti35 – 351V → F in Pitie-Salpetriere; O(2) affinity up.
    VAR_002918
    Natural varianti35 – 351V → L in Nantes; increased oxygen affinity. 1 Publication
    VAR_025395
    Natural varianti36 – 361Y → F in Philly; O(2) affinity up; unstable.
    VAR_002919
    Natural varianti37 – 371P → R in Sunnybrook.
    VAR_002920
    Natural varianti37 – 371P → S in North Chicago; O(2) affinity up. 1 Publication
    VAR_002921
    Natural varianti37 – 371P → T in Linkoping/Finlandia; O(2) affinity up. 1 Publication
    VAR_002922
    Natural varianti38 – 381W → G in Howick. 1 Publication
    VAR_002923
    Natural varianti38 – 381W → R in Rothschild; O(2) affinity down.
    VAR_002925
    Natural varianti38 – 381W → S in Hirose; O(2) affinity up.
    VAR_002924
    Natural varianti39 – 391T → N in Hinwil; O(2) affinity up. 1 Publication
    VAR_002926
    Natural varianti40 – 401Q → E in Vaasa; unstable.
    Corresponds to variant rs76728603 [ dbSNP | Ensembl ].
    VAR_002927
    Natural varianti40 – 401Q → K in Alabama. 1 Publication
    Corresponds to variant rs76728603 [ dbSNP | Ensembl ].
    VAR_002928
    Natural varianti40 – 401Q → R in Tianshui.
    VAR_002929
    Natural varianti42 – 421F → Y in Mequon.
    VAR_002930
    Natural varianti42 – 421Missing in Bruxelles. 1 Publication
    VAR_035237
    Natural varianti43 – 431F → L in Louisville; unstable. 1 Publication
    VAR_002931
    Natural varianti43 – 431F → S in Hammersmith. 1 Publication
    VAR_035239
    Natural varianti43 – 431Missing in Bruxelles. 1 Publication
    VAR_035238
    Natural varianti44 – 441E → Q in Hoshida/Chaya.
    VAR_002932
    Natural varianti45 – 451S → C in Mississippi.
    VAR_002933
    Natural varianti46 – 461F → S in Cheverly; unstable.
    VAR_002934
    Natural varianti47 – 471G → E in K-Ibadan.
    VAR_002935
    Natural varianti48 – 481D → A in Avicenna.
    VAR_002936
    Natural varianti48 – 481D → G in Gavello.
    VAR_002937
    Natural varianti48 – 481D → Y in Maputo. 1 Publication
    VAR_002938
    Natural varianti49 – 491L → P in Bab-Saadoum; slightly unstable.
    VAR_002939
    Natural varianti50 – 501S → F in Las Palmas; slightly unstable. 2 Publications
    VAR_002940
    Natural varianti51 – 511T → K in Edmonton.
    VAR_002941
    Natural varianti52 – 521P → R in Willamette; O(2) affinity up; unstable.
    VAR_002942
    Natural varianti53 – 531D → A in Ocho Rios.
    VAR_002943
    Natural varianti53 – 531D → H in Summer Hill.
    VAR_002944
    Natural varianti55 – 551V → D in Jacksonville; O(2) affinity up; unstable. 1 Publication
    VAR_002945
    Natural varianti56 – 561M → K in Matera; unstable. 1 Publication
    VAR_002946
    Natural varianti57 – 571G → R in Hamadan.
    VAR_002947
    Natural varianti58 – 581N → K in G-ferrara; unstable.
    VAR_002948
    Natural varianti59 – 591P → R in Dhofar/Yukuhashi.
    VAR_002949
    Natural varianti60 – 601K → E in I-High Wycombe.
    VAR_002950
    Natural varianti61 – 611V → A in Collingwood; unstable.
    VAR_002951
    Natural varianti62 – 621K → E in N-Seatlle.
    VAR_002952
    Natural varianti62 – 621K → M in Bologna; O(2) affinity down.
    VAR_002953
    Natural varianti62 – 621K → N in Hikari.
    VAR_002954
    Natural varianti63 – 631A → D in J-Europa. 1 Publication
    VAR_002955
    Natural varianti63 – 631A → P in Duarte; unstable.
    VAR_002956
    Natural varianti64 – 641H → Y in M-Saskatoon; O(2) affinity up. 1 Publication
    VAR_002957
    Natural varianti66 – 661K → M in J-Antakya. 1 Publication
    VAR_002958
    Natural varianti66 – 661K → N in J-Sicilia. 1 Publication
    VAR_002959
    Natural varianti66 – 661K → Q in J-Cairo. 1 Publication
    VAR_002960
    Natural varianti67 – 671K → T in Chico; O(2) affinity down.
    VAR_002961
    Natural varianti68 – 681V → A in Sydney; unstable.
    VAR_002962
    Natural varianti68 – 681V → D in Bristol. 1 Publication
    VAR_035240
    Natural varianti68 – 681V → G in non-spherocytic haemolytic anemia; Manukau. 1 Publication
    Corresponds to variant rs33918343 [ dbSNP | Ensembl ].
    VAR_040060
    Natural varianti68 – 681V → M in Alesha; unstable. 1 Publication
    VAR_002963
    Natural varianti69 – 691L → H in Brisbane; O(2) affinity up. 1 Publication
    VAR_002964
    Natural varianti69 – 691L → P in Mizuho; unstable. 1 Publication
    VAR_002965
    Natural varianti70 – 701G → D in Rambam. 1 Publication
    VAR_002966
    Natural varianti70 – 701G → R in Kenitra.
    VAR_002967
    Natural varianti70 – 701G → S in City of Hope. 1 Publication
    VAR_002968
    Natural varianti71 – 711A → D in Seattle; O(2) affinity down; unstable.
    VAR_002969
    Natural varianti72 – 721F → S in Christchurch; unstable.
    VAR_002970
    Natural varianti74 – 741D → G in Tilburg; O(2) affinity down.
    VAR_002971
    Natural varianti74 – 741D → V in Mobile; O(2) affinity down.
    VAR_002972
    Natural varianti74 – 741D → Y in Vancouver; O(2) affinity down.
    VAR_002973
    Natural varianti75 – 751G → R in Aalborg; unstable.
    VAR_002974
    Natural varianti75 – 751G → V in Bushwick; unstable.
    VAR_002975
    Natural varianti76 – 761L → P in Atlanta; unstable. 1 Publication
    VAR_002976
    Natural varianti76 – 761L → R in Pasadena; O(2) affinity up; unstable.
    VAR_002977
    Natural varianti77 – 771A → D in J-Chicago.
    VAR_002978
    Natural varianti78 – 781H → D in J-Iran.
    VAR_002979
    Natural varianti78 – 781H → R in Costa Rica. 1 Publication
    VAR_002980
    Natural varianti78 – 781H → Y in Fukuyama.
    VAR_002981
    Natural varianti79 – 791L → R in Quin-hai. 1 Publication
    VAR_002982
    Natural varianti80 – 801D → Y in Tampa.
    VAR_002983
    Natural varianti81 – 811N → K in G-Szuhu/Gifu.
    VAR_002984
    Natural varianti82 – 821L → H in La Roche-sur-Yon; unstable and O(2) affinity up. 1 Publication
    VAR_012663
    Natural varianti82 – 821L → R in Baylor; unstable.
    VAR_002985
    Natural varianti82 – 821L → V.
    Corresponds to variant rs11549406 [ dbSNP | Ensembl ].
    VAR_049273
    Natural varianti83 – 831K → M in Helsinki; O(2) affinity up. 1 Publication
    VAR_002986
    Natural varianti83 – 831K → N in Providence.
    VAR_012664
    Natural varianti84 – 841G → D in Pyrgos. 1 Publication
    VAR_025396
    Natural varianti84 – 841G → R in Muskegon.
    VAR_002987
    Natural varianti85 – 851T → I in Kofu. 1 Publication
    VAR_002988
    Natural varianti87 – 871A → D in Olomouc; O(2) affinity up. 1 Publication
    VAR_002989
    Natural varianti88 – 881T → I in Quebec-Chori.
    VAR_002990
    Natural varianti88 – 881T → K in D-Ibadan.
    VAR_002991
    Natural varianti88 – 881T → P in Valletta.
    VAR_002992
    Natural varianti89 – 891L → P in Santa Ana; unstable.
    VAR_002993
    Natural varianti89 – 891L → R in Boras; unstable.
    VAR_002994
    Natural varianti90 – 901S → N in Creteil; O(2) affinity up.
    VAR_002995
    Natural varianti90 – 901S → R in Vanderbilt; O(2) affinity up.
    VAR_002996
    Natural varianti91 – 911E → D in Pierre-Benite; O(2) affinity up. 1 Publication
    VAR_002997
    Natural varianti91 – 911E → K in Agenogi; O(2) affinity down.
    VAR_002998
    Natural varianti92 – 921L → P in Sabine; unstable.
    VAR_002999
    Natural varianti92 – 921L → R in Caribbean; O(2) affinity down; unstable. 1 Publication
    VAR_003000
    Natural varianti93 – 931H → D in J-Altgelds Gardens; unstable. 1 Publication
    VAR_003001
    Natural varianti93 – 931H → N in Isehara; unstable. 1 Publication
    VAR_003002
    Natural varianti93 – 931H → P in Newcastle and Duino; associated with S-104 in Duino; unstable. 1 Publication
    VAR_003003
    Natural varianti93 – 931H → Q in Istambul; O(2) affinity up; unstable. 1 Publication
    VAR_003004
    Natural varianti94 – 941C → R in Okazaki; O(2) affinity up; unstable.
    VAR_003005
    Natural varianti95 – 951D → G in Chandigarh.
    VAR_003006
    Natural varianti95 – 951D → H in Barcelona; O(2) affinity up.
    VAR_003007
    Natural varianti95 – 951D → N in Bunbury; O(2) affinity up. 1 Publication
    VAR_003008
    Natural varianti96 – 961K → M in J-Cordoba.
    VAR_003009
    Natural varianti96 – 961K → N in Detroit.
    VAR_003010
    Natural varianti97 – 971L → P in Debrousse; unstable; O(2) affinity up. 1 Publication
    VAR_003011
    Natural varianti97 – 971L → V in Regina; O(2) affinity up.
    VAR_003012
    Natural varianti98 – 981H → L in Wood; O(2) affinity up.
    VAR_003013
    Natural varianti98 – 981H → P in Nagoya; O(2) affinity up; unstable. 1 Publication
    VAR_003014
    Natural varianti98 – 981H → Q in Malmoe; O(2) affinity up.
    VAR_003015
    Natural varianti98 – 981H → Y in Moriguchi.
    VAR_003016
    Natural varianti99 – 991V → G in Nottingham; unstable.
    VAR_003017
    Natural varianti100 – 1001D → E in Coimbra; O(2) affinity up. 1 Publication
    VAR_003018
    Natural varianti101 – 1011P → L in Brigham; O(2) affinity up.
    VAR_003019
    Natural varianti101 – 1011P → R in New Mexico.
    VAR_003020
    Natural varianti102 – 1021E → D in Potomac; O(2) affinity up.
    VAR_003021
    Natural varianti102 – 1021E → G in Alberta; O(2) affinity up.
    VAR_003022
    Natural varianti102 – 1021E → K in British Columbia; O(2) affinity up.
    VAR_003023
    Natural varianti102 – 1021E → Q in Rush; unstable. 1 Publication
    VAR_003024
    Natural varianti103 – 1031N → S in Beth Israel; O(2) affinity down; unstable.
    VAR_003025
    Natural varianti103 – 1031N → Y in St Mande; O(2) affinity down. 1 Publication
    VAR_003026
    Natural varianti104 – 1041F → L in Heathrow; O(2) affinity up.
    VAR_003027
    Natural varianti105 – 1051R → S in Camperdown and Duino; associated with P-92 in Duino; unstable. 2 Publications
    VAR_003028
    Natural varianti105 – 1051R → T in Sherwood Forest.
    VAR_003029
    Natural varianti108 – 1081G → R in Burke; O(2) affinity down; unstable. 1 Publication
    VAR_003030
    Natural varianti109 – 1091N → K in Presbyterian; O(2) affinity down; unstable. 1 Publication
    VAR_003031
    Natural varianti110 – 1101V → M in San Diego; O(2) affinity up.
    VAR_003032
    Natural varianti111 – 1111L → P in Showa-Yakushiji.
    VAR_003033
    Natural varianti112 – 1121V → A in Stanmore; O(2) affinity down; unstable. 1 Publication
    VAR_003034
    Natural varianti113 – 1131C → F in Canterbury. 1 Publication
    VAR_025397
    Natural varianti113 – 1131C → R in Indianapolis. 2 Publications
    VAR_003035
    Natural varianti113 – 1131C → Y in Yahata. 1 Publication
    VAR_003036
    Natural varianti115 – 1151L → M in Zengcheng. 1 Publication
    VAR_010144
    Natural varianti115 – 1151L → P in Durham-N.C./Brescia; causes beta-thalassemia. 3 Publications
    VAR_010145
    Natural varianti116 – 1161A → D in Hradec Kralove; unstable; causes severe beta-thalassemia. 1 Publication
    VAR_003037
    Natural varianti116 – 1161A → P in Madrid; unstable.
    VAR_003038
    Natural varianti117 – 1171H → L in Vexin; increased oxygen affinity. 1 Publication
    VAR_025398
    Natural varianti117 – 1171H → Q in Hafnia.
    VAR_003039
    Natural varianti118 – 1181H → P in Saitama; unstable. 1 Publication
    VAR_003040
    Natural varianti118 – 1181H → R in P-Galveston.
    VAR_003041
    Natural varianti118 – 1181H → Y in Tsukumi. 1 Publication
    VAR_025399
    Natural varianti120 – 1201G → A in Iowa.
    VAR_003042
    Natural varianti121 – 1211K → E in Hijiyama.
    VAR_003043
    Natural varianti121 – 1211K → I in Jianghua. 1 Publication
    VAR_003044
    Natural varianti121 – 1211K → Q in Takamatsu.
    VAR_003045
    Natural varianti122 – 1221E → A in D-Neath. 1 Publication
    VAR_003046
    Natural varianti122 – 1221E → G in St Francis.
    VAR_003047
    Natural varianti122 – 1221E → K in O-Arab.
    VAR_003049
    Natural varianti122 – 1221E → Q in D-Los Angeles/D-Punjab/D-Portugal/D-Chicago/D-Oak Ridge.
    VAR_003048
    Natural varianti122 – 1221E → V in D-Camperdown/Beograd.
    VAR_003050
    Natural varianti124 – 1241T → I in Villejuif; asymptomatic variant. 1 Publication
    VAR_003051
    Natural varianti125 – 1251P → Q in Ty Gard; O(2) affinity up. 1 Publication
    VAR_003053
    Natural varianti125 – 1251P → R in Khartoum; unstable.
    VAR_003052
    Natural varianti125 – 1251P → S in Tunis.
    VAR_003054
    Natural varianti127 – 1271V → A in Beirut.
    VAR_003055
    Natural varianti127 – 1271V → E in Hofu; unstable.
    VAR_003057
    Natural varianti127 – 1271V → G in Dhonburi/Neapolis; unstable; beta-thalassemia. 1 Publication
    VAR_003056
    Natural varianti128 – 1281Q → E in Complutense. 1 Publication
    VAR_003058
    Natural varianti128 – 1281Q → K in Brest; unstable. 1 Publication
    VAR_003059
    Natural varianti129 – 1291A → D in J-Guantanamo; unstable.
    VAR_003060
    Natural varianti130 – 1301A → P in Crete; O(2) affinity up; unstable.
    VAR_003061
    Natural varianti130 – 1301A → V in La Desirade; O(2) affinity down; unstable. 1 Publication
    VAR_003062
    Natural varianti131 – 1311Y → D in Wien; unstable.
    VAR_003063
    Natural varianti131 – 1311Y → S in Nevers.
    VAR_003064
    Natural varianti132 – 1321Q → E in Camden/Tokuchi/Motown.
    VAR_003065
    Natural varianti132 – 1321Q → K in Shelby/Leslie/Deaconess; unstable. 1 Publication
    VAR_003066
    Natural varianti132 – 1321Q → P in Shangai; unstable.
    VAR_003067
    Natural varianti132 – 1321Q → R in Sarrebourg; unstable.
    VAR_003068
    Natural varianti133 – 1331K → N in Yamagata; O(2) affinity down.
    VAR_003069
    Natural varianti133 – 1331K → Q in K-Woolwich.
    VAR_003070
    Natural varianti134 – 1341V → L in Extredemura.
    VAR_003071
    Natural varianti135 – 1351V → E in North Shore-Caracas; unstable. 1 Publication
    VAR_003072
    Natural varianti136 – 1361A → E in Beckman; O(2) affinity down; unstable.
    VAR_003073
    Natural varianti136 – 1361A → P in Altdorf; O(2) affinity up; unstable.
    VAR_003074
    Natural varianti137 – 1371G → D in Hope; O(2) affinity down; unstable.
    VAR_003075
    Natural varianti139 – 1391A → P in Brockton; unstable.
    VAR_003076
    Natural varianti140 – 1401N → D in Geelong; unstable. 1 Publication
    VAR_003077
    Natural varianti140 – 1401N → K in Hinsdale; O(2) affinity down. 1 Publication
    VAR_003078
    Natural varianti140 – 1401N → S in S-Wake; associated with V-6. 1 Publication
    VAR_025335
    Natural varianti140 – 1401N → Y in Aurora; O(2) affinity up. 1 Publication
    VAR_003079
    Natural varianti141 – 1411A → D in Himeji; unstable; O(2) affinity down. 1 Publication
    VAR_003080
    Natural varianti141 – 1411A → T in St Jacques: O(2) affinity up.
    VAR_003081
    Natural varianti141 – 1411A → V in Puttelange; polycythemia; O(2) affinity up. 1 Publication
    VAR_003082
    Natural varianti142 – 1421L → R in Olmsted; unstable.
    VAR_003083
    Natural varianti143 – 1431A → D in Ohio; O(2) affinity up.
    VAR_003084
    Natural varianti144 – 1441H → D in Rancho Mirage.
    VAR_003085
    Natural varianti144 – 1441H → P in Syracuse; O(2) affinity up.
    VAR_003087
    Natural varianti144 – 1441H → Q in Little Rock; O(2) affinity up.
    Corresponds to variant rs36020563 [ dbSNP | Ensembl ].
    VAR_003086
    Natural varianti144 – 1441H → R in Abruzzo; O(2) affinity up.
    VAR_003088
    Natural varianti145 – 1451K → E in Mito; O(2) affinity up.
    VAR_003089
    Natural varianti146 – 1461Y → C in Rainier; O(2) affinity up.
    VAR_003090
    Natural varianti146 – 1461Y → H in Bethesda; O(2) affinity up.
    VAR_003091
    Natural varianti147 – 1471H → D in Hiroshima; O(2) affinity up.
    VAR_003092
    Natural varianti147 – 1471H → L in Cowtown; O(2) affinity up.
    VAR_003093
    Natural varianti147 – 1471H → P in York; O(2) affinity up.
    VAR_003094
    Natural varianti147 – 1471H → Q in Kodaira; O(2) affinity up. 1 Publication
    VAR_003095

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25079 mRNA. Translation: AAA35597.1.
    V00499 Genomic DNA. Translation: CAA23758.1.
    DQ126270 Genomic DNA. Translation: AAZ39745.1.
    DQ126271 Genomic DNA. Translation: AAZ39746.1.
    DQ126272 Genomic DNA. Translation: AAZ39747.1.
    DQ126273 Genomic DNA. Translation: AAZ39748.1.
    DQ126274 Genomic DNA. Translation: AAZ39749.1.
    DQ126275 Genomic DNA. Translation: AAZ39750.1.
    DQ126276 Genomic DNA. Translation: AAZ39751.1.
    DQ126277 Genomic DNA. Translation: AAZ39752.1.
    DQ126278 Genomic DNA. Translation: AAZ39753.1.
    DQ126279 Genomic DNA. Translation: AAZ39754.1.
    DQ126280 Genomic DNA. Translation: AAZ39755.1.
    DQ126281 Genomic DNA. Translation: AAZ39756.1.
    DQ126282 Genomic DNA. Translation: AAZ39757.1.
    DQ126283 Genomic DNA. Translation: AAZ39758.1.
    DQ126284 Genomic DNA. Translation: AAZ39759.1.
    DQ126285 Genomic DNA. Translation: AAZ39760.1.
    DQ126286 Genomic DNA. Translation: AAZ39761.1.
    DQ126287 Genomic DNA. Translation: AAZ39762.1.
    DQ126288 Genomic DNA. Translation: AAZ39763.1.
    DQ126289 Genomic DNA. Translation: AAZ39764.1.
    DQ126290 Genomic DNA. Translation: AAZ39765.1.
    DQ126291 Genomic DNA. Translation: AAZ39766.1.
    DQ126292 Genomic DNA. Translation: AAZ39767.1.
    DQ126293 Genomic DNA. Translation: AAZ39768.1.
    DQ126294 Genomic DNA. Translation: AAZ39769.1.
    DQ126295 Genomic DNA. Translation: AAZ39770.1.
    DQ126296 Genomic DNA. Translation: AAZ39771.1.
    DQ126297 Genomic DNA. Translation: AAZ39772.1.
    DQ126298 Genomic DNA. Translation: AAZ39773.1.
    DQ126299 Genomic DNA. Translation: AAZ39774.1.
    DQ126300 Genomic DNA. Translation: AAZ39775.1.
    DQ126301 Genomic DNA. Translation: AAZ39776.1.
    DQ126302 Genomic DNA. Translation: AAZ39777.1.
    DQ126303 Genomic DNA. Translation: AAZ39778.1.
    DQ126304 Genomic DNA. Translation: AAZ39779.1.
    DQ126305 Genomic DNA. Translation: AAZ39780.1.
    DQ126306 Genomic DNA. Translation: AAZ39781.1.
    DQ126307 Genomic DNA. Translation: AAZ39782.1.
    DQ126308 Genomic DNA. Translation: AAZ39783.1.
    DQ126309 Genomic DNA. Translation: AAZ39784.1.
    DQ126310 Genomic DNA. Translation: AAZ39785.1.
    DQ126311 Genomic DNA. Translation: AAZ39786.1.
    DQ126312 Genomic DNA. Translation: AAZ39787.1.
    DQ126313 Genomic DNA. Translation: AAZ39788.1.
    DQ126314 Genomic DNA. Translation: AAZ39789.1.
    DQ126315 Genomic DNA. Translation: AAZ39790.1.
    DQ126316 Genomic DNA. Translation: AAZ39791.1.
    DQ126317 Genomic DNA. Translation: AAZ39792.1.
    DQ126318 Genomic DNA. Translation: AAZ39793.1.
    DQ126319 Genomic DNA. Translation: AAZ39794.1.
    DQ126320 Genomic DNA. Translation: AAZ39795.1.
    DQ126321 Genomic DNA. Translation: AAZ39796.1.
    DQ126322 Genomic DNA. Translation: AAZ39797.1.
    DQ126323 Genomic DNA. Translation: AAZ39798.1.
    DQ126324 Genomic DNA. Translation: AAZ39799.1.
    DQ126325 Genomic DNA. Translation: AAZ39800.1.
    AF007546 Genomic DNA. Translation: AAB62944.1.
    AF083883 Genomic DNA. Translation: AAL68978.1.
    AF117710 mRNA. Translation: AAD19696.1.
    AF181989 mRNA. Translation: AAF00489.1.
    AF349114 mRNA. Translation: AAK29639.1.
    AF527577 Genomic DNA. Translation: AAM92001.1.
    AY136510 mRNA. Translation: AAN11320.1.
    AY163866 Genomic DNA. Translation: AAN84548.1.
    AY260740 Genomic DNA. Translation: AAP21062.1.
    AY509193 mRNA. Translation: AAR96398.1.
    EF450778 Genomic DNA. Translation: ABO36678.1.
    EU694432 mRNA. Translation: ACD39349.1.
    AK311825 mRNA. Translation: BAG34767.1.
    CR536530 mRNA. Translation: CAG38767.1.
    CR541913 mRNA. Translation: CAG46711.1.
    CH471064 Genomic DNA. Translation: EAW68806.1.
    BC007075 mRNA. Translation: AAH07075.1.
    U01317 Genomic DNA. Translation: AAA16334.1.
    V00497 mRNA. Translation: CAA23756.1.
    V00500 mRNA. Translation: CAA23759.1. Sequence problems.
    L26462 Genomic DNA. Translation: AAA21100.1.
    L26463 Genomic DNA. Translation: AAA21101.1.
    L26464 Genomic DNA. Translation: AAA21102.1.
    L26465 Genomic DNA. Translation: AAA21103.1.
    L26466 Genomic DNA. Translation: AAA21104.1.
    L26467 Genomic DNA. Translation: AAA21105.1.
    L26468 Genomic DNA. Translation: AAA21106.1.
    L26469 Genomic DNA. Translation: AAA21107.1.
    L26470 Genomic DNA. Translation: AAA21108.1.
    L26471 Genomic DNA. Translation: AAA21109.1.
    L26472 Genomic DNA. Translation: AAA21110.1.
    L26473 Genomic DNA. Translation: AAA21111.1.
    L26474 Genomic DNA. Translation: AAA21112.1.
    L26475 Genomic DNA. Translation: AAA21113.1.
    L26476 Genomic DNA. Translation: AAA21114.1.
    L26477 Genomic DNA. Translation: AAA21115.1.
    L26478 Genomic DNA. Translation: AAA21116.1.
    L48213 Genomic DNA. Translation: AAA88063.1.
    L48214 Genomic DNA. Translation: AAA88061.1.
    L48215 Genomic DNA. Translation: AAA88059.1.
    L48216 Genomic DNA. Translation: AAA88065.1.
    L48217 Genomic DNA. Translation: AAA88067.1.
    M36640 Genomic DNA. Translation: AAA52634.1.
    M11428 mRNA. Translation: AAA52633.1.
    M25113 mRNA. Translation: AAA35966.1.
    L48932 Genomic DNA. Translation: AAA88054.1.
    CCDSiCCDS7753.1.
    PIRiA53136. HBHU.
    RefSeqiNP_000509.1. NM_000518.4.
    UniGeneiHs.523443.

    Genome annotation databases

    EnsembliENST00000335295; ENSP00000333994; ENSG00000244734.
    GeneIDi3043.
    KEGGihsa:3043.
    UCSCiuc001mae.1. human.

    Polymorphism databases

    DMDMi56749856.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    HbVar

    Human hemoglobin variants and thalassemias

    SHMPD

    The Singapore human mutation and polymorphism database

    Wikipedia

    Hemoglobin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25079 mRNA. Translation: AAA35597.1 .
    V00499 Genomic DNA. Translation: CAA23758.1 .
    DQ126270 Genomic DNA. Translation: AAZ39745.1 .
    DQ126271 Genomic DNA. Translation: AAZ39746.1 .
    DQ126272 Genomic DNA. Translation: AAZ39747.1 .
    DQ126273 Genomic DNA. Translation: AAZ39748.1 .
    DQ126274 Genomic DNA. Translation: AAZ39749.1 .
    DQ126275 Genomic DNA. Translation: AAZ39750.1 .
    DQ126276 Genomic DNA. Translation: AAZ39751.1 .
    DQ126277 Genomic DNA. Translation: AAZ39752.1 .
    DQ126278 Genomic DNA. Translation: AAZ39753.1 .
    DQ126279 Genomic DNA. Translation: AAZ39754.1 .
    DQ126280 Genomic DNA. Translation: AAZ39755.1 .
    DQ126281 Genomic DNA. Translation: AAZ39756.1 .
    DQ126282 Genomic DNA. Translation: AAZ39757.1 .
    DQ126283 Genomic DNA. Translation: AAZ39758.1 .
    DQ126284 Genomic DNA. Translation: AAZ39759.1 .
    DQ126285 Genomic DNA. Translation: AAZ39760.1 .
    DQ126286 Genomic DNA. Translation: AAZ39761.1 .
    DQ126287 Genomic DNA. Translation: AAZ39762.1 .
    DQ126288 Genomic DNA. Translation: AAZ39763.1 .
    DQ126289 Genomic DNA. Translation: AAZ39764.1 .
    DQ126290 Genomic DNA. Translation: AAZ39765.1 .
    DQ126291 Genomic DNA. Translation: AAZ39766.1 .
    DQ126292 Genomic DNA. Translation: AAZ39767.1 .
    DQ126293 Genomic DNA. Translation: AAZ39768.1 .
    DQ126294 Genomic DNA. Translation: AAZ39769.1 .
    DQ126295 Genomic DNA. Translation: AAZ39770.1 .
    DQ126296 Genomic DNA. Translation: AAZ39771.1 .
    DQ126297 Genomic DNA. Translation: AAZ39772.1 .
    DQ126298 Genomic DNA. Translation: AAZ39773.1 .
    DQ126299 Genomic DNA. Translation: AAZ39774.1 .
    DQ126300 Genomic DNA. Translation: AAZ39775.1 .
    DQ126301 Genomic DNA. Translation: AAZ39776.1 .
    DQ126302 Genomic DNA. Translation: AAZ39777.1 .
    DQ126303 Genomic DNA. Translation: AAZ39778.1 .
    DQ126304 Genomic DNA. Translation: AAZ39779.1 .
    DQ126305 Genomic DNA. Translation: AAZ39780.1 .
    DQ126306 Genomic DNA. Translation: AAZ39781.1 .
    DQ126307 Genomic DNA. Translation: AAZ39782.1 .
    DQ126308 Genomic DNA. Translation: AAZ39783.1 .
    DQ126309 Genomic DNA. Translation: AAZ39784.1 .
    DQ126310 Genomic DNA. Translation: AAZ39785.1 .
    DQ126311 Genomic DNA. Translation: AAZ39786.1 .
    DQ126312 Genomic DNA. Translation: AAZ39787.1 .
    DQ126313 Genomic DNA. Translation: AAZ39788.1 .
    DQ126314 Genomic DNA. Translation: AAZ39789.1 .
    DQ126315 Genomic DNA. Translation: AAZ39790.1 .
    DQ126316 Genomic DNA. Translation: AAZ39791.1 .
    DQ126317 Genomic DNA. Translation: AAZ39792.1 .
    DQ126318 Genomic DNA. Translation: AAZ39793.1 .
    DQ126319 Genomic DNA. Translation: AAZ39794.1 .
    DQ126320 Genomic DNA. Translation: AAZ39795.1 .
    DQ126321 Genomic DNA. Translation: AAZ39796.1 .
    DQ126322 Genomic DNA. Translation: AAZ39797.1 .
    DQ126323 Genomic DNA. Translation: AAZ39798.1 .
    DQ126324 Genomic DNA. Translation: AAZ39799.1 .
    DQ126325 Genomic DNA. Translation: AAZ39800.1 .
    AF007546 Genomic DNA. Translation: AAB62944.1 .
    AF083883 Genomic DNA. Translation: AAL68978.1 .
    AF117710 mRNA. Translation: AAD19696.1 .
    AF181989 mRNA. Translation: AAF00489.1 .
    AF349114 mRNA. Translation: AAK29639.1 .
    AF527577 Genomic DNA. Translation: AAM92001.1 .
    AY136510 mRNA. Translation: AAN11320.1 .
    AY163866 Genomic DNA. Translation: AAN84548.1 .
    AY260740 Genomic DNA. Translation: AAP21062.1 .
    AY509193 mRNA. Translation: AAR96398.1 .
    EF450778 Genomic DNA. Translation: ABO36678.1 .
    EU694432 mRNA. Translation: ACD39349.1 .
    AK311825 mRNA. Translation: BAG34767.1 .
    CR536530 mRNA. Translation: CAG38767.1 .
    CR541913 mRNA. Translation: CAG46711.1 .
    CH471064 Genomic DNA. Translation: EAW68806.1 .
    BC007075 mRNA. Translation: AAH07075.1 .
    U01317 Genomic DNA. Translation: AAA16334.1 .
    V00497 mRNA. Translation: CAA23756.1 .
    V00500 mRNA. Translation: CAA23759.1 . Sequence problems.
    L26462 Genomic DNA. Translation: AAA21100.1 .
    L26463 Genomic DNA. Translation: AAA21101.1 .
    L26464 Genomic DNA. Translation: AAA21102.1 .
    L26465 Genomic DNA. Translation: AAA21103.1 .
    L26466 Genomic DNA. Translation: AAA21104.1 .
    L26467 Genomic DNA. Translation: AAA21105.1 .
    L26468 Genomic DNA. Translation: AAA21106.1 .
    L26469 Genomic DNA. Translation: AAA21107.1 .
    L26470 Genomic DNA. Translation: AAA21108.1 .
    L26471 Genomic DNA. Translation: AAA21109.1 .
    L26472 Genomic DNA. Translation: AAA21110.1 .
    L26473 Genomic DNA. Translation: AAA21111.1 .
    L26474 Genomic DNA. Translation: AAA21112.1 .
    L26475 Genomic DNA. Translation: AAA21113.1 .
    L26476 Genomic DNA. Translation: AAA21114.1 .
    L26477 Genomic DNA. Translation: AAA21115.1 .
    L26478 Genomic DNA. Translation: AAA21116.1 .
    L48213 Genomic DNA. Translation: AAA88063.1 .
    L48214 Genomic DNA. Translation: AAA88061.1 .
    L48215 Genomic DNA. Translation: AAA88059.1 .
    L48216 Genomic DNA. Translation: AAA88065.1 .
    L48217 Genomic DNA. Translation: AAA88067.1 .
    M36640 Genomic DNA. Translation: AAA52634.1 .
    M11428 mRNA. Translation: AAA52633.1 .
    M25113 mRNA. Translation: AAA35966.1 .
    L48932 Genomic DNA. Translation: AAA88054.1 .
    CCDSi CCDS7753.1.
    PIRi A53136. HBHU.
    RefSeqi NP_000509.1. NM_000518.4.
    UniGenei Hs.523443.

    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 B/D 3-147 [» ]
    1A01 X-ray 1.80 B/D 3-147 [» ]
    1A0U X-ray 2.14 B/D 3-147 [» ]
    1A0Z X-ray 2.00 B/D 3-147 [» ]
    1A3N X-ray 1.80 B/D 2-147 [» ]
    1A3O X-ray 1.80 B/D 2-147 [» ]
    1ABW X-ray 2.00 B/D 3-147 [» ]
    1ABY X-ray 2.60 B/D 3-147 [» ]
    1AJ9 X-ray 2.20 B 2-147 [» ]
    1B86 X-ray 2.50 B/D 2-147 [» ]
    1BAB X-ray 1.50 B/D 2-147 [» ]
    1BBB X-ray 1.70 B/D 2-147 [» ]
    1BIJ X-ray 2.30 B/D 2-147 [» ]
    1BUW X-ray 1.90 B/D 2-147 [» ]
    1BZ0 X-ray 1.50 B/D 2-147 [» ]
    1BZ1 X-ray 1.59 B/D 2-147 [» ]
    1BZZ X-ray 1.59 B/D 2-147 [» ]
    1C7B X-ray 1.80 B/D 2-147 [» ]
    1C7C X-ray 1.80 B/D 2-147 [» ]
    1C7D X-ray 1.80 B/D 2-147 [» ]
    1CBL X-ray 1.80 A/B/C/D 2-147 [» ]
    1CBM X-ray 1.74 A/B/C/D 2-147 [» ]
    1CH4 X-ray 2.50 A/B/C/D 2-146 [» ]
    1CLS X-ray 1.90 B/D 2-147 [» ]
    1CMY X-ray 3.00 B/D 2-147 [» ]
    1COH X-ray 2.90 B/D 2-147 [» ]
    1DKE X-ray 2.10 B/D 2-147 [» ]
    1DXT X-ray 1.70 B/D 1-147 [» ]
    1DXU X-ray 1.70 B/D 3-147 [» ]
    1DXV X-ray 1.70 B/D 3-147 [» ]
    1FN3 X-ray 2.48 B/D 2-147 [» ]
    1G9V X-ray 1.85 B/D 2-147 [» ]
    1GBU X-ray 1.80 B/D 2-147 [» ]
    1GBV X-ray 2.00 B/D 2-147 [» ]
    1GLI X-ray 2.50 B/D 3-147 [» ]
    1GZX X-ray 2.10 B/D 2-147 [» ]
    1HAB X-ray 2.30 B/D 2-147 [» ]
    1HAC X-ray 2.60 B/D 2-147 [» ]
    1HBA X-ray 2.10 B/D 2-147 [» ]
    1HBB X-ray 1.90 B/D 2-147 [» ]
    1HBS X-ray 3.00 B/D/F/H 2-147 [» ]
    1HCO X-ray 2.70 B 2-147 [» ]
    1HDB X-ray 2.20 B/D 2-147 [» ]
    1HGA X-ray 2.10 B/D 2-147 [» ]
    1HGB X-ray 2.10 B/D 2-147 [» ]
    1HGC X-ray 2.10 B/D 2-147 [» ]
    1HHO X-ray 2.10 B 2-147 [» ]
    1IRD X-ray 1.25 B 2-147 [» ]
    1J3Y X-ray 1.55 B/D/F/H 2-147 [» ]
    1J3Z X-ray 1.60 B/D/F/H 2-147 [» ]
    1J40 X-ray 1.45 B/D/F/H 2-147 [» ]
    1J41 X-ray 1.45 B/D/F/H 2-147 [» ]
    1J7S X-ray 2.20 B/D 2-147 [» ]
    1J7W X-ray 2.00 B/D 2-147 [» ]
    1J7Y X-ray 1.70 B/D 2-147 [» ]
    1JY7 X-ray 3.20 B/D/Q/S/V/X 2-147 [» ]
    1K0Y X-ray 1.87 B/D 2-147 [» ]
    1K1K X-ray 2.00 B 2-147 [» ]
    1KD2 X-ray 1.87 B/D 2-147 [» ]
    1LFL X-ray 2.70 B/D/Q/S 2-147 [» ]
    1LFQ X-ray 2.60 B 2-147 [» ]
    1LFT X-ray 2.60 B 2-147 [» ]
    1LFV X-ray 2.80 B 2-147 [» ]
    1LFY X-ray 3.30 B 2-147 [» ]
    1LFZ X-ray 3.10 B 2-147 [» ]
    1LJW X-ray 2.16 B 2-147 [» ]
    1M9P X-ray 2.10 B/D 2-147 [» ]
    1MKO X-ray 2.18 B/D 2-147 [» ]
    1NEJ X-ray 2.10 B/D 2-147 [» ]
    1NIH X-ray 2.60 B/D 2-147 [» ]
    1NQP X-ray 1.73 B/D 2-147 [» ]
    1O1I X-ray 2.30 B 1-147 [» ]
    1O1J X-ray 1.90 B/D 1-147 [» ]
    1O1K X-ray 2.00 B/D 1-147 [» ]
    1O1L X-ray 1.80 B/D 1-147 [» ]
    1O1M X-ray 1.85 B/D 1-147 [» ]
    1O1N X-ray 1.80 B/D 1-147 [» ]
    1O1O X-ray 1.80 B/D 1-147 [» ]
    1O1P X-ray 1.80 B/D 1-147 [» ]
    1QI8 X-ray 1.80 B/D 3-147 [» ]
    1QSH X-ray 1.70 B/D 2-147 [» ]
    1QSI X-ray 1.70 B/D 2-147 [» ]
    1QXD X-ray 2.25 B/D 2-147 [» ]
    1QXE X-ray 1.85 B/D 2-147 [» ]
    1R1X X-ray 2.15 B 2-147 [» ]
    1R1Y X-ray 1.80 B/D 2-147 [» ]
    1RPS X-ray 2.11 B/D 2-147 [» ]
    1RQ3 X-ray 1.91 B/D 2-147 [» ]
    1RQ4 X-ray 2.11 B/D 2-147 [» ]
    1RQA X-ray 2.11 B/D 2-147 [» ]
    1RVW X-ray 2.50 B 2-147 [» ]
    1SDK X-ray 1.80 B/D 2-147 [» ]
    1SDL X-ray 1.80 B/D 2-147 [» ]
    1THB X-ray 1.50 B/D 2-147 [» ]
    1UIW X-ray 1.50 B/D/F/H 2-147 [» ]
    1VWT X-ray 1.90 B/D 2-147 [» ]
    1XXT X-ray 1.91 B/D 2-147 [» ]
    1XY0 X-ray 1.99 B/D 2-147 [» ]
    1XYE X-ray 2.13 B/D 2-147 [» ]
    1XZ2 X-ray 1.90 B/D 2-147 [» ]
    1XZ4 X-ray 2.00 B/D 2-147 [» ]
    1XZ5 X-ray 2.11 B/D 2-147 [» ]
    1XZ7 X-ray 1.90 B/D 2-147 [» ]
    1XZU X-ray 2.16 B/D 2-147 [» ]
    1XZV X-ray 2.11 B/D 2-147 [» ]
    1Y09 X-ray 2.25 B/D 2-147 [» ]
    1Y0A X-ray 2.22 B/D 2-147 [» ]
    1Y0C X-ray 2.30 B/D 2-147 [» ]
    1Y0D X-ray 2.10 B/D 2-147 [» ]
    1Y0T X-ray 2.14 B/D 2-147 [» ]
    1Y0W X-ray 2.14 B/D 2-147 [» ]
    1Y22 X-ray 2.16 B/D 2-147 [» ]
    1Y2Z X-ray 2.07 B/D 2-147 [» ]
    1Y31 X-ray 2.13 B/D 2-147 [» ]
    1Y35 X-ray 2.12 B/D 2-147 [» ]
    1Y45 X-ray 2.00 B/D 2-147 [» ]
    1Y46 X-ray 2.22 B/D 2-147 [» ]
    1Y4B X-ray 2.10 B/D 2-147 [» ]
    1Y4F X-ray 2.00 B/D 2-147 [» ]
    1Y4G X-ray 1.91 B/D 2-147 [» ]
    1Y4P X-ray 1.98 B/D 2-147 [» ]
    1Y4Q X-ray 2.11 B/D 2-147 [» ]
    1Y4R X-ray 2.22 B/D 2-147 [» ]
    1Y4V X-ray 1.84 B/D 2-147 [» ]
    1Y5F X-ray 2.14 B/D 2-147 [» ]
    1Y5J X-ray 2.03 B/D 2-147 [» ]
    1Y5K X-ray 2.20 B/D 2-147 [» ]
    1Y7C X-ray 2.10 B/D 2-147 [» ]
    1Y7D X-ray 1.90 B/D 2-147 [» ]
    1Y7G X-ray 2.10 B/D 2-147 [» ]
    1Y7Z X-ray 1.98 B/D 2-147 [» ]
    1Y83 X-ray 1.90 B/D 2-145 [» ]
    1Y85 X-ray 2.13 B/D 2-146 [» ]
    1Y8W X-ray 2.90 B/D 2-147 [» ]
    1YDZ X-ray 3.30 B/D 2-147 [» ]
    1YE0 X-ray 2.50 B/D 2-147 [» ]
    1YE1 X-ray 4.50 B/D 2-147 [» ]
    1YE2 X-ray 1.80 B/D 2-147 [» ]
    1YEN X-ray 2.80 B/D 2-147 [» ]
    1YEO X-ray 2.22 B/D 2-147 [» ]
    1YEQ X-ray 2.75 B/D 2-147 [» ]
    1YEU X-ray 2.12 B/D 2-147 [» ]
    1YEV X-ray 2.11 B/D 2-147 [» ]
    1YFF X-ray 2.40 B/D/F/H 2-147 [» ]
    1YG5 X-ray 2.70 B/D 2-147 [» ]
    1YGD X-ray 2.73 B/D 2-147 [» ]
    1YGF X-ray 2.70 B/D 2-147 [» ]
    1YH9 X-ray 2.20 B/D 2-147 [» ]
    1YHE X-ray 2.10 B/D 2-147 [» ]
    1YHR X-ray 2.60 B/D 2-147 [» ]
    1YIE X-ray 2.40 B/D 2-147 [» ]
    1YIH X-ray 2.00 B/D 2-147 [» ]
    1YVQ X-ray 1.80 B/D 2-147 [» ]
    1YVT X-ray 1.80 B 2-147 [» ]
    1YZI X-ray 2.07 B 2-147 [» ]
    2D5Z X-ray 1.45 B/D 2-147 [» ]
    2D60 X-ray 1.70 B/D 2-147 [» ]
    2DN1 X-ray 1.25 B 2-147 [» ]
    2DN2 X-ray 1.25 B/D 2-147 [» ]
    2DN3 X-ray 1.25 B 2-147 [» ]
    2DXM neutron diffraction 2.10 B/D 2-147 [» ]
    2H35 NMR - B/D 2-147 [» ]
    2HBC X-ray 2.10 B 2-147 [» ]
    2HBD X-ray 2.20 B 2-147 [» ]
    2HBE X-ray 2.00 B 2-147 [» ]
    2HBF X-ray 2.20 B 2-147 [» ]
    2HBS X-ray 2.05 B/D/F/H 2-147 [» ]
    2HCO X-ray 2.70 B 2-147 [» ]
    2HHB X-ray 1.74 B/D 2-147 [» ]
    2HHD X-ray 2.20 B/D 2-147 [» ]
    2HHE X-ray 2.20 B/D 4-147 [» ]
    2M6Z NMR - B/D 2-147 [» ]
    2W6V X-ray 1.80 B/D 2-147 [» ]
    2W72 X-ray 1.07 B/D 3-147 [» ]
    2YRS X-ray 2.30 B/D/K/O 2-147 [» ]
    3B75 X-ray 2.30 B/D/F/H/T 2-147 [» ]
    3D17 X-ray 2.80 B/D 2-147 [» ]
    3D7O X-ray 1.80 B 2-147 [» ]
    3DUT X-ray 1.55 B/D 2-147 [» ]
    3HHB X-ray 1.74 B/D 2-147 [» ]
    3HXN X-ray 2.00 B/D 2-147 [» ]
    3IC0 X-ray 1.80 B/D 2-147 [» ]
    3IC2 X-ray 2.40 B/D 2-147 [» ]
    3KMF neutron diffraction 2.00 C/G 2-147 [» ]
    3NL7 X-ray 1.80 B 2-147 [» ]
    3NMM X-ray 1.60 B/D 2-147 [» ]
    3ODQ X-ray 3.10 B/D 2-147 [» ]
    3ONZ X-ray 2.09 B 2-147 [» ]
    3OO4 X-ray 1.90 B 2-147 [» ]
    3OO5 X-ray 2.10 B 2-147 [» ]
    3P5Q X-ray 2.00 B 2-147 [» ]
    3QJB X-ray 1.80 B 2-147 [» ]
    3QJC X-ray 2.00 B 2-147 [» ]
    3QJD X-ray 1.56 B/D 2-147 [» ]
    3QJE X-ray 1.80 B/D 2-147 [» ]
    3R5I X-ray 2.20 B/D 2-147 [» ]
    3S65 X-ray 1.80 B/D 2-147 [» ]
    3S66 X-ray 1.40 B 2-147 [» ]
    3SZK X-ray 3.01 B/E 2-147 [» ]
    3W4U X-ray 1.95 B/D/F 2-147 [» ]
    3WCP X-ray 1.94 B/D 2-147 [» ]
    4FC3 X-ray 2.26 B 2-147 [» ]
    4HHB X-ray 1.74 B/D 2-147 [» ]
    4IJ2 X-ray 4.24 B/D 2-147 [» ]
    4L7Y X-ray 1.80 B/D 2-147 [» ]
    4MQC X-ray 2.20 B 2-147 [» ]
    4MQG X-ray 1.68 B 2-147 [» ]
    4MQH X-ray 2.50 B 2-147 [» ]
    4MQI X-ray 1.92 B 2-147 [» ]
    4N7N X-ray 2.75 B/D/F/H/J/L 2-147 [» ]
    4N7O X-ray 2.50 B/D/F/H/J/L 2-147 [» ]
    4N7P X-ray 2.81 B/D/F/H/J/L 2-147 [» ]
    6HBW X-ray 2.00 B/D 2-147 [» ]
    ProteinModelPortali P68871.
    SMRi P68871. Positions 2-147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109293. 19 interactions.
    IntActi P68871. 8 interactions.
    MINTi MINT-5000306.

    Chemistry

    ChEMBLi CHEMBL4331.
    DrugBanki DB00893. Iron Dextran.

    PTM databases

    PhosphoSitei P68871.

    Polymorphism databases

    DMDMi 56749856.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00654755.
    P68871.
    SWISS-2DPAGE P68871.
    UCD-2DPAGE P02023.
    P68871.

    Proteomic databases

    MaxQBi P68871.
    PaxDbi P68871.
    PeptideAtlasi P68871.
    PRIDEi P68871.

    Protocols and materials databases

    DNASUi 3043.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335295 ; ENSP00000333994 ; ENSG00000244734 .
    GeneIDi 3043.
    KEGGi hsa:3043.
    UCSCi uc001mae.1. human.

    Organism-specific databases

    CTDi 3043.
    GeneCardsi GC11M005257.
    GeneReviewsi HBB.
    HGNCi HGNC:4827. HBB.
    HPAi CAB009526.
    HPA043234.
    MIMi 140700. phenotype.
    141900. gene+phenotype.
    603902. phenotype.
    603903. phenotype.
    613985. phenotype.
    neXtProti NX_P68871.
    Orphaneti 330041. Autosomal dominant methemoglobinemia.
    231222. Beta-thalassemia intermedia.
    231214. Beta-thalassemia major.
    231237. Delta-beta-thalassemia.
    231226. Dominant beta-thalassemia.
    178330. Heinz body anemia.
    231242. Hemoglobin C - beta-thalassemia.
    2132. Hemoglobin C disease.
    90039. Hemoglobin D disease.
    231249. Hemoglobin E - beta-thalassemia.
    2133. Hemoglobin E disease.
    330032. Hemoglobin Lepore - beta-thalassemia.
    46532. Hereditary persistence of fetal hemoglobin - beta-thalassemia.
    251380. Hereditary persistence of fetal hemoglobin - sickle cell disease.
    251359. Sickle cell - beta-thalassemia disease.
    251365. Sickle cell - hemoglobin C disease.
    251370. Sickle cell - hemoglobin D disease.
    251375. Sickle cell - hemoglobin E disease.
    232. Sickle cell anemia.
    PharmGKBi PA29202.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG269316.
    HOVERGENi HBG009709.
    InParanoidi P68871.
    KOi K13823.
    OrthoDBi EOG7B8S5H.
    PhylomeDBi P68871.
    TreeFami TF333268.

    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.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    ChiTaRSi HBB. human.
    EvolutionaryTracei P68871.
    GeneWikii HBB.
    GenomeRNAii 3043.
    NextBioi 12048.
    PMAP-CutDB P68871.
    PROi P68871.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P68871.
    Bgeei P68871.
    Genevestigatori P68871.

    Family and domain databases

    Gene3Di 1.10.490.10. 1 hit.
    InterProi IPR000971. Globin.
    IPR009050. Globin-like.
    IPR012292. Globin_dom.
    IPR002337. Haemoglobin_b.
    [Graphical view ]
    Pfami PF00042. Globin. 1 hit.
    [Graphical view ]
    PRINTSi PR00814. BETAHAEM.
    SUPFAMi SSF46458. SSF46458. 1 hit.
    PROSITEi PS01033. GLOBIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence analysis of coding and noncoding regions of human beta-globin mRNA."
      Marotta C., Forget B., Cohen-Solal M., Weissman S.M.
      Prog. Nucleic Acid Res. Mol. Biol. 19:165-175(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The nucleotide sequence of the human beta-globin gene."
      Lawn R.M., Efstratiadis A., O'Connell C., Maniatis T.
      Cell 21:647-651(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The beta-globin recombinational hotspot reduces the effects of strong selection around HbC, a recently arisen mutation providing resistance to malaria."
      Wood E.T., Stover D.A., Slatkin M., Nachman M.W., Hammer M.F.
      Am. J. Hum. Genet. 77:637-642(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-7.
    4. "DNA sequence of the human beta-globin gene isolated from a healthy Chinese."
      Lu L., Hu Z.H., Du C.S., Fu Y.S.
      Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Unexpected patterns of globin mutations in thalassemia patients from north of Portugal."
      Cabeda J.M., Correia C., Estevinho A., Cardoso C., Amorim M.L., Cleto E., Vale L., Coimbra E., Pinho L., Justica B.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-113.
    6. "Rapid detection of electrophoretically silent, unstable human hemoglobin 'Louisville', (Beta; Phe 42 Leu/TTT to CTT) by cDNA sequencing of mRNA."
      Kutlar F., Harbin J., Brisco J., Kutlar A.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LOUISVILLE LEU-43.
      Tissue: Blood.
    7. "Electrophoretically silent, very unstable, thalassemic mutation at codon 114 of beta globin (hemoglobin Durham-N.C.) detected by cDNA sequencing of mRNA, from a Russian women."
      Kutlar F., Abboud M., Leithner C., Holley L., Brisco J., Kutlar A.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT DURHAM-N.C. PRO-115.
      Tissue: Blood.
    8. "A rare beta chain variant 'Hemoglobin Ty Gard:Pro 124 Gln' found in a Caucasian female with erythrocytosis."
      Kutlar F., Holley L., Leithner C., Kutlar A.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TY GARD GLN-125.
      Tissue: Blood.
    9. "Heterozygote C->A beta-thalassemia mutation at the intron-2/848 nucleotide of beta globin gene was detected on a Northern European (Caucasian) individual."
      Kutlar A., Vercellotti G.M., Glendenning M., Holley L., Elam D., Kutlar F.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    10. "A new hemoglobin, beta chain variant 'Hb S-Wake' confirmed to be on the same chromosome with hemoglobin S mutation, detected in an African-American family."
      Kutlar F., Lallinger R.R., Holley L., Glendenning M., Kutlar A.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-7 AND SER-140.
      Tissue: Blood.
    11. "Coexistence of the hemoglobin O-Arab (Glu 121 Lys) and beta-thalassemia (intron-2; nucleotide 745 C->G) was detected in a Turkish patient."
      Kutlar F., Elam D., Glendenning M., Kutlar A., Dincol G.
      Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT O-ARAB.
      Tissue: Blood.
    12. "Thalassaemic trait cause by C-T substitution at position -90 in proximal CACCC box of beta-globin gene in China family."
      Li W.J.
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    13. "The differently expressed genes in the lymphocyte of recovered SARS patients."
      Fan B., Xie L., Guan X.
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS PHE-50 AND PRO-76.
      Tissue: Lymphocyte.
    14. "Beta-thalassemia G->C mutation at the nucleotide 5 position of intron 1 of beta globin gene was detected in Asian-Indian female with two polymorphisms in cis."
      Mehta S., Li T., Davis D.H., Nechtman J., Kutlar F.
      Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Blood.
    15. "Hb Dothan: a novel beta chain variant due to (-GTG) deletion between the codons 25/26 of beta globin gene detected in a Caucasian male baby."
      Hilliard L.M., Patel N., Li T., Zhang H., Kutlar A., Kutlar F.
      Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    16. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Spleen.
    17. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    18. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    19. "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].
      Tissue: Skeletal muscle.
    20. "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 2-147.
    21. "Isolation of a hemoglobin-derived opioid peptide from cerebrospinal fluid of patients with cerebrovascular bleedings."
      Glaemsta E.-L., Meyerson B., Silberring J., Terenius L., Nyberg F.
      Biochem. Biophys. Res. Commun. 184:1060-1066(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 33-42, MASS SPECTROMETRY.
    22. Cited for: PROTEIN SEQUENCE OF 33-42.
    23. "Globin chain synthesis in hemolytic anemia reticulocytes. A case of hemoglobin Burke."
      Suzuki H., Wada C., Kamata K., Takahashi E., Sato N., Kunitomo T.
      Biochem. Mol. Biol. Int. 30:425-431(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 97-121, NUCLEOTIDE SEQUENCE [MRNA] OF 106-113, VARIANT BURKE ARG-108.
    24. "Cloning specific complete polyadenylylated 3'-terminal cDNA segments."
      Lang K.M., Spritz R.A.
      Gene 33:191-196(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-147.
    25. "X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin."
      Arnone A.
      Nature 237:146-149(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: BISPHOSPHOGLYCERATE BINDING.
    26. Cited for: ACETYLATION AT LYS-60; LYS-83 AND LYS-145.
    27. "The glycosylation of hemoglobin: relevance to diabetes mellitus."
      Bunn H.F., Gabbay K.H., Gallop P.M.
      Science 200:21-27(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCATION AT VAL-2.
    28. "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-9; LYS-18; LYS-67; LYS-121 AND LYS-145, LACK OF GLYCATION AT LYS-60; LYS-83 AND LYS-96.
    29. "Human hemoglobin Portland II (zeta 2 beta 2). Isolation and characterization of Portland hemoglobin components and their constituent globin chains."
      Randhawa Z.I., Jones R.T., Lie-Injo L.E.
      J. Biol. Chem. 259:7325-7330(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, TISSUE SPECIFICITY, PARTIAL PROTEIN SEQUENCE.
    30. "Haemoglobin binding with haptoglobin. Localization of the haptoglobin-binding sites on the beta-chain of human haemoglobin by synthetic overlapping peptides encompassing the entire chain."
      Yoshioka N., Atassi M.Z.
      Biochem. J. 234:453-456(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HAPTOGLOBIN.
    31. "Beta 141 Leu is not deleted in the unstable haemoglobin Atlanta-Coventry but is replaced by a novel amino acid of mass 129 daltons."
      Brennan S.O., Shaw J., Allen J., George P.M.
      Br. J. Haematol. 81:99-103(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: OXIDATION AT LEU-142.
    32. "S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control."
      Jia L., Bonaventura C., Bonaventura J., Stamler J.S.
      Nature 380:221-226(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: S-NITROSYLATION AT CYS-94.
    33. "Crystal structure of the S-nitroso form of liganded human hemoglobin."
      Chan N.L., Rogers P.H., Arnone A.
      Biochemistry 37:16459-16464(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: S-NITROSYLATION AT CYS-94.
    34. "Ancient origins of nitric oxide signaling in biological systems."
      Durner J., Gow A.J., Stamler J.S., Glazebrook J.
      Proc. Natl. Acad. Sci. U.S.A. 96:14206-14207(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NITRIC OXIDE-BINDING.
    35. "The role of beta chains in the control of the hemoglobin oxygen binding function: chimeric human/mouse proteins, structure, and function."
      Kidd R.D., Russell J.E., Watmough N.J., Baker E.N., Brittain T.
      Biochemistry 40:15669-15675(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    36. "Spinorphin as an endogenous inhibitor of enkephalin-degrading enzymes: roles in pain and inflammation."
      Yamamoto Y., Ono H., Ueda A., Shimamura M., Nishimura K., Hazato T.
      Curr. Protein Pept. Sci. 3:587-599(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION OF SPINORPHIN.
    37. "Hemorphin and hemorphin-like peptides isolated from dog pancreas and sheep brain are able to potentiate bradykinin activity in vivo."
      Ianzer D., Konno K., Xavier C.H., Stoecklin R., Santos R.A.S., de Camargo A.C.M., Pimenta D.C.
      Peptides 27:2957-2966(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SYNTHESIS OF 33-42, FUNCTION.
    38. "Structure-activity relationship studies of spinorphin as a potent and selective human P2X(3) receptor antagonist."
      Jung K.Y., Moon H.D., Lee G.E., Lim H.H., Park C.S., Kim Y.C.
      J. Med. Chem. 50:4543-4547(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF SPINORPHIN.
    39. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    40. "Structure of sickled erythrocytes and of sickle-cell hemoglobin fibers."
      Finch J.T., Perutz M.F., Bertles J.F., Doebler J.
      Proc. Natl. Acad. Sci. U.S.A. 70:718-722(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: ELECTRON MICROSCOPY OF SICKLE-CELL HEMOGLOBIN FIBERS.
    41. "Crystal structure of sickle-cell deoxyhemoglobin at 5 A resolution."
      Wishner B.C., Ward K.B., Lattman E.E., Love W.E.
      J. Mol. Biol. 98:179-194(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (5 ANGSTROMS) OF MUTANT VAL-7.
    42. "Three-dimensional Fourier synthesis of human deoxyhaemoglobin at 2.5-A resolution: refinement of the atomic model."
      Fermi G.
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      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN.
    43. "The structure of human carbonmonoxy haemoglobin at 2.7-A resolution."
      Baldwin J.M.
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      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF CARBONMONOXY HEMOGLOBIN.
    44. "The crystal structure of human deoxyhaemoglobin at 1.74 A resolution."
      Fermi G., Perutz M.F., Shaanan B., Fourme R.
      J. Mol. Biol. 175:159-174(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF DEOXYHEMOGLOBIN.
    45. "High-resolution X-ray study of deoxyhemoglobin Rothschild 37 beta Trp-->Arg: a mutation that creates an intersubunit chloride-binding site."
      Kavanaugh J.S., Rogers P.H., Case D.A., Arnone A.
      Biochemistry 31:4111-4121(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ROTHSCHILD ARG-38.
    46. "Structure-function relationships in the low-affinity mutant haemoglobin Aalborg (Gly74 (E18)beta-->Arg)."
      Fermi G., Perutz M.F., Williamson D., Stein P., Shih D.T.
      J. Mol. Biol. 226:883-888(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ARG-75.
    47. "Human deoxyhaemoglobin-2,3-diphosphoglycerate complex low-salt structure at 2.5 A resolution."
      Richard V., Dodson G.G., Mauguen Y.
      J. Mol. Biol. 233:270-274(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), BISPHOSPHOGLYCERATE BINDING.
    48. "Crystal structure of T state haemoglobin with oxygen bound at all four haems."
      Paoli M., Liddington R., Tame J., Wilkinson A., Dodson G.
      J. Mol. Biol. 256:775-792(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    49. "High-resolution crystal structures of human hemoglobin with mutations at tryptophan 37beta: structural basis for a high-affinity T-state."
      Kavanaugh J.S., Weydert J.A., Rogers P.H., Arnone A.
      Biochemistry 37:4358-4373(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-38; GLU-38; GLY-38 AND TYR-38.
    50. "Crystal structure of deoxy-human hemoglobin beta6 Glu-->T