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P68871

- HBB_HUMAN

UniProt

P68871 - HBB_HUMAN

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Protein

Hemoglobin subunit beta

Gene

HBB

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

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
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

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. platelet aggregation Source: UniProtKB
  8. positive regulation of cell death Source: BHF-UCL
  9. positive regulation of nitric oxide biosynthetic process Source: UniProtKB
  10. protein heterooligomerization Source: BHF-UCL
  11. regulation of blood pressure Source: UniProtKB-KW
  12. regulation of blood vessel size Source: UniProtKB-KW
  13. renal absorption Source: UniProtKB
  14. response to hydrogen peroxide Source: BHF-UCL
  15. small molecule metabolic process Source: Reactome
Complete GO annotation...

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: UniProtKB
  6. haptoglobin-hemoglobin complex Source: BHF-UCL
  7. hemoglobin complex Source: UniProtKB
Complete GO annotation...

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

BgeeiP68871.
ExpressionAtlasiP68871. baseline and differential.
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. 34 interactions.
IntActiP68871. 8 interactions.
MINTiMINT-5000306.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4M4AX-ray2.05B2-147[»]
4M4BX-ray2.00B2-147[»]
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[»]
4N8TX-ray1.90B2-147[»]
4NI0X-ray2.15B2-147[»]
4NI1X-ray1.90B2-147[»]
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.
GeneTreeiENSGT00760000119197.
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.

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MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS
60 70 80 90 100
TPDAVMGNPK VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD
110 120 130 140
PENFRLLGNV LVCVLAHHFG KEFTPPVQAA YQKVVAGVAN ALAHKYH
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 [» ]
4M4A X-ray 2.05 B 2-147 [» ]
4M4B X-ray 2.00 B 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 [» ]
4N8T X-ray 1.90 B 2-147 [» ]
4NI0 X-ray 2.15 B 2-147 [» ]
4NI1 X-ray 1.90 B 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. 34 interactions.
IntActi P68871. 8 interactions.
MINTi MINT-5000306.

Chemistry

ChEMBLi CHEMBL2095168.
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 GC11M005264.
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.
GeneTreei ENSGT00760000119197.
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

Bgeei P68871.
ExpressionAtlasi P68871. baseline and differential.
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

« Hide 'large scale' publications
  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: MODIFICATION 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.