Details for: HBB

Gene ID: 3043

Symbol: HBB

Ensembl ID: ENSG00000244734

Description: hemoglobin subunit beta

Associated with

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: basophilic erythroblast (CL0000549)
    Fold Change: 322.5252
    Cell Significance Index: 146.8800
  • Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
    Fold Change: 27.1247
    Cell Significance Index: -6.8800
  • Cell Name: mononuclear cell (CL0000842)
    Fold Change: 18.8589
    Cell Significance Index: 78.4900
  • Cell Name: adipocyte of breast (CL0002617)
    Fold Change: 5.6535
    Cell Significance Index: 71.1900
  • Cell Name: hepatoblast (CL0005026)
    Fold Change: 4.2725
    Cell Significance Index: 71.8600
  • Cell Name: mesothelial cell of epicardium (CL0011019)
    Fold Change: 3.7389
    Cell Significance Index: 32.3400
  • Cell Name: stromal cell of bone marrow (CL0010001)
    Fold Change: 3.4592
    Cell Significance Index: -13.6500
  • Cell Name: fetal cardiomyocyte (CL0002495)
    Fold Change: 3.3952
    Cell Significance Index: 9.7300
  • Cell Name: preadipocyte (CL0002334)
    Fold Change: 3.0840
    Cell Significance Index: 60.1900
  • Cell Name: intestinal tuft cell (CL0019032)
    Fold Change: 2.1443
    Cell Significance Index: 131.4700
  • Cell Name: enteroendocrine cell of small intestine (CL0009006)
    Fold Change: 2.1156
    Cell Significance Index: 52.8900
  • Cell Name: eye photoreceptor cell (CL0000287)
    Fold Change: 2.0993
    Cell Significance Index: 132.3100
  • Cell Name: keratocyte (CL0002363)
    Fold Change: 1.8418
    Cell Significance Index: 29.2200
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 1.2393
    Cell Significance Index: 245.9500
  • Cell Name: stem cell of epidermis (CL1000428)
    Fold Change: 0.9852
    Cell Significance Index: 2.9300
  • Cell Name: umbrella cell of urothelium (CL4030056)
    Fold Change: 0.8926
    Cell Significance Index: 8.2200
  • Cell Name: cortical cell of adrenal gland (CL0002097)
    Fold Change: 0.8362
    Cell Significance Index: 22.4100
  • Cell Name: reticular cell (CL0000432)
    Fold Change: 0.5965
    Cell Significance Index: 3.8000
  • Cell Name: peg cell (CL4033014)
    Fold Change: 0.5900
    Cell Significance Index: 13.6300
  • Cell Name: forebrain neuroblast (CL1000042)
    Fold Change: 0.5060
    Cell Significance Index: 31.1000
  • Cell Name: tuft cell of colon (CL0009041)
    Fold Change: 0.4305
    Cell Significance Index: 388.7500
  • Cell Name: odontoblast (CL0000060)
    Fold Change: 0.3875
    Cell Significance Index: 49.6800
  • Cell Name: foveolar cell of stomach (CL0002179)
    Fold Change: 0.3819
    Cell Significance Index: 2.4900
  • Cell Name: interstitial cell of ovary (CL0002094)
    Fold Change: 0.3732
    Cell Significance Index: 4.7800
  • Cell Name: reticulocyte (CL0000558)
    Fold Change: 0.2889
    Cell Significance Index: 1.5200
  • Cell Name: neutrophil progenitor cell (CL0000834)
    Fold Change: 0.2176
    Cell Significance Index: 5.8200
  • Cell Name: enteroendocrine cell of colon (CL0009042)
    Fold Change: 0.1785
    Cell Significance Index: 33.9700
  • Cell Name: pulmonary alveolar epithelial cell (CL0000322)
    Fold Change: 0.1711
    Cell Significance Index: 129.5100
  • Cell Name: basal cell of urothelium (CL1000486)
    Fold Change: 0.1493
    Cell Significance Index: 18.3600
  • Cell Name: dopaminergic neuron (CL0000700)
    Fold Change: 0.0900
    Cell Significance Index: 25.8900
  • Cell Name: colon goblet cell (CL0009039)
    Fold Change: 0.0888
    Cell Significance Index: 8.7800
  • Cell Name: epithelial cell of small intestine (CL0002254)
    Fold Change: 0.0871
    Cell Significance Index: 14.1700
  • Cell Name: endocardial cell (CL0002350)
    Fold Change: 0.0847
    Cell Significance Index: 0.5000
  • Cell Name: ventricular cardiac muscle cell (CL2000046)
    Fold Change: 0.0813
    Cell Significance Index: 0.3600
  • Cell Name: intestinal crypt stem cell of colon (CL0009043)
    Fold Change: 0.0550
    Cell Significance Index: 5.9900
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: 0.0327
    Cell Significance Index: 3.3400
  • Cell Name: intermediate cell of urothelium (CL4030055)
    Fold Change: 0.0197
    Cell Significance Index: 3.5600
  • Cell Name: endothelial cell of venule (CL1000414)
    Fold Change: 0.0026
    Cell Significance Index: 0.0300
  • Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
    Fold Change: 0.0025
    Cell Significance Index: 0.1900
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: -0.0059
    Cell Significance Index: -11.0700
  • Cell Name: small intestine goblet cell (CL1000495)
    Fold Change: -0.0063
    Cell Significance Index: -0.2200
  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: -0.0078
    Cell Significance Index: -14.3500
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: -0.0116
    Cell Significance Index: -17.8000
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: -0.0133
    Cell Significance Index: -18.0200
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: -0.0194
    Cell Significance Index: -12.2900
  • Cell Name: pancreatic A cell (CL0000171)
    Fold Change: -0.0213
    Cell Significance Index: -15.8100
  • Cell Name: hair follicular keratinocyte (CL2000092)
    Fold Change: -0.0219
    Cell Significance Index: -9.6800
  • Cell Name: pancreatic PP cell (CL0002275)
    Fold Change: -0.0238
    Cell Significance Index: -14.8700
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: -0.0246
    Cell Significance Index: -11.1500
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: -0.0265
    Cell Significance Index: -14.4700
  • Cell Name: enterocyte of epithelium of small intestine (CL1000334)
    Fold Change: -0.0278
    Cell Significance Index: -0.8000
  • Cell Name: type B pancreatic cell (CL0000169)
    Fold Change: -0.0282
    Cell Significance Index: -15.9200
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: -0.0295
    Cell Significance Index: -1.3400
  • Cell Name: cortical interneuron (CL0008031)
    Fold Change: -0.0325
    Cell Significance Index: -0.7800
  • Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: -0.0347
    Cell Significance Index: -12.4300
  • Cell Name: lactocyte (CL0002325)
    Fold Change: -0.0488
    Cell Significance Index: -6.3000
  • Cell Name: stromal cell of ovary (CL0002132)
    Fold Change: -0.0504
    Cell Significance Index: -6.9200
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: -0.0595
    Cell Significance Index: -11.9400
  • Cell Name: pigmented ciliary epithelial cell (CL0002303)
    Fold Change: -0.0704
    Cell Significance Index: -10.2300
  • Cell Name: paneth cell of epithelium of small intestine (CL1000343)
    Fold Change: -0.0715
    Cell Significance Index: -1.5500
  • Cell Name: microfold cell of epithelium of small intestine (CL1000353)
    Fold Change: -0.0735
    Cell Significance Index: -5.0900
  • Cell Name: pancreatic D cell (CL0000173)
    Fold Change: -0.0742
    Cell Significance Index: -15.6200
  • Cell Name: early promyelocyte (CL0002154)
    Fold Change: -0.0768
    Cell Significance Index: -0.4900
  • Cell Name: pancreatic acinar cell (CL0002064)
    Fold Change: -0.0796
    Cell Significance Index: -13.5900
  • Cell Name: seromucus secreting cell (CL0000159)
    Fold Change: -0.0954
    Cell Significance Index: -1.9900
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: -0.1163
    Cell Significance Index: -13.7100
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: -0.1187
    Cell Significance Index: -9.1100
  • Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
    Fold Change: -0.1296
    Cell Significance Index: -6.0900
  • Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
    Fold Change: -0.1320
    Cell Significance Index: -13.7400
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: -0.1417
    Cell Significance Index: -16.2300
  • Cell Name: early pro-B cell (CL0002046)
    Fold Change: -0.1423
    Cell Significance Index: -9.1800
  • Cell Name: erythrocyte (CL0000232)
    Fold Change: -0.1629
    Cell Significance Index: -4.1500
  • Cell Name: mesenchymal cell (CL0008019)
    Fold Change: -0.1688
    Cell Significance Index: -2.8300
  • Cell Name: hippocampal granule cell (CL0001033)
    Fold Change: -0.1770
    Cell Significance Index: -11.9000
  • Cell Name: late promyelocyte (CL0002151)
    Fold Change: -0.1862
    Cell Significance Index: -1.2400
  • Cell Name: fallopian tube secretory epithelial cell (CL4030006)
    Fold Change: -0.1984
    Cell Significance Index: -3.0700
  • Cell Name: sebum secreting cell (CL0000317)
    Fold Change: -0.1998
    Cell Significance Index: -14.1300
  • Cell Name: placental villous trophoblast (CL2000060)
    Fold Change: -0.2069
    Cell Significance Index: -5.5300
  • Cell Name: vascular lymphangioblast (CL0005022)
    Fold Change: -0.2213
    Cell Significance Index: -3.9100
  • Cell Name: retinal rod cell (CL0000604)
    Fold Change: -0.2219
    Cell Significance Index: -2.6500
  • Cell Name: glycinergic neuron (CL1001509)
    Fold Change: -0.2426
    Cell Significance Index: -12.7400
  • Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
    Fold Change: -0.2537
    Cell Significance Index: -5.4000
  • Cell Name: retinal progenitor cell (CL0002672)
    Fold Change: -0.2730
    Cell Significance Index: -15.3200
  • Cell Name: CD4-positive, alpha-beta thymocyte (CL0000810)
    Fold Change: -0.2999
    Cell Significance Index: -5.1700
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: -0.3005
    Cell Significance Index: -15.6100
  • Cell Name: granulosa cell (CL0000501)
    Fold Change: -0.3016
    Cell Significance Index: -7.9300
  • Cell Name: periportal region hepatocyte (CL0019026)
    Fold Change: -0.3269
    Cell Significance Index: -4.8300
  • Cell Name: kidney epithelial cell (CL0002518)
    Fold Change: -0.3361
    Cell Significance Index: -9.9000
  • Cell Name: eukaryotic cell (CL0000255)
    Fold Change: -0.3406
    Cell Significance Index: -14.8100
  • Cell Name: acinar cell of salivary gland (CL0002623)
    Fold Change: -0.3516
    Cell Significance Index: -16.4000
  • Cell Name: indirect pathway medium spiny neuron (CL4023029)
    Fold Change: -0.3520
    Cell Significance Index: -15.5700
  • Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
    Fold Change: -0.3646
    Cell Significance Index: -12.6700
  • Cell Name: fibro/adipogenic progenitor cell (CL0009099)
    Fold Change: -0.3668
    Cell Significance Index: -18.5400
  • Cell Name: stratified epithelial cell (CL0000079)
    Fold Change: -0.3716
    Cell Significance Index: -13.6400
  • Cell Name: erythroblast (CL0000765)
    Fold Change: -0.4051
    Cell Significance Index: -4.8300
  • Cell Name: L6b glutamatergic cortical neuron (CL4023038)
    Fold Change: -0.4056
    Cell Significance Index: -13.2800
  • Cell Name: cardiac muscle cell (CL0000746)
    Fold Change: -0.4084
    Cell Significance Index: -6.0300
  • Cell Name: direct pathway medium spiny neuron (CL4023026)
    Fold Change: -0.4093
    Cell Significance Index: -15.5000
  • Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
    Fold Change: -0.4250
    Cell Significance Index: -14.8900
  • Cell Name: hippocampal pyramidal neuron (CL1001571)
    Fold Change: -0.4254
    Cell Significance Index: -12.1400

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Other Information

**Key Characteristics:** 1. **Structure**: The HBB gene encodes for a 146-amino acid protein, which is part of the hemoglobin protein complex. The beta subunit is composed of a globular domain and a helical domain, allowing for the binding of oxygen and the release of carbon dioxide. 2. **Function**: The beta subunit plays a critical role in oxygen transport by binding to oxygen and facilitating its release to tissues and organs. It also helps to maintain the pH balance of the blood by buffering excess hydrogen ions. 3. **Expression**: The HBB gene is expressed in various cell types, including erythrocytes, neutrophils, and macrophages. Its expression is tightly regulated by transcription factors and post-translational modifications. 4. **Regulation**: The HBB gene is subject to various regulatory mechanisms, including feedback inhibition by oxygen, allosteric modulation by other hemoglobin subunits, and post-translational modifications such as phosphorylation and ubiquitination. **Pathways and Functions:** 1. **Oxygen Transport**: The beta subunit plays a crucial role in oxygen transport by binding to oxygen and facilitating its release to tissues and organs. 2. **Carbon Dioxide Transport**: The beta subunit also helps to transport carbon dioxide from tissues and organs back to the lungs for exhalation. 3. **Autophagy**: The beta subunit is involved in autophagy, a process by which cells recycle damaged or dysfunctional proteins and organelles. 4. **Immune Response**: The beta subunit is expressed on the surface of neutrophils and macrophages, where it plays a role in the immune response by binding to pathogens and facilitating their clearance. 5. **Heme Signaling**: The beta subunit is involved in heme signaling, a process by which heme is released from hemoglobin and signals to various cellular pathways. **Clinical Significance:** 1. **Hemoglobinopathies**: Mutations in the HBB gene can lead to hemoglobinopathies, a group of genetic disorders characterized by abnormal hemoglobin production and oxygen transport. 2. **Anemia**: Deficiencies in the beta subunit can lead to anemia, a condition characterized by reduced red blood cell production or function. 3. **Sickle Cell Disease**: Mutations in the HBB gene can lead to sickle cell disease, a genetic disorder characterized by abnormal hemoglobin production and oxygen transport. 4. **Thalassemia**: Deficiencies in the beta subunit can also lead to thalassemia, a group of genetic disorders characterized by reduced hemoglobin production and oxygen transport. 5. **Cardiovascular Disease**: The beta subunit is involved in the regulation of blood pressure and the maintenance of vascular tone, making it a potential target for the treatment of cardiovascular disease. In conclusion, the HBB gene plays a critical role in oxygen transport and is essential for maintaining the health of the cardiovascular system. Mutations in the HBB gene can lead to a range of genetic disorders, including hemoglobinopathies, anemia, and cardiovascular disease. Further research is needed to fully understand the mechanisms by which the beta subunit regulates oxygen transport and to develop effective treatments for these disorders.

Genular Protein ID: 3052090986

Symbol: HBB_HUMAN

Name: Hemoglobin subunit beta

UniProtKB Accession Codes:

P68871 A4GX73 B2ZUE0 P02023 Q13852 Q14481 Q14510 Q45KT0 Q549N7 Q6FI08 Q6R7N2 Q8IZI1 Q9BX96 Q9UCD6 Q9UCP8 Q9UCP9

Database IDs:

ABCD 1 AGR 1 AlphaFoldDB 1 Antibodypedia 1 BMRB 1 Bgee 1 BindingDB 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 1 CDD 1 CPTAC 1 CTD 1 CarbonylDB 1 ChEBI 8 ChEMBL 1 ChiTaRS 1 ComplexPortal 3 DIP 1 DMDM 1 DNASU 1 DisGeNET 1 DrugBank 20 DrugCentral 1 EMBL 100 EMDB 7 Ensembl 2 EvolutionaryTrace 1 ExpressionAtlas 1 GO 28 Gene3D 1 GeneCards 1 GeneReviews 1 GeneTree 1 GeneWiki 1 GenomeRNAi 1 GlyConnect 1 GlyCosmos 1 GlyGen 1 HGNC 1 HOGENOM 1 HPA 1 InParanoid 1 IntAct 1 InterPro 5 KEGG 1 MANE-Select 1 MIM 10 MINT 1 MalaCards 1 MassIVE 1 MetOSite 1 NCBI Taxonomy 1 OMA 1 OpenTargets 1 Orphanet 19 OrthoDB 1 PANTHER 2 PDB 100 PDBsum 100 PIR 1 PRIDE 1 PRINTS 1 PRO 1 PROSITE 1 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 1 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 1 REPRODUCTION-2DPAGE 2 RNAct 1 Reactome 9 RefSeq 1 SASBDB 1 SIGNOR 1 SMR 1 STRING 1 SUPFAM 1 SignaLink 1 TCDB 1 TopDownProteomics 1 TreeFam 1 UCSC 1 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 1019344

Title: Nucleotide sequence analysis of coding and noncoding regions of human beta-globin mRNA.

PubMed ID: 1019344

DOI: 10.1016/s0079-6603(08)60917-4

PubMed ID: 6254664

Title: The nucleotide sequence of the human beta-globin gene.

PubMed ID: 6254664

DOI: 10.1016/0092-8674(80)90428-6

PubMed ID: 16175509

Title: The beta-globin recombinational hotspot reduces the effects of strong selection around HbC, a recently arisen mutation providing resistance to malaria.

PubMed ID: 16175509

DOI: 10.1086/491748

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 13872627

Title: The constitution of normal adult human haemoglobin.

PubMed ID: 13872627

DOI: 10.1515/bchm2.1961.325.1.283

PubMed ID: 13464827

Title: Gene mutations in human haemoglobin: the chemical difference between normal and sickle cell haemoglobin.

PubMed ID: 13464827

DOI: 10.1038/180326a0

PubMed ID: 25946035

Title: Human basal tear peptidome characterization by CID, HCD, and ETD followed by in silico and in vitro analyses for antimicrobial peptide identification.

PubMed ID: 25946035

DOI: 10.1021/acs.jproteome.5b00179

PubMed ID: 1575724

Title: Isolation of a hemoglobin-derived opioid peptide from cerebrospinal fluid of patients with cerebrovascular bleedings.

PubMed ID: 1575724

DOI: 10.1016/0006-291x(92)90699-l

PubMed ID: 8401300

Title: Globin chain synthesis in hemolytic anemia reticulocytes. A case of hemoglobin Burke.

PubMed ID: 8401300

PubMed ID: 2581851

Title: Cloning specific complete polyadenylylated 3'-terminal cDNA segments.

PubMed ID: 2581851

DOI: 10.1016/0378-1119(85)90093-9

PubMed ID: 4555506

Title: X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin.

PubMed ID: 4555506

DOI: 10.1038/237146a0

PubMed ID: 4531009

Title: Sites of acetylation of sickle cell hemoglobin by aspirin.

PubMed ID: 4531009

DOI: 10.1073/pnas.71.12.4693

PubMed ID: 635569

Title: The glycosylation of hemoglobin: relevance to diabetes mellitus.

PubMed ID: 635569

DOI: 10.1126/science.635569

PubMed ID: 7358733

Title: Sites of nonenzymatic glycosylation of human hemoglobin A.

PubMed ID: 7358733

DOI: 10.1016/s0021-9258(19)85860-x

PubMed ID: 6166632

Title: Molecular analysis of the beta-thalassemia phenotype associated with inheritance of hemoglobin E (alpha 2 beta2(26)Glu leads to Lys).

PubMed ID: 6166632

DOI: 10.1172/jci110226

PubMed ID: 6539334

Title: Human hemoglobin Portland II (zeta 2 beta 2). Isolation and characterization of Portland hemoglobin components and their constituent globin chains.

PubMed ID: 6539334

DOI: 10.1016/s0021-9258(17)39875-7

PubMed ID: 3718478

Title: 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.

PubMed ID: 3718478

DOI: 10.1042/bj2340453

PubMed ID: 1520632

Title: Beta 141 Leu is not deleted in the unstable haemoglobin Atlanta-Coventry but is replaced by a novel amino acid of mass 129 daltons.

PubMed ID: 1520632

DOI: 10.1111/j.1365-2141.1992.tb08179.x

PubMed ID: 8637569

Title: S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control.

PubMed ID: 8637569

DOI: 10.1038/380221a0

PubMed ID: 9843411

Title: Crystal structure of the S-nitroso form of liganded human hemoglobin.

PubMed ID: 9843411

DOI: 10.1021/bi9816711

PubMed ID: 10588683

Title: Ancient origins of nitric oxide signaling in biological systems.

PubMed ID: 10588683

DOI: 10.1073/pnas.96.25.14206

PubMed ID: 11001883

Title: Hemoglobin C associated with protection from severe malaria in the Dogon of Mali, a West African population with a low prevalence of hemoglobin S.

PubMed ID: 11001883

PubMed ID: 11747442

Title: The role of beta chains in the control of the hemoglobin oxygen binding function: chimeric human/mouse proteins, structure, and function.

PubMed ID: 11747442

DOI: 10.1021/bi011329f

PubMed ID: 12149194

Title: Hemoglobin E: a balanced polymorphism protective against high parasitemias and thus severe P falciparum malaria.

PubMed ID: 12149194

PubMed ID: 12470213

Title: Spinorphin as an endogenous inhibitor of enkephalin-degrading enzymes: roles in pain and inflammation.

PubMed ID: 12470213

DOI: 10.2174/1389203023380404

PubMed ID: 12552433

Title: Hookworm aspartic protease, Na-APR-2, cleaves human hemoglobin and serum proteins in a host-specific fashion.

PubMed ID: 12552433

DOI: 10.1086/367708

PubMed ID: 16001361

Title: How malaria has affected the human genome and what human genetics can teach us about malaria.

PubMed ID: 16001361

DOI: 10.1086/432519

PubMed ID: 16904236

Title: Hemorphin and hemorphin-like peptides isolated from dog pancreas and sheep brain are able to potentiate bradykinin activity in vivo.

PubMed ID: 16904236

DOI: 10.1016/j.peptides.2006.06.009

PubMed ID: 17676725

Title: Structure-activity relationship studies of spinorphin as a potent and selective human P2X(3) receptor antagonist.

PubMed ID: 17676725

DOI: 10.1021/jm070114m

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 4123689

Title: Structure of sickled erythrocytes and of sickle-cell hemoglobin fibers.

PubMed ID: 4123689

DOI: 10.1073/pnas.70.3.718

PubMed ID: 1195378

Title: Crystal structure of sickle-cell deoxyhemoglobin at 5 A resolution.

PubMed ID: 1195378

DOI: 10.1016/s0022-2836(75)80108-2

PubMed ID: 1177322

Title: Three-dimensional Fourier synthesis of human deoxyhaemoglobin at 2.5-A resolution: refinement of the atomic model.

PubMed ID: 1177322

DOI: 10.1016/s0022-2836(75)80037-4

PubMed ID: 7373648

Title: The structure of human carbonmonoxy haemoglobin at 2.7-A resolution.

PubMed ID: 7373648

DOI: 10.1016/0022-2836(80)90308-3

PubMed ID: 6726807

Title: The crystal structure of human deoxyhaemoglobin at 1.74 A resolution.

PubMed ID: 6726807

DOI: 10.1016/0022-2836(84)90472-8

PubMed ID: 1567857

Title: High-resolution X-ray study of deoxyhemoglobin Rothschild 37 beta Trp-->Arg: a mutation that creates an intersubunit chloride-binding site.

PubMed ID: 1567857

DOI: 10.1021/bi00131a030

PubMed ID: 1507231

Title: Structure-function relationships in the low-affinity mutant haemoglobin Aalborg (Gly74 (E18)beta-->Arg).

PubMed ID: 1507231

DOI: 10.1016/0022-2836(92)90638-z

PubMed ID: 8377203

Title: Human deoxyhaemoglobin-2,3-diphosphoglycerate complex low-salt structure at 2.5 A resolution.

PubMed ID: 8377203

DOI: 10.1006/jmbi.1993.1505

PubMed ID: 8642597

Title: Crystal structure of T state haemoglobin with oxygen bound at all four haems.

PubMed ID: 8642597

DOI: 10.1006/jmbi.1996.0124

PubMed ID: 9521756

Title: High-resolution crystal structures of human hemoglobin with mutations at tryptophan 37beta: structural basis for a high-affinity T-state.

PubMed ID: 9521756

DOI: 10.1021/bi9708702

PubMed ID: 9830011

Title: Crystal structure of deoxy-human hemoglobin beta6 Glu-->Trp. Implications for the structure and formation of the sickle cell fiber.

PubMed ID: 9830011

DOI: 10.1074/jbc.273.49.32690

PubMed ID: 12454462

Title: Structure of mutant human carbonmonoxyhemoglobin C (betaE6K) at 2.0 A resolution.

PubMed ID: 12454462

DOI: 10.1107/s0907444902016426

PubMed ID: 24100324

Title: Structure of fully liganded Hb zeta2beta2s trapped in a tense conformation.

PubMed ID: 24100324

DOI: 10.1107/s0907444913019197

PubMed ID: 5919752

Title: Hemoglobin Freiburg: abnormal hemoglobin due to deletion of a single amino acid residue.

PubMed ID: 5919752

DOI: 10.1126/science.154.3752.1024

PubMed ID: 1115799

Title: Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys) and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg).

PubMed ID: 1115799

PubMed ID: 186485

Title: Functional and physicochemical studies of hemoglobin St. Louis beta 28 (B10) Leu replaced by Gln: a variant with ferric beta heme iron.

PubMed ID: 186485

DOI: 10.1172/jci108561

PubMed ID: 1971109

Title: Molecular basis for dominantly inherited inclusion body beta-thalassemia.

PubMed ID: 1971109

DOI: 10.1073/pnas.87.10.3924

PubMed ID: 8330974

Title: Hb Alesha or alpha 2 beta (2)67(E11)Val-->Met: a new unstable hemoglobin variant identified through sequencing of amplified DNA.

PubMed ID: 8330974

DOI: 10.3109/03630269308998896

PubMed ID: 721609

Title: Hemoglobin J Altgeld Gardens. A hemoglobin variant with a substitution of the proximal histidine of the beta-chain.

PubMed ID: 721609

DOI: 10.3109/03630267809007075

PubMed ID: 4850241

Title: A new haemoglobin J from Turkey -- Hb Ankara (beta10 (A7) Ala-Asp).

PubMed ID: 4850241

DOI: 10.1016/0014-5793(74)80766-0

PubMed ID: 3707969

Title: Hb J-Antakya or alpha 2 beta (2)65(E9)Lys-->Met in a Turkish family and Hb complutense or alpha 2 beta (2)127(H5)Gln-->Glu in a Spanish family; correction of a previously published identification.

PubMed ID: 3707969

DOI: 10.1016/0167-4838(86)90178-0

PubMed ID: 3654265

Title: A new unstable and low oxygen affinity hemoglobin variant: Hb J-Auckland [beta 25(B7)Gly-->Asp].

PubMed ID: 3654265

DOI: 10.3109/03630268709017888

PubMed ID: 8718692

Title: Identification of a new high oxygen affinity hemoglobin variant: Hb Aurora [beta 139(H17) Asn-->Tyr].

PubMed ID: 8718692

DOI: 10.3109/03630269509005825

PubMed ID: 3384710

Title: Hemoglobin Brest [beta 127 (H5)Gln-->Lys] a new unstable human hemoglobin variant located at the alpha 1 beta 1 interface with specific electrophoretic behavior.

PubMed ID: 3384710

DOI: 10.3109/03630268808998024

PubMed ID: 6166590

Title: Hemoglobin Brisbane: beta68 Leu replaced by His. A new high oxygen affinity variant.

PubMed ID: 6166590

DOI: 10.3109/03630268108991807

PubMed ID: 6629823

Title: A new hemoglobin with high oxygen affinity -- hemoglobin Bunbury: alpha 2 beta 2 [94 (FG1) Asp replaced by Asn].

PubMed ID: 6629823

DOI: 10.3109/03630268309038410

PubMed ID: 1247583

Title: Hemoglobin J Cairo: beta 65 (E9) Lys leads to Gln, A new hemoglobin variant discovered in an Egyptian family.

PubMed ID: 1247583

DOI: 10.1016/0005-2795(76)90348-2

PubMed ID: 1138922

Title: A new haemoglobin variant, haemoglobin Camperdown (beta 104 (G6) arginine->serine).

PubMed ID: 1138922

DOI: 10.1016/0005-2795(75)90231-7

PubMed ID: 992050

Title: Haemoglobin caribbean beta91 (F7) Leu replaced by Arg: a mildly haemoglobin with a low oxygen affinity.

PubMed ID: 992050

DOI: 10.1016/0014-5793(76)80662-x

PubMed ID: 6434492

Title: A silent hemoglobin variant detected by HPLC: hemoglobin City of Hope beta 69 (E13) Gly-->Ser.

PubMed ID: 6434492

DOI: 10.3109/03630268408991716

PubMed ID: 1814856

Title: Hb Coimbra or alpha 2 beta (2)99(G1)Asp-->Glu, a newly discovered high oxygen affinity variant.

PubMed ID: 1814856

DOI: 10.3109/03630269109027896

PubMed ID: 8641705

Title: Hb Costa Rica or alpha 2 beta 2 77(EF1)His-->Arg: the first example of a somatic cell mutation in a globin gene.

PubMed ID: 8641705

DOI: 10.1007/s004390050145

PubMed ID: 8602627

Title: Hemoglobin Debrousse (beta 96[FG3]Leu-->Pro): a new unstable hemoglobin with twofold increased oxygen affinity.

PubMed ID: 8602627

DOI: 10.1002/(sici)1096-8652(199604)51:4<276::aid-ajh5>3.0.co;2-t

PubMed ID: 2399911

Title: Hemoglobin Dhonburi alpha 2 beta 2 126 (H4) Val-->Gly: a new unstable beta variant producing a beta-thalassemia intermedia phenotype in association with beta zero-thalassemia.

PubMed ID: 2399911

DOI: 10.1002/ajh.2830350206

PubMed ID: 1511986

Title: Two new human hemoglobin variants caused by unusual mutational events: Hb Zaire contains a five residue repetition within the alpha-chain and Hb Duino has two residues substituted in the beta-chain.

PubMed ID: 1511986

DOI: 10.1007/bf00221961

PubMed ID: 1301199

Title: A novel beta-globin structural mutant, Hb Brescia (beta 114 Leu-Pro), causing a severe beta-thalassemia intermedia phenotype.

PubMed ID: 1301199

DOI: 10.1002/humu.1380010207

PubMed ID: 8111050

Title: A novel beta-globin mutation, beta Durham-NC [beta 114 Leu-->Pro], produces a dominant thalassemia-like phenotype.

PubMed ID: 8111050

PubMed ID: 8811317

Title: Hb J-Europa [beta 62(E6)Ala-->Asp]: normal oxygen binding properties in a new variant involving a residue located distal to the heme.

PubMed ID: 8811317

DOI: 10.3109/03630269609027919

PubMed ID: 1917539

Title: Hb Geelong [beta 139(H17)Asn-->Asp].

PubMed ID: 1917539

DOI: 10.3109/03630269109072487

PubMed ID: 3666141

Title: Hemoglobin Grange-Blanche [beta 27(B9) Ala-->Val], a new variant with normal expression and increased affinity for oxygen.

PubMed ID: 3666141

DOI: 10.1016/0014-5793(87)80509-4

PubMed ID: 1487420

Title: Hb Graz or alpha 2 beta 2(2)(NA2)His-->Leu; a new beta chain variant observed in four families from southern Austria.

PubMed ID: 1487420

DOI: 10.3109/03630269208993117

PubMed ID: 826083

Title: Hb Helsinki: a variant with a high oxygen affinity and a substitution at a 2,3-DPG binding site (beta82[EF6] Lys replaced by Met).

PubMed ID: 826083

DOI: 10.1159/000207947

PubMed ID: 3754244

Title: Hb Himeji or beta 140 (H18) Ala-->Asp. A slightly unstable hemoglobin with increased beta N-terminal glycation.

PubMed ID: 3754244

DOI: 10.3109/03630268609046438

PubMed ID: 2513289

Title: Hb Hinsdale [beta 139 (H17)Asn-->Lys]: a variant in the central cavity showing reduced affinity for oxygen and 2,3-diphosphoglycerate.

PubMed ID: 2513289

DOI: 10.3109/03630268908998084

PubMed ID: 8745430

Title: HB Hinwil or beta 38(C4)Thr-->Asn: a new beta chain variant detected in a Swiss family.

PubMed ID: 8745430

DOI: 10.3109/03630269609027908

PubMed ID: 8144352

Title: Hb Howick [beta 37(C3)Trp-->Gly]: a new high oxygen affinity variant of the alpha 1 beta 2 contact.

PubMed ID: 8144352

DOI: 10.3109/03630269309043491

PubMed ID: 429365

Title: The structure of hemoglobin Indianapolis [beta112(G14) arginine]. An unstable variant detectable only by isotopic labeling.

PubMed ID: 429365

DOI: 10.1016/s0021-9258(18)50784-5

PubMed ID: 1787097

Title: Hb Isehara (or Hb Redondo) [beta 92 (F8) His-->Asn]: an unstable variant with a proximal histidine substitution at the heme contact.

PubMed ID: 1787097

DOI: 10.3109/03630269109027880

PubMed ID: 4639022

Title: Hemoglobin Istanbul: substitution of glutamine for histidine in a proximal histidine (F8(92)).

PubMed ID: 4639022

DOI: 10.1172/jci107050

PubMed ID: 2101840

Title: Hb Jacksonville [alpha 2 beta 2(54)(D5)Val-->Asp]: a new unstable variant found in a patient with hemolytic anemia.

PubMed ID: 2101840

PubMed ID: 6618888

Title: Hemoglobin Jianghua [beta 120(GH3) Lys leads to Ile]: a new fast-moving variant found in China.

PubMed ID: 6618888

PubMed ID: 8330972

Title: Hb Karlskoga or alpha 2 beta (2)21(B3) Asp-->His: a new slow-moving variant found in Sweden.

PubMed ID: 8330972

DOI: 10.3109/03630269308998894

PubMed ID: 7173395

Title: Structural study of hemoglobin Knossos, beta 27 (B9) Ala leads to Ser. A new abnormal hemoglobin present as a silent beta-thalassemia.

PubMed ID: 7173395

DOI: 10.1016/0014-5793(82)81052-1

PubMed ID: 1634367

Title: Hb Kodaira [beta 146(HC3)His-->Gln]: a new beta chain variant with an amino acid substitution at the C-terminus.

PubMed ID: 1634367

DOI: 10.3109/03630269209005681

PubMed ID: 3744871

Title: A new electrophoretically-silent hemoglobin variant: hemoglobin Kofu or alpha 2 beta 2 84 (EF8) Thr-->Ile.

PubMed ID: 3744871

DOI: 10.3109/03630268608996871

PubMed ID: 7693620

Title: Hb Hradec Kralove (Hb HK) or alpha 2 beta 2 115(G17)Ala-->Asp, a severely unstable hemoglobin variant resulting in a dominant beta-thalassemia trait in a Czech family.

PubMed ID: 7693620

DOI: 10.3109/03630269308997485

PubMed ID: 3557994

Title: Hemoglobin La Desirade alpha A2 beta 2 129 (H7) Ala-->Val: a new unstable hemoglobin.

PubMed ID: 3557994

DOI: 10.3109/03630268609036564

PubMed ID: 1540659

Title: Structure of the EF corner favors deamidation of asparaginyl residues in hemoglobin: the example of Hb La Roche-sur-Yon [beta 81 (EF5) Leu-->His].

PubMed ID: 1540659

DOI: 10.1016/0925-4439(92)90052-o

PubMed ID: 3384708

Title: Hb Las Palmas or alpha 2 beta 2(49)(CD8)Ser-->Phe, a mildly unstable hemoglobin variant.

PubMed ID: 3384708

DOI: 10.3109/03630268808998022

PubMed ID: 3691763

Title: Hb Linkoping (beta 36 Pro-->Thr): a new high oxygen affinity hemoglobin variant found in two families of Finnish origin.

PubMed ID: 3691763

DOI: 10.1111/j.1600-0609.1987.tb01455.x

PubMed ID: 6629824

Title: Hemoglobin Maputo: a new beta-chain variant (alpha 2 beta 2 47 (CD6) Asp replaced by Tyr) in combination with hemoglobin S, identified by high performance liquid chromatography (HPLC).

PubMed ID: 6629824

DOI: 10.3109/03630268309038411

PubMed ID: 2384314

Title: Hb Matera [beta 55(D6)Met-->Lys]: a new unstable hemoglobin variant in an Italian family.

PubMed ID: 2384314

DOI: 10.3109/03630269009002256

PubMed ID: 7338468

Title: Hemoglobin Miyashiro (beta 23[B5] val substituting for gly) an electrophoretically silent variant discovered by the isopropanol test.

PubMed ID: 7338468

DOI: 10.3109/03630268108991833

PubMed ID: 893142

Title: Hemoglobin Mizuho or beta 68 (E 12) leucine leads to proline, a new unstable variant associated with severe hemolytic anemia.

PubMed ID: 893142

DOI: 10.3109/03630267709027864

PubMed ID: 1517102

Title: A new variant, HB Muscat [alpha 2 beta (2)32(B14)Leu-->Val] observed in association with HB S in an Arabian family.

PubMed ID: 1517102

DOI: 10.3109/03630269208998866

PubMed ID: 2634671

Title: Hb N-Timone [alpha 2 beta 2(8)(A5)Lys-->Glu]: a new fast-moving variant with normal stability and oxygen affinity.

PubMed ID: 2634671

DOI: 10.3109/03630268908998848

PubMed ID: 3838976

Title: A new unstable, high oxygen affinity hemoglobin: Hb Nagoya or beta 97 (FG4) His-->Pro.

PubMed ID: 3838976

DOI: 10.3109/03630268508996978

PubMed ID: 8330979

Title: Hb D-Neath or beta 121 (GH4) Glu-->Ala: a new member of the Hb D family.

PubMed ID: 8330979

DOI: 10.3109/03630269308998901

Sequence Information:

  • Length: 147
  • Mass: 15998
  • Checksum: A31F6D621C6556A1
  • Sequence:
    • MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK 
VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG 
KEFTPPVQAA YQKVVAGVAN ALAHKYH

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.