Human Gene HBB (ENST00000647020.1) from GENCODE V39
  Description: Involved in oxygen transport from the lung to the various peripheral tissues. (from UniProt P68871)
RefSeq Summary (NM_000518): The alpha (HBA) and beta (HBB) loci determine the structure of the 2 types of polypeptide chains in adult hemoglobin, Hb A. The normal adult hemoglobin tetramer consists of two alpha chains and two beta chains. Mutant beta globin causes sickle cell anemia. Absence of beta chain causes beta-zero-thalassemia. Reduced amounts of detectable beta globin causes beta-plus-thalassemia. The order of the genes in the beta-globin cluster is 5'-epsilon -- gamma-G -- gamma-A -- delta -- beta--3'. [provided by RefSeq, Jul 2008].
Gencode Transcript: ENST00000647020.1
Gencode Gene: ENSG00000244734.4
Transcript (Including UTRs)
   Position: hg38 chr11:5,225,464-5,227,197 Size: 1,734 Total Exon Count: 3 Strand: -
Coding Region
   Position: hg38 chr11:5,225,598-5,227,021 Size: 1,424 Coding Exon Count: 3 

Page IndexSequence and LinksUniProtKB CommentsMalaCardsCTDRNA-Seq Expression
Microarray ExpressionRNA StructureProtein StructureOther SpeciesGO AnnotationsmRNA Descriptions
PathwaysOther NamesGeneReviewsMethods
Data last updated at UCSC: 2022-01-17 08:30:34

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr11:5,225,464-5,227,197)mRNA (may differ from genome)Protein (147 aa)
Gene SorterGenome BrowserOther Species FASTAGene interactionsTable SchemaBioGPS
CGAPEnsemblExonPrimerGencodeGeneCardsHGNC
HPRDLynxMGIneXtProtPubMedReactome
UniProtKBWikipedia

-  Comments and Description Text from UniProtKB
  ID: HBB_HUMAN
DESCRIPTION: RecName: Full=Hemoglobin subunit beta; AltName: Full=Beta-globin; AltName: Full=Hemoglobin beta chain; Contains: RecName: Full=LVV-hemorphin-7;
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
FUNCTION: LVV-hemorphin-7 potentiates the activity of bradykinin, causing a decrease in blood pressure.
SUBUNIT: Heterotetramer of two alpha chains and two beta chains in adult hemoglobin A (HbA).
INTERACTION: P69905:HBA2; NbExp=19; IntAct=EBI-715554, EBI-714680;
TISSUE SPECIFICITY: Red blood cells.
PTM: 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.
PTM: S-nitrosylated; a nitric oxide group is first bound to Fe(2+) and then transferred to Cys-94 to allow capture of O(2).
PTM: Acetylated on Lys-60, Lys-83 and Lys-145 upon aspirin exposure. PubMed:16916647 reports the identification of HBB acetylated on Lys-145 in the cytosolic fraction of HeLa cells. This may have resulted from contamination of the sample.
MASS SPECTROMETRY: Mass=1310; Method=FAB; Range=33-42; Source=PubMed:1575724;
DISEASE: Defects in HBB may be a cause of Heinz body anemias (HEIBAN) [MIM:140700]. This is a 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.
DISEASE: Defects in HBB are the cause of 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.
DISEASE: Defects in HBB are the cause of sickle cell anemia (SKCA) [MIM:603903]; also known as sickle cell disease. Sickle cell anemia is 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.
DISEASE: Defects in HBB are the cause of 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.
MISCELLANEOUS: One molecule of 2,3-bisphosphoglycerate can bind to two beta chains per hemoglobin tetramer.
SIMILARITY: Belongs to the globin family.
WEB RESOURCE: Name=HbVar; Note=Human hemoglobin variants and thalassemias; URL="http://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBB";
WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/HBB";
WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and polymorphism database; URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=HBB";
WEB RESOURCE: Name=Wikipedia; Note=Hemoglobin entry; URL="http://en.wikipedia.org/wiki/Hemoglobin";

-  MalaCards Disease Associations
  MalaCards Gene Search: HBB
Diseases sorted by gene-association score: thalassemia, hispanic gamma-delta-beta* (1707), sickle cell anemia* (1451), heinz body anemia* (1294), thalassemia-beta, dominant inclusion-body* (1275), fetal hemoglobin quantitative trait locus 1* (972), hemoglobin e disease* (499), thalassemia major* (462), hemoglobinopathy* (448), hemolytic anemia* (445), thalassemia intermedia* (440), hemoglobin c disease* (392), hemoglobin se disease* (375), hemoglobin e-beta-thalassemia syndrome* (375), sickle beta thalassemia* (368), hemoglobin d disease* (366), methemoglobinemia, beta-globin type* (350), sickle cell - hemoglobin d disease* (350), hemoglobin c-beta-thalassemia syndrome* (350), malaria* (311), hereditary persistence of fetal hemoglobin-sickle cell disease syndrome* (247), hemoglobin lepore-beta-thalassemia syndrome* (247), hereditary persistence of fetal hemoglobin-beta-thalassemia syndrome* (175), sickle cell disease* (164), hemoglobin s beta-thalassemia* (100), hemoglobin sd* (100), hemoglobin so* (100), thalassemia (60), thalassemia minor (28), splenic infarction (23), hypochromic microcytic anemia (14), congenital hemolytic anemia (13), thalassemias, alpha- (13), acute chest syndrome (12), splenic disease (12), splenic sequestration (11), autosomal genetic disease (11), methemoglobinemia (11), buruli ulcer (10), acute erythroid leukemia (10), siderosis (10), histiocytosis-lymphadenopathy plus syndrome (10), hemoglobinemia (9), c3 deficiency (9), hemoglobin h disease, nondeletional (8), anemia, sideroblastic, 1 (7), pyridoxine-responsive sideroblastic anemia (7), malignant secondary hypertension (7), cholelithiasis (7), deficiency anemia (6), angioid streaks (6), plasmodium falciparum malaria (6), polycythemia (6), glucosephosphate dehydrogenase deficiency (6), testicular infarct (6), osgood-schlatter's disease (5), spherocytosis, type 2 (5), kluver-bucy syndrome (5), malignant essential hypertension (5), rubeosis iridis (5), pleuropneumonia (4), tetanus neonatorum (4), extraosseous ewing's sarcoma (4), autosomal recessive disease (2), immune system disease (1), hereditary spherocytosis (1)
* = Manually curated disease association

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 219386.00 RPKM in Whole Blood
Total median expression: 225307.19 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -52.40176-0.298 Picture PostScript Text
3' UTR -25.20134-0.188 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR000971 - Globin
IPR009050 - Globin-like
IPR012292 - Globin_dom
IPR002337 - Haemoglobin_b

Pfam Domains:
PF00042 - Globin

Protein Data Bank (PDB) 3-D Structure
MuPIT help
1A00 - X-ray MuPIT 1A01 - X-ray MuPIT 1A0U - X-ray MuPIT 1A0Z - X-ray MuPIT 1A3N - X-ray 1A3O - X-ray 1ABW - X-ray MuPIT 1ABY - X-ray MuPIT 1AJ9 - X-ray 1B86 - X-ray 1BAB - X-ray MuPIT 1BBB - X-ray MuPIT 1BIJ - X-ray 1BUW - X-ray 1BZ0 - X-ray 1BZ1 - X-ray MuPIT 1BZZ - X-ray MuPIT 1C7B - X-ray MuPIT 1C7C - X-ray MuPIT 1C7D - X-ray MuPIT 1CBL - X-ray MuPIT 1CBM - X-ray MuPIT 1CH4 - X-ray MuPIT 1CLS - X-ray 1CMY - X-ray MuPIT 1COH - X-ray MuPIT 1DKE - X-ray 1DXT - X-ray MuPIT 1DXU - X-ray MuPIT 1DXV - X-ray MuPIT 1FN3 - X-ray 1G9V - X-ray 1GBU - X-ray 1GBV - X-ray 1GLI - X-ray MuPIT 1GZX - X-ray 1HAB - X-ray 1HAC - X-ray 1HBA - X-ray MuPIT 1HBB - X-ray MuPIT 1HBS - X-ray MuPIT 1HCO - X-ray MuPIT 1HDB - X-ray MuPIT 1HGA - X-ray MuPIT 1HGB - X-ray MuPIT 1HGC - X-ray MuPIT 1HHO - X-ray MuPIT 1IRD - X-ray 1J3Y - X-ray 1J3Z - X-ray 1J40 - X-ray 1J41 - X-ray 1J7S - X-ray MuPIT 1J7W - X-ray MuPIT 1J7Y - X-ray MuPIT 1JY7 - X-ray 1K0Y - X-ray 1K1K - X-ray 1KD2 - X-ray 1LFL - X-ray 1LFQ - X-ray 1LFT - X-ray 1LFV - X-ray 1LFY - X-ray 1LFZ - X-ray 1LJW - X-ray 1M9P - X-ray 1MKO - X-ray 1NEJ - X-ray 1NIH - X-ray MuPIT 1NQP - X-ray 1O1I - X-ray MuPIT 1O1J - X-ray MuPIT 1O1K - X-ray MuPIT 1O1L - X-ray MuPIT 1O1M - X-ray MuPIT 1O1N - X-ray MuPIT 1O1O - X-ray MuPIT 1O1P - X-ray MuPIT 1QI8 - X-ray MuPIT 1QSH - X-ray 1QSI - X-ray 1QXD - X-ray 1QXE - X-ray 1R1X - X-ray 1R1Y - X-ray 1RPS - X-ray 1RQ3 - X-ray 1RQ4 - X-ray 1RQA - X-ray MuPIT 1RVW - X-ray MuPIT 1SDK - X-ray 1SDL - X-ray 1THB - X-ray MuPIT 1UIW - X-ray 1VWT - X-ray MuPIT 1XXT - X-ray 1XY0 - X-ray MuPIT 1XYE - X-ray MuPIT 1XZ2 - X-ray 1XZ4 - X-ray MuPIT 1XZ5 - X-ray MuPIT 1XZ7 - X-ray MuPIT 1XZU - X-ray MuPIT 1XZV - X-ray MuPIT 1Y09 - X-ray MuPIT 1Y0A - X-ray MuPIT 1Y0C - X-ray MuPIT 1Y0D - X-ray 1Y0T - X-ray MuPIT 1Y0W - X-ray MuPIT 1Y22 - X-ray MuPIT 1Y2Z - X-ray MuPIT 1Y31 - X-ray MuPIT 1Y35 - X-ray MuPIT 1Y45 - X-ray MuPIT 1Y46 - X-ray MuPIT 1Y4B - X-ray MuPIT 1Y4F - X-ray MuPIT 1Y4G - X-ray MuPIT 1Y4P - X-ray MuPIT 1Y4Q - X-ray MuPIT 1Y4R - X-ray MuPIT 1Y4V - X-ray MuPIT 1Y5F - X-ray MuPIT 1Y5J - X-ray MuPIT 1Y5K - X-ray MuPIT 1Y7C - X-ray MuPIT 1Y7D - X-ray MuPIT 1Y7G - X-ray MuPIT 1Y7Z - X-ray MuPIT 1Y83 - X-ray MuPIT 1Y85 - X-ray 1Y8W - X-ray MuPIT 1YDZ - X-ray MuPIT 1YE0 - X-ray MuPIT 1YE1 - X-ray MuPIT 1YE2 - X-ray MuPIT 1YEN - X-ray MuPIT 1YEO - X-ray MuPIT 1YEQ - X-ray MuPIT 1YEU - X-ray MuPIT 1YEV - X-ray MuPIT 1YFF - X-ray 1YG5 - X-ray MuPIT 1YGD - X-ray MuPIT 1YGF - X-ray MuPIT 1YH9 - X-ray 1YHE - X-ray 1YHR - X-ray 1YIE - X-ray MuPIT 1YIH - X-ray MuPIT 1YVQ - X-ray MuPIT 1YVT - X-ray MuPIT 1YZI - X-ray 2D5Z - X-ray 2D60 - X-ray 2DN1 - X-ray 2DN2 - X-ray 2DN3 - X-ray 2DXM - Neutron MuPIT 2H35 - NMR MuPIT 2HBC - X-ray MuPIT 2HBD - X-ray MuPIT 2HBE - X-ray MuPIT 2HBF - X-ray MuPIT 2HBS - X-ray 2HCO - X-ray MuPIT 2HHB - X-ray 2HHD - X-ray 2HHE - X-ray MuPIT 2W6V - X-ray 2W72 - X-ray MuPIT 2YRS - X-ray 3B75 - X-ray 3D17 - X-ray 3D7O - X-ray 3DUT - X-ray 3HHB - X-ray 3HXN - X-ray 3IC0 - X-ray 3IC2 - X-ray 3KMF - Neutron 3NL7 - X-ray MuPIT 3NMM - X-ray MuPIT 3ODQ - X-ray 3ONZ - X-ray 3OO4 - X-ray 3OO5 - X-ray 3P5Q - X-ray 3QJB - X-ray MuPIT 3QJC - X-ray MuPIT 3QJD - X-ray MuPIT 3QJE - X-ray MuPIT 3R5I - X-ray 3S65 - X-ray MuPIT 3S66 - X-ray MuPIT 3SZK - X-ray 4HHB - X-ray MuPIT 6HBW - X-ray


ModBase Predicted Comparative 3D Structure on P68871
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The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologGenome BrowserNo orthologNo orthologNo orthologNo ortholog
      
      
 RGD    
 Protein Sequence    
 Alignment    

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0005344 oxygen transporter activity
GO:0005515 protein binding
GO:0019825 oxygen binding
GO:0020037 heme binding
GO:0030492 hemoglobin binding
GO:0046872 metal ion binding
GO:0004601 peroxidase activity
GO:0031720 haptoglobin binding

Biological Process:
GO:0006898 receptor-mediated endocytosis
GO:0007596 blood coagulation
GO:0008217 regulation of blood pressure
GO:0010942 positive regulation of cell death
GO:0015671 oxygen transport
GO:0015701 bicarbonate transport
GO:0030185 nitric oxide transport
GO:0042542 response to hydrogen peroxide
GO:0042744 hydrogen peroxide catabolic process
GO:0043312 neutrophil degranulation
GO:0045429 positive regulation of nitric oxide biosynthetic process
GO:0050880 regulation of blood vessel size
GO:0051291 protein heterooligomerization
GO:0070293 renal absorption
GO:0070527 platelet aggregation
GO:0098869 cellular oxidant detoxification

Cellular Component:
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005829 cytosol
GO:0005833 hemoglobin complex
GO:0031838 haptoglobin-hemoglobin complex
GO:0070062 extracellular exosome
GO:0071682 endocytic vesicle lumen
GO:0072562 blood microparticle
GO:1904724 tertiary granule lumen
GO:1904813 ficolin-1-rich granule lumen


-  Descriptions from all associated GenBank mRNAs
  BC007075 - Homo sapiens hemoglobin, beta, mRNA (cDNA clone MGC:14540 IMAGE:4292125), complete cds.
M11428 - Human beta-globin mRNA, 3' end.
M25113 - Human sickle beta-hemoglobin mRNA.
HW348671 - WO 2013147320-A/20: Microarray for detection of mutations of beta-globin gene and the method for detectioning of that.
LX064374 - JP 2017045451-A/20: Microarray for detection of mutations of beta-globin gene and the method for detectioning of that.
V00497 - Human messenger RNA for beta-globin.
AY509193 - Homo sapiens hemoglobin beta mRNA, complete cds.
V00500 - Human messenger RNA for beta-globin.
A18171 - Beta globin gene seq ID No:3.
AF181989 - Homo sapiens hemoglobin beta subunit variant (HBB) mRNA, complete cds.
AF349114 - Homo sapiens beta globin chain variant (HBB) mRNA, complete cds.
AF181832 - Homo sapiens hemoglobin beta subunit variant (HBB) mRNA, partial cds.
EU694432 - Homo sapiens hemoglobin beta chain variant (HBB) mRNA, HBB-Dothan allele, complete cds.
AY136510 - Homo sapiens hemoglobin beta chain variant Hb S-Wake (HBB) mRNA, complete cds.
AF117710 - Homo sapiens hemoglobin beta chain (HBB) mRNA, complete cds.
M25079 - Human sickle cell beta-globin mRNA, complete cds.
JD046448 - Sequence 27472 from Patent EP1572962.
DQ893159 - Synthetic construct clone IMAGE:100005789; FLH194450.01X; RZPDo839B0680D hemoglobin, beta (HBB) gene, encodes complete protein.
CR536530 - Homo sapiens full open reading frame cDNA clone RZPDo834D0222D for gene HBB, hemoglobin, beta; complete cds, incl. stopcodon.
KJ896959 - Synthetic construct Homo sapiens clone ccsbBroadEn_06353 HBB gene, encodes complete protein.
KR710226 - Synthetic construct Homo sapiens clone CCSBHm_00010498 HBB (HBB) mRNA, encodes complete protein.
KR710227 - Synthetic construct Homo sapiens clone CCSBHm_00010525 HBB (HBB) mRNA, encodes complete protein.
KR710228 - Synthetic construct Homo sapiens clone CCSBHm_00010601 HBB (HBB) mRNA, encodes complete protein.
KR710229 - Synthetic construct Homo sapiens clone CCSBHm_00010626 HBB (HBB) mRNA, encodes complete protein.
AK311825 - Homo sapiens cDNA, FLJ92086, Homo sapiens hemoglobin, beta (HBB), mRNA.
DQ896453 - Synthetic construct Homo sapiens clone IMAGE:100010913; FLH194446.01L; RZPDo839B0670D hemoglobin, beta (HBB) gene, encodes complete protein.
EU176774 - Synthetic construct Homo sapiens clone IMAGE:100011599; FLH263683.01L; RZPDo839F03256D hemoglobin, beta (HBB) gene, encodes complete protein.
CR541913 - Homo sapiens full open reading frame cDNA clone RZPDo834E0633D for gene HBB, hemoglobin, beta; complete cds, without stopcodon.
AM392537 - Synthetic construct Homo sapiens clone IMAGE:100002184 for hypothetical protein (HBB gene).
AM393351 - Synthetic construct Homo sapiens clone IMAGE:100002185 for hypothetical protein (HBB gene).
JC506088 - Sequence 107 from Patent EP2733219.
JC506717 - Sequence 85 from Patent EP2733220.
JC737512 - Sequence 107 from Patent WO2014075911.
JC737829 - Sequence 85 from Patent WO2014075939.
JC506939 - Sequence 307 from Patent EP2733220.
JC738051 - Sequence 307 from Patent WO2014075939.
LP986374 - Sequence 12 from Patent EP3201339.
MA014034 - JP 2017536338-A/12: TARGETED AUGMENTATION OF NUCLEAR GENE OUTPUT.
CU675537 - Synthetic construct Homo sapiens gateway clone IMAGE:100016702 5' read HBB mRNA.
DQ655983 - Homo sapiens clone Affy08248A01, mRNA sequence.
JD027508 - Sequence 8532 from Patent EP1572962.
M14574 - Human beta-globin gene mRNA precursor, 5' end.
LP986372 - Sequence 10 from Patent EP3201339.
MA014032 - JP 2017536338-A/10: TARGETED AUGMENTATION OF NUCLEAR GENE OUTPUT.

-  Biochemical and Signaling Pathways
  BioCarta from NCI Cancer Genome Anatomy Project
h_ahspPathway - Hemoglobin's Chaperone

Reactome (by CSHL, EBI, and GO)

Protein P68871 (Reactome details) participates in the following event(s):

R-HSA-2168884 Ferriheme is transferred from Methemoglobin to Hemopexin
R-HSA-6798745 Exocytosis of tertiary granule lumen proteins
R-HSA-6800434 Exocytosis of ficolin-rich granule lumen proteins
R-HSA-6806831 CYB5Rs reduce MetHb to HbA
R-HSA-1237325 Hemoglobin A is protonated and carbamated causing release of oxygen
R-HSA-1247668 Hemoglobin A binds oxygen and releases protons and carbon dioxide
R-HSA-2168885 Haptoglobin binds Hemoglobin
R-HSA-2168889 Haptoglobin-related Protein binds Hemoglobin
R-HSA-2168883 Haptoglobin:Hemoglobin binds CD163
R-HSA-983231 Factors involved in megakaryocyte development and platelet production
R-HSA-109582 Hemostasis
R-HSA-2168880 Scavenging of heme from plasma
R-HSA-6798695 Neutrophil degranulation
R-HSA-1237044 Erythrocytes take up carbon dioxide and release oxygen
R-HSA-1247673 Erythrocytes take up oxygen and release carbon dioxide
R-HSA-2173782 Binding and Uptake of Ligands by Scavenger Receptors
R-HSA-168249 Innate Immune System
R-HSA-1480926 O2/CO2 exchange in erythrocytes
R-HSA-5653656 Vesicle-mediated transport
R-HSA-168256 Immune System
R-HSA-382551 Transport of small molecules

-  Other Names for This Gene
  Alternate Gene Symbols: A4GX73, B2ZUE0, BC007075, HBB_HUMAN, P02023, P68871, Q13852, Q14481, Q14510, Q45KT0, Q549N7, Q6FI08, Q6R7N2, Q8IZI1, Q9BX96, Q9UCD6, Q9UCP8, Q9UCP9, uc285iqo.1
UCSC ID: ENST00000647020.1
RefSeq Accession: NM_000518
Protein: P68871 (aka HBB_HUMAN)
CCDS: CCDS7753.1

-  GeneReviews for This Gene
  GeneReviews article(s) related to gene HBB:
sickle (Sickle Cell Disease)
b-thal (Beta-Thalassemia)

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.