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P68871 (HBB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hemoglobin subunit beta
Alternative name(s):
Beta-globin
Hemoglobin beta chain

Cleaved into the following 2 chains:

  1. LVV-hemorphin-7
  2. Spinorphin
Gene names
Name:HBB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in oxygen transport from the lung to the various peripheral tissues. Ref.37 Ref.38

LVV-hemorphin-7 potentiates the activity of bradykinin, causing a decrease in blood pressure. Ref.37 Ref.38

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. Ref.37 Ref.38

Subunit structure

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.

Tissue specificity

Red blood cells.

Post-translational modification

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.

Acetylated on Lys-60, Lys-83 and Lys-145 upon aspirin exposure. Ref.26

Involvement in disease

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.
Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.55 Ref.129 Ref.130 Ref.133

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. Ref.56

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Miscellaneous

One molecule of 2,3-bisphosphoglycerate can bind to two beta chains per hemoglobin tetramer.

Sequence similarities

Belongs to the globin family.

Mass spectrometry

Molecular mass is 1310 Da from positions 33 - 42. Determined by FAB. Ref.21

Ontologies

Keywords
   Biological processOxygen transport
Transport
   Coding sequence diversityPolymorphism
   DiseaseCongenital dyserythropoietic anemia
Disease mutation
Hereditary hemolytic anemia
   LigandHeme
Iron
Metal-binding
Pyruvate
   Molecular functionHypotensive agent
Vasoactive
   PTMAcetylation
Glycation
Glycoprotein
S-nitrosylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbicarbonate transport

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

hydrogen peroxide catabolic process

Inferred from direct assay PubMed 19740759. Source: BHF-UCL

nitric oxide transport

Non-traceable author statement PubMed 8292032. Source: UniProtKB

oxidation-reduction process

Inferred from direct assay PubMed 19740759. Source: GOC

positive regulation of cell death

Inferred from direct assay PubMed 19740759. Source: BHF-UCL

positive regulation of nitric oxide biosynthetic process

Non-traceable author statement PubMed 7965120. Source: UniProtKB

protein heterooligomerization

Inferred from direct assay PubMed 19740759. Source: BHF-UCL

regulation of blood pressure

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of blood vessel size

Inferred from electronic annotation. Source: UniProtKB-KW

renal absorption

Inferred from mutant phenotype PubMed 18465053PubMed 18974585. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

endocytic vesicle lumen

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

haptoglobin-hemoglobin complex

Inferred from direct assay PubMed 19740759. Source: BHF-UCL

hemoglobin complex

Non-traceable author statement Ref.34Ref.75. Source: UniProtKB

   Molecular_functionheme binding

Inferred from electronic annotation. Source: InterPro

hemoglobin binding

Inferred from direct assay PubMed 1512262. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: InterPro

oxygen binding

Inferred from direct assay Ref.35. Source: UniProtKB

oxygen transporter activity

Non-traceable author statement Ref.35Ref.75. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HBA2P6990519EBI-715554,EBI-714680

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.20
Chain2 – 147146Hemoglobin subunit beta
PRO_0000052976
Peptide33 – 4210LVV-hemorphin-7 Ref.21 Ref.22
PRO_0000296641
Peptide33 – 397Spinorphin
PRO_0000424226

Sites

Metal binding641Iron (heme distal ligand)
Metal binding931Iron (heme proximal ligand)
Binding site212,3-bisphosphoglycerate; via amino nitrogen
Binding site312,3-bisphosphoglycerate
Binding site8312,3-bisphosphoglycerate
Binding site14412,3-bisphosphoglycerate
Site601Not glycated
Site831Not glycated
Site961Not glycated
Site1421Susceptible to oxidation; associated with variant Atlanta, variant non-spherocytic haemolytic anemia and variant Christchurch

Amino acid modifications

Modified residue21N-acetylalanine; in variant Raleigh
Modified residue21N-acetylvaline By similarity
Modified residue21N-pyruvate 2-iminyl-valine; in Hb A1b
Modified residue601N6-acetyllysine Ref.26
Modified residue831N6-acetyllysine Ref.26
Modified residue941S-nitrosocysteine Ref.32 Ref.33
Modified residue1451N6-acetyllysine; alternate Ref.26
Glycosylation21N-linked (Glc) (glycation); in Hb A1c Ref.27
Glycosylation91N-linked (Glc) (glycation) Ref.28
Glycosylation181N-linked (Glc) (glycation) Ref.28
Glycosylation671N-linked (Glc) (glycation) Ref.28
Glycosylation1211N-linked (Glc) (glycation) Ref.28
Glycosylation1451N-linked (Glc) (glycation), alternate; alternate

Natural variations

Natural variant21V → A in Raleigh; O(2) affinity down.
Corresponds to variant rs33949930 [ dbSNP | Ensembl ].
VAR_002856
Natural variant31H → L in Graz. Ref.80
Corresponds to variant rs35906307 [ dbSNP | Ensembl ].
VAR_002857
Natural variant31H → Q in Okayama; O(2) affinity up.
Corresponds to variant rs713040 [ dbSNP | Ensembl ].
VAR_002858
Natural variant31H → R in Deer Lodge; O(2) affinity up.
Corresponds to variant rs33983205 [ dbSNP | Ensembl ].
VAR_002859
Natural variant31H → Y in Fukuoka.
Corresponds to variant rs35906307 [ dbSNP | Ensembl ].
VAR_002860
Natural variant61P → R in Warwickshire.
Corresponds to variant rs34769005 [ dbSNP | Ensembl ].
VAR_002861
Natural variant71E → A in G-Makassar.
Corresponds to variant rs334 [ dbSNP | Ensembl ].
VAR_002862
Natural variant71E → K in C. Ref.3 Ref.51
Corresponds to variant rs33930165 [ dbSNP | Ensembl ].
VAR_002864
Natural variant71E → Q in Machida.
Corresponds to variant rs33930165 [ dbSNP | Ensembl ].
VAR_002865
Natural variant71E → V in S; sickle cell anemia. Ref.10 Ref.41
Corresponds to variant rs334 [ dbSNP | Ensembl ].
VAR_002863
Natural variant81E → G in G-San Jose; mildly unstable.
Corresponds to variant rs34948328 [ dbSNP | Ensembl ].
VAR_002866
Natural variant81E → K in G-Siriraj.
Corresponds to variant rs34948328 [ dbSNP | Ensembl ].
VAR_002867
Natural variant91K → E in N-Timone. Ref.105
Corresponds to variant rs33932981 [ dbSNP | Ensembl ].
VAR_002868
Natural variant91K → Q in J-Luhe.
Corresponds to variant rs33926764 [ dbSNP | Ensembl ].
VAR_002869
Natural variant91K → T in Rio Grande. Ref.118
VAR_002870
Natural variant101S → C in Porto Alegre; O(2) affinity up.
Corresponds to variant rs33918131 [ dbSNP | Ensembl ].
VAR_002871
Natural variant111A → D in Ankara. Ref.59
Corresponds to variant rs33947457 [ dbSNP | Ensembl ].
VAR_002872
Natural variant111A → V in Iraq-Halabja. Ref.134
VAR_025393
Natural variant121V → D in Windsor; O(2) affinity up; unstable. Ref.126
Corresponds to variant rs33974228 [ dbSNP | Ensembl ].
VAR_002873
Natural variant121V → I in Hamilton.
VAR_002874
Natural variant141A → D in J-Lens.
Corresponds to variant rs35203747 [ dbSNP | Ensembl ].
VAR_002875
Natural variant151L → P in Saki; unstable.
VAR_002876
Natural variant151L → R in Soegn; unstable.
Corresponds to variant rs33935445 [ dbSNP | Ensembl ].
VAR_002877
Natural variant161W → G in Randwick; unstable. Ref.117
Corresponds to variant rs33946157 [ dbSNP | Ensembl ].
VAR_002878
Natural variant161W → R in Belfast; O(2) affinity up; unstable.
Corresponds to variant rs33946157 [ dbSNP | Ensembl ].
VAR_002879
Natural variant171G → D in J-Baltimore/J-Trinidad/J-Ireland/J-Georgia/N-New Haven.
VAR_002880
Natural variant171G → R in D-Bushman.
VAR_002881
Natural variant181K → E in Nagasaki.
Corresponds to variant rs33986703 [ dbSNP | Ensembl ].
VAR_002882
Natural variant181K → N in J-Amiens.
Corresponds to variant rs36006214 [ dbSNP | Ensembl ].
VAR_002883
Natural variant181K → Q in Nikosia.
Corresponds to variant rs33986703 [ dbSNP | Ensembl ].
VAR_002884
Natural variant191V → M in Baden; slightly unstable.
Corresponds to variant rs35802118 [ dbSNP | Ensembl ].
VAR_002885
Natural variant201N → D in Alamo.
Corresponds to variant rs34866629 [ dbSNP | Ensembl ].
VAR_002886
Natural variant201N → K in D-Ouleh RABAH.
VAR_002887
Natural variant201N → S in Malay.
Corresponds to variant rs33972047 [ dbSNP | Ensembl ].
VAR_002888
Natural variant211V → M in Olympia; O(2) affinity up.
Corresponds to variant rs35890959 [ dbSNP | Ensembl ].
VAR_002889
Natural variant221D → G in Connecticut; O(2) affinity down.
Corresponds to variant rs33977536 [ dbSNP | Ensembl ].
VAR_002890
Natural variant221D → H in Karlskoga. Ref.91
Corresponds to variant rs33950093 [ dbSNP | Ensembl ].
VAR_002892
Natural variant221D → N in Cocody.
VAR_002891
Natural variant221D → Y in Yusa.
VAR_002893
Natural variant231E → A in G-Coushatta/G-Saskatoon/G-Taegu/Hsin Chu.
Corresponds to variant rs33936254 [ dbSNP | Ensembl ].
VAR_002894
Natural variant231E → G in G-Taipei.
VAR_002895
Natural variant231E → K in E-Saskatoon; unstable.
VAR_002896
Natural variant231E → Q in D-Iran.
VAR_002897
Natural variant231E → V in D-Granada.
VAR_002898
Natural variant241V → D in Strasbourg; O(2) affinity up.
VAR_002899
Natural variant241V → F in Palmerston North; O(2) affinity up; unstable. Ref.111
VAR_002900
Natural variant241V → G in Miyashiro; O(2) affinity up; unstable. Ref.102
VAR_002901
Natural variant241Missing in Freiburg. Ref.53
Corresponds to variant rs34160180 [ dbSNP | Ensembl ].
VAR_069169
Natural variant251G → D in Moscva; O(2) affinity down; unstable.
VAR_002902
Natural variant251G → R in Riverdale-Bronx; O(2) affinity up; unstable.
VAR_002903
Natural variant251G → V in Savannah; unstable.
VAR_002904
Natural variant261G → D in J-Auckland; unstable; O(2) affinity down. Ref.61
VAR_002905
Natural variant261G → R in G-Taiwan Ami.
VAR_002906
Natural variant271E → K in E. Ref.138 Ref.141
VAR_002907
Natural variant271E → V in Henri Mondor; slightly unstable.
VAR_002908
Natural variant281A → D in Volga/Drenthe; unstable.
VAR_002909
Natural variant281A → S in Knossos. Ref.92
VAR_002910
Natural variant281A → V in Grange-blanche; O(2) affinity up. Ref.79
VAR_002911
Natural variant291L → P in Genova/Hyogo; unstable.
VAR_002912
Natural variant291L → Q in St Louis. Ref.55
VAR_035236
Natural variant301G → D in Lufkin; unstable.
VAR_002913
Natural variant311R → S in Tacoma; unstable.
Corresponds to variant rs1135071 [ dbSNP | Ensembl ].
VAR_002914
Natural variant321L → P in Yokohama; unstable. Ref.128
VAR_002915
Natural variant331L → R in Castilla; unstable.
VAR_002916
Natural variant331L → V in Muscat; slightly unstable. Ref.104
VAR_002917
Natural variant351V → D in Santander; unstable. Ref.139
VAR_025394
Natural variant351V → F in Pitie-Salpetriere; O(2) affinity up.
VAR_002918
Natural variant351V → L in Nantes; increased oxygen affinity. Ref.140
VAR_025395
Natural variant361Y → F in Philly; O(2) affinity up; unstable.
VAR_002919
Natural variant371P → R in Sunnybrook.
VAR_002920
Natural variant371P → S in North Chicago; O(2) affinity up. Ref.108
VAR_002921
Natural variant371P → T in Linkoping/Finlandia; O(2) affinity up. Ref.99
VAR_002922
Natural variant381W → G in Howick. Ref.49 Ref.85
VAR_002923
Natural variant381W → R in Rothschild; O(2) affinity down. Ref.45
VAR_002925
Natural variant381W → S in Hirose; O(2) affinity up.
VAR_002924
Natural variant391T → N in Hinwil; O(2) affinity up. Ref.84
VAR_002926
Natural variant401Q → E in Vaasa; unstable.
Corresponds to variant rs76728603 [ dbSNP | Ensembl ].
VAR_002927
Natural variant401Q → K in Alabama. Ref.54
Corresponds to variant rs76728603 [ dbSNP | Ensembl ].
VAR_002928
Natural variant401Q → R in Tianshui.
VAR_002929
Natural variant421F → Y in Mequon.
VAR_002930
Natural variant421Missing in Bruxelles. Ref.130
VAR_035237
Natural variant431F → L in Louisville; unstable. Ref.6
VAR_002931
Natural variant431F → S in Hammersmith. Ref.129
VAR_035239
Natural variant431Missing in Bruxelles. Ref.130
VAR_035238
Natural variant441E → Q in Hoshida/Chaya.
VAR_002932
Natural variant451S → C in Mississippi.
VAR_002933
Natural variant461F → S in Cheverly; unstable.
VAR_002934
Natural variant471G → E in K-Ibadan.
VAR_002935
Natural variant481D → A in Avicenna.
VAR_002936
Natural variant481D → G in Gavello.
VAR_002937
Natural variant481D → Y in Maputo. Ref.100
VAR_002938
Natural variant491L → P in Bab-Saadoum; slightly unstable.
VAR_002939
Natural variant501S → F in Las Palmas; slightly unstable. Ref.13 Ref.98
VAR_002940
Natural variant511T → K in Edmonton.
VAR_002941
Natural variant521P → R in Willamette; O(2) affinity up; unstable.
VAR_002942
Natural variant531D → A in Ocho Rios.
VAR_002943
Natural variant531D → H in Summer Hill.
VAR_002944
Natural variant551V → D in Jacksonville; O(2) affinity up; unstable. Ref.89
VAR_002945
Natural variant561M → K in Matera; unstable. Ref.101
VAR_002946
Natural variant571G → R in Hamadan.
VAR_002947
Natural variant581N → K in G-ferrara; unstable.
VAR_002948
Natural variant591P → R in Dhofar/Yukuhashi.
VAR_002949
Natural variant601K → E in I-High Wycombe.
VAR_002950
Natural variant611V → A in Collingwood; unstable.
VAR_002951
Natural variant621K → E in N-Seatlle.
VAR_002952
Natural variant621K → M in Bologna; O(2) affinity down.
VAR_002953
Natural variant621K → N in Hikari.
VAR_002954
Natural variant631A → D in J-Europa. Ref.77
VAR_002955
Natural variant631A → P in Duarte; unstable.
VAR_002956
Natural variant641H → Y in M-Saskatoon; O(2) affinity up. Ref.121
VAR_002957
Natural variant661K → M in J-Antakya. Ref.60
VAR_002958
Natural variant661K → N in J-Sicilia. Ref.123
VAR_002959
Natural variant661K → Q in J-Cairo. Ref.66
VAR_002960
Natural variant671K → T in Chico; O(2) affinity down.
VAR_002961
Natural variant681V → A in Sydney; unstable.
VAR_002962
Natural variant681V → D in Bristol. Ref.133
VAR_035240
Natural variant681V → G in non-spherocytic haemolytic anemia; Manukau. Ref.132
Corresponds to variant rs33918343 [ dbSNP | Ensembl ].
VAR_040060
Natural variant681V → M in Alesha; unstable. Ref.57
VAR_002963
Natural variant691L → H in Brisbane; O(2) affinity up. Ref.64
VAR_002964
Natural variant691L → P in Mizuho; unstable. Ref.103
VAR_002965
Natural variant701G → D in Rambam. Ref.116
VAR_002966
Natural variant701G → R in Kenitra.
VAR_002967
Natural variant701G → S in City of Hope. Ref.69
VAR_002968
Natural variant711A → D in Seattle; O(2) affinity down; unstable.
VAR_002969
Natural variant721F → S in Christchurch; unstable.
VAR_002970
Natural variant741D → G in Tilburg; O(2) affinity down.
VAR_002971
Natural variant741D → V in Mobile; O(2) affinity down.
VAR_002972
Natural variant741D → Y in Vancouver; O(2) affinity down.
VAR_002973
Natural variant751G → R in Aalborg; unstable. Ref.46
VAR_002974
Natural variant751G → V in Bushwick; unstable.
VAR_002975
Natural variant761L → P in Atlanta; unstable. Ref.13
VAR_002976
Natural variant761L → R in Pasadena; O(2) affinity up; unstable.
VAR_002977
Natural variant771A → D in J-Chicago.
VAR_002978
Natural variant781H → D in J-Iran.
VAR_002979
Natural variant781H → R in Costa Rica. Ref.71
VAR_002980
Natural variant781H → Y in Fukuyama.
VAR_002981
Natural variant791L → R in Quin-hai. Ref.115
VAR_002982
Natural variant801D → Y in Tampa.
VAR_002983
Natural variant811N → K in G-Szuhu/Gifu.
VAR_002984
Natural variant821L → H in La Roche-sur-Yon; unstable and O(2) affinity up. Ref.97
VAR_012663
Natural variant821L → R in Baylor; unstable.
VAR_002985
Natural variant821L → V.
Corresponds to variant rs11549406 [ dbSNP | Ensembl ].
VAR_049273
Natural variant831K → M in Helsinki; O(2) affinity up. Ref.81
VAR_002986
Natural variant831K → N in Providence.
VAR_012664
Natural variant841G → D in Pyrgos. Ref.138
VAR_025396
Natural variant841G → R in Muskegon.
VAR_002987
Natural variant851T → I in Kofu. Ref.94
VAR_002988
Natural variant871A → D in Olomouc; O(2) affinity up. Ref.110
VAR_002989
Natural variant881T → I in Quebec-Chori.
VAR_002990
Natural variant881T → K in D-Ibadan.
VAR_002991
Natural variant881T → P in Valletta.
VAR_002992
Natural variant891L → P in Santa Ana; unstable.
VAR_002993
Natural variant891L → R in Boras; unstable.
VAR_002994
Natural variant901S → N in Creteil; O(2) affinity up.
VAR_002995
Natural variant901S → R in Vanderbilt; O(2) affinity up.
VAR_002996
Natural variant911E → D in Pierre-Benite; O(2) affinity up. Ref.112
VAR_002997
Natural variant911E → K in Agenogi; O(2) affinity down.
VAR_002998
Natural variant921L → P in Sabine; unstable.
VAR_002999
Natural variant921L → R in Caribbean; O(2) affinity down; unstable. Ref.68
VAR_003000
Natural variant931H → D in J-Altgelds Gardens; unstable. Ref.58
VAR_003001
Natural variant931H → N in Isehara; unstable. Ref.87
VAR_003002
Natural variant931H → P in Newcastle and Duino; associated with S-104 in Duino; unstable. Ref.74
VAR_003003
Natural variant931H → Q in Istambul; O(2) affinity up; unstable. Ref.88
VAR_003004
Natural variant941C → R in Okazaki; O(2) affinity up; unstable.
VAR_003005
Natural variant951D → G in Chandigarh.
VAR_003006
Natural variant951D → H in Barcelona; O(2) affinity up.
VAR_003007
Natural variant951D → N in Bunbury; O(2) affinity up. Ref.65
VAR_003008
Natural variant961K → M in J-Cordoba.
VAR_003009
Natural variant961K → N in Detroit.
VAR_003010
Natural variant971L → P in Debrousse; unstable; O(2) affinity up. Ref.72
VAR_003011
Natural variant971L → V in Regina; O(2) affinity up.
VAR_003012
Natural variant981H → L in Wood; O(2) affinity up.
VAR_003013
Natural variant981H → P in Nagoya; O(2) affinity up; unstable. Ref.106
VAR_003014
Natural variant981H → Q in Malmoe; O(2) affinity up.
VAR_003015
Natural variant981H → Y in Moriguchi.
VAR_003016
Natural variant991V → G in Nottingham; unstable.
VAR_003017
Natural variant1001D → E in Coimbra; O(2) affinity up. Ref.70
VAR_003018
Natural variant1011P → L in Brigham; O(2) affinity up.
VAR_003019
Natural variant1011P → R in New Mexico.
VAR_003020
Natural variant1021E → D in Potomac; O(2) affinity up.
VAR_003021
Natural variant1021E → G in Alberta; O(2) affinity up.
VAR_003022
Natural variant1021E → K in British Columbia; O(2) affinity up.
VAR_003023
Natural variant1021E → Q in Rush; unstable. Ref.119
VAR_003024
Natural variant1031N → S in Beth Israel; O(2) affinity down; unstable.
VAR_003025
Natural variant1031N → Y in St Mande; O(2) affinity down. Ref.125
VAR_003026
Natural variant1041F → L in Heathrow; O(2) affinity up.
VAR_003027
Natural variant1051R → S in Camperdown and Duino; associated with P-92 in Duino; unstable. Ref.67 Ref.74
VAR_003028
Natural variant1051R → T in Sherwood Forest.
VAR_003029
Natural variant1081G → R in Burke; O(2) affinity down; unstable. Ref.23
VAR_003030
Natural variant1091N → K in Presbyterian; O(2) affinity down; unstable. Ref.113
VAR_003031
Natural variant1101V → M in San Diego; O(2) affinity up.
VAR_003032
Natural variant1111L → P in Showa-Yakushiji.
VAR_003033
Natural variant1121V → A in Stanmore; O(2) affinity down; unstable. Ref.124
VAR_003034
Natural variant1131C → F in Canterbury. Ref.137
VAR_025397
Natural variant1131C → R in Indianapolis. Ref.5 Ref.86
VAR_003035
Natural variant1131C → Y in Yahata. Ref.127
VAR_003036
Natural variant1151L → M in Zengcheng. Ref.131
VAR_010144
Natural variant1151L → P in Durham-N.C./Brescia; causes beta-thalassemia. Ref.7 Ref.75 Ref.76
VAR_010145
Natural variant1161A → D in Hradec Kralove; unstable; causes severe beta-thalassemia. Ref.95
VAR_003037
Natural variant1161A → P in Madrid; unstable.
VAR_003038
Natural variant1171H → L in Vexin; increased oxygen affinity. Ref.140
VAR_025398
Natural variant1171H → Q in Hafnia.
VAR_003039
Natural variant1181H → P in Saitama; unstable. Ref.120
VAR_003040
Natural variant1181H → R in P-Galveston.
VAR_003041
Natural variant1181H → Y in Tsukumi. Ref.136
VAR_025399
Natural variant1201G → A in Iowa.
VAR_003042
Natural variant1211K → E in Hijiyama.
VAR_003043
Natural variant1211K → I in Jianghua. Ref.90
VAR_003044
Natural variant1211K → Q in Takamatsu.
VAR_003045
Natural variant1221E → A in D-Neath. Ref.107
VAR_003046
Natural variant1221E → G in St Francis.
VAR_003047
Natural variant1221E → K in O-Arab.
VAR_003049
Natural variant1221E → Q in D-Los Angeles/D-Punjab/D-Portugal/D-Chicago/D-Oak Ridge.
VAR_003048
Natural variant1221E → V in D-Camperdown/Beograd.
VAR_003050
Natural variant1241T → I in Villejuif; asymptomatic variant. Ref.135
VAR_003051
Natural variant1251P → Q in Ty Gard; O(2) affinity up. Ref.8
VAR_003053
Natural variant1251P → R in Khartoum; unstable.
VAR_003052
Natural variant1251P → S in Tunis.
VAR_003054
Natural variant1271V → A in Beirut.
VAR_003055
Natural variant1271V → E in Hofu; unstable.
VAR_003057
Natural variant1271V → G in Dhonburi/Neapolis; unstable; beta-thalassemia. Ref.73
VAR_003056
Natural variant1281Q → E in Complutense. Ref.60
VAR_003058
Natural variant1281Q → K in Brest; unstable. Ref.63
VAR_003059
Natural variant1291A → D in J-Guantanamo; unstable.
VAR_003060
Natural variant1301A → P in Crete; O(2) affinity up; unstable.
VAR_003061
Natural variant1301A → V in La Desirade; O(2) affinity down; unstable. Ref.96
VAR_003062
Natural variant1311Y → D in Wien; unstable.
VAR_003063
Natural variant1311Y → S in Nevers.
VAR_003064
Natural variant1321Q → E in Camden/Tokuchi/Motown.
VAR_003065
Natural variant1321Q → K in Shelby/Leslie/Deaconess; unstable. Ref.122
VAR_003066
Natural variant1321Q → P in Shangai; unstable.
VAR_003067
Natural variant1321Q → R in Sarrebourg; unstable.
VAR_003068
Natural variant1331K → N in Yamagata; O(2) affinity down.
VAR_003069
Natural variant1331K → Q in K-Woolwich.
VAR_003070
Natural variant1341V → L in Extredemura.
VAR_003071
Natural variant1351V → E in North Shore-Caracas; unstable. Ref.109
VAR_003072
Natural variant1361A → E in Beckman; O(2) affinity down; unstable.
VAR_003073
Natural variant1361A → P in Altdorf; O(2) affinity up; unstable.
VAR_003074
Natural variant1371G → D in Hope; O(2) affinity down; unstable.
VAR_003075
Natural variant1391A → P in Brockton; unstable.
VAR_003076
Natural variant1401N → D in Geelong; unstable. Ref.78
VAR_003077
Natural variant1401N → K in Hinsdale; O(2) affinity down. Ref.83
VAR_003078
Natural variant1401N → S in S-Wake; associated with V-6. Ref.10
VAR_025335
Natural variant1401N → Y in Aurora; O(2) affinity up. Ref.62
VAR_003079
Natural variant1411A → D in Himeji; unstable; O(2) affinity down. Ref.82
VAR_003080
Natural variant1411A → T in St Jacques: O(2) affinity up.
VAR_003081
Natural variant1411A → V in Puttelange; polycythemia; O(2) affinity up. Ref.114
VAR_003082
Natural variant1421L → R in Olmsted; unstable.
VAR_003083
Natural variant1431A → D in Ohio; O(2) affinity up.
VAR_003084
Natural variant1441H → D in Rancho Mirage.
VAR_003085
Natural variant1441H → P in Syracuse; O(2) affinity up.
VAR_003087
Natural variant1441H → Q in Little Rock; O(2) affinity up.
Corresponds to variant rs36020563 [ dbSNP | Ensembl ].
VAR_003086
Natural variant1441H → R in Abruzzo; O(2) affinity up.
VAR_003088
Natural variant1451K → E in Mito; O(2) affinity up.
VAR_003089
Natural variant1461Y → C in Rainier; O(2) affinity up.
VAR_003090
Natural variant1461Y → H in Bethesda; O(2) affinity up.
VAR_003091
Natural variant1471H → D in Hiroshima; O(2) affinity up.
VAR_003092
Natural variant1471H → L in Cowtown; O(2) affinity up.
VAR_003093
Natural variant1471H → P in York; O(2) affinity up.
VAR_003094
Natural variant1471H → Q in Kodaira; O(2) affinity up. Ref.93
VAR_003095

Experimental info

Sequence conflict261Missing in ACD39349. Ref.15
Sequence conflict421F → L in AAR96398. Ref.13

Secondary structure

....................... 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P68871 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A31F6D621C6556A1

FASTA14715,998
        10         20         30         40         50         60 
MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK 

        70         80         90        100        110        120 
VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG 

       130        140 
KEFTPPVQAA YQKVVAGVAN ALAHKYH 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]Ianzer D., Konno K., Xavier C.H., Stoecklin R., Santos R.A.S., de Camargo A.C.M., Pimenta D.C.
Submitted (JUN-2007) to UniProtKB
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]"Sites of acetylation of sickle cell hemoglobin by aspirin."
Shamsuddin M., Mason R.G., Ritchey J.M., Honig G.R., Klotz I.M.
Proc. Natl. Acad. Sci. U.S.A. 71:4693-4697(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-60; LYS-83 AND LYS-145.
[27]"The glycosylation of hemoglobin: relevance to diabetes mellitus."
Bunn H.F., Gabbay K.H., Gallop P.M.
Science 200:21-27(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCATION AT VAL-2.
[28]"Sites of nonenzymatic glycosylation of human hemoglobin A."
Shapiro R., McManus M.J., Zalut C., Bunn H.F.
J. Biol. Chem. 255:3120-3127(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCATION AT LYS-9; LYS-18; LYS-67; LYS-121 AND LYS-145, LACK OF GLYCATION AT LYS-60; LYS-83 AND LYS-96.
[29]"Human hemoglobin Portland II (zeta 2 beta 2). Isolation and characterization of Portland hemoglobin components and their constituent globin chains."
Randhawa Z.I., Jones R.T., Lie-Injo L.E.
J. Biol. Chem. 259:7325-7330(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, TISSUE SPECIFICITY, PARTIAL PROTEIN SEQUENCE.
[30]"Haemoglobin binding with haptoglobin. Localization of the haptoglobin-binding sites on the beta-chain of human haemoglobin by synthetic overlapping peptides encompassing the entire chain."
Yoshioka N., Atassi M.Z.
Biochem. J. 234:453-456(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HAPTOGLOBIN.
[31]"Beta 141 Leu is not deleted in the unstable haemoglobin Atlanta-Coventry but is replaced by a novel amino acid of mass 129 daltons."
Brennan S.O., Shaw J., Allen J., George P.M.
Br. J. Haematol. 81:99-103(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: OXIDATION AT LEU-142.
[32]"S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control."
Jia L., Bonaventura C., Bonaventura J., Stamler J.S.
Nature 380:221-226(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: S-NITROSYLATION AT CYS-94.
[33]"Crystal structure of the S-nitroso form of liganded human hemoglobin."
Chan N.L., Rogers P.H., Arnone A.
Biochemistry 37:16459-16464(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: S-NITROSYLATION AT CYS-94.
[34]"Ancient origins of nitric oxide signaling in biological systems."
Durner J., Gow A.J., Stamler J.S., Glazebrook J.
Proc. Natl. Acad. Sci. U.S.A. 96:14206-14207(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NITRIC OXIDE-BINDING.
[35]"The role of beta chains in the control of the hemoglobin oxygen binding function: chimeric human/mouse proteins, structure, and function."
Kidd R.D., Russell J.E., Watmough N.J., Baker E.N., Brittain T.
Biochemistry 40:15669-15675(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[36]"Spinorphin as an endogenous inhibitor of enkephalin-degrading enzymes: roles in pain and inflammation."
Yamamoto Y., Ono H., Ueda A., Shimamura M., Nishimura K., Hazato T.
Curr. Protein Pept. Sci. 3:587-599(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION OF SPINORPHIN.
[37]"Hemorphin and hemorphin-like peptides isolated from dog pancreas and sheep brain are able to potentiate bradykinin activity in vivo."
Ianzer D., Konno K., Xavier C.H., Stoecklin R., Santos R.A.S., de Camargo A.C.M., Pimenta D.C.
Peptides 27:2957-2966(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS OF 33-42, FUNCTION.
[38]"Structure-activity relationship studies of spinorphin as a potent and selective human P2X(3) receptor antagonist."
Jung K.Y., Moon H.D., Lee G.E., Lim H.H., Park C.S., Kim Y.C.
J. Med. Chem. 50:4543-4547(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF SPINORPHIN.
[39]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[40]"Structure of sickled erythrocytes and of sickle-cell hemoglobin fibers."
Finch J.T., Perutz M.F., Bertles J.F., Doebler J.
Proc. Natl. Acad. Sci. U.S.A. 70:718-722(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: ELECTRON MICROSCOPY OF SICKLE-CELL HEMOGLOBIN FIBERS.
[41]"Crystal structure of sickle-cell deoxyhemoglobin at 5 A resolution."
Wishner B.C., Ward K.B., Lattman E.E., Love W.E.
J. Mol. Biol. 98:179-194(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (5 ANGSTROMS) OF MUTANT VAL-7.
[42]"Three-dimensional Fourier synthesis of human deoxyhaemoglobin at 2.5-A resolution: refinement of the atomic model."
Fermi G.
J. Mol. Biol. 97:237-256(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN.
[43]"The structure of human carbonmonoxy haemoglobin at 2.7-A resolution."
Baldwin J.M.
J. Mol. Biol. 136:103-128(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF CARBONMONOXY HEMOGLOBIN.
[44]"The crystal structure of human deoxyhaemoglobin at 1.74 A resolution."
Fermi G., Perutz M.F., Shaanan B., Fourme R.
J. Mol. Biol. 175:159-174(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF DEOXYHEMOGLOBIN.
[45]"High-resolution X-ray study of deoxyhemoglobin Rothschild 37 beta Trp-->Arg: a mutation that creates an intersubunit chloride-binding site."
Kavanaugh J.S., Rogers P.H., Case D.A., Arnone A.
Biochemistry 31:4111-4121(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ROTHSCHILD ARG-38.
[46]"Structure-function relationships in the low-affinity mutant haemoglobin Aalborg (Gly74 (E18)beta-->Arg)."
Fermi G., Perutz M.F., Williamson D., Stein P., Shih D.T.
J. Mol. Biol. 226:883-888(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ARG-75.
[47]"Human deoxyhaemoglobin-2,3-diphosphoglycerate complex low-salt structure at 2.5 A resolution."
Richard V., Dodson G.G., Mauguen Y.
J. Mol. Biol. 233:270-274(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), BISPHOSPHOGLYCERATE BINDING.
[48]"Crystal structure of T state haemoglobin with oxygen bound at all four haems."
Paoli M., Liddington R., Tame J., Wilkinson A., Dodson G.
J. Mol. Biol. 256:775-792(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[49]"High-resolution crystal structures of human hemoglobin with mutations at tryptophan 37beta: structural basis for a high-affinity T-state."
Kavanaugh J.S., Weydert J.A., Rogers P.H., Arnone A.
Biochemistry 37:4358-4373(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-38; GLU-38; GLY-38 AND TYR-38.
[50]"Crystal structure of deoxy-human hemoglobin beta6 Glu-->Trp. Implications for the structure and formation of the sickle cell fiber."
Harrington D.J., Adachi K., Royer W.E. Jr.
J. Biol. Chem. 273:32690-32696(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT TRP-7.
[51]"Structure of mutant human carbonmonoxyhemoglobin C (betaE6K) at 2.0 A resolution."
Dewan J.C., Feeling-Taylor A., Puius Y.A., Patskovska L., Patskovsky Y., Nagel R.L., Almo S.C., Hirsch R.E.
Acta Crystallogr. D 58:2038-2042(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT LYS-7.
[52]"Structure of fully liganded Hb zeta2beta2s trapped in a tense conformation."
Safo M.K., Ko T.P., Abdulmalik O., He Z., Wang A.H., Schreiter E.R., Russell J.E.
Acta Crystallogr. D 69:2061-2071(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF VARIANT S VAL-7 IN COMPLEX WITH HEME AND HBZ, SUBUNIT.
[53]"Hemoglobin Freiburg: abnormal hemoglobin due to deletion of a single amino acid residue."
Jones R.T., Brimhall B., Huisman T.H., Kleihauer E., Betke K.
Science 154:1024-1027(1966) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FREIBURG VAL-24 DEL.
[54]"Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys) and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg)."
Brimhall B., Jones R.T., Schneider R.G., Hosty T.S., Tomlin G., Atkins R.
Biochim. Biophys. Acta 379:28-32(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALABAMA LYS-40.
[55]"Functional and physicochemical studies of hemoglobin St. Louis beta 28 (B10) Leu replaced by Gln: a variant with ferric beta heme iron."
Thillet J., Cohen-Solal M., Seligmann M., Rosa J.
J. Clin. Invest. 58:1098-1106(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HEIBAN, VARIANT ST LOUIS GLN-29.
[56]"Molecular basis for dominantly inherited inclusion body beta-thalassemia."
Thein S.L., Hesketh C., Taylor P., Temperley I.J., Hutchinson R.M., Old J.M., Wood W.G., Clegg J.B., Weatherall D.J.
Proc. Natl. Acad. Sci. U.S.A. 87:3924-3928(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN B-THALIB.
[57]"Hb Alesha or alpha 2 beta (2)67(E11)Val-->Met: a new unstable hemoglobin variant identified through sequencing of amplified DNA."
Molchanova T.P., Postnikov Y.V., Pobedimskaya D.D., Smetanina N.S., Moschan A.A., Kazanetz E.G., Tokarev Y.N., Huisman T.H.J.
Hemoglobin 17:217-225(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALESHA MET-68.
[58]"Hemoglobin J Altgeld Gardens. A hemoglobin variant with a substitution of the proximal histidine of the beta-chain."
Adams J.G. III, Przywara K.P., Heller P., Shamsuddin M.
Hemoglobin 2:403-415(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT J-ALTGELDS GARDENS ASP-93.
[59]"A new haemoglobin J from Turkey -- Hb Ankara (beta10 (A7) Ala-Asp)."
Arcasoy A., Casey R., Lehmann H., Cavdar A.O., Berki A.
FEBS Lett. 42:121-123(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ANKARA ASP-11.
[60]"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."
Huisman T.H.J., Wilson J.B., Kutlar A., Yang K.-G., Chen S.-S., Webber B.B., Altay C., Martinez A.V.
Biochim. Biophys. Acta 871:229-231(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS J-ANTAKYA MET-66 AND COMPLUTENSE GLU-128.
[61]"A new unstable and low oxygen affinity hemoglobin variant: Hb J-Auckland [beta 25(B7)Gly-->Asp]."
Williamson D., Wells R.M.G., Anderson R., Matthews J.
Hemoglobin 11:221-230(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT J-AUCKLAND ASP-26.
[62]"Identification of a new high oxygen affinity hemoglobin variant: Hb Aurora [beta 139(H17) Asn-->Tyr]."
Lafferty J., Ali M., Matthew K., Eng B., Patterson M., Waye J.S.
Hemoglobin 19:335-341(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AURORA TYR-140.
[63]"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."
Baudin-Chich V., Wajcman H., Gombaud-Saintonge G., Arous N., Riou J., Briere J., Galacteros F.
Hemoglobin 12:179-188(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BREST LYS-128.
[64]"Hemoglobin Brisbane: beta68 Leu replaced by His. A new high oxygen affinity variant."
Brennan S.O., Wells R.M., Smith H., Carrell R.W.
Hemoglobin 5:325-335(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BRISBANE HIS-69.
[65]"A new hemoglobin with high oxygen affinity -- hemoglobin Bunbury: alpha 2 beta 2 [94 (FG1) Asp replaced by Asn]."
Como P.F., Kennett D., Wilkinson T., Kronenberg H.
Hemoglobin 7:413-421(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BUNBURY ASN-95.
[66]"Hemoglobin J Cairo: beta 65 (E9) Lys leads to Gln, A new hemoglobin variant discovered in an Egyptian family."
Garel M.-C., Hassan W., Coquelet M.T., Goossens M., Rosa J., Arous N.
Biochim. Biophys. Acta 420:97-104(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT J-CAIRO GLN-66.
[67]"A new haemoglobin variant, haemoglobin Camperdown (beta 104 (G6) arginine->serine)."
Wilkinson T., Chua C.G., Carrell R.W., Robin H., Exner T., Lee K.M., Kronenberg H.
Biochim. Biophys. Acta 393:195-200(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CAMPERDOWN SER-105.
[68]"Haemoglobin caribbean beta91 (F7) Leu replaced by Arg: a mildly haemoglobin with a low oxygen affinity."
Ahern E., Ahern V., Hilton T., Serjeant G.R., Serjeant B.E., Seakins M., Lang A., Middleton A., Lehmann H.
FEBS Lett. 69:99-102(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CARIBBEAN ARG-92.
[69]"A silent hemoglobin variant detected by HPLC: hemoglobin City of Hope beta 69 (E13) Gly-->Ser."
Rahbar S., Asmerom Y., Blume K.G.
Hemoglobin 8:333-342(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CITY OF HOPE SER-70.
[70]"Hb Coimbra or alpha 2 beta (2)99(G1)Asp-->Glu, a newly discovered high oxygen affinity variant."
Tamagnini G.P., Ribeiro M.L., Valente V., Ramachandran M., Wilson J.B., Baysal E., Gu L.H., Huisman T.H.J.
Hemoglobin 15:487-496(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT COIMBRA GLU-100.
[71]"Hb Costa Rica or alpha 2 beta 2 77(EF1)His-->Arg: the first example of a somatic cell mutation in a globin gene."
Romero W.E.R., Castillo M., Chaves M.A., Saenz G.F., Gu L.-H., Wilson J.B., Baysal E., Smetanina N.S., Leonova J.Y., Huisman T.H.J.
Hum. Genet. 97:829-833(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT COSTA RICA ARG-78.
[72]"Hemoglobin Debrousse (beta 96[FG3]Leu-->Pro): a new unstable hemoglobin with twofold increased oxygen affinity."
Lacan P., Kister J., Francina A., Souillet G., Galacteros F., Delaunay J., Wajcman H.
Am. J. Hematol. 51:276-281(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DEBROUSSE PRO-97.
[73]"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."
Bardakdjian-Michau J., Fucharoen S., Delanoe-Garin J., Kister J., Lacombe C., Winichagoon P., Blouquit Y., Riou J., Wasi P., Galacteros F.
Am. J. Hematol. 35:96-99(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DHONBURI GLY-127.
[74]"Two new human hemoglobin variants caused by unusual mutational events: Hb Zaire contains a five residue repetition within the alpha-chain and Hb Duino has two residues substituted in the beta-chain."
Wajcman H., Blouquit Y., Vasseur C., le Querrec A., Laniece M., Melevendi C., Rasore A., Galacteros F.
Hum. Genet. 89:676-680(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NEWCASTLE PRO-93 AND CAMPERDOWN SER-105, DESCRIPTION OF VARIANT DUINO.
[75]"A novel beta-globin structural mutant, Hb Brescia (beta 114 Leu-Pro), causing a severe beta-thalassemia intermedia phenotype."
Murru S., Poddie D., Sciarratta G.V., Agosti S., Baffico M., Melevendi C., Pirastu M., Cao A.
Hum. Mutat. 1:124-128(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DURHAM-N.C. PRO-115.
[76]"A novel beta-globin mutation, beta Durham-NC [beta 114 Leu-->Pro], produces a dominant thalassemia-like phenotype."
de Castro C.M., Devlin B., Fleenor D.E., Lee M.E., Kaufman R.E.
Blood 83:1109-1116(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DURHAM-N.C. PRO-115.
[77]"Hb J-Europa [beta 62(E6)Ala-->Asp]: normal oxygen binding properties in a new variant involving a residue located distal to the heme."
Kiger L., Kister J., Groff P., Kalmes G., Prome D., Galacteros F., Wajcman H.
Hemoglobin 20:135-140(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT J-EUROPA ASP-63.
[78]"Hb Geelong [beta 139(H17)Asn-->Asp]."
Como P.F., Hocking D.R., Swinton G.W., Trent R.J., Holland R.A.B., Tibben E.A., Wilkinson T., Kronenberg H.
Hemoglobin 15:85-95(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GEELONG ASP-140.
[79]"Hemoglobin Grange-Blanche [beta 27(B9) Ala-->Val], a new variant with normal expression and increased affinity for oxygen."
Baklouti F., Giraud Y., Francina A., Richard G., Perier C., Geyssant A., Jaubert J., Brizard C., Delaunay J.
FEBS Lett. 223:59-62(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GRANGE-BLANCHE VAL-28.
[80]"Hb Graz or alpha 2 beta 2(2)(NA2)His-->Leu; a new beta chain variant observed in four families from southern Austria."
Liu J.S., Molchanova T.P., Gu L.H., Wilson J.B., Hopmeier P., Schnedl W., Balaun E., Krejs G.J., Huisman T.H.J.
Hemoglobin 16:493-501(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GRAZ LEU-3.
[81]"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)."
Ikkala E., Koskela J., Pikkarainen P., Rahiala E.-L., El-Hazmi M.A.F., Nagai K., Lang A., Lehmann H.
Acta Haematol. 56:257-275(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HELSINKI MET-83.
[82]"Hb Himeji or beta 140 (H18) Ala-->Asp. A slightly unstable hemoglobin with increased beta N-terminal glycation."
Ohba Y., Miyaji T., Murakami M., Kadowaki S., Fujita T., Oimomi M., Hatanaka H., Ishikawa K., Baba S., Hitaka K., Imai K.
Hemoglobin 10:109-126(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIMEJI ASP-141.
[83]"Hb Hinsdale [beta 139 (H17)Asn-->Lys]: a variant in the central cavity showing reduced affinity for oxygen and 2,3-diphosphoglycerate."
Moo-Penn W.F., Johnson M.H., Jue D.L., Lonser R.
Hemoglobin 13:455-464(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HINSDALE LYS-140.
[84]"HB Hinwil or beta 38(C4)Thr-->Asn: a new beta chain variant detected in a Swiss family."
Frischknecht H., Ventruto M., Hess D., Hunziker P., Rosatelli M.C., Cao A., Breitenstein U., Fehr J., Tuchschmid P.
Hemoglobin 20:31-40(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HINWIL ASN-39.
[85]"Hb Howick [beta 37(C3)Trp-->Gly]: a new high oxygen affinity variant of the alpha 1 beta 2 contact."
Owen M.C., Ockelford P.A., Wells R.M.G.
Hemoglobin 17:513-521(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HOWICK GLY-38.
[86]"The structure of hemoglobin Indianapolis [beta112(G14) arginine]. An unstable variant detectable only by isotopic labeling."
Adams J.G. III, Steinberg M.H., Boxer L.A., Baehner R.L., Forget B.G., Tsistrakis G.A.
J. Biol. Chem. 254:3479-3482(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT INDIANAPOLIS ARG-113.
[87]"Hb Isehara (or Hb Redondo) [beta 92 (F8) His-->Asn]: an unstable variant with a proximal histidine substitution at the heme contact."
Harano T., Harano K., Kushida Y., Ueda S., Yoshii A., Nishinarita M.
Hemoglobin 15:279-290(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ISEHARA ASN-93.
[88]"Hemoglobin Istanbul: substitution of glutamine for histidine in a proximal histidine (F8(92))."
Aksoy M., Erdem S., Efremov G.D., Wilson J.B., Huisman T.H.J., Schroeder W.A., Shelton J.R., Shelton J.B., Ulitin O.N., Muftuoglu A.
J. Clin. Invest. 51:2380-2387(1972) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ISTAMBUL GLN-93.
[89]"Hb Jacksonville [alpha 2 beta 2(54)(D5)Val-->Asp]: a new unstable variant found in a patient with hemolytic anemia."
Gaudry C.L. Jr., Pitel P.A., Jue D.L., Hine T.K., Johnson M.H., Moo-Penn W.F.
Hemoglobin 14:653-659(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT JACKSONVILLE ASP-55.
[90]"Hemoglobin Jianghua [beta 120(GH3) Lys leads to Ile]: a new fast-moving variant found in China."
Lu Y.Q., Fan J.L., Liu J.F., Hu H.L., Peng X.H., Huang C.-H., Huang P.Y., Chen S.S., Jai P.C., Yang K.G.
Hemoglobin 7:321-326(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT JIANGHUA ILE-121.
[91]"Hb Karlskoga or alpha 2 beta (2)21(B3) Asp-->His: a new slow-moving variant found in Sweden."
Landin B.
Hemoglobin 17:201-208(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT KARLSKOGA HIS-22.
[92]"Structural study of hemoglobin Knossos, beta 27 (B9) Ala leads to Ser. A new abnormal hemoglobin present as a silent beta-thalassemia."
Arous N., Galacteros F., Fessas P., Loukopoulos D., Blouquit Y., Komis G., Sellaye M., Boussiou M., Rosa J.
FEBS Lett. 147:247-250(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT KNOSSOS SER-28.
[93]"Hb Kodaira [beta 146(HC3)His-->Gln]: a new beta chain variant with an amino acid substitution at the C-terminus."
Harano T., Harano K., Kushida Y., Imai K., Nishinakamura R., Matsunaga T.
Hemoglobin 16:85-91(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT KODAIRA GLN-147.
[94]"A new electrophoretically-silent hemoglobin variant: hemoglobin Kofu or alpha 2 beta 2 84 (EF8) Thr-->Ile."
Harano T., Harano K., Ueda S., Imai N., Kitazumi T.
Hemoglobin 10:417-420(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT KOFU ILE-85.
[95]"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."
Divoky V., Svobodova M., Indrak K., Chrobak L., Molchanova T.P., Huisman T.H.J.
Hemoglobin 17:319-328(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HRADEC KRALOVE ASP-116.
[96]"Hemoglobin La Desirade alpha A2 beta 2 129 (H7) Ala-->Val: a new unstable hemoglobin."
Merault G., Keclard L., Garin J., Poyart C., Blouquit Y., Arous N., Galacteros F., Feingold J., Rosa J.
Hemoglobin 10:593-605(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LA DESIRADE VAL-130.
[97]"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]."
Wajcman H., Kister J., Vasseur C., Blouquit Y., Trastour J.C., Cottenceau D., Galacteros F.
Biochim. Biophys. Acta 1138:127-132(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LA ROCHE-SUR-YON HIS-82.
[98]"Hb Las Palmas or alpha 2 beta 2(49)(CD8)Ser-->Phe, a mildly unstable hemoglobin variant."
Malcorra-Azpiazu J.J., Balda-Aguirre M.I., Diaz-Chico J.C., Hu H., Wilson J.B., Webber B.B., Kutlar F., Kutlar A., Huisman T.H.J.
Hemoglobin 12:163-170(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LAS PALMAS PHE-50.
[99]"Hb Linkoping (beta 36 Pro-->Thr): a new high oxygen affinity hemoglobin variant found in two families of Finnish origin."
Berlin G., Wranne B., Jeppsson J.-O.
Eur. J. Haematol. 39:452-456(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LINKOPING THR-37.
[100]"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)."
Marinucci M., Boissel J.P., Massa A., Wajcman H., Tentori L., Labie D.
Hemoglobin 7:423-433(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MAPUTO TYR-48.
[101]"Hb Matera [beta 55(D6)Met-->Lys]: a new unstable hemoglobin variant in an Italian family."
Sciarratta G.V., Ivaldi G.
Hemoglobin 14:79-85(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MATERA LYS-56.
[102]"Hemoglobin Miyashiro (beta 23[B5] val substituting for gly) an electrophoretically silent variant discovered by the isopropanol test."
Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Miyata H., Shinohara T., Hori T., Takayama J.
Hemoglobin 5:653-666(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MIYASHIRO GLY-24.
[103]"Hemoglobin Mizuho or beta 68 (E 12) leucine leads to proline, a new unstable variant associated with severe hemolytic anemia."
Ohba Y., Miyaji T., Matsuoka M., Sugiyama K., Suzuki T., Sugiura T.
Hemoglobin 1:467-477(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MIZUHO PRO-69.
[104]"A new variant, HB Muscat [alpha 2 beta (2)32(B14)Leu-->Val] observed in association with HB S in an Arabian family."
Ramachandran M., Gu L.H., Wilson J.B., Kitundu M.N., Adekile A.D., Liu J.C., McKie K.M., Huisman T.H.J.
Hemoglobin 16:259-266(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MUSCAT VAL-33.
[105]"Hb N-Timone [alpha 2 beta 2(8)(A5)Lys-->Glu]: a new fast-moving variant with normal stability and oxygen affinity."
Lena-Russo D., Orsini A., Vovan L., Bardakdjian-Michau J., Lacombe C., Blouquit Y., Craescu C.T., Galacteros F.
Hemoglobin 13:743-747(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT N-TIMONE GLU-9.
[106]"A new unstable, high oxygen affinity hemoglobin: Hb Nagoya or beta 97 (FG4) His-->Pro."
Ohba Y., Imanaka M., Matsuoka M., Hattori Y., Miyaji T., Funaki C., Shibata K., Shimokata H., Kuzuya F., Miwa S.
Hemoglobin 9:11-24(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NAGOYA PRO-98.
[107]"Hb D-Neath or beta 121 (GH4) Glu-->Ala: a new member of the Hb D family."
Welch S.G., Bateman C.
Hemoglobin 17:255-259(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT D-NEATH ALA-122.
[108]"Hemoglobin North Chicago (beta 36 [C2] proline-->serine): a new high affinity hemoglobin."
Rahbar S., Louis J., Lee T., Asmerom Y.
Hemoglobin 9:559-576(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NORTH CHICAGO SER-37.
[109]"Haemoglobin North Shore-Caracas beta 134 (H12) valine replaced by glutamic acid."
Arends T., Lehmann H., Plowman D., Stathopoulou R.
FEBS Lett. 80:261-265(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NORTH SHORE-CARACAS GLU-135.
[110]"Hb Olomouc or alpha 2 beta 2(86)(F2)Ala-->Asp, a new high oxygen affinity variant."
Indrak K., Wiedermann B.F., Batek F., Wilson J.B., Webber B.B., Kutlar A., Huisman T.H.J.
Hemoglobin 11:151-155(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OLOMOUC ASP-87.
[111]"Hemoglobin Palmerston North beta 23 (B5) Val replaced by Phe. A new variant identified in a patient with polycythemia."
Brennan S.O., Williamson D., Whisson M.E., Carrell R.W.
Hemoglobin 6:569-575(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PALMERSTON NORTH PHE-24.
[112]"Hemoglobin Pierre-Benite [beta 90(F6)Glu-->Asp], a new high affinity variant found in a French family."
Baklouti F., Giraud Y., Francina A., Richard G., Favre-Gilly J., Delaunay J.
Hemoglobin 12:171-177(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PIERRE-BENITE ASP-91.
[113]"Hemoglobin Presbyterian: beta108 (G10) asparagine leads to lysine, A hemoglobin variant with low oxygen affinity."
Moo-Penn W.F., Wolff J.A., Simon G., Vacek M., Jue D.L., Johnson M.H.
FEBS Lett. 92:53-56(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PRESBYTERIAN LYS-109.
[114]"Germline mosaicism for an alanine to valine substitution at residue beta 140 in hemoglobin Puttelange, a new variant with high oxygen affinity."
Wajcman H., Girodon E., Prome D., North M.L., Plassa F., Duwig I., Kister J., Bergerat J.P., Oberling F., Lampert E., Lonsdorfer J., Goossens M., Galacteros F.
Hum. Genet. 96:711-716(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PUTTELANGE VAL-141.
[115]"Hemoglobin Quin-Hai, beta 78 (EF2) Leu replaced by Arg, a new abnormal hemoglobin found in Guangdong, China."
Jen P.C., Chen L.C., Chen P.F., Wong Y., Chen L.F., Guo Y.Y., Chang F.Q., Chow Y.C., Chiu Y.
Hemoglobin 7:407-412(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT QUIN-HAI ARG-79.
[116]"Hemoglobin Rambam (beta69[E13]Gly-->Asp), a pitfall in the assessment of diabetic control: characterization by electrospray mass spectrometry and HPLC."
Bisse E., Zorn N., Eigel A., Lizama M., Huamam-Guillen P., Marz W., van Dorsselaer A., Wieland H.
Clin. Chem. 44:2172-2177(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RAMBAM ASP-70.
[117]"Hemoglobin Randwick or beta 15 (A12)Trp-->Gly: a new unstable beta-chain hemoglobin variant."
Gilbert A.T., Fleming P.J., Sumner D.R., Hughes W.G., Ip F., Kwan Y.L., Holland R.A.B.
Hemoglobin 12:149-161(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RANDWICK GLY-16.
[118]"Hemoglobin Rio Grande [beta 8 (A5) Lys leads to Thr] a new variant found in a Mexican-American family."
Moo-Penn W.F., Johnson M.H., McGuffey J.E., Jue D.L., Therrell B.L. Jr.
Hemoglobin 7:91-95(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RIO GRANDE THR-9.
[119]"Hemoglobin Rush (beta 101 (g3) glutamine): a new unstable hemoglobin causing mild hemolytic anemia."
Adams J.G. III, Winter W.P., Tausk K., Heller P.
Blood 43:261-269(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RUSH GLN-102.
[120]"Hemoglobin Saitama or beta 117 (G19) His leads to Pro, a new variant causing hemolytic disease."
Ohba Y., Hasegawa Y., Amino H., Miwa S., Nakatsuji T., Hattori Y., Miyaji T.
Hemoglobin 7:47-56(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SAITAMA PRO-118.
[121]"Chemical studies of several varieties of Hb M."
Gerald P.S., Efron M.L.
Proc. Natl. Acad. Sci. U.S.A. 47:1758-1767(1961) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT M-SASKATOON TYR-64.
[122]"Hemoglobin Shelby [beta 131(H9) Gln-->Lys] a correction to the structure of hemoglobin Deaconess and hemoglobin Leslie."
Moo-Penn W.F., Johnson M.H., McGuffey J.E., Jue D.L.
Hemoglobin 8:583-593(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SHELBY/LESLIE/DEACONESS LYS-132.
[123]"Hb J Sicilia: beta 65 (E9) Lys-Asn, a beta homologue of Hb Zambia."
Ricco G., Pich P.G., Mazza U., Rossi G., Ajmar P., Arese P., Gallo E.
FEBS Lett. 39:200-204(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT J-SICILIA ASN-66.
[124]"A new unstable and low oxygen affinity hemoglobin variant: Hb Stanmore [beta 111(G13)Val-->Ala]."
Como P.F., Wylie B.R., Trent R.J., Bruce D., Volpato F., Wilkinson T., Kronenberg H., Holland R.A.B., Tibben E.A.
Hemoglobin 15:53-65(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT STANMORE ALA-112.
[125]"Hemoglobin Saint Mande beta 102 (G4) asn replaced by tyr: a new low oxygen affinity variant."
Arous N., Braconnier F., Thillet J., Blouquit Y., Galacteros F., Chevrier M., Bordahandy C., Rosa J.
FEBS Lett. 126:114-116(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ST MANDE TYR-103.
[126]"Hemoglobin Windsor or beta 11 (A8)Val-->Asp: a new unstable beta-chain hemoglobin variant producing a hemolytic anemia."
Gilbert A.T., Fleming P.J., Sumner D.R., Hughes W.G., Holland R.A.B., Tibben E.A.
Hemoglobin 13:437-453(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WINDSOR ASP-12.
[127]"A new abnormal variant, Hb Yahata or beta 112(G14)Cys-->Tyr, found in a Japanese: structural confirmation by DNA sequencing of the beta-globin gene."
Harano T., Harano K., Kushida Y., Ueda S.
Hemoglobin 15:109-113(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT YAHATA TYR-113.
[128]"A new unstable hemoglobin, Hb Yokohama beta 31 (B13)Leu substituting for Pro, causing hemolytic anemia."
Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Hino S., Matsumoto N.
Hemoglobin 5:667-678(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT YOKOHAMA PRO-32.
[129]"Hemoglobin Hammersmith (beta 42 (CD1) Phe replaced by Ser) associated with severe hemolytic anemia."
Rahbar S., Feagler R.J., Beutler E.
Hemoglobin 5:97-105(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HEIBAN, VARIANT HAMMERSMITH SER-43.
[130]"Hb Bruxelles: alpha 2A beta (2)41 or 42(C7 or CD1)Phe deleted."
Blouquit Y., Bardakdjian J., Lena-Russo D., Arous N., Perrimond H., Orsini A., Rosa J., Galacteros F.
Hemoglobin 13:465-474(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HEIBAN, VARIANTS BRUXELLES PHE-42 DEL AND PHE-43 DEL.
[131]"Hb Zengcheng or alpha 2 beta(2)114(G16)Leu-->Met."
Plaseska D., Wilson J.B., Gu L.H., Kutlar F., Huisman T.H.J., Zeng Y.T., Shen M.
Hemoglobin 14:555-557(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ZENGCHENG MET-115.
[132]"Haemoglobin Manukau beta 67[E11] Val-->Gly: transfusion-dependent haemolytic anaemia ameliorated by coexisting alpha thalassaemia."
Fay K.C., Brennan S.O., Costello J.M., Potter H.C., Williamson D.A., Trent R.J., Ockelford P.A., Boswell D.R.
Br. J. Haematol. 85:352-355(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NON-SPHEROCYTIC HAEMOLITIC ANEMIA GLY-68.
[133]"A novel silent posttranslational mechanism converts methionine to aspartate in hemoglobin Bristol (beta 67[E11] Val-Met->Asp)."
Rees D.C., Rochette J., Schofield C., Green B., Morris M., Parker N.E., Sasaki H., Tanaka A., Ohba Y., Clegg J.B.
Blood 88:341-348(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HEIBAN, VARIANT BRISTOL ASP-68.
[134]"Hb Iraq-Halabja beta10 (A7) Ala-->Val (GCC-->GTC): a new beta-chain silent variant in a family with multiple Hb disorders."
Deutsch S., Darbellay R., Offord R.E., Frutiger A., Kister J., Wajcman H., Beris P.
Am. J. Hematol. 61:187-193(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT IRAQ-HALABJA VAL-11.
[135]"Identification of Hb Villejuif [beta123(H1)Thr-->Ile] in Southern Italy."
Carbone V., Salzano A.M., Pagano L., Buffardi S., De Rosa C., Pucci P.
Hemoglobin 25:67-78(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VILLEJUIF ILE-124.
[136]"Hb Tsukumi [beta117(G19)His-->Tyr] found in a Moroccan woman."
North M.L., Duwig I., Riou J., Prome D., Yapo A.P., Kister J., Bardakdjian-Michau J., Cazenave J.-P., Wajcman H.
Hemoglobin 25:107-110(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TSUKUMI TYR-118.
[137]"Hb Canterbury [beta112(G14)Cys-->Phe]: a new, mildly unstable variant."
Brennan S.O., Potter H.C., Kubala L.M., Carnoutsos S.A., Ferguson M.M.
Hemoglobin 26:67-69(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CANTERBURY PHE-113.
[138]"Double heterozygosity for Hb Pyrgos [beta83(EF7)Gly-->Asp] and Hb E [beta26(B8)Glu-->Lys] found in association with alpha-thalassemia."
Sawangareetrakul P., Svasti S., Yodsowon B., Winichagoon P., Srisomsap C., Svasti J., Fucharoen S.
Hemoglobin 26:191-196(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PYRGOS ASP-84, VARIANT E LYS-27.
[139]"Hb Santander [beta34(B16)Val-->Asp (GTC-->GAC)]: a new unstable variant found as a de novo mutation in a Spanish patient."
Villegas A., Ropero P., Nogales A., Gonzalez F.A., Mateo M., Mazo E., Rodrigo E., Arias M.
Hemoglobin 27:31-35(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SANTANDER ASP-35.
[140]"Two new hemoglobin variants with increased oxygen affinity: Hb Nantes [beta34(B16)Val-->Leu] and Hb Vexin [beta116(G18)His-->Leu]."
Wajcman H., Bardakdjian-Michau J., Riou J., Prehu C., Kister J., Baudin-Creuza V., Prome D., Richelme-David S., Harousseau J.L., Galacteros F.
Hemoglobin 27:191-199(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NANTES LEU-35, VARIANT VEXIN LEU-117.
[141]"The 'hot-spot' of Hb E [beta26(B8)Glu-->Lys] in Southeast Asia: beta-globin anomalies in the Lao Theung population of southern Laos."
Flatz G., Sanguansermsri T., Sengchanh S., Horst D., Horst J.
Hemoglobin 28:197-204(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LYS-27.
+Additional computationally mapped references.

Web resources

HbVar

Human hemoglobin variants and thalassemias

GeneReviews
SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Hemoglobin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRHBHU. A53136.
RefSeqNP_000509.1. NM_000518.4.
UniGeneHs.523443.

3D structure databases

PDBe
RCSB PDB
PDBj
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/D3-147[»]
1C7CX-ray1.80B/D3-147[»]
1C7DX-ray1.80B/D3-147[»]
1CBLX-ray1.80A/B/C/D2-147[»]
1CBMX-ray1.74A/B/C/D1-147[»]
1CH4X-ray2.50A/B/C/D2-107[»]
1CLSX-ray1.90B/D1-147[»]
1CMYX-ray3.00B/D1-147[»]
1COHX-ray2.90B/D1-147[»]
1DKEX-ray2.10B/D1-147[»]
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/D2-146[»]
1HACX-ray2.60B/D2-146[»]
1HBAX-ray2.10B/D2-147[»]
1HBBX-ray1.90B/D2-147[»]
1HBSX-ray3.00B/D/F/H1-147[»]
1HCOX-ray2.70B2-147[»]
1HDBX-ray2.20B/D1-147[»]
1HGAX-ray2.10B/D1-147[»]
1HGBX-ray2.10B/D1-147[»]
1HGCX-ray2.10B/D1-147[»]
1HHOX-ray2.10B1-147[»]
1IRDX-ray1.25B1-147[»]
1J3YX-ray1.55B/D/F/H1-147[»]
1J3ZX-ray1.60B/D/F/H1-147[»]
1J40X-ray1.45B/D/F/H1-147[»]
1J41X-ray1.45B/D/F/H1-147[»]
1J7SX-ray2.20B/D3-147[»]
1J7WX-ray2.00B/D3-147[»]
1J7YX-ray1.70B/D3-147[»]
1JY7X-ray3.20B/D/Q/S/V/X1-147[»]
1K0YX-ray1.87B/D1-147[»]
1K1KX-ray2.00B1-147[»]
1KD2X-ray1.87B/D1-147[»]
1LFLX-ray2.70B/D/Q/S1-147[»]
1LFQX-ray2.60B1-147[»]
1LFTX-ray2.60B1-147[»]
1LFVX-ray2.80B1-147[»]
1LFYX-ray3.30B1-147[»]
1LFZX-ray3.10B1-147[»]
1LJWX-ray2.16B1-147[»]
1M9PX-ray2.10B/D1-147[»]
1MKOX-ray2.18B/D1-147[»]
1NEJX-ray2.10B/D1-147[»]
1NIHX-ray2.60B/D1-147[»]
1NQPX-ray1.73B/D1-147[»]
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/D1-147[»]
1QSIX-ray1.70B/D1-147[»]
1QXDX-ray2.25B/D1-147[»]
1QXEX-ray1.85B/D1-147[»]
1R1XX-ray2.15B1-147[»]
1R1YX-ray1.80B/D1-147[»]
1RPSX-ray2.11B/D1-147[»]
1RQ3X-ray1.91B/D1-147[»]
1RQ4X-ray2.11B/D1-147[»]
1RQAX-ray2.11B/D3-147[»]
1RVWX-ray2.50B1-147[»]
1SDKX-ray1.80B/D1-147[»]
1SDLX-ray1.80B/D1-147[»]
1THBX-ray1.50B/D1-147[»]
1UIWX-ray1.50B/D/F/H1-147[»]
1VWTX-ray1.90B/D1-147[»]
1XXTX-ray1.91B/D1-147[»]
1XY0X-ray1.99B/D1-147[»]
1XYEX-ray2.13B/D1-147[»]
1XZ2X-ray1.90B/D1-147[»]
1XZ4X-ray2.00B/D1-147[»]
1XZ5X-ray2.11B/D1-147[»]
1XZ7X-ray1.90B/D1-147[»]
1XZUX-ray2.16B/D1-147[»]
1XZVX-ray2.11B/D1-147[»]
1Y09X-ray2.25B/D1-147[»]
1Y0AX-ray2.22B/D1-147[»]
1Y0CX-ray2.30B/D1-147[»]
1Y0DX-ray2.10B/D1-147[»]
1Y0TX-ray2.14B/D3-147[»]
1Y0WX-ray2.14B/D3-147[»]
1Y22X-ray2.16B/D3-147[»]
1Y2ZX-ray2.07B/D3-147[»]
1Y31X-ray2.13B/D3-147[»]
1Y35X-ray2.12B/D3-147[»]
1Y45X-ray2.00B/D3-147[»]
1Y46X-ray2.22B/D3-147[»]
1Y4BX-ray2.10B/D3-147[»]
1Y4FX-ray2.00B/D3-147[»]
1Y4GX-ray1.91B/D3-147[»]
1Y4PX-ray1.98B/D3-147[»]
1Y4QX-ray2.11B/D3-147[»]
1Y4RX-ray2.22B/D3-147[»]
1Y4VX-ray1.84B/D3-147[»]
1Y5FX-ray2.14B/D3-147[»]
1Y5JX-ray2.03B/D3-147[»]
1Y5KX-ray2.20B/D3-147[»]
1Y7CX-ray2.10B/D3-147[»]
1Y7DX-ray1.90B/D3-147[»]
1Y7GX-ray2.10B/D3-147[»]
1Y7ZX-ray1.98B/D3-147[»]
1Y83X-ray1.90B/D3-147[»]
1Y85X-ray2.13B/D1-146[»]
1Y8WX-ray2.90B/D1-147[»]
1YDZX-ray3.30B/D1-147[»]
1YE0X-ray2.50B/D3-147[»]
1YE1X-ray4.50B/D3-147[»]
1YE2X-ray1.80B/D3-147[»]
1YENX-ray2.80B/D3-147[»]
1YEOX-ray2.22B/D3-147[»]
1YEQX-ray2.75B/D3-147[»]
1YEUX-ray2.12B/D3-147[»]
1YEVX-ray2.11B/D3-147[»]
1YFFX-ray2.40B/D/F/H1-147[»]
1YG5X-ray2.70B/D3-147[»]
1YGDX-ray2.73B/D3-147[»]
1YGFX-ray2.70B/D3-147[»]
1YH9X-ray2.20B/D1-147[»]
1YHEX-ray2.10B/D1-147[»]
1YHRX-ray2.60B/D1-147[»]
1YIEX-ray2.40B/D3-147[»]
1YIHX-ray2.00B/D3-147[»]
1YVQX-ray1.80B/D1-147[»]
1YVTX-ray1.80B1-147[»]
1YZIX-ray2.07B1-147[»]
2D5ZX-ray1.45B/D1-147[»]
2D60X-ray1.70B/D1-147[»]
2DN1X-ray1.25B1-147[»]
2DN2X-ray1.25B/D1-147[»]
2DN3X-ray1.25B2-147[»]
2DXMneutron diffraction2.10B/D2-147[»]
2H35NMR-B/D2-147[»]
2HBCX-ray2.10B1-147[»]
2HBDX-ray2.20B1-147[»]
2HBEX-ray2.00B1-147[»]
2HBFX-ray2.20B1-147[»]
2HBSX-ray2.05B/D/F/H1-147[»]
2HCOX-ray2.70B2-147[»]
2HHBX-ray1.74B/D2-147[»]
2HHDX-ray2.20B/D1-147[»]
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/D2-146[»]
3IC2X-ray2.40B/D2-147[»]
3KMFneutron diffraction2.00C/G2-147[»]
3NL7X-ray1.80B2-147[»]
3NMMX-ray1.60B/D2-147[»]
3ODQX-ray3.10B/D2-147[»]
3ONZX-ray2.09B2-147[»]
3OO4X-ray1.90B2-147[»]
3OO5X-ray2.10B2-147[»]
3P5QX-ray2.00B2-147[»]
3QJBX-ray1.80B2-147[»]
3QJCX-ray2.00B2-147[»]
3QJDX-ray1.56B/D2-147[»]
3QJEX-ray1.80B/D2-147[»]
3R5IX-ray2.20B/D2-147[»]
3S65X-ray1.80B/D2-147[»]
3S66X-ray1.40B2-147[»]
3SZKX-ray3.01B/E2-147[»]
3W4UX-ray1.95B/D/F2-147[»]
3WCPX-ray1.94B/D2-147[»]
4FC3X-ray2.26B2-147[»]
4HHBX-ray1.74B/D2-147[»]
4IJ2X-ray4.24B/D2-147[»]
4L7YX-ray1.80B/D2-147[»]
4MQCX-ray2.20B2-147[»]
4MQGX-ray1.68B2-147[»]
4MQHX-ray2.50B2-147[»]
4MQIX-ray1.92B2-147[»]
6HBWX-ray2.00B/D2-147[»]
ProteinModelPortalP68871.
SMRP68871. Positions 2-147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109293. 21 interactions.
IntActP68871. 6 interactions.
MINTMINT-5000306.

Chemistry

ChEMBLCHEMBL4331.
DrugBankDB00893. Iron Dextran.

PTM databases

PhosphoSiteP68871.

Polymorphism databases

DMDM56749856.

2D gel databases

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

Proteomic databases

PaxDbP68871.
PeptideAtlasP68871.
PRIDEP68871.

Protocols and materials databases

DNASU3043.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335295; ENSP00000333994; ENSG00000244734.
GeneID3043.
KEGGhsa:3043.
UCSCuc001mae.1. human.

Organism-specific databases

CTD3043.
GeneCardsGC11M005257.
HGNCHGNC:4827. HBB.
HPACAB009526.
HPA043234.
MIM140700. phenotype.
141900. gene+phenotype.
603902. phenotype.
603903. phenotype.
613985. phenotype.
neXtProtNX_P68871.
Orphanet330041. 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.
PharmGKBPA29202.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG269316.
HOVERGENHBG009709.
InParanoidP68871.
KOK13823.
OMADAVMNNP.
OrthoDBEOG7B8S5H.
TreeFamTF333268.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP68871.
BgeeP68871.
GenevestigatorP68871.

Family and domain databases

Gene3D1.10.490.10. 1 hit.
InterProIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002337. Haemoglobin_b.
[Graphical view]
PfamPF00042. Globin. 1 hit.
[Graphical view]
PRINTSPR00814. BETAHAEM.
SUPFAMSSF46458. SSF46458. 1 hit.
PROSITEPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHBB. human.
EvolutionaryTraceP68871.
GeneWikiHBB.
GenomeRNAi3043.
NextBio12048.
PMAP-CutDBP68871.
PROP68871.
SOURCESearch...

Entry information

Entry nameHBB_HUMAN
AccessionPrimary (citable) accession number: P68871
Secondary accession number(s): A4GX73 expand/collapse secondary AC list , B2ZUE0, P02023, Q13852, Q14481, Q14510, Q45KT0, Q549N7, Q6FI08, Q6R7N2, Q8IZI1, Q9BX96, Q9UCD6, Q9UCP8, Q9UCP9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM