P68871 (HBB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hemoglobin subunit beta

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

Cleaved into the following chain:

1. LVV-hemorphin-7

Gene names

Name:

HBB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in oxygen transport from the lung to the various peripheral tissues. Ref.34 LVV-hemorphin-7 potentiates the activity of bradykinin, causing a decrease in blood pressure. Ref.34
Subunit structure	Heterotetramer of two alpha chains and two beta chains in adult hemoglobin A (HbA).
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. 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.
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.50 Ref.124 Ref.125 Ref.128 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.51 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 process	Oxygen transport Transport
Coding sequence diversity	Polymorphism
Disease	Congenital dyserythropoietic anemia Disease mutation Hereditary hemolytic anemia
Ligand	Heme Iron Metal-binding Pyruvate
Molecular function	Hypotensive agent Vasoactive
PTM	Acetylation Glycation Glycoprotein S-nitrosylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	bicarbonate 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 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_component	endocytic vesicle lumen Traceable author statement. Source: Reactome extracellular region Traceable author statement. Source: Reactome haptoglobin-hemoglobin complex Inferred from direct assay PubMed 19740759. Source: BHF-UCL hemoglobin complex Non-traceable author statement Ref.33Ref.70. Source: UniProtKB
Molecular_function	heme 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 PubMed 11747442. Source: UniProtKB oxygen transporter activity Non-traceable author statement PubMed 11747442Ref.70. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HBA1	P69905	19	EBI-715554,EBI-714680

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.20

Chain

2 – 147

146

Hemoglobin subunit beta

PRO_0000052976

Peptide

33 – 42

10

LVV-hemorphin-7 Ref.21 Ref.22

PRO_0000296641

Sites

Metal binding

64

1

Iron (heme distal ligand)

Metal binding

93

1

Iron (heme proximal ligand)

Binding site

2

1

2,3-bisphosphoglycerate; via amino nitrogen

Binding site

3

1

2,3-bisphosphoglycerate

Binding site

83

1

2,3-bisphosphoglycerate

Binding site

144

1

2,3-bisphosphoglycerate

Site

60

1

Not glycated

Site

83

1

Not glycated

Site

96

1

Not glycated

Site

142

1

Susceptible to oxidation; associated with variant Atlanta, variant non-spherocytic haemolytic anemia and variant Christchurch

Site

145

1

Aspirin-acetylated lysine

Amino acid modifications

Modified residue

2

1

N-acetylalanine; in variant Raleigh

Modified residue

2

1

N-acetylvaline By similarity

Modified residue

2

1

N-pyruvate 2-iminyl-valine; in Hb A1b

Modified residue

94

1

S-nitrosocysteine Ref.31 Ref.32

Glycosylation

2

1

N-linked (Glc) (glycation); in Hb A1c Ref.27

Glycosylation

9

1

N-linked (Glc) (glycation) Ref.28

Glycosylation

18

1

N-linked (Glc) (glycation) Ref.28

Glycosylation

67

1

N-linked (Glc) (glycation) Ref.28

Glycosylation

121

1

N-linked (Glc) (glycation) Ref.28

Glycosylation

145

1

N-linked (Glc) (glycation) Ref.28

Natural variations

Natural variant

2

1

V → A in Raleigh; O(2) affinity down.
Corresponds to variant rs33949930 [ dbSNP | Ensembl ].

VAR_002856

Natural variant

3

1

H → L in Graz. Ref.75
Corresponds to variant rs35906307 [ dbSNP | Ensembl ].

VAR_002857

Natural variant

3

1

H → Q in Okayama; O(2) affinity up.
Corresponds to variant rs713040 [ dbSNP | Ensembl ].

VAR_002858

Natural variant

3

1

H → R in Deer Lodge; O(2) affinity up.
Corresponds to variant rs33983205 [ dbSNP | Ensembl ].

VAR_002859

Natural variant

3

1

H → Y in Fukuoka.
Corresponds to variant rs35906307 [ dbSNP | Ensembl ].

VAR_002860

Natural variant

6

1

P → R in Warwickshire.
Corresponds to variant rs34769005 [ dbSNP | Ensembl ].

VAR_002861

Natural variant

7

1

E → A in G-Makassar.

VAR_002862

Natural variant

7

1

E → K in C. Ref.3 Ref.47

VAR_002864

Natural variant

7

1

E → Q in Machida.
Corresponds to variant rs33930165 [ dbSNP | Ensembl ].

VAR_002865

Natural variant

7

1

E → V in S; sickle cell anemia. Ref.10 Ref.37
Corresponds to variant rs334 [ dbSNP | Ensembl ].

VAR_002863

Natural variant

8

1

E → G in G-San Jose; mildly unstable.
Corresponds to variant rs34948328 [ dbSNP | Ensembl ].

VAR_002866

Natural variant

8

1

E → K in G-Siriraj.
Corresponds to variant rs34948328 [ dbSNP | Ensembl ].

VAR_002867

Natural variant

9

1

K → E in N-Timone. Ref.100
Corresponds to variant rs33932981 [ dbSNP | Ensembl ].

VAR_002868

Natural variant

9

1

K → Q in J-Luhe.
Corresponds to variant rs33926764 [ dbSNP | Ensembl ].

VAR_002869

Natural variant

9

1

K → T in Rio Grande. Ref.113

VAR_002870

Natural variant

10

1

S → C in Porto Alegre; O(2) affinity up.
Corresponds to variant rs33918131 [ dbSNP | Ensembl ].

VAR_002871

Natural variant

11

1

A → D in Ankara. Ref.54
Corresponds to variant rs33947457 [ dbSNP | Ensembl ].

VAR_002872

Natural variant

11

1

A → V in Iraq-Halabja. Ref.129

VAR_025393

Natural variant

12

1

V → D in Windsor; O(2) affinity up; unstable. Ref.121
Corresponds to variant rs33974228 [ dbSNP | Ensembl ].

VAR_002873

Natural variant

12

1

V → I in Hamilton.

VAR_002874

Natural variant

14

1

A → D in J-Lens.
Corresponds to variant rs35203747 [ dbSNP | Ensembl ].

VAR_002875

Natural variant

15

1

L → P in Saki; unstable.

VAR_002876

Natural variant

15

1

L → R in Soegn; unstable.
Corresponds to variant rs33935445 [ dbSNP | Ensembl ].

VAR_002877

Natural variant

16

1

W → G in Randwick; unstable. Ref.112
Corresponds to variant rs33946157 [ dbSNP | Ensembl ].

VAR_002878

Natural variant

16

1

W → R in Belfast; O(2) affinity up; unstable.
Corresponds to variant rs33946157 [ dbSNP | Ensembl ].

VAR_002879

Natural variant

17

1

G → D in J-Baltimore/J-Trinidad/J-Ireland/J-Georgia/N-New Haven.

VAR_002880

Natural variant

17

1

G → R in D-Bushman.

VAR_002881

Natural variant

18

1

K → E in Nagasaki.
Corresponds to variant rs33986703 [ dbSNP | Ensembl ].

VAR_002882

Natural variant

18

1

K → N in J-Amiens.
Corresponds to variant rs36006214 [ dbSNP | Ensembl ].

VAR_002883

Natural variant

18

1

K → Q in Nikosia.
Corresponds to variant rs33986703 [ dbSNP | Ensembl ].

VAR_002884

Natural variant

19

1

V → M in Baden; slightly unstable.
Corresponds to variant rs35802118 [ dbSNP | Ensembl ].

VAR_002885

Natural variant

20

1

N → D in Alamo.
Corresponds to variant rs34866629 [ dbSNP | Ensembl ].

VAR_002886

Natural variant

20

1

N → K in D-Ouleh RABAH.

VAR_002887

Natural variant

20

1

N → S in Malay.
Corresponds to variant rs33972047 [ dbSNP | Ensembl ].

VAR_002888

Natural variant

21

1

V → M in Olympia; O(2) affinity up.
Corresponds to variant rs35890959 [ dbSNP | Ensembl ].

VAR_002889

Natural variant

22

1

D → G in Connecticut; O(2) affinity down.
Corresponds to variant rs33977536 [ dbSNP | Ensembl ].

VAR_002890

Natural variant

22

1

D → H in Karlskoga. Ref.86
Corresponds to variant rs33950093 [ dbSNP | Ensembl ].

VAR_002892

Natural variant

22

1

D → N in Cocody.

VAR_002891

Natural variant

22

1

D → Y in Yusa.

VAR_002893

Natural variant

23

1

E → A in G-Coushatta/G-Saskatoon/G-Taegu/Hsin Chu.
Corresponds to variant rs33936254 [ dbSNP | Ensembl ].

VAR_002894

Natural variant

23

1

E → G in G-Taipei.

VAR_002895

Natural variant

23

1

E → K in E-Saskatoon; unstable.

VAR_002896

Natural variant

23

1

E → Q in D-Iran.

VAR_002897

Natural variant

23

1

E → V in D-Granada.

VAR_002898

Natural variant

24

1

V → D in Strasbourg; O(2) affinity up.

VAR_002899

Natural variant

24

1

V → F in Palmerston North; O(2) affinity up; unstable. Ref.106

VAR_002900

Natural variant

24

1

V → G in Miyashiro; O(2) affinity up; unstable. Ref.97

VAR_002901

Natural variant

24

1

Missing in Freiburg. Ref.48
Corresponds to variant rs34160180 [ dbSNP | Ensembl ].

VAR_069169

Natural variant

25

1

G → D in Moscva; O(2) affinity down; unstable.

VAR_002902

Natural variant

25

1

G → R in Riverdale-Bronx; O(2) affinity up; unstable.

VAR_002903

Natural variant

25

1

G → V in Savannah; unstable.

VAR_002904

Natural variant

26

1

G → D in J-Auckland; unstable; O(2) affinity down. Ref.56

VAR_002905

Natural variant

26

1

G → R in G-Taiwan Ami.

VAR_002906

Natural variant

27

1

E → K in E. Ref.133 Ref.136

VAR_002907

Natural variant

27

1

E → V in Henri Mondor; slightly unstable.

VAR_002908

Natural variant

28

1

A → D in Volga/Drenthe; unstable.

VAR_002909

Natural variant

28

1

A → S in Knossos. Ref.87

VAR_002910

Natural variant

28

1

A → V in Grange-blanche; O(2) affinity up. Ref.74

VAR_002911

Natural variant

29

1

L → P in Genova/Hyogo; unstable.

VAR_002912

Natural variant

29

1

L → Q in St Louis. Ref.50

VAR_035236

Natural variant

30

1

G → D in Lufkin; unstable.

VAR_002913

Natural variant

31

1

R → S in Tacoma; unstable.

VAR_002914

Natural variant

32

1

L → P in Yokohama; unstable. Ref.123

VAR_002915

Natural variant

33

1

L → R in Castilla; unstable.

VAR_002916

Natural variant

33

1

L → V in Muscat; slightly unstable. Ref.99

VAR_002917

Natural variant

35

1

V → D in Santander; unstable. Ref.134

VAR_025394

Natural variant

35

1

V → F in Pitie-Salpetriere; O(2) affinity up.

VAR_002918

Natural variant

35

1

V → L in Nantes; increased oxygen affinity. Ref.135

VAR_025395

Natural variant

36

1

Y → F in Philly; O(2) affinity up; unstable.

VAR_002919

Natural variant

37

1

P → R in Sunnybrook.

VAR_002920

Natural variant

37

1

P → S in North Chicago; O(2) affinity up. Ref.103

VAR_002921

Natural variant

37

1

P → T in Linkoping/Finlandia; O(2) affinity up. Ref.94

VAR_002922

Natural variant

38

1

W → G in Howick. Ref.45 Ref.80

VAR_002923

Natural variant

38

1

W → R in Rothschild; O(2) affinity down. Ref.41

VAR_002925

Natural variant

38

1

W → S in Hirose; O(2) affinity up.

VAR_002924

Natural variant

39

1

T → N in Hinwil; O(2) affinity up. Ref.79

VAR_002926

Natural variant

40

1

Q → E in Vaasa; unstable.

VAR_002927

Natural variant

40

1

Q → K in Alabama. Ref.49

VAR_002928

Natural variant

40

1

Q → R in Tianshui.

VAR_002929

Natural variant

42

1

F → Y in Mequon.

VAR_002930

Natural variant

42

1

Missing in Bruxelles. Ref.125

VAR_035237

Natural variant

43

1

F → L in Louisville; unstable. Ref.6

VAR_002931

Natural variant

43

1

F → S in Hammersmith. Ref.124

VAR_035239

Natural variant

43

1

Missing in Bruxelles. Ref.125

VAR_035238

Natural variant

44

1

E → Q in Hoshida/Chaya.

VAR_002932

Natural variant

45

1

S → C in Mississippi.

VAR_002933

Natural variant

46

1

F → S in Cheverly; unstable.

VAR_002934

Natural variant

47

1

G → E in K-Ibadan.

VAR_002935

Natural variant

48

1

D → A in Avicenna.

VAR_002936

Natural variant

48

1

D → G in Gavello.

VAR_002937

Natural variant

48

1

D → Y in Maputo. Ref.95

VAR_002938

Natural variant

49

1

L → P in Bab-Saadoum; slightly unstable.

VAR_002939

Natural variant

50

1

S → F in Las Palmas; slightly unstable. Ref.13 Ref.93

VAR_002940

Natural variant

51

1

T → K in Edmonton.

VAR_002941

Natural variant

52

1

P → R in Willamette; O(2) affinity up; unstable.

VAR_002942

Natural variant

53

1

D → A in Ocho Rios.

VAR_002943

Natural variant

53

1

D → H in Summer Hill.

VAR_002944

Natural variant

55

1

V → D in Jacksonville; O(2) affinity up; unstable. Ref.84

VAR_002945

Natural variant

56

1

M → K in Matera; unstable. Ref.96

VAR_002946

Natural variant

57

1

G → R in Hamadan.

VAR_002947

Natural variant

58

1

N → K in G-ferrara; unstable.

VAR_002948

Natural variant

59

1

P → R in Dhofar/Yukuhashi.

VAR_002949

Natural variant

60

1

K → E in I-High Wycombe.

VAR_002950

Natural variant

61

1

V → A in Collingwood; unstable.

VAR_002951

Natural variant

62

1

K → E in N-Seatlle.

VAR_002952

Natural variant

62

1

K → M in Bologna; O(2) affinity down.

VAR_002953

Natural variant

62

1

K → N in Hikari.

VAR_002954

Natural variant

63

1

A → D in J-Europa. Ref.72

VAR_002955

Natural variant

63

1

A → P in Duarte; unstable.

VAR_002956

Natural variant

64

1

H → Y in M-Saskatoon; O(2) affinity up. Ref.116

VAR_002957

Natural variant

66

1

K → M in J-Antakya. Ref.55

VAR_002958

Natural variant

66

1

K → N in J-Sicilia. Ref.118

VAR_002959

Natural variant

66

1

K → Q in J-Cairo. Ref.61

VAR_002960

Natural variant

67

1

K → T in Chico; O(2) affinity down.

VAR_002961

Natural variant

68

1

V → A in Sydney; unstable.

VAR_002962

Natural variant

68

1

V → D in Bristol. Ref.128

VAR_035240

Natural variant

68

1

V → G in non-spherocytic haemolytic anemia; Manukau. Ref.127
Corresponds to variant rs33918343 [ dbSNP | Ensembl ].

VAR_040060

Natural variant

68

1

V → M in Alesha; unstable. Ref.52

VAR_002963

Natural variant

69

1

L → H in Brisbane; O(2) affinity up. Ref.59

VAR_002964

Natural variant

69

1

L → P in Mizuho; unstable. Ref.98

VAR_002965

Natural variant

70

1

G → D in Rambam. Ref.111

VAR_002966

Natural variant

70

1

G → R in Kenitra.

VAR_002967

Natural variant

70

1

G → S in City of Hope. Ref.64

VAR_002968

Natural variant

71

1

A → D in Seattle; O(2) affinity down; unstable.

VAR_002969

Natural variant

72

1

F → S in Christchurch; unstable.

VAR_002970

Natural variant

74

1

D → G in Tilburg; O(2) affinity down.

VAR_002971

Natural variant

74

1

D → V in Mobile; O(2) affinity down.

VAR_002972

Natural variant

74

1

D → Y in Vancouver; O(2) affinity down.

VAR_002973

Natural variant

75

1

G → R in Aalborg; unstable. Ref.42

VAR_002974

Natural variant

75

1

G → V in Bushwick; unstable.

VAR_002975

Natural variant

76

1

L → P in Atlanta; unstable. Ref.13

VAR_002976

Natural variant

76

1

L → R in Pasadena; O(2) affinity up; unstable.

VAR_002977

Natural variant

77

1

A → D in J-Chicago.

VAR_002978

Natural variant

78

1

H → D in J-Iran.

VAR_002979

Natural variant

78

1

H → R in Costa Rica. Ref.66

VAR_002980

Natural variant

78

1

H → Y in Fukuyama.

VAR_002981

Natural variant

79

1

L → R in Quin-hai. Ref.110

VAR_002982

Natural variant

80

1

D → Y in Tampa.

VAR_002983

Natural variant

81

1

N → K in G-Szuhu/Gifu.

VAR_002984

Natural variant

82

1

L → H in La Roche-sur-Yon; unstable and O(2) affinity up. Ref.92

VAR_012663

Natural variant

82

1

L → R in Baylor; unstable.

VAR_002985

Natural variant

82

1

L → V.
Corresponds to variant rs11549406 [ dbSNP | Ensembl ].

VAR_049273

Natural variant

83

1

K → M in Helsinki; O(2) affinity up. Ref.76

VAR_002986

Natural variant

83

1

K → N in Providence.

VAR_012664

Natural variant

84

1

G → D in Pyrgos. Ref.133

VAR_025396

Natural variant

84

1

G → R in Muskegon.

VAR_002987

Natural variant

85

1

T → I in Kofu. Ref.89

VAR_002988

Natural variant

87

1

A → D in Olomouc; O(2) affinity up. Ref.105

VAR_002989

Natural variant

88

1

T → I in Quebec-Chori.

VAR_002990

Natural variant

88

1

T → K in D-Ibadan.

VAR_002991

Natural variant

88

1

T → P in Valletta.

VAR_002992

Natural variant

89

1

L → P in Santa Ana; unstable.

VAR_002993

Natural variant

89

1

L → R in Boras; unstable.

VAR_002994

Natural variant

90

1

S → N in Creteil; O(2) affinity up.

VAR_002995

Natural variant

90

1

S → R in Vanderbilt; O(2) affinity up.

VAR_002996

Natural variant

91

1

E → D in Pierre-Benite; O(2) affinity up. Ref.107

VAR_002997

Natural variant

91

1

E → K in Agenogi; O(2) affinity down.

VAR_002998

Natural variant

92

1

L → P in Sabine; unstable.

VAR_002999

Natural variant

92

1

L → R in Caribbean; O(2) affinity down; unstable. Ref.63

VAR_003000

Natural variant

93

1

H → D in J-Altgelds Gardens; unstable. Ref.53

VAR_003001

Natural variant

93

1

H → N in Isehara; unstable. Ref.82

VAR_003002

Natural variant

93

1

H → P in Newcastle and Duino; associated with S-104 in Duino; unstable. Ref.69

VAR_003003

Natural variant

93

1

H → Q in Istambul; O(2) affinity up; unstable. Ref.83

VAR_003004

Natural variant

94

1

C → R in Okazaki; O(2) affinity up; unstable.

VAR_003005

Natural variant

95

1

D → G in Chandigarh.

VAR_003006

Natural variant

95

1

D → H in Barcelona; O(2) affinity up.

VAR_003007

Natural variant

95

1

D → N in Bunbury; O(2) affinity up. Ref.60

VAR_003008

Natural variant

96

1

K → M in J-Cordoba.

VAR_003009

Natural variant

96

1

K → N in Detroit.

VAR_003010

Natural variant

97

1

L → P in Debrousse; unstable; O(2) affinity up. Ref.67

VAR_003011

Natural variant

97

1

L → V in Regina; O(2) affinity up.

VAR_003012

Natural variant

98

1

H → L in Wood; O(2) affinity up.

VAR_003013

Natural variant

98

1

H → P in Nagoya; O(2) affinity up; unstable. Ref.101

VAR_003014

Natural variant

98

1

H → Q in Malmoe; O(2) affinity up.

VAR_003015

Natural variant

98

1

H → Y in Moriguchi.

VAR_003016

Natural variant

99

1

V → G in Nottingham; unstable.

VAR_003017

Natural variant

100

1

D → E in Coimbra; O(2) affinity up. Ref.65

VAR_003018

Natural variant

101

1

P → L in Brigham; O(2) affinity up.

VAR_003019

Natural variant

101

1

P → R in New Mexico.

VAR_003020

Natural variant

102

1

E → D in Potomac; O(2) affinity up.

VAR_003021

Natural variant

102

1

E → G in Alberta; O(2) affinity up.

VAR_003022

Natural variant

102

1

E → K in British Columbia; O(2) affinity up.

VAR_003023

Natural variant

102

1

E → Q in Rush; unstable. Ref.114

VAR_003024

Natural variant

103

1

N → S in Beth Israel; O(2) affinity down; unstable.

VAR_003025

Natural variant

103

1

N → Y in St Mande; O(2) affinity down. Ref.120

VAR_003026

Natural variant

104

1

F → L in Heathrow; O(2) affinity up.

VAR_003027

Natural variant

105

1

R → S in Camperdown and Duino; associated with P-92 in Duino; unstable. Ref.62 Ref.69

VAR_003028

Natural variant

105

1

R → T in Sherwood Forest.

VAR_003029

Natural variant

108

1

G → R in Burke; O(2) affinity down; unstable. Ref.23

VAR_003030

Natural variant

109

1

N → K in Presbyterian; O(2) affinity down; unstable. Ref.108

VAR_003031

Natural variant

110

1

V → M in San Diego; O(2) affinity up.

VAR_003032

Natural variant

111

1

L → P in Showa-Yakushiji.

VAR_003033

Natural variant

112

1

V → A in Stanmore; O(2) affinity down; unstable. Ref.119

VAR_003034

Natural variant

113

1

C → F in Canterbury. Ref.132

VAR_025397

Natural variant

113

1

C → R in Indianapolis. Ref.5 Ref.81

VAR_003035

Natural variant

113

1

C → Y in Yahata. Ref.122

VAR_003036

Natural variant

115

1

L → M in Zengcheng. Ref.126

VAR_010144

Natural variant

115

1

L → P in Durham-N.C./Brescia; causes beta-thalassemia. Ref.7 Ref.70 Ref.71

VAR_010145

Natural variant

116

1

A → D in Hradec Kralove; unstable; causes severe beta-thalassemia. Ref.90

VAR_003037

Natural variant

116

1

A → P in Madrid; unstable.

VAR_003038

Natural variant

117

1

H → L in Vexin; increased oxygen affinity. Ref.135

VAR_025398

Natural variant

117

1

H → Q in Hafnia.

VAR_003039

Natural variant

118

1

H → P in Saitama; unstable. Ref.115

VAR_003040

Natural variant

118

1

H → R in P-Galveston.

VAR_003041

Natural variant

118

1

H → Y in Tsukumi. Ref.131

VAR_025399

Natural variant

120

1

G → A in Iowa.

VAR_003042

Natural variant

121

1

K → E in Hijiyama.

VAR_003043

Natural variant

121

1

K → I in Jianghua. Ref.85

VAR_003044

Natural variant

121

1

K → Q in Takamatsu.

VAR_003045

Natural variant

122

1

E → A in D-Neath. Ref.102

VAR_003046

Natural variant

122

1

E → G in St Francis.

VAR_003047

Natural variant

122

1

E → K in O-Arab.

VAR_003049

Natural variant

122

1

E → Q in D-Los Angeles/D-Punjab/D-Portugal/D-Chicago/D-Oak Ridge.

VAR_003048

Natural variant

122

1

E → V in D-Camperdown/Beograd.

VAR_003050

Natural variant

124

1

T → I in Villejuif; asymptomatic variant. Ref.130

VAR_003051

Natural variant

125

1

P → Q in Ty Gard; O(2) affinity up. Ref.8

VAR_003053

Natural variant

125

1

P → R in Khartoum; unstable.

VAR_003052

Natural variant

125

1

P → S in Tunis.

VAR_003054

Natural variant

127

1

V → A in Beirut.

VAR_003055

Natural variant

127

1

V → E in Hofu; unstable.

VAR_003057

Natural variant

127

1

V → G in Dhonburi/Neapolis; unstable; beta-thalassemia. Ref.68

VAR_003056

Natural variant

128

1

Q → E in Complutense. Ref.55

VAR_003058

Natural variant

128

1

Q → K in Brest; unstable. Ref.58

VAR_003059

Natural variant

129

1

A → D in J-Guantanamo; unstable.

VAR_003060

Natural variant

130

1

A → P in Crete; O(2) affinity up; unstable.

VAR_003061

Natural variant

130

1

A → V in La Desirade; O(2) affinity down; unstable. Ref.91

VAR_003062

Natural variant

131

1

Y → D in Wien; unstable.

VAR_003063

Natural variant

131

1

Y → S in Nevers.

VAR_003064

Natural variant

132

1

Q → E in Camden/Tokuchi/Motown.

VAR_003065

Natural variant

132

1

Q → K in Shelby/Leslie/Deaconess; unstable. Ref.117

VAR_003066

Natural variant

132

1

Q → P in Shangai; unstable.

VAR_003067

Natural variant

132

1

Q → R in Sarrebourg; unstable.

VAR_003068

Natural variant

133

1

K → N in Yamagata; O(2) affinity down.

VAR_003069

Natural variant

133

1

K → Q in K-Woolwich.

VAR_003070

Natural variant

134

1

V → L in Extredemura.

VAR_003071

Natural variant

135

1

V → E in North Shore-Caracas; unstable. Ref.104

VAR_003072

Natural variant

136

1

A → E in Beckman; O(2) affinity down; unstable.

VAR_003073

Natural variant

136

1

A → P in Altdorf; O(2) affinity up; unstable.

VAR_003074

Natural variant

137

1

G → D in Hope; O(2) affinity down; unstable.

VAR_003075

Natural variant

139

1

A → P in Brockton; unstable.

VAR_003076

Natural variant

140

1

N → D in Geelong; unstable. Ref.73

VAR_003077

Natural variant

140

1

N → K in Hinsdale; O(2) affinity down. Ref.78

VAR_003078

Natural variant

140

1

N → S in S-Wake; associated with V-6. Ref.10

VAR_025335

Natural variant

140

1

N → Y in Aurora; O(2) affinity up. Ref.57

VAR_003079

Natural variant

141

1

A → D in Himeji; unstable; O(2) affinity down. Ref.77

VAR_003080

Natural variant

141

1

A → T in St Jacques: O(2) affinity up.

VAR_003081

Natural variant

141

1

A → V in Puttelange; polycythemia; O(2) affinity up. Ref.109

VAR_003082

Natural variant

142

1

L → R in Olmsted; unstable.

VAR_003083

Natural variant

143

1

A → D in Ohio; O(2) affinity up.

VAR_003084

Natural variant

144

1

H → D in Rancho Mirage.

VAR_003085

Natural variant

144

1

H → P in Syracuse; O(2) affinity up.

VAR_003087

Natural variant

144

1

H → Q in Little Rock; O(2) affinity up.

VAR_003086

Natural variant

144

1

H → R in Abruzzo; O(2) affinity up.

VAR_003088

Natural variant

145

1

K → E in Mito; O(2) affinity up.

VAR_003089

Natural variant

146

1

Y → C in Rainier; O(2) affinity up.

VAR_003090

Natural variant

146

1

Y → H in Bethesda; O(2) affinity up.

VAR_003091

Natural variant

147

1

H → D in Hiroshima; O(2) affinity up.

VAR_003092

Natural variant

147

1

H → L in Cowtown; O(2) affinity up.

VAR_003093

Natural variant

147

1

H → P in York; O(2) affinity up.

VAR_003094

Natural variant

147

1

H → Q in Kodaira; O(2) affinity up. Ref.88

VAR_003095

Experimental info

Sequence conflict

26

1

Missing in ACD39349. Ref.15

Sequence conflict

42

1

F → L in AAR96398. Ref.13

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

147

Helix Strand Turn

Details...

Helix

6 – 17

12

Helix

21 – 35

15

Helix

37 – 42

6

Helix

44 – 46

3

Helix

52 – 57

6

Helix

59 – 75

17

Turn

78 – 80

3

Helix

82 – 95

14

Helix

102 – 119

18

Helix

120 – 122

3

Helix

125 – 143

19

Helix

144 – 146

3

Sequences

	Sequence		Length	Mass (Da)
	P68871 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: A31F6D621C6556A1	FASTA	147	15,998
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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-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]	"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.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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].
[36]	"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.
[37]	"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.
[38]	"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.
[39]	"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.
[40]	"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.
[41]	"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.
[42]	"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.
[43]	"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.
[44]	"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).
[45]	"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.
[46]	"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.
[47]	"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.
[48]	"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.
[49]	"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.
[50]	"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.
[51]	"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.
[52]	"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.
[53]	"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.
[54]	"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.
[55]	"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.
[56]	"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.
[57]	"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.
[58]	"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.
[59]	"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.
[60]	"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.
[61]	"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.
[62]	"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.
[63]	"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.
[64]	"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.
[65]	"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.
[66]	"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.
[67]	"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.
[68]	"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.
[69]	"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.
[70]	"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.
[71]	"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.
[72]	"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.
[73]	"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.
[74]	"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.
[75]	"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.
[76]	"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.
[77]	"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.
[78]	"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.
[79]	"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.
[80]	"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.
[81]	"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.
[82]	"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.
[83]	"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.
[84]	"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.
[85]	"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.
[86]	"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.
[87]	"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.
[88]	"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.
[89]	"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.
[90]	"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.
[91]	"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.
[92]	"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.
[93]	"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.
[94]	"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.
[95]	"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.
[96]	"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.
[97]	"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.
[98]	"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.
[99]	"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.
[100]	"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.
[101]	"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.
[102]	"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.
[103]	"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.
[104]	"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.
[105]	"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.
[106]	"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.
[107]	"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.
[108]	"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.
[109]	"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.
[110]	"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.
[111]	"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.
[112]	"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.
[113]	"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.
[114]	"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.
[115]	"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.
[116]	"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.
[117]	"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.
[118]	"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.
[119]	"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.
[120]	"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.
[121]	"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.
[122]	"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.
[123]	"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.
[124]	"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.
[125]	"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.
[126]	"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.
[127]	"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.
[128]	"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.
[129]	"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.
[130]	"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.
[131]	"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.
[132]	"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.
[133]	"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.
[134]	"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.
[135]	"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.
[136]	"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.

IPI

IPI00654755.

PIR

HBHU. A53136.

RefSeq

NP_000509.1. NM_000518.4.

UniGene

Hs.523443.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A00	X-ray	2.00	B/D	3-147	[»]
1A01	X-ray	1.80	B/D	3-147	[»]
1A0U	X-ray	2.14	B/D	3-147	[»]
1A0Z	X-ray	2.00	B/D	3-147	[»]
1A3N	X-ray	1.80	B/D	2-147	[»]
1A3O	X-ray	1.80	B/D	2-147	[»]
1ABW	X-ray	2.00	B/D	3-147	[»]
1ABY	X-ray	2.60	B/D	3-147	[»]
1AJ9	X-ray	2.20	B	2-147	[»]
1B86	X-ray	2.50	B/D	2-147	[»]
1BAB	X-ray	1.50	B/D	2-147	[»]
1BBB	X-ray	1.70	B/D	2-147	[»]
1BIJ	X-ray	2.30	B/D	2-147	[»]
1BUW	X-ray	1.90	B/D	2-147	[»]
1BZ0	X-ray	1.50	B/D	2-147	[»]
1BZ1	X-ray	1.59	B/D	2-147	[»]
1BZZ	X-ray	1.59	B/D	2-147	[»]
1C7B	X-ray	1.80	B/D	3-147	[»]
1C7C	X-ray	1.80	B/D	3-147	[»]
1C7D	X-ray	1.80	B/D	3-147	[»]
1CBL	X-ray	1.80	A/B/C/D	2-147	[»]
1CBM	X-ray	1.74	A/B/C/D	1-147	[»]
1CH4	X-ray	2.50	A/B/C/D	2-107	[»]
1CLS	X-ray	1.90	B/D	1-147	[»]
1CMY	X-ray	3.00	B/D	1-147	[»]
1COH	X-ray	2.90	B/D	1-147	[»]
1DKE	X-ray	2.10	B/D	1-147	[»]
1DXT	X-ray	1.70	B/D	1-147	[»]
1DXU	X-ray	1.70	B/D	3-147	[»]
1DXV	X-ray	1.70	B/D	3-147	[»]
1FN3	X-ray	2.48	B/D	2-147	[»]
1G9V	X-ray	1.85	B/D	2-147	[»]
1GBU	X-ray	1.80	B/D	2-147	[»]
1GBV	X-ray	2.00	B/D	2-147	[»]
1GLI	X-ray	2.50	B/D	3-147	[»]
1GZX	X-ray	2.10	B/D	2-147	[»]
1HAB	X-ray	2.30	B/D	2-146	[»]
1HAC	X-ray	2.60	B/D	2-146	[»]
1HBA	X-ray	2.10	B/D	2-147	[»]
1HBB	X-ray	1.90	B/D	2-147	[»]
1HBS	X-ray	3.00	B/D/F/H	1-147	[»]
1HCO	X-ray	2.70	B	2-147	[»]
1HDB	X-ray	2.20	B/D	1-147	[»]
1HGA	X-ray	2.10	B/D	1-147	[»]
1HGB	X-ray	2.10	B/D	1-147	[»]
1HGC	X-ray	2.10	B/D	1-147	[»]
1HHO	X-ray	2.10	B	1-147	[»]
1IRD	X-ray	1.25	B	1-147	[»]
1J3Y	X-ray	1.55	B/D/F/H	1-147	[»]
1J3Z	X-ray	1.60	B/D/F/H	1-147	[»]
1J40	X-ray	1.45	B/D/F/H	1-147	[»]
1J41	X-ray	1.45	B/D/F/H	1-147	[»]
1J7S	X-ray	2.20	B/D	3-147	[»]
1J7W	X-ray	2.00	B/D	3-147	[»]
1J7Y	X-ray	1.70	B/D	3-147	[»]
1JY7	X-ray	3.20	B/D/Q/S/V/X	1-147	[»]
1K0Y	X-ray	1.87	B/D	1-147	[»]
1K1K	X-ray	2.00	B	1-147	[»]
1KD2	X-ray	1.87	B/D	1-147	[»]
1LFL	X-ray	2.70	B/D/Q/S	1-147	[»]
1LFQ	X-ray	2.60	B	1-147	[»]
1LFT	X-ray	2.60	B	1-147	[»]
1LFV	X-ray	2.80	B	1-147	[»]
1LFY	X-ray	3.30	B	1-147	[»]
1LFZ	X-ray	3.10	B	1-147	[»]
1LJW	X-ray	2.16	B	1-147	[»]
1M9P	X-ray	2.10	B/D	1-147	[»]
1MKO	X-ray	2.18	B/D	1-147	[»]
1NEJ	X-ray	2.10	B/D	1-147	[»]
1NIH	X-ray	2.60	B/D	1-147	[»]
1NQP	X-ray	1.73	B/D	1-147	[»]
1O1I	X-ray	2.30	B	1-147	[»]
1O1J	X-ray	1.90	B/D	1-147	[»]
1O1K	X-ray	2.00	B/D	1-147	[»]
1O1L	X-ray	1.80	B/D	1-147	[»]
1O1M	X-ray	1.85	B/D	1-147	[»]
1O1N	X-ray	1.80	B/D	1-147	[»]
1O1O	X-ray	1.80	B/D	1-147	[»]
1O1P	X-ray	1.80	B/D	1-147	[»]
1QI8	X-ray	1.80	B/D	3-147	[»]
1QSH	X-ray	1.70	B/D	1-147	[»]
1QSI	X-ray	1.70	B/D	1-147	[»]
1QXD	X-ray	2.25	B/D	1-147	[»]
1QXE	X-ray	1.85	B/D	1-147	[»]
1R1X	X-ray	2.15	B	1-147	[»]
1R1Y	X-ray	1.80	B/D	1-147	[»]
1RPS	X-ray	2.11	B/D	1-147	[»]
1RQ3	X-ray	1.91	B/D	1-147	[»]
1RQ4	X-ray	2.11	B/D	1-147	[»]
1RQA	X-ray	2.11	B/D	3-147	[»]
1RVW	X-ray	2.50	B	1-147	[»]
1SDK	X-ray	1.80	B/D	1-147	[»]
1SDL	X-ray	1.80	B/D	1-147	[»]
1THB	X-ray	1.50	B/D	1-147	[»]
1UIW	X-ray	1.50	B/D/F/H	1-147	[»]
1VWT	X-ray	1.90	B/D	1-147	[»]
1XXT	X-ray	1.91	B/D	1-147	[»]
1XY0	X-ray	1.99	B/D	1-147	[»]
1XYE	X-ray	2.13	B/D	1-147	[»]
1XZ2	X-ray	1.90	B/D	1-147	[»]
1XZ4	X-ray	2.00	B/D	1-147	[»]
1XZ5	X-ray	2.11	B/D	1-147	[»]
1XZ7	X-ray	1.90	B/D	1-147	[»]
1XZU	X-ray	2.16	B/D	1-147	[»]
1XZV	X-ray	2.11	B/D	1-147	[»]
1Y09	X-ray	2.25	B/D	1-147	[»]
1Y0A	X-ray	2.22	B/D	1-147	[»]
1Y0C	X-ray	2.30	B/D	1-147	[»]
1Y0D	X-ray	2.10	B/D	1-147	[»]
1Y0T	X-ray	2.14	B/D	3-147	[»]
1Y0W	X-ray	2.14	B/D	3-147	[»]
1Y22	X-ray	2.16	B/D	3-147	[»]
1Y2Z	X-ray	2.07	B/D	3-147	[»]
1Y31	X-ray	2.13	B/D	3-147	[»]
1Y35	X-ray	2.12	B/D	3-147	[»]
1Y45	X-ray	2.00	B/D	3-147	[»]
1Y46	X-ray	2.22	B/D	3-147	[»]
1Y4B	X-ray	2.10	B/D	3-147	[»]
1Y4F	X-ray	2.00	B/D	3-147	[»]
1Y4G	X-ray	1.91	B/D	3-147	[»]
1Y4P	X-ray	1.98	B/D	3-147	[»]
1Y4Q	X-ray	2.11	B/D	3-147	[»]
1Y4R	X-ray	2.22	B/D	3-147	[»]
1Y4V	X-ray	1.84	B/D	3-147	[»]
1Y5F	X-ray	2.14	B/D	3-147	[»]
1Y5J	X-ray	2.03	B/D	3-147	[»]
1Y5K	X-ray	2.20	B/D	3-147	[»]
1Y7C	X-ray	2.10	B/D	3-147	[»]
1Y7D	X-ray	1.90	B/D	3-147	[»]
1Y7G	X-ray	2.10	B/D	3-147	[»]
1Y7Z	X-ray	1.98	B/D	3-147	[»]
1Y83	X-ray	1.90	B/D	3-147	[»]
1Y85	X-ray	2.13	B/D	1-146	[»]
1Y8W	X-ray	2.90	B/D	1-147	[»]
1YDZ	X-ray	3.30	B/D	1-147	[»]
1YE0	X-ray	2.50	B/D	3-147	[»]
1YE1	X-ray	4.50	B/D	3-147	[»]
1YE2	X-ray	1.80	B/D	3-147	[»]
1YEN	X-ray	2.80	B/D	3-147	[»]
1YEO	X-ray	2.22	B/D	3-147	[»]
1YEQ	X-ray	2.75	B/D	3-147	[»]
1YEU	X-ray	2.12	B/D	3-147	[»]
1YEV	X-ray	2.11	B/D	3-147	[»]
1YFF	X-ray	2.40	B/D/F/H	1-147	[»]
1YG5	X-ray	2.70	B/D	3-147	[»]
1YGD	X-ray	2.73	B/D	3-147	[»]
1YGF	X-ray	2.70	B/D	3-147	[»]
1YH9	X-ray	2.20	B/D	1-147	[»]
1YHE	X-ray	2.10	B/D	1-147	[»]
1YHR	X-ray	2.60	B/D	1-147	[»]
1YIE	X-ray	2.40	B/D	3-147	[»]
1YIH	X-ray	2.00	B/D	3-147	[»]
1YVQ	X-ray	1.80	B/D	1-147	[»]
1YVT	X-ray	1.80	B	1-147	[»]
1YZI	X-ray	2.07	B	1-147	[»]
2D5Z	X-ray	1.45	B/D	1-147	[»]
2D60	X-ray	1.70	B/D	1-147	[»]
2DN1	X-ray	1.25	B	1-147	[»]
2DN2	X-ray	1.25	B/D	1-147	[»]
2DN3	X-ray	1.25	B	2-147	[»]
2DXM	neutron diffraction	2.10	B/D	2-147	[»]
2H35	NMR	-	B/D	2-147	[»]
2HBC	X-ray	2.10	B	1-147	[»]
2HBD	X-ray	2.20	B	1-147	[»]
2HBE	X-ray	2.00	B	1-147	[»]
2HBF	X-ray	2.20	B	1-147	[»]
2HBS	X-ray	2.05	B/D/F/H	1-147	[»]
2HCO	X-ray	2.70	B	2-147	[»]
2HHB	X-ray	1.74	B/D	2-147	[»]
2HHD	X-ray	2.20	B/D	1-147	[»]
2HHE	X-ray	2.20	B/D	4-147	[»]
2W6V	X-ray	1.80	B/D	2-147	[»]
2W72	X-ray	1.07	B/D	3-147	[»]
2YRS	X-ray	2.30	B/D/K/O	2-147	[»]
3B75	X-ray	2.30	B/D/F/H/T	2-147	[»]
3D17	X-ray	2.80	B/D	2-147	[»]
3D7O	X-ray	1.80	B	2-147	[»]
3DUT	X-ray	1.55	B/D	2-147	[»]
3HHB	X-ray	1.74	B/D	2-147	[»]
3HXN	X-ray	2.00	B/D	2-147	[»]
3IC0	X-ray	1.80	B/D	2-146	[»]
3IC2	X-ray	2.40	B/D	2-147	[»]
3KMF	neutron diffraction	2.00	C/G	2-147	[»]
3NL7	X-ray	1.80	B	2-147	[»]
3NMM	X-ray	1.60	B/D	2-147	[»]
3ODQ	X-ray	3.10	B/D	2-147	[»]
3ONZ	X-ray	2.09	B	2-147	[»]
3OO4	X-ray	1.90	B	2-147	[»]
3OO5	X-ray	2.10	B	2-147	[»]
3P5Q	X-ray	2.00	B	2-147	[»]
3QJB	X-ray	1.80	B	2-147	[»]
3QJC	X-ray	2.00	B	2-147	[»]
3QJD	X-ray	1.56	B/D	2-147	[»]
3QJE	X-ray	1.80	B/D	2-147	[»]
3R5I	X-ray	2.20	B/D	2-147	[»]
3S65	X-ray	1.80	B/D	2-147	[»]
3S66	X-ray	1.40	B	2-147	[»]
3SZK	X-ray	3.01	B/E	2-147	[»]
3W4U	X-ray	1.95	B/D/F	2-147	[»]
4HHB	X-ray	1.74	B/D	2-147	[»]
6HBW	X-ray	2.00	B/D	2-147	[»]

ProteinModelPortal

P68871.

ModBase

Search...

Protein-protein interaction databases

IntAct

P68871. 6 interactions.

MINT

MINT-5000306.

PTM databases

PhosphoSite

P68871.

Polymorphism databases

DMDM

56749856.

2D gel databases

REPRODUCTION-2DPAGE

IPI00654755.
P68871.

SWISS-2DPAGE

P68871.

UCD-2DPAGE

P02023.
P68871.

Proteomic databases

PaxDb

P68871.

PeptideAtlas

P68871.

PRIDE

P68871.

Protocols and materials databases

DNASU

3043.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000335295; ENSP00000333994; ENSG00000244734.

GeneID

3043.

KEGG

hsa:3043.

UCSC

uc001mae.1. human.

Organism-specific databases

CTD

3043.

GeneCards

GC11M005250.

HGNC

HGNC:4827. HBB.

HPA

CAB009526.
HPA043234.

MIM

140700. phenotype.
141900. gene+phenotype.
603902. phenotype.
603903. phenotype.
613985. phenotype.

neXtProt

NX_P68871.

Orphanet

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.
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.

PharmGKB

PA29202.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG269316.

HOVERGEN

HBG009709.

InParanoid

P68871.

KO

K13823.

OMA

WGKVKVD.

OrthoDB

EOG4THVVF.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P68871.

Bgee

P68871.

Genevestigator

P68871.

GermOnline

ENSG00000188170. Homo sapiens.

Family and domain databases

Gene3D

1.10.490.10. 1 hit.

InterPro

IPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002337. Haemoglobin_b.
[Graphical view]

Pfam

PF00042. Globin. 1 hit.
[Graphical view]

PRINTS

PR00814. BETAHAEM.

SUPFAM

SSF46458. Globin_like. 1 hit.

PROSITE

PS01033. GLOBIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL4331.

ChiTaRS

HBB. human.

DrugBank

DB00893. Iron Dextran.

EvolutionaryTrace

P68871.

GenomeRNAi

3043.

NextBio

12048.

PMAP-CutDB

P68871.

SOURCE

Search...

Entry information

Entry name

HBB_HUMAN

Accession

Primary (citable) accession number: P68871
Secondary accession number(s): A4GX73 , 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:	May 29, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.