Hemoglobin subunit beta - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
    Hemoglobin subunit beta
Alternative name(s):
    Hemoglobin beta chain
    Beta-globin
Cleaved into the following chain:
    1- Recommended name:
            LVV-hemorphin-7

Gene names

Name:

HBB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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. LVV-hemorphin-7 potentiates the activity of bradykinin, causing a decrease in blood pressure.
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 Fe(2+) and then transferred to Cys-94 to allow capture of O(2). Acetylated on Lys-60, Lys-83 and Lys-145 upon aspirin exposure. Ref.27 reports the identification of HBB acetylated on Lys-145 in the cytosolic fraction of HeLa cells. This may results from a contamination of the sample.
Involvement in disease	Defects in HBB may be a cause of Heinz body anemias [MIM:140700]. This is a form of non-spherocytic hemolytic anemia of Dacie type 1. After splenectomy, which has little benefit, basophilic inclusions called Heinz bodies are demonstrable in the erythrocytes. Before splenectomy, diffuse or punctate basophilia may be evident. Most of these cases are probably instances of hemoglobinopathy. The hemoglobin demonstrates heat lability. Heinz bodies are observed also with the Ivemark syndrome (asplenia with cardiovascular anomalies) and with glutathione peroxidase deficiency. Defects in HBB are the cause of beta-thalassemia [MIM:141900, 604131]. The thalassemias are the most common monogenic diseases and occur 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 (transfusion dependent), thalassemia intermedia (of intermediate severity), and thalassemia minor (asymptomatic). Defects in HBB are the cause of sickle cell anemia [MIM:603903]; also known as sickle cell disease. Sickle cell anemia is characterized by abnormally shaped red cells resulting in chronic anemia and periodic episodes of pain, serious infections and damage to vital organs. Normal red blood cells are round and flexible and flow easily through blood vessels, but in sickle cell anemia, the abnormal hemoglobin (called Hb S) causes red blood cells to become stiff. They are C-shaped and resembles a sickle. These stiffer red blood cells can led to microvascular occlusion thus cutting off the blood supply to nearby tissues. Defects in HBB are the cause of dominant beta-thalassemia inclusion body type [MIM:603902]. This form of beta-thalassemia is transmitted in an autosomal dominant fashion and is characterized by anemia, enlargement of the spleen, and gross abnormalities of the erythrocytes and their precursors.
Miscellaneous	One molecule of 2,3-bisphospoglycerate can bind to two beta chains per hemoglobin tetramer.
Sequence similarities	Belongs to the globin family.
Mass spectrometry	Molecular weight is 1310 Da from positions 33 - 42. Determined by FAB. Ref.15

Ontologies

Keywords
Biological process	Oxygen transport Transport
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Ligand	Heme Iron Metal-binding Pyruvate
Molecular function	Hypotensive agent Vasoactive
PTM	Acetylation Glycation Glycoprotein Phosphoprotein S-nitrosylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	nitric oxide transport Non-traceable author statement. Source: UniProtKB oxygen transport Ref.85 Traceable author statement. Source: UniProtKB positive regulation of nitric oxide biosynthetic process Non-traceable author statement. Source: UniProtKB
Cellular component	hemoglobin complex Ref.26 Ref.85 Traceable author statement. Source: UniProtKB
Molecular function	hemoglobin binding Inferred from direct assay. Source: UniProtKB oxygen binding Inferred from direct assay. Source: UniProtKB oxygen transporter activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HBA1	P69905	1	EBI-715554,EBI-714680

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 147

146

Hemoglobin subunit beta

PRO_0000052976

Peptide

33 – 42

LVV-hemorphin-7

PRO_0000296641

Sites

Metal binding

Iron (heme distal ligand)

Metal binding

Iron (heme proximal ligand)

Binding site

2,3-bisphosphoglycerate; via amino nitrogen

Binding site

2,3-bisphosphoglycerate

Binding site

2,3-bisphosphoglycerate

Binding site

2,3-bisphosphoglycerate

Site

Not glycated

Site

Not glycated

Site

Not glycated

Site

142

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

Site

145

Aspirin-acetylated lysine

Amino acid modifications

Modified residue

N-acetylalanine; in variant Raleigh

Modified residue

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

Modified residue

S-nitrosocysteine

Modified residue

131

Phosphotyrosine

Glycosylation

N-linked (Glc) (glycation); in Hb A1c

Glycosylation

N-linked (Glc) (glycation)

Glycosylation

N-linked (Glc) (glycation)

Glycosylation

N-linked (Glc) (glycation)

Glycosylation

N-linked (Glc) (glycation)

Glycosylation

145

N-linked (Glc) (glycation)

Natural variations

Natural variant

V → A in Raleigh; O(2) affinity down.

VAR_002856

Natural variant

H → L in Graz. dbSNP rs35906307.

VAR_002857

Natural variant

H → Q in Okayama; O(2) affinity up. dbSNP rs713040.

VAR_002858

Natural variant

H → R in Deer Lodge; O(2) affinity up.

VAR_002859

Natural variant

H → Y in Fukuoka.

VAR_002860

Natural variant

P → R in Warwickshire. dbSNP rs34769005.

VAR_002861

Natural variant

E → A in G-Makassar.

VAR_002862

Natural variant

E → K in C.

VAR_002864

Natural variant

E → Q in Machida.

VAR_002865

Natural variant

E → V in S; sickle cell anemia. dbSNP rs334.

VAR_002863

Natural variant

E → G in G-San Jose; mildly unstable. dbSNP rs34948328.

VAR_002866

Natural variant

E → K in G-Siriraj.

VAR_002867

Natural variant

K → E in N-Timone. dbSNP rs33932981.

VAR_002868

Natural variant

K → Q in J-Luhe.

VAR_002869

Natural variant

K → T in Rio Grande.

VAR_002870

Natural variant

S → C in Porto Alegre; O(2) affinity up.

VAR_002871

Natural variant

A → D in Ankara.

VAR_002872

Natural variant

A → V in Iraq-Halabja.

VAR_025393

Natural variant

V → D in Windsor; O(2) affinity up; unstable. dbSNP rs33974228.

VAR_002873

Natural variant

V → I in Hamilton.

VAR_002874

Natural variant

A → D in J-Lens. dbSNP rs35203747.

VAR_002875

Natural variant

L → P in Saki; unstable.

VAR_002876

Natural variant

L → R in Soegn; unstable.

VAR_002877

Natural variant

W → G in Randwick; unstable. dbSNP rs33946157.

VAR_002878

Natural variant

W → R in Belfast; O(2) affinity up; unstable.

VAR_002879

Natural variant

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

VAR_002880

Natural variant

G → R in D-Bushman.

VAR_002881

Natural variant

K → E in Nagasaki. dbSNP rs33986703.

VAR_002882

Natural variant

K → N in J-Amiens.

VAR_002883

Natural variant

K → Q in Nikosia.

VAR_002884

Natural variant

V → M in Baden; slightly unstable. dbSNP rs35802118.

VAR_002885

Natural variant

N → D in Alamo.

VAR_002886

Natural variant

N → K in D-Ouleh RABAH.

VAR_002887

Natural variant

N → S in Malay.

VAR_002888

Natural variant

V → M in Olympia; O(2) affinity up.

VAR_002889

Natural variant

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

VAR_002890

Natural variant

D → H in Karlskoga.

VAR_002892

Natural variant

D → N in Cocody.

VAR_002891

Natural variant

D → Y in Yusa.

VAR_002893

Natural variant

E → A in G-Coushatta/G-Saskatoon/G-Taegu/Hsin Chu.

VAR_002894

Natural variant

E → G in G-Taipei.

VAR_002895

Natural variant

E → K in E-Saskatoon; unstable.

VAR_002896

Natural variant

E → Q in D-Iran.

VAR_002897

Natural variant

E → V in D-Granada.

VAR_002898

Natural variant

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

VAR_002899

Natural variant

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

VAR_002900

Natural variant

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

VAR_002901

Natural variant

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

VAR_002902

Natural variant

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

VAR_002903

Natural variant

G → V in Savannah; unstable.

VAR_002904

Natural variant

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

VAR_002905

Natural variant

G → R in G-Taiwan Ami.

VAR_002906

Natural variant

E → K in E.

VAR_002907

Natural variant

E → V in Henri Mondor; slightly unstable.

VAR_002908

Natural variant

A → D in Volga/Drenthe; unstable.

VAR_002909

Natural variant

A → S in Knossos.

VAR_002910

Natural variant

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

VAR_002911

Natural variant

L → P in Genova/Hyogo; unstable.

VAR_002912

Natural variant

L → Q in St Louis.

VAR_035236

Natural variant

G → D in Lufkin; unstable.

VAR_002913

Natural variant

R → S in Tacoma; unstable.

VAR_002914

Natural variant

L → P in Yokohama; unstable.

VAR_002915

Natural variant

L → R in Castilla; unstable.

VAR_002916

Natural variant

L → V in Muscat; slightly unstable.

VAR_002917

Natural variant

V → D in Santander; unstable.

VAR_025394

Natural variant

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

VAR_002918

Natural variant

V → L in Nantes; increased oxygen affinity.

VAR_025395

Natural variant

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

VAR_002919

Natural variant

P → R in Sunnybrook.

VAR_002920

Natural variant

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

VAR_002921

Natural variant

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

VAR_002922

Natural variant

W → G in Howick.

VAR_002923

Natural variant

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

VAR_002925

Natural variant

W → S in Hirose; O(2) affinity up.

VAR_002924

Natural variant

T → N in Hinwil; O(2) affinity up.

VAR_002926

Natural variant

Q → E in Vaasa; unstable.

VAR_002927

Natural variant

Q → K in Alabama.

VAR_002928

Natural variant

Q → R in Tianshui.

VAR_002929

Natural variant

F → Y in Mequon.

VAR_002930

Natural variant

Missing in Bruxelles.

VAR_035237

Natural variant

F → L in Louisville; unstable.

VAR_002931

Natural variant

F → S in Hammersmith.

VAR_035239

Natural variant

Missing in Bruxelles.

VAR_035238

Natural variant

E → Q in Hoshida/Chaya.

VAR_002932

Natural variant

S → C in Mississippi.

VAR_002933

Natural variant

F → S in Cheverly; unstable.

VAR_002934

Natural variant

G → E in K-Ibadan.

VAR_002935

Natural variant

D → A in Avicenna.

VAR_002936

Natural variant

D → G in Gavello.

VAR_002937

Natural variant

D → Y in Maputo.

VAR_002938

Natural variant

L → P in Bab-Saadoum; slightly unstable.

VAR_002939

Natural variant

S → F in Las Palmas; slightly unstable.

VAR_002940

Natural variant

T → K in Edmonton.

VAR_002941

Natural variant

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

VAR_002942

Natural variant

D → A in Ocho Rios.

VAR_002943

Natural variant

D → H in Summer Hill.

VAR_002944

Natural variant

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

VAR_002945

Natural variant

M → K in Matera; unstable.

VAR_002946

Natural variant

G → R in Hamadan.

VAR_002947

Natural variant

N → K in G-ferrara; unstable.

VAR_002948

Natural variant

P → R in Dhofar/Yukuhashi.

VAR_002949

Natural variant

K → E in I-High Wycombe.

VAR_002950

Natural variant

V → A in Collingwood; unstable.

VAR_002951

Natural variant

K → E in N-Seatlle.

VAR_002952

Natural variant

K → M in Bologna; O(2) affinity down.

VAR_002953

Natural variant

K → N in Hikari.

VAR_002954

Natural variant

A → D in J-Europa.

VAR_002955

Natural variant

A → P in Duarte; unstable.

VAR_002956

Natural variant

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

VAR_002957

Natural variant

K → M in J-Antakya.

VAR_002958

Natural variant

K → N in J-Sicilia.

VAR_002959

Natural variant

K → Q in J-Cairo.

VAR_002960

Natural variant

K → T in Chico; O(2) affinity down.

VAR_002961

Natural variant

V → A in Sydney; unstable.

VAR_002962

Natural variant

V → D in Bristol.

VAR_035240

Natural variant

V → G in non-spherocytic haemolytic anemia; Manukau. dbSNP rs33918343.

VAR_040060

Natural variant

V → M in Alesha; unstable.

VAR_002963

Natural variant

L → H in Brisbane; O(2) affinity up.

VAR_002964

Natural variant

L → P in Mizuho; unstable.

VAR_002965

Natural variant

G → D in Rambam.

VAR_002966

Natural variant

G → R in Kenitra.

VAR_002967

Natural variant

G → S in City of Hope.

VAR_002968

Natural variant

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

VAR_002969

Natural variant

F → S in Christchurch; unstable.

VAR_002970

Natural variant

D → G in Tilburg; O(2) affinity down.

VAR_002971

Natural variant

D → V in Mobile; O(2) affinity down.

VAR_002972

Natural variant

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

VAR_002973

Natural variant

G → R in Aalborg; unstable.

VAR_002974

Natural variant

G → V in Bushwick; unstable.

VAR_002975

Natural variant

L → P in Atlanta; unstable.

VAR_002976

Natural variant

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

VAR_002977

Natural variant

A → D in J-Chicago.

VAR_002978

Natural variant

H → D in J-Iran.

VAR_002979

Natural variant

H → R in Costa Rica.

VAR_002980

Natural variant

H → Y in Fukuyama.

VAR_002981

Natural variant

L → R in Quin-hai.

VAR_002982

Natural variant

D → Y in Tampa.

VAR_002983

Natural variant

N → K in G-Szuhu/Gifu.

VAR_002984

Natural variant

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

VAR_012663

Natural variant

L → R in Baylor; unstable.

VAR_002985

Natural variant

K → M in Helsinki; O(2) affinity up.

VAR_002986

Natural variant

K → N in Providence.

VAR_012664

Natural variant

G → D in Pyrgos.

VAR_025396

Natural variant

G → R in Muskegon.

VAR_002987

Natural variant

T → I in Kofu.

VAR_002988

Natural variant

A → D in Olomouc; O(2) affinity up.

VAR_002989

Natural variant

T → I in Quebec-Chori.

VAR_002990

Natural variant

T → K in D-Ibadan.

VAR_002991

Natural variant

T → P in Valletta.

VAR_002992

Natural variant

L → P in Santa Ana; unstable.

VAR_002993

Natural variant

L → R in Boras; unstable.

VAR_002994

Natural variant

S → N in Creteil; O(2) affinity up.

VAR_002995

Natural variant

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

VAR_002996

Natural variant

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

VAR_002997

Natural variant

E → K in Agenogi; O(2) affinity down.

VAR_002998

Natural variant

L → P in Sabine; unstable.

VAR_002999

Natural variant

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

VAR_003000

Natural variant

H → D in J-Altgelds Gardens; unstable.

VAR_003001

Natural variant

H → N in Isehara; unstable.

VAR_003002

Natural variant

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

VAR_003003

Natural variant

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

VAR_003004

Natural variant

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

VAR_003005

Natural variant

D → G in Chandigarh.

VAR_003006

Natural variant

D → H in Barcelona; O(2) affinity up.

VAR_003007

Natural variant

D → N in Bunbury; O(2) affinity up.

VAR_003008

Natural variant

K → M in J-Cordoba.

VAR_003009

Natural variant

K → N in Detroit.

VAR_003010

Natural variant

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

VAR_003011

Natural variant

L → V in Regina; O(2) affinity up.

VAR_003012

Natural variant

H → L in Wood; O(2) affinity up.

VAR_003013

Natural variant

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

VAR_003014

Natural variant

H → Q in Malmoe; O(2) affinity up.

VAR_003015

Natural variant

H → Y in Moriguchi.

VAR_003016

Natural variant

V → G in Nottingham; unstable.

VAR_003017

Natural variant

100

D → E in Coimbra; O(2) affinity up.

VAR_003018

Natural variant

101

P → L in Brigham; O(2) affinity up.

VAR_003019

Natural variant

101

P → R in New Mexico.

VAR_003020

Natural variant

E → D in Potomac; O(2) affinity up.

VAR_003021

Natural variant

E → G in Alberta; O(2) affinity up.

VAR_003022

Natural variant

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

VAR_003023

Natural variant

E → Q in Rush; unstable.

VAR_003024

Natural variant

103

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

VAR_003025

Natural variant

103

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

VAR_003026

Natural variant

104

F → L in Heathrow; O(2) affinity up.

VAR_003027

Natural variant

105

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

VAR_003028

Natural variant

105

R → T in Sherwood Forest.

VAR_003029

Natural variant

108

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

VAR_003030

Natural variant

109

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

VAR_003031

Natural variant

110

V → M in San Diego; O(2) affinity up.

VAR_003032

Natural variant

111

L → P in Showa-Yakushiji.

VAR_003033

Natural variant

112

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

VAR_003034

Natural variant

113

C → F in Canterbury.

VAR_025397

Natural variant

113

C → R in Indianapolis.

VAR_003035

Natural variant

113

C → Y in Yahata.

VAR_003036

Natural variant

115

L → M in Zengcheng.

VAR_010144

Natural variant

115

L → P in Durham-N.C./Brescia; causes beta-thalassemia.

VAR_010145

Natural variant

116

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

VAR_003037

Natural variant

116

A → P in Madrid; unstable.

VAR_003038

Natural variant

117

H → L in Vexin; increased oxygen affinity.

VAR_025398

Natural variant

117

H → Q in Hafnia.

VAR_003039

Natural variant

118

H → P in Saitama; unstable.

VAR_003040

Natural variant

118

H → R in P-Galveston.

VAR_003041

Natural variant

118

H → Y in Tsukumi.

VAR_025399

Natural variant

120

G → A in Iowa.

VAR_003042

Natural variant

K → E in Hijiyama.

VAR_003043

Natural variant

K → I in Jianghua.

VAR_003044

Natural variant

K → Q in Takamatsu.

VAR_003045

Natural variant

E → A in D-Neath.

VAR_003046

Natural variant

E → G in St Francis.

VAR_003047

Natural variant

E → K in O-Arab.

VAR_003049

Natural variant

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

VAR_003048

Natural variant

E → V in D-Camperdown/Beograd.

VAR_003050

Natural variant

124

T → I in Villejuif; asymptomatic variant.

VAR_003051

Natural variant

125

P → Q in Ty Gard; O(2) affinity up.

VAR_003053

Natural variant

125

P → R in Khartoum; unstable.

VAR_003052

Natural variant

125

P → S in Tunis.

VAR_003054

Natural variant

127

V → A in Beirut.

VAR_003055

Natural variant

127

V → E in Hofu; unstable.

VAR_003057

Natural variant

127

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

VAR_003056

Natural variant

128

Q → E in Complutense.

VAR_003058

Natural variant

128

Q → K in Brest; unstable.

VAR_003059

Natural variant

129

A → D in J-Guantanamo; unstable.

VAR_003060

Natural variant

130

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

VAR_003061

Natural variant

130

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

VAR_003062

Natural variant

131

Y → D in Wien; unstable.

VAR_003063

Natural variant

131

Y → S in Nevers.

VAR_003064

Natural variant

Q → E in Camden/Tokuchi/Motown.

VAR_003065

Natural variant

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

VAR_003066

Natural variant

Q → P in Shangai; unstable.

VAR_003067

Natural variant

Q → R in Sarrebourg; unstable.

VAR_003068

Natural variant

133

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

VAR_003069

Natural variant

133

K → Q in K-Woolwich.

VAR_003070

Natural variant

134

V → L in Extredemura.

VAR_003071

Natural variant

135

V → E in North Shore-Caracas; unstable.

VAR_003072

Natural variant

136

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

VAR_003073

Natural variant

136

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

VAR_003074

Natural variant

137

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

VAR_003075

Natural variant

139

A → P in Brockton; unstable.

VAR_003076

Natural variant

N → D in Geelong; unstable.

VAR_003077

Natural variant

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

VAR_003078

Natural variant

N → S in S-Wake; associated with V-6.

VAR_025335

Natural variant

N → Y in Aurora; O(2) affinity up.

VAR_003079

Natural variant

141

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

VAR_003080

Natural variant

141

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

VAR_003081

Natural variant

141

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

VAR_003082

Natural variant

142

L → R in Olmsted; unstable.

VAR_003083

Natural variant

143

A → D in Ohio; O(2) affinity up.

VAR_003084

Natural variant

H → D in Rancho Mirage.

VAR_003085

Natural variant

H → P in Syracuse; O(2) affinity up.

VAR_003087

Natural variant

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

VAR_003086

Natural variant

H → R in Abruzzo; O(2) affinity up.

VAR_003088

Natural variant

145

K → E in Mito; O(2) affinity up.

VAR_003089

Natural variant

146

Y → C in Rainier; O(2) affinity up.

VAR_003090

Natural variant

146

Y → H in Bethesda; O(2) affinity up.

VAR_003091

Natural variant

H → D in Hiroshima; O(2) affinity up.

VAR_003092

Natural variant

H → L in Cowtown; O(2) affinity up.

VAR_003093

Natural variant

H → P in York; O(2) affinity up.

VAR_003094

Natural variant

H → Q in Kodaira; O(2) affinity up.

VAR_003095

Secondary structure

147

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P68871-1 [UniParc].

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

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References

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[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: 1019344] [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: 6254664] [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: 16175509] [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]	"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.
[6]	"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.
[7]	"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.
[8]	"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].
[9]	"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.
[10]	"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.
[11]	"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].
[12]	"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].
[13]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skeletal muscle.
[14]	"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: 13872627] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-147.
[15]	"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: 1575724] [Abstract] Cited for: PROTEIN SEQUENCE OF 33-42, MASS SPECTROMETRY.
[16]	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.
[17]	"Cloning specific complete polyadenylylated 3'-terminal cDNA segments." Lang K.M., Spritz R.A. Gene 33:191-196(1985) [PubMed: 2581851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-147.
[18]	"X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin." Arnone A. Nature 237:146-149(1972) [PubMed: 4555506] [Abstract] Cited for: BISPHOSPHOGLYCERATE BINDING.
[19]	"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: 4531009] [Abstract] Cited for: ACETYLATION AT LYS-145.
[20]	"The glycosylation of hemoglobin: relevance to diabetes mellitus." Bunn H.F., Gabbay K.H., Gallop P.M. Science 200:21-27(1978) [PubMed: 635569] [Abstract] Cited for: GLYCATION AT VAL-2.
[21]	"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: 7358733] [Abstract] Cited for: GLYCATION AT LYS-9; LYS-18; LYS-67; LYS-121 AND LYS-145, ABSENCE OF GLYCATION AT LYS-60; LYS-83 AND LYS-96.
[22]	"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: 3718478] [Abstract] Cited for: INTERACTION WITH HAPTOGLOBIN.
[23]	"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: 1520632] [Abstract] Cited for: OXIDATION AT LEU-142.
[24]	"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: 8637569] [Abstract] Cited for: S-NITROSYLATION AT CYS-94.
[25]	"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: 9843411] [Abstract] Cited for: S-NITROSYLATION AT CYS-94.
[26]	"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: 10588683] [Abstract] Cited for: NITRIC OXIDE-BINDING.
[27]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-145, MASS SPECTROMETRY. Tissue: Epithelium.
[28]	"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: 16904236] [Abstract] Cited for: SYNTHESIS OF 33-42, FUNCTION.
[29]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-131, MASS SPECTROMETRY.
[30]	"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: 4123689] [Abstract] Cited for: ELECTRON MICROSCOPY OF SICKLE-CELL HEMOGLOBIN FIBERS.
[31]	"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: 1195378] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (5 ANGSTROMS) OF MUTANT VAL-7.
[32]	"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: 1177322] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN.
[33]	"The structure of human carbonmonoxy haemoglobin at 2.7-A resolution." Baldwin J.M. J. Mol. Biol. 136:103-128(1980) [PubMed: 7373648] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF CARBONMONOXY HEMOGLOBIN.
[34]	"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: 6726807] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF DEOXYHEMOGLOBIN.
[35]	"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: 1567857] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ROTHSCHILD ARG-38.
[36]	"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: 1507231] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ARG-75.
[37]	"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: 8377203] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), BISPHOSPHOGLYCERATE BINDING.
[38]	"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: 8642597] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[39]	"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: 9521756] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-38; GLU-38; GLY-38 AND TYR-38.
[40]	"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: 9830011] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT TRP-7.
[41]	"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: 12454462] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT LYS-7.
[42]	"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: 1115799] [Abstract] Cited for: VARIANT ALABAMA LYS-40.
[43]	"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: 186485] [Abstract] Cited for: INVOLVEMENT IN HEINZ BODY ANEMIAS, VARIANT ST LOUIS GLN-29.
[44]	"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: 1971109] [Abstract] Cited for: INVOLVEMENT IN DOMINANT BETA-THALASSEMIA INCLUSION BODY TYPE.
[45]	"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: 8330974] [Abstract] Cited for: VARIANT ALESHA MET-68.
[46]	"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: 721609] [Abstract] Cited for: VARIANT J-ALTGELDS GARDENS ASP-93.
[47]	"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: 4850241] [Abstract] Cited for: VARIANT ANKARA ASP-11.
[48]	"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: 3707969] [Abstract] Cited for: VARIANTS J-ANTAKYA MET-66 AND COMPLUTENSE GLU-128.
[49]	"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: 3654265] [Abstract] Cited for: VARIANT J-AUCKLAND ASP-26.
[50]	"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: 8718692] [Abstract] Cited for: VARIANT AURORA TYR-140.
[51]	"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: 3384710] [Abstract] Cited for: VARIANT BREST LYS-128.
[52]	"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: 6166590] [Abstract] Cited for: VARIANT BRISBANE HIS-69.
[53]	"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: 6629823] [Abstract] Cited for: VARIANT BUNBURY ASN-95.
[54]	"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: 1247583] [Abstract] Cited for: VARIANT J-CAIRO GLN-66.
[55]	"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: 1138922] [Abstract] Cited for: VARIANT CAMPERDOWN SER-105.
[56]	"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: 992050] [Abstract] Cited for: VARIANT CARIBBEAN ARG-92.
[57]	"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: 6434492] [Abstract] Cited for: VARIANT CITY OF HOPE SER-70.
[58]	"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: 1814856] [Abstract] Cited for: VARIANT COIMBRA GLU-100.
[59]	"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: 8641705] [Abstract] Cited for: VARIANT COSTA RICA ARG-78.
[60]	"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: 8602627] [Abstract] Cited for: VARIANT DEBROUSSE PRO-97.
[61]	"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: 2399911] [Abstract] Cited for: VARIANT DHONBURI GLY-127.
[62]	"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: 1511986] [Abstract] Cited for: VARIANTS NEWCASTLE PRO-93 AND CAMPERDOWN SER-105, DESCRIPTION OF VARIANT DUINO.
[63]	"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: 1301199] [Abstract] Cited for: VARIANT DURHAM-N.C. PRO-115.
[64]	"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: 8111050] [Abstract] Cited for: VARIANT DURHAM-N.C. PRO-115.
[65]	"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: 8811317] [Abstract] Cited for: VARIANT J-EUROPA ASP-63.
[66]	"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: 1917539] [Abstract] Cited for: VARIANT GEELONG ASP-140.
[67]	"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: 3666141] [Abstract] Cited for: VARIANT GRANGE-BLANCHE VAL-28.
[68]	"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: 1487420] [Abstract] Cited for: VARIANT GRAZ LEU-3.
[69]	"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: 826083] [Abstract] Cited for: VARIANT HELSINKI MET-83.
[70]	"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: 3754244] [Abstract] Cited for: VARIANT HIMEJI ASP-141.
[71]	"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: 2513289] [Abstract] Cited for: VARIANT HINSDALE LYS-140.
[72]	"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: 8745430] [Abstract] Cited for: VARIANT HINWIL ASN-39.
[73]	"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: 8144352] [Abstract] Cited for: VARIANT HOWICK GLY-38.
[74]	"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: 429365] [Abstract] Cited for: VARIANT INDIANAPOLIS ARG-113.
[75]	"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: 1787097] [Abstract] Cited for: VARIANT ISEHARA ASN-93.
[76]	"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: 4639022] [Abstract] Cited for: VARIANT ISTAMBUL GLN-93.
[77]	"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: 2101840] [Abstract] Cited for: VARIANT JACKSONVILLE ASP-55.
[78]	"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: 6618888] [Abstract] Cited for: VARIANT JIANGHUA ILE-121.
[79]	"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: 8330972] [Abstract] Cited for: VARIANT KARLSKOGA HIS-22.
[80]	"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: 7173395] [Abstract] Cited for: VARIANT KNOSSOS SER-28.
[81]	"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: 1634367] [Abstract] Cited for: VARIANT KODAIRA GLN-147.
[82]	"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: 3744871] [Abstract] Cited for: VARIANT KOFU ILE-85.
[83]	"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: 7693620] [Abstract] Cited for: VARIANT HRADEC KRALOVE ASP-116.
[84]	"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: 3557994] [Abstract] Cited for: VARIANT LA DESIRADE VAL-130.
[85]	"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: 1540659] [Abstract] Cited for: VARIANT LA ROCHE-SUR-YON HIS-82.
[86]	"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: 3384708] [Abstract] Cited for: VARIANT LAS PALMAS PHE-50.
[87]	"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: 3691763] [Abstract] Cited for: VARIANT LINKOPING THR-37.
[88]	"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: 6629824] [Abstract] Cited for: VARIANT MAPUTO TYR-48.
[89]	"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: 2384314] [Abstract] Cited for: VARIANT MATERA LYS-56.
[90]	"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: 7338468] [Abstract] Cited for: VARIANT MIYASHIRO GLY-24.
[91]	"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: 893142] [Abstract] Cited for: VARIANT MIZUHO PRO-69.
[92]	"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: 1517102] [Abstract] Cited for: VARIANT MUSCAT VAL-33.
[93]	"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: 2634671] [Abstract] Cited for: VARIANT N-TIMONE GLU-9.
[94]	"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: 3838976] [Abstract] Cited for: VARIANT NAGOYA PRO-98.
[95]	"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: 8330979] [Abstract] Cited for: VARIANT D-NEATH ALA-122.
[96]	"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: 3937824] [Abstract] Cited for: VARIANT NORTH CHICAGO SER-37.
[97]	"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: 891976] [Abstract] Cited for: VARIANT NORTH SHORE-CARACAS GLU-135.
[98]	"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: 3623975] [Abstract] Cited for: VARIANT OLOMOUC ASP-87.
[99]	"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: 7161106] [Abstract] Cited for: VARIANT PALMERSTON NORTH PHE-24.
[100]	"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: 3384709] [Abstract] Cited for: VARIANT PIERRE-BENITE ASP-91.
[101]	"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: 668922] [Abstract] Cited for: VARIANT PRESBYTERIAN LYS-109.
[102]	"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: 8522332] [Abstract] Cited for: VARIANT PUTTELANGE VAL-141.
[103]	"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: 6629822] [Abstract] Cited for: VARIANT QUIN-HAI ARG-79.
[104]	"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: 9761252] [Abstract] Cited for: VARIANT RAMBAM ASP-70.
[105]	"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: 3384707] [Abstract] Cited for: VARIANT RANDWICK GLY-16.
[106]	"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: 6857757] [Abstract] Cited for: VARIANT RIO GRANDE THR-9.
[107]	"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: 4129558] [Abstract] Cited for: VARIANT RUSH GLN-102.
[108]	"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: 6687721] [Abstract] Cited for: VARIANT SAITAMA PRO-118.
[109]	"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: 13897827] [Abstract] Cited for: VARIANT M-SASKATOON TYR-64.
[110]	"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: 6526653] [Abstract] Cited for: VARIANT SHELBY/LESLIE/DEACONESS LYS-132.
[111]	"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: 4852224] [Abstract] Cited for: VARIANT J-SICILIA ASN-66.
[112]	"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: 1917537] [Abstract] Cited for: VARIANT STANMORE ALA-112.
[113]	"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: 7238856] [Abstract] Cited for: VARIANT ST MANDE TYR-103.
[114]	"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: 2599880] [Abstract] Cited for: VARIANT WINDSOR ASP-12.
[115]	"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: 1917530] [Abstract] Cited for: VARIANT YAHATA TYR-113.
[116]	"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: 7338469] [Abstract] Cited for: VARIANT YOKOHAMA PRO-32.
[117]	"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: 6259091] [Abstract] Cited for: INVOLVEMENT IN HEINZ BODY ANEMIAS, VARIANT HAMMERSMITH SER-43.
[118]	"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: 2599881] [Abstract] Cited for: INVOLVEMENT IN HEINZ BODY ANEMIAS, VARIANTS BRUXELLES PHE-42 DEL AND PHE-43 DEL.
[119]	"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: 2079435] [Abstract] Cited for: VARIANT ZENGCHENG MET-115.
[120]	"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: 8280608] [Abstract] Cited for: VARIANT NON-SPHEROCYTIC HAEMOLITIC ANEMIA GLY-68.
[121]	"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: 8704193] [Abstract] Cited for: INVOLVEMENT IN HEINZ BODY ANEMIAS, VARIANT BRISTOL ASP-68.
[122]	"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: 10398311] [Abstract] Cited for: VARIANT IRAQ-HALABJA VAL-11.
[123]	"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: 11300351] [Abstract] Cited for: VARIANT VILLEJUIF ILE-124.
[124]	"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: 11300344] [Abstract] Cited for: VARIANT TSUKUMI TYR-118.
[125]	"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: 11939514] [Abstract] Cited for: VARIANT CANTERBURY PHE-113.
[126]	"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: 12144064] [Abstract] Cited for: VARIANT PYRGOS ASP-84, VARIANT E LYS-27.
[127]	"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: 12603091] [Abstract] Cited for: VARIANT SANTANDER ASP-35.
[128]	"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: 12908805] [Abstract] Cited for: VARIANT NANTES LEU-35, VARIANT VEXIN LEU-117.
[129]	"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: 15481886] [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

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.
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.
CR536530 mRNA. Translation: CAG38767.1.
CR541913 mRNA. Translation: CAG46711.1.
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.
A01592 Unassigned DNA. Translation: CAA00182.1.

PIR

HBHU. A53136.

RefSeq

NP_000509.1.

UniGene

Hs.523443

3D structure databases

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	1-147	[»]
1A3O	X-ray	1.80	B/D	1-147	[»]
1ABW	X-ray	2.00	B/D	3-147	[»]
1ABY	X-ray	2.60	B/D	3-147	[»]
1AJ9	X-ray	2.20	B	1-147	[»]
1B86	X-ray	2.50	B/D	1-147	[»]
1BAB	X-ray	1.50	B/D	1-147	[»]
1BBB	X-ray	1.70	B/D	1-147	[»]
1BIJ	X-ray	2.30	B/D	1-147	[»]
1BUW	X-ray	1.90	B/D	2-147	[»]
1BZ0	X-ray	1.50	B/D	1-147	[»]
1BZ1	X-ray	1.59	B/D	1-147	[»]
1BZZ	X-ray	1.59	B/D	1-147	[»]
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	1-147	[»]
1CBM	X-ray	1.74	A/B/C/D	1-147	[»]
1CH4	X-ray	2.50	A	2-129	[»]
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	1-147	[»]
1G9V	X-ray	1.85	B/D	1-147	[»]
1GBU	X-ray	1.80	B/D	1-147	[»]
1GBV	X-ray	2.00	B/D	1-147	[»]
1GLI	X-ray	2.50	B/D	3-147	[»]
1GZX	X-ray	2.10	B/D	1-147	[»]
1HAB	X-ray	2.30	B/D	1-147	[»]
1HAC	X-ray	2.60	B/D	1-147	[»]
1HBA	X-ray	2.10	B/D	1-147	[»]
1HBB	X-ray	1.90	B/D	1-147	[»]
1HBS	X-ray	3.00	B/D/F/H	1-147	[»]
1HCO	X-ray	2.70	B	1-147	[»]
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	1-147	[»]
2HHD	X-ray	2.20	B/D	1-147	[»]
2HHE	X-ray	2.20	B/D	4-147	[»]
2YRS	X-ray	2.30	B/D/K/O	2-147	[»]
3D17	X-ray	2.80	B/D	2-147	[»]
4HHB	X-ray	1.74	B/D	1-147	[»]
6HBW	X-ray	2.00	B/D	1-147	[»]

ModBase

Protein-protein interaction databases

IntAct

P68871.

PTM databases

PhosphoSite

P68871.

2-D gel databases

SWISS-2DPAGE

P68871.

HSC-2DPAGE

P68871.

PMMA-2DPAGE

P68871.

REPRODUCTION-2DPAGE

IPI00654755.
P68871.

Siena-2DPAGE

P68871.

Proteomic databases

PeptideAtlas

P68871.

Genome annotation databases

Ensembl

ENSG00000188170. Homo sapiens. [Contig view]

GeneID

3043.

KEGG

hsa:3043.

Organism-specific databases

HGNC

HGNC:4827. HBB.

HPA

CAB009526.

MIM

140700. phenotype.
141900. gene+phenotype.
603902. phenotype.
603903. phenotype.
604131. phenotype.

Orphanet

848. Beta-thalassemia.
2132. Hemoglobin C disease.
2133. Hemoglobin E disease.
232. Sickle cell anaemia.

PharmGKB

PA29202.

GenAtlas

GeneCards

Phylogenomic databases

HOVERGEN

P68871.

Gene expression databases

ArrayExpress

P68871.

GermOnline

ENSG00000188170. Homo sapiens.

Family and domain databases

InterPro

IPR012292. Globin.
IPR000971. Globin_subset.
IPR002337. Haemoglobin_b.
[Graphical view]

Gene3D

G3DSA:1.10.490.10. Globin_related. 1 hit.

Pfam

PF00042. Globin. 1 hit.
[Graphical view]

PRINTS

PR00814. BETAHAEM.

PROSITE

PS01033. GLOBIN. 1 hit.
[Graphical view]

BLOCKS

ProtoNet

Other Resources

DrugBank

DB00893. Iron Dextran.

LinkHub

P68871.

NextBio

12048.

SOURCE

Entry information

Entry name

HBB_HUMAN

Accession

Primary (citable) accession number: P68871
Secondary accession number(s): P02023

Q9UCP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	November 4, 2008
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)