Hemoglobin subunit alpha - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
    Hemoglobin subunit alpha
Alternative name(s):
    Hemoglobin alpha chain
    Alpha-globin

Gene names

Name:	HBA1
AND
Name:	HBA2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	142 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.
Subunit structure	Heterotetramer of two alpha chains and two beta chains in adult hemoglobin A (HbA); two alpha chains and two delta chains in adult hemoglobin A2 (HbA2); two alpha chains and two epsilon chains in early embryonic hemoglobin Gower-2; two alpha chains and two gamma chains in fetal hemoglobin F (HbF).
Tissue specificity	Red blood cells.
Post-translational modification	The initiator Met is not cleaved in variant Thionville and is acetylated.
Involvement in disease	Defects in HBA1/HBA2 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 HBA1/HBA2 are the cause of alpha-thalassemia [MIM:141800, 604131]. The thalassemias are the most common monogenic diseases and occur mostly in Mediterranean and Southeast Asian populations. The hallmark of alpha-thalassemia is an imbalance in globin-chain production in the adult HbA molecule. The level of alpha chain production can range from none to very nearly normal levels. Deletion of both copies of each of the two alpha-globin genes causes alpha(0)-thalassemia, also known as homozygous alpha thalassemia. Due to the complete absence of alpha chains, the predominant fetal hemoglobin is a tetramer of gamma-chains (Bart hemoglobin) that has essentially no oxygen carrying capacity. This causes oxygen starvation in the fetal tissues leading to prenatal lethality or early neonatal death. The loss of three alpha genes results in high levels of a tetramer of four beta chains (hemoglobin H), causing a severe and life-threatening anemia known as hemoglobin H disease. Untreated, most patients die in childhood or early adolescence. The loss of two alpha genes results in mild alpha-thalassemia, also known as heterozygous alpha-thalassemia. Affected individuals have small red cells and a mild anemia (microcytosis). If three of the four alpha-globin genes are functional, individuals are completely asymptomatic. Some rare forms of alpha-thalassemia are due to point mutations (non-deletional alpha-thalassemia). The thalassemic phenotype is due to unstable globin alpha chains that are rapidly catabolized prior to formation of the alpha-beta heterotetramers. Alpha(0)-thalassemia is associated with nonimmune hydrops fetalis [MIM:236750]. Hydrops fetalis is a generalized edema of the fetus with fluid accumulation in the body cavities.
Miscellaneous	Gives blood its red color.
Sequence similarities	Belongs to the globin family.

Ontologies

Keywords
Biological process	Oxygen transport Transport
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Ligand	Heme Iron Metal-binding
PTM	Acetylation Glycation Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxygen transport Traceable author statement. Source: UniProtKB
Cellular component	cytosolic small ribosomal subunit Inferred from direct assay. Source: UniProtKB hemoglobin complex Traceable author statement. Source: UniProtKB
Molecular function	heme binding Inferred from electronic annotation. Source: InterPro oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AHSP	Q9NZD4	1	EBI-714680,EBI-720250
HBB	P68871	1	EBI-714680,EBI-715554

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.17 Ref.18 Ref.19 Ref.20

Chain

2 – 142

141

Hemoglobin subunit alpha

PRO_0000052653

Sites

Metal binding

Iron (heme distal ligand)

Metal binding

Iron (heme proximal ligand)

Site

Not glycated

Site

Not glycated

Site

Not glycated

Site

Not glycated

Site

100

Not glycated

Amino acid modifications

Modified residue

N6-acetyllysine Ref.25

Modified residue

Phosphotyrosine Ref.23

Modified residue

Phosphotyrosine Ref.23

Glycosylation

N-linked (Glc) (glycation) Ref.22

Glycosylation

N-linked (Glc) (glycation) Ref.22

Glycosylation

N-linked (Glc) (glycation) Ref.22

Glycosylation

N-linked (Glc) (glycation) Ref.22

Natural variations

Natural variant

V → E in Thionville; O(2) affinity down. Ref.63

VAR_002719

Natural variant

L → R in ChongQing; O(2) affinity up. dbSNP rs36030576. Ref.36

VAR_002720

Natural variant

A → D in J-Toronto. dbSNP rs34090856.

VAR_002721

Natural variant

A → P in Karachi. dbSNP rs34751764.

VAR_002722

Natural variant

D → A in Sawara; O(2) affinity up. dbSNP rs33986902. Ref.57

VAR_002723

Natural variant

D → G in Swan River. Ref.62

VAR_002724

Natural variant

D → N in Dunn; O(2) affinity up. dbSNP rs33961916.

VAR_002725

Natural variant

D → V in Ferndown; O(2) affinity up.

VAR_002726

Natural variant

D → Y in Woodville; O(2) affinity up. Ref.68

VAR_002727

Natural variant

K → E in Kurosaki. dbSNP rs34817956. Ref.50

VAR_002728

Natural variant

N → T in Broomfield.

VAR_038149

Natural variant

V → F: dbSNP rs1799896.

VAR_014605

Natural variant

K → E in Anantharaj.

VAR_002729

Natural variant

A → D in J-Paris 1/J-Aljezur. dbSNP rs35615982.

VAR_002730

Natural variant

A → P in Ravenscourt Park; causes alpha-thalassemia. dbSNP rs35331909.

VAR_038150

Natural variant

W → R in Evanston; O(2) affinity up. dbSNP rs33964317.

VAR_002731

Natural variant

G → R in Ottawa/Siam. dbSNP rs35816645.

VAR_002732

Natural variant

K → M in Harbin; slightly unstable. dbSNP rs35210126. Ref.36

VAR_002733

Natural variant

K → N in Beijing. dbSNP rs33923844.

VAR_002734

Natural variant

G → D in Al-Ain Abu Dhabi. dbSNP rs35993097. Ref.31

VAR_002735

Natural variant

G → R in Handsworth. dbSNP rs34504387.

VAR_002736

Natural variant

A → D in J-Kurosh.

VAR_002737

Natural variant

A → E in J-Tashikuergan. dbSNP rs35628685.

VAR_002738

Natural variant

H → Q in Le Lamentin. dbSNP rs41525149.

VAR_002739

Natural variant

H → R in Hobart. dbSNP rs33943087. Ref.46

VAR_002740

Natural variant

A → D in J-Nyanza. dbSNP rs11548605.

VAR_002741

Natural variant

A → P in Fontainebleau. dbSNP rs34324664.

VAR_002742

Natural variant

G → D in J-Medellin. dbSNP rs34608326.

VAR_002743

Natural variant

E → G in Reims; slightly unstable. dbSNP rs33939421.

VAR_002744

Natural variant

E → K in Chad.

VAR_002745

Natural variant

Y → H in Luxembourg; unstable.

VAR_002746

Natural variant

A → E in Shenyang; unstable. Ref.58

VAR_002747

Natural variant

A → V in Campinas. Ref.72

VAR_025387

Natural variant

E → D in Hekinan.

VAR_002748

Natural variant

E → G in Fort Worth.

VAR_002749

Natural variant

E → V in Spanish town. Ref.40

VAR_002750

Natural variant

E → K in O-Padova.

VAR_002751

Natural variant

R → K Causes alpha-thalassemia. Ref.5

VAR_025002

Natural variant

R → S in Prato; unstable.

VAR_002752

Natural variant

L → R in Queens/Ogi.

VAR_002753

Natural variant

P → PE in Catonsville. Ref.30

VAR_002755

Natural variant

P → R in Bourmedes.

VAR_002754

Natural variant

K → M in Kanagawa; O(2) affinity up. Ref.48

VAR_002756

Natural variant

T → S in Miyano; O(2) affinity up.

VAR_002757

Natural variant

F → L in Hirosaki; unstable.

VAR_002758

Natural variant

P → L in Milledgeville; O(2) affinity up. dbSNP rs41514946.

VAR_002759

Natural variant

P → R in Kawachi; O(2) affinity up.

VAR_002760

Natural variant

H → Q in Bari.

VAR_002761

Natural variant

H → R in Fort de France; O(2) affinity up. Ref.40

VAR_002762

Natural variant

D → A in Cordele; unstable.

VAR_002763

Natural variant

D → G in Umi/Michigan; unstable.

VAR_002764

Natural variant

D → H in Hasharon/Sinai; unstable. Ref.45

VAR_002765

Natural variant

D → Y in Kurdistan. Ref.49

VAR_002766

Natural variant

L → R in Montgomery. Ref.53

VAR_002767

Natural variant

S → R in Savaria.

VAR_002768

Natural variant

H → R in Aichi; slightly unstable.

VAR_002769

Natural variant

G → D in J-Abidjan.

VAR_002770

Natural variant

G → R in Russ.

VAR_002771

Natural variant

A → D in J-Rovigo; unstable.

VAR_002772

Natural variant

Q → R in Hikoshima/Shimonoseki.

VAR_002773

Natural variant

K → R in Port Huron. Ref.56

VAR_002774

Natural variant

K → T in Thailand.

VAR_002775

Natural variant

G → R in L-Persian Gulf.

VAR_002776

Natural variant

H → Q in Boghe. Ref.71

VAR_025388

Natural variant

H → Y in M-Boston/M-Osaka; O(2) affinity down.

VAR_002777

Natural variant

G → D in Adana; unstable; causes alpha-thalassemia. dbSNP rs28928878.

VAR_002778

Natural variant

G → V in Tottori; unstable.

VAR_002779

Natural variant

K → N in Zambia. dbSNP rs28928887.

VAR_002780

Natural variant

Missing in Clinic; unstable; causes alpha-thalassemia.

VAR_002781

Natural variant

K → N in J-Buda. Ref.34

VAR_002782

Natural variant

K → T in J-Anatolia.

VAR_002783

Natural variant

V → M in Evans; unstable. Ref.11 Ref.39

VAR_002784

Natural variant

A → D in Pontoise; unstable.

VAR_002785

Natural variant

D → Y in Persepolis.

VAR_002786

Natural variant

N → K in G-Philadelphia. dbSNP rs1060339. Ref.12

VAR_002787

Natural variant

A → E in J-Habana.

VAR_002788

Natural variant

A → V in Ozieri.

VAR_002789

Natural variant

H → R in Daneskgah-Teheran.

VAR_002790

Natural variant

D → A in Lille.

VAR_002791

Natural variant

D → G in Chapel Hill.

VAR_002792

Natural variant

D → N in G-Pest. Ref.34

VAR_002793

Natural variant

D → A in Duan.

VAR_002794

Natural variant

D → H in Q-Iran.

VAR_002795

Natural variant

M → K in Noko.

VAR_002796

Natural variant

M → T in Aztec.

VAR_002797

Natural variant

P → R in Guizhou.

VAR_002798

Natural variant

N → H in Davenport. Ref.38

VAR_002799

Natural variant

N → K in Stanleyville-2.

VAR_002800

Natural variant

A → G in Singapore.

VAR_012662

Natural variant

L → R in Ann Arbor; unstable.

VAR_002801

Natural variant

S → C in Nigeria.

VAR_002802

Natural variant

A → D in Garden State.

VAR_002803

Natural variant

S → R in Etobicoke; O(2) affinity up.

VAR_002804

Natural variant

D → V in Inkster; O(2) affinity up. Ref.47

VAR_002805

Natural variant

D → Y in Atago; O(2) affinity up. Ref.32

VAR_002806

Natural variant

L → R in Moabit; unstable.

VAR_002807

Natural variant

H → N in Auckland; unstable. Ref.33

VAR_002808

Natural variant

H → R in Iwata; unstable.

VAR_002809

Natural variant

A → S in Loire; O(2) affinity up.

VAR_002810

Natural variant

K → M in Handa; O(2) affinity up. Ref.44

VAR_002811

Natural variant

L → F: dbSNP rs17407508.

VAR_049272

Natural variant

L → P in Port Phillip; unstable. dbSNP rs17407508.

VAR_002812

Natural variant

R → Q in J-Cape Town; O(2) affinity up.

VAR_002813

Natural variant

R → W in Cemenelum; O(2) affinity up. Ref.35

VAR_020775

Natural variant

D → A in Bassett; markedly reduced oxygen affinity. Ref.73

VAR_025389

Natural variant

D → Y in Setif; unstable.

VAR_002814

Natural variant

P → A in Denmark Hill; O(2) affinity up.

VAR_002815

Natural variant

P → T in Godavari; O(2) affinity up. Ref.41

VAR_002816

Natural variant

N → K in Dallas; O(2) affinity up.

VAR_002817

Natural variant

100

K → E in Turriff. Ref.65

VAR_002818

Natural variant

103

S → R in Manitoba; slightly unstable. dbSNP rs41344646.

VAR_002819

Natural variant

104

H → R in Contaldo; unstable.

VAR_002820

Natural variant

104

H → Y in Charolles. Ref.71

VAR_025390

Natural variant

110

L → R in Suan-Dok; unstable; causes alpha-thalassemia. Ref.59

VAR_002821

Natural variant

111

A → D in Petah Tikva; unstable; causes alpha-thalassemia. Ref.54

VAR_002822

Natural variant

113

H → D in Hopkins-II; unstable.

VAR_002823

Natural variant

114

L → H in Twin Peaks.

VAR_002824

Natural variant

115

P → L in Nouakchott.

VAR_002825

Natural variant

115

P → R in Chiapas.

VAR_002826

Natural variant

115

P → S in Melusine. Ref.52

VAR_002827

Natural variant

116

A → D in J-Tongariki.

VAR_002828

Natural variant

117

E → A in Ube-4.

VAR_002829

Natural variant

117

E → EHLPAE in Zaire.

VAR_002830

Natural variant

118

F → FI in Phnom Penh. Ref.55

VAR_002831

Natural variant

119

T → TEFT in Grady.

VAR_002832

Natural variant

121

A → E in J-Meerut/J-Birmingham. Ref.51

VAR_002833

Natural variant

122

V → M in Owari.

VAR_002834

Natural variant

123

H → Q in Westmead. Ref.67

VAR_002835

Natural variant

126

L → P in Quong Sze; causes alpha-thalassemia.

VAR_002836

Natural variant

126

L → R in Plasencia; family with moderate microcytosis and hypochromia. Ref.74

VAR_025391

Natural variant

127

D → G in West One. Ref.72

VAR_025392

Natural variant

127

D → V in Fukutomi; O(2) affinity up.

VAR_002837

Natural variant

127

D → Y in Monteriore; O(2) affinity up.

VAR_002838

Natural variant

128

K → N in Jackson.

VAR_002839

Natural variant

130

L → P in Tunis-Bizerte; unstable; causes alpha-thalassemia. Ref.64

VAR_002840

Natural variant

131

A → D in Yuda; O(2) affinity down. Ref.69

VAR_002842

Natural variant

131

A → P in Sun Prairie; unstable. Ref.61

VAR_002841

Natural variant

132

S → P in Questembert; highly unstable; causes alpha-thalassemia.

VAR_002843

Natural variant

134

S → R in Val de Marne; O(2) affinity up. Ref.66

VAR_002844

Natural variant

136

V → E in Pavie.

VAR_002845

Natural variant

137

L → M in Chicago.

VAR_002846

Natural variant

137

L → P in Bibba; unstable; causes alpha-thalassemia.

VAR_002847

Natural variant

137

L → R in Toyama. Ref.60

VAR_035242

Natural variant

139

S → P in Attleboro; O(2) affinity up.

VAR_002848

Natural variant

140

K → E in Hanamaki; O(2) affinity up. Ref.43

VAR_002849

Natural variant

140

K → T in Tokoname; O(2) affinity up.

VAR_002850

Natural variant

141

Y → H in Rouen/Ethiopia; O(2) affinity up. Ref.21

VAR_002851

Natural variant

R → C in Nunobiki; O(2) affinity up.

VAR_002852

Natural variant

R → H in Suresnes; O(2) affinity up.

VAR_002854

Natural variant

R → L in Legnano; O(2) affinity up.

VAR_002853

Natural variant

R → P in Singapore.

VAR_002855

Experimental info

Sequence conflict

N → H in BAD97112. Ref.13

Secondary structure

142

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P69905-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 15E13666573BBBAE
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FASTA

142

15,258

        10         20         30         40         50         60 
MVLSPADKTN VKAAWGKVGA HAGEYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG 

        70         80         90        100        110        120 
KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHLPAEFTP 

       130        140 
AVHASLDKFL ASVSTVLTSK YR

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The 3' untranslated regions of the duplicated human alpha-globin genes are unexpectedly divergent." Michelson A.M., Orkin S.H. Cell 22:371-377(1980) [PubMed: 7448866] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1).
[2]	"Nucleotide sequence of the coding portion of human alpha globin messenger RNA." Wilson J.T., Wilson L.B., Reddy V.B., Cavallesco C., Ghosh P.K., Deriel J.K., Forget B.G., Weissman S.M. J. Biol. Chem. 255:2807-2815(1980) [PubMed: 6244294] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (HBA2).
[3]	"Cloning and complete nucleotide sequence of human 5'-alpha-globin gene." Liebhaber S.A., Goossens M.J., Kan Y.W. Proc. Natl. Acad. Sci. U.S.A. 77:7054-7058(1980) [PubMed: 6452630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2).
[4]	"Mutation in an intervening sequence splice junction in man." Orkin S.H., Goff S.C., Hechtman R.L. Proc. Natl. Acad. Sci. U.S.A. 78:5041-5045(1981) [PubMed: 6946451] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Alpha2(CD31 AGG-->AAG, Arg-->Lys) causing non-deletional alpha-thalassemia in a Chinese family with HbH disease." Zhao Y., Xu X. Haematologica 86:541-542(2001) [PubMed: 11410421] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-32.
[6]	"Rapid detection of the common alpha-thalassemia-2 determinants by PCR assay." Zhao Y., Zhong M., Liu Z., Xu X. Zhonghua Yi Xue Yi Chuan Xue Za Zhi 18:216-218(2001) [PubMed: 11402454] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1).
[7]	"A regulatory SNP causes a human genetic disease by creating a new transcriptional promoter." De Gobbi M., Viprakasit V., Hughes J.R., Fisher C., Buckle V.J., Ayyub H., Gibbons R.J., Vernimmen D., Yoshinaga Y., de Jong P., Cheng J.-F., Rubin E.M., Wood W.G., Bowden D., Higgs D.R. Science 312:1215-1217(2006) [PubMed: 16728641] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALPHA-1 AND ALPHA-2).
[8]	"Rapid sequencing of mRNA of the human alpha two globin, directly isolated from reticulocytes in whole blood." Kutlar F., Leithner C., Kutlar A. Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (HBA2). Tissue: Blood.
[9]	"cDNA sequencing of human alpha one globin mRNA, the 3'untranslated region is different than alpha two globin." Kutlar F., Leithner C., Kutlar A. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (HBA1). Tissue: Blood.
[10]	"An alpha chain variant 'Hemoglobin J-Toronto (Cd.5 /Ala to Asp)' mutation was detected on the alpha-1 globin mRNA by sequencing of cDNA." Kutlar F., Holley L., Leithner C., Kutlar A. Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Blood.
[11]	"Unstable Hb 'Evans' (GTG->ATG/Val 62 Met) was detected on the alpha-2 globin gene of an Hispanic girl." Kutlar F., Elam D., Hoff J.V., Holley L., Kutlar A. Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2), VARIANT EVANS MET-63. Tissue: Blood.
[12]	"Hb G-Philadelphia (Alpha,Codon 68;AAC>AAG/Asn>Lys)in black is detected on a chromosome that carries alpha 3.7 kb deletion showed completely normal alpha-2 globin gene sequence." Kutlar F., Davis D.H., Nechtman J., Elam D. Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2), VARIANT G-PHILADELPHIA LYS-69.
[13]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thymus.
[14]	"Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16." Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R. Hum. Mol. Genet. 10:339-352(2001) [PubMed: 11157797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HBA1 AND HBA2).
[15]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. Pennacchio L.A. Nature 432:988-994(2004) [PubMed: 15616553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HBA1 AND HBA2).
[16]	"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] (HBA1 AND HBA2). Tissue: Bone marrow, Brain, Lung and Spleen.
[17]	"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 2-142.
[18]	"The structure of human hemoglobin: IV. The chymotryptic digestion of the alpha chain of human hemoglobin." Hill R.J., Konigsberg W. J. Biol. Chem. 237:3151-3156(1962) [PubMed: 13954546] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-142.
[19]	"The amino acid sequence of the alpha chain of human fetal hemoglobin." Schroeder W.A., Shelton J.R., Shelton J.B., Cormick J. Biochemistry 2:1353-1357(1963) [PubMed: 14093912] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-142.
[20]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-32. Tissue: Platelet.
[21]	"Hb Ethiopia or alpha 2(140)(HC2)Tyr----His beta 2." Webber B.B., Wilson J.B., Gu L.-H., Huisman T.H.J. Hemoglobin 16:441-443(1992) [PubMed: 1428951] [Abstract] Cited for: PROTEIN SEQUENCE OF 128-142, VARIANT ETHIOPIA HIS-141. Tissue: Umbilical cord blood.
[22]	"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-8; LYS-17; LYS-41 AND LYS-62, LACK OF GLYCATION AT LYS-12; LYS-57; LYS-61; LYS-91 AND LYS-100.
[23]	"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-25 AND TYR-43, MASS SPECTROMETRY.
[24]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[25]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17, MASS SPECTROMETRY.
[26]	"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.
[27]	"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).
[28]	"A third quaternary structure of human hemoglobin A at 1.7-A resolution." Silva M.M., Rogers P.H., Arnone A. J. Biol. Chem. 267:17248-17256(1992) [PubMed: 1512262] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF LIGANDED R2 STATE.
[29]	"Crystal structure of a human embryonic haemoglobin: the carbonmonoxy form of Gower II (alpha2 epsilon2) haemoglobin at 2.9-A resolution." Sutherland-Smith A.J., Baker H.M., Hofmann O.M., Brittain T., Baker E.N. J. Mol. Biol. 280:475-484(1998) [PubMed: 9665850] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF HB GOWER-2.
[30]	"Accommodation of insertions in helices: the mutation in hemoglobin Catonsville (Pro 37 alpha-Glu-Thr 38 alpha) generates a 3(10)-->alpha bulge." Kavanaugh J.S., Moo-Penn W.F., Arnone A. Biochemistry 32:2509-2513(1993) [PubMed: 8448109] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF VARIANT HB CATONSVILLE GLU-38 INS.
[31]	"HB Al-Ain Abu Dhabi [alpha 18(A16)Gly-->Asp]: a new hemoglobin variant discovered in an Emiratee family." Abbes S., M'Rad A., Fitzgerald P.A., Dormer P., Blouquit Y., Kister J., Galacteros F., Wajcman H. Hemoglobin 16:355-362(1992) [PubMed: 1428941] [Abstract] Cited for: VARIANT AL-AIN ABU DHABI ASP-19.
[32]	"Hemoglobin Atago (alpha2-85 Tyr beta-2) a new abnormal human hemoglobin found in Nagasaki. Biochemical studies on hemoglobins and myoglobins. VI." Fujiwara N., Maekawa T., Matsuda G. Int. J. Protein Res. 3:35-39(1971) [PubMed: 5115619] [Abstract] Cited for: VARIANT ATAGO TYR-86.
[33]	"Hb Auckland [alpha 87(F8) His-->Asn]: a new mutation of the proximal histidine identified by electrospray mass spectrometry." Brennan S.O., Matthews J.R. Hemoglobin 21:393-403(1997) [PubMed: 9322075] [Abstract] Cited for: VARIANT AUCKLAND ASN-88.
[34]	"Structural characterizations of hemoglobins J-Buda (alpha 61 (E10) Lys-to-Asn) and G-Pest (alpha 74 (EF3) Asp-to-Asn)." Brimhall B.J., Duerst M., Hollan S.R., Stenzel P., Szelenyi J., Jones R.T. Biochim. Biophys. Acta 336:344-360(1974) Cited for: VARIANTS J-BUDA ASN-62 AND G-PEST ASN-75.
[35]	"Hb Cemenelum [alpha 92 (FG4) Arg-->Trp]: a hemoglobin variant of the alpha 1/beta 2 interface that displays a moderate increase in oxygen affinity." Wajcman H., Kister J., M'Rad A., Soummer A.M., Galacteros F. Ann. Hematol. 68:73-76(1994) [PubMed: 8148419] [Abstract] Cited for: VARIANT CEMENELUM TRP-93.
[36]	"Hemoglobin Chongqing [alpha 2(NA2)Leu-->Arg] and hemoglobin Harbin [alpha 16(A14)Lys-->Met] found in China." Zeng Y.-T., Huang S.-Z., Qiu X.-K., Cheng G.-C., Ren Z.-R., Jin Q.-C., Chen C.-Y., Jiao C.-T., Tang Z.-G., Liu R.-H., Bao X.-H., Zeng L.-Z., Duan Y.-Q., Zhang G.-Y. Hemoglobin 8:569-581(1984) [PubMed: 6526652] [Abstract] Cited for: VARIANTS CHONGQING ARG-3 AND HARBIN MET-17.
[37]	"Alpha-thalassaemia due to a single codon deletion in the alpha 1-globin gene. Computational structural analysis of the new alpha-chain variant." Ayala S., Colomer D., Gelpi J.L., Corron J.L.V. Hum. Mutat. 11:412-412(1998) [PubMed: 10206681] [Abstract] Cited for: VARIANT CLINIC LYS-61 DEL.
[38]	"Hb Davenport or alpha 2(78)(EF7)Asn-->His beta 2." Wilson J.B., Webber B.B., Plaseska D., de Alarcon P.A., McMillan S.K., Huisman T.H.J. Hemoglobin 14:599-605(1990) [PubMed: 2101836] [Abstract] Cited for: VARIANT DAVENPORT HIS-79.
[39]	"Hb Evans or alpha 262(E11)Val-->Met beta 2; an unstable hemoglobin causing a mild hemolytic anemia." Wilson J.B., Webber B.B., Kutlar A., Reese A.L., McKie V.C., Lutcher C.L., Felice A.E., Huisman T.H.J. Hemoglobin 13:557-566(1989) [PubMed: 2606724] [Abstract] Cited for: VARIANT EVANS MET-63.
[40]	"Locus assignment of two alpha-globin structural mutants from the Caribbean basin: alpha Fort de France (alpha 45 Arg) and alpha Spanish Town (alpha 27 Val)." Cash F.E., Monplaisir N., Goossens M., Liebhaber S.A. Blood 74:833-835(1989) [PubMed: 2752146] [Abstract] Cited for: VARIANTS SPANISH TOWN VAL-28 AND FORT DE FRANCE ARG-46.
[41]	"Hb Godavari [alpha 95(G2)Pro-->Thr]: a neutral amino acid substitution in the alpha 1 beta 2 interface that modifies the electrophoretic mobility of hemoglobin." Wajcman H., Kister J., Riou J., Galacteros F., Girot R., Maier-Redelsperger M., Nayudu N.V.S., Giordano P.C. Hemoglobin 22:11-22(1998) [PubMed: 9494044] [Abstract] Cited for: VARIANT GODAVARI THR-96.
[42]	"Hemoglobin Grady: the first example of a variant with elongated chains due to an insertion of residues." Huisman T.H.J., Wilson J.B., Gravely M., Hubbard M. Proc. Natl. Acad. Sci. U.S.A. 71:3270-3273(1974) [PubMed: 4528583] [Abstract] Cited for: VARIANT GRADY GLU-PHE-THR-119 INS.
[43]	"A new alpha chain variant, Hb Hanamaki or alpha 2(139)(HC1)Lys-->Glu beta 2, found in a Japanese family." Orisaka M., Tajima T., Harano T., Harano K., Kushida Y., Imai K. Hemoglobin 16:67-71(1992) [PubMed: 1634363] [Abstract] Cited for: VARIANT HANAMAKI GLU-140.
[44]	"HB Handa [alpha 90 (FG 2) Lys replaced by Met]: structure and biosynthesis of a new slightly higher oxygen affinity variant." Harano T., Harano K., Shibata S., Ueda S., Imai K., Seki M. Hemoglobin 6:379-389(1982) [PubMed: 6815131] [Abstract] Cited for: VARIANT HANDA MET-91.
[45]	"Hemoglobin Hasharon (alpha-2-47 his(CD5)beta-2): a hemoglobin found in low concentration." Charache S., Mondzac A.M., Gessner U. J. Clin. Invest. 48:834-847(1969) [PubMed: 5780195] [Abstract] Cited for: VARIANT HASHARON HIS-48.
[46]	"Hemoglobin Hobart or alpha 20(Bl)His-->Arg: a new alpha chain hemoglobin variant." Fleming P.J., Sumner D.R., Wyatt K., Hughes W.G., Melrose W.D., Jupe D.M.D., Baikie M.J. Hemoglobin 11:211-220(1987) [PubMed: 3654264] [Abstract] Cited for: VARIANT HOBART ARG-21.
[47]	"Haemoglobin inkster (alpha2 85aspartic acid leads to valine beta2) coexisting with beta-thalassaemia in a Caucasian family." Reed R.E., Winter W.P., Rucknagel D.L. Br. J. Haematol. 26:475-484(1974) [PubMed: 4212045] [Abstract] Cited for: VARIANT INKSTER VAL-86.
[48]	"Hb Kanagawa [alpha 40(C5)Lys-->Met]: a new alpha chain variant with an increased oxygen affinity." Miyashita H., Hashimoto K., Mohri H., Ohokubo T., Harano T., Harano K., Imai K. Hemoglobin 16:1-10(1992) [PubMed: 1634355] [Abstract] Cited for: VARIANT KANAGAWA MET-41.
[49]	"Hb Kurdistan [alpha 47(CE5)Asp-->Tyr], a new alpha chain variant in combination with beta (0)-thalassemia." Giordano P.C., Harteveld C.L., Streng H., Oosterwijk J.C., Heister J.G.A.M., Amons R., Bernini L.F. Hemoglobin 18:11-18(1994) [PubMed: 8195005] [Abstract] Cited for: VARIANT KURDISTAN TYR-48.
[50]	"Hb Kurosaki [alpha 7(A5)Lys-->Glu]: a new alpha chain variant found in a Japanese woman." Harano T., Harano K., Imai K., Murakami T., Matsubara H. Hemoglobin 19:197-201(1995) [PubMed: 7558876] [Abstract] Cited for: VARIANT KUROSAKI GLU-8.
[51]	"A case of HB J-Meerut (or Hb J-Birmingham) [alpha 120(H3)Ala-->Glu]." Yalcin A., Avcu F., Beyan C., Guergey A., Ural A.U. Hemoglobin 18:433-435(1994) [PubMed: 7713747] [Abstract] Cited for: VARIANT J-MEERUT/J-BIRMINGHAM GLU-121.
[52]	"Hb Melusine [alpha 114(GH2)Pro-->Ser]: a new neutral hemoglobin variant." Wacjman H., Klames G., Groff P., Prome D., Riou J., Galacteros F. Hemoglobin 17:397-405(1993) [PubMed: 8294199] [Abstract] Cited for: VARIANT MELUSINE SER-115.
[53]	"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 MONTGOMERY ARG-49.
[54]	"Hemoglobin Petah Tikva (alpha 110 Ala replaced by Asp): a new unstable variant with alpha-thalassemia-like expression." Honig G.R., Shamsuddin M., Zaizov R., Steinherz M., Solar I., Kirschman C. Blood 57:705-711(1981) [PubMed: 7470621] [Abstract] Cited for: VARIANT PETAH TIKVA ASP-111.
[55]	"Hemoglobin Phnom Penh [alpha117Phe(H1)-Ile-alpha118Thr(H2)]; evidence for a hotspot for insertion of residues in the third exon of the alpha1-globin gene." Wajcman H., Prehu M.O., Prehu C., Blouquit Y., Prome D., Galacteros F. Hum. Mutat. Suppl. 1:S20-S22(1998) [PubMed: 9452028] [Abstract] Cited for: VARIANT PHNOM PENH ILE-118 INS.
[56]	"Hb Port Huron [alpha 56 (E5)Lys-->Arg]: a new alpha chain variant." Zwerdling T., Williams S., Nasr S.A., Rucknagel D.L. Hemoglobin 15:381-391(1991) [PubMed: 1802882] [Abstract] Cited for: VARIANT PORT HURON ARG-57.
[57]	"Hemoglobin Sawara: alpha 6(A4) aspartic acid leads to alanine." Sumida I., Ohta Y., Imamura T., Yanase T. Biochim. Biophys. Acta 322:23-26(1973) [PubMed: 4744335] [Abstract] Cited for: VARIANT SAWARA ALA-7.
[58]	"Hb Shenyang (alpha 26 (B7) Ala replaced by Glu): a new unstable variant found in China." Zeng Y.-T., Huang S.-Z., Zhou X., Qiu X.-K., Dong Q., Li M., Bai J. Hemoglobin 6:625-628(1982) [PubMed: 7161109] [Abstract] Cited for: VARIANT SHENYANG GLU-27.
[59]	"Hemoglobin Suan-Dok (alpha 2 109 (G16) Leu replaced by Arg beta 2): an unstable variant associated with alpha-thalassemia." Sanguansermsri T., Matragoon S., Changloah L., Flatz G. Hemoglobin 3:161-174(1979) [PubMed: 478977] [Abstract] Cited for: VARIANT SUAN-DOK ARG-110.
[60]	"Hyperunstable hemoglobin Toyama [alpha 2 136(H19)Leu----Arg beta 2]: detection and identification by in vitro biosynthesis with radioactive amino acids." Ohba Y., Yamamoto K., Hattori Y., Kawata R., Miyaji T. Hemoglobin 11:539-556(1987) [PubMed: 2833478] [Abstract] Cited for: INVOLVEMENT IN HEINZ BODY ANEMIAS, VARIANT TOYAMA ARG-137.
[61]	"Hb Sun Prairie or alpha(2)130(H13)Ala-->Pro beta 2, a new unstable variant occurring in low quantities." Harkness M., Harkness D.R., Kutlar F., Kutlar A., Wilson J.B., Webber B.B., Codrington J.F., Huisman T.H.J. Hemoglobin 14:479-489(1990) [PubMed: 2079430] [Abstract] Cited for: VARIANT SUN PRAIRIE PRO-131.
[62]	"HB Swan River [alpha 6(A4)Asp-->Gly] observed in a Japanese man." Harano T., Harano K., Imai K., Terunuma S. Hemoglobin 20:75-78(1996) [PubMed: 8745434] [Abstract] Cited for: VARIANT SWAN RIVER GLY-7.
[63]	"Hemoglobin Thionville. An alpha-chain variant with a substitution of a glutamate for valine at NA-1 and having an acetylated methionine NH2 terminus." Vasseur C., Blouquit Y., Kister J., Prome D., Kavanaugh J.S., Rogers P.H., Guillemin C., Arnone A., Galacteros F., Poyart C., Rosa J., Wajcman H. J. Biol. Chem. 267:12682-12691(1992) [PubMed: 1618774] [Abstract] Cited for: VARIANT THIONVILLE GLU-2.
[64]	"Haemoglobin Tunis-Bizerte: a new alpha 1 globin 129 Leu-->Pro unstable variant with thalassaemic phenotype." Darbellay R., Mach-Pascual S., Rose K., Graf J., Beris P. Br. J. Haematol. 90:71-76(1995) [PubMed: 7786798] [Abstract] Cited for: VARIANT TUNIS-BIZERTE PRO-130.
[65]	"A new alpha chain variant, Hb Turriff [alpha 99(G6)Lys-->Glu]: the interference of abnormal hemoglobins in Hb A1c determination." Langdown J.V., Davidson R.J., Williamson D. Hemoglobin 16:11-17(1992) [PubMed: 1634357] [Abstract] Cited for: VARIANT TURRIFF GLU-100.
[66]	"Hb Val de Marne [alpha 133(H16)Ser-->Arg]: a new hemoglobin variant with moderate increase in oxygen affinity." Wacjman H., Kister J., M'Rad A., Marden M.C., Riou J., Galacteros F. Hemoglobin 17:407-417(1993) [PubMed: 8294200] [Abstract] Cited for: VARIANT VAL DE MARNE ARG-134.
[67]	"Hb Westmead: an alpha 2-globin gene mutation detected by polymerase chain reaction and Stu I cleavage." Jiang N.H., Liang S., Wen X.J., Liang R., Su C., Tang Z. Hemoglobin 15:291-295(1991) [PubMed: 1686260] [Abstract] Cited for: VARIANT WESTMEAD GLN-123.
[68]	"Hemoglobin Woodville: alpha (2)6(A4) aspartic acid-->tyrosine." Como P.F., Barber S., Sage R.E., Kronenberg H. Hemoglobin 10:135-141(1986) [PubMed: 3754246] [Abstract] Cited for: VARIANT WOODVILLE TYR-7.
[69]	"Hb Yuda or alpha 130(H13)Ala-->Asp; a new alpha chain variant with low oxygen affinity." Fujisawa K., Hattori Y., Ohba Y., Ando S. Hemoglobin 16:435-439(1992) [PubMed: 1428950] [Abstract] Cited for: VARIANT YUDA ASP-131.
[70]	"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: VARIANT ZAIRE HIS-LEU-PRO-ALA-GLU-117 INS.
[71]	"Two new alpha chain variants: Hb Boghe [alpha58(E7)His-->Gln, alpha2], a variant on the distal histidine, and Hb CHarolles [alpha103(G10)His-Tyr, alpha1]." Lacan P., Francina A., Souillet G., Aubry M., Couprie N., Dementhon L., Becchi M. Hemoglobin 23:345-352(1999) [PubMed: 10569723] [Abstract] Cited for: VARIANT BOGHE GLN-59, VARIANT CHAROLLES TYR-104.
[72]	"Screening for mutations in human alpha-globin genes by nonradioactive single-strand conformation polymorphism." Jorge S.B., Melo M.B., Costa F.F., Sonati M.F. Braz. J. Med. Biol. Res. 36:1471-1474(2003) [PubMed: 14576901] [Abstract] Cited for: VARIANT CAMPINAS VAL-27, VARIANT WEST ONE GLY-127.
[73]	"Characterization of hemoglobin bassett (alpha94Asp-->Ala), a variant with very low oxygen affinity." Abdulmalik O., Safo M.K., Lerner N.B., Ochotorena J., Daikhin E., Lakka V., Santacroce R., Abraham D.J., Asakura T. Am. J. Hematol. 77:268-276(2004) [PubMed: 15495251] [Abstract] Cited for: VARIANT BASSETT ALA-95, CHARACTERIZATION OF VARIANT BASSETT ALA-95.
[74]	"A novel mutation of the alpha2-globin causing alpha(+)-thalassemia: Hb Plasencia [alpha125(H8)Leu-->Arg (alpha2)." Martin G., Villegas A., Gonzalez F.A., Ropero P., Hojas R., Polo M., Mateo M., Salvador M., Benavente C. Hemoglobin 29:113-117(2005) [PubMed: 15921163] [Abstract] Cited for: VARIANT PLASENCIA ARG-126.
+	Additional computationally mapped references.

Web resources

HbVar

Human hemoglobin variants and thalassemias

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

J00153 Genomic DNA. Translation: AAB59407.1.
J00153 Genomic DNA. Translation: AAB59408.1.
V00491 Genomic DNA. Translation: CAA23750.1.
V00493 mRNA. Translation: CAA23752.1.
V00488 Genomic DNA. Translation: CAA23748.1.
V00516 Genomic DNA. Translation: CAA23774.1.
AF230076 Genomic DNA. Translation: AAF72612.1.
AF525460 Genomic DNA. Translation: AAM83102.1.
DQ431198 Genomic DNA. Translation: ABD95910.1.
DQ431198 Genomic DNA. Translation: ABD95911.1.
AF097635 mRNA. Translation: AAC72839.1.
AF105974 mRNA. Translation: AAC97373.1.
AF349571 mRNA. Translation: AAK37554.1.
AF536204 Genomic DNA. Translation: AAN04486.1.
DQ499017 Genomic DNA. Translation: ABF56144.1.
DQ499018 Genomic DNA. Translation: ABF56145.1.
AK223392 mRNA. Translation: BAD97112.1. Different initiation.
AE006462 Genomic DNA. Translation: AAK61215.1.
AE006462 Genomic DNA. Translation: AAK61216.1.
Z84721 Genomic DNA. Translation: CAB06554.1.
Z84721 Genomic DNA. Translation: CAB06555.1.
BC005931 mRNA. Translation: AAH05931.1.
BC008572 mRNA. Translation: AAH08572.1.
BC032122 mRNA. Translation: AAH32122.1.
BC050661 mRNA. Translation: AAH50661.1.
BC101846 mRNA. Translation: AAI01847.1.
BC101848 mRNA. Translation: AAI01849.1.

IPI

IPI00410714.

PIR

HAHU. A90807.
HACZP. C93303.
HACZ. I58217.

RefSeq

NP_000508.1.
NP_000549.1.

UniGene

Hs.449630
Hs.654744

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A00	X-ray	2.00	A/C	2-142	[»]
1A01	X-ray	1.80	A/C	2-142	[»]
1A0U	X-ray	2.14	A/C	2-142	[»]
1A0Z	X-ray	2.00	A/C	2-142	[»]
1A3N	X-ray	1.80	A/C	2-142	[»]
1A3O	X-ray	1.80	A/C	2-142	[»]
1A9W	X-ray	2.90	A/C	2-142	[»]
1ABW	X-ray	2.00	A	2-142	[»]
1ABY	X-ray	2.60	A	2-142	[»]
1AJ9	X-ray	2.20	A	2-142	[»]
1B86	X-ray	2.50	A/C	2-142	[»]
1BAB	X-ray	1.50	A/C	3-142	[»]
1BBB	X-ray	1.70	A/C	2-142	[»]
1BIJ	X-ray	2.30	A/C	2-142	[»]
1BUW	X-ray	1.90	A/C	2-142	[»]
1BZ0	X-ray	1.50	A/C	2-142	[»]
1BZ1	X-ray	1.59	A/C	2-142	[»]
1BZZ	X-ray	1.59	A/C	3-142	[»]
1C7B	X-ray	1.80	A/C	3-142	[»]
1C7C	X-ray	1.80	A	2-142	[»]
1C7D	X-ray	1.80	A	2-142	[»]
1CLS	X-ray	1.90	A/C	2-142	[»]
1CMY	X-ray	3.00	A/C	2-142	[»]
1COH	X-ray	2.90	A/C	2-142	[»]
1DKE	X-ray	2.10	A/C	2-142	[»]
1DXT	X-ray	1.70	A/C	2-142	[»]
1DXU	X-ray	1.70	A/C	2-142	[»]
1DXV	X-ray	1.70	A/C	2-142	[»]
1FDH	X-ray	2.50	A/B	2-142	[»]
1FN3	X-ray	2.48	A/C	2-142	[»]
1G9V	X-ray	1.85	A/C	2-142	[»]
1GBU	X-ray	1.80	A/C	2-142	[»]
1GBV	X-ray	2.00	A/C	2-142	[»]
1GLI	X-ray	2.50	A/C	3-142	[»]
1GZX	X-ray	2.10	A/C	2-142	[»]
1HAB	X-ray	2.30	A/C	2-142	[»]
1HAC	X-ray	2.60	A/C	2-142	[»]
1HBA	X-ray	2.10	A/C	2-142	[»]
1HBB	X-ray	1.90	A/C	2-142	[»]
1HBS	X-ray	3.00	A/C/E/G	2-141	[»]
1HCO	X-ray	2.70	A	2-142	[»]
1HDB	X-ray	2.20	A/C	2-142	[»]
1HGA	X-ray	2.10	A/C	2-142	[»]
1HGB	X-ray	2.10	A/C	2-142	[»]
1HGC	X-ray	2.10	A/C	2-142	[»]
1HHO	X-ray	2.10	A	2-141	[»]
1IRD	X-ray	1.25	A	2-142	[»]
1J3Y	X-ray	1.55	A/C/E/G	2-142	[»]
1J3Z	X-ray	1.60	A/C/E/G	2-142	[»]
1J40	X-ray	1.45	A/C/E/G	2-142	[»]
1J41	X-ray	1.45	A/C/E/G	2-142	[»]
1J7S	X-ray	2.20	A/C	3-142	[»]
1J7W	X-ray	2.00	A/C	3-142	[»]
1J7Y	X-ray	1.70	A/C	3-142	[»]
1JY7	X-ray	3.20	A/C/P/R/U/W	2-142	[»]
1K0Y	X-ray	1.87	A/C	2-142	[»]
1K1K	X-ray	2.00	A	2-142	[»]
1KD2	X-ray	1.87	A/C	2-142	[»]
1LFL	X-ray	2.70	A/C/P/R	2-142	[»]
1LFQ	X-ray	2.60	A	2-142	[»]
1LFT	X-ray	2.60	A	2-142	[»]
1LFV	X-ray	2.80	A	2-142	[»]
1LFY	X-ray	3.30	A	2-142	[»]
1LFZ	X-ray	3.10	A	2-142	[»]
1LJW	X-ray	2.16	A	2-142	[»]
1M9P	X-ray	2.10	A/C	2-142	[»]
1MKO	X-ray	2.18	A/C	2-142	[»]
1NEJ	X-ray	2.10	A/C	2-142	[»]
1NIH	X-ray	2.60	A/C	2-142	[»]
1NQP	X-ray	1.73	A/C	2-142	[»]
1O1I	X-ray	2.30	A	2-142	[»]
1O1J	X-ray	1.90	A	2-142	[»]
1O1K	X-ray	2.00	A/C	3-142	[»]
1O1L	X-ray	1.80	A	2-142	[»]
1O1M	X-ray	1.85	A	2-142	[»]
1O1N	X-ray	1.80	A	2-142	[»]
1O1O	X-ray	1.80	A/C	2-142	[»]
1O1P	X-ray	1.80	A	2-142	[»]
1QI8	X-ray	1.80	A/C	3-142	[»]
1QSH	X-ray	1.70	A/C	2-142	[»]
1QSI	X-ray	1.70	A/C	2-142	[»]
1QXD	X-ray	2.25	A/C	2-142	[»]
1QXE	X-ray	1.85	A/C	2-142	[»]
1R1X	X-ray	2.15	A	2-142	[»]
1R1Y	X-ray	1.80	A/C	2-142	[»]
1RPS	X-ray	2.11	A/C	2-142	[»]
1RQ3	X-ray	1.91	A/C	2-142	[»]
1RQ4	X-ray	2.11	A/C	2-142	[»]
1RQA	X-ray	2.11	A/C	2-141	[»]
1RVW	X-ray	2.50	A	2-142	[»]
1SDK	X-ray	1.80	A/C	2-142	[»]
1SDL	X-ray	1.80	A/C	2-142	[»]
1SHR	X-ray	1.88	A/C	2-142	[»]
1SI4	X-ray	2.20	A/C	2-142	[»]
1THB	X-ray	1.50	A/C	2-142	[»]
1UIW	X-ray	1.50	A/C/E/G	2-142	[»]
1VWT	X-ray	1.90	A/C	2-141	[»]
1XXT	X-ray	1.91	A/C	2-142	[»]
1XY0	X-ray	1.99	A/C	3-142	[»]
1XYE	X-ray	2.13	A/C	3-142	[»]
1XZ2	X-ray	1.90	A/C	1-142	[»]
1XZ4	X-ray	2.00	A/C	3-142	[»]
1XZ5	X-ray	2.11	A/C	3-142	[»]
1XZ7	X-ray	1.90	A/C	3-142	[»]
1XZU	X-ray	2.16	A/C	3-142	[»]
1XZV	X-ray	2.11	A/C	3-142	[»]
1Y01	X-ray	2.80	B	2-141	[»]
1Y09	X-ray	2.25	A/C	3-142	[»]
1Y0A	X-ray	2.22	A/C	3-142	[»]
1Y0C	X-ray	2.30	A/C	3-142	[»]
1Y0D	X-ray	2.10	A/C	1-141	[»]
1Y0T	X-ray	2.14	A/C	1-142	[»]
1Y0W	X-ray	2.14	A/C	1-142	[»]
1Y22	X-ray	2.16	A/C	1-142	[»]
1Y2Z	X-ray	2.07	A/C	1-142	[»]
1Y31	X-ray	2.13	A/C	2-141	[»]
1Y35	X-ray	2.12	A/C	1-142	[»]
1Y45	X-ray	2.00	A/C	1-142	[»]
1Y46	X-ray	2.22	A/C	1-142	[»]
1Y4B	X-ray	2.10	A/C	1-142	[»]
1Y4F	X-ray	2.00	A/C	1-142	[»]
1Y4G	X-ray	1.91	A/C	1-142	[»]
1Y4P	X-ray	1.98	A/C	1-142	[»]
1Y4Q	X-ray	2.11	A/C	1-142	[»]
1Y4R	X-ray	2.22	A/C	1-142	[»]
1Y4V	X-ray	1.84	A/C	1-142	[»]
1Y5F	X-ray	2.14	A/C	1-142	[»]
1Y5J	X-ray	2.03	A/C	1-142	[»]
1Y5K	X-ray	2.20	A/C	1-142	[»]
1Y7C	X-ray	2.10	A/C	1-142	[»]
1Y7D	X-ray	1.90	A/C	1-142	[»]
1Y7G	X-ray	2.10	A/C	1-142	[»]
1Y7Z	X-ray	1.98	A/C	1-142	[»]
1Y83	X-ray	1.90	A/C	1-142	[»]
1Y85	X-ray	2.13	A/C	1-142	[»]
1Y8W	X-ray	2.90	A/C	3-142	[»]
1YDZ	X-ray	3.30	A/C	3-142	[»]
1YE0	X-ray	2.50	A/C	1-142	[»]
1YE1	X-ray	4.50	A/C	1-142	[»]
1YE2	X-ray	1.80	A/C	1-142	[»]
1YEN	X-ray	2.80	A/C	1-142	[»]
1YEO	X-ray	2.22	A/C	1-142	[»]
1YEQ	X-ray	2.75	A/C	1-142	[»]
1YEU	X-ray	2.12	A/C	1-142	[»]
1YEV	X-ray	2.11	A/C	1-142	[»]
1YFF	X-ray	2.40	A/C/E/G	2-142	[»]
1YG5	X-ray	2.70	A/C	1-142	[»]
1YGD	X-ray	2.73	A/C	1-142	[»]
1YGF	X-ray	2.70	A/C	1-142	[»]
1YH9	X-ray	2.20	A/C	1-142	[»]
1YHE	X-ray	2.10	A/C	1-142	[»]
1YHR	X-ray	2.60	A/C	1-142	[»]
1YIE	X-ray	2.40	A/C	1-142	[»]
1YIH	X-ray	2.00	A/C	1-142	[»]
1YVQ	X-ray	1.80	A/C	2-142	[»]
1YVT	X-ray	1.80	A	1-142	[»]
1YZI	X-ray	2.07	A	1-142	[»]
1Z8U	X-ray	2.40	B/D	1-142	[»]
2D5Z	X-ray	1.45	A/C	1-142	[»]
2D60	X-ray	1.70	A/C	1-142	[»]
2DN1	X-ray	1.25	A	1-142	[»]
2DN2	X-ray	1.25	A/C	1-142	[»]
2DN3	X-ray	1.25	A	1-142	[»]
2DXM	neutron diffraction	2.10	A/C	2-142	[»]
2H35	NMR	-	A	1-142	[»]
			C	2-142	[»]
2HBC	X-ray	2.10	A	1-142	[»]
2HBD	X-ray	2.20	A	2-142	[»]
2HBE	X-ray	2.00	A	1-142	[»]
2HBF	X-ray	2.20	A	1-142	[»]
2HBS	X-ray	2.05	A/C/E/G	1-142	[»]
2HCO	X-ray	2.70	A	2-142	[»]
2HHB	X-ray	1.74	A/C	2-142	[»]
2HHD	X-ray	2.20	A/C	2-142	[»]
2HHE	X-ray	2.20	A/C	1-142	[»]
2W6V	X-ray	1.80	A/C	2-142	[»]
2W72	X-ray	1.07	A	2-142	[»]
			C	3-142	[»]
2YRS	X-ray	2.30	A/C/I/M	2-142	[»]
3B75	X-ray	2.30	A/C/E/G/S	2-142	[»]
3D17	X-ray	2.80	A/C	2-142	[»]
3D7O	X-ray	1.80	A	2-142	[»]
3DUT	X-ray	1.55	A/C	2-142	[»]
3HHB	X-ray	1.74	A/C	2-142	[»]
3IA3	X-ray	3.20	B/D	2-142	[»]
3IC0	X-ray	1.80	A/C	2-141	[»]
3IC2	X-ray	2.40	A/C	2-142	[»]
4HHB	X-ray	1.74	A/C	1-142	[»]
6HBW	X-ray	2.00	A/C	1-142	[»]

ModBase

Protein-protein interaction databases

IntAct

P69905. 9 interactions.

STRING

P69905.

PTM databases

PhosphoSite

P69905.

2-D gel databases

SWISS-2DPAGE

P69905.

DOSAC-COBS-2DPAGE

P69905.

REPRODUCTION-2DPAGE

IPI00410714.

Siena-2DPAGE

P69905.

Proteomic databases

PeptideAtlas

P69905.

PRIDE

P69905.

Genome annotation databases

Ensembl

ENST00000251595; ENSP00000251595; ENSG00000188536; Homo sapiens. [Genome view]
ENST00000320868; ENSP00000322421; ENSG00000206172; Homo sapiens. [Genome view]

GeneID

3039.
3040.

KEGG

hsa:3039.
hsa:3040.

UCSC

uc002cfv.2. human.

Organism-specific databases

CTD

3039.
3040.

GeneCards

GC16P000162.
GC16P000166.

H-InvDB

HIX0012641.
HIX0079739.

HGNC

HGNC:4823. HBA1.
HGNC:4824. HBA2.

MIM

140700. phenotype.
141800. gene+phenotype.
141850. gene.
141860. gene.
236750. phenotype.
604131. phenotype.

Orphanet

846. Alpha-thalassemia.
93615. Hemoglobin Constant Spring.
93616. Hemoglobin H disease.
163596. Hydrops fetalis of Barts.

PharmGKB

PA29198.

GenAtlas

Phylogenomic databases

eggNOG

prNOG15450.

HOVERGEN

P69905.

InParanoid

P69905.

OMA

TPEVHAS.

Gene expression databases

ArrayExpress

P69905.

Bgee

P69905.

CleanEx

HS_HBA1.
HS_HBA2.

Genevestigator

P69905.

GermOnline

ENSG00000188536. Homo sapiens.
ENSG00000206172. Homo sapiens.

Family and domain databases

InterPro

IPR009050. Globin-like.
IPR000971. Globin_subset.
IPR002338. Haemoglobin_a.
IPR018331. Haemoglobin_alpha_chain.
IPR002339. Haemoglobin_pi.
[Graphical view]

PANTHER

PTHR11442:SF14. Pi_haem. 1 hit.

Pfam

PF00042. Globin. 1 hit.
[Graphical view]

PRINTS

PR00612. ALPHAHAEM.
PR00815. PIHAEM.

PROSITE

PS01033. GLOBIN. 1 hit.
[Graphical view]

ProtoNet

Other Resources

DrugBank

DB00613. Amodiaquine.
DB00608. Chloroquine.
DB00893. Iron Dextran.
DB00358. Mefloquine.
DB01087. Primaquine.
DB00468. Quinine.

NextBio

12034.

PMAP-CutDB

P69905.

SOURCE

Entry information

Entry name

HBA_HUMAN

Accession

Primary (citable) accession number: P69905
Secondary accession number(s): P01922

Q9UCM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.