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P69905 (HBA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hemoglobin subunit alpha
Alternative name(s):
Alpha-globin
Hemoglobin alpha chain
Gene names
Name:HBA1
AND
Name:HBA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length142 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

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

Heinz body anemias (HEIBAN) [MIM:140700]: Form of non-spherocytic hemolytic anemia of Dacie type 1. After splenectomy, which has little benefit, basophilic inclusions called Heinz bodies are demonstrable in the erythrocytes. Before splenectomy, diffuse or punctate basophilia may be evident. Most of these cases are probably instances of hemoglobinopathy. The hemoglobin demonstrates heat lability. Heinz bodies are observed also with the Ivemark syndrome (asplenia with cardiovascular anomalies) and with glutathione peroxidase deficiency.
Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.59

Alpha-thalassemia (A-THAL) [MIM:604131]: A form of thalassemia. Thalassemias are common monogenic diseases occurring 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 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).
Note: The disease is caused by mutations affecting the gene represented in this entry.

Alpha(0)-thalassemia is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders.

Hemoglobin H disease (HBH) [MIM:613978]: A form of alpha-thalassemia due to the loss of three alpha genes. This results in high levels of a tetramer of four beta chains (hemoglobin H), causing a severe and life-threatening anemia. Untreated, most patients die in childhood or early adolescence.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.70

Miscellaneous

Gives blood its red color.

Sequence similarities

Belongs to the globin family.

Sequence caution

The sequence BAD97112.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processOxygen transport
Transport
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Hereditary hemolytic anemia
   LigandHeme
Iron
Metal-binding
   PTMAcetylation
Glycation
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbicarbonate transport

Traceable author statement. Source: Reactome

hydrogen peroxide catabolic process

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

oxidation-reduction process

Inferred from direct assay PubMed 19740759. Source: GOC

oxygen transport

Traceable author statement PubMed 7518430. Source: UniProtKB

positive regulation of cell death

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

protein heterooligomerization

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

response to hydrogen peroxide

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

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cytosol

Traceable author statement. Source: Reactome

cytosolic small ribosomal subunit

Inferred from direct assay PubMed 8706699. Source: UniProtKB

endocytic vesicle lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

haptoglobin-hemoglobin complex

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

hemoglobin complex

Traceable author statement PubMed 7555018. Source: UniProtKB

   Molecular_functionheme binding

Inferred from electronic annotation. Source: InterPro

iron ion 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 PubMed 12072504. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HBBP6887120EBI-714680,EBI-715554

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.17 Ref.18 Ref.19 Ref.20
Chain2 – 142141Hemoglobin subunit alpha
PRO_0000052653

Sites

Metal binding591Iron (heme distal ligand)
Metal binding881Iron (heme proximal ligand)
Site121Not glycated
Site571Not glycated
Site611Not glycated
Site911Not glycated
Site1001Not glycated

Amino acid modifications

Modified residue81N6-succinyllysine; alternate By similarity
Modified residue171N6-acetyllysine; alternate Ref.23
Modified residue171N6-succinyllysine; alternate By similarity
Modified residue411N6-succinyllysine; alternate By similarity
Glycosylation81N-linked (Glc) (glycation); alternate Ref.22
Glycosylation171N-linked (Glc) (glycation); alternate Ref.22
Glycosylation411N-linked (Glc) (glycation); alternate Ref.22
Glycosylation621N-linked (Glc) (glycation) Ref.22

Natural variations

Natural variant21V → E in Thionville; O(2) affinity down. Ref.62
VAR_002719
Natural variant31L → R in ChongQing; O(2) affinity up. Ref.35
Corresponds to variant rs36030576 [ dbSNP | Ensembl ].
VAR_002720
Natural variant61A → D in J-Toronto.
Corresponds to variant rs34090856 [ dbSNP | Ensembl ].
VAR_002721
Natural variant61A → P in Karachi.
Corresponds to variant rs34751764 [ dbSNP | Ensembl ].
VAR_002722
Natural variant71D → A in Sawara; O(2) affinity up. Ref.56
Corresponds to variant rs33986902 [ dbSNP | Ensembl ].
VAR_002723
Natural variant71D → G in Swan River. Ref.61
VAR_002724
Natural variant71D → N in Dunn; O(2) affinity up.
Corresponds to variant rs33961916 [ dbSNP | Ensembl ].
VAR_002725
Natural variant71D → V in Ferndown; O(2) affinity up.
VAR_002726
Natural variant71D → Y in Woodville; O(2) affinity up. Ref.67
VAR_002727
Natural variant81K → E in Kurosaki. Ref.49
Corresponds to variant rs34817956 [ dbSNP | Ensembl ].
VAR_002728
Natural variant101N → T in Broomfield.
VAR_038149
Natural variant111V → F.
Corresponds to variant rs1799896 [ dbSNP | Ensembl ].
VAR_014605
Natural variant121K → E in Anantharaj.
VAR_002729
Natural variant131A → D in J-Paris 1/J-Aljezur.
Corresponds to variant rs35615982 [ dbSNP | Ensembl ].
VAR_002730
Natural variant141A → P in Ravenscourt Park; causes alpha-thalassemia.
Corresponds to variant rs35331909 [ dbSNP | Ensembl ].
VAR_038150
Natural variant151W → R in Evanston; O(2) affinity up.
Corresponds to variant rs33964317 [ dbSNP | Ensembl ].
VAR_002731
Natural variant161G → R in Ottawa/Siam.
Corresponds to variant rs35816645 [ dbSNP | Ensembl ].
VAR_002732
Natural variant171K → M in Harbin; slightly unstable. Ref.35
Corresponds to variant rs35210126 [ dbSNP | Ensembl ].
VAR_002733
Natural variant171K → N in Beijing.
Corresponds to variant rs33923844 [ dbSNP | Ensembl ].
VAR_002734
Natural variant191G → D in Al-Ain Abu Dhabi. Ref.30
Corresponds to variant rs35993097 [ dbSNP | Ensembl ].
VAR_002735
Natural variant191G → R in Handsworth.
Corresponds to variant rs34504387 [ dbSNP | Ensembl ].
VAR_002736
Natural variant201A → D in J-Kurosh.
VAR_002737
Natural variant201A → E in J-Tashikuergan.
Corresponds to variant rs35628685 [ dbSNP | Ensembl ].
VAR_002738
Natural variant211H → Q in Le Lamentin.
Corresponds to variant rs41525149 [ dbSNP | Ensembl ].
VAR_002739
Natural variant211H → R in Hobart. Ref.45
Corresponds to variant rs33943087 [ dbSNP | Ensembl ].
VAR_002740
Natural variant221A → D in J-Nyanza.
Corresponds to variant rs11548605 [ dbSNP | Ensembl ].
VAR_002741
Natural variant221A → P in Fontainebleau.
Corresponds to variant rs34324664 [ dbSNP | Ensembl ].
VAR_002742
Natural variant231G → D in J-Medellin.
Corresponds to variant rs34608326 [ dbSNP | Ensembl ].
VAR_002743
Natural variant241E → G in Reims; slightly unstable.
Corresponds to variant rs33939421 [ dbSNP | Ensembl ].
VAR_002744
Natural variant241E → K in Chad.
VAR_002745
Natural variant251Y → H in Luxembourg; unstable.
VAR_002746
Natural variant271A → E in Shenyang; unstable. Ref.57
VAR_002747
Natural variant271A → V in Campinas. Ref.72
VAR_025387
Natural variant281E → D in Hekinan.
VAR_002748
Natural variant281E → G in Fort Worth.
VAR_002749
Natural variant281E → V in Spanish town. Ref.39
VAR_002750
Natural variant311E → K in O-Padova.
VAR_002751
Natural variant321R → K Causes alpha-thalassemia. Ref.5
VAR_025002
Natural variant321R → S in Prato; unstable.
VAR_002752
Natural variant351L → R in Queens/Ogi.
VAR_002753
Natural variant381P → PE in Catonsville. Ref.29
VAR_002755
Natural variant381P → R in Bourmedes.
VAR_002754
Natural variant411K → M in Kanagawa; O(2) affinity up. Ref.47
VAR_002756
Natural variant421T → S in Miyano; O(2) affinity up.
VAR_002757
Natural variant441F → L in Hirosaki; unstable.
VAR_002758
Natural variant451P → L in Milledgeville; O(2) affinity up.
Corresponds to variant rs41514946 [ dbSNP | Ensembl ].
VAR_002759
Natural variant451P → R in Kawachi; O(2) affinity up.
VAR_002760
Natural variant461H → Q in Bari.
VAR_002761
Natural variant461H → R in Fort de France; O(2) affinity up. Ref.39
VAR_002762
Natural variant481D → A in Cordele; unstable.
VAR_002763
Natural variant481D → G in Umi/Michigan; unstable.
VAR_002764
Natural variant481D → H in Hasharon/Sinai; unstable. Ref.44
VAR_002765
Natural variant481D → Y in Kurdistan. Ref.48
VAR_002766
Natural variant491L → R in Montgomery. Ref.52
VAR_002767
Natural variant501S → R in Savaria.
VAR_002768
Natural variant511H → R in Aichi; slightly unstable.
VAR_002769
Natural variant521G → D in J-Abidjan.
VAR_002770
Natural variant521G → R in Russ.
VAR_002771
Natural variant541A → D in J-Rovigo; unstable.
VAR_002772
Natural variant551Q → R in Hikoshima/Shimonoseki.
VAR_002773
Natural variant571K → R in Port Huron. Ref.55
VAR_002774
Natural variant571K → T in Thailand.
VAR_002775
Natural variant581G → R in L-Persian Gulf.
VAR_002776
Natural variant591H → Q in Boghe. Ref.71
VAR_025388
Natural variant591H → Y in M-Boston/M-Osaka; O(2) affinity down.
VAR_002777
Natural variant601G → D in Adana; unstable; causes alpha-thalassemia.
Corresponds to variant rs28928878 [ dbSNP | Ensembl ].
VAR_002778
Natural variant601G → V in Tottori; unstable.
VAR_002779
Natural variant611K → N in Zambia.
Corresponds to variant rs28928887 [ dbSNP | Ensembl ].
VAR_002780
Natural variant611Missing in Clinic; unstable; causes alpha-thalassemia. Ref.36
VAR_002781
Natural variant621K → N in J-Buda. Ref.33
VAR_002782
Natural variant621K → T in J-Anatolia.
VAR_002783
Natural variant631V → M in Evans; unstable. Ref.11 Ref.38
VAR_002784
Natural variant631Missing in HBH; hemoglobin Aghia Sophia. Ref.70
VAR_066401
Natural variant641A → D in Pontoise; unstable.
VAR_002785
Natural variant651D → Y in Persepolis.
VAR_002786
Natural variant691N → K in G-Philadelphia. Ref.12
Corresponds to variant rs1060339 [ dbSNP | Ensembl ].
VAR_002787
Natural variant721A → E in J-Habana.
VAR_002788
Natural variant721A → V in Ozieri.
VAR_002789
Natural variant731H → R in Daneskgah-Teheran.
VAR_002790
Natural variant751D → A in Lille.
VAR_002791
Natural variant751D → G in Chapel Hill.
VAR_002792
Natural variant751D → N in G-Pest. Ref.33
VAR_002793
Natural variant761D → A in Duan.
VAR_002794
Natural variant761D → H in Q-Iran.
VAR_002795
Natural variant771M → K in Noko.
VAR_002796
Natural variant771M → T in Aztec.
VAR_002797
Natural variant781P → R in Guizhou.
VAR_002798
Natural variant791N → H in Davenport. Ref.37
VAR_002799
Natural variant791N → K in Stanleyville-2.
VAR_002800
Natural variant801A → G in Singapore.
VAR_012662
Natural variant811L → R in Ann Arbor; unstable.
VAR_002801
Natural variant821S → C in Nigeria.
VAR_002802
Natural variant831A → D in Garden State.
VAR_002803
Natural variant851S → R in Etobicoke; O(2) affinity up.
VAR_002804
Natural variant861D → V in Inkster; O(2) affinity up. Ref.46
VAR_002805
Natural variant861D → Y in Atago; O(2) affinity up. Ref.31
VAR_002806
Natural variant871L → R in Moabit; unstable.
VAR_002807
Natural variant881H → N in Auckland; unstable. Ref.32
VAR_002808
Natural variant881H → R in Iwata; unstable.
VAR_002809
Natural variant891A → S in Loire; O(2) affinity up.
VAR_002810
Natural variant911K → M in Handa; O(2) affinity up. Ref.43
VAR_002811
Natural variant921L → F.
Corresponds to variant rs17407508 [ dbSNP | Ensembl ].
VAR_049272
Natural variant921L → P in Port Phillip; unstable.
Corresponds to variant rs17407508 [ dbSNP | Ensembl ].
VAR_002812
Natural variant931R → Q in J-Cape Town; O(2) affinity up.
VAR_002813
Natural variant931R → W in Cemenelum; O(2) affinity up. Ref.34
VAR_020775
Natural variant951D → A in Bassett; markedly reduced oxygen affinity. Ref.73
VAR_025389
Natural variant951D → Y in Setif; unstable.
VAR_002814
Natural variant961P → A in Denmark Hill; O(2) affinity up.
VAR_002815
Natural variant961P → T in Godavari; O(2) affinity up. Ref.40
VAR_002816
Natural variant981N → K in Dallas; O(2) affinity up.
VAR_002817
Natural variant1001K → E in Turriff. Ref.64
VAR_002818
Natural variant1031S → R in Manitoba; slightly unstable.
Corresponds to variant rs41344646 [ dbSNP | Ensembl ].
VAR_002819
Natural variant1041H → R in Contaldo; unstable.
VAR_002820
Natural variant1041H → Y in Charolles. Ref.71
VAR_025390
Natural variant1101L → R in Suan-Dok; unstable; causes alpha-thalassemia. Ref.58
VAR_002821
Natural variant1111A → D in Petah Tikva; unstable; causes alpha-thalassemia. Ref.53
VAR_002822
Natural variant1131H → D in Hopkins-II; unstable.
VAR_002823
Natural variant1141L → H in Twin Peaks.
VAR_002824
Natural variant1151P → L in Nouakchott.
VAR_002825
Natural variant1151P → R in Chiapas.
VAR_002826
Natural variant1151P → S in Melusine. Ref.51
VAR_002827
Natural variant1161A → D in J-Tongariki.
VAR_002828
Natural variant1171E → A in Ube-4.
VAR_002829
Natural variant1171E → EHLPAE in Zaire.
VAR_002830
Natural variant1181F → FI in Phnom Penh. Ref.54
VAR_002831
Natural variant1191T → TEFT in Grady.
VAR_002832
Natural variant1211A → E in J-Meerut/J-Birmingham. Ref.50
VAR_002833
Natural variant1221V → M in Owari.
VAR_002834
Natural variant1231H → Q in Westmead. Ref.66
VAR_002835
Natural variant1261L → P in Quong Sze; causes alpha-thalassemia.
VAR_002836
Natural variant1261L → R in Plasencia; family with moderate microcytosis and hypochromia. Ref.74
VAR_025391
Natural variant1271D → G in West One. Ref.72
VAR_025392
Natural variant1271D → V in Fukutomi; O(2) affinity up.
VAR_002837
Natural variant1271D → Y in Monteriore; O(2) affinity up.
VAR_002838
Natural variant1281K → N in Jackson.
VAR_002839
Natural variant1301L → P in Tunis-Bizerte; unstable; causes alpha-thalassemia. Ref.63
VAR_002840
Natural variant1311A → D in Yuda; O(2) affinity down. Ref.68
VAR_002842
Natural variant1311A → P in Sun Prairie; unstable. Ref.60
VAR_002841
Natural variant1321S → P in Questembert; highly unstable; causes alpha-thalassemia.
VAR_002843
Natural variant1341S → R in Val de Marne; O(2) affinity up. Ref.65
VAR_002844
Natural variant1361V → E in Pavie.
VAR_002845
Natural variant1371L → M in Chicago.
VAR_002846
Natural variant1371L → P in Bibba; unstable; causes alpha-thalassemia.
VAR_002847
Natural variant1371L → R in Toyama. Ref.59
VAR_035242
Natural variant1391S → P in Attleboro; O(2) affinity up.
VAR_002848
Natural variant1401K → E in Hanamaki; O(2) affinity up. Ref.42
VAR_002849
Natural variant1401K → T in Tokoname; O(2) affinity up.
VAR_002850
Natural variant1411Y → H in Rouen/Ethiopia; O(2) affinity up. Ref.21
VAR_002851
Natural variant1421R → C in Nunobiki; O(2) affinity up.
VAR_002852
Natural variant1421R → H in Suresnes; O(2) affinity up.
VAR_002854
Natural variant1421R → L in Legnano; O(2) affinity up.
VAR_002853
Natural variant1421R → P in Singapore.
VAR_002855

Experimental info

Sequence conflict101N → H in BAD97112. Ref.13

Secondary structure

.......................... 142
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P69905 [UniParc].

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

FASTA14215,258
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Three-dimensional Fourier synthesis of human deoxyhaemoglobin at 2.5-A resolution: refinement of the atomic model."
Fermi G.
J. Mol. Biol. 97:237-256(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN.
[26]"The structure of human carbonmonoxy haemoglobin at 2.7-A resolution."
Baldwin J.M.
J. Mol. Biol. 136:103-128(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[27]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF LIGANDED R2 STATE.
[28]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF HB GOWER-2.
[29]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF VARIANT HB CATONSVILLE GLU-38 INS.
[30]"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] [Europe PMC] [Abstract]
Cited for: VARIANT AL-AIN ABU DHABI ASP-19.
[31]"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] [Europe PMC] [Abstract]
Cited for: VARIANT ATAGO TYR-86.
[32]"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] [Europe PMC] [Abstract]
Cited for: VARIANT AUCKLAND ASN-88.
[33]"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.
[34]"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] [Europe PMC] [Abstract]
Cited for: VARIANT CEMENELUM TRP-93.
[35]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS CHONGQING ARG-3 AND HARBIN MET-17.
[36]"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] [Europe PMC] [Abstract]
Cited for: VARIANT CLINIC LYS-61 DEL.
[37]"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] [Europe PMC] [Abstract]
Cited for: VARIANT DAVENPORT HIS-79.
[38]"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] [Europe PMC] [Abstract]
Cited for: VARIANT EVANS MET-63.
[39]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS SPANISH TOWN VAL-28 AND FORT DE FRANCE ARG-46.
[40]"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] [Europe PMC] [Abstract]
Cited for: VARIANT GODAVARI THR-96.
[41]"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] [Europe PMC] [Abstract]
Cited for: VARIANT GRADY GLU-PHE-THR-119 INS.
[42]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HANAMAKI GLU-140.
[43]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HANDA MET-91.
[44]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HASHARON HIS-48.
[45]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HOBART ARG-21.
[46]"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] [Europe PMC] [Abstract]
Cited for: VARIANT INKSTER VAL-86.
[47]"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] [Europe PMC] [Abstract]
Cited for: VARIANT KANAGAWA MET-41.
[48]"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] [Europe PMC] [Abstract]
Cited for: VARIANT KURDISTAN TYR-48.
[49]"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] [Europe PMC] [Abstract]
Cited for: VARIANT KUROSAKI GLU-8.
[50]"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] [Europe PMC] [Abstract]
Cited for: VARIANT J-MEERUT/J-BIRMINGHAM GLU-121.
[51]"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] [Europe PMC] [Abstract]
Cited for: VARIANT MELUSINE SER-115.
[52]"Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys) and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg)."
Brimhall B., Jones R.T., Schneider R.G., Hosty T.S., Tomlin G., Atkins R.
Biochim. Biophys. Acta 379:28-32(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MONTGOMERY ARG-49.
[53]"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] [Europe PMC] [Abstract]
Cited for: VARIANT PETAH TIKVA ASP-111.
[54]"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] [Europe PMC] [Abstract]
Cited for: VARIANT PHNOM PENH ILE-118 INS.
[55]"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] [Europe PMC] [Abstract]
Cited for: VARIANT PORT HURON ARG-57.
[56]"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] [Europe PMC] [Abstract]
Cited for: VARIANT SAWARA ALA-7.
[57]"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] [Europe PMC] [Abstract]
Cited for: VARIANT SHENYANG GLU-27.
[58]"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] [Europe PMC] [Abstract]
Cited for: VARIANT SUAN-DOK ARG-110.
[59]"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] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HEIBAN, VARIANT TOYAMA ARG-137.
[60]"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] [Europe PMC] [Abstract]
Cited for: VARIANT SUN PRAIRIE PRO-131.
[61]"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] [Europe PMC] [Abstract]
Cited for: VARIANT SWAN RIVER GLY-7.
[62]"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] [Europe PMC] [Abstract]
Cited for: VARIANT THIONVILLE GLU-2.
[63]"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] [Europe PMC] [Abstract]
Cited for: VARIANT TUNIS-BIZERTE PRO-130.
[64]"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] [Europe PMC] [Abstract]
Cited for: VARIANT TURRIFF GLU-100.
[65]"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] [Europe PMC] [Abstract]
Cited for: VARIANT VAL DE MARNE ARG-134.
[66]"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] [Europe PMC] [Abstract]
Cited for: VARIANT WESTMEAD GLN-123.
[67]"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] [Europe PMC] [Abstract]
Cited for: VARIANT WOODVILLE TYR-7.
[68]"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] [Europe PMC] [Abstract]
Cited for: VARIANT YUDA ASP-131.
[69]"Two new human hemoglobin variants caused by unusual mutational events: Hb Zaire contains a five residue repetition within the alpha-chain and Hb Duino has two residues substituted in the beta-chain."
Wajcman H., Blouquit Y., Vasseur C., le Querrec A., Laniece M., Melevendi C., Rasore A., Galacteros F.
Hum. Genet. 89:676-680(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ZAIRE HIS-LEU-PRO-ALA-GLU-117 INS.
[70]"Hb Aghia Sophia [alpha62(E11)Val-->0 (alpha1)], an 'in-frame' deletion causing alpha-thalassemia."
Traeger-Synodinos J., Harteveld C.L., Kanavakis E., Giordano P.C., Kattamis C., Bernini L.F.
Hemoglobin 23:317-324(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HBH VAL-63 DEL.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Hemoglobin entry

Protein Spotlight

Journey into a tiny world - Issue 84 of July 2007

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.
CCDSCCDS10398.1.
CCDS10399.1.
PIRHAHU. A90807.
HACZP. C93303.
HACZ. I58217.
RefSeqNP_000508.1. NM_000517.4.
NP_000549.1. NM_000558.3.
UniGeneHs.449630.
Hs.654744.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A00X-ray2.00A/C2-142[»]
1A01X-ray1.80A/C2-142[»]
1A0UX-ray2.14A/C2-142[»]
1A0ZX-ray2.00A/C2-142[»]
1A3NX-ray1.80A/C2-142[»]
1A3OX-ray1.80A/C2-142[»]
1A9WX-ray2.90A/C2-142[»]
1ABWX-ray2.00A1-142[»]
1ABYX-ray2.60A1-142[»]
1AJ9X-ray2.20A2-142[»]
1B86X-ray2.50A/C2-142[»]
1BABX-ray1.50A/C1-142[»]
1BBBX-ray1.70A/C2-142[»]
1BIJX-ray2.30A/C2-142[»]
1BUWX-ray1.90A/C2-142[»]
1BZ0X-ray1.50A/C2-142[»]
1BZ1X-ray1.59A/C1-142[»]
1BZZX-ray1.59A/C2-142[»]
1C7BX-ray1.80A/C2-142[»]
1C7CX-ray1.80A2-142[»]
1C7DX-ray1.80A2-142[»]
1CLSX-ray1.90A/C2-142[»]
1CMYX-ray3.00A/C2-142[»]
1COHX-ray2.90A/C2-142[»]
1DKEX-ray2.10A/C2-142[»]
1DXTX-ray1.70A/C2-142[»]
1DXUX-ray1.70A/C2-142[»]
1DXVX-ray1.70A/C2-142[»]
1FDHX-ray2.50A/B2-142[»]
1FN3X-ray2.48A/C2-142[»]
1G9VX-ray1.85A/C2-142[»]
1GBUX-ray1.80A/C2-142[»]
1GBVX-ray2.00A/C2-142[»]
1GLIX-ray2.50A/C3-142[»]
1GZXX-ray2.10A/C2-142[»]
1HABX-ray2.30A/C2-142[»]
1HACX-ray2.60A/C2-142[»]
1HBAX-ray2.10A/C2-142[»]
1HBBX-ray1.90A/C2-142[»]
1HBSX-ray3.00A/C/E/G2-142[»]
1HCOX-ray2.70A2-142[»]
1HDBX-ray2.20A/C2-142[»]
1HGAX-ray2.10A/C2-142[»]
1HGBX-ray2.10A/C2-142[»]
1HGCX-ray2.10A/C2-142[»]
1HHOX-ray2.10A2-142[»]
1IRDX-ray1.25A2-142[»]
1J3YX-ray1.55A/C/E/G2-142[»]
1J3ZX-ray1.60A/C/E/G2-142[»]
1J40X-ray1.45A/C/E/G2-142[»]
1J41X-ray1.45A/C/E/G2-142[»]
1J7SX-ray2.20A/C2-142[»]
1J7WX-ray2.00A/C2-142[»]
1J7YX-ray1.70A/C2-142[»]
1JY7X-ray3.20A/C/P/R/U/W2-142[»]
1K0YX-ray1.87A/C2-142[»]
1K1KX-ray2.00A2-142[»]
1KD2X-ray1.87A/C2-142[»]
1LFLX-ray2.70A/C/P/R2-142[»]
1LFQX-ray2.60A2-142[»]
1LFTX-ray2.60A2-142[»]
1LFVX-ray2.80A2-142[»]
1LFYX-ray3.30A2-142[»]
1LFZX-ray3.10A2-142[»]
1LJWX-ray2.16A2-142[»]
1M9PX-ray2.10A/C2-142[»]
1MKOX-ray2.18A/C2-142[»]
1NEJX-ray2.10A/C2-142[»]
1NIHX-ray2.60A/C2-142[»]
1NQPX-ray1.73A/C2-142[»]
1O1IX-ray2.30A2-142[»]
1O1JX-ray1.90A2-142[»]
1O1KX-ray2.00A/C3-142[»]
1O1LX-ray1.80A2-142[»]
1O1MX-ray1.85A2-142[»]
1O1NX-ray1.80A2-142[»]
1O1OX-ray1.80A/C2-142[»]
1O1PX-ray1.80A2-142[»]
1QI8X-ray1.80A/C3-142[»]
1QSHX-ray1.70A/C2-142[»]
1QSIX-ray1.70A/C2-142[»]
1QXDX-ray2.25A/C2-142[»]
1QXEX-ray1.85A/C2-142[»]
1R1XX-ray2.15A2-142[»]
1R1YX-ray1.80A/C2-142[»]
1RPSX-ray2.11A/C2-142[»]
1RQ3X-ray1.91A/C2-142[»]
1RQ4X-ray2.11A/C2-142[»]
1RQAX-ray2.11A/C2-142[»]
1RVWX-ray2.50A2-142[»]
1SDKX-ray1.80A/C2-142[»]
1SDLX-ray1.80A/C2-142[»]
1SHRX-ray1.88A/C2-142[»]
1SI4X-ray2.20A/C2-142[»]
1THBX-ray1.50A/C2-142[»]
1UIWX-ray1.50A/C/E/G2-142[»]
1VWTX-ray1.90A/C2-142[»]
1XXTX-ray1.91A/C2-142[»]
1XY0X-ray1.99A/C2-142[»]
1XYEX-ray2.13A/C3-142[»]
1XZ2X-ray1.90A/C2-142[»]
1XZ4X-ray2.00A/C3-142[»]
1XZ5X-ray2.11A/C2-142[»]
1XZ7X-ray1.90A/C2-142[»]
1XZUX-ray2.16A/C2-142[»]
1XZVX-ray2.11A/C2-142[»]
1Y01X-ray2.80B1-142[»]
1Y09X-ray2.25A/C2-142[»]
1Y0AX-ray2.22A/C2-140[»]
1Y0CX-ray2.30A/C2-140[»]
1Y0DX-ray2.10A/C2-141[»]
1Y0TX-ray2.14A/C2-142[»]
1Y0WX-ray2.14A/C2-142[»]
1Y22X-ray2.16A/C2-142[»]
1Y2ZX-ray2.07A/C2-142[»]
1Y31X-ray2.13A/C2-142[»]
1Y35X-ray2.12A/C2-142[»]
1Y45X-ray2.00A/C2-142[»]
1Y46X-ray2.22A/C2-142[»]
1Y4BX-ray2.10A/C2-142[»]
1Y4FX-ray2.00A/C2-142[»]
1Y4GX-ray1.91A/C2-142[»]
1Y4PX-ray1.98A/C2-142[»]
1Y4QX-ray2.11A/C2-142[»]
1Y4RX-ray2.22A/C2-142[»]
1Y4VX-ray1.84A/C2-142[»]
1Y5FX-ray2.14A/C2-142[»]
1Y5JX-ray2.03A/C2-142[»]
1Y5KX-ray2.20A/C2-142[»]
1Y7CX-ray2.10A/C2-142[»]
1Y7DX-ray1.90A/C2-142[»]
1Y7GX-ray2.10A/C2-142[»]
1Y7ZX-ray1.98A/C2-142[»]
1Y83X-ray1.90A/C2-142[»]
1Y85X-ray2.13A/C2-141[»]
1Y8WX-ray2.90A/C2-142[»]
1YDZX-ray3.30A/C2-140[»]
1YE0X-ray2.50A/C2-142[»]
1YE1X-ray4.50A/C2-142[»]
1YE2X-ray1.80A/C2-142[»]
1YENX-ray2.80A/C2-142[»]
1YEOX-ray2.22A/C2-142[»]
1YEQX-ray2.75A/C2-142[»]
1YEUX-ray2.12A/C2-142[»]
1YEVX-ray2.11A/C2-142[»]
1YFFX-ray2.40A/C/E/G2-142[»]
1YG5X-ray2.70A/C2-142[»]
1YGDX-ray2.73A/C2-142[»]
1YGFX-ray2.70A/C2-142[»]
1YH9X-ray2.20A/C2-142[»]
1YHEX-ray2.10A/C2-142[»]
1YHRX-ray2.60A/C2-142[»]
1YIEX-ray2.40A/C2-142[»]
1YIHX-ray2.00A/C2-142[»]
1YVQX-ray1.80A/C2-142[»]
1YVTX-ray1.80A2-142[»]
1YZIX-ray2.07A2-142[»]
1Z8UX-ray2.40B/D1-142[»]
2D5ZX-ray1.45A/C2-142[»]
2D60X-ray1.70A/C2-142[»]
2DN1X-ray1.25A2-142[»]
2DN2X-ray1.25A/C2-142[»]
2DN3X-ray1.25A2-142[»]
2DXMneutron diffraction2.10A/C2-142[»]
2H35NMR-A/C2-142[»]
2HBCX-ray2.10A2-142[»]
2HBDX-ray2.20A2-142[»]
2HBEX-ray2.00A2-142[»]
2HBFX-ray2.20A2-142[»]
2HBSX-ray2.05A/C/E/G2-142[»]
2HCOX-ray2.70A2-142[»]
2HHBX-ray1.74A/C2-142[»]
2HHDX-ray2.20A/C2-142[»]
2HHEX-ray2.20A/C2-142[»]
2M6ZNMR-A/C2-142[»]
2W6VX-ray1.80A/C2-142[»]
2W72X-ray1.07A2-142[»]
C3-142[»]
2YRSX-ray2.30A/C/I/M2-142[»]
3B75X-ray2.30A/C/E/G/S2-142[»]
3D17X-ray2.80A/C2-142[»]
3D7OX-ray1.80A2-142[»]
3DUTX-ray1.55A/C2-142[»]
3HHBX-ray1.74A/C2-142[»]
3HXNX-ray2.00A/C2-142[»]
3IA3X-ray3.20B/D1-142[»]
3IC0X-ray1.80A/C2-142[»]
3IC2X-ray2.40A/C2-142[»]
3KMFneutron diffraction2.00A/E2-142[»]
3NL7X-ray1.80A2-142[»]
3NMMX-ray1.60A/C2-142[»]
3ODQX-ray3.10A/C2-142[»]
3ONZX-ray2.09A2-142[»]
3OO4X-ray1.90A2-142[»]
3OO5X-ray2.10A2-142[»]
3OVUX-ray2.83C2-142[»]
3P5QX-ray2.00A2-142[»]
3QJBX-ray1.80A2-142[»]
3QJCX-ray2.00A2-142[»]
3QJDX-ray1.56A/C2-142[»]
3QJEX-ray1.80A/C2-142[»]
3R5IX-ray2.20A/C2-142[»]
3S48X-ray3.05C/D2-142[»]
3S65X-ray1.80A/C2-142[»]
3S66X-ray1.40A2-142[»]
3SZKX-ray3.01A/D2-142[»]
3WCPX-ray1.94A/C2-142[»]
4FC3X-ray2.26A2-142[»]
4HHBX-ray1.74A/C2-142[»]
4IJ2X-ray4.24A/C2-142[»]
4L7YX-ray1.80A/C2-142[»]
4MQCX-ray2.20A2-142[»]
4MQGX-ray1.68A2-142[»]
4MQHX-ray2.50A2-140[»]
4MQIX-ray1.92A2-141[»]
4MQJX-ray1.80A/C/E/G2-142[»]
4MQKX-ray2.24A/C/E/G2-142[»]
4N7NX-ray2.75A/C/E/G/I/K2-142[»]
4N7OX-ray2.50A/C/E/G/I/K2-142[»]
4N7PX-ray2.81A/C/E/G/I/K2-142[»]
6HBWX-ray2.00A/C2-142[»]
ProteinModelPortalP69905.
SMRP69905. Positions 2-142.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109289. 42 interactions.
109290. 7 interactions.
DIPDIP-35199N.
IntActP69905. 20 interactions.
MINTMINT-1519936.
STRING9606.ENSP00000251595.

Chemistry

ChEMBLCHEMBL2095168.
DrugBankDB00613. Amodiaquine.
DB00608. Chloroquine.
DB00893. Iron Dextran.
DB00358. Mefloquine.
DB01087. Primaquine.
DB00468. Quinine.

PTM databases

PhosphoSiteP69905.

Polymorphism databases

DMDM57013850.

2D gel databases

DOSAC-COBS-2DPAGEP69905.
REPRODUCTION-2DPAGEIPI00410714.
SWISS-2DPAGEP69905.
UCD-2DPAGEP01922.
P69905.

Proteomic databases

MaxQBP69905.
PaxDbP69905.
PeptideAtlasP69905.
PRIDEP69905.

Protocols and materials databases

DNASU3039.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000251595; ENSP00000251595; ENSG00000188536.
ENST00000320868; ENSP00000322421; ENSG00000206172.
GeneID3039.
3040.
KEGGhsa:3039.
hsa:3040.
UCSCuc002cfv.4. human.

Organism-specific databases

CTD3039.
3040.
GeneCardsGC16P000291.
GC16P000292.
GeneReviewsHBA1.
HBA2.
HGNCHGNC:4823. HBA1.
HGNC:4824. HBA2.
HPACAB032534.
CAB038417.
HPA043780.
MIM140700. phenotype.
141800. gene+phenotype.
141850. gene.
141860. gene.
604131. phenotype.
613978. phenotype.
neXtProtNX_P69905.
Orphanet98791. Alpha-thalassemia - intellectual disability syndrome linked to chromosome 16.
330041. Autosomal dominant methemoglobinemia.
163596. Hb Bart's hydrops fetalis.
93616. Hemoglobin H disease.
PharmGKBPA29199.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283543.
HOVERGENHBG009709.
InParanoidP69905.
KOK13822.
OMADKFLCAV.
OrthoDBEOG7KH9MP.
PhylomeDBP69905.
TreeFamTF332328.

Enzyme and pathway databases

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

Gene expression databases

BgeeP69905.
CleanExHS_HBA1.
HS_HBA2.
GenevestigatorP69905.

Family and domain databases

Gene3D1.10.490.10. 1 hit.
InterProIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002338. Haemoglobin_a.
IPR002339. Haemoglobin_pi.
[Graphical view]
PfamPF00042. Globin. 1 hit.
[Graphical view]
PRINTSPR00612. ALPHAHAEM.
PR00815. PIHAEM.
SUPFAMSSF46458. SSF46458. 1 hit.
PROSITEPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHBA2. human.
EvolutionaryTraceP69905.
GeneWikiHBA2.
Hemoglobin,_alpha_1.
Hemoglobin,_alpha_2.
NextBio12034.
PMAP-CutDBP69905.
PROP69905.
SOURCESearch...

Entry information

Entry nameHBA_HUMAN
AccessionPrimary (citable) accession number: P69905
Secondary accession number(s): P01922 expand/collapse secondary AC list , Q1HDT5, Q3MIF5, Q53F97, Q96KF1, Q9NYR7, Q9UCM0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM