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Hemoglobin subunit alpha (Alpha-globin) (Hemoglobin alpha chain)

 HBA_HUMAN               Reviewed;         142 AA.
P69905; P01922; Q1HDT5; Q3MIF5; Q53F97; Q96KF1; Q9NYR7; Q9UCM0;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
27-SEP-2017, entry version 165.
RecName: Full=Hemoglobin subunit alpha;
AltName: Full=Alpha-globin;
AltName: Full=Hemoglobin alpha chain;
Name=HBA1;
and
Name=HBA2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1).
PubMed=7448866; DOI=10.1016/0092-8674(80)90347-5;
Michelson A.M., Orkin S.H.;
"The 3' untranslated regions of the duplicated human alpha-globin
genes are unexpectedly divergent.";
Cell 22:371-377(1980).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (HBA2).
PubMed=6244294;
Wilson J.T., Wilson L.B., Reddy V.B., Cavallesco C., Ghosh P.K.,
Deriel J.K., Forget B.G., Weissman S.M.;
"Nucleotide sequence of the coding portion of human alpha globin
messenger RNA.";
J. Biol. Chem. 255:2807-2815(1980).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2).
PubMed=6452630; DOI=10.1073/pnas.77.12.7054;
Liebhaber S.A., Goossens M.J., Kan Y.W.;
"Cloning and complete nucleotide sequence of human 5'-alpha-globin
gene.";
Proc. Natl. Acad. Sci. U.S.A. 77:7054-7058(1980).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6946451; DOI=10.1073/pnas.78.8.5041;
Orkin S.H., Goff S.C., Hechtman R.L.;
"Mutation in an intervening sequence splice junction in man.";
Proc. Natl. Acad. Sci. U.S.A. 78:5041-5045(1981).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-32.
PubMed=11410421;
Zhao Y., Xu X.;
"Alpha2(CD31 AGG-->AAG, Arg-->Lys) causing non-deletional alpha-
thalassemia in a Chinese family with HbH disease.";
Haematologica 86:541-542(2001).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1).
PubMed=11402454;
Zhao Y., Zhong M., Liu Z., Xu X.;
"Rapid detection of the common alpha-thalassemia-2 determinants by PCR
assay.";
Zhonghua Yi Xue Yi Chuan Xue Za Zhi 18:216-218(2001).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALPHA-1 AND ALPHA-2).
PubMed=16728641; DOI=10.1126/science.1126431;
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.;
"A regulatory SNP causes a human genetic disease by creating a new
transcriptional promoter.";
Science 312:1215-1217(2006).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (HBA2).
TISSUE=Blood;
Kutlar F., Leithner C., Kutlar A.;
"Rapid sequencing of mRNA of the human alpha two globin, directly
isolated from reticulocytes in whole blood.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] (HBA1).
TISSUE=Blood;
Kutlar F., Leithner C., Kutlar A.;
"cDNA sequencing of human alpha one globin mRNA, the 3'untranslated
region is different than alpha two globin.";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Blood;
Kutlar F., Holley L., Leithner C., Kutlar A.;
"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.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2), AND VARIANT EVANS MET-63.
TISSUE=Blood;
Kutlar F., Elam D., Hoff J.V., Holley L., Kutlar A.;
"Unstable Hb 'Evans' (GTG->ATG/Val 62 Met) was detected on the alpha-2
globin gene of an Hispanic girl.";
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2), AND VARIANT G-PHILADELPHIA
LYS-69.
Kutlar F., Davis D.H., Nechtman J., Elam D.;
"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.";
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HBA1 AND HBA2).
PubMed=11157797; DOI=10.1093/hmg/10.4.339;
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.;
"Sequence, structure and pathology of the fully annotated terminal 2
Mb of the short arm of human chromosome 16.";
Hum. Mol. Genet. 10:339-352(2001).
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HBA1 AND HBA2).
PubMed=15616553; DOI=10.1038/nature03187;
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.,
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.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[16]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HBA1 AND HBA2).
TISSUE=Bone marrow, Brain, Lung, and Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[17]
PROTEIN SEQUENCE OF 2-142.
PubMed=13872627; DOI=10.1515/bchm2.1961.325.1.283;
Braunitzer G., Gehring-Muller R., Hilschmann N., Hilse K., Hobom G.,
Rudloff V., Wittmann-Liebold B.;
"The constitution of normal adult human haemoglobin.";
Hoppe-Seyler's Z. Physiol. Chem. 325:283-286(1961).
[18]
PROTEIN SEQUENCE OF 2-142.
PubMed=13954546;
Hill R.J., Konigsberg W.;
"The structure of human hemoglobin: IV. The chymotryptic digestion of
the alpha chain of human hemoglobin.";
J. Biol. Chem. 237:3151-3156(1962).
[19]
PROTEIN SEQUENCE OF 2-142.
PubMed=14093912; DOI=10.1021/bi00906a030;
Schroeder W.A., Shelton J.R., Shelton J.B., Cormick J.;
"The amino acid sequence of the alpha chain of human fetal
hemoglobin.";
Biochemistry 2:1353-1357(1963).
[20]
PROTEIN SEQUENCE OF 2-32.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[21]
PROTEIN SEQUENCE OF 128-142, AND VARIANT ETHIOPIA HIS-141.
TISSUE=Umbilical cord blood;
PubMed=1428951; DOI=10.3109/03630269209005699;
Webber B.B., Wilson J.B., Gu L.-H., Huisman T.H.J.;
"Hb Ethiopia or alpha 2(140)(HC2)Tyr----His beta 2.";
Hemoglobin 16:441-443(1992).
[22]
GLYCATION AT LYS-8; LYS-17; LYS-41 AND LYS-62, AND LACK OF GLYCATION
AT LYS-12; LYS-57; LYS-61; LYS-91 AND LYS-100.
PubMed=7358733;
Shapiro R., McManus M.J., Zalut C., Bunn H.F.;
"Sites of nonenzymatic glycosylation of human hemoglobin A.";
J. Biol. Chem. 255:3120-3127(1980).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; THR-9; TYR-25; SER-36
AND SER-50, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[27]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN.
PubMed=1177322; DOI=10.1016/S0022-2836(75)80037-4;
Fermi G.;
"Three-dimensional Fourier synthesis of human deoxyhaemoglobin at 2.5-
A resolution: refinement of the atomic model.";
J. Mol. Biol. 97:237-256(1975).
[28]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
PubMed=7373648; DOI=10.1016/0022-2836(80)90308-3;
Baldwin J.M.;
"The structure of human carbonmonoxy haemoglobin at 2.7-A
resolution.";
J. Mol. Biol. 136:103-128(1980).
[29]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF LIGANDED R2 STATE.
PubMed=1512262;
Silva M.M., Rogers P.H., Arnone A.;
"A third quaternary structure of human hemoglobin A at 1.7-A
resolution.";
J. Biol. Chem. 267:17248-17256(1992).
[30]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF HB GOWER-2.
PubMed=9665850; DOI=10.1006/jmbi.1998.1868;
Sutherland-Smith A.J., Baker H.M., Hofmann O.M., Brittain T.,
Baker E.N.;
"Crystal structure of a human embryonic haemoglobin: the carbonmonoxy
form of Gower II (alpha2 epsilon2) haemoglobin at 2.9-A resolution.";
J. Mol. Biol. 280:475-484(1998).
[31]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF VARIANT HB CATONSVILLE GLU-38
INS.
PubMed=8448109; DOI=10.1021/bi00061a007;
Kavanaugh J.S., Moo-Penn W.F., Arnone A.;
"Accommodation of insertions in helices: the mutation in hemoglobin
Catonsville (Pro 37 alpha-Glu-Thr 38 alpha) generates a 3(10)-->alpha
bulge.";
Biochemistry 32:2509-2513(1993).
[32]
VARIANT J-CAPE TOWN GLN-93.
PubMed=5988206; DOI=10.1038/212792a0;
Botha M.C., Beale D., Isaacs W.A., Lehmann H.;
"Hemoglobin J Cape Town-alpha-2 92 arginine replaced by glutamine
beta-2.";
Nature 212:792-795(1966).
[33]
VARIANT BIBBA PRO-137.
PubMed=5440849;
Smith L.L., Barton B.P., Huisman T.H.;
"Subunit dissociation of the unstable hemoglobin Bibba (alpha 2-
136Pro(H19)beta 2).";
J. Biol. Chem. 245:2185-2188(1970).
[34]
CHARACTERIZATION OF VARIANT J-CAPE TOWN GLN-93.
PubMed=5091982; DOI=10.1016/0022-2836(71)90029-5;
Nagel R.L., Gibson Q.H., Jenkins T.;
"Ligand binding in hemoglobin J Capetown.";
J. Mol. Biol. 58:643-650(1971).
[35]
VARIANT HOPKINS-II ASP-113.
PubMed=5288820;
Charache S., Ostertag W., von Ehrenstein G.;
"Clinical studies and physiological properties of Hopkins-2
haemoglobin.";
Nature New Biol. 234:248-251(1971).
[36]
VARIANT DENMARK HILL ALA-96.
PubMed=5085669;
Wiltshire B.G., Clark K.G., Lorkin P.A., Lehmann H.;
"Haemoglobin Denmark Hill 95 (G2) Pro-Ala, a variant with unusual
electrophoretic and oxygen-binding properties.";
Biochim. Biophys. Acta 278:459-464(1972).
[37]
VARIANT SETIF TYR-95.
PubMed=4667378; DOI=10.1016/0014-5793(72)80645-8;
Wajcman H., Belkhodja O., Labie D.;
"Hb Setif: G1 (94) Asp-Tyr. A new chain hemoglobin variant with
substitution of the residue involved in hydrogen bond between unlike
subunits.";
FEBS Lett. 27:298-300(1972).
[38]
VARIANT ANN ARBOR ARG-81.
PubMed=5033650; DOI=10.1126/science.176.4042.1427;
Adams J.G. III, Winter W.P., Rucknagel D.L., Spencer H.H.;
"Biosynthesis of hemoglobin Ann Arbor: evidence for catabolic and
feedback regulation.";
Science 176:1427-1429(1972).
[39]
VARIANT SAWARA ALA-7.
PubMed=4744335;
Sumida I., Ohta Y., Imamura T., Yanase T.;
"Hemoglobin Sawara: alpha 6(A4) aspartic acid leads to alanine.";
Biochim. Biophys. Acta 322:23-26(1973).
[40]
VARIANT M-BOSTON/M-OSAKA TYR-59.
PubMed=4521212; DOI=10.1073/pnas.70.12.3870;
Pulsinelli P.D., Perutz M.F., Nagel R.L.;
"Structure of hemoglobin M Boston, a variant with a five-coordinated
ferric heme.";
Proc. Natl. Acad. Sci. U.S.A. 70:3870-3874(1973).
[41]
VARIANT J-ROVIGO ASP-54.
PubMed=4824923;
Alberti R., Mariuzzi G.M., Artibani L., Bruni E., Tentori L.;
"A new haemoglobin variant: J-Rovigo alpha 53 (E-2) alanine leads to
aspartic acid.";
Biochim. Biophys. Acta 342:1-4(1974).
[42]
VARIANT HIROSAKI LEU-44.
PubMed=1182166;
Ohba Y., Miyaji T., Matsuoka M., Yokoyama M., Numakura H.;
"Hemoglobin Hirosaki (alpha 43 [CE 1] Phe replaced by Leu), a new
unstable variant.";
Biochim. Biophys. Acta 405:155-160(1975).
[43]
VARIANT PONTOISE ASP-64.
PubMed=849454; DOI=10.1016/0005-2795(77)90036-8;
Thillet J., Blouquit Y., Perrone F., Rosa J.;
"Hemoglobin Pontoise alpha63 Ala replaced by Asp(E12). A new fast
moving variant.";
Biochim. Biophys. Acta 491:16-22(1977).
[44]
CHARACTERIZATION OF VARIANT SAWARA ALA-7.
PubMed=20980; DOI=10.1016/0005-2795(77)90253-7;
Sasaki J., Imamura T., Sumida I., Yanase T., Ohya M.;
"Increased oxygen affinity for hemoglobin Sawara: alphaA4(6) aspartic
acid replaced by alanine.";
Biochim. Biophys. Acta 495:183-186(1977).
[45]
VARIANT PORT PHILLIP PRO-92.
PubMed=902765; DOI=10.1016/0014-5793(77)80940-X;
Brennan S.O., Tauro G.P., Melrose W.;
"Haemoglobin Port Phillip alpha91 (FG3) Leu replaced by Pro, a new
unstable haemoglobin.";
FEBS Lett. 81:115-117(1977).
[46]
VARIANT MOABIT ARG-87.
PubMed=108887;
Knuth A., Pribilla W., Marti H.R., Winterhalter K.H.;
"Hemoglobin Moabit: alpha 86 (F7) Leu leads to Arg: a new unstable
abnormal hemoglobin.";
Acta Haematol. 61:121-124(1979).
[47]
VARIANT PRATO SER-32.
PubMed=486536; DOI=10.1016/0005-2795(79)90184-3;
Marinucci M., Mavilio F., Massa A., Gabbianelli M., Fontanarosa P.P.,
Camagna A., Ignesti C., Tentori L.;
"A new abnormal human hemoglobin: Hb Prato (alpha 2 31 (B12) Arg leads
to Ser beta 2).";
Biochim. Biophys. Acta 578:534-540(1979).
[48]
VARIANT DUNN ASN-7.
PubMed=478975; DOI=10.3109/03630267908998909;
Jue D.L., Johnson M.H., Patchen L.C., Moo-Penn W.F.;
"Hemoglobin Dunn: alpha 6 (A4) aspartic acid replaced by asparagine.";
Hemoglobin 3:137-143(1979).
[49]
CHARACTERIZATION OF VARIANT DUNN ASN-7.
PubMed=7435503; DOI=10.1002/ajh.2830090203;
Charache S., Brimhall B., Zaatari G.;
"Oxygen affinity and stability of hemoglobin Dunn alpha 6(A4)Asp
replaced by Asn): use of isoelectric focusing in recognition of a new
abnormal hemoglobin.";
Am. J. Hematol. 9:151-160(1980).
[50]
VARIANT MILLEDGEVILLE LEU-45.
PubMed=7213661; DOI=10.1016/0005-2795(80)90138-5;
Honig G.R., Vida L.N., Shamsuddin M., Mason R.G., Schlumpf H.W.,
Luke R.A.;
"Hemoglobin Milledgeville (alpha 44 (CD2) Pro leads to Leu): a new
variant with increased oxygen affinity.";
Biochim. Biophys. Acta 626:424-431(1980).
[51]
VARIANT LEGNANO LEU-142.
PubMed=7462179;
Giuliani A., Maffi D., Cappabianca M.P., Tentori L.;
"Hemoglobin Legnano (alpha 2 141 (HC3) Arg leads to Leu beta2) a new
high oxygen affinity variant. Functional and structural studies.";
J. Biochem. 88:1233-1237(1980).
[52]
VARIANT SURESNES HIS-142.
PubMed=7410435;
Poyart C., Bursaux E., Arnone A., Bonaventura J., Bonaventura C.;
"Structural and functional studies of hemoglobin Suresnes (arg 141
alpha 2 replaced by His beta 2). Consequences of disrupting an oxygen-
linked anion-binding site.";
J. Biol. Chem. 255:9465-9473(1980).
[53]
VARIANT FERNDOWN VAL-7.
PubMed=7238857; DOI=10.1016/0014-5793(81)81047-2;
Lee-Potter J.P., Deacon-Smith R.A., Lehmann H., Robb L.;
"Haemoglobin Ferndown (alpha 6 [A4] aspartic acid replaced by
valine).";
FEBS Lett. 126:117-119(1981).
[54]
VARIANT TOTTORI VAL-60.
PubMed=7275660; DOI=10.3109/03630268108991818;
Nakatsuji T., Miwa S., Ohba Y., Miyaji T., Matsumoto N., Matsuoka I.;
"Hemoglobin Tottori (alpha 59[E8] glycine replaced by valine).";
Hemoglobin 5:427-439(1981).
[55]
VARIANT KAWACHI ARG-45.
PubMed=7068434; DOI=10.3109/03630268208996932;
Harano T., Harano K., Ueda S., Shibata S., Imai K., Ohba Y.,
Shinohara T., Horio S., Nishioka K., Shirotani H.;
"Hemoglobin Kawachi [alpha 44 (CE2) Pro leads to Arg]: a new
hemoglobin variant of high oxygen affinity with amino acid
substitution at alpha 1 beta 2 contact.";
Hemoglobin 6:43-49(1982).
[56]
VARIANT KOKURA GLY-48.
PubMed=7068437; DOI=10.3109/03630268208996936;
Ohba Y., Hattori Y., Matsuoka M., Miyaji T., Fuyuno K.;
"HB Kokura [alpha 47 (CE 5) Asp leads to Gly]: a slightly unstable
variant.";
Hemoglobin 6:69-74(1982).
[57]
VARIANT EVANSTON ARG-15.
PubMed=6882779; DOI=10.1016/0167-4838(83)90122-X;
Moo-Penn W.F., Baine R.M., Jue D.L., Johnson M.H., McGuffey J.E.,
Benson J.M.;
"Hemoglobin Evanston: alpha 14(A12) Trp leads to Arg. A variant
hemoglobin associated with alpha-thalassemia-2.";
Biochim. Biophys. Acta 747:65-70(1983).
[58]
VARIANT TOKONAME THR-140.
PubMed=6188720; DOI=10.3109/03630268309038404;
Harano T., Harano K., Shibata S., Ueda S., Imai K., Seki M.;
"Hemoglobin Tokoname [alpha 139 (HC 1) Lys leads to Thr]: a new
hemoglobin variant with a slightly increased oxygen affinity.";
Hemoglobin 7:85-90(1983).
[59]
VARIANT IWATA ARG-88.
PubMed=6874376;
Liu G.Y., Zhang G.X., Nie S.Y., Luo H.Y., Teng Y.Q., Liu S.P.,
Song M., Son L., Chen S.S., Jia P.C., Liang C.C.;
"A case of hemoglobin Iwata [alpha 87(F8)His leads to Arg] in China.";
Hemoglobin 7:279-282(1983).
[60]
VARIANT ETOBICOKE ARG-85.
PubMed=6874377; DOI=10.3109/03630268309048660;
Headlee M.G., Nakatsuji T., Lam H., Wrightstone R.N., Huisman T.H.;
"Hb Etobicoke, alpha 85(F5) Ser leads to Arg found in a newborn of
French-Indian-English descent.";
Hemoglobin 7:285-287(1983).
[61]
VARIANT AICHI ARG-51.
PubMed=6714429; DOI=10.1016/0014-5793(84)80337-3;
Harano T., Harano K., Shibata S., Ueda S., Mori H., Seki M.;
"Hemoglobin Aichi [alpha 50(CE8) His----Arg]: a new slightly unstable
hemoglobin variant discovered in Japan.";
FEBS Lett. 169:297-299(1984).
[62]
VARIANT CORDELE ALA-48.
PubMed=6547117; DOI=10.3109/03630268408996959;
Nakatsuji T., Wilson J.B., Huisman T.H.;
"Hb Cordele alpha(2)47 (CE5)Asp----Ala beta 2. A mildly unstable
variant observed in black twins.";
Hemoglobin 8:37-46(1984).
[63]
VARIANT MANITOBA ARG-103, AND VARIANT CONTALDO ARG-104.
PubMed=6547932; DOI=10.3109/03630268408991710;
Sciarratta G.V., Ivaldi G., Molaro G.L., Sansone G., Salkie M.L.,
Wilson J.B., Reese A.L., Huisman T.H.;
"The characterization of hemoglobin Manitoba or alpha
(2)102(G9)Ser----Arg beta 2 and hemoglobin Contaldo or alpha
(2)103(G10)His----Arg beta 2 by high performance liquid
chromatography.";
Hemoglobin 8:169-181(1984).
[64]
CHARACTERIZATION OF VARIANT EVANSTON ARG-15.
PubMed=6725558; DOI=10.1172/JCI111382;
Honig G.R., Shamsuddin M., Vida L.N., Mompoint M., Valcourt E.,
Bowie L.J., Jones E.C., Powers P.A., Spritz R.A., Guis M.;
"Hemoglobin Evanston (alpha 14 Trp----Arg). An unstable alpha-chain
variant expressed as alpha-thalassemia.";
J. Clin. Invest. 73:1740-1749(1984).
[65]
VARIANT NUNOBIKI CYS-142.
PubMed=3973024; DOI=10.1172/JCI111749;
Shimasaki S.;
"A new hemoglobin variant, hemoglobin Nunobiki [alpha 141 (HC3)
Arg----Cys]. Notable influence of the carboxy-terminal cysteine upon
various physico-chemical characteristics of hemoglobin.";
J. Clin. Invest. 75:695-701(1985).
[66]
VARIANT LOIRE SER-89.
PubMed=3142772; DOI=10.1111/j.1432-1033.1988.tb14377.x;
Baklouti F., Baudin-Chich V., Kister J., Marden M., Teyssier G.,
Poyart C., Delaunay J., Wajcman H.;
"Increased oxygen affinity with normal heterotropic effects in
hemoglobin Loire [alpha 88(F9)Ala----Ser].";
Eur. J. Biochem. 177:307-312(1988).
[67]
VARIANT LUXEMBOURG HIS-25.
PubMed=2599879; DOI=10.3109/03630268908998082;
Groff P., Galacteros F., Kalmes G., Blouquit Y., Wajcman H.;
"Hb Luxembourg [alpha 24(B5) Tyr----His]: a new unstable variant.";
Hemoglobin 13:429-436(1989).
[68]
VARIANT MIYANO SER-42.
PubMed=2634665; DOI=10.3109/03630268908998841;
Ohba Y., Imai K., Uenaka R., Ami M., Fujisawa K., Itoh K.,
Hirakawa K., Miyaji T.;
"Hb Miyano or alpha 41(C6)Thr----Ser: a new high oxygen affinity alpha
chain variant found in an erythremic blood donor.";
Hemoglobin 13:637-647(1989).
[69]
VARIANT REIMS GLY-24.
PubMed=2634669; DOI=10.3109/03630268908998846;
Bardakdjian-Michau J., Rosa J., Galacteros F., Lancelot M.,
Marquart F.X.;
"Hb Reims [alpha 2(23)(B4)Glu----Gly beta 2]: a new alpha chain
variant with slightly decreased stability.";
Hemoglobin 13:733-735(1989).
[70]
VARIANT ATTLEBORO PRO-139.
PubMed=2108715; DOI=10.1021/bi00453a023;
McDonald M.J., Michalski L.A., Turci S.M., Guillette R.A., Jue D.L.,
Johnson M.H., Moo-Penn W.F.;
"Structural, functional, and subunit assembly properties of hemoglobin
Attleboro [alpha 138 (H21) Ser----Pro], a variant possessing a site
maturation at a critical C-terminal residue.";
Biochemistry 29:173-178(1990).
[71]
VARIANT FUKUTOMI VAL-127.
PubMed=2079432; DOI=10.3109/03630269009005803;
Hidaka K., Iuchi I., Kobayashi T., Katoh K., Yaguchi K.;
"Hb Fukutomi [alpha 126(H9)Asp----Val]: a new hemoglobin variant with
high oxygen affinity.";
Hemoglobin 14:499-509(1990).
[72]
VARIANT DALLAS LYS-98.
PubMed=1390940; DOI=10.1016/0925-4439(92)90021-E;
Lendaro E., Ippoliti R., Brancaccio A., Bellelli A., Vallone B.,
Ivaldi G., Sciarratta G.V., Castello C., Tomova S., Brunori M.;
"Hemoglobin Dallas (alpha 97(G4)Asn-->Lys): functional
characterization of a high oxygen affinity natural mutant.";
Biochim. Biophys. Acta 1180:15-20(1992).
[73]
VARIANT ROUEN/ETHIOPIA HIS-141.
PubMed=1390944; DOI=10.1016/0925-4439(92)90026-J;
Wajcman H., Kister J., Marden M., Lahary A., Monconduit M.,
Galacteros F.;
"Hemoglobin Rouen (alpha-140 (HC2) Tyr-->His): alteration of the
alpha-chain C-terminal region and moderate increase in oxygen
affinity.";
Biochim. Biophys. Acta 1180:53-57(1992).
[74]
VARIANT AL-AIN ABU DHABI ASP-19.
PubMed=1428941; DOI=10.3109/03630269209005687;
Abbes S., M'Rad A., Fitzgerald P.A., Dormer P., Blouquit Y.,
Kister J., Galacteros F., Wajcman H.;
"HB Al-Ain Abu Dhabi [alpha 18(A16)Gly-->Asp]: a new hemoglobin
variant discovered in an Emiratee family.";
Hemoglobin 16:355-362(1992).
[75]
VARIANT QUESTEMBERT PRO-132.
PubMed=8493987; DOI=10.1002/ajh.2830420407;
Wajcman H., Vasseur C., Blouquit Y., Rosa J., Labie D., Najman A.,
Reman O., Leporrier M., Galacteros F.;
"Unstable alpha-chain hemoglobin variants with factitious beta-
thalassemia biosynthetic ratio: Hb Questembert (alpha
131[H14]Ser-->Pro) and Hb Caen (alpha 132[H15]Val-->Gly).";
Am. J. Hematol. 42:367-374(1993).
[76]
VARIANT ADANA ASP-60.
PubMed=8237999; DOI=10.1002/ajh.2830440410;
Cueruek M.A., Dimovski A.J., Baysal E., Gu L.H., Kutlar F.,
Molchanova T.P., Webber B.B., Altay C., Guergey A., Huisman T.H.;
"Hb Adana or alpha 2(59)(E8)Gly-->Asp beta 2, a severely unstable
alpha 1-globin variant, observed in combination with the -(alpha)20.5
Kb alpha-thal-1 deletion in two Turkish patients.";
Am. J. Hematol. 44:270-275(1993).
[77]
VARIANT MONTEFIORE TYR-127.
PubMed=8798486; DOI=10.1074/jbc.271.38.22990;
Wajcman H., Kister J., Galacteros F., Spielvogel A., Lin M.J.,
Vidugiris G.J., Hirsch R.E., Friedman J.M., Nagel R.L.;
"Hb Montefiore (126(H9)Asp-->Tyr). High oxygen affinity and loss of
cooperativity secondary to C-terminal disruption.";
J. Biol. Chem. 271:22990-22998(1996).
[78]
VARIANT ATAGO TYR-86.
PubMed=5115619;
Fujiwara N., Maekawa T., Matsuda G.;
"Hemoglobin Atago (alpha2-85 Tyr beta-2) a new abnormal human
hemoglobin found in Nagasaki. Biochemical studies on hemoglobins and
myoglobins. VI.";
Int. J. Protein Res. 3:35-39(1971).
[79]
VARIANT AUCKLAND ASN-88.
PubMed=9322075; DOI=10.3109/03630269708993126;
Brennan S.O., Matthews J.R.;
"Hb Auckland [alpha 87(F8) His-->Asn]: a new mutation of the proximal
histidine identified by electrospray mass spectrometry.";
Hemoglobin 21:393-403(1997).
[80]
VARIANTS J-BUDA ASN-62 AND G-PEST ASN-75.
Brimhall B.J., Duerst M., Hollan S.R., Stenzel P., Szelenyi J.,
Jones R.T.;
"Structural characterizations of hemoglobins J-Buda (alpha 61 (E10)
Lys-to-Asn) and G-Pest (alpha 74 (EF3) Asp-to-Asn).";
Biochim. Biophys. Acta 336:344-360(1974).
[81]
VARIANT CEMENELUM TRP-93.
PubMed=8148419; DOI=10.1007/BF01715134;
Wajcman H., Kister J., M'Rad A., Soummer A.M., Galacteros F.;
"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.";
Ann. Hematol. 68:73-76(1994).
[82]
VARIANTS CHONGQING ARG-3 AND HARBIN MET-17.
PubMed=6526652; DOI=10.3109/03630268408991742;
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 Chongqing [alpha 2(NA2)Leu-->Arg] and hemoglobin Harbin
[alpha 16(A14)Lys-->Met] found in China.";
Hemoglobin 8:569-581(1984).
[83]
VARIANT CLINIC LYS-61 DEL.
PubMed=10206681;
DOI=10.1002/(SICI)1098-1004(1998)11:5<412::AID-HUMU14>3.0.CO;2-R;
Ayala S., Colomer D., Gelpi J.L., Corron J.L.V.;
"Alpha-thalassaemia due to a single codon deletion in the alpha 1-
globin gene. Computational structural analysis of the new alpha-chain
variant.";
Hum. Mutat. 11:412-412(1998).
[84]
VARIANT DAVENPORT HIS-79.
PubMed=2101836; DOI=10.3109/03630269009046968;
Wilson J.B., Webber B.B., Plaseska D., de Alarcon P.A., McMillan S.K.,
Huisman T.H.J.;
"Hb Davenport or alpha 2(78)(EF7)Asn-->His beta 2.";
Hemoglobin 14:599-605(1990).
[85]
VARIANT EVANS MET-63.
PubMed=2606724; DOI=10.3109/03630268908993106;
Wilson J.B., Webber B.B., Kutlar A., Reese A.L., McKie V.C.,
Lutcher C.L., Felice A.E., Huisman T.H.J.;
"Hb Evans or alpha 262(E11)Val-->Met beta 2; an unstable hemoglobin
causing a mild hemolytic anemia.";
Hemoglobin 13:557-566(1989).
[86]
VARIANTS SPANISH TOWN VAL-28 AND FORT DE FRANCE ARG-46.
PubMed=2752146;
Cash F.E., Monplaisir N., Goossens M., Liebhaber S.A.;
"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).";
Blood 74:833-835(1989).
[87]
VARIANT GODAVARI THR-96.
PubMed=9494044; DOI=10.3109/03630269809071513;
Wajcman H., Kister J., Riou J., Galacteros F., Girot R.,
Maier-Redelsperger M., Nayudu N.V.S., Giordano P.C.;
"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.";
Hemoglobin 22:11-22(1998).
[88]
VARIANT GRADY GLU-PHE-THR-119 INS.
PubMed=4528583; DOI=10.1073/pnas.71.8.3270;
Huisman T.H.J., Wilson J.B., Gravely M., Hubbard M.;
"Hemoglobin Grady: the first example of a variant with elongated
chains due to an insertion of residues.";
Proc. Natl. Acad. Sci. U.S.A. 71:3270-3273(1974).
[89]
VARIANT HANAMAKI GLU-140.
PubMed=1634363; DOI=10.3109/03630269209005677;
Orisaka M., Tajima T., Harano T., Harano K., Kushida Y., Imai K.;
"A new alpha chain variant, Hb Hanamaki or alpha 2(139)(HC1)Lys-->Glu
beta 2, found in a Japanese family.";
Hemoglobin 16:67-71(1992).
[90]
VARIANT HANDA MET-91.
PubMed=6815131; DOI=10.3109/03630268208996943;
Harano T., Harano K., Shibata S., Ueda S., Imai K., Seki M.;
"HB Handa [alpha 90 (FG 2) Lys replaced by Met]: structure and
biosynthesis of a new slightly higher oxygen affinity variant.";
Hemoglobin 6:379-389(1982).
[91]
VARIANT HASHARON HIS-48.
PubMed=5780195; DOI=10.1172/JCI106041;
Charache S., Mondzac A.M., Gessner U.;
"Hemoglobin Hasharon (alpha-2-47 his(CD5)beta-2): a hemoglobin found
in low concentration.";
J. Clin. Invest. 48:834-847(1969).
[92]
VARIANT HOBART ARG-21.
PubMed=3654264; DOI=10.3109/03630268709017887;
Fleming P.J., Sumner D.R., Wyatt K., Hughes W.G., Melrose W.D.,
Jupe D.M.D., Baikie M.J.;
"Hemoglobin Hobart or alpha 20(Bl)His-->Arg: a new alpha chain
hemoglobin variant.";
Hemoglobin 11:211-220(1987).
[93]
VARIANT INKSTER VAL-86.
PubMed=4212045; DOI=10.1111/j.1365-2141.1974.tb00489.x;
Reed R.E., Winter W.P., Rucknagel D.L.;
"Haemoglobin Inkster (alpha2 85aspartic acid leads to valine beta2)
coexisting with beta-thalassaemia in a Caucasian family.";
Br. J. Haematol. 26:475-484(1974).
[94]
VARIANT KANAGAWA MET-41.
PubMed=1634355; DOI=10.3109/03630269209005670;
Miyashita H., Hashimoto K., Mohri H., Ohokubo T., Harano T.,
Harano K., Imai K.;
"Hb Kanagawa [alpha 40(C5)Lys-->Met]: a new alpha chain variant with
an increased oxygen affinity.";
Hemoglobin 16:1-10(1992).
[95]
VARIANT KURDISTAN TYR-48.
PubMed=8195005; DOI=10.3109/03630269409014141;
Giordano P.C., Harteveld C.L., Streng H., Oosterwijk J.C.,
Heister J.G.A.M., Amons R., Bernini L.F.;
"Hb Kurdistan [alpha 47(CE5)Asp-->Tyr], a new alpha chain variant in
combination with beta (0)-thalassemia.";
Hemoglobin 18:11-18(1994).
[96]
VARIANT KUROSAKI GLU-8.
PubMed=7558876; DOI=10.3109/03630269509036940;
Harano T., Harano K., Imai K., Murakami T., Matsubara H.;
"Hb Kurosaki [alpha 7(A5)Lys-->Glu]: a new alpha chain variant found
in a Japanese woman.";
Hemoglobin 19:197-201(1995).
[97]
VARIANT J-MEERUT/J-BIRMINGHAM GLU-121.
PubMed=7713747; DOI=10.3109/03630269409045775;
Yalcin A., Avcu F., Beyan C., Guergey A., Ural A.U.;
"A case of HB J-Meerut (or Hb J-Birmingham) [alpha
120(H3)Ala-->Glu].";
Hemoglobin 18:433-435(1994).
[98]
VARIANT MELUSINE SER-115.
PubMed=8294199; DOI=10.3109/03630269308997494;
Wacjman H., Klames G., Groff P., Prome D., Riou J., Galacteros F.;
"Hb Melusine [alpha 114(GH2)Pro-->Ser]: a new neutral hemoglobin
variant.";
Hemoglobin 17:397-405(1993).
[99]
VARIANT MONTGOMERY ARG-49.
PubMed=1115799;
Brimhall B., Jones R.T., Schneider R.G., Hosty T.S., Tomlin G.,
Atkins R.;
"Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys)
and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg).";
Biochim. Biophys. Acta 379:28-32(1975).
[100]
VARIANT PETAH TIKVA ASP-111.
PubMed=7470621;
Honig G.R., Shamsuddin M., Zaizov R., Steinherz M., Solar I.,
Kirschman C.;
"Hemoglobin Petah Tikva (alpha 110 Ala replaced by Asp): a new
unstable variant with alpha-thalassemia-like expression.";
Blood 57:705-711(1981).
[101]
VARIANT PHNOM PENH ILE-118 INS.
PubMed=9452028;
Wajcman H., Prehu M.O., Prehu C., Blouquit Y., Prome D.,
Galacteros F.;
"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.";
Hum. Mutat. Suppl. 1:S20-S22(1998).
[102]
VARIANT PORT HURON ARG-57.
PubMed=1802882; DOI=10.3109/03630269108998858;
Zwerdling T., Williams S., Nasr S.A., Rucknagel D.L.;
"Hb Port Huron [alpha 56 (E5)Lys-->Arg]: a new alpha chain variant.";
Hemoglobin 15:381-391(1991).
[103]
VARIANT SHENYANG GLU-27.
PubMed=7161109;
Zeng Y.-T., Huang S.-Z., Zhou X., Qiu X.-K., Dong Q., Li M., Bai J.;
"Hb Shenyang (alpha 26 (B7) Ala replaced by Glu): a new unstable
variant found in China.";
Hemoglobin 6:625-628(1982).
[104]
VARIANT SUAN-DOK ARG-110.
PubMed=478977; DOI=10.3109/03630267908998911;
Sanguansermsri T., Matragoon S., Changloah L., Flatz G.;
"Hemoglobin Suan-Dok (alpha 2 109 (G16) Leu replaced by Arg beta 2):
an unstable variant associated with alpha-thalassemia.";
Hemoglobin 3:161-174(1979).
[105]
INVOLVEMENT IN HEIBAN, AND VARIANT TOYAMA ARG-137.
PubMed=2833478; DOI=10.3109/03630268709027870;
Ohba Y., Yamamoto K., Hattori Y., Kawata R., Miyaji T.;
"Hyperunstable hemoglobin Toyama [alpha 2 136(H19)Leu----Arg beta 2]:
detection and identification by in vitro biosynthesis with radioactive
amino acids.";
Hemoglobin 11:539-556(1987).
[106]
VARIANT SUN PRAIRIE PRO-131.
PubMed=2079430; DOI=10.3109/03630269009005801;
Harkness M., Harkness D.R., Kutlar F., Kutlar A., Wilson J.B.,
Webber B.B., Codrington J.F., Huisman T.H.J.;
"Hb Sun Prairie or alpha(2)130(H13)Ala-->Pro beta 2, a new unstable
variant occurring in low quantities.";
Hemoglobin 14:479-489(1990).
[107]
VARIANT SWAN RIVER GLY-7.
PubMed=8745434; DOI=10.3109/03630269609027912;
Harano T., Harano K., Imai K., Terunuma S.;
"HB Swan River [alpha 6(A4)Asp-->Gly] observed in a Japanese man.";
Hemoglobin 20:75-78(1996).
[108]
VARIANT THIONVILLE GLU-2.
PubMed=1618774;
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.;
"Hemoglobin Thionville. An alpha-chain variant with a substitution of
a glutamate for valine at NA-1 and having an acetylated methionine NH2
terminus.";
J. Biol. Chem. 267:12682-12691(1992).
[109]
VARIANT TUNIS-BIZERTE PRO-130.
PubMed=7786798; DOI=10.1111/j.1365-2141.1995.tb03382.x;
Darbellay R., Mach-Pascual S., Rose K., Graf J., Beris P.;
"Haemoglobin Tunis-Bizerte: a new alpha 1 globin 129 Leu-->Pro
unstable variant with thalassaemic phenotype.";
Br. J. Haematol. 90:71-76(1995).
[110]
VARIANT TURRIFF GLU-100.
PubMed=1634357; DOI=10.3109/03630269209005671;
Langdown J.V., Davidson R.J., Williamson D.;
"A new alpha chain variant, Hb Turriff [alpha 99(G6)Lys-->Glu]: the
interference of abnormal hemoglobins in Hb A1c determination.";
Hemoglobin 16:11-17(1992).
[111]
VARIANT VAL DE MARNE ARG-134.
PubMed=8294200; DOI=10.3109/03630269308997495;
Wacjman H., Kister J., M'Rad A., Marden M.C., Riou J., Galacteros F.;
"Hb Val de Marne [alpha 133(H16)Ser-->Arg]: a new hemoglobin variant
with moderate increase in oxygen affinity.";
Hemoglobin 17:407-417(1993).
[112]
VARIANT WESTMEAD GLN-123.
PubMed=1686260; DOI=10.3109/03630269109027881;
Jiang N.H., Liang S., Wen X.J., Liang R., Su C., Tang Z.;
"Hb Westmead: an alpha 2-globin gene mutation detected by polymerase
chain reaction and Stu I cleavage.";
Hemoglobin 15:291-295(1991).
[113]
VARIANT WOODVILLE TYR-7.
PubMed=3754246; DOI=10.3109/03630268609046440;
Como P.F., Barber S., Sage R.E., Kronenberg H.;
"Hemoglobin Woodville: alpha (2)6(A4) aspartic acid-->tyrosine.";
Hemoglobin 10:135-141(1986).
[114]
VARIANT YUDA ASP-131.
PubMed=1428950; DOI=10.3109/03630269209005698;
Fujisawa K., Hattori Y., Ohba Y., Ando S.;
"Hb Yuda or alpha 130(H13)Ala-->Asp; a new alpha chain variant with
low oxygen affinity.";
Hemoglobin 16:435-439(1992).
[115]
VARIANT ZAIRE HIS-LEU-PRO-ALA-GLU-117 INS.
PubMed=1511986; DOI=10.1007/BF00221961;
Wajcman H., Blouquit Y., Vasseur C., le Querrec A., Laniece M.,
Melevendi C., Rasore A., Galacteros F.;
"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.";
Hum. Genet. 89:676-680(1992).
[116]
VARIANT HBH VAL-63 DEL.
PubMed=10569720; DOI=10.3109/03630269909090747;
Traeger-Synodinos J., Harteveld C.L., Kanavakis E., Giordano P.C.,
Kattamis C., Bernini L.F.;
"Hb Aghia Sophia [alpha62(E11)Val-->0 (alpha1)], an 'in-frame'
deletion causing alpha-thalassemia.";
Hemoglobin 23:317-324(1999).
[117]
VARIANT BOGHE GLN-59, AND VARIANT CHAROLLES TYR-104.
PubMed=10569723; DOI=10.3109/03630269909090750;
Lacan P., Francina A., Souillet G., Aubry M., Couprie N.,
Dementhon L., Becchi M.;
"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].";
Hemoglobin 23:345-352(1999).
[118]
VARIANT CAMPINAS VAL-27, AND VARIANT WEST ONE GLY-127.
PubMed=14576901; DOI=10.1590/S0100-879X2003001100004;
Jorge S.B., Melo M.B., Costa F.F., Sonati M.F.;
"Screening for mutations in human alpha-globin genes by nonradioactive
single-strand conformation polymorphism.";
Braz. J. Med. Biol. Res. 36:1471-1474(2003).
[119]
VARIANT BASSETT ALA-95, AND CHARACTERIZATION OF VARIANT BASSETT
ALA-95.
PubMed=15495251; DOI=10.1002/ajh.20184;
Abdulmalik O., Safo M.K., Lerner N.B., Ochotorena J., Daikhin E.,
Lakka V., Santacroce R., Abraham D.J., Asakura T.;
"Characterization of hemoglobin Bassett (alpha94Asp-->Ala), a variant
with very low oxygen affinity.";
Am. J. Hematol. 77:268-276(2004).
[120]
VARIANT PLASENCIA ARG-126.
PubMed=15921163; DOI=10.1081/HEM-58578;
Martin G., Villegas A., Gonzalez F.A., Ropero P., Hojas R., Polo M.,
Mateo M., Salvador M., Benavente C.;
"A novel mutation of the alpha2-globin causing alpha(+)-thalassemia:
Hb Plasencia [alpha125(H8)Leu-->Arg (alpha2).";
Hemoglobin 29:113-117(2005).
-!- FUNCTION: Involved in oxygen transport from the lung to the
various peripheral tissues.
-!- SUBUNIT: 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).
-!- INTERACTION:
Q2TAC2:CCDC57; NbExp=3; IntAct=EBI-714680, EBI-2808286;
P68871:HBB; NbExp=22; IntAct=EBI-714680, EBI-715554;
P02100:HBE1; NbExp=3; IntAct=EBI-714680, EBI-6190240;
P69892:HBG2; NbExp=3; IntAct=EBI-714680, EBI-3910089;
Q6A162:KRT40; NbExp=3; IntAct=EBI-714680, EBI-10171697;
-!- TISSUE SPECIFICITY: Red blood cells.
-!- PTM: The initiator Met is not cleaved in variant Thionville and is
acetylated.
-!- 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.
{ECO:0000269|PubMed:2833478}. Note=The disease may be caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: 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.
-!- DISEASE: Note=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.
-!- DISEASE: 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.
{ECO:0000269|PubMed:10569720}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Gives blood its red color.
-!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
ProRule:PRU00238}.
-!- SEQUENCE CAUTION:
Sequence=BAD97112.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=HbVar; Note=Human hemoglobin variants and
thalassemias;
URL="http://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBA1";
-!- WEB RESOURCE: Name=HbVar; Note=Human hemoglobin variants and
thalassemias;
URL="http://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBA2";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=HBA1";
-!- WEB RESOURCE: Name=Wikipedia; Note=Hemoglobin entry;
URL="https://en.wikipedia.org/wiki/Hemoglobin";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Journey into a tiny
world - Issue 84 of July 2007;
URL="http://web.expasy.org/spotlight/back_issues/084/";
-----------------------------------------------------------------------
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EMBL; J00153; AAB59407.1; -; Genomic_DNA.
EMBL; J00153; AAB59408.1; -; Genomic_DNA.
EMBL; V00491; CAA23750.1; -; Genomic_DNA.
EMBL; V00493; CAA23752.1; -; mRNA.
EMBL; V00488; CAA23748.1; -; Genomic_DNA.
EMBL; V00516; CAA23774.1; -; Genomic_DNA.
EMBL; AF230076; AAF72612.1; -; Genomic_DNA.
EMBL; AF525460; AAM83102.1; -; Genomic_DNA.
EMBL; DQ431198; ABD95910.1; -; Genomic_DNA.
EMBL; DQ431198; ABD95911.1; -; Genomic_DNA.
EMBL; AF097635; AAC72839.1; -; mRNA.
EMBL; AF105974; AAC97373.1; -; mRNA.
EMBL; AF349571; AAK37554.1; -; mRNA.
EMBL; AF536204; AAN04486.1; -; Genomic_DNA.
EMBL; DQ499017; ABF56144.1; -; Genomic_DNA.
EMBL; DQ499018; ABF56145.1; -; Genomic_DNA.
EMBL; AK223392; BAD97112.1; ALT_INIT; mRNA.
EMBL; AE006462; AAK61215.1; -; Genomic_DNA.
EMBL; AE006462; AAK61216.1; -; Genomic_DNA.
EMBL; Z84721; CAB06554.1; -; Genomic_DNA.
EMBL; Z84721; CAB06555.1; -; Genomic_DNA.
EMBL; BC005931; AAH05931.1; -; mRNA.
EMBL; BC008572; AAH08572.1; -; mRNA.
EMBL; BC032122; AAH32122.1; -; mRNA.
EMBL; BC050661; AAH50661.1; -; mRNA.
EMBL; BC101846; AAI01847.1; -; mRNA.
EMBL; BC101848; AAI01849.1; -; mRNA.
CCDS; CCDS10398.1; -.
CCDS; CCDS10399.1; -.
PIR; A90807; HAHU.
PIR; C93303; HACZP.
PIR; I58217; HACZ.
RefSeq; NP_000508.1; NM_000517.4.
RefSeq; NP_000549.1; NM_000558.4.
UniGene; Hs.449630; -.
UniGene; Hs.654744; -.
PDB; 1A00; X-ray; 2.00 A; A/C=2-142.
PDB; 1A01; X-ray; 1.80 A; A/C=2-142.
PDB; 1A0U; X-ray; 2.14 A; A/C=2-142.
PDB; 1A0Z; X-ray; 2.00 A; A/C=2-142.
PDB; 1A3N; X-ray; 1.80 A; A/C=2-142.
PDB; 1A3O; X-ray; 1.80 A; A/C=2-142.
PDB; 1A9W; X-ray; 2.90 A; A/C=2-142.
PDB; 1ABW; X-ray; 2.00 A; A=1-142.
PDB; 1ABY; X-ray; 2.60 A; A=1-142.
PDB; 1AJ9; X-ray; 2.20 A; A=2-142.
PDB; 1B86; X-ray; 2.50 A; A/C=2-142.
PDB; 1BAB; X-ray; 1.50 A; A/C=1-142.
PDB; 1BBB; X-ray; 1.70 A; A/C=2-142.
PDB; 1BIJ; X-ray; 2.30 A; A/C=2-142.
PDB; 1BUW; X-ray; 1.90 A; A/C=2-142.
PDB; 1BZ0; X-ray; 1.50 A; A/C=2-142.
PDB; 1BZ1; X-ray; 1.59 A; A/C=1-142.
PDB; 1BZZ; X-ray; 1.59 A; A/C=2-142.
PDB; 1C7B; X-ray; 1.80 A; A/C=2-142.
PDB; 1C7C; X-ray; 1.80 A; A=2-142.
PDB; 1C7D; X-ray; 1.80 A; A=2-142.
PDB; 1CLS; X-ray; 1.90 A; A/C=2-142.
PDB; 1CMY; X-ray; 3.00 A; A/C=2-142.
PDB; 1COH; X-ray; 2.90 A; A/C=2-142.
PDB; 1DKE; X-ray; 2.10 A; A/C=2-142.
PDB; 1DXT; X-ray; 1.70 A; A/C=2-142.
PDB; 1DXU; X-ray; 1.70 A; A/C=2-142.
PDB; 1DXV; X-ray; 1.70 A; A/C=2-142.
PDB; 1FDH; X-ray; 2.50 A; A/B=2-142.
PDB; 1FN3; X-ray; 2.48 A; A/C=2-142.
PDB; 1G9V; X-ray; 1.85 A; A/C=2-142.
PDB; 1GBU; X-ray; 1.80 A; A/C=2-142.
PDB; 1GBV; X-ray; 2.00 A; A/C=2-142.
PDB; 1GLI; X-ray; 2.50 A; A/C=3-142.
PDB; 1GZX; X-ray; 2.10 A; A/C=2-142.
PDB; 1HAB; X-ray; 2.30 A; A/C=2-142.
PDB; 1HAC; X-ray; 2.60 A; A/C=2-142.
PDB; 1HBA; X-ray; 2.10 A; A/C=2-142.
PDB; 1HBB; X-ray; 1.90 A; A/C=2-142.
PDB; 1HBS; X-ray; 3.00 A; A/C/E/G=2-142.
PDB; 1HCO; X-ray; 2.70 A; A=2-142.
PDB; 1HDB; X-ray; 2.20 A; A/C=2-142.
PDB; 1HGA; X-ray; 2.10 A; A/C=2-142.
PDB; 1HGB; X-ray; 2.10 A; A/C=2-142.
PDB; 1HGC; X-ray; 2.10 A; A/C=2-142.
PDB; 1HHO; X-ray; 2.10 A; A=2-142.
PDB; 1IRD; X-ray; 1.25 A; A=2-142.
PDB; 1J3Y; X-ray; 1.55 A; A/C/E/G=2-142.
PDB; 1J3Z; X-ray; 1.60 A; A/C/E/G=2-142.
PDB; 1J40; X-ray; 1.45 A; A/C/E/G=2-142.
PDB; 1J41; X-ray; 1.45 A; A/C/E/G=2-142.
PDB; 1J7S; X-ray; 2.20 A; A/C=2-142.
PDB; 1J7W; X-ray; 2.00 A; A/C=2-142.
PDB; 1J7Y; X-ray; 1.70 A; A/C=2-142.
PDB; 1JY7; X-ray; 3.20 A; A/C/P/R/U/W=2-142.
PDB; 1K0Y; X-ray; 1.87 A; A/C=2-142.
PDB; 1K1K; X-ray; 2.00 A; A=2-142.
PDB; 1KD2; X-ray; 1.87 A; A/C=2-142.
PDB; 1LFL; X-ray; 2.70 A; A/C/P/R=2-142.
PDB; 1LFQ; X-ray; 2.60 A; A=2-142.
PDB; 1LFT; X-ray; 2.60 A; A=2-142.
PDB; 1LFV; X-ray; 2.80 A; A=2-142.
PDB; 1LFY; X-ray; 3.30 A; A=2-142.
PDB; 1LFZ; X-ray; 3.10 A; A=2-142.
PDB; 1LJW; X-ray; 2.16 A; A=2-142.
PDB; 1M9P; X-ray; 2.10 A; A/C=2-142.
PDB; 1MKO; X-ray; 2.18 A; A/C=2-142.
PDB; 1NEJ; X-ray; 2.10 A; A/C=2-142.
PDB; 1NIH; X-ray; 2.60 A; A/C=2-142.
PDB; 1NQP; X-ray; 1.73 A; A/C=2-142.
PDB; 1O1I; X-ray; 2.30 A; A=2-142.
PDB; 1O1J; X-ray; 1.90 A; A=2-142.
PDB; 1O1K; X-ray; 2.00 A; A/C=3-142.
PDB; 1O1L; X-ray; 1.80 A; A=2-142.
PDB; 1O1M; X-ray; 1.85 A; A=2-142.
PDB; 1O1N; X-ray; 1.80 A; A=2-142.
PDB; 1O1O; X-ray; 1.80 A; A/C=2-142.
PDB; 1O1P; X-ray; 1.80 A; A=2-142.
PDB; 1QI8; X-ray; 1.80 A; A/C=3-142.
PDB; 1QSH; X-ray; 1.70 A; A/C=2-142.
PDB; 1QSI; X-ray; 1.70 A; A/C=2-142.
PDB; 1QXD; X-ray; 2.25 A; A/C=2-142.
PDB; 1QXE; X-ray; 1.85 A; A/C=2-142.
PDB; 1R1X; X-ray; 2.15 A; A=2-142.
PDB; 1R1Y; X-ray; 1.80 A; A/C=2-142.
PDB; 1RPS; X-ray; 2.11 A; A/C=2-142.
PDB; 1RQ3; X-ray; 1.91 A; A/C=2-142.
PDB; 1RQ4; X-ray; 2.11 A; A/C=2-142.
PDB; 1RQA; X-ray; 2.11 A; A/C=2-142.
PDB; 1RVW; X-ray; 2.50 A; A=2-142.
PDB; 1SDK; X-ray; 1.80 A; A/C=2-142.
PDB; 1SDL; X-ray; 1.80 A; A/C=2-142.
PDB; 1SHR; X-ray; 1.88 A; A/C=2-142.
PDB; 1SI4; X-ray; 2.20 A; A/C=2-142.
PDB; 1THB; X-ray; 1.50 A; A/C=2-142.
PDB; 1UIW; X-ray; 1.50 A; A/C/E/G=2-142.
PDB; 1VWT; X-ray; 1.90 A; A/C=2-142.
PDB; 1XXT; X-ray; 1.91 A; A/C=2-142.
PDB; 1XY0; X-ray; 1.99 A; A/C=2-142.
PDB; 1XYE; X-ray; 2.13 A; A/C=3-142.
PDB; 1XZ2; X-ray; 1.90 A; A/C=2-142.
PDB; 1XZ4; X-ray; 2.00 A; A/C=3-142.
PDB; 1XZ5; X-ray; 2.11 A; A/C=2-142.
PDB; 1XZ7; X-ray; 1.90 A; A/C=2-142.
PDB; 1XZU; X-ray; 2.16 A; A/C=2-142.
PDB; 1XZV; X-ray; 2.11 A; A/C=2-142.
PDB; 1Y01; X-ray; 2.80 A; B=1-142.
PDB; 1Y09; X-ray; 2.25 A; A/C=2-142.
PDB; 1Y0A; X-ray; 2.22 A; A/C=2-140.
PDB; 1Y0C; X-ray; 2.30 A; A/C=2-140.
PDB; 1Y0D; X-ray; 2.10 A; A/C=2-141.
PDB; 1Y0T; X-ray; 2.14 A; A/C=2-142.
PDB; 1Y0W; X-ray; 2.14 A; A/C=2-142.
PDB; 1Y22; X-ray; 2.16 A; A/C=2-142.
PDB; 1Y2Z; X-ray; 2.07 A; A/C=2-142.
PDB; 1Y31; X-ray; 2.13 A; A/C=2-142.
PDB; 1Y35; X-ray; 2.12 A; A/C=2-142.
PDB; 1Y45; X-ray; 2.00 A; A/C=2-142.
PDB; 1Y46; X-ray; 2.22 A; A/C=2-142.
PDB; 1Y4B; X-ray; 2.10 A; A/C=2-142.
PDB; 1Y4F; X-ray; 2.00 A; A/C=2-142.
PDB; 1Y4G; X-ray; 1.91 A; A/C=2-142.
PDB; 1Y4P; X-ray; 1.98 A; A/C=2-142.
PDB; 1Y4Q; X-ray; 2.11 A; A/C=2-142.
PDB; 1Y4R; X-ray; 2.22 A; A/C=2-142.
PDB; 1Y4V; X-ray; 1.84 A; A/C=2-142.
PDB; 1Y5F; X-ray; 2.14 A; A/C=2-142.
PDB; 1Y5J; X-ray; 2.03 A; A/C=2-142.
PDB; 1Y5K; X-ray; 2.20 A; A/C=2-142.
PDB; 1Y7C; X-ray; 2.10 A; A/C=2-142.
PDB; 1Y7D; X-ray; 1.90 A; A/C=2-142.
PDB; 1Y7G; X-ray; 2.10 A; A/C=2-142.
PDB; 1Y7Z; X-ray; 1.98 A; A/C=2-142.
PDB; 1Y83; X-ray; 1.90 A; A/C=2-142.
PDB; 1Y85; X-ray; 2.13 A; A/C=2-142.
PDB; 1Y8W; X-ray; 2.90 A; A/C=2-142.
PDB; 1YDZ; X-ray; 3.30 A; A/C=2-140.
PDB; 1YE0; X-ray; 2.50 A; A/C=2-142.
PDB; 1YE1; X-ray; 4.50 A; A/C=2-142.
PDB; 1YE2; X-ray; 1.80 A; A/C=2-142.
PDB; 1YEN; X-ray; 2.80 A; A/C=2-142.
PDB; 1YEO; X-ray; 2.22 A; A/C=2-142.
PDB; 1YEQ; X-ray; 2.75 A; A/C=2-142.
PDB; 1YEU; X-ray; 2.12 A; A/C=2-142.
PDB; 1YEV; X-ray; 2.11 A; A/C=2-142.
PDB; 1YFF; X-ray; 2.40 A; A/C/E/G=2-142.
PDB; 1YG5; X-ray; 2.70 A; A/C=2-142.
PDB; 1YGD; X-ray; 2.73 A; A/C=2-142.
PDB; 1YGF; X-ray; 2.70 A; A/C=2-142.
PDB; 1YH9; X-ray; 2.20 A; A/C=2-142.
PDB; 1YHE; X-ray; 2.10 A; A/C=2-142.
PDB; 1YHR; X-ray; 2.60 A; A/C=2-142.
PDB; 1YIE; X-ray; 2.40 A; A/C=2-142.
PDB; 1YIH; X-ray; 2.00 A; A/C=2-142.
PDB; 1YVQ; X-ray; 1.80 A; A/C=2-142.
PDB; 1YVT; X-ray; 1.80 A; A=2-142.
PDB; 1YZI; X-ray; 2.07 A; A=2-142.
PDB; 1Z8U; X-ray; 2.40 A; B/D=1-142.
PDB; 2D5Z; X-ray; 1.45 A; A/C=2-142.
PDB; 2D60; X-ray; 1.70 A; A/C=2-142.
PDB; 2DN1; X-ray; 1.25 A; A=2-142.
PDB; 2DN2; X-ray; 1.25 A; A/C=2-142.
PDB; 2DN3; X-ray; 1.25 A; A=2-142.
PDB; 2DXM; Neutron; 2.10 A; A/C=2-142.
PDB; 2H35; NMR; -; A/C=2-142.
PDB; 2HBC; X-ray; 2.10 A; A=2-142.
PDB; 2HBD; X-ray; 2.20 A; A=2-142.
PDB; 2HBE; X-ray; 2.00 A; A=2-142.
PDB; 2HBF; X-ray; 2.20 A; A=2-142.
PDB; 2HBS; X-ray; 2.05 A; A/C/E/G=2-142.
PDB; 2HCO; X-ray; 2.70 A; A=2-142.
PDB; 2HHB; X-ray; 1.74 A; A/C=2-142.
PDB; 2HHD; X-ray; 2.20 A; A/C=2-142.
PDB; 2HHE; X-ray; 2.20 A; A/C=2-142.
PDB; 2M6Z; NMR; -; A/C=2-142.
PDB; 2W6V; X-ray; 1.80 A; A/C=2-142.
PDB; 2W72; X-ray; 1.07 A; A=2-142, C=3-142.
PDB; 2YRS; X-ray; 2.30 A; A/C/I/M=2-142.
PDB; 3B75; X-ray; 2.30 A; A/C/E/G/S=2-142.
PDB; 3D17; X-ray; 2.80 A; A/C=2-142.
PDB; 3D7O; X-ray; 1.80 A; A=2-142.
PDB; 3DUT; X-ray; 1.55 A; A/C=2-142.
PDB; 3HHB; X-ray; 1.74 A; A/C=2-142.
PDB; 3HXN; X-ray; 2.00 A; A/C=2-142.
PDB; 3IA3; X-ray; 3.20 A; B/D=1-142.
PDB; 3IC0; X-ray; 1.80 A; A/C=2-142.
PDB; 3IC2; X-ray; 2.40 A; A/C=2-142.
PDB; 3KMF; Neutron; 2.00 A; A/E=2-142.
PDB; 3NL7; X-ray; 1.80 A; A=2-142.
PDB; 3NMM; X-ray; 1.60 A; A/C=2-142.
PDB; 3ODQ; X-ray; 3.10 A; A/C=2-142.
PDB; 3ONZ; X-ray; 2.09 A; A=2-142.
PDB; 3OO4; X-ray; 1.90 A; A=2-142.
PDB; 3OO5; X-ray; 2.10 A; A=2-142.
PDB; 3OVU; X-ray; 2.83 A; C=2-142.
PDB; 3P5Q; X-ray; 2.00 A; A=2-142.
PDB; 3QJB; X-ray; 1.80 A; A=2-142.
PDB; 3QJC; X-ray; 2.00 A; A=2-142.
PDB; 3QJD; X-ray; 1.56 A; A/C=2-142.
PDB; 3QJE; X-ray; 1.80 A; A/C=2-142.
PDB; 3R5I; X-ray; 2.20 A; A/C=2-142.
PDB; 3S48; X-ray; 3.05 A; C/D=2-142.
PDB; 3S65; X-ray; 1.80 A; A/C=2-142.
PDB; 3S66; X-ray; 1.40 A; A=2-142.
PDB; 3SZK; X-ray; 3.01 A; A/D=2-142.
PDB; 3WCP; X-ray; 1.94 A; A/C=2-142.
PDB; 3WHM; X-ray; 1.85 A; A/E=2-142.
PDB; 4FC3; X-ray; 2.26 A; A=2-142.
PDB; 4HHB; X-ray; 1.74 A; A/C=2-142.
PDB; 4IJ2; X-ray; 4.24 A; A/C=2-142.
PDB; 4L7Y; X-ray; 1.80 A; A/C=2-142.
PDB; 4M4A; X-ray; 2.05 A; A=2-142.
PDB; 4M4B; X-ray; 2.00 A; A=2-142.
PDB; 4MQC; X-ray; 2.20 A; A=2-142.
PDB; 4MQG; X-ray; 1.68 A; A=2-142.
PDB; 4MQH; X-ray; 2.50 A; A=2-140.
PDB; 4MQI; X-ray; 1.92 A; A=2-141.
PDB; 4MQJ; X-ray; 1.80 A; A/C/E/G=2-142.
PDB; 4MQK; X-ray; 2.24 A; A/C/E/G=2-142.
PDB; 4N7N; X-ray; 2.75 A; A/C/E/G/I/K=2-142.
PDB; 4N7O; X-ray; 2.50 A; A/C/E/G/I/K=2-142.
PDB; 4N7P; X-ray; 2.81 A; A/C/E/G/I/K=2-142.
PDB; 4N8T; X-ray; 1.90 A; A=2-142.
PDB; 4NI0; X-ray; 2.15 A; A=2-142.
PDB; 4NI1; X-ray; 1.90 A; A=2-142.
PDB; 4ROL; X-ray; 1.70 A; A/C=2-142.
PDB; 4ROM; X-ray; 1.90 A; A/C=2-142.
PDB; 4WJG; X-ray; 3.10 A; A/F/K/P/U/Z=2-142.
PDB; 4X0L; X-ray; 2.05 A; A=2-142.
PDB; 4XS0; X-ray; 2.55 A; A=2-142.
PDB; 5E29; X-ray; 1.85 A; A/C=2-142.
PDB; 5E6E; X-ray; 1.76 A; A=2-142.
PDB; 5E83; X-ray; 1.80 A; A/C=2-142.
PDB; 5EE4; X-ray; 2.30 A; C/E=2-142.
PDB; 5HU6; X-ray; 2.90 A; A=2-142.
PDB; 5HY8; X-ray; 2.30 A; A/C/E/G/S=2-142.
PDB; 5JDO; X-ray; 3.20 A; C=2-142, E=2-141.
PDB; 5KDQ; X-ray; 2.15 A; A/C=3-142.
PDB; 5ME2; EM; 3.20 A; A/C=2-141.
PDB; 5NI1; EM; 3.20 A; A/C=2-142.
PDB; 5SW7; X-ray; 1.85 A; A=2-142.
PDB; 5U3I; X-ray; 1.95 A; A/C=2-142.
PDB; 5UCU; X-ray; 1.80 A; A=2-142.
PDB; 5UFJ; X-ray; 2.05 A; A/C=2-142.
PDB; 5URC; X-ray; 1.85 A; A/C=2-142.
PDB; 6HBW; X-ray; 2.00 A; A/C=2-142.
PDBsum; 1A00; -.
PDBsum; 1A01; -.
PDBsum; 1A0U; -.
PDBsum; 1A0Z; -.
PDBsum; 1A3N; -.
PDBsum; 1A3O; -.
PDBsum; 1A9W; -.
PDBsum; 1ABW; -.
PDBsum; 1ABY; -.
PDBsum; 1AJ9; -.
PDBsum; 1B86; -.
PDBsum; 1BAB; -.
PDBsum; 1BBB; -.
PDBsum; 1BIJ; -.
PDBsum; 1BUW; -.
PDBsum; 1BZ0; -.
PDBsum; 1BZ1; -.
PDBsum; 1BZZ; -.
PDBsum; 1C7B; -.
PDBsum; 1C7C; -.
PDBsum; 1C7D; -.
PDBsum; 1CLS; -.
PDBsum; 1CMY; -.
PDBsum; 1COH; -.
PDBsum; 1DKE; -.
PDBsum; 1DXT; -.
PDBsum; 1DXU; -.
PDBsum; 1DXV; -.
PDBsum; 1FDH; -.
PDBsum; 1FN3; -.
PDBsum; 1G9V; -.
PDBsum; 1GBU; -.
PDBsum; 1GBV; -.
PDBsum; 1GLI; -.
PDBsum; 1GZX; -.
PDBsum; 1HAB; -.
PDBsum; 1HAC; -.
PDBsum; 1HBA; -.
PDBsum; 1HBB; -.
PDBsum; 1HBS; -.
PDBsum; 1HCO; -.
PDBsum; 1HDB; -.
PDBsum; 1HGA; -.
PDBsum; 1HGB; -.
PDBsum; 1HGC; -.
PDBsum; 1HHO; -.
PDBsum; 1IRD; -.
PDBsum; 1J3Y; -.
PDBsum; 1J3Z; -.
PDBsum; 1J40; -.
PDBsum; 1J41; -.
PDBsum; 1J7S; -.
PDBsum; 1J7W; -.
PDBsum; 1J7Y; -.
PDBsum; 1JY7; -.
PDBsum; 1K0Y; -.
PDBsum; 1K1K; -.
PDBsum; 1KD2; -.
PDBsum; 1LFL; -.
PDBsum; 1LFQ; -.
PDBsum; 1LFT; -.
PDBsum; 1LFV; -.
PDBsum; 1LFY; -.
PDBsum; 1LFZ; -.
PDBsum; 1LJW; -.
PDBsum; 1M9P; -.
PDBsum; 1MKO; -.
PDBsum; 1NEJ; -.
PDBsum; 1NIH; -.
PDBsum; 1NQP; -.
PDBsum; 1O1I; -.
PDBsum; 1O1J; -.
PDBsum; 1O1K; -.
PDBsum; 1O1L; -.
PDBsum; 1O1M; -.
PDBsum; 1O1N; -.
PDBsum; 1O1O; -.
PDBsum; 1O1P; -.
PDBsum; 1QI8; -.
PDBsum; 1QSH; -.
PDBsum; 1QSI; -.
PDBsum; 1QXD; -.
PDBsum; 1QXE; -.
PDBsum; 1R1X; -.
PDBsum; 1R1Y; -.
PDBsum; 1RPS; -.
PDBsum; 1RQ3; -.
PDBsum; 1RQ4; -.
PDBsum; 1RQA; -.
PDBsum; 1RVW; -.
PDBsum; 1SDK; -.
PDBsum; 1SDL; -.
PDBsum; 1SHR; -.
PDBsum; 1SI4; -.
PDBsum; 1THB; -.
PDBsum; 1UIW; -.
PDBsum; 1VWT; -.
PDBsum; 1XXT; -.
PDBsum; 1XY0; -.
PDBsum; 1XYE; -.
PDBsum; 1XZ2; -.
PDBsum; 1XZ4; -.
PDBsum; 1XZ5; -.
PDBsum; 1XZ7; -.
PDBsum; 1XZU; -.
PDBsum; 1XZV; -.
PDBsum; 1Y01; -.
PDBsum; 1Y09; -.
PDBsum; 1Y0A; -.
PDBsum; 1Y0C; -.
PDBsum; 1Y0D; -.
PDBsum; 1Y0T; -.
PDBsum; 1Y0W; -.
PDBsum; 1Y22; -.
PDBsum; 1Y2Z; -.
PDBsum; 1Y31; -.
PDBsum; 1Y35; -.
PDBsum; 1Y45; -.
PDBsum; 1Y46; -.
PDBsum; 1Y4B; -.
PDBsum; 1Y4F; -.
PDBsum; 1Y4G; -.
PDBsum; 1Y4P; -.
PDBsum; 1Y4Q; -.
PDBsum; 1Y4R; -.
PDBsum; 1Y4V; -.
PDBsum; 1Y5F; -.
PDBsum; 1Y5J; -.
PDBsum; 1Y5K; -.
PDBsum; 1Y7C; -.
PDBsum; 1Y7D; -.
PDBsum; 1Y7G; -.
PDBsum; 1Y7Z; -.
PDBsum; 1Y83; -.
PDBsum; 1Y85; -.
PDBsum; 1Y8W; -.
PDBsum; 1YDZ; -.
PDBsum; 1YE0; -.
PDBsum; 1YE1; -.
PDBsum; 1YE2; -.
PDBsum; 1YEN; -.
PDBsum; 1YEO; -.
PDBsum; 1YEQ; -.
PDBsum; 1YEU; -.
PDBsum; 1YEV; -.
PDBsum; 1YFF; -.
PDBsum; 1YG5; -.
PDBsum; 1YGD; -.
PDBsum; 1YGF; -.
PDBsum; 1YH9; -.
PDBsum; 1YHE; -.
PDBsum; 1YHR; -.
PDBsum; 1YIE; -.
PDBsum; 1YIH; -.
PDBsum; 1YVQ; -.
PDBsum; 1YVT; -.
PDBsum; 1YZI; -.
PDBsum; 1Z8U; -.
PDBsum; 2D5Z; -.
PDBsum; 2D60; -.
PDBsum; 2DN1; -.
PDBsum; 2DN2; -.
PDBsum; 2DN3; -.
PDBsum; 2DXM; -.
PDBsum; 2H35; -.
PDBsum; 2HBC; -.
PDBsum; 2HBD; -.
PDBsum; 2HBE; -.
PDBsum; 2HBF; -.
PDBsum; 2HBS; -.
PDBsum; 2HCO; -.
PDBsum; 2HHB; -.
PDBsum; 2HHD; -.
PDBsum; 2HHE; -.
PDBsum; 2M6Z; -.
PDBsum; 2W6V; -.
PDBsum; 2W72; -.
PDBsum; 2YRS; -.
PDBsum; 3B75; -.
PDBsum; 3D17; -.
PDBsum; 3D7O; -.
PDBsum; 3DUT; -.
PDBsum; 3HHB; -.
PDBsum; 3HXN; -.
PDBsum; 3IA3; -.
PDBsum; 3IC0; -.
PDBsum; 3IC2; -.
PDBsum; 3KMF; -.
PDBsum; 3NL7; -.
PDBsum; 3NMM; -.
PDBsum; 3ODQ; -.
PDBsum; 3ONZ; -.
PDBsum; 3OO4; -.
PDBsum; 3OO5; -.
PDBsum; 3OVU; -.
PDBsum; 3P5Q; -.
PDBsum; 3QJB; -.
PDBsum; 3QJC; -.
PDBsum; 3QJD; -.
PDBsum; 3QJE; -.
PDBsum; 3R5I; -.
PDBsum; 3S48; -.
PDBsum; 3S65; -.
PDBsum; 3S66; -.
PDBsum; 3SZK; -.
PDBsum; 3WCP; -.
PDBsum; 3WHM; -.
PDBsum; 4FC3; -.
PDBsum; 4HHB; -.
PDBsum; 4IJ2; -.
PDBsum; 4L7Y; -.
PDBsum; 4M4A; -.
PDBsum; 4M4B; -.
PDBsum; 4MQC; -.
PDBsum; 4MQG; -.
PDBsum; 4MQH; -.
PDBsum; 4MQI; -.
PDBsum; 4MQJ; -.
PDBsum; 4MQK; -.
PDBsum; 4N7N; -.
PDBsum; 4N7O; -.
PDBsum; 4N7P; -.
PDBsum; 4N8T; -.
PDBsum; 4NI0; -.
PDBsum; 4NI1; -.
PDBsum; 4ROL; -.
PDBsum; 4ROM; -.
PDBsum; 4WJG; -.
PDBsum; 4X0L; -.
PDBsum; 4XS0; -.
PDBsum; 5E29; -.
PDBsum; 5E6E; -.
PDBsum; 5E83; -.
PDBsum; 5EE4; -.
PDBsum; 5HU6; -.
PDBsum; 5HY8; -.
PDBsum; 5JDO; -.
PDBsum; 5KDQ; -.
PDBsum; 5ME2; -.
PDBsum; 5NI1; -.
PDBsum; 5SW7; -.
PDBsum; 5U3I; -.
PDBsum; 5UCU; -.
PDBsum; 5UFJ; -.
PDBsum; 5URC; -.
PDBsum; 6HBW; -.
ProteinModelPortal; P69905; -.
SMR; P69905; -.
BioGrid; 109289; 22.
BioGrid; 109290; 45.
DIP; DIP-35199N; -.
IntAct; P69905; 31.
MINT; MINT-1519936; -.
STRING; 9606.ENSP00000322421; -.
ChEMBL; CHEMBL2887; -.
DrugBank; DB07427; 2-[(2-methoxy-5-methylphenoxy)methyl]pyridine.
DrugBank; DB07428; 4-[(5-methoxy-2-methylphenoxy)methyl]pyridine.
DrugBank; DB02126; 4-Carboxycinnamic Acid.
DrugBank; DB00893; Iron Dextran.
DrugBank; DB09146; Iron saccharate.
DrugBank; DB00358; Mefloquine.
DrugBank; DB07645; SEBACIC ACID.
TCDB; 1.A.107.1.1; the pore-forming globin (globin) family.
iPTMnet; P69905; -.
PhosphoSitePlus; P69905; -.
BioMuta; HBA1; -.
DMDM; 57013850; -.
DOSAC-COBS-2DPAGE; P69905; -.
REPRODUCTION-2DPAGE; IPI00410714; -.
SWISS-2DPAGE; P69905; -.
UCD-2DPAGE; P69905; -.
EPD; P69905; -.
MaxQB; P69905; -.
PaxDb; P69905; -.
PeptideAtlas; P69905; -.
PRIDE; P69905; -.
TopDownProteomics; P69905; -.
DNASU; 3039; -.
Ensembl; ENST00000251595; ENSP00000251595; ENSG00000188536.
Ensembl; ENST00000320868; ENSP00000322421; ENSG00000206172.
GeneID; 3039; -.
GeneID; 3040; -.
KEGG; hsa:3039; -.
KEGG; hsa:3040; -.
UCSC; uc002cfv.4; human.
CTD; 3039; -.
CTD; 3040; -.
DisGeNET; 3039; -.
DisGeNET; 3040; -.
EuPathDB; HostDB:ENSG00000188536.12; -.
EuPathDB; HostDB:ENSG00000206172.8; -.
GeneCards; HBA1; -.
GeneCards; HBA2; -.
GeneReviews; HBA1; -.
GeneReviews; HBA2; -.
HGNC; HGNC:4823; HBA1.
HGNC; HGNC:4824; HBA2.
HPA; CAB032534; -.
HPA; CAB038417; -.
HPA; HPA043780; -.
MalaCards; HBA1; -.
MalaCards; HBA2; -.
MIM; 140700; phenotype.
MIM; 141800; gene+phenotype.
MIM; 141850; gene.
MIM; 141860; gene.
MIM; 604131; phenotype.
MIM; 613978; phenotype.
neXtProt; NX_P69905; -.
OpenTargets; ENSG00000188536; -.
OpenTargets; ENSG00000206172; -.
Orphanet; 98791; Alpha-thalassemia - intellectual disability syndrome linked to chromosome 16.
Orphanet; 330041; Autosomal dominant methemoglobinemia.
Orphanet; 163596; Hb Bart's hydrops fetalis.
Orphanet; 93616; Hemoglobin H disease.
PharmGKB; PA29199; -.
eggNOG; KOG3378; Eukaryota.
eggNOG; COG1018; LUCA.
GeneTree; ENSGT00760000119197; -.
HOVERGEN; HBG009709; -.
InParanoid; P69905; -.
KO; K13822; -.
OMA; DKFLCAV; -.
OrthoDB; EOG091G0S0X; -.
PhylomeDB; P69905; -.
TreeFam; TF332328; -.
Reactome; R-HSA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
Reactome; R-HSA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
Reactome; R-HSA-2168880; Scavenging of heme from plasma.
SIGNOR; P69905; -.
ChiTaRS; HBA1; human.
ChiTaRS; HBA2; human.
EvolutionaryTrace; P69905; -.
GeneWiki; HBA2; -.
GeneWiki; Hemoglobin,_alpha_1; -.
GeneWiki; Hemoglobin,_alpha_2; -.
PMAP-CutDB; P69905; -.
PRO; PR:P69905; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000188536; -.
CleanEx; HS_HBA1; -.
CleanEx; HS_HBA2; -.
ExpressionAtlas; P69905; baseline and differential.
Genevisible; P69905; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0031838; C:haptoglobin-hemoglobin complex; IDA:BHF-UCL.
GO; GO:0005833; C:hemoglobin complex; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0019825; F:oxygen binding; IEA:InterPro.
GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW.
GO; GO:0015701; P:bicarbonate transport; TAS:Reactome.
GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:BHF-UCL.
GO; GO:0015671; P:oxygen transport; TAS:UniProtKB.
GO; GO:0010942; P:positive regulation of cell death; IDA:BHF-UCL.
GO; GO:0051291; P:protein heterooligomerization; IDA:BHF-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0042542; P:response to hydrogen peroxide; IDA:BHF-UCL.
CDD; cd08927; Hb-alpha_like; 1.
InterPro; IPR000971; Globin.
InterPro; IPR009050; Globin-like.
InterPro; IPR002338; Haemoglobin_a-typ.
InterPro; IPR002339; Haemoglobin_pi.
Pfam; PF00042; Globin; 1.
PRINTS; PR00612; ALPHAHAEM.
PRINTS; PR00815; PIHAEM.
SUPFAM; SSF46458; SSF46458; 1.
PROSITE; PS01033; GLOBIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Disease mutation; Glycation; Glycoprotein;
Heme; Hereditary hemolytic anemia; Iron; Metal-binding;
Oxygen transport; Phosphoprotein; Polymorphism; Reference proteome;
Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:13872627,
ECO:0000269|PubMed:13954546,
ECO:0000269|PubMed:14093912}.
CHAIN 2 142 Hemoglobin subunit alpha.
/FTId=PRO_0000052653.
METAL 59 59 Iron (heme distal ligand).
METAL 88 88 Iron (heme proximal ligand).
SITE 12 12 Not glycated.
{ECO:0000269|PubMed:7358733}.
SITE 57 57 Not glycated.
{ECO:0000269|PubMed:7358733}.
SITE 61 61 Not glycated.
{ECO:0000269|PubMed:7358733}.
SITE 91 91 Not glycated.
{ECO:0000269|PubMed:7358733}.
SITE 100 100 Not glycated.
{ECO:0000269|PubMed:7358733}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 8 8 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 9 9 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 12 12 N6-succinyllysine.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 17 17 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 17 17 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 25 25 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 36 36 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 41 41 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 109 109 Phosphothreonine.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 132 132 Phosphoserine.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 135 135 Phosphothreonine.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 138 138 Phosphothreonine.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000250|UniProtKB:P01942}.
CARBOHYD 8 8 N-linked (Glc) (glycation) lysine;
alternate.
CARBOHYD 17 17 N-linked (Glc) (glycation) lysine;
alternate.
CARBOHYD 41 41 N-linked (Glc) (glycation) lysine;
alternate.
CARBOHYD 62 62 N-linked (Glc) (glycation) lysine.
VARIANT 2 2 V -> E (in Thionville; O(2) affinity
down; dbSNP:rs33981821).
{ECO:0000269|PubMed:1618774}.
/FTId=VAR_002719.
VARIANT 3 3 L -> R (in ChongQing; O(2) affinity up;
dbSNP:rs36030576).
{ECO:0000269|PubMed:6526652}.
/FTId=VAR_002720.
VARIANT 6 6 A -> D (in J-Toronto; dbSNP:rs34090856).
/FTId=VAR_002721.
VARIANT 6 6 A -> P (in Karachi; dbSNP:rs34751764).
/FTId=VAR_002722.
VARIANT 7 7 D -> A (in Sawara; O(2) affinity up;
dbSNP:rs33986902).
{ECO:0000269|PubMed:20980,
ECO:0000269|PubMed:4744335}.
/FTId=VAR_002723.
VARIANT 7 7 D -> G (in Swan River;
dbSNP:rs281864805).
{ECO:0000269|PubMed:8745434}.
/FTId=VAR_002724.
VARIANT 7 7 D -> N (in Dunn; O(2) affinity up;
dbSNP:rs33961916).
{ECO:0000269|PubMed:478975,
ECO:0000269|PubMed:7435503}.
/FTId=VAR_002725.
VARIANT 7 7 D -> V (in Ferndown; O(2) affinity up;
dbSNP:rs281864805).
{ECO:0000269|PubMed:7238857}.
/FTId=VAR_002726.
VARIANT 7 7 D -> Y (in Woodville; O(2) affinity up;
dbSNP:rs281864806).
{ECO:0000269|PubMed:3754246}.
/FTId=VAR_002727.
VARIANT 8 8 K -> E (in Kurosaki; dbSNP:rs34817956).
{ECO:0000269|PubMed:7558876}.
/FTId=VAR_002728.
VARIANT 10 10 N -> T (in Broomfield;
dbSNP:rs281860608).
/FTId=VAR_038149.
VARIANT 12 12 K -> E (in Anantharaj; dbSNP:rs33938574).
/FTId=VAR_002729.
VARIANT 13 13 A -> D (in J-Paris 1/J-Aljezur;
dbSNP:rs35615982).
/FTId=VAR_002730.
VARIANT 14 14 A -> P (in Ravenscourt Park; causes
alpha-thalassemia; dbSNP:rs35331909).
/FTId=VAR_038150.
VARIANT 15 15 W -> R (in Evanston; O(2) affinity up;
dbSNP:rs33964317).
{ECO:0000269|PubMed:6725558,
ECO:0000269|PubMed:6882779}.
/FTId=VAR_002731.
VARIANT 16 16 G -> R (in Ottawa/Siam;
dbSNP:rs35816645).
/FTId=VAR_002732.
VARIANT 17 17 K -> M (in Harbin; slightly unstable;
dbSNP:rs35210126).
{ECO:0000269|PubMed:6526652}.
/FTId=VAR_002733.
VARIANT 17 17 K -> N (in Beijing; dbSNP:rs281860648 and
dbSNP:rs281860619).
/FTId=VAR_002734.
VARIANT 19 19 G -> D (in Al-Ain Abu Dhabi;
dbSNP:rs35993097).
{ECO:0000269|PubMed:1428941}.
/FTId=VAR_002735.
VARIANT 19 19 G -> R (in Handsworth; dbSNP:rs34504387).
/FTId=VAR_002736.
VARIANT 20 20 A -> D (in J-Kurosh).
/FTId=VAR_002737.
VARIANT 20 20 A -> E (in J-Tashikuergan;
dbSNP:rs35628685).
/FTId=VAR_002738.
VARIANT 21 21 H -> Q (in Le Lamentin;
dbSNP:rs41525149).
/FTId=VAR_002739.
VARIANT 21 21 H -> R (in Hobart; dbSNP:rs33943087).
{ECO:0000269|PubMed:3654264}.
/FTId=VAR_002740.
VARIANT 22 22 A -> D (in J-Nyanza; dbSNP:rs11548605).
/FTId=VAR_002741.
VARIANT 22 22 A -> P (in Fontainebleau;
dbSNP:rs34324664).
/FTId=VAR_002742.
VARIANT 23 23 G -> D (in J-Medellin; dbSNP:rs34608326).
/FTId=VAR_002743.
VARIANT 24 24 E -> G (in Reims; slightly unstable;
dbSNP:rs33939421).
{ECO:0000269|PubMed:2634669}.
/FTId=VAR_002744.
VARIANT 24 24 E -> K (in Chad; dbSNP:rs281864819).
/FTId=VAR_002745.
VARIANT 25 25 Y -> H (in Luxembourg; unstable;
dbSNP:rs281864821).
{ECO:0000269|PubMed:2599879}.
/FTId=VAR_002746.
VARIANT 27 27 A -> E (in Shenyang; unstable;
dbSNP:rs281864822).
{ECO:0000269|PubMed:7161109}.
/FTId=VAR_002747.
VARIANT 27 27 A -> V (in Campinas; dbSNP:rs281864822).
{ECO:0000269|PubMed:14576901}.
/FTId=VAR_025387.
VARIANT 28 28 E -> D (in Hekinan; dbSNP:rs281865556).
/FTId=VAR_002748.
VARIANT 28 28 E -> G (in Fort Worth;
dbSNP:rs281864823).
/FTId=VAR_002749.
VARIANT 28 28 E -> V (in Spanish town;
dbSNP:rs281864823).
{ECO:0000269|PubMed:2752146}.
/FTId=VAR_002750.
VARIANT 31 31 E -> K (in O-Padova; dbSNP:rs111033605).
/FTId=VAR_002751.
VARIANT 32 32 R -> K (causes alpha-thalassemia;
dbSNP:rs281864543).
{ECO:0000269|PubMed:11410421}.
/FTId=VAR_025002.
VARIANT 32 32 R -> S (in Prato; unstable;
dbSNP:rs111033606).
{ECO:0000269|PubMed:486536}.
/FTId=VAR_002752.
VARIANT 35 35 L -> R (in Queens/Ogi;
dbSNP:rs281864825).
/FTId=VAR_002753.
VARIANT 38 38 P -> PE (in Catonsville).
{ECO:0000269|PubMed:8448109}.
/FTId=VAR_002755.
VARIANT 38 38 P -> R (in Bourmedes; dbSNP:rs281864826).
/FTId=VAR_002754.
VARIANT 41 41 K -> M (in Kanagawa; O(2) affinity up;
dbSNP:rs281864828).
{ECO:0000269|PubMed:1634355}.
/FTId=VAR_002756.
VARIANT 42 42 T -> S (in Miyano; O(2) affinity up;
dbSNP:rs281860623).
{ECO:0000269|PubMed:2634665}.
/FTId=VAR_002757.
VARIANT 44 44 F -> L (in Hirosaki; unstable;
dbSNP:rs41491146).
{ECO:0000269|PubMed:1182166}.
/FTId=VAR_002758.
VARIANT 45 45 P -> L (in Milledgeville; O(2) affinity
up; dbSNP:rs41514946).
{ECO:0000269|PubMed:7213661}.
/FTId=VAR_002759.
VARIANT 45 45 P -> R (in Kawachi; O(2) affinity up;
dbSNP:rs281864830).
{ECO:0000269|PubMed:7068434}.
/FTId=VAR_002760.
VARIANT 46 46 H -> Q (in Bari; dbSNP:rs281860624).
/FTId=VAR_002761.
VARIANT 46 46 H -> R (in Fort de France; O(2) affinity
up; dbSNP:rs281864831).
{ECO:0000269|PubMed:2752146}.
/FTId=VAR_002762.
VARIANT 48 48 D -> A (in Cordele; unstable;
dbSNP:rs281864833).
{ECO:0000269|PubMed:6547117}.
/FTId=VAR_002763.
VARIANT 48 48 D -> G (in Kokura; also in Umi/Michigan;
unstable; dbSNP:rs281864833).
{ECO:0000269|PubMed:7068437}.
/FTId=VAR_002764.
VARIANT 48 48 D -> H (in Hasharon/Sinai; unstable;
dbSNP:rs281864834).
{ECO:0000269|PubMed:5780195}.
/FTId=VAR_002765.
VARIANT 48 48 D -> Y (in Kurdistan; dbSNP:rs281864834).
{ECO:0000269|PubMed:8195005}.
/FTId=VAR_002766.
VARIANT 49 49 L -> R (in Montgomery; dbSNP:rs41392146).
{ECO:0000269|PubMed:1115799}.
/FTId=VAR_002767.
VARIANT 50 50 S -> R (in Savaria; dbSNP:rs41518249).
/FTId=VAR_002768.
VARIANT 51 51 H -> R (in Aichi; slightly unstable;
dbSNP:rs281864835).
{ECO:0000269|PubMed:6714429}.
/FTId=VAR_002769.
VARIANT 52 52 G -> D (in J-Abidjan; dbSNP:rs281864836).
/FTId=VAR_002770.
VARIANT 52 52 G -> R (in Russ; dbSNP:rs281864837).
/FTId=VAR_002771.
VARIANT 54 54 A -> D (in J-Rovigo; unstable;
dbSNP:rs281864838).
{ECO:0000269|PubMed:4824923}.
/FTId=VAR_002772.
VARIANT 55 55 Q -> R (in Hikoshima/Shimonoseki;
dbSNP:rs281864839).
/FTId=VAR_002773.
VARIANT 57 57 K -> R (in Port Huron;
dbSNP:rs281864841).
{ECO:0000269|PubMed:1802882}.
/FTId=VAR_002774.
VARIANT 57 57 K -> T (in Thailand; dbSNP:rs281864841).
/FTId=VAR_002775.
VARIANT 58 58 G -> R (in L-Persian Gulf;
dbSNP:rs281864843).
/FTId=VAR_002776.
VARIANT 59 59 H -> Q (in Boghe; dbSNP:rs41378349).
{ECO:0000269|PubMed:10569723}.
/FTId=VAR_025388.
VARIANT 59 59 H -> Y (in M-Boston/M-Osaka; O(2)
affinity down; dbSNP:rs281864845).
{ECO:0000269|PubMed:4521212}.
/FTId=VAR_002777.
VARIANT 60 60 G -> D (in Adana; unstable; causes alpha-
thalassemia; dbSNP:rs28928878).
{ECO:0000269|PubMed:8237999}.
/FTId=VAR_002778.
VARIANT 60 60 G -> V (in Tottori; unstable;
dbSNP:rs281864846).
{ECO:0000269|PubMed:7275660}.
/FTId=VAR_002779.
VARIANT 61 61 K -> N (in Zambia; dbSNP:rs281860659 and
dbSNP:rs111033598).
/FTId=VAR_002780.
VARIANT 61 61 Missing (in Clinic; unstable; causes
alpha-thalassemia).
{ECO:0000269|PubMed:10206681}.
/FTId=VAR_002781.
VARIANT 62 62 K -> N (in J-Buda; dbSNP:rs33985574).
{ECO:0000269|Ref.80}.
/FTId=VAR_002782.
VARIANT 62 62 K -> T (in J-Anatolia;
dbSNP:rs281865558).
/FTId=VAR_002783.
VARIANT 63 63 V -> M (in Evans; unstable;
dbSNP:rs41515649).
{ECO:0000269|PubMed:2606724,
ECO:0000269|Ref.11}.
/FTId=VAR_002784.
VARIANT 63 63 Missing (in HBH; hemoglobin Aghia
Sophia). {ECO:0000269|PubMed:10569720}.
/FTId=VAR_066401.
VARIANT 64 64 A -> D (in Pontoise; unstable;
dbSNP:rs281864848).
{ECO:0000269|PubMed:849454}.
/FTId=VAR_002785.
VARIANT 65 65 D -> Y (in Persepolis;
dbSNP:rs281864849).
/FTId=VAR_002786.
VARIANT 69 69 N -> K (in G-Philadelphia;
dbSNP:rs1060339). {ECO:0000269|Ref.12}.
/FTId=VAR_002787.
VARIANT 72 72 A -> E (in J-Habana; dbSNP:rs281864853).
/FTId=VAR_002788.
VARIANT 72 72 A -> V (in Ozieri; dbSNP:rs281864853).
/FTId=VAR_002789.
VARIANT 73 73 H -> R (in Daneskgah-Teheran;
dbSNP:rs281864854).
/FTId=VAR_002790.
VARIANT 75 75 D -> A (in Lille; dbSNP:rs281864856).
/FTId=VAR_002791.
VARIANT 75 75 D -> G (in Chapel Hill;
dbSNP:rs33921047).
/FTId=VAR_002792.
VARIANT 75 75 D -> N (in G-Pest; dbSNP:rs281864857).
{ECO:0000269|Ref.80}.
/FTId=VAR_002793.
VARIANT 76 76 D -> A (in Duan; dbSNP:rs33991223).
/FTId=VAR_002794.
VARIANT 76 76 D -> H (in Q-Iran; dbSNP:rs281864858).
/FTId=VAR_002795.
VARIANT 77 77 M -> K (in Noko; dbSNP:rs281864860).
/FTId=VAR_002796.
VARIANT 77 77 M -> T (in Aztec; dbSNP:rs281864860).
/FTId=VAR_002797.
VARIANT 78 78 P -> R (in Guizhou; dbSNP:rs281864861).
/FTId=VAR_002798.
VARIANT 79 79 N -> H (in Davenport; dbSNP:rs111033602).
{ECO:0000269|PubMed:2101836}.
/FTId=VAR_002799.
VARIANT 79 79 N -> K (in Stanleyville-2;
dbSNP:rs281860607).
/FTId=VAR_002800.
VARIANT 80 80 A -> G (in Singapore; dbSNP:rs281860603).
/FTId=VAR_012662.
VARIANT 81 81 L -> R (in Ann Arbor; unstable;
dbSNP:rs281864863).
{ECO:0000269|PubMed:5033650}.
/FTId=VAR_002801.
VARIANT 82 82 S -> C (in Nigeria; dbSNP:rs281864864).
/FTId=VAR_002802.
VARIANT 83 83 A -> D (in Garden State;
dbSNP:rs281864865).
/FTId=VAR_002803.
VARIANT 85 85 S -> R (in Etobicoke; O(2) affinity up;
dbSNP:rs281860612).
{ECO:0000269|PubMed:6874377}.
/FTId=VAR_002804.
VARIANT 86 86 D -> V (in Inkster; O(2) affinity up;
dbSNP:rs41331747).
{ECO:0000269|PubMed:4212045}.
/FTId=VAR_002805.
VARIANT 86 86 D -> Y (in Atago; O(2) affinity up;
dbSNP:rs281864777).
{ECO:0000269|PubMed:5115619}.
/FTId=VAR_002806.
VARIANT 87 87 L -> R (in Moabit; unstable;
dbSNP:rs281864866).
{ECO:0000269|PubMed:108887}.
/FTId=VAR_002807.
VARIANT 88 88 H -> N (in Auckland; unstable;
dbSNP:rs281864868).
{ECO:0000269|PubMed:9322075}.
/FTId=VAR_002808.
VARIANT 88 88 H -> R (in Iwata; unstable;
dbSNP:rs281864867).
/FTId=VAR_002809.
VARIANT 89 89 A -> S (in Loire; O(2) affinity up;
dbSNP:rs281864869).
{ECO:0000269|PubMed:3142772}.
/FTId=VAR_002810.
VARIANT 91 91 K -> M (in Handa; O(2) affinity up;
dbSNP:rs281864873).
{ECO:0000269|PubMed:6815131}.
/FTId=VAR_002811.
VARIANT 92 92 L -> F (in dbSNP:rs17407508).
/FTId=VAR_049272.
VARIANT 92 92 L -> P (in Port Phillip; unstable;
dbSNP:rs17407508).
{ECO:0000269|PubMed:902765}.
/FTId=VAR_002812.
VARIANT 93 93 R -> Q (in J-Cape Town; O(2) affinity up;
dbSNP:rs281864875).
{ECO:0000269|PubMed:5091982,
ECO:0000269|PubMed:5988206}.
/FTId=VAR_002813.
VARIANT 93 93 R -> W (in Cemenelum; O(2) affinity up;
dbSNP:rs281864876).
{ECO:0000269|PubMed:8148419}.
/FTId=VAR_020775.
VARIANT 95 95 D -> A (in Bassett; markedly reduced
oxygen affinity; dbSNP:rs281864879).
{ECO:0000269|PubMed:15495251}.
/FTId=VAR_025389.
VARIANT 95 95 D -> Y (in Setif; unstable;
dbSNP:rs281864878).
{ECO:0000269|PubMed:4667378}.
/FTId=VAR_002814.
VARIANT 96 96 P -> A (in Denmark Hill; O(2) affinity
up; dbSNP:rs281864881).
{ECO:0000269|PubMed:5085669}.
/FTId=VAR_002815.
VARIANT 96 96 P -> T (in Godavari; O(2) affinity up;
dbSNP:rs281864881).
{ECO:0000269|PubMed:9494044}.
/FTId=VAR_002816.
VARIANT 98 98 N -> K (in Dallas; O(2) affinity up;
dbSNP:rs41338947).
{ECO:0000269|PubMed:1390940}.
/FTId=VAR_002817.
VARIANT 100 100 K -> E (in Turriff; dbSNP:rs281864882).
{ECO:0000269|PubMed:1634357}.
/FTId=VAR_002818.
VARIANT 103 103 S -> R (in Manitoba; slightly unstable;
dbSNP:rs41344646).
{ECO:0000269|PubMed:6547932}.
/FTId=VAR_002819.
VARIANT 104 104 H -> R (in Contaldo; unstable;
dbSNP:rs63750752).
{ECO:0000269|PubMed:6547932}.
/FTId=VAR_002820.
VARIANT 104 104 H -> Y (in Charolles; dbSNP:rs63750073).
{ECO:0000269|PubMed:10569723}.
/FTId=VAR_025390.
VARIANT 110 110 L -> R (in Suan-Dok; unstable; causes
alpha-thalassemia; dbSNP:rs41479844).
{ECO:0000269|PubMed:478977}.
/FTId=VAR_002821.
VARIANT 111 111 A -> D (in Petah Tikva; unstable; causes
alpha-thalassemia; dbSNP:rs28928889).
{ECO:0000269|PubMed:7470621}.
/FTId=VAR_002822.
VARIANT 113 113 H -> D (in Hopkins-II; unstable;
dbSNP:rs281864885).
{ECO:0000269|PubMed:5288820}.
/FTId=VAR_002823.
VARIANT 114 114 L -> H (in Twin Peaks;
dbSNP:rs281860618).
/FTId=VAR_002824.
VARIANT 115 115 P -> L (in Nouakchott;
dbSNP:rs267607269).
/FTId=VAR_002825.
VARIANT 115 115 P -> R (in Chiapas; dbSNP:rs267607269).
/FTId=VAR_002826.
VARIANT 115 115 P -> S (in Melusine; dbSNP:rs281864887).
{ECO:0000269|PubMed:8294199}.
/FTId=VAR_002827.
VARIANT 116 116 A -> D (in J-Tongariki;
dbSNP:rs281864888).
/FTId=VAR_002828.
VARIANT 117 117 E -> A (in Ube-4; dbSNP:rs281864946).
/FTId=VAR_002829.
VARIANT 117 117 E -> EHLPAE (in Zaire).
{ECO:0000269|PubMed:1511986}.
/FTId=VAR_002830.
VARIANT 118 118 F -> FI (in Phnom Penh).
{ECO:0000269|PubMed:9452028}.
/FTId=VAR_002831.
VARIANT 119 119 T -> TEFT (in Grady).
{ECO:0000269|PubMed:4528583}.
/FTId=VAR_002832.
VARIANT 121 121 A -> E (in J-Meerut/J-Birmingham;
dbSNP:rs36075744).
{ECO:0000269|PubMed:7713747}.
/FTId=VAR_002833.
VARIANT 122 122 V -> M (in Owari; dbSNP:rs35187567).
/FTId=VAR_002834.
VARIANT 123 123 H -> Q (in Westmead; dbSNP:rs41479347).
{ECO:0000269|PubMed:1686260}.
/FTId=VAR_002835.
VARIANT 126 126 L -> P (in Quong Sze; causes alpha-
thalassemia; dbSNP:rs41397847).
/FTId=VAR_002836.
VARIANT 126 126 L -> R (in Plasencia; family with
moderate microcytosis and hypochromia;
dbSNP:rs41397847).
{ECO:0000269|PubMed:15921163}.
/FTId=VAR_025391.
VARIANT 127 127 D -> G (in West One; dbSNP:rs33957766).
{ECO:0000269|PubMed:14576901}.
/FTId=VAR_025392.
VARIANT 127 127 D -> V (in Fukutomi; O(2) affinity up;
dbSNP:rs33957766).
{ECO:0000269|PubMed:2079432}.
/FTId=VAR_002837.
VARIANT 127 127 D -> Y (in Montefiore; O(2) affinity up;
dbSNP:rs33933481).
{ECO:0000269|PubMed:8798486}.
/FTId=VAR_002838.
VARIANT 128 128 K -> N (in Jackson; dbSNP:rs33972894).
/FTId=VAR_002839.
VARIANT 130 130 L -> P (in Tunis-Bizerte; unstable;
causes alpha-thalassemia;
dbSNP:rs281864889).
{ECO:0000269|PubMed:7786798}.
/FTId=VAR_002840.
VARIANT 131 131 A -> D (in Yuda; O(2) affinity down;
dbSNP:rs41528545).
{ECO:0000269|PubMed:1428950}.
/FTId=VAR_002842.
VARIANT 131 131 A -> P (in Sun Prairie; unstable;
dbSNP:rs41529844).
{ECO:0000269|PubMed:2079430}.
/FTId=VAR_002841.
VARIANT 132 132 S -> P (in Questembert; highly unstable;
causes alpha-thalassemia;
dbSNP:rs63751417).
{ECO:0000269|PubMed:8493987}.
/FTId=VAR_002843.
VARIANT 134 134 S -> R (in Val de Marne; O(2) affinity
up; dbSNP:rs41514946).
{ECO:0000269|PubMed:8294200}.
/FTId=VAR_002844.
VARIANT 136 136 V -> E (in Pavie; dbSNP:rs63749809).
/FTId=VAR_002845.
VARIANT 137 137 L -> M (in Chicago; dbSNP:rs41364652).
/FTId=VAR_002846.
VARIANT 137 137 L -> P (in Bibba; unstable; causes alpha-
thalassemia; dbSNP:rs41469945).
{ECO:0000269|PubMed:5440849}.
/FTId=VAR_002847.
VARIANT 137 137 L -> R (in Toyama; dbSNP:rs41469945).
{ECO:0000269|PubMed:2833478}.
/FTId=VAR_035242.
VARIANT 139 139 S -> P (in Attleboro; O(2) affinity up;
dbSNP:rs63750801).
{ECO:0000269|PubMed:2108715}.
/FTId=VAR_002848.
VARIANT 140 140 K -> E (in Hanamaki; O(2) affinity up;
dbSNP:rs41361546).
{ECO:0000269|PubMed:1634363}.
/FTId=VAR_002849.
VARIANT 140 140 K -> T (in Tokoname; O(2) affinity up;
dbSNP:rs56348461).
{ECO:0000269|PubMed:6188720}.
/FTId=VAR_002850.
VARIANT 141 141 Y -> H (in Rouen/Ethiopia; O(2) affinity
up; dbSNP:rs55870409).
{ECO:0000269|PubMed:1390944,
ECO:0000269|PubMed:1428951}.
/FTId=VAR_002851.
VARIANT 142 142 R -> C (in Nunobiki; O(2) affinity up;
dbSNP:rs63750134).
{ECO:0000269|PubMed:3973024}.
/FTId=VAR_002852.
VARIANT 142 142 R -> H (in Suresnes; O(2) affinity up;
dbSNP:rs63751282).
{ECO:0000269|PubMed:7410435}.
/FTId=VAR_002854.
VARIANT 142 142 R -> L (in Legnano; O(2) affinity up;
dbSNP:rs63751282).
{ECO:0000269|PubMed:7462179}.
/FTId=VAR_002853.
VARIANT 142 142 R -> P (in Singapore; dbSNP:rs63751282).
/FTId=VAR_002855.
CONFLICT 10 10 N -> H (in Ref. 13; BAD97112).
{ECO:0000305}.
HELIX 5 18 {ECO:0000244|PDB:2W72}.
HELIX 19 21 {ECO:0000244|PDB:2W72}.
HELIX 22 36 {ECO:0000244|PDB:2W72}.
HELIX 38 43 {ECO:0000244|PDB:2W72}.
STRAND 45 47 {ECO:0000244|PDB:1M9P}.
STRAND 50 52 {ECO:0000244|PDB:1NEJ}.
HELIX 54 72 {ECO:0000244|PDB:2W72}.
TURN 73 75 {ECO:0000244|PDB:2W72}.
HELIX 77 80 {ECO:0000244|PDB:2W72}.
HELIX 82 90 {ECO:0000244|PDB:2W72}.
TURN 91 93 {ECO:0000244|PDB:2M6Z}.
HELIX 97 113 {ECO:0000244|PDB:2W72}.
TURN 115 117 {ECO:0000244|PDB:2W72}.
HELIX 120 138 {ECO:0000244|PDB:2W72}.
HELIX 139 141 {ECO:0000244|PDB:1SDL}.
SEQUENCE 142 AA; 15258 MW; 15E13666573BBBAE CRC64;
MVLSPADKTN VKAAWGKVGA HAGEYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG
KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHLPAEFTP
AVHASLDKFL ASVSTVLTSK YR


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