HBA_HUMAN
ID HBA_HUMAN Reviewed; 142 AA.
AC P69905; P01922; Q1HDT5; Q3MIF5; Q53F97; Q96KF1; Q9NYR7; Q9UCM0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Hemoglobin subunit alpha;
DE AltName: Full=Alpha-globin;
DE AltName: Full=Hemoglobin alpha chain;
DE Contains:
DE RecName: Full=Hemopressin {ECO:0000303|PubMed:18077343};
GN Name=HBA1;
GN and
GN Name=HBA2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1).
RX PubMed=7448866; DOI=10.1016/0092-8674(80)90347-5;
RA Michelson A.M., Orkin S.H.;
RT "The 3' untranslated regions of the duplicated human alpha-globin genes are
RT unexpectedly divergent.";
RL Cell 22:371-377(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (HBA2).
RX PubMed=6244294; DOI=10.1016/s0021-9258(19)85810-6;
RA Wilson J.T., Wilson L.B., Reddy V.B., Cavallesco C., Ghosh P.K.,
RA Deriel J.K., Forget B.G., Weissman S.M.;
RT "Nucleotide sequence of the coding portion of human alpha globin messenger
RT RNA.";
RL J. Biol. Chem. 255:2807-2815(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2).
RX PubMed=6452630; DOI=10.1073/pnas.77.12.7054;
RA Liebhaber S.A., Goossens M.J., Kan Y.W.;
RT "Cloning and complete nucleotide sequence of human 5'-alpha-globin gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:7054-7058(1980).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6946451; DOI=10.1073/pnas.78.8.5041;
RA Orkin S.H., Goff S.C., Hechtman R.L.;
RT "Mutation in an intervening sequence splice junction in man.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:5041-5045(1981).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-32.
RX PubMed=11410421;
RA Zhao Y., Xu X.;
RT "Alpha2(CD31 AGG-->AAG, Arg-->Lys) causing non-deletional alpha-thalassemia
RT in a Chinese family with HbH disease.";
RL Haematologica 86:541-542(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1).
RX PubMed=11402454;
RA Zhao Y., Zhong M., Liu Z., Xu X.;
RT "Rapid detection of the common alpha-thalassemia-2 determinants by PCR
RT assay.";
RL Zhonghua Yi Xue Yi Chuan Xue Za Zhi 18:216-218(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALPHA-1 AND ALPHA-2).
RX PubMed=16728641; DOI=10.1126/science.1126431;
RA De Gobbi M., Viprakasit V., Hughes J.R., Fisher C., Buckle V.J., Ayyub H.,
RA Gibbons R.J., Vernimmen D., Yoshinaga Y., de Jong P., Cheng J.-F.,
RA Rubin E.M., Wood W.G., Bowden D., Higgs D.R.;
RT "A regulatory SNP causes a human genetic disease by creating a new
RT transcriptional promoter.";
RL Science 312:1215-1217(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (HBA2).
RC TISSUE=Blood;
RA Kutlar F., Leithner C., Kutlar A.;
RT "Rapid sequencing of mRNA of the human alpha two globin, directly isolated
RT from reticulocytes in whole blood.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] (HBA1).
RC TISSUE=Blood;
RA Kutlar F., Leithner C., Kutlar A.;
RT "cDNA sequencing of human alpha one globin mRNA, the 3'untranslated region
RT is different than alpha two globin.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RA Kutlar F., Holley L., Leithner C., Kutlar A.;
RT "An alpha chain variant 'Hemoglobin J-Toronto (Cd.5 /Ala to Asp)' mutation
RT was detected on the alpha-1 globin mRNA by sequencing of cDNA.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2), AND VARIANT EVANS MET-63.
RC TISSUE=Blood;
RA Kutlar F., Elam D., Hoff J.V., Holley L., Kutlar A.;
RT "Unstable Hb 'Evans' (GTG->ATG/Val 62 Met) was detected on the alpha-2
RT globin gene of an Hispanic girl.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2), AND VARIANT G-PHILADELPHIA
RP LYS-69.
RA Kutlar F., Davis D.H., Nechtman J., Elam D.;
RT "Hb G-Philadelphia (Alpha,Codon 68;AAC>AAG/Asn>Lys)in black is detected on
RT a chromosome that carries alpha 3.7 kb deletion showed completely normal
RT alpha-2 globin gene sequence.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HBA1 AND HBA2).
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [15]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HBA1 AND HBA2).
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [16]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HBA1 AND HBA2).
RC TISSUE=Bone marrow, Brain, Lung, and Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [17]
RP PROTEIN SEQUENCE OF 2-142.
RX PubMed=13872627; DOI=10.1515/bchm2.1961.325.1.283;
RA Braunitzer G., Gehring-Muller R., Hilschmann N., Hilse K., Hobom G.,
RA Rudloff V., Wittmann-Liebold B.;
RT "The constitution of normal adult human haemoglobin.";
RL Hoppe-Seyler's Z. Physiol. Chem. 325:283-286(1961).
RN [18]
RP PROTEIN SEQUENCE OF 2-142.
RX PubMed=13954546;
RA Hill R.J., Konigsberg W.;
RT "The structure of human hemoglobin: IV. The chymotryptic digestion of the
RT alpha chain of human hemoglobin.";
RL J. Biol. Chem. 237:3151-3156(1962).
RN [19]
RP PROTEIN SEQUENCE OF 2-142.
RX PubMed=14093912; DOI=10.1021/bi00906a030;
RA Schroeder W.A., Shelton J.R., Shelton J.B., Cormick J.;
RT "The amino acid sequence of the alpha chain of human fetal hemoglobin.";
RL Biochemistry 2:1353-1357(1963).
RN [20]
RP PROTEIN SEQUENCE OF 2-32.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [21]
RP PROTEIN SEQUENCE OF 128-142, AND VARIANT ETHIOPIA HIS-141.
RC TISSUE=Umbilical cord blood;
RX PubMed=1428951; DOI=10.3109/03630269209005699;
RA Webber B.B., Wilson J.B., Gu L.-H., Huisman T.H.J.;
RT "Hb Ethiopia or alpha 2(140)(HC2)Tyr----His beta 2.";
RL Hemoglobin 16:441-443(1992).
RN [22]
RP GLYCATION AT LYS-8; LYS-17; LYS-41 AND LYS-62, AND LACK OF GLYCATION AT
RP LYS-12; LYS-57; LYS-61; LYS-91 AND LYS-100.
RX PubMed=7358733; DOI=10.1016/s0021-9258(19)85860-x;
RA Shapiro R., McManus M.J., Zalut C., Bunn H.F.;
RT "Sites of nonenzymatic glycosylation of human hemoglobin A.";
RL J. Biol. Chem. 255:3120-3127(1980).
RN [23]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY N.AMERICANUS APR-2, AND
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=12552433; DOI=10.1086/367708;
RA Williamson A.L., Brindley P.J., Abbenante G., Datu B.J., Prociv P.,
RA Berry C., Girdwood K., Pritchard D.I., Fairlie D.P., Hotez P.J., Zhan B.,
RA Loukas A.;
RT "Hookworm aspartic protease, Na-APR-2, cleaves human hemoglobin and serum
RT proteins in a host-specific fashion.";
RL J. Infect. Dis. 187:484-494(2003).
RN [24]
RP FUNCTION (HEMOPRESSIN).
RX PubMed=18077343; DOI=10.1073/pnas.0706980105;
RA Heimann A.S., Gomes I., Dale C.S., Pagano R.L., Gupta A., de Souza L.L.,
RA Luchessi A.D., Castro L.M., Giorgi R., Rioli V., Ferro E.S., Devi L.A.;
RT "Hemopressin is an inverse agonist of CB1 cannabinoid receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:20588-20593(2007).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; THR-9; TYR-25; SER-36 AND
RP SER-50, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN.
RX PubMed=1177322; DOI=10.1016/s0022-2836(75)80037-4;
RA Fermi G.;
RT "Three-dimensional Fourier synthesis of human deoxyhaemoglobin at 2.5-A
RT resolution: refinement of the atomic model.";
RL J. Mol. Biol. 97:237-256(1975).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=7373648; DOI=10.1016/0022-2836(80)90308-3;
RA Baldwin J.M.;
RT "The structure of human carbonmonoxy haemoglobin at 2.7-A resolution.";
RL J. Mol. Biol. 136:103-128(1980).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF LIGANDED R2 STATE.
RX PubMed=1512262; DOI=10.1016/s0021-9258(18)41919-9;
RA Silva M.M., Rogers P.H., Arnone A.;
RT "A third quaternary structure of human hemoglobin A at 1.7-A resolution.";
RL J. Biol. Chem. 267:17248-17256(1992).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF HB GOWER-2.
RX PubMed=9665850; DOI=10.1006/jmbi.1998.1868;
RA Sutherland-Smith A.J., Baker H.M., Hofmann O.M., Brittain T., Baker E.N.;
RT "Crystal structure of a human embryonic haemoglobin: the carbonmonoxy form
RT of Gower II (alpha2 epsilon2) haemoglobin at 2.9-A resolution.";
RL J. Mol. Biol. 280:475-484(1998).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF VARIANT HB CATONSVILLE GLU-38 INS.
RX PubMed=8448109; DOI=10.1021/bi00061a007;
RA Kavanaugh J.S., Moo-Penn W.F., Arnone A.;
RT "Accommodation of insertions in helices: the mutation in hemoglobin
RT Catonsville (Pro 37 alpha-Glu-Thr 38 alpha) generates a 3(10)-->alpha
RT bulge.";
RL Biochemistry 32:2509-2513(1993).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS), AND INTERACTION WITH STAPHYLOCOCCUS
RP AUREUS PROTEIN ISDB.
RX PubMed=29109153; DOI=10.1074/jbc.m117.806562;
RA Bowden C.F.M., Chan A.C.K., Li E.J.W., Arrieta A.L., Eltis L.D.,
RA Murphy M.E.P.;
RT "Structure-function analyses reveal key features in Staphylococcus aureus
RT IsdB-associated unfolding of the heme-binding pocket of human hemoglobin.";
RL J. Biol. Chem. 293:177-190(2018).
RN [35]
RP VARIANT J-CAPE TOWN GLN-93.
RX PubMed=5988206; DOI=10.1038/212792a0;
RA Botha M.C., Beale D., Isaacs W.A., Lehmann H.;
RT "Hemoglobin J Cape Town-alpha-2 92 arginine replaced by glutamine beta-2.";
RL Nature 212:792-795(1966).
RN [36]
RP VARIANT BIBBA PRO-137.
RX PubMed=5440849; DOI=10.1016/s0021-9258(18)63222-3;
RA Smith L.L., Barton B.P., Huisman T.H.;
RT "Subunit dissociation of the unstable hemoglobin Bibba (alpha 2-
RT 136Pro(H19)beta 2).";
RL J. Biol. Chem. 245:2185-2188(1970).
RN [37]
RP CHARACTERIZATION OF VARIANT J-CAPE TOWN GLN-93.
RX PubMed=5091982; DOI=10.1016/0022-2836(71)90029-5;
RA Nagel R.L., Gibson Q.H., Jenkins T.;
RT "Ligand binding in hemoglobin J Capetown.";
RL J. Mol. Biol. 58:643-650(1971).
RN [38]
RP VARIANT HOPKINS-II ASP-113.
RX PubMed=5288820; DOI=10.1038/newbio234248a0;
RA Charache S., Ostertag W., von Ehrenstein G.;
RT "Clinical studies and physiological properties of Hopkins-2 haemoglobin.";
RL Nature New Biol. 234:248-251(1971).
RN [39]
RP VARIANT DENMARK HILL ALA-96.
RX PubMed=5085669; DOI=10.1016/0005-2795(72)90006-2;
RA Wiltshire B.G., Clark K.G., Lorkin P.A., Lehmann H.;
RT "Haemoglobin Denmark Hill 95 (G2) Pro-Ala, a variant with unusual
RT electrophoretic and oxygen-binding properties.";
RL Biochim. Biophys. Acta 278:459-464(1972).
RN [40]
RP VARIANT SETIF TYR-95.
RX PubMed=4667378; DOI=10.1016/0014-5793(72)80645-8;
RA Wajcman H., Belkhodja O., Labie D.;
RT "Hb Setif: G1 (94) Asp-Tyr. A new chain hemoglobin variant with
RT substitution of the residue involved in hydrogen bond between unlike
RT subunits.";
RL FEBS Lett. 27:298-300(1972).
RN [41]
RP VARIANT ANN ARBOR ARG-81.
RX PubMed=5033650; DOI=10.1126/science.176.4042.1427;
RA Adams J.G. III, Winter W.P., Rucknagel D.L., Spencer H.H.;
RT "Biosynthesis of hemoglobin Ann Arbor: evidence for catabolic and feedback
RT regulation.";
RL Science 176:1427-1429(1972).
RN [42]
RP VARIANT SAWARA ALA-7.
RX PubMed=4744335; DOI=10.1016/0005-2795(73)90169-4;
RA Sumida I., Ohta Y., Imamura T., Yanase T.;
RT "Hemoglobin Sawara: alpha 6(A4) aspartic acid leads to alanine.";
RL Biochim. Biophys. Acta 322:23-26(1973).
RN [43]
RP VARIANT M-BOSTON/M-OSAKA TYR-59.
RX PubMed=4521212; DOI=10.1073/pnas.70.12.3870;
RA Pulsinelli P.D., Perutz M.F., Nagel R.L.;
RT "Structure of hemoglobin M Boston, a variant with a five-coordinated ferric
RT heme.";
RL Proc. Natl. Acad. Sci. U.S.A. 70:3870-3874(1973).
RN [44]
RP VARIANT J-ROVIGO ASP-54.
RX PubMed=4824923; DOI=10.1016/0005-2795(74)90099-3;
RA Alberti R., Mariuzzi G.M., Artibani L., Bruni E., Tentori L.;
RT "A new haemoglobin variant: J-Rovigo alpha 53 (E-2) alanine leads to
RT aspartic acid.";
RL Biochim. Biophys. Acta 342:1-4(1974).
RN [45]
RP VARIANT HIROSAKI LEU-44.
RX PubMed=1182166; DOI=10.1016/0005-2795(75)90325-6;
RA Ohba Y., Miyaji T., Matsuoka M., Yokoyama M., Numakura H.;
RT "Hemoglobin Hirosaki (alpha 43 [CE 1] Phe replaced by Leu), a new unstable
RT variant.";
RL Biochim. Biophys. Acta 405:155-160(1975).
RN [46]
RP VARIANT PONTOISE ASP-64.
RX PubMed=849454; DOI=10.1016/0005-2795(77)90036-8;
RA Thillet J., Blouquit Y., Perrone F., Rosa J.;
RT "Hemoglobin Pontoise alpha63 Ala replaced by Asp(E12). A new fast moving
RT variant.";
RL Biochim. Biophys. Acta 491:16-22(1977).
RN [47]
RP CHARACTERIZATION OF VARIANT SAWARA ALA-7.
RX PubMed=20980; DOI=10.1016/0005-2795(77)90253-7;
RA Sasaki J., Imamura T., Sumida I., Yanase T., Ohya M.;
RT "Increased oxygen affinity for hemoglobin Sawara: alphaA4(6) aspartic acid
RT replaced by alanine.";
RL Biochim. Biophys. Acta 495:183-186(1977).
RN [48]
RP VARIANT PORT PHILLIP PRO-92.
RX PubMed=902765; DOI=10.1016/0014-5793(77)80940-x;
RA Brennan S.O., Tauro G.P., Melrose W.;
RT "Haemoglobin Port Phillip alpha91 (FG3) Leu replaced by Pro, a new unstable
RT haemoglobin.";
RL FEBS Lett. 81:115-117(1977).
RN [49]
RP VARIANT MOABIT ARG-87.
RX PubMed=108887; DOI=10.1159/000207643;
RA Knuth A., Pribilla W., Marti H.R., Winterhalter K.H.;
RT "Hemoglobin Moabit: alpha 86 (F7) Leu leads to Arg: a new unstable abnormal
RT hemoglobin.";
RL Acta Haematol. 61:121-124(1979).
RN [50]
RP VARIANT PRATO SER-32.
RX PubMed=486536; DOI=10.1016/0005-2795(79)90184-3;
RA Marinucci M., Mavilio F., Massa A., Gabbianelli M., Fontanarosa P.P.,
RA Camagna A., Ignesti C., Tentori L.;
RT "A new abnormal human hemoglobin: Hb Prato (alpha 2 31 (B12) Arg leads to
RT Ser beta 2).";
RL Biochim. Biophys. Acta 578:534-540(1979).
RN [51]
RP VARIANT DUNN ASN-7.
RX PubMed=478975; DOI=10.3109/03630267908998909;
RA Jue D.L., Johnson M.H., Patchen L.C., Moo-Penn W.F.;
RT "Hemoglobin Dunn: alpha 6 (A4) aspartic acid replaced by asparagine.";
RL Hemoglobin 3:137-143(1979).
RN [52]
RP CHARACTERIZATION OF VARIANT DUNN ASN-7.
RX PubMed=7435503; DOI=10.1002/ajh.2830090203;
RA Charache S., Brimhall B., Zaatari G.;
RT "Oxygen affinity and stability of hemoglobin Dunn alpha 6(A4)Asp replaced
RT by Asn): use of isoelectric focusing in recognition of a new abnormal
RT hemoglobin.";
RL Am. J. Hematol. 9:151-160(1980).
RN [53]
RP VARIANT MILLEDGEVILLE LEU-45.
RX PubMed=7213661; DOI=10.1016/0005-2795(80)90138-5;
RA Honig G.R., Vida L.N., Shamsuddin M., Mason R.G., Schlumpf H.W., Luke R.A.;
RT "Hemoglobin Milledgeville (alpha 44 (CD2) Pro leads to Leu): a new variant
RT with increased oxygen affinity.";
RL Biochim. Biophys. Acta 626:424-431(1980).
RN [54]
RP VARIANT LEGNANO LEU-142.
RX PubMed=7462179; DOI=10.1093/oxfordjournals.jbchem.a133091;
RA Giuliani A., Maffi D., Cappabianca M.P., Tentori L.;
RT "Hemoglobin Legnano (alpha 2 141 (HC3) Arg leads to Leu beta2) a new high
RT oxygen affinity variant. Functional and structural studies.";
RL J. Biochem. 88:1233-1237(1980).
RN [55]
RP VARIANT SURESNES HIS-142.
RX PubMed=7410435; DOI=10.1016/s0021-9258(19)70585-7;
RA Poyart C., Bursaux E., Arnone A., Bonaventura J., Bonaventura C.;
RT "Structural and functional studies of hemoglobin Suresnes (arg 141 alpha 2
RT replaced by His beta 2). Consequences of disrupting an oxygen-linked anion-
RT binding site.";
RL J. Biol. Chem. 255:9465-9473(1980).
RN [56]
RP VARIANT FERNDOWN VAL-7.
RX PubMed=7238857; DOI=10.1016/0014-5793(81)81047-2;
RA Lee-Potter J.P., Deacon-Smith R.A., Lehmann H., Robb L.;
RT "Haemoglobin Ferndown (alpha 6 [A4] aspartic acid replaced by valine).";
RL FEBS Lett. 126:117-119(1981).
RN [57]
RP VARIANT TOTTORI VAL-60.
RX PubMed=7275660; DOI=10.3109/03630268108991818;
RA Nakatsuji T., Miwa S., Ohba Y., Miyaji T., Matsumoto N., Matsuoka I.;
RT "Hemoglobin Tottori (alpha 59[E8] glycine replaced by valine).";
RL Hemoglobin 5:427-439(1981).
RN [58]
RP VARIANT KAWACHI ARG-45.
RX PubMed=7068434; DOI=10.3109/03630268208996932;
RA Harano T., Harano K., Ueda S., Shibata S., Imai K., Ohba Y., Shinohara T.,
RA Horio S., Nishioka K., Shirotani H.;
RT "Hemoglobin Kawachi [alpha 44 (CE2) Pro leads to Arg]: a new hemoglobin
RT variant of high oxygen affinity with amino acid substitution at alpha 1
RT beta 2 contact.";
RL Hemoglobin 6:43-49(1982).
RN [59]
RP VARIANT KOKURA GLY-48.
RX PubMed=7068437; DOI=10.3109/03630268208996936;
RA Ohba Y., Hattori Y., Matsuoka M., Miyaji T., Fuyuno K.;
RT "HB Kokura [alpha 47 (CE 5) Asp leads to Gly]: a slightly unstable
RT variant.";
RL Hemoglobin 6:69-74(1982).
RN [60]
RP VARIANT EVANSTON ARG-15.
RX PubMed=6882779; DOI=10.1016/0167-4838(83)90122-x;
RA Moo-Penn W.F., Baine R.M., Jue D.L., Johnson M.H., McGuffey J.E.,
RA Benson J.M.;
RT "Hemoglobin Evanston: alpha 14(A12) Trp leads to Arg. A variant hemoglobin
RT associated with alpha-thalassemia-2.";
RL Biochim. Biophys. Acta 747:65-70(1983).
RN [61]
RP VARIANT TOKONAME THR-140.
RX PubMed=6188720; DOI=10.3109/03630268309038404;
RA Harano T., Harano K., Shibata S., Ueda S., Imai K., Seki M.;
RT "Hemoglobin Tokoname [alpha 139 (HC 1) Lys leads to Thr]: a new hemoglobin
RT variant with a slightly increased oxygen affinity.";
RL Hemoglobin 7:85-90(1983).
RN [62]
RP VARIANT IWATA ARG-88.
RX PubMed=6874376;
RA Liu G.Y., Zhang G.X., Nie S.Y., Luo H.Y., Teng Y.Q., Liu S.P., Song M.,
RA Son L., Chen S.S., Jia P.C., Liang C.C.;
RT "A case of hemoglobin Iwata [alpha 87(F8)His leads to Arg] in China.";
RL Hemoglobin 7:279-282(1983).
RN [63]
RP VARIANT ETOBICOKE ARG-85.
RX PubMed=6874377; DOI=10.3109/03630268309048660;
RA Headlee M.G., Nakatsuji T., Lam H., Wrightstone R.N., Huisman T.H.;
RT "Hb Etobicoke, alpha 85(F5) Ser leads to Arg found in a newborn of French-
RT Indian-English descent.";
RL Hemoglobin 7:285-287(1983).
RN [64]
RP VARIANT AICHI ARG-51.
RX PubMed=6714429; DOI=10.1016/0014-5793(84)80337-3;
RA Harano T., Harano K., Shibata S., Ueda S., Mori H., Seki M.;
RT "Hemoglobin Aichi [alpha 50(CE8) His----Arg]: a new slightly unstable
RT hemoglobin variant discovered in Japan.";
RL FEBS Lett. 169:297-299(1984).
RN [65]
RP VARIANT CORDELE ALA-48.
RX PubMed=6547117; DOI=10.3109/03630268408996959;
RA Nakatsuji T., Wilson J.B., Huisman T.H.;
RT "Hb Cordele alpha(2)47 (CE5)Asp----Ala beta 2. A mildly unstable variant
RT observed in black twins.";
RL Hemoglobin 8:37-46(1984).
RN [66]
RP VARIANT MANITOBA ARG-103, AND VARIANT CONTALDO ARG-104.
RX PubMed=6547932; DOI=10.3109/03630268408991710;
RA Sciarratta G.V., Ivaldi G., Molaro G.L., Sansone G., Salkie M.L.,
RA Wilson J.B., Reese A.L., Huisman T.H.;
RT "The characterization of hemoglobin Manitoba or alpha (2)102(G9)Ser----Arg
RT beta 2 and hemoglobin Contaldo or alpha (2)103(G10)His----Arg beta 2 by
RT high performance liquid chromatography.";
RL Hemoglobin 8:169-181(1984).
RN [67]
RP CHARACTERIZATION OF VARIANT EVANSTON ARG-15.
RX PubMed=6725558; DOI=10.1172/jci111382;
RA Honig G.R., Shamsuddin M., Vida L.N., Mompoint M., Valcourt E., Bowie L.J.,
RA Jones E.C., Powers P.A., Spritz R.A., Guis M.;
RT "Hemoglobin Evanston (alpha 14 Trp----Arg). An unstable alpha-chain variant
RT expressed as alpha-thalassemia.";
RL J. Clin. Invest. 73:1740-1749(1984).
RN [68]
RP VARIANT NUNOBIKI CYS-142.
RX PubMed=3973024; DOI=10.1172/jci111749;
RA Shimasaki S.;
RT "A new hemoglobin variant, hemoglobin Nunobiki [alpha 141 (HC3) Arg----
RT Cys]. Notable influence of the carboxy-terminal cysteine upon various
RT physico-chemical characteristics of hemoglobin.";
RL J. Clin. Invest. 75:695-701(1985).
RN [69]
RP VARIANT LOIRE SER-89.
RX PubMed=3142772; DOI=10.1111/j.1432-1033.1988.tb14377.x;
RA Baklouti F., Baudin-Chich V., Kister J., Marden M., Teyssier G., Poyart C.,
RA Delaunay J., Wajcman H.;
RT "Increased oxygen affinity with normal heterotropic effects in hemoglobin
RT Loire [alpha 88(F9)Ala----Ser].";
RL Eur. J. Biochem. 177:307-312(1988).
RN [70]
RP VARIANT LUXEMBOURG HIS-25.
RX PubMed=2599879; DOI=10.3109/03630268908998082;
RA Groff P., Galacteros F., Kalmes G., Blouquit Y., Wajcman H.;
RT "Hb Luxembourg [alpha 24(B5) Tyr----His]: a new unstable variant.";
RL Hemoglobin 13:429-436(1989).
RN [71]
RP VARIANT MIYANO SER-42.
RX PubMed=2634665; DOI=10.3109/03630268908998841;
RA Ohba Y., Imai K., Uenaka R., Ami M., Fujisawa K., Itoh K., Hirakawa K.,
RA Miyaji T.;
RT "Hb Miyano or alpha 41(C6)Thr----Ser: a new high oxygen affinity alpha
RT chain variant found in an erythremic blood donor.";
RL Hemoglobin 13:637-647(1989).
RN [72]
RP VARIANT REIMS GLY-24.
RX PubMed=2634669; DOI=10.3109/03630268908998846;
RA Bardakdjian-Michau J., Rosa J., Galacteros F., Lancelot M., Marquart F.X.;
RT "Hb Reims [alpha 2(23)(B4)Glu----Gly beta 2]: a new alpha chain variant
RT with slightly decreased stability.";
RL Hemoglobin 13:733-735(1989).
RN [73]
RP VARIANT ATTLEBORO PRO-139.
RX PubMed=2108715; DOI=10.1021/bi00453a023;
RA McDonald M.J., Michalski L.A., Turci S.M., Guillette R.A., Jue D.L.,
RA Johnson M.H., Moo-Penn W.F.;
RT "Structural, functional, and subunit assembly properties of hemoglobin
RT Attleboro [alpha 138 (H21) Ser----Pro], a variant possessing a site
RT maturation at a critical C-terminal residue.";
RL Biochemistry 29:173-178(1990).
RN [74]
RP VARIANT FUKUTOMI VAL-127.
RX PubMed=2079432; DOI=10.3109/03630269009005803;
RA Hidaka K., Iuchi I., Kobayashi T., Katoh K., Yaguchi K.;
RT "Hb Fukutomi [alpha 126(H9)Asp----Val]: a new hemoglobin variant with high
RT oxygen affinity.";
RL Hemoglobin 14:499-509(1990).
RN [75]
RP VARIANT DALLAS LYS-98.
RX PubMed=1390940; DOI=10.1016/0925-4439(92)90021-e;
RA Lendaro E., Ippoliti R., Brancaccio A., Bellelli A., Vallone B., Ivaldi G.,
RA Sciarratta G.V., Castello C., Tomova S., Brunori M.;
RT "Hemoglobin Dallas (alpha 97(G4)Asn-->Lys): functional characterization of
RT a high oxygen affinity natural mutant.";
RL Biochim. Biophys. Acta 1180:15-20(1992).
RN [76]
RP VARIANT ROUEN/ETHIOPIA HIS-141.
RX PubMed=1390944; DOI=10.1016/0925-4439(92)90026-j;
RA Wajcman H., Kister J., Marden M., Lahary A., Monconduit M., Galacteros F.;
RT "Hemoglobin Rouen (alpha-140 (HC2) Tyr-->His): alteration of the alpha-
RT chain C-terminal region and moderate increase in oxygen affinity.";
RL Biochim. Biophys. Acta 1180:53-57(1992).
RN [77]
RP VARIANT AL-AIN ABU DHABI ASP-19.
RX PubMed=1428941; DOI=10.3109/03630269209005687;
RA Abbes S., M'Rad A., Fitzgerald P.A., Dormer P., Blouquit Y., Kister J.,
RA Galacteros F., Wajcman H.;
RT "HB Al-Ain Abu Dhabi [alpha 18(A16)Gly-->Asp]: a new hemoglobin variant
RT discovered in an Emiratee family.";
RL Hemoglobin 16:355-362(1992).
RN [78]
RP VARIANT QUESTEMBERT PRO-132.
RX PubMed=8493987; DOI=10.1002/ajh.2830420407;
RA Wajcman H., Vasseur C., Blouquit Y., Rosa J., Labie D., Najman A.,
RA Reman O., Leporrier M., Galacteros F.;
RT "Unstable alpha-chain hemoglobin variants with factitious beta-thalassemia
RT biosynthetic ratio: Hb Questembert (alpha 131[H14]Ser-->Pro) and Hb Caen
RT (alpha 132[H15]Val-->Gly).";
RL Am. J. Hematol. 42:367-374(1993).
RN [79]
RP VARIANT ADANA ASP-60.
RX PubMed=8237999; DOI=10.1002/ajh.2830440410;
RA Cueruek M.A., Dimovski A.J., Baysal E., Gu L.H., Kutlar F.,
RA Molchanova T.P., Webber B.B., Altay C., Guergey A., Huisman T.H.;
RT "Hb Adana or alpha 2(59)(E8)Gly-->Asp beta 2, a severely unstable alpha 1-
RT globin variant, observed in combination with the -(alpha)20.5 Kb alpha-
RT thal-1 deletion in two Turkish patients.";
RL Am. J. Hematol. 44:270-275(1993).
RN [80]
RP VARIANT MONTEFIORE TYR-127.
RX PubMed=8798486; DOI=10.1074/jbc.271.38.22990;
RA Wajcman H., Kister J., Galacteros F., Spielvogel A., Lin M.J.,
RA Vidugiris G.J., Hirsch R.E., Friedman J.M., Nagel R.L.;
RT "Hb Montefiore (126(H9)Asp-->Tyr). High oxygen affinity and loss of
RT cooperativity secondary to C-terminal disruption.";
RL J. Biol. Chem. 271:22990-22998(1996).
RN [81]
RP VARIANT ATAGO TYR-86.
RX PubMed=5115619;
RA Fujiwara N., Maekawa T., Matsuda G.;
RT "Hemoglobin Atago (alpha2-85 Tyr beta-2) a new abnormal human hemoglobin
RT found in Nagasaki. Biochemical studies on hemoglobins and myoglobins. VI.";
RL Int. J. Protein Res. 3:35-39(1971).
RN [82]
RP VARIANT AUCKLAND ASN-88.
RX PubMed=9322075; DOI=10.3109/03630269708993126;
RA Brennan S.O., Matthews J.R.;
RT "Hb Auckland [alpha 87(F8) His-->Asn]: a new mutation of the proximal
RT histidine identified by electrospray mass spectrometry.";
RL Hemoglobin 21:393-403(1997).
RN [83]
RP VARIANTS J-BUDA ASN-62 AND G-PEST ASN-75.
RA Brimhall B.J., Duerst M., Hollan S.R., Stenzel P., Szelenyi J., Jones R.T.;
RT "Structural characterizations of hemoglobins J-Buda (alpha 61 (E10) Lys-to-
RT Asn) and G-Pest (alpha 74 (EF3) Asp-to-Asn).";
RL Biochim. Biophys. Acta 336:344-360(1974).
RN [84]
RP VARIANT CEMENELUM TRP-93.
RX PubMed=8148419; DOI=10.1007/bf01715134;
RA Wajcman H., Kister J., M'Rad A., Soummer A.M., Galacteros F.;
RT "Hb Cemenelum [alpha 92 (FG4) Arg-->Trp]: a hemoglobin variant of the alpha
RT 1/beta 2 interface that displays a moderate increase in oxygen affinity.";
RL Ann. Hematol. 68:73-76(1994).
RN [85]
RP VARIANTS CHONGQING ARG-3 AND HARBIN MET-17.
RX PubMed=6526652; DOI=10.3109/03630268408991742;
RA Zeng Y.-T., Huang S.-Z., Qiu X.-K., Cheng G.-C., Ren Z.-R., Jin Q.-C.,
RA Chen C.-Y., Jiao C.-T., Tang Z.-G., Liu R.-H., Bao X.-H., Zeng L.-Z.,
RA Duan Y.-Q., Zhang G.-Y.;
RT "Hemoglobin Chongqing [alpha 2(NA2)Leu-->Arg] and hemoglobin Harbin [alpha
RT 16(A14)Lys-->Met] found in China.";
RL Hemoglobin 8:569-581(1984).
RN [86]
RP VARIANT CLINIC LYS-61 DEL.
RX PubMed=10206681;
RX DOI=10.1002/(sici)1098-1004(1998)11:5<412::aid-humu15>3.0.co;2-o;
RA Ayala S., Colomer D., Gelpi J.L., Corron J.L.V.;
RT "Alpha-thalassaemia due to a single codon deletion in the alpha 1-globin
RT gene. Computational structural analysis of the new alpha-chain variant.";
RL Hum. Mutat. 11:412-412(1998).
RN [87]
RP VARIANT DAVENPORT HIS-79.
RX PubMed=2101836; DOI=10.3109/03630269009046968;
RA Wilson J.B., Webber B.B., Plaseska D., de Alarcon P.A., McMillan S.K.,
RA Huisman T.H.J.;
RT "Hb Davenport or alpha 2(78)(EF7)Asn-->His beta 2.";
RL Hemoglobin 14:599-605(1990).
RN [88]
RP VARIANT EVANS MET-63.
RX PubMed=2606724; DOI=10.3109/03630268908993106;
RA Wilson J.B., Webber B.B., Kutlar A., Reese A.L., McKie V.C., Lutcher C.L.,
RA Felice A.E., Huisman T.H.J.;
RT "Hb Evans or alpha 262(E11)Val-->Met beta 2; an unstable hemoglobin causing
RT a mild hemolytic anemia.";
RL Hemoglobin 13:557-566(1989).
RN [89]
RP VARIANTS SPANISH TOWN VAL-28 AND FORT DE FRANCE ARG-46.
RX PubMed=2752146;
RA Cash F.E., Monplaisir N., Goossens M., Liebhaber S.A.;
RT "Locus assignment of two alpha-globin structural mutants from the Caribbean
RT basin: alpha Fort de France (alpha 45 Arg) and alpha Spanish Town (alpha 27
RT Val).";
RL Blood 74:833-835(1989).
RN [90]
RP VARIANT GODAVARI THR-96.
RX PubMed=9494044; DOI=10.3109/03630269809071513;
RA Wajcman H., Kister J., Riou J., Galacteros F., Girot R.,
RA Maier-Redelsperger M., Nayudu N.V.S., Giordano P.C.;
RT "Hb Godavari [alpha 95(G2)Pro-->Thr]: a neutral amino acid substitution in
RT the alpha 1 beta 2 interface that modifies the electrophoretic mobility of
RT hemoglobin.";
RL Hemoglobin 22:11-22(1998).
RN [91]
RP VARIANT GRADY GLU-PHE-THR-119 INS.
RX PubMed=4528583; DOI=10.1073/pnas.71.8.3270;
RA Huisman T.H.J., Wilson J.B., Gravely M., Hubbard M.;
RT "Hemoglobin Grady: the first example of a variant with elongated chains due
RT to an insertion of residues.";
RL Proc. Natl. Acad. Sci. U.S.A. 71:3270-3273(1974).
RN [92]
RP VARIANT HANAMAKI GLU-140.
RX PubMed=1634363; DOI=10.3109/03630269209005677;
RA Orisaka M., Tajima T., Harano T., Harano K., Kushida Y., Imai K.;
RT "A new alpha chain variant, Hb Hanamaki or alpha 2(139)(HC1)Lys-->Glu beta
RT 2, found in a Japanese family.";
RL Hemoglobin 16:67-71(1992).
RN [93]
RP VARIANT HANDA MET-91.
RX PubMed=6815131; DOI=10.3109/03630268208996943;
RA Harano T., Harano K., Shibata S., Ueda S., Imai K., Seki M.;
RT "HB Handa [alpha 90 (FG 2) Lys replaced by Met]: structure and biosynthesis
RT of a new slightly higher oxygen affinity variant.";
RL Hemoglobin 6:379-389(1982).
RN [94]
RP VARIANT HASHARON HIS-48.
RX PubMed=5780195; DOI=10.1172/jci106041;
RA Charache S., Mondzac A.M., Gessner U.;
RT "Hemoglobin Hasharon (alpha-2-47 his(CD5)beta-2): a hemoglobin found in low
RT concentration.";
RL J. Clin. Invest. 48:834-847(1969).
RN [95]
RP VARIANT HOBART ARG-21.
RX PubMed=3654264; DOI=10.3109/03630268709017887;
RA Fleming P.J., Sumner D.R., Wyatt K., Hughes W.G., Melrose W.D.,
RA Jupe D.M.D., Baikie M.J.;
RT "Hemoglobin Hobart or alpha 20(Bl)His-->Arg: a new alpha chain hemoglobin
RT variant.";
RL Hemoglobin 11:211-220(1987).
RN [96]
RP VARIANT INKSTER VAL-86.
RX PubMed=4212045; DOI=10.1111/j.1365-2141.1974.tb00489.x;
RA Reed R.E., Winter W.P., Rucknagel D.L.;
RT "Haemoglobin Inkster (alpha2 85aspartic acid leads to valine beta2)
RT coexisting with beta-thalassaemia in a Caucasian family.";
RL Br. J. Haematol. 26:475-484(1974).
RN [97]
RP VARIANT KANAGAWA MET-41.
RX PubMed=1634355; DOI=10.3109/03630269209005670;
RA Miyashita H., Hashimoto K., Mohri H., Ohokubo T., Harano T., Harano K.,
RA Imai K.;
RT "Hb Kanagawa [alpha 40(C5)Lys-->Met]: a new alpha chain variant with an
RT increased oxygen affinity.";
RL Hemoglobin 16:1-10(1992).
RN [98]
RP VARIANT KURDISTAN TYR-48.
RX PubMed=8195005; DOI=10.3109/03630269409014141;
RA Giordano P.C., Harteveld C.L., Streng H., Oosterwijk J.C.,
RA Heister J.G.A.M., Amons R., Bernini L.F.;
RT "Hb Kurdistan [alpha 47(CE5)Asp-->Tyr], a new alpha chain variant in
RT combination with beta (0)-thalassemia.";
RL Hemoglobin 18:11-18(1994).
RN [99]
RP VARIANT KUROSAKI GLU-8.
RX PubMed=7558876; DOI=10.3109/03630269509036940;
RA Harano T., Harano K., Imai K., Murakami T., Matsubara H.;
RT "Hb Kurosaki [alpha 7(A5)Lys-->Glu]: a new alpha chain variant found in a
RT Japanese woman.";
RL Hemoglobin 19:197-201(1995).
RN [100]
RP VARIANT J-MEERUT/J-BIRMINGHAM GLU-121.
RX PubMed=7713747; DOI=10.3109/03630269409045775;
RA Yalcin A., Avcu F., Beyan C., Guergey A., Ural A.U.;
RT "A case of HB J-Meerut (or Hb J-Birmingham) [alpha 120(H3)Ala-->Glu].";
RL Hemoglobin 18:433-435(1994).
RN [101]
RP VARIANT MELUSINE SER-115.
RX PubMed=8294199; DOI=10.3109/03630269308997494;
RA Wacjman H., Klames G., Groff P., Prome D., Riou J., Galacteros F.;
RT "Hb Melusine [alpha 114(GH2)Pro-->Ser]: a new neutral hemoglobin variant.";
RL Hemoglobin 17:397-405(1993).
RN [102]
RP VARIANT MONTGOMERY ARG-49.
RX PubMed=1115799;
RA Brimhall B., Jones R.T., Schneider R.G., Hosty T.S., Tomlin G., Atkins R.;
RT "Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys) and
RT hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg).";
RL Biochim. Biophys. Acta 379:28-32(1975).
RN [103]
RP VARIANT PETAH TIKVA ASP-111.
RX PubMed=7470621;
RA Honig G.R., Shamsuddin M., Zaizov R., Steinherz M., Solar I., Kirschman C.;
RT "Hemoglobin Petah Tikva (alpha 110 Ala replaced by Asp): a new unstable
RT variant with alpha-thalassemia-like expression.";
RL Blood 57:705-711(1981).
RN [104]
RP VARIANT PHNOM PENH ILE-118 INS.
RX PubMed=9452028; DOI=10.1002/humu.1380110107;
RA Wajcman H., Prehu M.O., Prehu C., Blouquit Y., Prome D., Galacteros F.;
RT "Hemoglobin Phnom Penh [alpha117Phe(H1)-Ile-alpha118Thr(H2)]; evidence for
RT a hotspot for insertion of residues in the third exon of the alpha1-globin
RT gene.";
RL Hum. Mutat. Suppl. 1:S20-S22(1998).
RN [105]
RP VARIANT PORT HURON ARG-57.
RX PubMed=1802882; DOI=10.3109/03630269108998858;
RA Zwerdling T., Williams S., Nasr S.A., Rucknagel D.L.;
RT "Hb Port Huron [alpha 56 (E5)Lys-->Arg]: a new alpha chain variant.";
RL Hemoglobin 15:381-391(1991).
RN [106]
RP VARIANT SHENYANG GLU-27.
RX PubMed=7161109;
RA Zeng Y.-T., Huang S.-Z., Zhou X., Qiu X.-K., Dong Q., Li M., Bai J.;
RT "Hb Shenyang (alpha 26 (B7) Ala replaced by Glu): a new unstable variant
RT found in China.";
RL Hemoglobin 6:625-628(1982).
RN [107]
RP VARIANT SUAN-DOK ARG-110.
RX PubMed=478977; DOI=10.3109/03630267908998911;
RA Sanguansermsri T., Matragoon S., Changloah L., Flatz G.;
RT "Hemoglobin Suan-Dok (alpha 2 109 (G16) Leu replaced by Arg beta 2): an
RT unstable variant associated with alpha-thalassemia.";
RL Hemoglobin 3:161-174(1979).
RN [108]
RP INVOLVEMENT IN HEIBAN, AND VARIANT TOYAMA ARG-137.
RX PubMed=2833478; DOI=10.3109/03630268709027870;
RA Ohba Y., Yamamoto K., Hattori Y., Kawata R., Miyaji T.;
RT "Hyperunstable hemoglobin Toyama [alpha 2 136(H19)Leu----Arg beta 2]:
RT detection and identification by in vitro biosynthesis with radioactive
RT amino acids.";
RL Hemoglobin 11:539-556(1987).
RN [109]
RP VARIANT SUN PRAIRIE PRO-131.
RX PubMed=2079430; DOI=10.3109/03630269009005801;
RA Harkness M., Harkness D.R., Kutlar F., Kutlar A., Wilson J.B., Webber B.B.,
RA Codrington J.F., Huisman T.H.J.;
RT "Hb Sun Prairie or alpha(2)130(H13)Ala-->Pro beta 2, a new unstable variant
RT occurring in low quantities.";
RL Hemoglobin 14:479-489(1990).
RN [110]
RP VARIANT SWAN RIVER GLY-7.
RX PubMed=8745434; DOI=10.3109/03630269609027912;
RA Harano T., Harano K., Imai K., Terunuma S.;
RT "HB Swan River [alpha 6(A4)Asp-->Gly] observed in a Japanese man.";
RL Hemoglobin 20:75-78(1996).
RN [111]
RP VARIANT THIONVILLE GLU-2.
RX PubMed=1618774; DOI=10.1016/s0021-9258(18)42331-9;
RA Vasseur C., Blouquit Y., Kister J., Prome D., Kavanaugh J.S., Rogers P.H.,
RA Guillemin C., Arnone A., Galacteros F., Poyart C., Rosa J., Wajcman H.;
RT "Hemoglobin Thionville. An alpha-chain variant with a substitution of a
RT glutamate for valine at NA-1 and having an acetylated methionine NH2
RT terminus.";
RL J. Biol. Chem. 267:12682-12691(1992).
RN [112]
RP VARIANT TUNIS-BIZERTE PRO-130.
RX PubMed=7786798; DOI=10.1111/j.1365-2141.1995.tb03382.x;
RA Darbellay R., Mach-Pascual S., Rose K., Graf J., Beris P.;
RT "Haemoglobin Tunis-Bizerte: a new alpha 1 globin 129 Leu-->Pro unstable
RT variant with thalassaemic phenotype.";
RL Br. J. Haematol. 90:71-76(1995).
RN [113]
RP VARIANT TURRIFF GLU-100.
RX PubMed=1634357; DOI=10.3109/03630269209005671;
RA Langdown J.V., Davidson R.J., Williamson D.;
RT "A new alpha chain variant, Hb Turriff [alpha 99(G6)Lys-->Glu]: the
RT interference of abnormal hemoglobins in Hb A1c determination.";
RL Hemoglobin 16:11-17(1992).
RN [114]
RP VARIANT VAL DE MARNE ARG-134.
RX PubMed=8294200; DOI=10.3109/03630269308997495;
RA Wacjman H., Kister J., M'Rad A., Marden M.C., Riou J., Galacteros F.;
RT "Hb Val de Marne [alpha 133(H16)Ser-->Arg]: a new hemoglobin variant with
RT moderate increase in oxygen affinity.";
RL Hemoglobin 17:407-417(1993).
RN [115]
RP VARIANT WESTMEAD GLN-123.
RX PubMed=1686260; DOI=10.3109/03630269109027881;
RA Jiang N.H., Liang S., Wen X.J., Liang R., Su C., Tang Z.;
RT "Hb Westmead: an alpha 2-globin gene mutation detected by polymerase chain
RT reaction and Stu I cleavage.";
RL Hemoglobin 15:291-295(1991).
RN [116]
RP VARIANT WOODVILLE TYR-7.
RX PubMed=3754246; DOI=10.3109/03630268609046440;
RA Como P.F., Barber S., Sage R.E., Kronenberg H.;
RT "Hemoglobin Woodville: alpha (2)6(A4) aspartic acid-->tyrosine.";
RL Hemoglobin 10:135-141(1986).
RN [117]
RP VARIANT YUDA ASP-131.
RX PubMed=1428950; DOI=10.3109/03630269209005698;
RA Fujisawa K., Hattori Y., Ohba Y., Ando S.;
RT "Hb Yuda or alpha 130(H13)Ala-->Asp; a new alpha chain variant with low
RT oxygen affinity.";
RL Hemoglobin 16:435-439(1992).
RN [118]
RP VARIANT ZAIRE HIS-LEU-PRO-ALA-GLU-117 INS.
RX PubMed=1511986; DOI=10.1007/bf00221961;
RA Wajcman H., Blouquit Y., Vasseur C., le Querrec A., Laniece M.,
RA Melevendi C., Rasore A., Galacteros F.;
RT "Two new human hemoglobin variants caused by unusual mutational events: Hb
RT Zaire contains a five residue repetition within the alpha-chain and Hb
RT Duino has two residues substituted in the beta-chain.";
RL Hum. Genet. 89:676-680(1992).
RN [119]
RP VARIANT HBH VAL-63 DEL.
RX PubMed=10569720; DOI=10.3109/03630269909090747;
RA Traeger-Synodinos J., Harteveld C.L., Kanavakis E., Giordano P.C.,
RA Kattamis C., Bernini L.F.;
RT "Hb Aghia Sophia [alpha62(E11)Val-->0 (alpha1)], an 'in-frame' deletion
RT causing alpha-thalassemia.";
RL Hemoglobin 23:317-324(1999).
RN [120]
RP VARIANT BOGHE GLN-59, AND VARIANT CHAROLLES TYR-104.
RX PubMed=10569723; DOI=10.3109/03630269909090750;
RA Lacan P., Francina A., Souillet G., Aubry M., Couprie N., Dementhon L.,
RA Becchi M.;
RT "Two new alpha chain variants: Hb Boghe [alpha58(E7)His-->Gln, alpha2], a
RT variant on the distal histidine, and Hb Charolles [alpha103(G10)His-Tyr,
RT alpha1].";
RL Hemoglobin 23:345-352(1999).
RN [121]
RP VARIANT CAMPINAS VAL-27, AND VARIANT WEST ONE GLY-127.
RX PubMed=14576901; DOI=10.1590/s0100-879x2003001100004;
RA Jorge S.B., Melo M.B., Costa F.F., Sonati M.F.;
RT "Screening for mutations in human alpha-globin genes by nonradioactive
RT single-strand conformation polymorphism.";
RL Braz. J. Med. Biol. Res. 36:1471-1474(2003).
RN [122]
RP VARIANT BASSETT ALA-95, AND CHARACTERIZATION OF VARIANT BASSETT ALA-95.
RX PubMed=15495251; DOI=10.1002/ajh.20184;
RA Abdulmalik O., Safo M.K., Lerner N.B., Ochotorena J., Daikhin E., Lakka V.,
RA Santacroce R., Abraham D.J., Asakura T.;
RT "Characterization of hemoglobin Bassett (alpha94Asp-->Ala), a variant with
RT very low oxygen affinity.";
RL Am. J. Hematol. 77:268-276(2004).
RN [123]
RP VARIANT PLASENCIA ARG-126.
RX PubMed=15921163; DOI=10.1081/hem-58578;
RA Martin G., Villegas A., Gonzalez F.A., Ropero P., Hojas R., Polo M.,
RA Mateo M., Salvador M., Benavente C.;
RT "A novel mutation of the alpha2-globin causing alpha(+)-thalassemia: Hb
RT Plasencia [alpha125(H8)Leu-->Arg (alpha2).";
RL Hemoglobin 29:113-117(2005).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues.
CC -!- FUNCTION: [Hemopressin]: Hemopressin acts as an antagonist peptide of
CC the cannabinoid receptor CNR1 (PubMed:18077343). Hemopressin-binding
CC efficiently blocks cannabinoid receptor CNR1 and subsequent signaling
CC (PubMed:18077343). {ECO:0000269|PubMed:18077343}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in
CC adult hemoglobin A (HbA); two alpha chains and two delta chains in
CC adult hemoglobin A2 (HbA2); two alpha chains and two epsilon chains in
CC early embryonic hemoglobin Gower-2; two alpha chains and two gamma
CC chains in fetal hemoglobin F (HbF).
CC -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
CC protein isdB. {ECO:0000269|PubMed:29109153}.
CC -!- INTERACTION:
CC P69905; Q9NZD4: AHSP; NbExp=2; IntAct=EBI-714680, EBI-720250;
CC P69905; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-714680, EBI-2808286;
CC P69905; P00387: CYB5R3; NbExp=2; IntAct=EBI-714680, EBI-1046040;
CC P69905; P68871: HBB; NbExp=29; IntAct=EBI-714680, EBI-715554;
CC P69905; P02042: HBD; NbExp=3; IntAct=EBI-714680, EBI-6152722;
CC P69905; P02100: HBE1; NbExp=4; IntAct=EBI-714680, EBI-6190240;
CC P69905; P69892: HBG2; NbExp=3; IntAct=EBI-714680, EBI-3910089;
CC P69905; P09105: HBQ1; NbExp=3; IntAct=EBI-714680, EBI-10193656;
CC P69905; Q15323: KRT31; NbExp=3; IntAct=EBI-714680, EBI-948001;
CC P69905; O76011: KRT34; NbExp=3; IntAct=EBI-714680, EBI-1047093;
CC P69905; Q6A162: KRT40; NbExp=3; IntAct=EBI-714680, EBI-10171697;
CC P69905; P29474: NOS3; NbExp=2; IntAct=EBI-714680, EBI-1391623;
CC P69905; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-714680, EBI-22310682;
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- PTM: The initiator Met is not cleaved in variant Thionville and is
CC acetylated.
CC -!- DISEASE: Heinz body anemias (HEIBAN) [MIM:140700]: Form of non-
CC spherocytic hemolytic anemia of Dacie type 1. After splenectomy, which
CC has little benefit, basophilic inclusions called Heinz bodies are
CC demonstrable in the erythrocytes. Before splenectomy, diffuse or
CC punctate basophilia may be evident. Most of these cases are probably
CC instances of hemoglobinopathy. The hemoglobin demonstrates heat
CC lability. Heinz bodies are observed also with the Ivemark syndrome
CC (asplenia with cardiovascular anomalies) and with glutathione
CC peroxidase deficiency. {ECO:0000269|PubMed:2833478}. Note=The disease
CC may be caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Alpha-thalassemia (A-THAL) [MIM:604131]: A form of
CC thalassemia. Thalassemias are common monogenic diseases occurring
CC mostly in Mediterranean and Southeast Asian populations. The hallmark
CC of alpha-thalassemia is an imbalance in globin-chain production in the
CC adult HbA molecule. The level of alpha chain production can range from
CC none to very nearly normal levels. Deletion of both copies of each of
CC the two alpha-globin genes causes alpha(0)-thalassemia, also known as
CC homozygous alpha thalassemia. Due to the complete absence of alpha
CC chains, the predominant fetal hemoglobin is a tetramer of gamma-chains
CC (Bart hemoglobin) that has essentially no oxygen carrying capacity.
CC This causes oxygen starvation in the fetal tissues leading to prenatal
CC lethality or early neonatal death. The loss of two alpha genes results
CC in mild alpha-thalassemia, also known as heterozygous alpha-
CC thalassemia. Affected individuals have small red cells and a mild
CC anemia (microcytosis). If three of the four alpha-globin genes are
CC functional, individuals are completely asymptomatic. Some rare forms of
CC alpha-thalassemia are due to point mutations (non-deletional alpha-
CC thalassemia). Note=The disease is caused by variants affecting the gene
CC represented in this entry.
CC -!- DISEASE: Note=Alpha(0)-thalassemia is associated with non-immune
CC hydrops fetalis, a generalized edema of the fetus with fluid
CC accumulation in the body cavities due to non-immune causes. Non-immune
CC hydrops fetalis is not a diagnosis in itself but a symptom, a feature
CC of many genetic disorders, and the end-stage of a wide variety of
CC disorders.
CC -!- DISEASE: Hemoglobin H disease (HBH) [MIM:613978]: A form of alpha-
CC thalassemia due to the loss of three alpha genes. This results in high
CC levels of a tetramer of four beta chains (hemoglobin H), causing a
CC severe and life-threatening anemia. Untreated, most patients die in
CC childhood or early adolescence. {ECO:0000269|PubMed:10569720}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Gives blood its red color.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD97112.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=HbVar; Note=Human hemoglobin variants and
CC thalassemias;
CC URL="https://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBA1";
CC -!- WEB RESOURCE: Name=HbVar; Note=Human hemoglobin variants and
CC thalassemias;
CC URL="https://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBA2";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Hemoglobin entry;
CC URL="https://en.wikipedia.org/wiki/Hemoglobin";
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Journey into a tiny world
CC - Issue 84 of July 2007;
CC URL="https://web.expasy.org/spotlight/back_issues/084/";
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DR EMBL; J00153; AAB59407.1; -; Genomic_DNA.
DR EMBL; J00153; AAB59408.1; -; Genomic_DNA.
DR EMBL; V00491; CAA23750.1; -; Genomic_DNA.
DR EMBL; V00493; CAA23752.1; -; mRNA.
DR EMBL; V00488; CAA23748.1; -; Genomic_DNA.
DR EMBL; V00516; CAA23774.1; -; Genomic_DNA.
DR EMBL; AF230076; AAF72612.1; -; Genomic_DNA.
DR EMBL; AF525460; AAM83102.1; -; Genomic_DNA.
DR EMBL; DQ431198; ABD95910.1; -; Genomic_DNA.
DR EMBL; DQ431198; ABD95911.1; -; Genomic_DNA.
DR EMBL; AF097635; AAC72839.1; -; mRNA.
DR EMBL; AF105974; AAC97373.1; -; mRNA.
DR EMBL; AF349571; AAK37554.1; -; mRNA.
DR EMBL; AF536204; AAN04486.1; -; Genomic_DNA.
DR EMBL; DQ499017; ABF56144.1; -; Genomic_DNA.
DR EMBL; DQ499018; ABF56145.1; -; Genomic_DNA.
DR EMBL; AK223392; BAD97112.1; ALT_INIT; mRNA.
DR EMBL; AE006462; AAK61215.1; -; Genomic_DNA.
DR EMBL; AE006462; AAK61216.1; -; Genomic_DNA.
DR EMBL; Z84721; CAB06554.1; -; Genomic_DNA.
DR EMBL; Z84721; CAB06555.1; -; Genomic_DNA.
DR EMBL; BC005931; AAH05931.1; -; mRNA.
DR EMBL; BC008572; AAH08572.1; -; mRNA.
DR EMBL; BC032122; AAH32122.1; -; mRNA.
DR EMBL; BC050661; AAH50661.1; -; mRNA.
DR EMBL; BC101846; AAI01847.1; -; mRNA.
DR EMBL; BC101848; AAI01849.1; -; mRNA.
DR CCDS; CCDS10398.1; -.
DR CCDS; CCDS10399.1; -.
DR PIR; A90807; HAHU.
DR PIR; C93303; HACZP.
DR PIR; I58217; HACZ.
DR RefSeq; NP_000508.1; NM_000517.4.
DR RefSeq; NP_000549.1; NM_000558.4.
DR PDB; 1A00; X-ray; 2.00 A; A/C=2-142.
DR PDB; 1A01; X-ray; 1.80 A; A/C=2-142.
DR PDB; 1A0U; X-ray; 2.14 A; A/C=2-142.
DR PDB; 1A0Z; X-ray; 2.00 A; A/C=2-142.
DR PDB; 1A3N; X-ray; 1.80 A; A/C=2-142.
DR PDB; 1A3O; X-ray; 1.80 A; A/C=2-142.
DR PDB; 1A9W; X-ray; 2.90 A; A/C=2-142.
DR PDB; 1ABW; X-ray; 2.00 A; A=1-142.
DR PDB; 1ABY; X-ray; 2.60 A; A=1-142.
DR PDB; 1AJ9; X-ray; 2.20 A; A=2-142.
DR PDB; 1B86; X-ray; 2.50 A; A/C=2-142.
DR PDB; 1BAB; X-ray; 1.50 A; A/C=1-142.
DR PDB; 1BBB; X-ray; 1.70 A; A/C=2-142.
DR PDB; 1BIJ; X-ray; 2.30 A; A/C=2-142.
DR PDB; 1BUW; X-ray; 1.90 A; A/C=2-142.
DR PDB; 1BZ0; X-ray; 1.50 A; A/C=2-142.
DR PDB; 1BZ1; X-ray; 1.59 A; A/C=1-142.
DR PDB; 1BZZ; X-ray; 1.59 A; A/C=2-142.
DR PDB; 1C7B; X-ray; 1.80 A; A/C=2-142.
DR PDB; 1C7C; X-ray; 1.80 A; A=2-142.
DR PDB; 1C7D; X-ray; 1.80 A; A=2-142.
DR PDB; 1CLS; X-ray; 1.90 A; A/C=2-142.
DR PDB; 1CMY; X-ray; 3.00 A; A/C=2-142.
DR PDB; 1COH; X-ray; 2.90 A; A/C=2-142.
DR PDB; 1DKE; X-ray; 2.10 A; A/C=2-142.
DR PDB; 1DXT; X-ray; 1.70 A; A/C=2-142.
DR PDB; 1DXU; X-ray; 1.70 A; A/C=2-142.
DR PDB; 1DXV; X-ray; 1.70 A; A/C=2-142.
DR PDB; 1FDH; X-ray; 2.50 A; A/B=2-142.
DR PDB; 1FN3; X-ray; 2.48 A; A/C=2-142.
DR PDB; 1G9V; X-ray; 1.85 A; A/C=2-142.
DR PDB; 1GBU; X-ray; 1.80 A; A/C=2-142.
DR PDB; 1GBV; X-ray; 2.00 A; A/C=2-142.
DR PDB; 1GLI; X-ray; 2.50 A; A/C=3-142.
DR PDB; 1GZX; X-ray; 2.10 A; A/C=2-142.
DR PDB; 1HAB; X-ray; 2.30 A; A/C=2-142.
DR PDB; 1HAC; X-ray; 2.60 A; A/C=2-142.
DR PDB; 1HBA; X-ray; 2.10 A; A/C=2-142.
DR PDB; 1HBB; X-ray; 1.90 A; A/C=2-142.
DR PDB; 1HBS; X-ray; 3.00 A; A/C/E/G=2-142.
DR PDB; 1HCO; X-ray; 2.70 A; A=2-142.
DR PDB; 1HDB; X-ray; 2.20 A; A/C=2-142.
DR PDB; 1HGA; X-ray; 2.10 A; A/C=2-142.
DR PDB; 1HGB; X-ray; 2.10 A; A/C=2-142.
DR PDB; 1HGC; X-ray; 2.10 A; A/C=2-142.
DR PDB; 1HHO; X-ray; 2.10 A; A=2-142.
DR PDB; 1IRD; X-ray; 1.25 A; A=2-142.
DR PDB; 1J3Y; X-ray; 1.55 A; A/C/E/G=2-142.
DR PDB; 1J3Z; X-ray; 1.60 A; A/C/E/G=2-142.
DR PDB; 1J40; X-ray; 1.45 A; A/C/E/G=2-142.
DR PDB; 1J41; X-ray; 1.45 A; A/C/E/G=2-142.
DR PDB; 1J7S; X-ray; 2.20 A; A/C=2-142.
DR PDB; 1J7W; X-ray; 2.00 A; A/C=2-142.
DR PDB; 1J7Y; X-ray; 1.70 A; A/C=2-142.
DR PDB; 1JY7; X-ray; 3.20 A; A/C/P/R/U/W=2-142.
DR PDB; 1K0Y; X-ray; 1.87 A; A/C=2-142.
DR PDB; 1K1K; X-ray; 2.00 A; A=2-142.
DR PDB; 1KD2; X-ray; 1.87 A; A/C=2-142.
DR PDB; 1LFL; X-ray; 2.70 A; A/C/P/R=2-142.
DR PDB; 1LFQ; X-ray; 2.60 A; A=2-142.
DR PDB; 1LFT; X-ray; 2.60 A; A=2-142.
DR PDB; 1LFV; X-ray; 2.80 A; A=2-142.
DR PDB; 1LFY; X-ray; 3.30 A; A=2-142.
DR PDB; 1LFZ; X-ray; 3.10 A; A=2-142.
DR PDB; 1LJW; X-ray; 2.16 A; A=2-142.
DR PDB; 1M9P; X-ray; 2.10 A; A/C=2-142.
DR PDB; 1MKO; X-ray; 2.18 A; A/C=2-142.
DR PDB; 1NEJ; X-ray; 2.10 A; A/C=2-142.
DR PDB; 1NIH; X-ray; 2.60 A; A/C=2-142.
DR PDB; 1NQP; X-ray; 1.73 A; A/C=2-142.
DR PDB; 1O1I; X-ray; 2.30 A; A=2-142.
DR PDB; 1O1J; X-ray; 1.90 A; A=2-142.
DR PDB; 1O1K; X-ray; 2.00 A; A/C=3-142.
DR PDB; 1O1L; X-ray; 1.80 A; A=2-142.
DR PDB; 1O1M; X-ray; 1.85 A; A=2-142.
DR PDB; 1O1N; X-ray; 1.80 A; A=2-142.
DR PDB; 1O1O; X-ray; 1.80 A; A/C=2-142.
DR PDB; 1O1P; X-ray; 1.80 A; A=2-142.
DR PDB; 1QI8; X-ray; 1.80 A; A/C=3-142.
DR PDB; 1QSH; X-ray; 1.70 A; A/C=2-142.
DR PDB; 1QSI; X-ray; 1.70 A; A/C=2-142.
DR PDB; 1QXD; X-ray; 2.25 A; A/C=2-142.
DR PDB; 1QXE; X-ray; 1.85 A; A/C=2-142.
DR PDB; 1R1X; X-ray; 2.15 A; A=2-142.
DR PDB; 1R1Y; X-ray; 1.80 A; A/C=2-142.
DR PDB; 1RPS; X-ray; 2.11 A; A/C=2-142.
DR PDB; 1RQ3; X-ray; 1.91 A; A/C=2-142.
DR PDB; 1RQ4; X-ray; 2.11 A; A/C=2-142.
DR PDB; 1RQA; X-ray; 2.11 A; A/C=2-142.
DR PDB; 1RVW; X-ray; 2.50 A; A=2-142.
DR PDB; 1SDK; X-ray; 1.80 A; A/C=2-142.
DR PDB; 1SDL; X-ray; 1.80 A; A/C=2-142.
DR PDB; 1SHR; X-ray; 1.88 A; A/C=2-142.
DR PDB; 1SI4; X-ray; 2.20 A; A/C=2-142.
DR PDB; 1THB; X-ray; 1.50 A; A/C=2-142.
DR PDB; 1UIW; X-ray; 1.50 A; A/C/E/G=2-142.
DR PDB; 1VWT; X-ray; 1.90 A; A/C=2-142.
DR PDB; 1XXT; X-ray; 1.91 A; A/C=2-142.
DR PDB; 1XY0; X-ray; 1.99 A; A/C=2-142.
DR PDB; 1XYE; X-ray; 2.13 A; A/C=3-142.
DR PDB; 1XZ2; X-ray; 1.90 A; A/C=2-142.
DR PDB; 1XZ4; X-ray; 2.00 A; A/C=3-142.
DR PDB; 1XZ5; X-ray; 2.11 A; A/C=2-142.
DR PDB; 1XZ7; X-ray; 1.90 A; A/C=2-142.
DR PDB; 1XZU; X-ray; 2.16 A; A/C=2-142.
DR PDB; 1XZV; X-ray; 2.11 A; A/C=2-142.
DR PDB; 1Y01; X-ray; 2.80 A; B=1-142.
DR PDB; 1Y09; X-ray; 2.25 A; A/C=2-142.
DR PDB; 1Y0A; X-ray; 2.22 A; A/C=2-140.
DR PDB; 1Y0C; X-ray; 2.30 A; A/C=2-140.
DR PDB; 1Y0D; X-ray; 2.10 A; A/C=2-141.
DR PDB; 1Y0T; X-ray; 2.14 A; A/C=2-142.
DR PDB; 1Y0W; X-ray; 2.14 A; A/C=2-142.
DR PDB; 1Y22; X-ray; 2.16 A; A/C=2-142.
DR PDB; 1Y2Z; X-ray; 2.07 A; A/C=2-142.
DR PDB; 1Y31; X-ray; 2.13 A; A/C=2-142.
DR PDB; 1Y35; X-ray; 2.12 A; A/C=2-142.
DR PDB; 1Y45; X-ray; 2.00 A; A/C=2-142.
DR PDB; 1Y46; X-ray; 2.22 A; A/C=2-142.
DR PDB; 1Y4B; X-ray; 2.10 A; A/C=2-142.
DR PDB; 1Y4F; X-ray; 2.00 A; A/C=2-142.
DR PDB; 1Y4G; X-ray; 1.91 A; A/C=2-142.
DR PDB; 1Y4P; X-ray; 1.98 A; A/C=2-142.
DR PDB; 1Y4Q; X-ray; 2.11 A; A/C=2-142.
DR PDB; 1Y4R; X-ray; 2.22 A; A/C=2-142.
DR PDB; 1Y4V; X-ray; 1.84 A; A/C=2-142.
DR PDB; 1Y5F; X-ray; 2.14 A; A/C=2-142.
DR PDB; 1Y5J; X-ray; 2.03 A; A/C=2-142.
DR PDB; 1Y5K; X-ray; 2.20 A; A/C=2-142.
DR PDB; 1Y7C; X-ray; 2.10 A; A/C=2-142.
DR PDB; 1Y7D; X-ray; 1.90 A; A/C=2-142.
DR PDB; 1Y7G; X-ray; 2.10 A; A/C=2-142.
DR PDB; 1Y7Z; X-ray; 1.98 A; A/C=2-142.
DR PDB; 1Y83; X-ray; 1.90 A; A/C=2-142.
DR PDB; 1Y85; X-ray; 2.13 A; A/C=2-142.
DR PDB; 1Y8W; X-ray; 2.90 A; A/C=2-142.
DR PDB; 1YDZ; X-ray; 3.30 A; A/C=2-140.
DR PDB; 1YE0; X-ray; 2.50 A; A/C=2-142.
DR PDB; 1YE1; X-ray; 4.50 A; A/C=2-142.
DR PDB; 1YE2; X-ray; 1.80 A; A/C=2-142.
DR PDB; 1YEN; X-ray; 2.80 A; A/C=2-142.
DR PDB; 1YEO; X-ray; 2.22 A; A/C=2-142.
DR PDB; 1YEQ; X-ray; 2.75 A; A/C=2-142.
DR PDB; 1YEU; X-ray; 2.12 A; A/C=2-142.
DR PDB; 1YEV; X-ray; 2.11 A; A/C=2-142.
DR PDB; 1YFF; X-ray; 2.40 A; A/C/E/G=2-142.
DR PDB; 1YG5; X-ray; 2.70 A; A/C=2-142.
DR PDB; 1YGD; X-ray; 2.73 A; A/C=2-142.
DR PDB; 1YGF; X-ray; 2.70 A; A/C=2-142.
DR PDB; 1YH9; X-ray; 2.20 A; A/C=2-142.
DR PDB; 1YHE; X-ray; 2.10 A; A/C=2-142.
DR PDB; 1YHR; X-ray; 2.60 A; A/C=2-142.
DR PDB; 1YIE; X-ray; 2.40 A; A/C=2-142.
DR PDB; 1YIH; X-ray; 2.00 A; A/C=2-142.
DR PDB; 1YVQ; X-ray; 1.80 A; A/C=2-142.
DR PDB; 1YVT; X-ray; 1.80 A; A=2-142.
DR PDB; 1YZI; X-ray; 2.07 A; A=2-142.
DR PDB; 1Z8U; X-ray; 2.40 A; B/D=1-142.
DR PDB; 2D5Z; X-ray; 1.45 A; A/C=2-142.
DR PDB; 2D60; X-ray; 1.70 A; A/C=2-142.
DR PDB; 2DN1; X-ray; 1.25 A; A=2-142.
DR PDB; 2DN2; X-ray; 1.25 A; A/C=2-142.
DR PDB; 2DN3; X-ray; 1.25 A; A=2-142.
DR PDB; 2DXM; Neutron; 2.10 A; A/C=2-142.
DR PDB; 2H35; NMR; -; A/C=2-142.
DR PDB; 2HBC; X-ray; 2.10 A; A=2-142.
DR PDB; 2HBD; X-ray; 2.20 A; A=2-142.
DR PDB; 2HBE; X-ray; 2.00 A; A=2-142.
DR PDB; 2HBF; X-ray; 2.20 A; A=2-142.
DR PDB; 2HBS; X-ray; 2.05 A; A/C/E/G=2-142.
DR PDB; 2HCO; X-ray; 2.70 A; A=2-142.
DR PDB; 2HHB; X-ray; 1.74 A; A/C=2-142.
DR PDB; 2HHD; X-ray; 2.20 A; A/C=2-142.
DR PDB; 2HHE; X-ray; 2.20 A; A/C=2-142.
DR PDB; 2M6Z; NMR; -; A/C=2-142.
DR PDB; 2W6V; X-ray; 1.80 A; A/C=2-142.
DR PDB; 2W72; X-ray; 1.07 A; A=2-142, C=3-142.
DR PDB; 2YRS; X-ray; 2.30 A; A/C/I/M=2-142.
DR PDB; 3B75; X-ray; 2.30 A; A/C/E/G/S=2-142.
DR PDB; 3D17; X-ray; 2.80 A; A/C=2-142.
DR PDB; 3D7O; X-ray; 1.80 A; A=2-142.
DR PDB; 3DUT; X-ray; 1.55 A; A/C=2-142.
DR PDB; 3HHB; X-ray; 1.74 A; A/C=2-142.
DR PDB; 3HXN; X-ray; 2.00 A; A/C=2-142.
DR PDB; 3IA3; X-ray; 3.20 A; B/D=1-142.
DR PDB; 3IC0; X-ray; 1.80 A; A/C=2-142.
DR PDB; 3IC2; X-ray; 2.40 A; A/C=2-142.
DR PDB; 3KMF; Neutron; 2.00 A; A/E=2-142.
DR PDB; 3NL7; X-ray; 1.80 A; A=2-142.
DR PDB; 3NMM; X-ray; 1.60 A; A/C=2-142.
DR PDB; 3ODQ; X-ray; 3.10 A; A/C=2-142.
DR PDB; 3ONZ; X-ray; 2.09 A; A=2-142.
DR PDB; 3OO4; X-ray; 1.90 A; A=2-142.
DR PDB; 3OO5; X-ray; 2.10 A; A=2-142.
DR PDB; 3OVU; X-ray; 2.83 A; C=2-142.
DR PDB; 3P5Q; X-ray; 2.00 A; A=2-142.
DR PDB; 3QJB; X-ray; 1.80 A; A=2-142.
DR PDB; 3QJC; X-ray; 2.00 A; A=2-142.
DR PDB; 3QJD; X-ray; 1.56 A; A/C=2-142.
DR PDB; 3QJE; X-ray; 1.80 A; A/C=2-142.
DR PDB; 3R5I; X-ray; 2.20 A; A/C=2-142.
DR PDB; 3S48; X-ray; 3.05 A; C/D=2-142.
DR PDB; 3S65; X-ray; 1.80 A; A/C=2-142.
DR PDB; 3S66; X-ray; 1.40 A; A=2-142.
DR PDB; 3SZK; X-ray; 3.01 A; A/D=2-142.
DR PDB; 3WCP; X-ray; 1.94 A; A/C=2-142.
DR PDB; 3WHM; X-ray; 1.85 A; A/E=2-142.
DR PDB; 4FC3; X-ray; 2.26 A; A=2-142.
DR PDB; 4HHB; X-ray; 1.74 A; A/C=2-142.
DR PDB; 4IJ2; X-ray; 4.24 A; A/C=2-142.
DR PDB; 4L7Y; X-ray; 1.80 A; A/C=2-142.
DR PDB; 4M4A; X-ray; 2.05 A; A=2-142.
DR PDB; 4M4B; X-ray; 2.00 A; A=2-142.
DR PDB; 4MQC; X-ray; 2.20 A; A=2-142.
DR PDB; 4MQG; X-ray; 1.68 A; A=2-142.
DR PDB; 4MQH; X-ray; 2.50 A; A=2-140.
DR PDB; 4MQI; X-ray; 1.92 A; A=2-141.
DR PDB; 4MQJ; X-ray; 1.80 A; A/C/E/G=2-142.
DR PDB; 4MQK; X-ray; 2.24 A; A/C/E/G=2-142.
DR PDB; 4N7N; X-ray; 2.75 A; A/C/E/G/I/K=2-142.
DR PDB; 4N7O; X-ray; 2.50 A; A/C/E/G/I/K=2-142.
DR PDB; 4N7P; X-ray; 2.81 A; A/C/E/G/I/K=2-142.
DR PDB; 4N8T; X-ray; 1.90 A; A=2-142.
DR PDB; 4NI0; X-ray; 2.15 A; A=2-142.
DR PDB; 4NI1; X-ray; 1.90 A; A=2-142.
DR PDB; 4ROL; X-ray; 1.70 A; A/C=2-142.
DR PDB; 4ROM; X-ray; 1.90 A; A/C=2-142.
DR PDB; 4WJG; X-ray; 3.10 A; A/F/K/P/U/Z=2-142.
DR PDB; 4X0L; X-ray; 2.05 A; A=2-142.
DR PDB; 4XS0; X-ray; 2.55 A; A=2-142.
DR PDB; 5E29; X-ray; 1.85 A; A/C=2-142.
DR PDB; 5E6E; X-ray; 1.76 A; A=2-142.
DR PDB; 5E83; X-ray; 1.80 A; A/C=2-142.
DR PDB; 5EE4; X-ray; 2.30 A; C/E=2-142.
DR PDB; 5HU6; X-ray; 2.90 A; A=2-142.
DR PDB; 5HY8; X-ray; 2.30 A; A/C/E/G/S=2-142.
DR PDB; 5JDO; X-ray; 3.20 A; C=2-142, E=2-141.
DR PDB; 5KDQ; X-ray; 2.15 A; A/C=3-142.
DR PDB; 5KSI; X-ray; 1.80 A; A/C=2-142.
DR PDB; 5KSJ; X-ray; 2.40 A; A/C=2-142.
DR PDB; 5NI1; EM; 3.20 A; A/C=2-142.
DR PDB; 5SW7; X-ray; 1.85 A; A=2-142.
DR PDB; 5U3I; X-ray; 1.95 A; A/C=2-142.
DR PDB; 5UCU; X-ray; 1.80 A; A=2-142.
DR PDB; 5UFJ; X-ray; 2.05 A; A/C=2-142.
DR PDB; 5URC; X-ray; 1.85 A; A/C=2-142.
DR PDB; 5VMM; X-ray; 3.60 A; A/C=2-142.
DR PDB; 5WOG; X-ray; 1.54 A; A/B=3-139.
DR PDB; 5WOH; X-ray; 1.58 A; A/C=3-139.
DR PDB; 5X2R; X-ray; 2.70 A; A/C/E/G/I/K=2-142.
DR PDB; 5X2S; X-ray; 2.39 A; A/C/E/G/I/K=2-142.
DR PDB; 5X2T; X-ray; 2.64 A; A/C/E/G/I/K=2-142.
DR PDB; 5X2U; X-ray; 2.53 A; A/C/E/G/I/K=2-142.
DR PDB; 6BB5; X-ray; 2.28 A; A=3-141.
DR PDB; 6BNR; X-ray; 1.95 A; A/C=2-142.
DR PDB; 6BWP; X-ray; 1.70 A; A/C=2-142.
DR PDB; 6BWU; X-ray; 2.00 A; A=2-142.
DR PDB; 6DI4; X-ray; 1.90 A; A/C=2-142.
DR PDB; 6HAL; X-ray; 2.20 A; A/C=3-141.
DR PDB; 6HBW; X-ray; 2.00 A; A/C=2-142.
DR PDB; 6HK2; X-ray; 1.55 A; A/C=2-142.
DR PDB; 6KA9; X-ray; 1.40 A; A/C/E/G=2-142.
DR PDB; 6KAE; X-ray; 1.45 A; A/C/E/G=2-142.
DR PDB; 6KAH; X-ray; 1.45 A; A/C/E/G=2-142.
DR PDB; 6KAI; X-ray; 1.45 A; A/C/E/G=2-142.
DR PDB; 6KAO; X-ray; 1.40 A; A=2-142.
DR PDB; 6KAP; X-ray; 1.45 A; A=2-142.
DR PDB; 6KAQ; X-ray; 1.50 A; A=2-142.
DR PDB; 6KAR; X-ray; 1.60 A; A=2-142.
DR PDB; 6KAS; X-ray; 1.65 A; A/C=2-142.
DR PDB; 6KAT; X-ray; 1.70 A; A/C=2-142.
DR PDB; 6KAU; X-ray; 1.60 A; A/C=2-142.
DR PDB; 6KAV; X-ray; 1.70 A; A/C=2-142.
DR PDB; 6KYE; X-ray; 2.28 A; A/C/E/G/I/K=1-142.
DR PDB; 6L5V; X-ray; 1.45 A; A=2-142.
DR PDB; 6L5W; X-ray; 1.50 A; A=2-142.
DR PDB; 6L5X; X-ray; 1.65 A; A/C=2-142.
DR PDB; 6L5Y; X-ray; 1.65 A; A/C=2-142.
DR PDB; 6LCW; X-ray; 1.40 A; A/C/E/G=2-142.
DR PDB; 6LCX; X-ray; 1.40 A; A/C/E/G=2-142.
DR PDB; 6NBC; EM; 2.80 A; A/C=2-141.
DR PDB; 6NBD; EM; 3.20 A; A/C=2-141.
DR PDB; 6NQ5; X-ray; 1.85 A; A=2-142.
DR PDB; 6TB2; X-ray; 2.90 A; A=2-142.
DR PDB; 6XD9; X-ray; 2.10 A; A/C=2-142.
DR PDB; 6XDT; X-ray; 1.90 A; A/C=2-142.
DR PDB; 6XE7; X-ray; 2.00 A; A/C=2-142.
DR PDB; 7AET; X-ray; 2.53 A; AAA/CCC=3-141.
DR PDB; 7AEU; X-ray; 2.54 A; AAA/CCC=3-141.
DR PDB; 7AEV; X-ray; 2.77 A; AAA/CCC=3-141.
DR PDB; 7CUE; X-ray; 2.75 A; A/C=1-142.
DR PDB; 7DY3; X-ray; 1.40 A; A/C/E/G=2-142.
DR PDB; 7DY4; X-ray; 1.30 A; A/C/E/G=2-142.
DR PDB; 7JJQ; X-ray; 2.15 A; A/C=2-142.
DR PDB; 7JXZ; X-ray; 2.23 A; A/C=2-142.
DR PDB; 7JY0; X-ray; 1.63 A; A/C=2-142.
DR PDB; 7JY1; X-ray; 1.59 A; A/C=2-142.
DR PDB; 7JY3; X-ray; 1.48 A; A/C=2-142.
DR PDB; 7K4M; X-ray; 2.50 A; A/C/E/G/I=1-142.
DR PDB; 7PCF; EM; 5.82 A; A=2-142.
DR PDB; 7PCH; EM; 2.89 A; A/C=2-142.
DR PDB; 7PCQ; EM; 3.62 A; A/C=2-142.
DR PDB; 7UD7; X-ray; 1.80 A; A/C=1-142.
DR PDB; 7UD8; X-ray; 1.80 A; A/C=1-142.
DR PDB; 7UF6; X-ray; 2.00 A; A/C=1-142.
DR PDB; 7UF7; X-ray; 2.00 A; A/C=1-142.
DR PDB; 7VDE; EM; 3.20 A; A/C=1-142.
DR PDBsum; 1A00; -.
DR PDBsum; 1A01; -.
DR PDBsum; 1A0U; -.
DR PDBsum; 1A0Z; -.
DR PDBsum; 1A3N; -.
DR PDBsum; 1A3O; -.
DR PDBsum; 1A9W; -.
DR PDBsum; 1ABW; -.
DR PDBsum; 1ABY; -.
DR PDBsum; 1AJ9; -.
DR PDBsum; 1B86; -.
DR PDBsum; 1BAB; -.
DR PDBsum; 1BBB; -.
DR PDBsum; 1BIJ; -.
DR PDBsum; 1BUW; -.
DR PDBsum; 1BZ0; -.
DR PDBsum; 1BZ1; -.
DR PDBsum; 1BZZ; -.
DR PDBsum; 1C7B; -.
DR PDBsum; 1C7C; -.
DR PDBsum; 1C7D; -.
DR PDBsum; 1CLS; -.
DR PDBsum; 1CMY; -.
DR PDBsum; 1COH; -.
DR PDBsum; 1DKE; -.
DR PDBsum; 1DXT; -.
DR PDBsum; 1DXU; -.
DR PDBsum; 1DXV; -.
DR PDBsum; 1FDH; -.
DR PDBsum; 1FN3; -.
DR PDBsum; 1G9V; -.
DR PDBsum; 1GBU; -.
DR PDBsum; 1GBV; -.
DR PDBsum; 1GLI; -.
DR PDBsum; 1GZX; -.
DR PDBsum; 1HAB; -.
DR PDBsum; 1HAC; -.
DR PDBsum; 1HBA; -.
DR PDBsum; 1HBB; -.
DR PDBsum; 1HBS; -.
DR PDBsum; 1HCO; -.
DR PDBsum; 1HDB; -.
DR PDBsum; 1HGA; -.
DR PDBsum; 1HGB; -.
DR PDBsum; 1HGC; -.
DR PDBsum; 1HHO; -.
DR PDBsum; 1IRD; -.
DR PDBsum; 1J3Y; -.
DR PDBsum; 1J3Z; -.
DR PDBsum; 1J40; -.
DR PDBsum; 1J41; -.
DR PDBsum; 1J7S; -.
DR PDBsum; 1J7W; -.
DR PDBsum; 1J7Y; -.
DR PDBsum; 1JY7; -.
DR PDBsum; 1K0Y; -.
DR PDBsum; 1K1K; -.
DR PDBsum; 1KD2; -.
DR PDBsum; 1LFL; -.
DR PDBsum; 1LFQ; -.
DR PDBsum; 1LFT; -.
DR PDBsum; 1LFV; -.
DR PDBsum; 1LFY; -.
DR PDBsum; 1LFZ; -.
DR PDBsum; 1LJW; -.
DR PDBsum; 1M9P; -.
DR PDBsum; 1MKO; -.
DR PDBsum; 1NEJ; -.
DR PDBsum; 1NIH; -.
DR PDBsum; 1NQP; -.
DR PDBsum; 1O1I; -.
DR PDBsum; 1O1J; -.
DR PDBsum; 1O1K; -.
DR PDBsum; 1O1L; -.
DR PDBsum; 1O1M; -.
DR PDBsum; 1O1N; -.
DR PDBsum; 1O1O; -.
DR PDBsum; 1O1P; -.
DR PDBsum; 1QI8; -.
DR PDBsum; 1QSH; -.
DR PDBsum; 1QSI; -.
DR PDBsum; 1QXD; -.
DR PDBsum; 1QXE; -.
DR PDBsum; 1R1X; -.
DR PDBsum; 1R1Y; -.
DR PDBsum; 1RPS; -.
DR PDBsum; 1RQ3; -.
DR PDBsum; 1RQ4; -.
DR PDBsum; 1RQA; -.
DR PDBsum; 1RVW; -.
DR PDBsum; 1SDK; -.
DR PDBsum; 1SDL; -.
DR PDBsum; 1SHR; -.
DR PDBsum; 1SI4; -.
DR PDBsum; 1THB; -.
DR PDBsum; 1UIW; -.
DR PDBsum; 1VWT; -.
DR PDBsum; 1XXT; -.
DR PDBsum; 1XY0; -.
DR PDBsum; 1XYE; -.
DR PDBsum; 1XZ2; -.
DR PDBsum; 1XZ4; -.
DR PDBsum; 1XZ5; -.
DR PDBsum; 1XZ7; -.
DR PDBsum; 1XZU; -.
DR PDBsum; 1XZV; -.
DR PDBsum; 1Y01; -.
DR PDBsum; 1Y09; -.
DR PDBsum; 1Y0A; -.
DR PDBsum; 1Y0C; -.
DR PDBsum; 1Y0D; -.
DR PDBsum; 1Y0T; -.
DR PDBsum; 1Y0W; -.
DR PDBsum; 1Y22; -.
DR PDBsum; 1Y2Z; -.
DR PDBsum; 1Y31; -.
DR PDBsum; 1Y35; -.
DR PDBsum; 1Y45; -.
DR PDBsum; 1Y46; -.
DR PDBsum; 1Y4B; -.
DR PDBsum; 1Y4F; -.
DR PDBsum; 1Y4G; -.
DR PDBsum; 1Y4P; -.
DR PDBsum; 1Y4Q; -.
DR PDBsum; 1Y4R; -.
DR PDBsum; 1Y4V; -.
DR PDBsum; 1Y5F; -.
DR PDBsum; 1Y5J; -.
DR PDBsum; 1Y5K; -.
DR PDBsum; 1Y7C; -.
DR PDBsum; 1Y7D; -.
DR PDBsum; 1Y7G; -.
DR PDBsum; 1Y7Z; -.
DR PDBsum; 1Y83; -.
DR PDBsum; 1Y85; -.
DR PDBsum; 1Y8W; -.
DR PDBsum; 1YDZ; -.
DR PDBsum; 1YE0; -.
DR PDBsum; 1YE1; -.
DR PDBsum; 1YE2; -.
DR PDBsum; 1YEN; -.
DR PDBsum; 1YEO; -.
DR PDBsum; 1YEQ; -.
DR PDBsum; 1YEU; -.
DR PDBsum; 1YEV; -.
DR PDBsum; 1YFF; -.
DR PDBsum; 1YG5; -.
DR PDBsum; 1YGD; -.
DR PDBsum; 1YGF; -.
DR PDBsum; 1YH9; -.
DR PDBsum; 1YHE; -.
DR PDBsum; 1YHR; -.
DR PDBsum; 1YIE; -.
DR PDBsum; 1YIH; -.
DR PDBsum; 1YVQ; -.
DR PDBsum; 1YVT; -.
DR PDBsum; 1YZI; -.
DR PDBsum; 1Z8U; -.
DR PDBsum; 2D5Z; -.
DR PDBsum; 2D60; -.
DR PDBsum; 2DN1; -.
DR PDBsum; 2DN2; -.
DR PDBsum; 2DN3; -.
DR PDBsum; 2DXM; -.
DR PDBsum; 2H35; -.
DR PDBsum; 2HBC; -.
DR PDBsum; 2HBD; -.
DR PDBsum; 2HBE; -.
DR PDBsum; 2HBF; -.
DR PDBsum; 2HBS; -.
DR PDBsum; 2HCO; -.
DR PDBsum; 2HHB; -.
DR PDBsum; 2HHD; -.
DR PDBsum; 2HHE; -.
DR PDBsum; 2M6Z; -.
DR PDBsum; 2W6V; -.
DR PDBsum; 2W72; -.
DR PDBsum; 2YRS; -.
DR PDBsum; 3B75; -.
DR PDBsum; 3D17; -.
DR PDBsum; 3D7O; -.
DR PDBsum; 3DUT; -.
DR PDBsum; 3HHB; -.
DR PDBsum; 3HXN; -.
DR PDBsum; 3IA3; -.
DR PDBsum; 3IC0; -.
DR PDBsum; 3IC2; -.
DR PDBsum; 3KMF; -.
DR PDBsum; 3NL7; -.
DR PDBsum; 3NMM; -.
DR PDBsum; 3ODQ; -.
DR PDBsum; 3ONZ; -.
DR PDBsum; 3OO4; -.
DR PDBsum; 3OO5; -.
DR PDBsum; 3OVU; -.
DR PDBsum; 3P5Q; -.
DR PDBsum; 3QJB; -.
DR PDBsum; 3QJC; -.
DR PDBsum; 3QJD; -.
DR PDBsum; 3QJE; -.
DR PDBsum; 3R5I; -.
DR PDBsum; 3S48; -.
DR PDBsum; 3S65; -.
DR PDBsum; 3S66; -.
DR PDBsum; 3SZK; -.
DR PDBsum; 3WCP; -.
DR PDBsum; 3WHM; -.
DR PDBsum; 4FC3; -.
DR PDBsum; 4HHB; -.
DR PDBsum; 4IJ2; -.
DR PDBsum; 4L7Y; -.
DR PDBsum; 4M4A; -.
DR PDBsum; 4M4B; -.
DR PDBsum; 4MQC; -.
DR PDBsum; 4MQG; -.
DR PDBsum; 4MQH; -.
DR PDBsum; 4MQI; -.
DR PDBsum; 4MQJ; -.
DR PDBsum; 4MQK; -.
DR PDBsum; 4N7N; -.
DR PDBsum; 4N7O; -.
DR PDBsum; 4N7P; -.
DR PDBsum; 4N8T; -.
DR PDBsum; 4NI0; -.
DR PDBsum; 4NI1; -.
DR PDBsum; 4ROL; -.
DR PDBsum; 4ROM; -.
DR PDBsum; 4WJG; -.
DR PDBsum; 4X0L; -.
DR PDBsum; 4XS0; -.
DR PDBsum; 5E29; -.
DR PDBsum; 5E6E; -.
DR PDBsum; 5E83; -.
DR PDBsum; 5EE4; -.
DR PDBsum; 5HU6; -.
DR PDBsum; 5HY8; -.
DR PDBsum; 5JDO; -.
DR PDBsum; 5KDQ; -.
DR PDBsum; 5KSI; -.
DR PDBsum; 5KSJ; -.
DR PDBsum; 5NI1; -.
DR PDBsum; 5SW7; -.
DR PDBsum; 5U3I; -.
DR PDBsum; 5UCU; -.
DR PDBsum; 5UFJ; -.
DR PDBsum; 5URC; -.
DR PDBsum; 5VMM; -.
DR PDBsum; 5WOG; -.
DR PDBsum; 5WOH; -.
DR PDBsum; 5X2R; -.
DR PDBsum; 5X2S; -.
DR PDBsum; 5X2T; -.
DR PDBsum; 5X2U; -.
DR PDBsum; 6BB5; -.
DR PDBsum; 6BNR; -.
DR PDBsum; 6BWP; -.
DR PDBsum; 6BWU; -.
DR PDBsum; 6DI4; -.
DR PDBsum; 6HAL; -.
DR PDBsum; 6HBW; -.
DR PDBsum; 6HK2; -.
DR PDBsum; 6KA9; -.
DR PDBsum; 6KAE; -.
DR PDBsum; 6KAH; -.
DR PDBsum; 6KAI; -.
DR PDBsum; 6KAO; -.
DR PDBsum; 6KAP; -.
DR PDBsum; 6KAQ; -.
DR PDBsum; 6KAR; -.
DR PDBsum; 6KAS; -.
DR PDBsum; 6KAT; -.
DR PDBsum; 6KAU; -.
DR PDBsum; 6KAV; -.
DR PDBsum; 6KYE; -.
DR PDBsum; 6L5V; -.
DR PDBsum; 6L5W; -.
DR PDBsum; 6L5X; -.
DR PDBsum; 6L5Y; -.
DR PDBsum; 6LCW; -.
DR PDBsum; 6LCX; -.
DR PDBsum; 6NBC; -.
DR PDBsum; 6NBD; -.
DR PDBsum; 6NQ5; -.
DR PDBsum; 6TB2; -.
DR PDBsum; 6XD9; -.
DR PDBsum; 6XDT; -.
DR PDBsum; 6XE7; -.
DR PDBsum; 7AET; -.
DR PDBsum; 7AEU; -.
DR PDBsum; 7AEV; -.
DR PDBsum; 7CUE; -.
DR PDBsum; 7DY3; -.
DR PDBsum; 7DY4; -.
DR PDBsum; 7JJQ; -.
DR PDBsum; 7JXZ; -.
DR PDBsum; 7JY0; -.
DR PDBsum; 7JY1; -.
DR PDBsum; 7JY3; -.
DR PDBsum; 7K4M; -.
DR PDBsum; 7PCF; -.
DR PDBsum; 7PCH; -.
DR PDBsum; 7PCQ; -.
DR PDBsum; 7UD7; -.
DR PDBsum; 7UD8; -.
DR PDBsum; 7UF6; -.
DR PDBsum; 7UF7; -.
DR PDBsum; 7VDE; -.
DR AlphaFoldDB; P69905; -.
DR SMR; P69905; -.
DR BioGRID; 109289; 46.
DR BioGRID; 109290; 131.
DR ComplexPortal; CPX-2158; Hemoglobin HbA complex.
DR ComplexPortal; CPX-2419; Hemoglobin HbA2 complex.
DR ComplexPortal; CPX-2927; Hemoglobin E complex.
DR ComplexPortal; CPX-2932; Hemoglobin HbF Variant 1 complex.
DR ComplexPortal; CPX-2933; Hemoglobin HbF Variant 2 complex.
DR DIP; DIP-35199N; -.
DR IntAct; P69905; 64.
DR MINT; P69905; -.
DR STRING; 9606.ENSP00000251595; -.
DR ChEMBL; CHEMBL2887; -.
DR DrugBank; DB08262; 2,6-dicarboxynaphthalene.
DR DrugBank; DB07427; 2-[(2-methoxy-5-methylphenoxy)methyl]pyridine.
DR DrugBank; DB08077; 2-[4-({[(3,5-DICHLOROPHENYL)AMINO]CARBONYL}AMINO)PHENOXY]-2-METHYLPROPANOIC ACID.
DR DrugBank; DB07428; 4-[(5-methoxy-2-methylphenoxy)methyl]pyridine.
DR DrugBank; DB02126; 4-Carboxycinnamic Acid.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB08486; Efaproxiral.
DR DrugBank; DB15617; Ferric derisomaltose.
DR DrugBank; DB09147; Ferric pyrophosphate.
DR DrugBank; DB13995; Ferric pyrophosphate citrate.
DR DrugBank; DB14490; Ferrous ascorbate.
DR DrugBank; DB14491; Ferrous fumarate.
DR DrugBank; DB14488; Ferrous gluconate.
DR DrugBank; DB14501; Ferrous glycine sulfate.
DR DrugBank; DB14489; Ferrous succinate.
DR DrugBank; DB13257; Ferrous sulfate anhydrous.
DR DrugBank; DB01592; Iron.
DR DrugBank; DB00893; Iron Dextran.
DR DrugBank; DB09112; Nitrous acid.
DR DrugBank; DB09140; Oxygen.
DR DrugBank; DB06154; Pentaerythritol tetranitrate.
DR DrugBank; DB07645; Sebacic acid.
DR DrugBank; DB09517; Sodium ferric gluconate complex.
DR DrugBank; DB08632; Trimesic acid.
DR DrugBank; DB14975; Voxelotor.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR DrugCentral; P69905; -.
DR TCDB; 1.A.107.1.1; the pore-forming globin (globin) family.
DR CarbonylDB; P69905; -.
DR GlyConnect; 2851; 1 O-Linked glycan (3 sites).
DR GlyGen; P69905; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P69905; -.
DR PhosphoSitePlus; P69905; -.
DR BioMuta; HBA1; -.
DR DMDM; 57013850; -.
DR DOSAC-COBS-2DPAGE; P69905; -.
DR REPRODUCTION-2DPAGE; IPI00410714; -.
DR SWISS-2DPAGE; P69905; -.
DR UCD-2DPAGE; P69905; -.
DR CPTAC; non-CPTAC-1129; -.
DR CPTAC; non-CPTAC-1130; -.
DR EPD; P69905; -.
DR jPOST; P69905; -.
DR MassIVE; P69905; -.
DR MaxQB; P69905; -.
DR PaxDb; P69905; -.
DR PeptideAtlas; P69905; -.
DR PRIDE; P69905; -.
DR ProteomicsDB; 57547; -.
DR TopDownProteomics; P69905; -.
DR ABCD; P69905; 2 sequenced antibodies.
DR Antibodypedia; 65596; 231 antibodies from 18 providers.
DR Antibodypedia; 8893; 213 antibodies from 29 providers.
DR DNASU; 3039; -.
DR Ensembl; ENST00000251595.11; ENSP00000251595.6; ENSG00000188536.13.
DR Ensembl; ENST00000320868.9; ENSP00000322421.5; ENSG00000206172.8.
DR GeneID; 3039; -.
DR GeneID; 3040; -.
DR KEGG; hsa:3039; -.
DR KEGG; hsa:3040; -.
DR MANE-Select; ENST00000251595.11; ENSP00000251595.6; NM_000517.6; NP_000508.1.
DR MANE-Select; ENST00000320868.9; ENSP00000322421.5; NM_000558.5; NP_000549.1.
DR UCSC; uc002cfv.4; human.
DR CTD; 3039; -.
DR CTD; 3040; -.
DR DisGeNET; 3039; -.
DR DisGeNET; 3040; -.
DR GeneCards; HBA1; -.
DR GeneCards; HBA2; -.
DR GeneReviews; HBA1; -.
DR GeneReviews; HBA2; -.
DR HGNC; HGNC:4823; HBA1.
DR HGNC; HGNC:4824; HBA2.
DR HPA; ENSG00000188536; Tissue enriched (bone).
DR HPA; ENSG00000206172; Tissue enriched (bone).
DR MalaCards; HBA1; -.
DR MalaCards; HBA2; -.
DR MIM; 140700; phenotype.
DR MIM; 141800; gene+phenotype.
DR MIM; 141850; gene.
DR MIM; 141860; gene.
DR MIM; 604131; phenotype.
DR MIM; 613978; phenotype.
DR neXtProt; NX_P69905; -.
DR OpenTargets; ENSG00000188536; -.
DR OpenTargets; ENSG00000206172; -.
DR Orphanet; 98791; Alpha-thalassemia-intellectual disability syndrome linked to chromosome 16.
DR Orphanet; 247511; Autosomal dominant secondary polycythemia.
DR Orphanet; 163596; Hb Bart's hydrops fetalis.
DR Orphanet; 93616; Hemoglobin H disease.
DR Orphanet; 330041; Hemoglobin M disease.
DR PharmGKB; PA29199; -.
DR VEuPathDB; HostDB:ENSG00000188536; -.
DR VEuPathDB; HostDB:ENSG00000206172; -.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000154590; -.
DR InParanoid; P69905; -.
DR OMA; FGKIGGQ; -.
DR OrthoDB; 1479834at2759; -.
DR PhylomeDB; P69905; -.
DR TreeFam; TF332328; -.
DR PathwayCommons; P69905; -.
DR Reactome; R-HSA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-HSA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-HSA-2168880; Scavenging of heme from plasma.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR Reactome; R-HSA-9707616; Heme signaling.
DR SignaLink; P69905; -.
DR SIGNOR; P69905; -.
DR BioGRID-ORCS; 3039; 11 hits in 551 CRISPR screens.
DR BioGRID-ORCS; 3040; 2 hits in 252 CRISPR screens.
DR ChiTaRS; HBA1; human.
DR ChiTaRS; HBA2; human.
DR EvolutionaryTrace; P69905; -.
DR GeneWiki; HBA2; -.
DR GeneWiki; Hemoglobin,_alpha_1; -.
DR GeneWiki; Hemoglobin,_alpha_2; -.
DR Pharos; P69905; Tclin.
DR PRO; PR:P69905; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P69905; protein.
DR Bgee; ENSG00000188536; Expressed in monocyte and 101 other tissues.
DR ExpressionAtlas; P69905; baseline and differential.
DR Genevisible; P69905; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IDA:BHF-UCL.
DR GO; GO:0005833; C:hemoglobin complex; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0043177; F:organic acid binding; IBA:GO_Central.
DR GO; GO:0019825; F:oxygen binding; IBA:GO_Central.
DR GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central.
DR GO; GO:0015670; P:carbon dioxide transport; IC:ComplexPortal.
DR GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:BHF-UCL.
DR GO; GO:0030185; P:nitric oxide transport; IDA:ComplexPortal.
DR GO; GO:0015671; P:oxygen transport; IDA:ComplexPortal.
DR GO; GO:0010942; P:positive regulation of cell death; IDA:BHF-UCL.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:BHF-UCL.
DR CDD; cd08927; Hb-alpha-like; 1.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR002338; Hemoglobin_a-typ.
DR InterPro; IPR002339; Hemoglobin_pi.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00612; ALPHAHAEM.
DR PRINTS; PR00815; PIHAEM.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Disease variant;
KW Glycation; Glycoprotein; Heme; Hereditary hemolytic anemia; Iron;
KW Metal-binding; Oxygen transport; Phosphoprotein; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:13872627, ECO:0000269|PubMed:13954546,
FT ECO:0000269|PubMed:14093912"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000052653"
FT PEPTIDE 96..104
FT /note="Hemopressin"
FT /evidence="ECO:0000305|PubMed:18077343"
FT /id="PRO_0000455882"
FT BINDING 59
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="distal binding residue"
FT BINDING 88
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT SITE 9..10
FT /note="(Microbial infection) Cleavage; by N.americanus apr-
FT 2"
FT /evidence="ECO:0000269|PubMed:12552433"
FT SITE 12
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:7358733"
FT SITE 14..15
FT /note="(Microbial infection) Cleavage; by N.americanus apr-
FT 2"
FT /evidence="ECO:0000269|PubMed:12552433"
FT SITE 25..26
FT /note="(Microbial infection) Cleavage; by N.americanus apr-
FT 2"
FT /evidence="ECO:0000269|PubMed:12552433"
FT SITE 30..31
FT /note="(Microbial infection) Cleavage; by N.americanus apr-
FT 2"
FT /evidence="ECO:0000269|PubMed:12552433"
FT SITE 46..47
FT /note="(Microbial infection) Cleavage; by N.americanus apr-
FT 2"
FT /evidence="ECO:0000269|PubMed:12552433"
FT SITE 48..49
FT /note="(Microbial infection) Cleavage; by N.americanus apr-
FT 2"
FT /evidence="ECO:0000269|PubMed:12552433"
FT SITE 53..54
FT /note="(Microbial infection) Cleavage; by N.americanus apr-
FT 2"
FT /evidence="ECO:0000269|PubMed:12552433"
FT SITE 56..57
FT /note="(Microbial infection) Cleavage; by N.americanus apr-
FT 2"
FT /evidence="ECO:0000269|PubMed:12552433"
FT SITE 57
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:7358733"
FT SITE 60..61
FT /note="(Microbial infection) Cleavage; by N.americanus apr-
FT 2"
FT /evidence="ECO:0000269|PubMed:12552433"
FT SITE 61
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:7358733"
FT SITE 91
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:7358733"
FT SITE 92..93
FT /note="(Microbial infection) Cleavage; by N.americanus apr-
FT 2"
FT /evidence="ECO:0000269|PubMed:12552433"
FT SITE 100
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:7358733"
FT SITE 107..108
FT /note="(Microbial infection) Cleavage; by N.americanus apr-
FT 2"
FT /evidence="ECO:0000269|PubMed:12552433"
FT SITE 109..110
FT /note="(Microbial infection) Cleavage; by N.americanus apr-
FT 2"
FT /evidence="ECO:0000269|PubMed:12552433"
FT SITE 122..123
FT /note="(Microbial infection) Cleavage; by N.americanus apr-
FT 2"
FT /evidence="ECO:0000269|PubMed:12552433"
FT SITE 134..135
FT /note="(Microbial infection) Cleavage; by N.americanus apr-
FT 2"
FT /evidence="ECO:0000269|PubMed:12552433"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 8
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 12
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 17
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 17
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 25
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 41
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT CARBOHYD 8
FT /note="N-linked (Glc) (glycation) lysine; alternate"
FT /evidence="ECO:0000269|PubMed:7358733"
FT CARBOHYD 17
FT /note="N-linked (Glc) (glycation) lysine; alternate"
FT /evidence="ECO:0000269|PubMed:7358733"
FT CARBOHYD 41
FT /note="N-linked (Glc) (glycation) lysine; alternate"
FT /evidence="ECO:0000269|PubMed:7358733"
FT CARBOHYD 62
FT /note="N-linked (Glc) (glycation) lysine"
FT /evidence="ECO:0000269|PubMed:7358733"
FT VARIANT 2
FT /note="V -> E (in Thionville; O(2) affinity down;
FT dbSNP:rs33981821)"
FT /evidence="ECO:0000269|PubMed:1618774"
FT /id="VAR_002719"
FT VARIANT 3
FT /note="L -> R (in ChongQing; O(2) affinity up;
FT dbSNP:rs36030576)"
FT /evidence="ECO:0000269|PubMed:6526652"
FT /id="VAR_002720"
FT VARIANT 6
FT /note="A -> D (in J-Toronto; dbSNP:rs34090856)"
FT /id="VAR_002721"
FT VARIANT 6
FT /note="A -> P (in Karachi; dbSNP:rs34751764)"
FT /id="VAR_002722"
FT VARIANT 7
FT /note="D -> A (in Sawara; O(2) affinity up;
FT dbSNP:rs33986902)"
FT /evidence="ECO:0000269|PubMed:20980,
FT ECO:0000269|PubMed:4744335"
FT /id="VAR_002723"
FT VARIANT 7
FT /note="D -> G (in Swan River; dbSNP:rs281864805)"
FT /evidence="ECO:0000269|PubMed:8745434"
FT /id="VAR_002724"
FT VARIANT 7
FT /note="D -> N (in Dunn; O(2) affinity up;
FT dbSNP:rs33961916)"
FT /evidence="ECO:0000269|PubMed:478975,
FT ECO:0000269|PubMed:7435503"
FT /id="VAR_002725"
FT VARIANT 7
FT /note="D -> V (in Ferndown; O(2) affinity up;
FT dbSNP:rs281864805)"
FT /evidence="ECO:0000269|PubMed:7238857"
FT /id="VAR_002726"
FT VARIANT 7
FT /note="D -> Y (in Woodville; O(2) affinity up;
FT dbSNP:rs281864806)"
FT /evidence="ECO:0000269|PubMed:3754246"
FT /id="VAR_002727"
FT VARIANT 8
FT /note="K -> E (in Kurosaki; dbSNP:rs34817956)"
FT /evidence="ECO:0000269|PubMed:7558876"
FT /id="VAR_002728"
FT VARIANT 10
FT /note="N -> T (in Broomfield; dbSNP:rs281860608)"
FT /id="VAR_038149"
FT VARIANT 12
FT /note="K -> E (in Anantharaj; dbSNP:rs33938574)"
FT /id="VAR_002729"
FT VARIANT 13
FT /note="A -> D (in J-Paris 1/J-Aljezur; dbSNP:rs35615982)"
FT /id="VAR_002730"
FT VARIANT 14
FT /note="A -> P (in Ravenscourt Park; causes alpha-
FT thalassemia; dbSNP:rs35331909)"
FT /id="VAR_038150"
FT VARIANT 15
FT /note="W -> R (in Evanston; O(2) affinity up;
FT dbSNP:rs33964317)"
FT /evidence="ECO:0000269|PubMed:6725558,
FT ECO:0000269|PubMed:6882779"
FT /id="VAR_002731"
FT VARIANT 16
FT /note="G -> R (in Ottawa/Siam; dbSNP:rs35816645)"
FT /id="VAR_002732"
FT VARIANT 17
FT /note="K -> M (in Harbin; slightly unstable;
FT dbSNP:rs35210126)"
FT /evidence="ECO:0000269|PubMed:6526652"
FT /id="VAR_002733"
FT VARIANT 17
FT /note="K -> N (in Beijing; dbSNP:rs281860648 and
FT dbSNP:rs281860619)"
FT /id="VAR_002734"
FT VARIANT 19
FT /note="G -> D (in Al-Ain Abu Dhabi; dbSNP:rs35993097)"
FT /evidence="ECO:0000269|PubMed:1428941"
FT /id="VAR_002735"
FT VARIANT 19
FT /note="G -> R (in Handsworth; dbSNP:rs34504387)"
FT /id="VAR_002736"
FT VARIANT 20
FT /note="A -> D (in J-Kurosh)"
FT /id="VAR_002737"
FT VARIANT 20
FT /note="A -> E (in J-Tashikuergan; dbSNP:rs35628685)"
FT /id="VAR_002738"
FT VARIANT 21
FT /note="H -> Q (in Le Lamentin; dbSNP:rs41525149)"
FT /id="VAR_002739"
FT VARIANT 21
FT /note="H -> R (in Hobart; dbSNP:rs33943087)"
FT /evidence="ECO:0000269|PubMed:3654264"
FT /id="VAR_002740"
FT VARIANT 22
FT /note="A -> D (in J-Nyanza; dbSNP:rs11548605)"
FT /id="VAR_002741"
FT VARIANT 22
FT /note="A -> P (in Fontainebleau; dbSNP:rs34324664)"
FT /id="VAR_002742"
FT VARIANT 23
FT /note="G -> D (in J-Medellin; dbSNP:rs34608326)"
FT /id="VAR_002743"
FT VARIANT 24
FT /note="E -> G (in Reims; slightly unstable;
FT dbSNP:rs33939421)"
FT /evidence="ECO:0000269|PubMed:2634669"
FT /id="VAR_002744"
FT VARIANT 24
FT /note="E -> K (in Chad; dbSNP:rs281864819)"
FT /id="VAR_002745"
FT VARIANT 25
FT /note="Y -> H (in Luxembourg; unstable; dbSNP:rs281864821)"
FT /evidence="ECO:0000269|PubMed:2599879"
FT /id="VAR_002746"
FT VARIANT 27
FT /note="A -> E (in Shenyang; unstable; dbSNP:rs281864822)"
FT /evidence="ECO:0000269|PubMed:7161109"
FT /id="VAR_002747"
FT VARIANT 27
FT /note="A -> V (in Campinas; dbSNP:rs281864822)"
FT /evidence="ECO:0000269|PubMed:14576901"
FT /id="VAR_025387"
FT VARIANT 28
FT /note="E -> D (in Hekinan; dbSNP:rs281865556)"
FT /id="VAR_002748"
FT VARIANT 28
FT /note="E -> G (in Fort Worth; dbSNP:rs281864823)"
FT /id="VAR_002749"
FT VARIANT 28
FT /note="E -> V (in Spanish town; dbSNP:rs281864823)"
FT /evidence="ECO:0000269|PubMed:2752146"
FT /id="VAR_002750"
FT VARIANT 31
FT /note="E -> K (in O-Padova; dbSNP:rs111033605)"
FT /id="VAR_002751"
FT VARIANT 32
FT /note="R -> K (causes alpha-thalassemia;
FT dbSNP:rs281864543)"
FT /evidence="ECO:0000269|PubMed:11410421"
FT /id="VAR_025002"
FT VARIANT 32
FT /note="R -> S (in Prato; unstable; dbSNP:rs111033606)"
FT /evidence="ECO:0000269|PubMed:486536"
FT /id="VAR_002752"
FT VARIANT 35
FT /note="L -> R (in Queens/Ogi; dbSNP:rs281864825)"
FT /id="VAR_002753"
FT VARIANT 38
FT /note="P -> PE (in Catonsville)"
FT /evidence="ECO:0000269|PubMed:8448109"
FT /id="VAR_002755"
FT VARIANT 38
FT /note="P -> R (in Bourmedes; dbSNP:rs281864826)"
FT /id="VAR_002754"
FT VARIANT 41
FT /note="K -> M (in Kanagawa; O(2) affinity up;
FT dbSNP:rs281864828)"
FT /evidence="ECO:0000269|PubMed:1634355"
FT /id="VAR_002756"
FT VARIANT 42
FT /note="T -> S (in Miyano; O(2) affinity up;
FT dbSNP:rs281860623)"
FT /evidence="ECO:0000269|PubMed:2634665"
FT /id="VAR_002757"
FT VARIANT 44
FT /note="F -> L (in Hirosaki; unstable; dbSNP:rs41491146)"
FT /evidence="ECO:0000269|PubMed:1182166"
FT /id="VAR_002758"
FT VARIANT 45
FT /note="P -> L (in Milledgeville; O(2) affinity up;
FT dbSNP:rs33978134 and dbSNP:rs281864830)"
FT /evidence="ECO:0000269|PubMed:7213661"
FT /id="VAR_002759"
FT VARIANT 45
FT /note="P -> R (in Kawachi; O(2) affinity up;
FT dbSNP:rs281864830)"
FT /evidence="ECO:0000269|PubMed:7068434"
FT /id="VAR_002760"
FT VARIANT 46
FT /note="H -> Q (in Bari; dbSNP:rs281860624)"
FT /id="VAR_002761"
FT VARIANT 46
FT /note="H -> R (in Fort de France; O(2) affinity up;
FT dbSNP:rs281864831)"
FT /evidence="ECO:0000269|PubMed:2752146"
FT /id="VAR_002762"
FT VARIANT 48
FT /note="D -> A (in Cordele; unstable; dbSNP:rs281864833)"
FT /evidence="ECO:0000269|PubMed:6547117"
FT /id="VAR_002763"
FT VARIANT 48
FT /note="D -> G (in Kokura; also in Umi/Michigan; unstable;
FT dbSNP:rs281864833)"
FT /evidence="ECO:0000269|PubMed:7068437"
FT /id="VAR_002764"
FT VARIANT 48
FT /note="D -> H (in Hasharon/Sinai; unstable;
FT dbSNP:rs281864834)"
FT /evidence="ECO:0000269|PubMed:5780195"
FT /id="VAR_002765"
FT VARIANT 48
FT /note="D -> Y (in Kurdistan; dbSNP:rs281864834)"
FT /evidence="ECO:0000269|PubMed:8195005"
FT /id="VAR_002766"
FT VARIANT 49
FT /note="L -> R (in Montgomery; dbSNP:rs41392146)"
FT /evidence="ECO:0000269|PubMed:1115799"
FT /id="VAR_002767"
FT VARIANT 50
FT /note="S -> R (in Savaria; dbSNP:rs41518249)"
FT /id="VAR_002768"
FT VARIANT 51
FT /note="H -> R (in Aichi; slightly unstable;
FT dbSNP:rs281864835)"
FT /evidence="ECO:0000269|PubMed:6714429"
FT /id="VAR_002769"
FT VARIANT 52
FT /note="G -> D (in J-Abidjan; dbSNP:rs281864836)"
FT /id="VAR_002770"
FT VARIANT 52
FT /note="G -> R (in Russ; dbSNP:rs281864837)"
FT /id="VAR_002771"
FT VARIANT 54
FT /note="A -> D (in J-Rovigo; unstable; dbSNP:rs281864838)"
FT /evidence="ECO:0000269|PubMed:4824923"
FT /id="VAR_002772"
FT VARIANT 55
FT /note="Q -> R (in Hikoshima/Shimonoseki;
FT dbSNP:rs281864839)"
FT /id="VAR_002773"
FT VARIANT 57
FT /note="K -> R (in Port Huron; dbSNP:rs281864841)"
FT /evidence="ECO:0000269|PubMed:1802882"
FT /id="VAR_002774"
FT VARIANT 57
FT /note="K -> T (in Thailand; dbSNP:rs281864841)"
FT /id="VAR_002775"
FT VARIANT 58
FT /note="G -> R (in L-Persian Gulf; dbSNP:rs281864843)"
FT /id="VAR_002776"
FT VARIANT 59
FT /note="H -> Q (in Boghe; dbSNP:rs41378349)"
FT /evidence="ECO:0000269|PubMed:10569723"
FT /id="VAR_025388"
FT VARIANT 59
FT /note="H -> Y (in M-Boston/M-Osaka; O(2) affinity down;
FT dbSNP:rs281864845)"
FT /evidence="ECO:0000269|PubMed:4521212"
FT /id="VAR_002777"
FT VARIANT 60
FT /note="G -> D (in Adana; unstable; causes alpha-
FT thalassemia; dbSNP:rs28928878)"
FT /evidence="ECO:0000269|PubMed:8237999"
FT /id="VAR_002778"
FT VARIANT 60
FT /note="G -> V (in Tottori; unstable; dbSNP:rs281864846)"
FT /evidence="ECO:0000269|PubMed:7275660"
FT /id="VAR_002779"
FT VARIANT 61
FT /note="K -> N (in Zambia; dbSNP:rs281860659 and
FT dbSNP:rs111033598)"
FT /id="VAR_002780"
FT VARIANT 61
FT /note="Missing (in Clinic; unstable; causes alpha-
FT thalassemia)"
FT /evidence="ECO:0000269|PubMed:10206681"
FT /id="VAR_002781"
FT VARIANT 62
FT /note="K -> N (in J-Buda; dbSNP:rs33985574)"
FT /evidence="ECO:0000269|Ref.83"
FT /id="VAR_002782"
FT VARIANT 62
FT /note="K -> T (in J-Anatolia; dbSNP:rs281865558)"
FT /id="VAR_002783"
FT VARIANT 63
FT /note="V -> M (in Evans; unstable; dbSNP:rs41515649)"
FT /evidence="ECO:0000269|PubMed:2606724, ECO:0000269|Ref.11"
FT /id="VAR_002784"
FT VARIANT 63
FT /note="Missing (in HBH; hemoglobin Aghia Sophia)"
FT /evidence="ECO:0000269|PubMed:10569720"
FT /id="VAR_066401"
FT VARIANT 64
FT /note="A -> D (in Pontoise; unstable; dbSNP:rs34502246)"
FT /evidence="ECO:0000269|PubMed:849454"
FT /id="VAR_002785"
FT VARIANT 65
FT /note="D -> Y (in Persepolis; dbSNP:rs33984024)"
FT /id="VAR_002786"
FT VARIANT 69
FT /note="N -> K (in G-Philadelphia; dbSNP:rs1060339)"
FT /evidence="ECO:0000269|Ref.12"
FT /id="VAR_002787"
FT VARIANT 72
FT /note="A -> E (in J-Habana; dbSNP:rs281864853)"
FT /id="VAR_002788"
FT VARIANT 72
FT /note="A -> V (in Ozieri; dbSNP:rs281864853)"
FT /id="VAR_002789"
FT VARIANT 73
FT /note="H -> R (in Daneskgah-Teheran; dbSNP:rs281864854)"
FT /id="VAR_002790"
FT VARIANT 75
FT /note="D -> A (in Lille; dbSNP:rs281864856)"
FT /id="VAR_002791"
FT VARIANT 75
FT /note="D -> G (in Chapel Hill; dbSNP:rs33921047)"
FT /id="VAR_002792"
FT VARIANT 75
FT /note="D -> N (in G-Pest; dbSNP:rs281864857)"
FT /evidence="ECO:0000269|Ref.83"
FT /id="VAR_002793"
FT VARIANT 76
FT /note="D -> A (in Duan; dbSNP:rs33991223)"
FT /id="VAR_002794"
FT VARIANT 76
FT /note="D -> H (in Q-Iran; dbSNP:rs281864858)"
FT /id="VAR_002795"
FT VARIANT 77
FT /note="M -> K (in Noko; dbSNP:rs33969953)"
FT /id="VAR_002796"
FT VARIANT 77
FT /note="M -> T (in Aztec; dbSNP:rs33969953)"
FT /id="VAR_002797"
FT VARIANT 78
FT /note="P -> R (in Guizhou; dbSNP:rs281864861)"
FT /id="VAR_002798"
FT VARIANT 79
FT /note="N -> H (in Davenport; dbSNP:rs111033602)"
FT /evidence="ECO:0000269|PubMed:2101836"
FT /id="VAR_002799"
FT VARIANT 79
FT /note="N -> K (in Stanleyville-2; dbSNP:rs281860607)"
FT /id="VAR_002800"
FT VARIANT 80
FT /note="A -> G (in Singapore; dbSNP:rs281860603)"
FT /id="VAR_012662"
FT VARIANT 81
FT /note="L -> R (in Ann Arbor; unstable; dbSNP:rs281864863)"
FT /evidence="ECO:0000269|PubMed:5033650"
FT /id="VAR_002801"
FT VARIANT 82
FT /note="S -> C (in Nigeria; dbSNP:rs281864864)"
FT /id="VAR_002802"
FT VARIANT 83
FT /note="A -> D (in Garden State; dbSNP:rs281864865)"
FT /id="VAR_002803"
FT VARIANT 85
FT /note="S -> R (in Etobicoke; O(2) affinity up;
FT dbSNP:rs281860612)"
FT /evidence="ECO:0000269|PubMed:6874377"
FT /id="VAR_002804"
FT VARIANT 86
FT /note="D -> V (in Inkster; O(2) affinity up;
FT dbSNP:rs41331747)"
FT /evidence="ECO:0000269|PubMed:4212045"
FT /id="VAR_002805"
FT VARIANT 86
FT /note="D -> Y (in Atago; O(2) affinity up;
FT dbSNP:rs281864777)"
FT /evidence="ECO:0000269|PubMed:5115619"
FT /id="VAR_002806"
FT VARIANT 87
FT /note="L -> R (in Moabit; unstable; dbSNP:rs281864866)"
FT /evidence="ECO:0000269|PubMed:108887"
FT /id="VAR_002807"
FT VARIANT 88
FT /note="H -> N (in Auckland; unstable; dbSNP:rs281864868)"
FT /evidence="ECO:0000269|PubMed:9322075"
FT /id="VAR_002808"
FT VARIANT 88
FT /note="H -> R (in Iwata; unstable; dbSNP:rs281864867)"
FT /id="VAR_002809"
FT VARIANT 89
FT /note="A -> S (in Loire; O(2) affinity up;
FT dbSNP:rs35239527)"
FT /evidence="ECO:0000269|PubMed:3142772"
FT /id="VAR_002810"
FT VARIANT 91
FT /note="K -> M (in Handa; O(2) affinity up;
FT dbSNP:rs281864873)"
FT /evidence="ECO:0000269|PubMed:6815131"
FT /id="VAR_002811"
FT VARIANT 92
FT /note="L -> F (in dbSNP:rs281864494)"
FT /id="VAR_049272"
FT VARIANT 92
FT /note="L -> P (in Port Phillip; unstable;
FT dbSNP:rs281864874)"
FT /evidence="ECO:0000269|PubMed:902765"
FT /id="VAR_002812"
FT VARIANT 93
FT /note="R -> Q (in J-Cape Town; O(2) affinity up;
FT dbSNP:rs281864875)"
FT /evidence="ECO:0000269|PubMed:5091982,
FT ECO:0000269|PubMed:5988206"
FT /id="VAR_002813"
FT VARIANT 93
FT /note="R -> W (in Cemenelum; O(2) affinity up;
FT dbSNP:rs281864876)"
FT /evidence="ECO:0000269|PubMed:8148419"
FT /id="VAR_020775"
FT VARIANT 95
FT /note="D -> A (in Bassett; markedly reduced oxygen
FT affinity; dbSNP:rs281864879)"
FT /evidence="ECO:0000269|PubMed:15495251"
FT /id="VAR_025389"
FT VARIANT 95
FT /note="D -> Y (in Setif; unstable; dbSNP:rs281864878)"
FT /evidence="ECO:0000269|PubMed:4667378"
FT /id="VAR_002814"
FT VARIANT 96
FT /note="P -> A (in Denmark Hill; O(2) affinity up;
FT dbSNP:rs281864881)"
FT /evidence="ECO:0000269|PubMed:5085669"
FT /id="VAR_002815"
FT VARIANT 96
FT /note="P -> T (in Godavari; O(2) affinity up;
FT dbSNP:rs281864881)"
FT /evidence="ECO:0000269|PubMed:9494044"
FT /id="VAR_002816"
FT VARIANT 98
FT /note="N -> K (in Dallas; O(2) affinity up;
FT dbSNP:rs41338947)"
FT /evidence="ECO:0000269|PubMed:1390940"
FT /id="VAR_002817"
FT VARIANT 100
FT /note="K -> E (in Turriff; dbSNP:rs281864882)"
FT /evidence="ECO:0000269|PubMed:1634357"
FT /id="VAR_002818"
FT VARIANT 103
FT /note="S -> R (in Manitoba; slightly unstable;
FT dbSNP:rs41344646)"
FT /evidence="ECO:0000269|PubMed:6547932"
FT /id="VAR_002819"
FT VARIANT 104
FT /note="H -> R (in Contaldo; unstable; dbSNP:rs63750752)"
FT /evidence="ECO:0000269|PubMed:6547932"
FT /id="VAR_002820"
FT VARIANT 104
FT /note="H -> Y (in Charolles; dbSNP:rs63750073)"
FT /evidence="ECO:0000269|PubMed:10569723"
FT /id="VAR_025390"
FT VARIANT 110
FT /note="L -> R (in Suan-Dok; unstable; causes alpha-
FT thalassemia; dbSNP:rs41479844)"
FT /evidence="ECO:0000269|PubMed:478977"
FT /id="VAR_002821"
FT VARIANT 111
FT /note="A -> D (in Petah Tikva; unstable; causes alpha-
FT thalassemia; dbSNP:rs28928889)"
FT /evidence="ECO:0000269|PubMed:7470621"
FT /id="VAR_002822"
FT VARIANT 113
FT /note="H -> D (in Hopkins-II; unstable; dbSNP:rs281864885)"
FT /evidence="ECO:0000269|PubMed:5288820"
FT /id="VAR_002823"
FT VARIANT 114
FT /note="L -> H (in Twin Peaks; dbSNP:rs281860618)"
FT /id="VAR_002824"
FT VARIANT 115
FT /note="P -> L (in Nouakchott; dbSNP:rs267607269)"
FT /id="VAR_002825"
FT VARIANT 115
FT /note="P -> R (in Chiapas; dbSNP:rs267607269)"
FT /id="VAR_002826"
FT VARIANT 115
FT /note="P -> S (in Melusine; dbSNP:rs281864887)"
FT /evidence="ECO:0000269|PubMed:8294199"
FT /id="VAR_002827"
FT VARIANT 116
FT /note="A -> D (in J-Tongariki; dbSNP:rs281864888)"
FT /id="VAR_002828"
FT VARIANT 117
FT /note="E -> A (in Ube-4; dbSNP:rs281864946)"
FT /id="VAR_002829"
FT VARIANT 117
FT /note="E -> EHLPAE (in Zaire)"
FT /evidence="ECO:0000269|PubMed:1511986"
FT /id="VAR_002830"
FT VARIANT 118
FT /note="F -> FI (in Phnom Penh)"
FT /evidence="ECO:0000269|PubMed:9452028"
FT /id="VAR_002831"
FT VARIANT 119
FT /note="T -> TEFT (in Grady)"
FT /evidence="ECO:0000269|PubMed:4528583"
FT /id="VAR_002832"
FT VARIANT 121
FT /note="A -> E (in J-Meerut/J-Birmingham; dbSNP:rs36075744)"
FT /evidence="ECO:0000269|PubMed:7713747"
FT /id="VAR_002833"
FT VARIANT 122
FT /note="V -> M (in Owari; dbSNP:rs35187567)"
FT /id="VAR_002834"
FT VARIANT 123
FT /note="H -> Q (in Westmead; dbSNP:rs41479347)"
FT /evidence="ECO:0000269|PubMed:1686260"
FT /id="VAR_002835"
FT VARIANT 126
FT /note="L -> P (in Quong Sze; causes alpha-thalassemia;
FT dbSNP:rs41397847)"
FT /id="VAR_002836"
FT VARIANT 126
FT /note="L -> R (in Plasencia; family with moderate
FT microcytosis and hypochromia; dbSNP:rs41397847)"
FT /evidence="ECO:0000269|PubMed:15921163"
FT /id="VAR_025391"
FT VARIANT 127
FT /note="D -> G (in West One; dbSNP:rs33957766)"
FT /evidence="ECO:0000269|PubMed:14576901"
FT /id="VAR_025392"
FT VARIANT 127
FT /note="D -> V (in Fukutomi; O(2) affinity up;
FT dbSNP:rs33957766)"
FT /evidence="ECO:0000269|PubMed:2079432"
FT /id="VAR_002837"
FT VARIANT 127
FT /note="D -> Y (in Montefiore; O(2) affinity up;
FT dbSNP:rs33933481)"
FT /evidence="ECO:0000269|PubMed:8798486"
FT /id="VAR_002838"
FT VARIANT 128
FT /note="K -> N (in Jackson; dbSNP:rs33972894)"
FT /id="VAR_002839"
FT VARIANT 130
FT /note="L -> P (in Tunis-Bizerte; unstable; causes alpha-
FT thalassemia; dbSNP:rs281864889)"
FT /evidence="ECO:0000269|PubMed:7786798"
FT /id="VAR_002840"
FT VARIANT 131
FT /note="A -> D (in Yuda; O(2) affinity down;
FT dbSNP:rs41528545)"
FT /evidence="ECO:0000269|PubMed:1428950"
FT /id="VAR_002842"
FT VARIANT 131
FT /note="A -> P (in Sun Prairie; unstable; dbSNP:rs41529844)"
FT /evidence="ECO:0000269|PubMed:2079430"
FT /id="VAR_002841"
FT VARIANT 132
FT /note="S -> P (in Questembert; highly unstable; causes
FT alpha-thalassemia; dbSNP:rs63751417)"
FT /evidence="ECO:0000269|PubMed:8493987"
FT /id="VAR_002843"
FT VARIANT 134
FT /note="S -> R (in Val de Marne; O(2) affinity up;
FT dbSNP:rs56308100 and dbSNP:rs55948437)"
FT /evidence="ECO:0000269|PubMed:8294200"
FT /id="VAR_002844"
FT VARIANT 136
FT /note="V -> E (in Pavie; dbSNP:rs63749809)"
FT /id="VAR_002845"
FT VARIANT 137
FT /note="L -> M (in Chicago; dbSNP:rs41364652)"
FT /id="VAR_002846"
FT VARIANT 137
FT /note="L -> P (in Bibba; unstable; causes alpha-
FT thalassemia; dbSNP:rs41469945)"
FT /evidence="ECO:0000269|PubMed:5440849"
FT /id="VAR_002847"
FT VARIANT 137
FT /note="L -> R (in Toyama; dbSNP:rs41469945)"
FT /evidence="ECO:0000269|PubMed:2833478"
FT /id="VAR_035242"
FT VARIANT 139
FT /note="S -> P (in Attleboro; O(2) affinity up;
FT dbSNP:rs63750801)"
FT /evidence="ECO:0000269|PubMed:2108715"
FT /id="VAR_002848"
FT VARIANT 140
FT /note="K -> E (in Hanamaki; O(2) affinity up;
FT dbSNP:rs41361546)"
FT /evidence="ECO:0000269|PubMed:1634363"
FT /id="VAR_002849"
FT VARIANT 140
FT /note="K -> T (in Tokoname; O(2) affinity up;
FT dbSNP:rs56348461)"
FT /evidence="ECO:0000269|PubMed:6188720"
FT /id="VAR_002850"
FT VARIANT 141
FT /note="Y -> H (in Rouen/Ethiopia; O(2) affinity up;
FT dbSNP:rs55870409)"
FT /evidence="ECO:0000269|PubMed:1390944,
FT ECO:0000269|PubMed:1428951"
FT /id="VAR_002851"
FT VARIANT 142
FT /note="R -> C (in Nunobiki; O(2) affinity up;
FT dbSNP:rs63750134)"
FT /evidence="ECO:0000269|PubMed:3973024"
FT /id="VAR_002852"
FT VARIANT 142
FT /note="R -> H (in Suresnes; O(2) affinity up;
FT dbSNP:rs33935328)"
FT /evidence="ECO:0000269|PubMed:7410435"
FT /id="VAR_002854"
FT VARIANT 142
FT /note="R -> L (in Legnano; O(2) affinity up;
FT dbSNP:rs33935328)"
FT /evidence="ECO:0000269|PubMed:7462179"
FT /id="VAR_002853"
FT VARIANT 142
FT /note="R -> P (in Singapore; dbSNP:rs33935328)"
FT /id="VAR_002855"
FT CONFLICT 10
FT /note="N -> H (in Ref. 13; BAD97112)"
FT /evidence="ECO:0000305"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:2W72"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:2W72"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:2W72"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:2W72"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1M9P"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:6XDT"
FT HELIX 54..72
FT /evidence="ECO:0007829|PDB:2W72"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2W72"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:2W72"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:2W72"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2M6Z"
FT HELIX 97..113
FT /evidence="ECO:0007829|PDB:2W72"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2W72"
FT HELIX 120..138
FT /evidence="ECO:0007829|PDB:2W72"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:6HK2"
SQ SEQUENCE 142 AA; 15258 MW; 15E13666573BBBAE CRC64;
MVLSPADKTN VKAAWGKVGA HAGEYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG
KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHLPAEFTP
AVHASLDKFL ASVSTVLTSK YR
