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 27-MAR-2024, entry version 209. 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 ASN-62 AND 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 ARG-3 AND 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 VAL-28 AND 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 7QU4; X-ray; 1.66 A; A/B=1-142. 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; 7UVB; X-ray; 2.05 A; A/C=2-142. DR PDB; 7VDE; EM; 3.20 A; A/C=1-142. DR PDB; 7XGY; EM; 3.50 A; A/C=1-142. DR PDB; 8DOV; X-ray; 2.10 A; A/C/E/G=2-142. DR PDB; 8EGI; X-ray; 2.30 A; A/C=1-142. DR PDB; 8FDK; X-ray; 1.89 A; A/C=2-142. DR PDB; 8FDL; X-ray; 1.75 A; A/C=2-142. DR PDB; 8FDM; X-ray; 1.91 A; A/C=2-142. DR PDB; 8FDN; X-ray; 2.20 A; A/C=2-142. 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; 7QU4; -. DR PDBsum; 7UD7; -. DR PDBsum; 7UD8; -. DR PDBsum; 7UF6; -. DR PDBsum; 7UF7; -. DR PDBsum; 7UVB; -. DR PDBsum; 7VDE; -. DR PDBsum; 7XGY; -. DR PDBsum; 8DOV; -. DR PDBsum; 8EGI; -. DR PDBsum; 8FDK; -. DR PDBsum; 8FDL; -. DR PDBsum; 8FDM; -. DR PDBsum; 8FDN; -. DR AlphaFoldDB; P69905; -. DR EMDB; EMD-0407; -. DR EMDB; EMD-0408; -. DR EMDB; EMD-13319; -. DR EMDB; EMD-13320; -. DR EMDB; EMD-13325; -. DR EMDB; EMD-31915; -. DR EMDB; EMD-33189; -. DR SASBDB; P69905; -. DR SMR; P69905; -. DR BioGRID; 109289; 60. DR BioGRID; 109290; 136. 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; 66. DR MINT; P69905; -. DR STRING; 9606.ENSP00000251595; -. DR BindingDB; P69905; -. 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-GlcNAc glycan (3 sites). DR GlyCosmos; P69905; 7 sites, 1 glycan. DR GlyGen; P69905; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P69905; -. DR MetOSite; P69905; -. DR PhosphoSitePlus; P69905; -. DR BioMuta; HBA1; -. DR DMDM; 57013850; -. DR DOSAC-COBS-2DPAGE; P69905; -. DR REPRODUCTION-2DPAGE; IPI00410714; -. DR CPTAC; non-CPTAC-1129; -. DR CPTAC; non-CPTAC-1130; -. DR EPD; P69905; -. DR jPOST; P69905; -. DR MassIVE; P69905; -. DR MaxQB; P69905; -. DR PaxDb; 9606-ENSP00000251595; -. DR PeptideAtlas; P69905; -. DR PRIDE; P69905; -. DR ProteomicsDB; 57547; -. DR TopDownProteomics; P69905; -. DR ABCD; P69905; 2 sequenced antibodies. DR Antibodypedia; 65596; 238 antibodies from 18 providers. DR Antibodypedia; 8893; 251 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 AGR; HGNC:4823; -. DR AGR; HGNC:4824; -. 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; VIATMFP; -. DR OrthoDB; 2939502at2759; -. 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; 13 hits in 607 CRISPR screens. DR BioGRID-ORCS; 3040; 2 hits in 290 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 102 other cell types or tissues. DR ExpressionAtlas; P69905; baseline and differential. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. 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: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; NAS: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:0042542; P:response to hydrogen peroxide; IDA:BHF-UCL. DR CDD; cd08927; Hb-alpha-like; 1. DR Gene3D; 1.10.490.10; Globins; 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 PANTHER; PTHR11442; HEMOGLOBIN FAMILY MEMBER; 1. DR PANTHER; PTHR11442:SF48; HEMOGLOBIN SUBUNIT ALPHA; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR00612; ALPHAHAEM. DR PRINTS; PR00815; PIHAEM. DR SUPFAM; SSF46458; Globin-like; 1. DR PROSITE; PS01033; GLOBIN; 1. DR SWISS-2DPAGE; P69905; -. DR UCD-2DPAGE; P69905; -. DR Genevisible; P69905; HS. 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="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238" 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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00238" 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 FT alpha-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 FT alpha-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 FT alpha-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 FT alpha-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 FT alpha-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 FT alpha-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 FT alpha-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 //