ID HBB_HUMAN Reviewed; 147 AA. AC P68871; A4GX73; B2ZUE0; P02023; Q13852; Q14481; Q14510; Q45KT0; Q549N7; AC Q6FI08; Q6R7N2; Q8IZI1; Q9BX96; Q9UCD6; Q9UCP8; Q9UCP9; 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 beta; DE AltName: Full=Beta-globin; DE AltName: Full=Hemoglobin beta chain; DE Contains: DE RecName: Full=LVV-hemorphin-7; DE Contains: DE RecName: Full=Spinorphin; GN Name=HBB; 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]. RX PubMed=1019344; DOI=10.1016/s0079-6603(08)60917-4; RA Marotta C., Forget B., Cohen-Solal M., Weissman S.M.; RT "Nucleotide sequence analysis of coding and noncoding regions of human RT beta-globin mRNA."; RL Prog. Nucleic Acid Res. Mol. Biol. 19:165-175(1976). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6254664; DOI=10.1016/0092-8674(80)90428-6; RA Lawn R.M., Efstratiadis A., O'Connell C., Maniatis T.; RT "The nucleotide sequence of the human beta-globin gene."; RL Cell 21:647-651(1980). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-7. RX PubMed=16175509; DOI=10.1086/491748; RA Wood E.T., Stover D.A., Slatkin M., Nachman M.W., Hammer M.F.; RT "The beta-globin recombinational hotspot reduces the effects of strong RT selection around HbC, a recently arisen mutation providing resistance to RT malaria."; RL Am. J. Hum. Genet. 77:637-642(2005). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Lu L., Hu Z.H., Du C.S., Fu Y.S.; RT "DNA sequence of the human beta-globin gene isolated from a healthy RT Chinese."; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-113. RA Cabeda J.M., Correia C., Estevinho A., Cardoso C., Amorim M.L., Cleto E., RA Vale L., Coimbra E., Pinho L., Justica B.; RT "Unexpected patterns of globin mutations in thalassemia patients from north RT of Portugal."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LOUISVILLE LEU-43. RC TISSUE=Blood; RA Kutlar F., Harbin J., Brisco J., Kutlar A.; RT "Rapid detection of electrophoretically silent, unstable human hemoglobin RT 'Louisville', (Beta; Phe 42 Leu/TTT to CTT) by cDNA sequencing of mRNA."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT DURHAM-N.C. PRO-115. RC TISSUE=Blood; RA Kutlar F., Abboud M., Leithner C., Holley L., Brisco J., Kutlar A.; RT "Electrophoretically silent, very unstable, thalassemic mutation at codon RT 114 of beta globin (hemoglobin Durham-N.C.) detected by cDNA sequencing of RT mRNA, from a Russian women."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT TY GARD GLN-125. RC TISSUE=Blood; RA Kutlar F., Holley L., Leithner C., Kutlar A.; RT "A rare beta chain variant 'Hemoglobin Ty Gard:Pro 124 Gln' found in a RT Caucasian female with erythrocytosis."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kutlar A., Vercellotti G.M., Glendenning M., Holley L., Elam D., Kutlar F.; RT "Heterozygote C->A beta-thalassemia mutation at the intron-2/848 nucleotide RT of beta globin gene was detected on a Northern European (Caucasian) RT individual."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT SKCA VAL-7, AND VARIANT SER-140. RC TISSUE=Blood; RA Kutlar F., Lallinger R.R., Holley L., Glendenning M., Kutlar A.; RT "A new hemoglobin, beta chain variant 'Hb S-Wake' confirmed to be on the RT same chromosome with hemoglobin S mutation, detected in an African-American RT family."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT O-ARAB LYS-122. RC TISSUE=Blood; RA Kutlar F., Elam D., Glendenning M., Kutlar A., Dincol G.; RT "Coexistence of the hemoglobin O-Arab (Glu 121 Lys) and beta-thalassemia RT (intron-2; nucleotide 745 C->G) was detected in a Turkish patient."; RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Li W.J.; RT "Thalassaemic trait cause by C-T substitution at position -90 in proximal RT CACCC box of beta-globin gene in China family."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PHE-50 AND PRO-76. RC TISSUE=Lymphocyte; RA Fan B., Xie L., Guan X.; RT "The differently expressed genes in the lymphocyte of recovered SARS RT patients."; RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Blood; RA Mehta S., Li T., Davis D.H., Nechtman J., Kutlar F.; RT "Beta-thalassemia G->C mutation at the nucleotide 5 position of intron 1 of RT beta globin gene was detected in Asian-Indian female with two polymorphisms RT in cis."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [15] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Hilliard L.M., Patel N., Li T., Zhang H., Kutlar A., Kutlar F.; RT "Hb Dothan: a novel beta chain variant due to (-GTG) deletion between the RT codons 25/26 of beta globin gene detected in a Caucasian male baby."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. RN [16] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Spleen; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [17] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [18] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [19] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; 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 [20] RP PROTEIN SEQUENCE OF 2-147. 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 [21] RP PROTEIN SEQUENCE OF 3-9, INVOLVEMENT IN SKCA, AND VARIANT SKCA VAL-7. RX PubMed=13464827; DOI=10.1038/180326a0; RA Ingram V.M.; RT "Gene mutations in human haemoglobin: the chemical difference between RT normal and sickle cell haemoglobin."; RL Nature 180:326-328(1957). RN [22] RP PROTEIN SEQUENCE OF 19-31, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Tear; RX PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179; RA Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I., RA Suarez T., Elortza F.; RT "Human basal tear peptidome characterization by CID, HCD, and ETD followed RT by in silico and in vitro analyses for antimicrobial peptide RT identification."; RL J. Proteome Res. 14:2649-2658(2015). RN [23] RP PROTEIN SEQUENCE OF 33-42, AND MASS SPECTROMETRY. RX PubMed=1575724; DOI=10.1016/0006-291x(92)90699-l; RA Glaemsta E.-L., Meyerson B., Silberring J., Terenius L., Nyberg F.; RT "Isolation of a hemoglobin-derived opioid peptide from cerebrospinal fluid RT of patients with cerebrovascular bleedings."; RL Biochem. Biophys. Res. Commun. 184:1060-1066(1992). RN [24] RP PROTEIN SEQUENCE OF 33-42. RA Ianzer D., Konno K., Xavier C.H., Stoecklin R., Santos R.A.S., RA de Camargo A.C.M., Pimenta D.C.; RL Submitted (JUN-2007) to UniProtKB. RN [25] RP PROTEIN SEQUENCE OF 97-121, NUCLEOTIDE SEQUENCE [MRNA] OF 106-113, AND RP VARIANT BURKE ARG-108. RX PubMed=8401300; RA Suzuki H., Wada C., Kamata K., Takahashi E., Sato N., Kunitomo T.; RT "Globin chain synthesis in hemolytic anemia reticulocytes. A case of RT hemoglobin Burke."; RL Biochem. Mol. Biol. Int. 30:425-431(1993). RN [26] RP NUCLEOTIDE SEQUENCE [MRNA] OF 122-147. RX PubMed=2581851; DOI=10.1016/0378-1119(85)90093-9; RA Lang K.M., Spritz R.A.; RT "Cloning specific complete polyadenylylated 3'-terminal cDNA segments."; RL Gene 33:191-196(1985). RN [27] RP BISPHOSPHOGLYCERATE BINDING. RX PubMed=4555506; DOI=10.1038/237146a0; RA Arnone A.; RT "X-ray diffraction study of binding of 2,3-diphosphoglycerate to human RT deoxyhaemoglobin."; RL Nature 237:146-149(1972). RN [28] RP ACETYLATION AT LYS-60; LYS-83 AND LYS-145. RX PubMed=4531009; DOI=10.1073/pnas.71.12.4693; RA Shamsuddin M., Mason R.G., Ritchey J.M., Honig G.R., Klotz I.M.; RT "Sites of acetylation of sickle cell hemoglobin by aspirin."; RL Proc. Natl. Acad. Sci. U.S.A. 71:4693-4697(1974). RN [29] RP GLYCATION AT VAL-2. RX PubMed=635569; DOI=10.1126/science.635569; RA Bunn H.F., Gabbay K.H., Gallop P.M.; RT "The glycosylation of hemoglobin: relevance to diabetes mellitus."; RL Science 200:21-27(1978). RN [30] RP GLYCATION AT LYS-9; LYS-18; LYS-67; LYS-121 AND LYS-145, AND LACK OF RP GLYCATION AT LYS-60; LYS-83 AND LYS-96. 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 [31] RP INVOLVEMENT IN B-THAL, AND VARIANT B-THAL LYS-27. RX PubMed=6166632; DOI=10.1172/jci110226; RA Benz E.J. Jr., Berman B.W., Tonkonow B.L., Coupal E., Coates T., RA Boxer L.A., Altman A., Adams J.G. III; RT "Molecular analysis of the beta-thalassemia phenotype associated with RT inheritance of hemoglobin E (alpha 2 beta2(26)Glu leads to Lys)."; RL J. Clin. Invest. 68:118-126(1981). RN [32] RP SUBUNIT, TISSUE SPECIFICITY, AND PARTIAL PROTEIN SEQUENCE. RX PubMed=6539334; DOI=10.1016/s0021-9258(17)39875-7; RA Randhawa Z.I., Jones R.T., Lie-Injo L.E.; RT "Human hemoglobin Portland II (zeta 2 beta 2). Isolation and RT characterization of Portland hemoglobin components and their constituent RT globin chains."; RL J. Biol. Chem. 259:7325-7330(1984). RN [33] RP INTERACTION WITH HAPTOGLOBIN. RX PubMed=3718478; DOI=10.1042/bj2340453; RA Yoshioka N., Atassi M.Z.; RT "Haemoglobin binding with haptoglobin. Localization of the haptoglobin- RT binding sites on the beta-chain of human haemoglobin by synthetic RT overlapping peptides encompassing the entire chain."; RL Biochem. J. 234:453-456(1986). RN [34] RP MODIFICATION AT LEU-142. RX PubMed=1520632; DOI=10.1111/j.1365-2141.1992.tb08179.x; RA Brennan S.O., Shaw J., Allen J., George P.M.; RT "Beta 141 Leu is not deleted in the unstable haemoglobin Atlanta-Coventry RT but is replaced by a novel amino acid of mass 129 daltons."; RL Br. J. Haematol. 81:99-103(1992). RN [35] RP S-NITROSYLATION AT CYS-94. RX PubMed=8637569; DOI=10.1038/380221a0; RA Jia L., Bonaventura C., Bonaventura J., Stamler J.S.; RT "S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular RT control."; RL Nature 380:221-226(1996). RN [36] RP S-NITROSYLATION AT CYS-94. RX PubMed=9843411; DOI=10.1021/bi9816711; RA Chan N.L., Rogers P.H., Arnone A.; RT "Crystal structure of the S-nitroso form of liganded human hemoglobin."; RL Biochemistry 37:16459-16464(1998). RN [37] RP NITRIC OXIDE-BINDING. RX PubMed=10588683; DOI=10.1073/pnas.96.25.14206; RA Durner J., Gow A.J., Stamler J.S., Glazebrook J.; RT "Ancient origins of nitric oxide signaling in biological systems."; RL Proc. Natl. Acad. Sci. U.S.A. 96:14206-14207(1999). RN [38] RP POLYMORPHISM, AND ASSOCIATION OF VARIANT LYS-7 WITH RESISTANCE TO MALARIA. RX PubMed=11001883; RA Agarwal A., Guindo A., Cissoko Y., Taylor J.G., Coulibaly D., Kone A., RA Kayentao K., Djimde A., Plowe C.V., Doumbo O., Wellems T.E., Diallo D.; RT "Hemoglobin C associated with protection from severe malaria in the Dogon RT of Mali, a West African population with a low prevalence of hemoglobin S."; RL Blood 96:2358-2363(2000). RN [39] RP SUBUNIT. RX PubMed=11747442; DOI=10.1021/bi011329f; RA Kidd R.D., Russell J.E., Watmough N.J., Baker E.N., Brittain T.; RT "The role of beta chains in the control of the hemoglobin oxygen binding RT function: chimeric human/mouse proteins, structure, and function."; RL Biochemistry 40:15669-15675(2001). RN [40] RP POLYMORPHISM, AND ASSOCIATION OF VARIANT B-THAL LYS-27 WITH RESISTANCE TO RP MALARIA. RX PubMed=12149194; RA Chotivanich K., Udomsangpetch R., Pattanapanyasat K., Chierakul W., RA Simpson J., Looareesuwan S., White N.; RT "Hemoglobin E: a balanced polymorphism protective against high parasitemias RT and thus severe P falciparum malaria."; RL Blood 100:1172-1176(2002). RN [41] RP REVIEW ON FUNCTION OF SPINORPHIN. RX PubMed=12470213; DOI=10.2174/1389203023380404; RA Yamamoto Y., Ono H., Ueda A., Shimamura M., Nishimura K., Hazato T.; RT "Spinorphin as an endogenous inhibitor of enkephalin-degrading enzymes: RT roles in pain and inflammation."; RL Curr. Protein Pept. Sci. 3:587-599(2002). RN [42] 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 [43] RP POLYMORPHISM, AND ASSOCIATION OF VARIANT SKCA VAL-7 WITH RESISTANCE TO RP MALARIA. RX PubMed=16001361; DOI=10.1086/432519; RA Kwiatkowski D.P.; RT "How malaria has affected the human genome and what human genetics can RT teach us about malaria."; RL Am. J. Hum. Genet. 77:171-192(2005). RN [44] RP SYNTHESIS OF 33-42, AND FUNCTION. RX PubMed=16904236; DOI=10.1016/j.peptides.2006.06.009; RA Ianzer D., Konno K., Xavier C.H., Stoecklin R., Santos R.A.S., RA de Camargo A.C.M., Pimenta D.C.; RT "Hemorphin and hemorphin-like peptides isolated from dog pancreas and sheep RT brain are able to potentiate bradykinin activity in vivo."; RL Peptides 27:2957-2966(2006). RN [45] RP FUNCTION OF SPINORPHIN. RX PubMed=17676725; DOI=10.1021/jm070114m; RA Jung K.Y., Moon H.D., Lee G.E., Lim H.H., Park C.S., Kim Y.C.; RT "Structure-activity relationship studies of spinorphin as a potent and RT selective human P2X(3) receptor antagonist."; RL J. Med. Chem. 50:4543-4547(2007). RN [46] 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 [47] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; THR-13; SER-45; THR-51 RP AND THR-88, 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 [48] RP ELECTRON MICROSCOPY OF SICKLE-CELL HEMOGLOBIN FIBERS. RX PubMed=4123689; DOI=10.1073/pnas.70.3.718; RA Finch J.T., Perutz M.F., Bertles J.F., Doebler J.; RT "Structure of sickled erythrocytes and of sickle-cell hemoglobin fibers."; RL Proc. Natl. Acad. Sci. U.S.A. 70:718-722(1973). RN [49] RP X-RAY CRYSTALLOGRAPHY (5 ANGSTROMS) OF VARIANT SKCA VAL-7. RX PubMed=1195378; DOI=10.1016/s0022-2836(75)80108-2; RA Wishner B.C., Ward K.B., Lattman E.E., Love W.E.; RT "Crystal structure of sickle-cell deoxyhemoglobin at 5 A resolution."; RL J. Mol. Biol. 98:179-194(1975). RN [50] 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 [51] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF CARBONMONOXY HEMOGLOBIN. 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 [52] RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF DEOXYHEMOGLOBIN. RX PubMed=6726807; DOI=10.1016/0022-2836(84)90472-8; RA Fermi G., Perutz M.F., Shaanan B., Fourme R.; RT "The crystal structure of human deoxyhaemoglobin at 1.74 A resolution."; RL J. Mol. Biol. 175:159-174(1984). RN [53] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ROTHSCHILD ARG-38. RX PubMed=1567857; DOI=10.1021/bi00131a030; RA Kavanaugh J.S., Rogers P.H., Case D.A., Arnone A.; RT "High-resolution X-ray study of deoxyhemoglobin Rothschild 37 beta RT Trp-->Arg: a mutation that creates an intersubunit chloride-binding site."; RL Biochemistry 31:4111-4121(1992). RN [54] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ARG-75. RX PubMed=1507231; DOI=10.1016/0022-2836(92)90638-z; RA Fermi G., Perutz M.F., Williamson D., Stein P., Shih D.T.; RT "Structure-function relationships in the low-affinity mutant haemoglobin RT Aalborg (Gly74 (E18)beta-->Arg)."; RL J. Mol. Biol. 226:883-888(1992). RN [55] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND BISPHOSPHOGLYCERATE BINDING. RX PubMed=8377203; DOI=10.1006/jmbi.1993.1505; RA Richard V., Dodson G.G., Mauguen Y.; RT "Human deoxyhaemoglobin-2,3-diphosphoglycerate complex low-salt structure RT at 2.5 A resolution."; RL J. Mol. Biol. 233:270-274(1993). RN [56] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX PubMed=8642597; DOI=10.1006/jmbi.1996.0124; RA Paoli M., Liddington R., Tame J., Wilkinson A., Dodson G.; RT "Crystal structure of T state haemoglobin with oxygen bound at all four RT haems."; RL J. Mol. Biol. 256:775-792(1996). RN [57] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-38; GLU-38; GLY-38 AND RP TYR-38. RX PubMed=9521756; DOI=10.1021/bi9708702; RA Kavanaugh J.S., Weydert J.A., Rogers P.H., Arnone A.; RT "High-resolution crystal structures of human hemoglobin with mutations at RT tryptophan 37beta: structural basis for a high-affinity T-state."; RL Biochemistry 37:4358-4373(1998). RN [58] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT TRP-7. RX PubMed=9830011; DOI=10.1074/jbc.273.49.32690; RA Harrington D.J., Adachi K., Royer W.E. Jr.; RT "Crystal structure of deoxy-human hemoglobin beta6 Glu-->Trp. Implications RT for the structure and formation of the sickle cell fiber."; RL J. Biol. Chem. 273:32690-32696(1998). RN [59] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF VARIANT LYS-7. RX PubMed=12454462; DOI=10.1107/s0907444902016426; RA Dewan J.C., Feeling-Taylor A., Puius Y.A., Patskovska L., Patskovsky Y., RA Nagel R.L., Almo S.C., Hirsch R.E.; RT "Structure of mutant human carbonmonoxyhemoglobin C (betaE6K) at 2.0 A RT resolution."; RL Acta Crystallogr. D 58:2038-2042(2002). RN [60] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF VARIANT SKCA VAL-7 IN COMPLEX RP WITH HEME AND HBZ, AND SUBUNIT. RX PubMed=24100324; DOI=10.1107/s0907444913019197; RA Safo M.K., Ko T.P., Abdulmalik O., He Z., Wang A.H., Schreiter E.R., RA Russell J.E.; RT "Structure of fully liganded Hb zeta2beta2s trapped in a tense RT conformation."; RL Acta Crystallogr. D 69:2061-2071(2013). RN [61] RP VARIANT FREIBURG VAL-24 DEL. RX PubMed=5919752; DOI=10.1126/science.154.3752.1024; RA Jones R.T., Brimhall B., Huisman T.H., Kleihauer E., Betke K.; RT "Hemoglobin Freiburg: abnormal hemoglobin due to deletion of a single amino RT acid residue."; RL Science 154:1024-1027(1966). RN [62] RP VARIANT ALABAMA LYS-40. 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 [63] RP INVOLVEMENT IN HEIBAN, AND VARIANT ST LOUIS GLN-29. RX PubMed=186485; DOI=10.1172/jci108561; RA Thillet J., Cohen-Solal M., Seligmann M., Rosa J.; RT "Functional and physicochemical studies of hemoglobin St. Louis beta 28 RT (B10) Leu replaced by Gln: a variant with ferric beta heme iron."; RL J. Clin. Invest. 58:1098-1106(1976). RN [64] RP INVOLVEMENT IN B-THALIB. RX PubMed=1971109; DOI=10.1073/pnas.87.10.3924; RA Thein S.L., Hesketh C., Taylor P., Temperley I.J., Hutchinson R.M., RA Old J.M., Wood W.G., Clegg J.B., Weatherall D.J.; RT "Molecular basis for dominantly inherited inclusion body beta- RT thalassemia."; RL Proc. Natl. Acad. Sci. U.S.A. 87:3924-3928(1990). RN [65] RP VARIANT ALESHA MET-68. RX PubMed=8330974; DOI=10.3109/03630269308998896; RA Molchanova T.P., Postnikov Y.V., Pobedimskaya D.D., Smetanina N.S., RA Moschan A.A., Kazanetz E.G., Tokarev Y.N., Huisman T.H.J.; RT "Hb Alesha or alpha 2 beta (2)67(E11)Val-->Met: a new unstable hemoglobin RT variant identified through sequencing of amplified DNA."; RL Hemoglobin 17:217-225(1993). RN [66] RP VARIANT J-ALTGELDS GARDENS ASP-93. RX PubMed=721609; DOI=10.3109/03630267809007075; RA Adams J.G. III, Przywara K.P., Heller P., Shamsuddin M.; RT "Hemoglobin J Altgeld Gardens. A hemoglobin variant with a substitution of RT the proximal histidine of the beta-chain."; RL Hemoglobin 2:403-415(1978). RN [67] RP VARIANT ANKARA ASP-11. RX PubMed=4850241; DOI=10.1016/0014-5793(74)80766-0; RA Arcasoy A., Casey R., Lehmann H., Cavdar A.O., Berki A.; RT "A new haemoglobin J from Turkey -- Hb Ankara (beta10 (A7) Ala-Asp)."; RL FEBS Lett. 42:121-123(1974). RN [68] RP VARIANT J-ANTAKYA MET-66, AND VARIANT COMPLUTENSE GLU-128. RX PubMed=3707969; DOI=10.1016/0167-4838(86)90178-0; RA Huisman T.H.J., Wilson J.B., Kutlar A., Yang K.-G., Chen S.-S., RA Webber B.B., Altay C., Martinez A.V.; RT "Hb J-Antakya or alpha 2 beta (2)65(E9)Lys-->Met in a Turkish family and Hb RT complutense or alpha 2 beta (2)127(H5)Gln-->Glu in a Spanish family; RT correction of a previously published identification."; RL Biochim. Biophys. Acta 871:229-231(1986). RN [69] RP VARIANT J-AUCKLAND ASP-26. RX PubMed=3654265; DOI=10.3109/03630268709017888; RA Williamson D., Wells R.M.G., Anderson R., Matthews J.; RT "A new unstable and low oxygen affinity hemoglobin variant: Hb J-Auckland RT [beta 25(B7)Gly-->Asp]."; RL Hemoglobin 11:221-230(1987). RN [70] RP VARIANT AURORA TYR-140. RX PubMed=8718692; DOI=10.3109/03630269509005825; RA Lafferty J., Ali M., Matthew K., Eng B., Patterson M., Waye J.S.; RT "Identification of a new high oxygen affinity hemoglobin variant: Hb Aurora RT [beta 139(H17) Asn-->Tyr]."; RL Hemoglobin 19:335-341(1995). RN [71] RP VARIANT BREST LYS-128. RX PubMed=3384710; DOI=10.3109/03630268808998024; RA Baudin-Chich V., Wajcman H., Gombaud-Saintonge G., Arous N., Riou J., RA Briere J., Galacteros F.; RT "Hemoglobin Brest [beta 127 (H5)Gln-->Lys] a new unstable human hemoglobin RT variant located at the alpha 1 beta 1 interface with specific RT electrophoretic behavior."; RL Hemoglobin 12:179-188(1988). RN [72] RP VARIANT BRISBANE HIS-69. RX PubMed=6166590; DOI=10.3109/03630268108991807; RA Brennan S.O., Wells R.M., Smith H., Carrell R.W.; RT "Hemoglobin Brisbane: beta68 Leu replaced by His. A new high oxygen RT affinity variant."; RL Hemoglobin 5:325-335(1981). RN [73] RP VARIANT BUNBURY ASN-95. RX PubMed=6629823; DOI=10.3109/03630268309038410; RA Como P.F., Kennett D., Wilkinson T., Kronenberg H.; RT "A new hemoglobin with high oxygen affinity -- hemoglobin Bunbury: alpha 2 RT beta 2 [94 (FG1) Asp replaced by Asn]."; RL Hemoglobin 7:413-421(1983). RN [74] RP VARIANT J-CAIRO GLN-66. RX PubMed=1247583; DOI=10.1016/0005-2795(76)90348-2; RA Garel M.-C., Hassan W., Coquelet M.T., Goossens M., Rosa J., Arous N.; RT "Hemoglobin J Cairo: beta 65 (E9) Lys leads to Gln, A new hemoglobin RT variant discovered in an Egyptian family."; RL Biochim. Biophys. Acta 420:97-104(1976). RN [75] RP VARIANT CAMPERDOWN SER-105. RX PubMed=1138922; DOI=10.1016/0005-2795(75)90231-7; RA Wilkinson T., Chua C.G., Carrell R.W., Robin H., Exner T., Lee K.M., RA Kronenberg H.; RT "A new haemoglobin variant, haemoglobin Camperdown (beta 104 (G6) RT arginine->serine)."; RL Biochim. Biophys. Acta 393:195-200(1975). RN [76] RP VARIANT CARIBBEAN ARG-92. RX PubMed=992050; DOI=10.1016/0014-5793(76)80662-x; RA Ahern E., Ahern V., Hilton T., Serjeant G.R., Serjeant B.E., Seakins M., RA Lang A., Middleton A., Lehmann H.; RT "Haemoglobin caribbean beta91 (F7) Leu replaced by Arg: a mildly RT haemoglobin with a low oxygen affinity."; RL FEBS Lett. 69:99-102(1976). RN [77] RP VARIANT CITY OF HOPE SER-70. RX PubMed=6434492; DOI=10.3109/03630268408991716; RA Rahbar S., Asmerom Y., Blume K.G.; RT "A silent hemoglobin variant detected by HPLC: hemoglobin City of Hope beta RT 69 (E13) Gly-->Ser."; RL Hemoglobin 8:333-342(1984). RN [78] RP VARIANT COIMBRA GLU-100. RX PubMed=1814856; DOI=10.3109/03630269109027896; RA Tamagnini G.P., Ribeiro M.L., Valente V., Ramachandran M., Wilson J.B., RA Baysal E., Gu L.H., Huisman T.H.J.; RT "Hb Coimbra or alpha 2 beta (2)99(G1)Asp-->Glu, a newly discovered high RT oxygen affinity variant."; RL Hemoglobin 15:487-496(1991). RN [79] RP VARIANT COSTA RICA ARG-78. RX PubMed=8641705; DOI=10.1007/s004390050145; RA Romero W.E.R., Castillo M., Chaves M.A., Saenz G.F., Gu L.-H., Wilson J.B., RA Baysal E., Smetanina N.S., Leonova J.Y., Huisman T.H.J.; RT "Hb Costa Rica or alpha 2 beta 2 77(EF1)His-->Arg: the first example of a RT somatic cell mutation in a globin gene."; RL Hum. Genet. 97:829-833(1996). RN [80] RP VARIANT DEBROUSSE PRO-97. RX PubMed=8602627; RX DOI=10.1002/(sici)1096-8652(199604)51:4<276::aid-ajh5>3.0.co;2-t; RA Lacan P., Kister J., Francina A., Souillet G., Galacteros F., Delaunay J., RA Wajcman H.; RT "Hemoglobin Debrousse (beta 96[FG3]Leu-->Pro): a new unstable hemoglobin RT with twofold increased oxygen affinity."; RL Am. J. Hematol. 51:276-281(1996). RN [81] RP VARIANT B-THAL GLY-127. RX PubMed=2399911; DOI=10.1002/ajh.2830350206; RA Bardakdjian-Michau J., Fucharoen S., Delanoe-Garin J., Kister J., RA Lacombe C., Winichagoon P., Blouquit Y., Riou J., Wasi P., Galacteros F.; RT "Hemoglobin Dhonburi alpha 2 beta 2 126 (H4) Val-->Gly: a new unstable beta RT variant producing a beta-thalassemia intermedia phenotype in association RT with beta zero-thalassemia."; RL Am. J. Hematol. 35:96-99(1990). RN [82] RP VARIANT NEWCASTLE PRO-93, VARIANT CAMPERDOWN SER-105, AND DESCRIPTION OF RP VARIANT DUINO. 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 [83] RP VARIANT DURHAM-N.C. PRO-115. RX PubMed=1301199; DOI=10.1002/humu.1380010207; RA Murru S., Poddie D., Sciarratta G.V., Agosti S., Baffico M., Melevendi C., RA Pirastu M., Cao A.; RT "A novel beta-globin structural mutant, Hb Brescia (beta 114 Leu-Pro), RT causing a severe beta-thalassemia intermedia phenotype."; RL Hum. Mutat. 1:124-128(1992). RN [84] RP VARIANT DURHAM-N.C. PRO-115. RX PubMed=8111050; RA de Castro C.M., Devlin B., Fleenor D.E., Lee M.E., Kaufman R.E.; RT "A novel beta-globin mutation, beta Durham-NC [beta 114 Leu-->Pro], RT produces a dominant thalassemia-like phenotype."; RL Blood 83:1109-1116(1994). RN [85] RP VARIANT J-EUROPA ASP-63. RX PubMed=8811317; DOI=10.3109/03630269609027919; RA Kiger L., Kister J., Groff P., Kalmes G., Prome D., Galacteros F., RA Wajcman H.; RT "Hb J-Europa [beta 62(E6)Ala-->Asp]: normal oxygen binding properties in a RT new variant involving a residue located distal to the heme."; RL Hemoglobin 20:135-140(1996). RN [86] RP VARIANT GEELONG ASP-140. RX PubMed=1917539; DOI=10.3109/03630269109072487; RA Como P.F., Hocking D.R., Swinton G.W., Trent R.J., Holland R.A.B., RA Tibben E.A., Wilkinson T., Kronenberg H.; RT "Hb Geelong [beta 139(H17)Asn-->Asp]."; RL Hemoglobin 15:85-95(1991). RN [87] RP VARIANT GRANGE-BLANCHE VAL-28. RX PubMed=3666141; DOI=10.1016/0014-5793(87)80509-4; RA Baklouti F., Giraud Y., Francina A., Richard G., Perier C., Geyssant A., RA Jaubert J., Brizard C., Delaunay J.; RT "Hemoglobin Grange-Blanche [beta 27(B9) Ala-->Val], a new variant with RT normal expression and increased affinity for oxygen."; RL FEBS Lett. 223:59-62(1987). RN [88] RP VARIANT GRAZ LEU-3. RX PubMed=1487420; DOI=10.3109/03630269208993117; RA Liu J.S., Molchanova T.P., Gu L.H., Wilson J.B., Hopmeier P., Schnedl W., RA Balaun E., Krejs G.J., Huisman T.H.J.; RT "Hb Graz or alpha 2 beta 2(2)(NA2)His-->Leu; a new beta chain variant RT observed in four families from southern Austria."; RL Hemoglobin 16:493-501(1992). RN [89] RP VARIANT HELSINKI MET-83. RX PubMed=826083; DOI=10.1159/000207947; RA Ikkala E., Koskela J., Pikkarainen P., Rahiala E.-L., El-Hazmi M.A.F., RA Nagai K., Lang A., Lehmann H.; RT "Hb Helsinki: a variant with a high oxygen affinity and a substitution at a RT 2,3-DPG binding site (beta82[EF6] Lys replaced by Met)."; RL Acta Haematol. 56:257-275(1976). RN [90] RP VARIANT HIMEJI ASP-141. RX PubMed=3754244; DOI=10.3109/03630268609046438; RA Ohba Y., Miyaji T., Murakami M., Kadowaki S., Fujita T., Oimomi M., RA Hatanaka H., Ishikawa K., Baba S., Hitaka K., Imai K.; RT "Hb Himeji or beta 140 (H18) Ala-->Asp. A slightly unstable hemoglobin with RT increased beta N-terminal glycation."; RL Hemoglobin 10:109-126(1986). RN [91] RP VARIANT HINSDALE LYS-140. RX PubMed=2513289; DOI=10.3109/03630268908998084; RA Moo-Penn W.F., Johnson M.H., Jue D.L., Lonser R.; RT "Hb Hinsdale [beta 139 (H17)Asn-->Lys]: a variant in the central cavity RT showing reduced affinity for oxygen and 2,3-diphosphoglycerate."; RL Hemoglobin 13:455-464(1989). RN [92] RP VARIANT HINWIL ASN-39. RX PubMed=8745430; DOI=10.3109/03630269609027908; RA Frischknecht H., Ventruto M., Hess D., Hunziker P., Rosatelli M.C., Cao A., RA Breitenstein U., Fehr J., Tuchschmid P.; RT "HB Hinwil or beta 38(C4)Thr-->Asn: a new beta chain variant detected in a RT Swiss family."; RL Hemoglobin 20:31-40(1996). RN [93] RP VARIANT HOWICK GLY-38. RX PubMed=8144352; DOI=10.3109/03630269309043491; RA Owen M.C., Ockelford P.A., Wells R.M.G.; RT "Hb Howick [beta 37(C3)Trp-->Gly]: a new high oxygen affinity variant of RT the alpha 1 beta 2 contact."; RL Hemoglobin 17:513-521(1993). RN [94] RP VARIANT INDIANAPOLIS ARG-113. RX PubMed=429365; DOI=10.1016/s0021-9258(18)50784-5; RA Adams J.G. III, Steinberg M.H., Boxer L.A., Baehner R.L., Forget B.G., RA Tsistrakis G.A.; RT "The structure of hemoglobin Indianapolis [beta112(G14) arginine]. An RT unstable variant detectable only by isotopic labeling."; RL J. Biol. Chem. 254:3479-3482(1979). RN [95] RP VARIANT ISEHARA ASN-93. RX PubMed=1787097; DOI=10.3109/03630269109027880; RA Harano T., Harano K., Kushida Y., Ueda S., Yoshii A., Nishinarita M.; RT "Hb Isehara (or Hb Redondo) [beta 92 (F8) His-->Asn]: an unstable variant RT with a proximal histidine substitution at the heme contact."; RL Hemoglobin 15:279-290(1991). RN [96] RP VARIANT ISTAMBUL GLN-93. RX PubMed=4639022; DOI=10.1172/jci107050; RA Aksoy M., Erdem S., Efremov G.D., Wilson J.B., Huisman T.H.J., RA Schroeder W.A., Shelton J.R., Shelton J.B., Ulitin O.N., Muftuoglu A.; RT "Hemoglobin Istanbul: substitution of glutamine for histidine in a proximal RT histidine (F8(92))."; RL J. Clin. Invest. 51:2380-2387(1972). RN [97] RP VARIANT JACKSONVILLE ASP-55. RX PubMed=2101840; RA Gaudry C.L. Jr., Pitel P.A., Jue D.L., Hine T.K., Johnson M.H., RA Moo-Penn W.F.; RT "Hb Jacksonville [alpha 2 beta 2(54)(D5)Val-->Asp]: a new unstable variant RT found in a patient with hemolytic anemia."; RL Hemoglobin 14:653-659(1990). RN [98] RP VARIANT JIANGHUA ILE-121. RX PubMed=6618888; RA Lu Y.Q., Fan J.L., Liu J.F., Hu H.L., Peng X.H., Huang C.-H., Huang P.Y., RA Chen S.S., Jai P.C., Yang K.G.; RT "Hemoglobin Jianghua [beta 120(GH3) Lys leads to Ile]: a new fast-moving RT variant found in China."; RL Hemoglobin 7:321-326(1983). RN [99] RP VARIANT KARLSKOGA HIS-22. RX PubMed=8330972; DOI=10.3109/03630269308998894; RA Landin B.; RT "Hb Karlskoga or alpha 2 beta (2)21(B3) Asp-->His: a new slow-moving RT variant found in Sweden."; RL Hemoglobin 17:201-208(1993). RN [100] RP VARIANT KNOSSOS SER-28. RX PubMed=7173395; DOI=10.1016/0014-5793(82)81052-1; RA Arous N., Galacteros F., Fessas P., Loukopoulos D., Blouquit Y., Komis G., RA Sellaye M., Boussiou M., Rosa J.; RT "Structural study of hemoglobin Knossos, beta 27 (B9) Ala leads to Ser. A RT new abnormal hemoglobin present as a silent beta-thalassemia."; RL FEBS Lett. 147:247-250(1982). RN [101] RP VARIANT KODAIRA GLN-147. RX PubMed=1634367; DOI=10.3109/03630269209005681; RA Harano T., Harano K., Kushida Y., Imai K., Nishinakamura R., Matsunaga T.; RT "Hb Kodaira [beta 146(HC3)His-->Gln]: a new beta chain variant with an RT amino acid substitution at the C-terminus."; RL Hemoglobin 16:85-91(1992). RN [102] RP VARIANT KOFU ILE-85. RX PubMed=3744871; DOI=10.3109/03630268608996871; RA Harano T., Harano K., Ueda S., Imai N., Kitazumi T.; RT "A new electrophoretically-silent hemoglobin variant: hemoglobin Kofu or RT alpha 2 beta 2 84 (EF8) Thr-->Ile."; RL Hemoglobin 10:417-420(1986). RN [103] RP VARIANT B-THAL ASP-116. RX PubMed=7693620; DOI=10.3109/03630269308997485; RA Divoky V., Svobodova M., Indrak K., Chrobak L., Molchanova T.P., RA Huisman T.H.J.; RT "Hb Hradec Kralove (Hb HK) or alpha 2 beta 2 115(G17)Ala-->Asp, a severely RT unstable hemoglobin variant resulting in a dominant beta-thalassemia trait RT in a Czech family."; RL Hemoglobin 17:319-328(1993). RN [104] RP VARIANT LA DESIRADE VAL-130. RX PubMed=3557994; DOI=10.3109/03630268609036564; RA Merault G., Keclard L., Garin J., Poyart C., Blouquit Y., Arous N., RA Galacteros F., Feingold J., Rosa J.; RT "Hemoglobin La Desirade alpha A2 beta 2 129 (H7) Ala-->Val: a new unstable RT hemoglobin."; RL Hemoglobin 10:593-605(1986). RN [105] RP VARIANT LA ROCHE-SUR-YON HIS-82. RX PubMed=1540659; DOI=10.1016/0925-4439(92)90052-o; RA Wajcman H., Kister J., Vasseur C., Blouquit Y., Trastour J.C., RA Cottenceau D., Galacteros F.; RT "Structure of the EF corner favors deamidation of asparaginyl residues in RT hemoglobin: the example of Hb La Roche-sur-Yon [beta 81 (EF5) Leu-->His]."; RL Biochim. Biophys. Acta 1138:127-132(1992). RN [106] RP VARIANT LAS PALMAS PHE-50. RX PubMed=3384708; DOI=10.3109/03630268808998022; RA Malcorra-Azpiazu J.J., Balda-Aguirre M.I., Diaz-Chico J.C., Hu H., RA Wilson J.B., Webber B.B., Kutlar F., Kutlar A., Huisman T.H.J.; RT "Hb Las Palmas or alpha 2 beta 2(49)(CD8)Ser-->Phe, a mildly unstable RT hemoglobin variant."; RL Hemoglobin 12:163-170(1988). RN [107] RP VARIANT LINKOPING THR-37. RX PubMed=3691763; DOI=10.1111/j.1600-0609.1987.tb01455.x; RA Berlin G., Wranne B., Jeppsson J.-O.; RT "Hb Linkoping (beta 36 Pro-->Thr): a new high oxygen affinity hemoglobin RT variant found in two families of Finnish origin."; RL Eur. J. Haematol. 39:452-456(1987). RN [108] RP VARIANT MAPUTO TYR-48. RX PubMed=6629824; DOI=10.3109/03630268309038411; RA Marinucci M., Boissel J.P., Massa A., Wajcman H., Tentori L., Labie D.; RT "Hemoglobin Maputo: a new beta-chain variant (alpha 2 beta 2 47 (CD6) Asp RT replaced by Tyr) in combination with hemoglobin S, identified by high RT performance liquid chromatography (HPLC)."; RL Hemoglobin 7:423-433(1983). RN [109] RP VARIANT MATERA LYS-56. RX PubMed=2384314; DOI=10.3109/03630269009002256; RA Sciarratta G.V., Ivaldi G.; RT "Hb Matera [beta 55(D6)Met-->Lys]: a new unstable hemoglobin variant in an RT Italian family."; RL Hemoglobin 14:79-85(1990). RN [110] RP VARIANT MIYASHIRO GLY-24. RX PubMed=7338468; DOI=10.3109/03630268108991833; RA Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Miyata H., RA Shinohara T., Hori T., Takayama J.; RT "Hemoglobin Miyashiro (beta 23[B5] val substituting for gly) an RT electrophoretically silent variant discovered by the isopropanol test."; RL Hemoglobin 5:653-666(1981). RN [111] RP VARIANT MIZUHO PRO-69. RX PubMed=893142; DOI=10.3109/03630267709027864; RA Ohba Y., Miyaji T., Matsuoka M., Sugiyama K., Suzuki T., Sugiura T.; RT "Hemoglobin Mizuho or beta 68 (E 12) leucine leads to proline, a new RT unstable variant associated with severe hemolytic anemia."; RL Hemoglobin 1:467-477(1977). RN [112] RP VARIANT MUSCAT VAL-33. RX PubMed=1517102; DOI=10.3109/03630269208998866; RA Ramachandran M., Gu L.H., Wilson J.B., Kitundu M.N., Adekile A.D., RA Liu J.C., McKie K.M., Huisman T.H.J.; RT "A new variant, HB Muscat [alpha 2 beta (2)32(B14)Leu-->Val] observed in RT association with HB S in an Arabian family."; RL Hemoglobin 16:259-266(1992). RN [113] RP VARIANT N-TIMONE GLU-9. RX PubMed=2634671; DOI=10.3109/03630268908998848; RA Lena-Russo D., Orsini A., Vovan L., Bardakdjian-Michau J., Lacombe C., RA Blouquit Y., Craescu C.T., Galacteros F.; RT "Hb N-Timone [alpha 2 beta 2(8)(A5)Lys-->Glu]: a new fast-moving variant RT with normal stability and oxygen affinity."; RL Hemoglobin 13:743-747(1989). RN [114] RP VARIANT NAGOYA PRO-98. RX PubMed=3838976; DOI=10.3109/03630268508996978; RA Ohba Y., Imanaka M., Matsuoka M., Hattori Y., Miyaji T., Funaki C., RA Shibata K., Shimokata H., Kuzuya F., Miwa S.; RT "A new unstable, high oxygen affinity hemoglobin: Hb Nagoya or beta 97 RT (FG4) His-->Pro."; RL Hemoglobin 9:11-24(1985). RN [115] RP VARIANT D-NEATH ALA-122. RX PubMed=8330979; DOI=10.3109/03630269308998901; RA Welch S.G., Bateman C.; RT "Hb D-Neath or beta 121 (GH4) Glu-->Ala: a new member of the Hb D family."; RL Hemoglobin 17:255-259(1993). RN [116] RP VARIANT NORTH CHICAGO SER-37. RX PubMed=3937824; DOI=10.3109/03630268508997038; RA Rahbar S., Louis J., Lee T., Asmerom Y.; RT "Hemoglobin North Chicago (beta 36 [C2] proline-->serine): a new high RT affinity hemoglobin."; RL Hemoglobin 9:559-576(1985). RN [117] RP VARIANT NORTH SHORE-CARACAS GLU-135. RX PubMed=891976; DOI=10.1016/0014-5793(77)80453-5; RA Arends T., Lehmann H., Plowman D., Stathopoulou R.; RT "Haemoglobin North Shore-Caracas beta 134 (H12) valine replaced by glutamic RT acid."; RL FEBS Lett. 80:261-265(1977). RN [118] RP VARIANT OLOMOUC ASP-87. RX PubMed=3623975; DOI=10.3109/03630268709005790; RA Indrak K., Wiedermann B.F., Batek F., Wilson J.B., Webber B.B., Kutlar A., RA Huisman T.H.J.; RT "Hb Olomouc or alpha 2 beta 2(86)(F2)Ala-->Asp, a new high oxygen affinity RT variant."; RL Hemoglobin 11:151-155(1987). RN [119] RP VARIANT PALMERSTON NORTH PHE-24. RX PubMed=7161106; DOI=10.3109/03630268209046450; RA Brennan S.O., Williamson D., Whisson M.E., Carrell R.W.; RT "Hemoglobin Palmerston North beta 23 (B5) Val replaced by Phe. A new RT variant identified in a patient with polycythemia."; RL Hemoglobin 6:569-575(1982). RN [120] RP VARIANT PIERRE-BENITE ASP-91. RX PubMed=3384709; DOI=10.3109/03630268808998023; RA Baklouti F., Giraud Y., Francina A., Richard G., Favre-Gilly J., RA Delaunay J.; RT "Hemoglobin Pierre-Benite [beta 90(F6)Glu-->Asp], a new high affinity RT variant found in a French family."; RL Hemoglobin 12:171-177(1988). RN [121] RP VARIANT PRESBYTERIAN LYS-109. RX PubMed=668922; DOI=10.1016/0014-5793(78)80720-0; RA Moo-Penn W.F., Wolff J.A., Simon G., Vacek M., Jue D.L., Johnson M.H.; RT "Hemoglobin Presbyterian: beta108 (G10) asparagine leads to lysine, A RT hemoglobin variant with low oxygen affinity."; RL FEBS Lett. 92:53-56(1978). RN [122] RP VARIANT PUTTELANGE VAL-141. RX PubMed=8522332; DOI=10.1007/bf00210304; RA Wajcman H., Girodon E., Prome D., North M.L., Plassa F., Duwig I., RA Kister J., Bergerat J.P., Oberling F., Lampert E., Lonsdorfer J., RA Goossens M., Galacteros F.; RT "Germline mosaicism for an alanine to valine substitution at residue beta RT 140 in hemoglobin Puttelange, a new variant with high oxygen affinity."; RL Hum. Genet. 96:711-716(1995). RN [123] RP VARIANT QUIN-HAI ARG-79. RX PubMed=6629822; DOI=10.3109/03630268309038409; RA Jen P.C., Chen L.C., Chen P.F., Wong Y., Chen L.F., Guo Y.Y., Chang F.Q., RA Chow Y.C., Chiu Y.; RT "Hemoglobin Quin-Hai, beta 78 (EF2) Leu replaced by Arg, a new abnormal RT hemoglobin found in Guangdong, China."; RL Hemoglobin 7:407-412(1983). RN [124] RP VARIANT RAMBAM ASP-70. RX PubMed=9761252; RA Bisse E., Zorn N., Eigel A., Lizama M., Huamam-Guillen P., Marz W., RA van Dorsselaer A., Wieland H.; RT "Hemoglobin Rambam (beta69[E13]Gly-->Asp), a pitfall in the assessment of RT diabetic control: characterization by electrospray mass spectrometry and RT HPLC."; RL Clin. Chem. 44:2172-2177(1998). RN [125] RP VARIANT RANDWICK GLY-16. RX PubMed=3384707; DOI=10.3109/03630268808998021; RA Gilbert A.T., Fleming P.J., Sumner D.R., Hughes W.G., Ip F., Kwan Y.L., RA Holland R.A.B.; RT "Hemoglobin Randwick or beta 15 (A12)Trp-->Gly: a new unstable beta-chain RT hemoglobin variant."; RL Hemoglobin 12:149-161(1988). RN [126] RP VARIANT RIO GRANDE THR-9. RX PubMed=6857757; DOI=10.3109/03630268309038405; RA Moo-Penn W.F., Johnson M.H., McGuffey J.E., Jue D.L., Therrell B.L. Jr.; RT "Hemoglobin Rio Grande [beta 8 (A5) Lys leads to Thr] a new variant found RT in a Mexican-American family."; RL Hemoglobin 7:91-95(1983). RN [127] RP VARIANT RUSH GLN-102. RX PubMed=4129558; RA Adams J.G. III, Winter W.P., Tausk K., Heller P.; RT "Hemoglobin Rush (beta 101 (g3) glutamine): a new unstable hemoglobin RT causing mild hemolytic anemia."; RL Blood 43:261-269(1974). RN [128] RP VARIANT SAITAMA PRO-118. RX PubMed=6687721; DOI=10.3109/03630268309038400; RA Ohba Y., Hasegawa Y., Amino H., Miwa S., Nakatsuji T., Hattori Y., RA Miyaji T.; RT "Hemoglobin Saitama or beta 117 (G19) His leads to Pro, a new variant RT causing hemolytic disease."; RL Hemoglobin 7:47-56(1983). RN [129] RP VARIANT M-SASKATOON TYR-64. RX PubMed=13897827; DOI=10.1073/pnas.47.11.1758; RA Gerald P.S., Efron M.L.; RT "Chemical studies of several varieties of Hb M."; RL Proc. Natl. Acad. Sci. U.S.A. 47:1758-1767(1961). RN [130] RP VARIANT SHELBY/LESLIE/DEACONESS LYS-132. RX PubMed=6526653; DOI=10.3109/03630268408991743; RA Moo-Penn W.F., Johnson M.H., McGuffey J.E., Jue D.L.; RT "Hemoglobin Shelby [beta 131(H9) Gln-->Lys] a correction to the structure RT of hemoglobin Deaconess and hemoglobin Leslie."; RL Hemoglobin 8:583-593(1984). RN [131] RP VARIANT J-SICILIA ASN-66. RX PubMed=4852224; DOI=10.1016/0014-5793(74)80050-5; RA Ricco G., Pich P.G., Mazza U., Rossi G., Ajmar P., Arese P., Gallo E.; RT "Hb J Sicilia: beta 65 (E9) Lys-Asn, a beta homologue of Hb Zambia."; RL FEBS Lett. 39:200-204(1974). RN [132] RP VARIANT STANMORE ALA-112. RX PubMed=1917537; DOI=10.3109/03630269109072484; RA Como P.F., Wylie B.R., Trent R.J., Bruce D., Volpato F., Wilkinson T., RA Kronenberg H., Holland R.A.B., Tibben E.A.; RT "A new unstable and low oxygen affinity hemoglobin variant: Hb Stanmore RT [beta 111(G13)Val-->Ala]."; RL Hemoglobin 15:53-65(1991). RN [133] RP VARIANT ST MANDE TYR-103. RX PubMed=7238856; DOI=10.1016/0014-5793(81)81046-0; RA Arous N., Braconnier F., Thillet J., Blouquit Y., Galacteros F., RA Chevrier M., Bordahandy C., Rosa J.; RT "Hemoglobin Saint Mande beta 102 (G4) asn replaced by tyr: a new low oxygen RT affinity variant."; RL FEBS Lett. 126:114-116(1981). RN [134] RP VARIANT WINDSOR ASP-12. RX PubMed=2599880; DOI=10.3109/03630268908998083; RA Gilbert A.T., Fleming P.J., Sumner D.R., Hughes W.G., Holland R.A.B., RA Tibben E.A.; RT "Hemoglobin Windsor or beta 11 (A8)Val-->Asp: a new unstable beta-chain RT hemoglobin variant producing a hemolytic anemia."; RL Hemoglobin 13:437-453(1989). RN [135] RP VARIANT YAHATA TYR-113. RX PubMed=1917530; DOI=10.3109/03630269109072490; RA Harano T., Harano K., Kushida Y., Ueda S.; RT "A new abnormal variant, Hb Yahata or beta 112(G14)Cys-->Tyr, found in a RT Japanese: structural confirmation by DNA sequencing of the beta-globin RT gene."; RL Hemoglobin 15:109-113(1991). RN [136] RP VARIANT YOKOHAMA PRO-32. RX PubMed=7338469; DOI=10.3109/03630268108991834; RA Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Hino S., RA Matsumoto N.; RT "A new unstable hemoglobin, Hb Yokohama beta 31 (B13)Leu substituting for RT Pro, causing hemolytic anemia."; RL Hemoglobin 5:667-678(1981). RN [137] RP INVOLVEMENT IN HEIBAN, AND VARIANT HAMMERSMITH SER-43. RX PubMed=6259091; DOI=10.3109/03630268108996914; RA Rahbar S., Feagler R.J., Beutler E.; RT "Hemoglobin Hammersmith (beta 42 (CD1) Phe replaced by Ser) associated with RT severe hemolytic anemia."; RL Hemoglobin 5:97-105(1981). RN [138] RP INVOLVEMENT IN HEIBAN, AND VARIANTS BRUXELLES PHE-42 DEL AND PHE-43 DEL. RX PubMed=2599881; DOI=10.3109/03630268908998085; RA Blouquit Y., Bardakdjian J., Lena-Russo D., Arous N., Perrimond H., RA Orsini A., Rosa J., Galacteros F.; RT "Hb Bruxelles: alpha 2A beta (2)41 or 42(C7 or CD1)Phe deleted."; RL Hemoglobin 13:465-474(1989). RN [139] RP VARIANT ZENGCHENG MET-115. RX PubMed=2079435; DOI=10.3109/03630269009005808; RA Plaseska D., Wilson J.B., Gu L.H., Kutlar F., Huisman T.H.J., Zeng Y.T., RA Shen M.; RT "Hb Zengcheng or alpha 2 beta(2)114(G16)Leu-->Met."; RL Hemoglobin 14:555-557(1990). RN [140] RP VARIANT BECKMAN ASP-136. RA Rahbar S., Lee T., Asmeron Y.; RT "Hb Beckman alpha135 (H13) ala-to-glu: a new unstable variant and reduced RT oxygen affinity."; RL Blood 78:204A-204A(1991). RN [141] RP VARIANT NON-SPHEROCYTIC HAEMOLITIC ANEMIA GLY-68. RX PubMed=8280608; DOI=10.1111/j.1365-2141.1993.tb03178.x; RA Fay K.C., Brennan S.O., Costello J.M., Potter H.C., Williamson D.A., RA Trent R.J., Ockelford P.A., Boswell D.R.; RT "Haemoglobin Manukau beta 67[E11] Val-->Gly: transfusion-dependent RT haemolytic anaemia ameliorated by coexisting alpha thalassaemia."; RL Br. J. Haematol. 85:352-355(1993). RN [142] RP INVOLVEMENT IN HEIBAN, AND VARIANT BRISTOL ASP-68. RX PubMed=8704193; RA Rees D.C., Rochette J., Schofield C., Green B., Morris M., Parker N.E., RA Sasaki H., Tanaka A., Ohba Y., Clegg J.B.; RT "A novel silent posttranslational mechanism converts methionine to RT aspartate in hemoglobin Bristol (beta 67[E11] Val-Met->Asp)."; RL Blood 88:341-348(1996). RN [143] RP VARIANT IRAQ-HALABJA VAL-11. RX PubMed=10398311; RX DOI=10.1002/(sici)1096-8652(199907)61:3<187::aid-ajh5>3.0.co;2-7; RA Deutsch S., Darbellay R., Offord R.E., Frutiger A., Kister J., Wajcman H., RA Beris P.; RT "Hb Iraq-Halabja beta10 (A7) Ala-->Val (GCC-->GTC): a new beta-chain silent RT variant in a family with multiple Hb disorders."; RL Am. J. Hematol. 61:187-193(1999). RN [144] RP VARIANT VILLEJUIF ILE-124. RX PubMed=11300351; DOI=10.1081/hem-100103071; RA Carbone V., Salzano A.M., Pagano L., Buffardi S., De Rosa C., Pucci P.; RT "Identification of Hb Villejuif [beta123(H1)Thr-->Ile] in Southern Italy."; RL Hemoglobin 25:67-78(2001). RN [145] RP VARIANT TSUKUMI TYR-118. RX PubMed=11300344; DOI=10.1081/hem-100103076; RA North M.L., Duwig I., Riou J., Prome D., Yapo A.P., Kister J., RA Bardakdjian-Michau J., Cazenave J.-P., Wajcman H.; RT "Hb Tsukumi [beta117(G19)His-->Tyr] found in a Moroccan woman."; RL Hemoglobin 25:107-110(2001). RN [146] RP VARIANT CANTERBURY PHE-113. RX PubMed=11939514; DOI=10.1081/hem-120002942; RA Brennan S.O., Potter H.C., Kubala L.M., Carnoutsos S.A., Ferguson M.M.; RT "Hb Canterbury [beta112(G14)Cys-->Phe]: a new, mildly unstable variant."; RL Hemoglobin 26:67-69(2002). RN [147] RP VARIANT PYRGOS ASP-84, AND VARIANT B-THAL LYS-27. RX PubMed=12144064; DOI=10.1081/hem-120005459; RA Sawangareetrakul P., Svasti S., Yodsowon B., Winichagoon P., Srisomsap C., RA Svasti J., Fucharoen S.; RT "Double heterozygosity for Hb Pyrgos [beta83(EF7)Gly-->Asp] and Hb E RT [beta26(B8)Glu-->Lys] found in association with alpha-thalassemia."; RL Hemoglobin 26:191-196(2002). RN [148] RP VARIANT SANTANDER ASP-35. RX PubMed=12603091; DOI=10.1081/hem-120016378; RA Villegas A., Ropero P., Nogales A., Gonzalez F.A., Mateo M., Mazo E., RA Rodrigo E., Arias M.; RT "Hb Santander [beta34(B16)Val-->Asp (GTC-->GAC)]: a new unstable variant RT found as a de novo mutation in a Spanish patient."; RL Hemoglobin 27:31-35(2003). RN [149] RP VARIANT NANTES LEU-35, AND VARIANT VEXIN LEU-117. RX PubMed=12908805; DOI=10.1081/hem-120023384; RA Wajcman H., Bardakdjian-Michau J., Riou J., Prehu C., Kister J., RA Baudin-Creuza V., Prome D., Richelme-David S., Harousseau J.L., RA Galacteros F.; RT "Two new hemoglobin variants with increased oxygen affinity: Hb Nantes RT [beta34(B16)Val-->Leu] and Hb Vexin [beta116(G18)His-->Leu]."; RL Hemoglobin 27:191-199(2003). RN [150] RP VARIANT B-THAL LYS-27. RX PubMed=15481886; DOI=10.1081/hem-120040334; RA Flatz G., Sanguansermsri T., Sengchanh S., Horst D., Horst J.; RT "The 'hot-spot' of Hb E [beta26(B8)Glu-->Lys] in Southeast Asia: beta- RT globin anomalies in the Lao Theung population of southern Laos."; RL Hemoglobin 28:197-204(2004). RN [151] RP VARIANT BECKMAN ASP-136. RX PubMed=19453576; DOI=10.1111/j.1751-553x.2009.01156.x; RA Kim S.Y., Kim G.Y., Jo S.A., Lee E.H., Cho E.H., Hwang S.H., Lee E.Y.; RT "A novel hemoglobin variant beta135(H13) Ala > Asp identified in an RT asymptomatic Korean family by direct sequencing: suggesting a new insight RT into Hb Beckman mutation."; RL Int. J. Lab. Hematol. 32:E175-E178(2010). RN [152] RP VARIANT BECKMAN ASP-136, AND MASS SPECTROMETRY. RX PubMed=26209877; DOI=10.1016/j.ab.2015.07.010; RA Das R., Muralidharan M., Mitra G., Bhat V., Mathew B., Pal D., Ross C., RA Mandal A.K.; RT "Mass spectrometry based characterization of Hb Beckman variant in a RT falsely elevated HbA(1c) sample."; RL Anal. Biochem. 489:53-58(2015). RN [153] RP VARIANT VIGO ILE-67, AND FUNCTION. RX PubMed=28066926; DOI=10.1002/ajh.24649; RA Manu Pereira M.D., Ropero P., Loureiro C., Vives Corrons J.L.; RT "Low affinity hemoglobinopathy (Hb Vigo) due to a new mutation of beta RT globin gene (c200 A>T; Lys>Ile). A cause of rare anemia misdiagnosis."; RL Am. J. Hematol. 92:38-40(2017). CC -!- FUNCTION: Involved in oxygen transport from the lung to the various CC peripheral tissues. {ECO:0000269|PubMed:28066926}. CC -!- FUNCTION: LVV-hemorphin-7 potentiates the activity of bradykinin, CC causing a decrease in blood pressure. CC -!- FUNCTION: [Spinorphin]: Functions as an endogenous inhibitor of CC enkephalin-degrading enzymes such as DPP3, and as a selective CC antagonist of the P2RX3 receptor which is involved in pain signaling, CC these properties implicate it as a regulator of pain and inflammation. CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in CC adult hemoglobin A (HbA). Heterotetramer of two zeta chains and two CC beta chains in hemoglobin Portland-2, detected in fetuses and neonates CC with homozygous alpha-thalassemia. {ECO:0000269|PubMed:11747442, CC ECO:0000269|PubMed:24100324, ECO:0000269|PubMed:6539334}. CC -!- INTERACTION: CC P68871; P69905: HBA2; NbExp=29; IntAct=EBI-715554, EBI-714680; CC P68871; Q6B0K9: HBM; NbExp=3; IntAct=EBI-715554, EBI-12805802; CC P68871; P09105: HBQ1; NbExp=3; IntAct=EBI-715554, EBI-10193656; CC P68871; P02008: HBZ; NbExp=7; IntAct=EBI-715554, EBI-719843; CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000269|PubMed:6539334}. CC -!- PTM: Glucose reacts non-enzymatically with the N-terminus of the beta CC chain to form a stable ketoamine linkage. This takes place slowly and CC continuously throughout the 120-day life span of the red blood cell. CC The rate of glycation is increased in patients with diabetes mellitus. CC -!- PTM: S-nitrosylated; a nitric oxide group is first bound to Fe(2+) and CC then transferred to Cys-94 to allow capture of O(2). CC {ECO:0000269|PubMed:1520632, ECO:0000269|PubMed:8637569, CC ECO:0000269|PubMed:9843411}. CC -!- PTM: Acetylated on Lys-60, Lys-83 and Lys-145 upon aspirin exposure. CC {ECO:0000269|PubMed:4531009}. CC -!- MASS SPECTROMETRY: [LVV-hemorphin-7]: Mass=1310; Method=FAB; CC Evidence={ECO:0000269|PubMed:1575724}; CC -!- POLYMORPHISM: Genetic variations in HBB are involved in resistance to CC malaria [MIM:611162]. Hemoglobin S (Hb S), which at homozygosity is CC responsible for sickle cell anemia, is not associated with any clinical CC abnormality when heterozygous. At heterozygosity, Hb S confers an CC increase in protection from life-threatening malaria. Additional CC variants conferring resistance against severe malaria are hemoglobin C CC (Hb C) and hemoglobin E (Hb E). {ECO:0000269|PubMed:11001883, CC ECO:0000269|PubMed:12149194, ECO:0000269|PubMed:16001361}. 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:186485, CC ECO:0000269|PubMed:2599881, ECO:0000269|PubMed:6259091, CC ECO:0000269|PubMed:8704193}. Note=The disease may be caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Beta-thalassemia (B-THAL) [MIM:613985]: A form of thalassemia. CC Thalassemias are common monogenic diseases occurring mostly in CC Mediterranean and Southeast Asian populations. The hallmark of beta- CC thalassemia is an imbalance in globin-chain production in the adult HbA CC molecule. Absence of beta chain causes beta(0)-thalassemia, while CC reduced amounts of detectable beta globin causes beta(+)-thalassemia. CC In the severe forms of beta-thalassemia, the excess alpha globin chains CC accumulate in the developing erythroid precursors in the marrow. Their CC deposition leads to a vast increase in erythroid apoptosis that in turn CC causes ineffective erythropoiesis and severe microcytic hypochromic CC anemia. Clinically, beta-thalassemia is divided into thalassemia major CC which is transfusion dependent, thalassemia intermedia (of intermediate CC severity), and thalassemia minor that is asymptomatic. CC {ECO:0000269|PubMed:12144064, ECO:0000269|PubMed:12149194, CC ECO:0000269|PubMed:15481886, ECO:0000269|PubMed:2399911, CC ECO:0000269|PubMed:6166632, ECO:0000269|PubMed:7693620}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Sickle cell disease (SKCA) [MIM:603903]: Characterized by CC abnormally shaped red cells resulting in chronic anemia and periodic CC episodes of pain, serious infections and damage to vital organs. Normal CC red blood cells are round and flexible and flow easily through blood CC vessels, but in sickle cell anemia, the abnormal hemoglobin (called Hb CC S) causes red blood cells to become stiff. They are C-shaped and CC resembles a sickle. These stiffer red blood cells can led to CC microvascular occlusion thus cutting off the blood supply to nearby CC tissues. {ECO:0000269|PubMed:1195378, ECO:0000269|PubMed:13464827, CC ECO:0000269|PubMed:16001361, ECO:0000269|PubMed:24100324, CC ECO:0000269|Ref.10}. Note=The disease is caused by variants affecting CC the gene represented in this entry. CC -!- DISEASE: Beta-thalassemia, dominant, inclusion body type (B-THALIB) CC [MIM:603902]: An autosomal dominant form of beta thalassemia CC characterized by moderate anemia, lifelong jaundice, cholelithiasis and CC splenomegaly, marked morphologic changes in the red cells, erythroid CC hyperplasia of the bone marrow with increased numbers of multinucleate CC red cell precursors, and the presence of large inclusion bodies in the CC normoblasts, both in the marrow and in the peripheral blood after CC splenectomy. {ECO:0000269|PubMed:1971109}. Note=The disease is caused CC by variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: One molecule of 2,3-bisphosphoglycerate can bind to two CC beta chains per hemoglobin tetramer. CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE- CC ProRule:PRU00238}. CC -!- CAUTION: The modification form of Leu-142 is subject of controversy and CC could be the artifactual result of sample handling. CC {ECO:0000305|PubMed:1520632}. CC -!- CAUTION: It is unclear if hemoglobin Beckman (Hb Beckman) is defined by CC p.Ala136Glu or p.Ala136Asp. Hb Beckman has been originally identified CC by reverse phase-HPLC and tandem mass spectrometry, and has been CC reported as variant p.Ala136Glu (Ref.140). Subsequently, variant CC p.Ala136Asp has been reported based on HBB gene complete sequencing CC results (PubMed:19453576). Variant p.Ala136Asp has also been detected CC by mass spectrometry (PubMed:26209877). Although the name Hb Beckman is CC currently used for variant p.Ala136Asp, it cannot be ruled out that Hb CC Beckman is indeed variant p.Ala136Glu (PubMed:19453576). CC {ECO:0000269|PubMed:19453576, ECO:0000269|PubMed:26209877, CC ECO:0000269|Ref.140, ECO:0000303|PubMed:19453576}. 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=HBB"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Hemoglobin entry; CC URL="https://en.wikipedia.org/wiki/Hemoglobin"; 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; M25079; AAA35597.1; -; mRNA. DR EMBL; V00499; CAA23758.1; -; Genomic_DNA. DR EMBL; DQ126270; AAZ39745.1; -; Genomic_DNA. DR EMBL; DQ126271; AAZ39746.1; -; Genomic_DNA. DR EMBL; DQ126272; AAZ39747.1; -; Genomic_DNA. DR EMBL; DQ126273; AAZ39748.1; -; Genomic_DNA. DR EMBL; DQ126274; AAZ39749.1; -; Genomic_DNA. DR EMBL; DQ126275; AAZ39750.1; -; Genomic_DNA. DR EMBL; DQ126276; AAZ39751.1; -; Genomic_DNA. DR EMBL; DQ126277; AAZ39752.1; -; Genomic_DNA. DR EMBL; DQ126278; AAZ39753.1; -; Genomic_DNA. DR EMBL; DQ126279; AAZ39754.1; -; Genomic_DNA. DR EMBL; DQ126280; AAZ39755.1; -; Genomic_DNA. DR EMBL; DQ126281; AAZ39756.1; -; Genomic_DNA. DR EMBL; DQ126282; AAZ39757.1; -; Genomic_DNA. DR EMBL; DQ126283; AAZ39758.1; -; Genomic_DNA. DR EMBL; DQ126284; AAZ39759.1; -; Genomic_DNA. DR EMBL; DQ126285; AAZ39760.1; -; Genomic_DNA. DR EMBL; DQ126286; AAZ39761.1; -; Genomic_DNA. DR EMBL; DQ126287; AAZ39762.1; -; Genomic_DNA. DR EMBL; DQ126288; AAZ39763.1; -; Genomic_DNA. DR EMBL; DQ126289; AAZ39764.1; -; Genomic_DNA. DR EMBL; DQ126290; AAZ39765.1; -; Genomic_DNA. DR EMBL; DQ126291; AAZ39766.1; -; Genomic_DNA. DR EMBL; DQ126292; AAZ39767.1; -; Genomic_DNA. DR EMBL; DQ126293; AAZ39768.1; -; Genomic_DNA. DR EMBL; DQ126294; AAZ39769.1; -; Genomic_DNA. DR EMBL; DQ126295; AAZ39770.1; -; Genomic_DNA. DR EMBL; DQ126296; AAZ39771.1; -; Genomic_DNA. DR EMBL; DQ126297; AAZ39772.1; -; Genomic_DNA. DR EMBL; DQ126298; AAZ39773.1; -; Genomic_DNA. DR EMBL; DQ126299; AAZ39774.1; -; Genomic_DNA. DR EMBL; DQ126300; AAZ39775.1; -; Genomic_DNA. DR EMBL; DQ126301; AAZ39776.1; -; Genomic_DNA. DR EMBL; DQ126302; AAZ39777.1; -; Genomic_DNA. DR EMBL; DQ126303; AAZ39778.1; -; Genomic_DNA. DR EMBL; DQ126304; AAZ39779.1; -; Genomic_DNA. DR EMBL; DQ126305; AAZ39780.1; -; Genomic_DNA. DR EMBL; DQ126306; AAZ39781.1; -; Genomic_DNA. DR EMBL; DQ126307; AAZ39782.1; -; Genomic_DNA. DR EMBL; DQ126308; AAZ39783.1; -; Genomic_DNA. DR EMBL; DQ126309; AAZ39784.1; -; Genomic_DNA. DR EMBL; DQ126310; AAZ39785.1; -; Genomic_DNA. DR EMBL; DQ126311; AAZ39786.1; -; Genomic_DNA. DR EMBL; DQ126312; AAZ39787.1; -; Genomic_DNA. DR EMBL; DQ126313; AAZ39788.1; -; Genomic_DNA. DR EMBL; DQ126314; AAZ39789.1; -; Genomic_DNA. DR EMBL; DQ126315; AAZ39790.1; -; Genomic_DNA. DR EMBL; DQ126316; AAZ39791.1; -; Genomic_DNA. DR EMBL; DQ126317; AAZ39792.1; -; Genomic_DNA. DR EMBL; DQ126318; AAZ39793.1; -; Genomic_DNA. DR EMBL; DQ126319; AAZ39794.1; -; Genomic_DNA. DR EMBL; DQ126320; AAZ39795.1; -; Genomic_DNA. DR EMBL; DQ126321; AAZ39796.1; -; Genomic_DNA. DR EMBL; DQ126322; AAZ39797.1; -; Genomic_DNA. DR EMBL; DQ126323; AAZ39798.1; -; Genomic_DNA. DR EMBL; DQ126324; AAZ39799.1; -; Genomic_DNA. DR EMBL; DQ126325; AAZ39800.1; -; Genomic_DNA. DR EMBL; AF007546; AAB62944.1; -; Genomic_DNA. DR EMBL; AF083883; AAL68978.1; -; Genomic_DNA. DR EMBL; AF117710; AAD19696.1; -; mRNA. DR EMBL; AF181989; AAF00489.1; -; mRNA. DR EMBL; AF349114; AAK29639.1; -; mRNA. DR EMBL; AF527577; AAM92001.1; -; Genomic_DNA. DR EMBL; AY136510; AAN11320.1; -; mRNA. DR EMBL; AY163866; AAN84548.1; -; Genomic_DNA. DR EMBL; AY260740; AAP21062.1; -; Genomic_DNA. DR EMBL; AY509193; AAR96398.1; -; mRNA. DR EMBL; EF450778; ABO36678.1; -; Genomic_DNA. DR EMBL; EU694432; ACD39349.1; -; mRNA. DR EMBL; AK311825; BAG34767.1; -; mRNA. DR EMBL; CR536530; CAG38767.1; -; mRNA. DR EMBL; CR541913; CAG46711.1; -; mRNA. DR EMBL; CH471064; EAW68806.1; -; Genomic_DNA. DR EMBL; BC007075; AAH07075.1; -; mRNA. DR EMBL; U01317; AAA16334.1; -; Genomic_DNA. DR EMBL; V00497; CAA23756.1; -; mRNA. DR EMBL; V00500; CAA23759.1; ALT_SEQ; mRNA. DR EMBL; L26462; AAA21100.1; -; Genomic_DNA. DR EMBL; L26463; AAA21101.1; -; Genomic_DNA. DR EMBL; L26464; AAA21102.1; -; Genomic_DNA. DR EMBL; L26465; AAA21103.1; -; Genomic_DNA. DR EMBL; L26466; AAA21104.1; -; Genomic_DNA. DR EMBL; L26467; AAA21105.1; -; Genomic_DNA. DR EMBL; L26468; AAA21106.1; -; Genomic_DNA. DR EMBL; L26469; AAA21107.1; -; Genomic_DNA. DR EMBL; L26470; AAA21108.1; -; Genomic_DNA. DR EMBL; L26471; AAA21109.1; -; Genomic_DNA. DR EMBL; L26472; AAA21110.1; -; Genomic_DNA. DR EMBL; L26473; AAA21111.1; -; Genomic_DNA. DR EMBL; L26474; AAA21112.1; -; Genomic_DNA. DR EMBL; L26475; AAA21113.1; -; Genomic_DNA. DR EMBL; L26476; AAA21114.1; -; Genomic_DNA. DR EMBL; L26477; AAA21115.1; -; Genomic_DNA. DR EMBL; L26478; AAA21116.1; -; Genomic_DNA. DR EMBL; L48213; AAA88063.1; -; Genomic_DNA. DR EMBL; L48214; AAA88061.1; -; Genomic_DNA. DR EMBL; L48215; AAA88059.1; -; Genomic_DNA. DR EMBL; L48216; AAA88065.1; -; Genomic_DNA. DR EMBL; L48217; AAA88067.1; -; Genomic_DNA. DR EMBL; M36640; AAA52634.1; -; Genomic_DNA. DR EMBL; M11428; AAA52633.1; -; mRNA. DR EMBL; M25113; AAA35966.1; -; mRNA. DR EMBL; L48932; AAA88054.1; -; Genomic_DNA. DR CCDS; CCDS7753.1; -. DR PIR; A53136; HBHU. DR RefSeq; NP_000509.1; NM_000518.4. DR PDB; 1A00; X-ray; 2.00 A; B/D=3-147. DR PDB; 1A01; X-ray; 1.80 A; B/D=3-147. DR PDB; 1A0U; X-ray; 2.14 A; B/D=3-147. DR PDB; 1A0Z; X-ray; 2.00 A; B/D=3-147. DR PDB; 1A3N; X-ray; 1.80 A; B/D=2-147. DR PDB; 1A3O; X-ray; 1.80 A; B/D=2-147. DR PDB; 1ABW; X-ray; 2.00 A; B/D=3-147. DR PDB; 1ABY; X-ray; 2.60 A; B/D=3-147. DR PDB; 1AJ9; X-ray; 2.20 A; B=2-147. DR PDB; 1B86; X-ray; 2.50 A; B/D=2-147. DR PDB; 1BAB; X-ray; 1.50 A; B/D=2-147. DR PDB; 1BBB; X-ray; 1.70 A; B/D=2-147. DR PDB; 1BIJ; X-ray; 2.30 A; B/D=2-147. DR PDB; 1BUW; X-ray; 1.90 A; B/D=2-147. DR PDB; 1BZ0; X-ray; 1.50 A; B/D=2-147. DR PDB; 1BZ1; X-ray; 1.59 A; B/D=2-147. DR PDB; 1BZZ; X-ray; 1.59 A; B/D=2-147. DR PDB; 1C7B; X-ray; 1.80 A; B/D=2-147. DR PDB; 1C7C; X-ray; 1.80 A; B/D=2-147. DR PDB; 1C7D; X-ray; 1.80 A; B/D=2-147. DR PDB; 1CBL; X-ray; 1.80 A; A/B/C/D=2-147. DR PDB; 1CBM; X-ray; 1.74 A; A/B/C/D=2-147. DR PDB; 1CH4; X-ray; 2.50 A; A/B/C/D=2-146. DR PDB; 1CLS; X-ray; 1.90 A; B/D=2-147. DR PDB; 1CMY; X-ray; 3.00 A; B/D=2-147. DR PDB; 1COH; X-ray; 2.90 A; B/D=2-147. DR PDB; 1DKE; X-ray; 2.10 A; B/D=2-147. DR PDB; 1DXT; X-ray; 1.70 A; B/D=1-147. DR PDB; 1DXU; X-ray; 1.70 A; B/D=3-147. DR PDB; 1DXV; X-ray; 1.70 A; B/D=3-147. DR PDB; 1FN3; X-ray; 2.48 A; B/D=2-147. DR PDB; 1G9V; X-ray; 1.85 A; B/D=2-147. DR PDB; 1GBU; X-ray; 1.80 A; B/D=2-147. DR PDB; 1GBV; X-ray; 2.00 A; B/D=2-147. DR PDB; 1GLI; X-ray; 2.50 A; B/D=3-147. DR PDB; 1GZX; X-ray; 2.10 A; B/D=2-147. DR PDB; 1HAB; X-ray; 2.30 A; B/D=2-147. DR PDB; 1HAC; X-ray; 2.60 A; B/D=2-147. DR PDB; 1HBA; X-ray; 2.10 A; B/D=2-147. DR PDB; 1HBB; X-ray; 1.90 A; B/D=2-147. DR PDB; 1HBS; X-ray; 3.00 A; B/D/F/H=2-147. DR PDB; 1HCO; X-ray; 2.70 A; B=2-147. DR PDB; 1HDB; X-ray; 2.20 A; B/D=2-147. DR PDB; 1HGA; X-ray; 2.10 A; B/D=2-147. DR PDB; 1HGB; X-ray; 2.10 A; B/D=2-147. DR PDB; 1HGC; X-ray; 2.10 A; B/D=2-147. DR PDB; 1HHO; X-ray; 2.10 A; B=2-147. DR PDB; 1IRD; X-ray; 1.25 A; B=2-147. DR PDB; 1J3Y; X-ray; 1.55 A; B/D/F/H=2-147. DR PDB; 1J3Z; X-ray; 1.60 A; B/D/F/H=2-147. DR PDB; 1J40; X-ray; 1.45 A; B/D/F/H=2-147. DR PDB; 1J41; X-ray; 1.45 A; B/D/F/H=2-147. DR PDB; 1J7S; X-ray; 2.20 A; B/D=2-147. DR PDB; 1J7W; X-ray; 2.00 A; B/D=2-147. DR PDB; 1J7Y; X-ray; 1.70 A; B/D=2-147. DR PDB; 1JY7; X-ray; 3.20 A; B/D/Q/S/V/X=2-147. DR PDB; 1K0Y; X-ray; 1.87 A; B/D=2-147. DR PDB; 1K1K; X-ray; 2.00 A; B=2-147. DR PDB; 1KD2; X-ray; 1.87 A; B/D=2-147. DR PDB; 1LFL; X-ray; 2.70 A; B/D/Q/S=2-147. DR PDB; 1LFQ; X-ray; 2.60 A; B=2-147. DR PDB; 1LFT; X-ray; 2.60 A; B=2-147. DR PDB; 1LFV; X-ray; 2.80 A; B=2-147. DR PDB; 1LFY; X-ray; 3.30 A; B=2-147. DR PDB; 1LFZ; X-ray; 3.10 A; B=2-147. DR PDB; 1LJW; X-ray; 2.16 A; B=2-147. DR PDB; 1M9P; X-ray; 2.10 A; B/D=2-147. DR PDB; 1MKO; X-ray; 2.18 A; B/D=2-147. DR PDB; 1NEJ; X-ray; 2.10 A; B/D=2-147. DR PDB; 1NIH; X-ray; 2.60 A; B/D=2-147. DR PDB; 1NQP; X-ray; 1.73 A; B/D=2-147. DR PDB; 1O1I; X-ray; 2.30 A; B=2-147. DR PDB; 1O1J; X-ray; 1.90 A; B/D=2-147. DR PDB; 1O1K; X-ray; 2.00 A; B/D=2-147. DR PDB; 1O1L; X-ray; 1.80 A; B/D=2-147. DR PDB; 1O1M; X-ray; 1.85 A; B/D=2-147. DR PDB; 1O1N; X-ray; 1.80 A; B/D=2-147. DR PDB; 1O1O; X-ray; 1.80 A; B/D=2-147. DR PDB; 1O1P; X-ray; 1.80 A; B/D=2-147. DR PDB; 1QI8; X-ray; 1.80 A; B/D=3-147. DR PDB; 1QSH; X-ray; 1.70 A; B/D=2-147. DR PDB; 1QSI; X-ray; 1.70 A; B/D=2-147. DR PDB; 1QXD; X-ray; 2.25 A; B/D=2-147. DR PDB; 1QXE; X-ray; 1.85 A; B/D=2-147. DR PDB; 1R1X; X-ray; 2.15 A; B=2-147. DR PDB; 1R1Y; X-ray; 1.80 A; B/D=2-147. DR PDB; 1RPS; X-ray; 2.11 A; B/D=2-147. DR PDB; 1RQ3; X-ray; 1.91 A; B/D=2-147. DR PDB; 1RQ4; X-ray; 2.11 A; B/D=2-147. DR PDB; 1RQA; X-ray; 2.11 A; B/D=2-147. DR PDB; 1RVW; X-ray; 2.50 A; B=2-147. DR PDB; 1SDK; X-ray; 1.80 A; B/D=2-147. DR PDB; 1SDL; X-ray; 1.80 A; B/D=2-147. DR PDB; 1THB; X-ray; 1.50 A; B/D=2-147. DR PDB; 1UIW; X-ray; 1.50 A; B/D/F/H=2-147. DR PDB; 1VWT; X-ray; 1.90 A; B/D=2-147. DR PDB; 1XXT; X-ray; 1.91 A; B/D=2-147. DR PDB; 1XY0; X-ray; 1.99 A; B/D=2-147. DR PDB; 1XYE; X-ray; 2.13 A; B/D=2-147. DR PDB; 1XZ2; X-ray; 1.90 A; B/D=2-147. DR PDB; 1XZ4; X-ray; 2.00 A; B/D=2-147. DR PDB; 1XZ5; X-ray; 2.11 A; B/D=2-147. DR PDB; 1XZ7; X-ray; 1.90 A; B/D=2-147. DR PDB; 1XZU; X-ray; 2.16 A; B/D=2-147. DR PDB; 1XZV; X-ray; 2.11 A; B/D=2-147. DR PDB; 1Y09; X-ray; 2.25 A; B/D=2-147. DR PDB; 1Y0A; X-ray; 2.22 A; B/D=2-147. DR PDB; 1Y0C; X-ray; 2.30 A; B/D=2-147. DR PDB; 1Y0D; X-ray; 2.10 A; B/D=2-147. DR PDB; 1Y0T; X-ray; 2.14 A; B/D=2-147. DR PDB; 1Y0W; X-ray; 2.14 A; B/D=2-147. DR PDB; 1Y22; X-ray; 2.16 A; B/D=2-147. DR PDB; 1Y2Z; X-ray; 2.07 A; B/D=2-147. DR PDB; 1Y31; X-ray; 2.13 A; B/D=2-147. DR PDB; 1Y35; X-ray; 2.12 A; B/D=2-147. DR PDB; 1Y45; X-ray; 2.00 A; B/D=2-147. DR PDB; 1Y46; X-ray; 2.22 A; B/D=2-147. DR PDB; 1Y4B; X-ray; 2.10 A; B/D=2-147. DR PDB; 1Y4F; X-ray; 2.00 A; B/D=2-147. DR PDB; 1Y4G; X-ray; 1.91 A; B/D=2-147. DR PDB; 1Y4P; X-ray; 1.98 A; B/D=2-147. DR PDB; 1Y4Q; X-ray; 2.11 A; B/D=2-147. DR PDB; 1Y4R; X-ray; 2.22 A; B/D=2-147. DR PDB; 1Y4V; X-ray; 1.84 A; B/D=2-147. DR PDB; 1Y5F; X-ray; 2.14 A; B/D=2-147. DR PDB; 1Y5J; X-ray; 2.03 A; B/D=2-147. DR PDB; 1Y5K; X-ray; 2.20 A; B/D=2-147. DR PDB; 1Y7C; X-ray; 2.10 A; B/D=2-147. DR PDB; 1Y7D; X-ray; 1.90 A; B/D=2-147. DR PDB; 1Y7G; X-ray; 2.10 A; B/D=2-147. DR PDB; 1Y7Z; X-ray; 1.98 A; B/D=2-147. DR PDB; 1Y83; X-ray; 1.90 A; B/D=2-145. DR PDB; 1Y85; X-ray; 2.13 A; B/D=2-146. DR PDB; 1Y8W; X-ray; 2.90 A; B/D=2-147. DR PDB; 1YDZ; X-ray; 3.30 A; B/D=2-147. DR PDB; 1YE0; X-ray; 2.50 A; B/D=2-147. DR PDB; 1YE1; X-ray; 4.50 A; B/D=2-147. DR PDB; 1YE2; X-ray; 1.80 A; B/D=2-147. DR PDB; 1YEN; X-ray; 2.80 A; B/D=2-147. DR PDB; 1YEO; X-ray; 2.22 A; B/D=2-147. DR PDB; 1YEQ; X-ray; 2.75 A; B/D=2-147. DR PDB; 1YEU; X-ray; 2.12 A; B/D=2-147. DR PDB; 1YEV; X-ray; 2.11 A; B/D=2-147. DR PDB; 1YFF; X-ray; 2.40 A; B/D/F/H=2-147. DR PDB; 1YG5; X-ray; 2.70 A; B/D=2-147. DR PDB; 1YGD; X-ray; 2.73 A; B/D=2-147. DR PDB; 1YGF; X-ray; 2.70 A; B/D=2-147. DR PDB; 1YH9; X-ray; 2.20 A; B/D=2-147. DR PDB; 1YHE; X-ray; 2.10 A; B/D=2-147. DR PDB; 1YHR; X-ray; 2.60 A; B/D=2-147. DR PDB; 1YIE; X-ray; 2.40 A; B/D=2-147. DR PDB; 1YIH; X-ray; 2.00 A; B/D=2-147. DR PDB; 1YVQ; X-ray; 1.80 A; B/D=2-147. DR PDB; 1YVT; X-ray; 1.80 A; B=2-147. DR PDB; 1YZI; X-ray; 2.07 A; B=2-147. DR PDB; 2D5Z; X-ray; 1.45 A; B/D=2-147. DR PDB; 2D60; X-ray; 1.70 A; B/D=2-147. DR PDB; 2DN1; X-ray; 1.25 A; B=2-147. DR PDB; 2DN2; X-ray; 1.25 A; B/D=2-147. DR PDB; 2DN3; X-ray; 1.25 A; B=2-147. DR PDB; 2DXM; Neutron; 2.10 A; B/D=2-147. DR PDB; 2H35; NMR; -; B/D=2-147. DR PDB; 2HBC; X-ray; 2.10 A; B=2-147. DR PDB; 2HBD; X-ray; 2.20 A; B=2-147. DR PDB; 2HBE; X-ray; 2.00 A; B=2-147. DR PDB; 2HBF; X-ray; 2.20 A; B=2-147. DR PDB; 2HBS; X-ray; 2.05 A; B/D/F/H=2-147. DR PDB; 2HCO; X-ray; 2.70 A; B=2-147. DR PDB; 2HHB; X-ray; 1.74 A; B/D=2-147. DR PDB; 2HHD; X-ray; 2.20 A; B/D=2-147. DR PDB; 2HHE; X-ray; 2.20 A; B/D=4-147. DR PDB; 2M6Z; NMR; -; B/D=2-147. DR PDB; 2W6V; X-ray; 1.80 A; B/D=2-147. DR PDB; 2W72; X-ray; 1.07 A; B/D=3-147. DR PDB; 2YRS; X-ray; 2.30 A; B/D/K/O=2-147. DR PDB; 3B75; X-ray; 2.30 A; B/D/F/H/T=2-147. DR PDB; 3D17; X-ray; 2.80 A; B/D=2-147. DR PDB; 3D7O; X-ray; 1.80 A; B=2-147. DR PDB; 3DUT; X-ray; 1.55 A; B/D=2-147. DR PDB; 3HHB; X-ray; 1.74 A; B/D=2-147. DR PDB; 3HXN; X-ray; 2.00 A; B/D=2-147. DR PDB; 3IC0; X-ray; 1.80 A; B/D=2-147. DR PDB; 3IC2; X-ray; 2.40 A; B/D=2-147. DR PDB; 3KMF; Neutron; 2.00 A; C/G=2-147. DR PDB; 3NL7; X-ray; 1.80 A; B=2-147. DR PDB; 3NMM; X-ray; 1.60 A; B/D=2-147. DR PDB; 3ODQ; X-ray; 3.10 A; B/D=2-147. DR PDB; 3ONZ; X-ray; 2.09 A; B=2-147. DR PDB; 3OO4; X-ray; 1.90 A; B=2-147. DR PDB; 3OO5; X-ray; 2.10 A; B=2-147. DR PDB; 3P5Q; X-ray; 2.00 A; B=2-147. DR PDB; 3QJB; X-ray; 1.80 A; B=2-147. DR PDB; 3QJC; X-ray; 2.00 A; B=2-147. DR PDB; 3QJD; X-ray; 1.56 A; B/D=2-147. DR PDB; 3QJE; X-ray; 1.80 A; B/D=2-147. DR PDB; 3R5I; X-ray; 2.20 A; B/D=2-147. DR PDB; 3S65; X-ray; 1.80 A; B/D=2-147. DR PDB; 3S66; X-ray; 1.40 A; B=2-147. DR PDB; 3SZK; X-ray; 3.01 A; B/E=2-147. DR PDB; 3W4U; X-ray; 1.95 A; B/D/F=2-147. DR PDB; 3WCP; X-ray; 1.94 A; B/D=2-147. DR PDB; 3WHM; X-ray; 1.85 A; B/F=2-147. DR PDB; 4FC3; X-ray; 2.26 A; B=2-147. DR PDB; 4HHB; X-ray; 1.74 A; B/D=2-147. DR PDB; 4IJ2; X-ray; 4.24 A; B/D=2-147. DR PDB; 4L7Y; X-ray; 1.80 A; B/D=2-147. DR PDB; 4M4A; X-ray; 2.05 A; B=2-147. DR PDB; 4M4B; X-ray; 2.00 A; B=2-147. DR PDB; 4MQC; X-ray; 2.20 A; B=2-147. DR PDB; 4MQG; X-ray; 1.68 A; B=2-147. DR PDB; 4MQH; X-ray; 2.50 A; B=2-147. DR PDB; 4MQI; X-ray; 1.92 A; B=2-147. DR PDB; 4N7N; X-ray; 2.75 A; B/D/F/H/J/L=2-147. DR PDB; 4N7O; X-ray; 2.50 A; B/D/F/H/J/L=2-147. DR PDB; 4N7P; X-ray; 2.81 A; B/D/F/H/J/L=2-147. DR PDB; 4N8T; X-ray; 1.90 A; B=2-147. DR PDB; 4NI0; X-ray; 2.15 A; B=2-147. DR PDB; 4NI1; X-ray; 1.90 A; B=2-147. DR PDB; 4ROL; X-ray; 1.70 A; B/D=2-147. DR PDB; 4ROM; X-ray; 1.90 A; B/D=2-147. DR PDB; 4WJG; X-ray; 3.10 A; 1/B/G/L/Q/V=2-147. DR PDB; 4X0L; X-ray; 2.05 A; B=2-147. DR PDB; 4XS0; X-ray; 2.55 A; B=2-147. DR PDB; 5E29; X-ray; 1.85 A; B/D=3-147. DR PDB; 5E6E; X-ray; 1.76 A; B=2-147. DR PDB; 5E83; X-ray; 1.80 A; B/D=2-147. DR PDB; 5EE4; X-ray; 2.30 A; D/F=2-147. DR PDB; 5HU6; X-ray; 2.90 A; B=3-143. DR PDB; 5HY8; X-ray; 2.30 A; B/D/F/H/T=2-147. DR PDB; 5JDO; X-ray; 3.20 A; D=3-147, F=3-146. DR PDB; 5KDQ; X-ray; 2.15 A; B/D=2-147. DR PDB; 5KSI; X-ray; 1.80 A; B/D=2-147. DR PDB; 5KSJ; X-ray; 2.40 A; B/D=2-147. DR PDB; 5NI1; EM; 3.20 A; B/D=2-147. DR PDB; 5SW7; X-ray; 1.85 A; B=2-147. DR PDB; 5U3I; X-ray; 1.95 A; B/D=2-147. DR PDB; 5UCU; X-ray; 1.80 A; B=2-147. DR PDB; 5UFJ; X-ray; 2.05 A; B/D=2-147. DR PDB; 5URC; X-ray; 1.85 A; B/D=2-147. DR PDB; 5VMM; X-ray; 3.60 A; B/D=2-147. DR PDB; 5WOG; X-ray; 1.54 A; C/D=2-147. DR PDB; 5WOH; X-ray; 1.58 A; B/D=2-147. DR PDB; 5X2R; X-ray; 2.70 A; B/D/F/H/J/L=2-147. DR PDB; 5X2S; X-ray; 2.39 A; B/D/F/H/J/L=2-147. DR PDB; 5X2T; X-ray; 2.64 A; B/D/F/H/J/L=2-147. DR PDB; 5X2U; X-ray; 2.53 A; B/D/F/H/J/L=2-147. DR PDB; 6BB5; X-ray; 2.28 A; B=3-147. DR PDB; 6BNR; X-ray; 1.95 A; B/D=2-147. DR PDB; 6BWP; X-ray; 1.70 A; B/D=2-147. DR PDB; 6BWU; X-ray; 2.00 A; B=2-147. DR PDB; 6DI4; X-ray; 1.90 A; B/D=2-147. DR PDB; 6FQF; X-ray; 2.10 A; A/B/C/D=2-147. DR PDB; 6HAL; X-ray; 2.20 A; B/D=3-147. DR PDB; 6HBW; X-ray; 2.00 A; B/D=2-147. DR PDB; 6HK2; X-ray; 1.55 A; B/D=2-147. DR PDB; 6KA9; X-ray; 1.40 A; B/D/F/H=2-147. DR PDB; 6KAE; X-ray; 1.45 A; B/D/F/H=2-147. DR PDB; 6KAH; X-ray; 1.45 A; B/D/F/H=2-147. DR PDB; 6KAI; X-ray; 1.45 A; B/D/F/H=2-147. DR PDB; 6KAO; X-ray; 1.40 A; B=2-147. DR PDB; 6KAP; X-ray; 1.45 A; B=2-147. DR PDB; 6KAQ; X-ray; 1.50 A; B=2-147. DR PDB; 6KAR; X-ray; 1.60 A; B=2-147. DR PDB; 6KAS; X-ray; 1.65 A; B/D=2-147. DR PDB; 6KAT; X-ray; 1.70 A; B/D=2-147. DR PDB; 6KAU; X-ray; 1.60 A; B/D=2-147. DR PDB; 6KAV; X-ray; 1.70 A; B/D=2-147. DR PDB; 6KYE; X-ray; 2.28 A; B/D/F/H/J/L=1-147. DR PDB; 6L5V; X-ray; 1.45 A; B=2-147. DR PDB; 6L5W; X-ray; 1.50 A; B=2-147. DR PDB; 6L5X; X-ray; 1.65 A; B/D=2-147. DR PDB; 6L5Y; X-ray; 1.65 A; B/D=2-147. DR PDB; 6LCW; X-ray; 1.40 A; B/D/F/H=2-147. DR PDB; 6LCX; X-ray; 1.40 A; B/D/F/H=2-147. DR PDB; 6NBC; EM; 2.80 A; B/D=2-144. DR PDB; 6NBD; EM; 3.20 A; B/D=2-144. DR PDB; 6NQ5; X-ray; 1.85 A; B=2-147. DR PDB; 6TB2; X-ray; 2.90 A; B=2-147. DR PDB; 6XD9; X-ray; 2.10 A; B/D=2-147. DR PDB; 6XDT; X-ray; 1.90 A; B/D=2-147. DR PDB; 6XE7; X-ray; 2.00 A; B/D=2-147. DR PDB; 7AET; X-ray; 2.53 A; BBB/DDD=3-147. DR PDB; 7AEU; X-ray; 2.54 A; BBB/DDD=3-147. DR PDB; 7AEV; X-ray; 2.77 A; BBB/DDD=3-147. DR PDB; 7CUE; X-ray; 2.75 A; B/D=1-147. DR PDB; 7DY3; X-ray; 1.40 A; B/D/F/H=2-147. DR PDB; 7DY4; X-ray; 1.30 A; B/D/F/H=2-147. DR PDB; 7JJQ; X-ray; 2.15 A; B/D=2-147. DR PDB; 7JXZ; X-ray; 2.23 A; B/D=2-147. DR PDB; 7JY0; X-ray; 1.63 A; B/D=2-147. DR PDB; 7JY1; X-ray; 1.59 A; B/D=2-147. DR PDB; 7JY3; X-ray; 1.48 A; B/D=2-147. DR PDB; 7K4M; X-ray; 2.50 A; B/D/F/H/J=1-147. DR PDB; 7PCF; EM; 5.82 A; B=2-147. DR PDB; 7PCH; EM; 2.89 A; B/D=2-147. DR PDB; 7PCQ; EM; 3.62 A; B/D=2-147. DR PDB; 7UD7; X-ray; 1.80 A; B/D=1-147. DR PDB; 7UD8; X-ray; 1.80 A; B/D=1-147. DR PDB; 7UF6; X-ray; 2.00 A; B/D=1-147. DR PDB; 7UF7; X-ray; 2.00 A; B/D=1-147. DR PDB; 7UVB; X-ray; 2.05 A; B/D=2-147. DR PDB; 7VDE; EM; 3.20 A; B/D=1-147. DR PDB; 7XGY; EM; 3.50 A; B/D=1-147. DR PDB; 8DOV; X-ray; 2.10 A; B/D/F/H=2-147. DR PDB; 8EGI; X-ray; 2.30 A; B/D=1-147. DR PDB; 8FDK; X-ray; 1.89 A; B/D=2-147. DR PDB; 8FDL; X-ray; 1.75 A; B/D=2-147. DR PDB; 8FDM; X-ray; 1.91 A; B/D=2-147. DR PDB; 8FDN; X-ray; 2.20 A; B/D=2-147. DR PDBsum; 1A00; -. DR PDBsum; 1A01; -. DR PDBsum; 1A0U; -. DR PDBsum; 1A0Z; -. DR PDBsum; 1A3N; -. DR PDBsum; 1A3O; -. 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; 1CBL; -. DR PDBsum; 1CBM; -. DR PDBsum; 1CH4; -. DR PDBsum; 1CLS; -. DR PDBsum; 1CMY; -. DR PDBsum; 1COH; -. DR PDBsum; 1DKE; -. DR PDBsum; 1DXT; -. DR PDBsum; 1DXU; -. DR PDBsum; 1DXV; -. 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; 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; 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; 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; 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; 3P5Q; -. DR PDBsum; 3QJB; -. DR PDBsum; 3QJC; -. DR PDBsum; 3QJD; -. DR PDBsum; 3QJE; -. DR PDBsum; 3R5I; -. DR PDBsum; 3S65; -. DR PDBsum; 3S66; -. DR PDBsum; 3SZK; -. DR PDBsum; 3W4U; -. 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; 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; 6FQF; -. DR PDBsum; 6HAL; -. DR PDBsum; 6HBW; -. DR PDBsum; 6HK2; -. DR PDBsum; 6KA9; -. DR PDBsum; 6KAE; -. DR PDBsum; 6KAH; -. DR PDBsum; 6KAI; -. DR PDBsum; 6KAO; -. DR PDBsum; 6KAP; -. DR PDBsum; 6KAQ; -. DR PDBsum; 6KAR; -. DR PDBsum; 6KAS; -. DR PDBsum; 6KAT; -. DR PDBsum; 6KAU; -. DR PDBsum; 6KAV; -. DR PDBsum; 6KYE; -. DR PDBsum; 6L5V; -. DR PDBsum; 6L5W; -. DR PDBsum; 6L5X; -. DR PDBsum; 6L5Y; -. DR PDBsum; 6LCW; -. DR PDBsum; 6LCX; -. DR PDBsum; 6NBC; -. DR PDBsum; 6NBD; -. DR PDBsum; 6NQ5; -. DR PDBsum; 6TB2; -. DR PDBsum; 6XD9; -. DR PDBsum; 6XDT; -. DR PDBsum; 6XE7; -. DR PDBsum; 7AET; -. DR PDBsum; 7AEU; -. DR PDBsum; 7AEV; -. DR PDBsum; 7CUE; -. DR PDBsum; 7DY3; -. DR PDBsum; 7DY4; -. DR PDBsum; 7JJQ; -. DR PDBsum; 7JXZ; -. DR PDBsum; 7JY0; -. DR PDBsum; 7JY1; -. DR PDBsum; 7JY3; -. DR PDBsum; 7K4M; -. DR PDBsum; 7PCF; -. DR PDBsum; 7PCH; -. DR PDBsum; 7PCQ; -. DR PDBsum; 7UD7; -. DR PDBsum; 7UD8; -. DR PDBsum; 7UF6; -. DR PDBsum; 7UF7; -. DR PDBsum; 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; P68871; -. DR BMRB; P68871; -. 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; P68871; -. DR SMR; P68871; -. DR BioGRID; 109293; 214. DR ComplexPortal; CPX-2158; Hemoglobin HbA complex. DR ComplexPortal; CPX-2929; Hemoglobin Portland-2 complex. DR ComplexPortal; CPX-2936; Hemoglobin HbH complex. DR DIP; DIP-35526N; -. DR IntAct; P68871; 55. DR MINT; P68871; -. DR STRING; 9606.ENSP00000494175; -. DR BindingDB; P68871; -. DR ChEMBL; CHEMBL4331; -. 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; DB09147; Ferric pyrophosphate. DR DrugBank; DB13995; Ferric pyrophosphate citrate. 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; DB01593; Zinc. DR DrugBank; DB14487; Zinc acetate. DR DrugBank; DB14533; Zinc chloride. DR DrugBank; DB14548; Zinc sulfate, unspecified form. DR DrugCentral; P68871; -. DR TCDB; 1.A.107.1.2; the pore-forming globin (globin) family. DR CarbonylDB; P68871; -. DR GlyConnect; 2875; 1 O-GlcNAc glycan (3 sites). DR GlyCosmos; P68871; 10 sites, 2 glycans. DR GlyGen; P68871; 4 sites, 2 O-linked glycans (4 sites). DR iPTMnet; P68871; -. DR MetOSite; P68871; -. DR PhosphoSitePlus; P68871; -. DR BioMuta; HBB; -. DR DMDM; 56749856; -. DR REPRODUCTION-2DPAGE; IPI00654755; -. DR REPRODUCTION-2DPAGE; P68871; -. DR CPTAC; CPTAC-5884; -. DR EPD; P68871; -. DR jPOST; P68871; -. DR MassIVE; P68871; -. DR MaxQB; P68871; -. DR PaxDb; 9606-ENSP00000333994; -. DR PeptideAtlas; P68871; -. DR PRIDE; P68871; -. DR ProteomicsDB; 57543; -. DR TopDownProteomics; P68871; -. DR ABCD; P68871; 2 sequenced antibodies. DR Antibodypedia; 34986; 437 antibodies from 34 providers. DR DNASU; 3043; -. DR Ensembl; ENST00000335295.4; ENSP00000333994.3; ENSG00000244734.4. DR Ensembl; ENST00000647020.1; ENSP00000494175.1; ENSG00000244734.4. DR GeneID; 3043; -. DR KEGG; hsa:3043; -. DR MANE-Select; ENST00000335295.4; ENSP00000333994.3; NM_000518.5; NP_000509.1. DR UCSC; uc001mae.2; human. DR AGR; HGNC:4827; -. DR CTD; 3043; -. DR DisGeNET; 3043; -. DR GeneCards; HBB; -. DR GeneReviews; HBB; -. DR HGNC; HGNC:4827; HBB. DR HPA; ENSG00000244734; Tissue enriched (bone). DR MalaCards; HBB; -. DR MIM; 140700; phenotype. DR MIM; 141900; gene+phenotype. DR MIM; 603902; phenotype. DR MIM; 603903; phenotype. DR MIM; 611162; phenotype. DR MIM; 613985; phenotype. DR neXtProt; NX_P68871; -. DR OpenTargets; ENSG00000244734; -. DR Orphanet; 247511; Autosomal dominant secondary polycythemia. DR Orphanet; 231222; Beta-thalassemia intermedia. DR Orphanet; 231214; Beta-thalassemia major. DR Orphanet; 231237; Delta-beta-thalassemia. DR Orphanet; 231226; Dominant beta-thalassemia. DR Orphanet; 2132; Hemoglobin C disease. DR Orphanet; 231242; Hemoglobin C-beta-thalassemia syndrome. DR Orphanet; 90039; Hemoglobin D disease. DR Orphanet; 2133; Hemoglobin E disease. DR Orphanet; 231249; Hemoglobin E-beta-thalassemia syndrome. DR Orphanet; 330032; Hemoglobin Lepore-beta-thalassemia syndrome. DR Orphanet; 330041; Hemoglobin M disease. DR Orphanet; 46532; Hereditary persistence of fetal hemoglobin-beta-thalassemia syndrome. DR Orphanet; 251380; Hereditary persistence of fetal hemoglobin-sickle cell disease syndrome. DR Orphanet; 232; Sickle cell anemia. DR Orphanet; 251359; Sickle cell-beta-thalassemia disease syndrome. DR Orphanet; 251365; Sickle cell-hemoglobin C disease syndrome. DR Orphanet; 251370; Sickle cell-hemoglobin D disease syndrome. DR Orphanet; 251375; Sickle cell-hemoglobin E disease syndrome. DR PharmGKB; PA29202; -. DR VEuPathDB; HostDB:ENSG00000244734; -. DR eggNOG; KOG3378; Eukaryota. DR GeneTree; ENSGT00940000163476; -. DR HOGENOM; CLU_003827_10_0_1; -. DR InParanoid; P68871; -. DR OMA; ISTIWAK; -. DR OrthoDB; 5356926at2759; -. DR PhylomeDB; P68871; -. DR TreeFam; TF333268; -. DR PathwayCommons; P68871; -. 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-6798695; Neutrophil degranulation. DR Reactome; R-HSA-9613829; Chaperone Mediated Autophagy. DR Reactome; R-HSA-9615710; Late endosomal microautophagy. DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1. DR Reactome; R-HSA-9707616; Heme signaling. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SignaLink; P68871; -. DR SIGNOR; P68871; -. DR BioGRID-ORCS; 3043; 14 hits in 1155 CRISPR screens. DR ChiTaRS; HBB; human. DR EvolutionaryTrace; P68871; -. DR GeneWiki; HBB; -. DR GenomeRNAi; 3043; -. DR Pharos; P68871; Tbio. DR PRO; PR:P68871; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P68871; Protein. DR Bgee; ENSG00000244734; Expressed in trabecular bone tissue and 206 other cell types or tissues. DR ExpressionAtlas; P68871; 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:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome. DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IDA:BHF-UCL. DR GO; GO:0005833; C:hemoglobin complex; IDA:BHF-UCL. DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome. DR GO; GO:0020037; F:heme binding; IBA:GO_Central. DR GO; GO:0031721; F:hemoglobin alpha binding; IBA:GO_Central. DR GO; GO:0030492; F:hemoglobin binding; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043177; F:organic acid binding; IBA:GO_Central. DR GO; GO:0019825; F:oxygen binding; IDA:UniProtKB. DR GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central. DR GO; GO:0097746; P:blood vessel diameter maintenance; IEA:UniProtKB-KW. 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:0070527; P:platelet aggregation; HMP:UniProtKB. DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; NAS:UniProtKB. DR GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW. DR GO; GO:0070293; P:renal absorption; IMP:UniProtKB. DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:BHF-UCL. DR CDD; cd08925; Hb-beta-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; IPR002337; Hemoglobin_b. DR PANTHER; PTHR11442; HEMOGLOBIN FAMILY MEMBER; 1. DR PANTHER; PTHR11442:SF42; HEMOGLOBIN SUBUNIT BETA; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR00814; BETAHAEM. DR SUPFAM; SSF46458; Globin-like; 1. DR PROSITE; PS01033; GLOBIN; 1. DR SWISS-2DPAGE; P68871; -. DR UCD-2DPAGE; P68871; -. DR Genevisible; P68871; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Congenital dyserythropoietic anemia; KW Direct protein sequencing; Disease variant; Glycation; Glycoprotein; Heme; KW Hereditary hemolytic anemia; Hypotensive agent; Iron; Metal-binding; KW Oxygen transport; Phosphoprotein; Pyruvate; Reference proteome; KW S-nitrosylation; Transport; Vasoactive. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P02086, FT ECO:0000269|PubMed:13872627" FT CHAIN 2..147 FT /note="Hemoglobin subunit beta" FT /id="PRO_0000052976" FT PEPTIDE 33..42 FT /note="LVV-hemorphin-7" FT /id="PRO_0000296641" FT PEPTIDE 33..39 FT /note="Spinorphin" FT /id="PRO_0000424226" FT BINDING 2 FT /ligand="(2R)-2,3-bisphosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58248" FT BINDING 3 FT /ligand="(2R)-2,3-bisphosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58248" FT BINDING 64 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="distal binding residue" FT BINDING 83 FT /ligand="(2R)-2,3-bisphosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58248" FT BINDING 93 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 BINDING 144 FT /ligand="(2R)-2,3-bisphosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58248" FT SITE 8..9 FT /note="(Microbial infection) Cleavage; by N.americanus apr- FT 2" FT /evidence="ECO:0000269|PubMed:12552433" FT SITE 26..27 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 36..37 FT /note="(Microbial infection) Cleavage; by N.americanus apr- FT 2" FT /evidence="ECO:0000269|PubMed:12552433" FT SITE 38..39 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 53..54 FT /note="(Microbial infection) Cleavage; by N.americanus apr- FT 2" FT /evidence="ECO:0000269|PubMed:12552433" FT SITE 57..58 FT /note="(Microbial infection) Cleavage; by N.americanus apr- FT 2" FT /evidence="ECO:0000269|PubMed:12552433" FT SITE 60 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:7358733" FT SITE 72..73 FT /note="(Microbial infection) Cleavage; by N.americanus apr- FT 2" FT /evidence="ECO:0000269|PubMed:12552433" FT SITE 75..76 FT /note="(Microbial infection) Cleavage; by N.americanus apr- FT 2" FT /evidence="ECO:0000269|PubMed:12552433" FT SITE 83 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:7358733" FT SITE 85..86 FT /note="(Microbial infection) Cleavage; by N.americanus apr- FT 2" FT /evidence="ECO:0000269|PubMed:12552433" FT SITE 93..94 FT /note="(Microbial infection) Cleavage; by N.americanus apr- FT 2" FT /evidence="ECO:0000269|PubMed:12552433" FT SITE 96 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:7358733" FT SITE 105..106 FT /note="(Microbial infection) Cleavage; by N.americanus apr- FT 2" FT /evidence="ECO:0000269|PubMed:12552433" FT SITE 111..112 FT /note="(Microbial infection) Cleavage; by N.americanus apr- FT 2" FT /evidence="ECO:0000269|PubMed:12552433" FT SITE 120..121 FT /note="(Microbial infection) Cleavage; by N.americanus apr- FT 2" FT /evidence="ECO:0000269|PubMed:12552433" FT SITE 123..124 FT /note="(Microbial infection) Cleavage; by N.americanus apr- FT 2" FT /evidence="ECO:0000269|PubMed:12552433" FT SITE 129..130 FT /note="(Microbial infection) Cleavage; by N.americanus apr- FT 2" FT /evidence="ECO:0000269|PubMed:12552433" FT SITE 141..142 FT /note="(Microbial infection) Cleavage; by N.americanus apr- FT 2" FT /evidence="ECO:0000269|PubMed:12552433" FT SITE 145..146 FT /note="(Microbial infection) Cleavage; by N.americanus apr- FT 2" FT /evidence="ECO:0000269|PubMed:12552433" FT MOD_RES 2 FT /note="N-acetylvaline" FT /evidence="ECO:0000250|UniProtKB:P02086" FT MOD_RES 2 FT /note="N-pyruvate 2-iminyl-valine; in Hb A1b" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 13 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 45 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 51 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 60 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:4531009" FT MOD_RES 83 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:4531009" FT MOD_RES 88 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 94 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000269|PubMed:8637569, FT ECO:0000269|PubMed:9843411" FT MOD_RES 145 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:4531009" FT CARBOHYD 2 FT /note="N-linked (Glc) (glycation) valine; in Hb A1c" FT /evidence="ECO:0000269|PubMed:635569" FT CARBOHYD 9 FT /note="N-linked (Glc) (glycation) lysine" FT /evidence="ECO:0000269|PubMed:7358733" FT CARBOHYD 18 FT /note="N-linked (Glc) (glycation) lysine" FT /evidence="ECO:0000269|PubMed:7358733" FT CARBOHYD 67 FT /note="N-linked (Glc) (glycation) lysine" FT /evidence="ECO:0000269|PubMed:7358733" FT CARBOHYD 121 FT /note="N-linked (Glc) (glycation) lysine" FT /evidence="ECO:0000269|PubMed:7358733" FT CARBOHYD 145 FT /note="N-linked (Glc) (glycation) lysine; alternate" FT /evidence="ECO:0000269|PubMed:7358733" FT VARIANT 2 FT /note="V -> A (in Raleigh; O(2) affinity down; FT dbSNP:rs33949930)" FT /id="VAR_002856" FT VARIANT 3 FT /note="H -> L (in Graz; dbSNP:rs33983205)" FT /evidence="ECO:0000269|PubMed:1487420" FT /id="VAR_002857" FT VARIANT 3 FT /note="H -> Q (in Okayama; O(2) affinity up; FT dbSNP:rs713040)" FT /id="VAR_002858" FT VARIANT 3 FT /note="H -> R (in Deer Lodge; O(2) affinity up; FT dbSNP:rs33983205)" FT /id="VAR_002859" FT VARIANT 3 FT /note="H -> Y (in Fukuoka; dbSNP:rs35906307)" FT /id="VAR_002860" FT VARIANT 6 FT /note="P -> R (in Warwickshire; dbSNP:rs34769005)" FT /id="VAR_002861" FT VARIANT 7 FT /note="E -> A (in G-Makassar; dbSNP:rs334)" FT /id="VAR_002862" FT VARIANT 7 FT /note="E -> K (in Hb C; confers resistance to severe FT malaria; dbSNP:rs33930165)" FT /evidence="ECO:0000269|PubMed:11001883, FT ECO:0000269|PubMed:16175509" FT /id="VAR_002864" FT VARIANT 7 FT /note="E -> Q (in Machida; dbSNP:rs33930165)" FT /id="VAR_002865" FT VARIANT 7 FT /note="E -> V (in SKCA; Hb S; at heterozygosity confers FT resistance to malaria; dbSNP:rs334)" FT /evidence="ECO:0000269|PubMed:13464827, FT ECO:0000269|PubMed:16001361, ECO:0000269|Ref.10" FT /id="VAR_002863" FT VARIANT 8 FT /note="E -> G (in G-San Jose; mildly unstable; FT dbSNP:rs34387455)" FT /id="VAR_002866" FT VARIANT 8 FT /note="E -> K (in G-Siriraj; dbSNP:rs34948328)" FT /id="VAR_002867" FT VARIANT 9 FT /note="K -> E (in N-Timone; dbSNP:rs33926764)" FT /evidence="ECO:0000269|PubMed:2634671" FT /id="VAR_002868" FT VARIANT 9 FT /note="K -> Q (in J-Luhe; dbSNP:rs33926764)" FT /id="VAR_002869" FT VARIANT 9 FT /note="K -> T (in Rio Grande; dbSNP:rs33932981)" FT /evidence="ECO:0000269|PubMed:6857757" FT /id="VAR_002870" FT VARIANT 10 FT /note="S -> C (in Porto Alegre; O(2) affinity up; FT dbSNP:rs33918131)" FT /id="VAR_002871" FT VARIANT 11 FT /note="A -> D (in Ankara; dbSNP:rs33947457)" FT /evidence="ECO:0000269|PubMed:4850241" FT /id="VAR_002872" FT VARIANT 11 FT /note="A -> V (in Iraq-Halabja; dbSNP:rs33947457)" FT /evidence="ECO:0000269|PubMed:10398311" FT /id="VAR_025393" FT VARIANT 12 FT /note="V -> D (in Windsor; O(2) affinity up; unstable; FT dbSNP:rs35140348)" FT /evidence="ECO:0000269|PubMed:2599880" FT /id="VAR_002873" FT VARIANT 12 FT /note="V -> I (in Hamilton; dbSNP:rs33974228)" FT /id="VAR_002874" FT VARIANT 14 FT /note="A -> D (in J-Lens; dbSNP:rs35203747)" FT /id="VAR_002875" FT VARIANT 15 FT /note="L -> P (in Saki; unstable; dbSNP:rs33935445)" FT /id="VAR_002876" FT VARIANT 15 FT /note="L -> R (in Soegn; unstable; dbSNP:rs33935445)" FT /id="VAR_002877" FT VARIANT 16 FT /note="W -> G (in Randwick; unstable; dbSNP:rs33946157)" FT /evidence="ECO:0000269|PubMed:3384707" FT /id="VAR_002878" FT VARIANT 16 FT /note="W -> R (in Belfast; O(2) affinity up; unstable; FT dbSNP:rs33946157)" FT /id="VAR_002879" FT VARIANT 17 FT /note="G -> D (in FT J-Baltimore/J-Trinidad/J-Ireland/J-Georgia/N-New Haven; FT dbSNP:rs33962676)" FT /id="VAR_002880" FT VARIANT 17 FT /note="G -> R (in D-Bushman; dbSNP:rs63751285)" FT /id="VAR_002881" FT VARIANT 18 FT /note="K -> E (in Nagasaki; dbSNP:rs33986703)" FT /id="VAR_002882" FT VARIANT 18 FT /note="K -> N (in J-Amiens; dbSNP:rs36006214)" FT /id="VAR_002883" FT VARIANT 18 FT /note="K -> Q (in Nikosia; dbSNP:rs33986703)" FT /id="VAR_002884" FT VARIANT 19 FT /note="V -> M (in Baden; slightly unstable; FT dbSNP:rs35802118)" FT /id="VAR_002885" FT VARIANT 20 FT /note="N -> D (in Alamo; dbSNP:rs34866629)" FT /id="VAR_002886" FT VARIANT 20 FT /note="N -> K (in D-Ouleh RABAH; dbSNP:rs63750840)" FT /id="VAR_002887" FT VARIANT 20 FT /note="N -> S (in Malay; dbSNP:rs33972047)" FT /id="VAR_002888" FT VARIANT 21 FT /note="V -> M (in Olympia; O(2) affinity up; FT dbSNP:rs35890959)" FT /id="VAR_002889" FT VARIANT 22 FT /note="D -> G (in Connecticut; O(2) affinity down; FT dbSNP:rs33977536)" FT /id="VAR_002890" FT VARIANT 22 FT /note="D -> H (in Karlskoga; dbSNP:rs33950093)" FT /evidence="ECO:0000269|PubMed:8330972" FT /id="VAR_002892" FT VARIANT 22 FT /note="D -> N (in Cocody; dbSNP:rs33950093)" FT /id="VAR_002891" FT VARIANT 22 FT /note="D -> Y (in Yusa; dbSNP:rs33950093)" FT /id="VAR_002893" FT VARIANT 23 FT /note="E -> A (in G-Coushatta/G-Saskatoon/G-Taegu/Hsin Chu; FT dbSNP:rs33936254)" FT /id="VAR_002894" FT VARIANT 23 FT /note="E -> G (in G-Taipei; dbSNP:rs33936254)" FT /id="VAR_002895" FT VARIANT 23 FT /note="E -> K (in E-Saskatoon; dbSNP:rs33959855)" FT /id="VAR_002896" FT VARIANT 23 FT /note="E -> Q (in D-Iran; dbSNP:rs33959855)" FT /id="VAR_002897" FT VARIANT 23 FT /note="E -> V (in D-Granada; dbSNP:rs33936254)" FT /id="VAR_002898" FT VARIANT 24 FT /note="V -> D (in Strasbourg; O(2) affinity up; FT dbSNP:rs33945546)" FT /id="VAR_002899" FT VARIANT 24 FT /note="V -> F (in Palmerston North; O(2) affinity up; FT unstable; dbSNP:rs33929459)" FT /evidence="ECO:0000269|PubMed:7161106" FT /id="VAR_002900" FT VARIANT 24 FT /note="V -> G (in Miyashiro; O(2) affinity up; unstable; FT dbSNP:rs33945546)" FT /evidence="ECO:0000269|PubMed:7338468" FT /id="VAR_002901" FT VARIANT 24 FT /note="Missing (in Freiburg; dbSNP:rs34160180)" FT /evidence="ECO:0000269|PubMed:5919752" FT /id="VAR_069169" FT VARIANT 25 FT /note="G -> D (in Moscva; O(2) affinity down; unstable; FT dbSNP:rs33968721)" FT /id="VAR_002902" FT VARIANT 25 FT /note="G -> R (in Riverdale-Bronx; O(2) affinity up; FT unstable; dbSNP:rs33972975)" FT /id="VAR_002903" FT VARIANT 25 FT /note="G -> V (in Savannah; unstable; dbSNP:rs33968721)" FT /id="VAR_002904" FT VARIANT 26 FT /note="G -> D (in J-Auckland; unstable; O(2) affinity down; FT dbSNP:rs35474880)" FT /evidence="ECO:0000269|PubMed:3654265" FT /id="VAR_002905" FT VARIANT 26 FT /note="G -> R (in G-Taiwan Ami; dbSNP:rs34404985)" FT /id="VAR_002906" FT VARIANT 27 FT /note="E -> K (in B-THAL; Hb E; confers resistance to FT severe malaria; dbSNP:rs33950507)" FT /evidence="ECO:0000269|PubMed:12144064, FT ECO:0000269|PubMed:12149194, ECO:0000269|PubMed:15481886, FT ECO:0000269|PubMed:6166632" FT /id="VAR_002907" FT VARIANT 27 FT /note="E -> V (in Henri Mondor; slightly unstable; FT dbSNP:rs33915112)" FT /id="VAR_002908" FT VARIANT 28 FT /note="A -> D (in Volga/Drenthe; unstable; FT dbSNP:rs33954632)" FT /id="VAR_002909" FT VARIANT 28 FT /note="A -> S (in Knossos; dbSNP:rs35424040)" FT /evidence="ECO:0000269|PubMed:7173395" FT /id="VAR_002910" FT VARIANT 28 FT /note="A -> V (in Grange-blanche; O(2) affinity up; FT dbSNP:rs33954632)" FT /evidence="ECO:0000269|PubMed:3666141" FT /id="VAR_002911" FT VARIANT 29 FT /note="L -> P (in Genova/Hyogo; unstable; FT dbSNP:rs33916412)" FT /id="VAR_002912" FT VARIANT 29 FT /note="L -> Q (in St Louis; dbSNP:rs33916412)" FT /evidence="ECO:0000269|PubMed:186485" FT /id="VAR_035236" FT VARIANT 30 FT /note="G -> D (in Lufkin; unstable; dbSNP:rs35685286)" FT /id="VAR_002913" FT VARIANT 31 FT /note="R -> S (in Tacoma; unstable; dbSNP:rs1135071)" FT /id="VAR_002914" FT VARIANT 32 FT /note="L -> P (in Yokohama; unstable; dbSNP:rs33920173)" FT /evidence="ECO:0000269|PubMed:7338469" FT /id="VAR_002915" FT VARIANT 33 FT /note="L -> R (in Castilla; unstable; dbSNP:rs33948578)" FT /id="VAR_002916" FT VARIANT 33 FT /note="L -> V (in Muscat; slightly unstable; FT dbSNP:rs34314652)" FT /evidence="ECO:0000269|PubMed:1517102" FT /id="VAR_002917" FT VARIANT 35 FT /note="V -> D (in Santander; unstable; dbSNP:rs1135101)" FT /evidence="ECO:0000269|PubMed:12603091" FT /id="VAR_025394" FT VARIANT 35 FT /note="V -> F (in Pitie-Salpetriere; O(2) affinity up; FT dbSNP:rs1141387)" FT /id="VAR_002918" FT VARIANT 35 FT /note="V -> L (in Nantes; increased oxygen affinity; FT dbSNP:rs1141387)" FT /evidence="ECO:0000269|PubMed:12908805" FT /id="VAR_025395" FT VARIANT 36 FT /note="Y -> F (in Philly; O(2) affinity up; unstable; FT dbSNP:rs35857380)" FT /id="VAR_002919" FT VARIANT 37 FT /note="P -> R (in Sunnybrook; dbSNP:rs33993004)" FT /id="VAR_002920" FT VARIANT 37 FT /note="P -> S (in North Chicago; O(2) affinity up; FT dbSNP:rs33948615)" FT /evidence="ECO:0000269|PubMed:3937824" FT /id="VAR_002921" FT VARIANT 37 FT /note="P -> T (in Linkoping/Finlandia; O(2) affinity up; FT dbSNP:rs33948615)" FT /evidence="ECO:0000269|PubMed:3691763" FT /id="VAR_002922" FT VARIANT 38 FT /note="W -> G (in Howick; dbSNP:rs33994623)" FT /evidence="ECO:0000269|PubMed:8144352" FT /id="VAR_002923" FT VARIANT 38 FT /note="W -> R (in Rothschild; O(2) affinity down; FT dbSNP:rs33994623)" FT /evidence="ECO:0000269|PubMed:1567857" FT /id="VAR_002925" FT VARIANT 38 FT /note="W -> S (in Hirose; O(2) affinity up; FT dbSNP:rs33991059)" FT /id="VAR_002924" FT VARIANT 39 FT /note="T -> N (in Hinwil; O(2) affinity up; FT dbSNP:rs34703513)" FT /evidence="ECO:0000269|PubMed:8745430" FT /id="VAR_002926" FT VARIANT 40 FT /note="Q -> E (in Vaasa; unstable; dbSNP:rs11549407)" FT /id="VAR_002927" FT VARIANT 40 FT /note="Q -> K (in Alabama; dbSNP:rs11549407)" FT /evidence="ECO:0000269|PubMed:1115799" FT /id="VAR_002928" FT VARIANT 40 FT /note="Q -> R (in Tianshui; dbSNP:rs35973315)" FT /id="VAR_002929" FT VARIANT 42 FT /note="F -> Y (in Mequon; dbSNP:rs33926796)" FT /id="VAR_002930" FT VARIANT 42 FT /note="Missing (in Bruxelles)" FT /evidence="ECO:0000269|PubMed:2599881" FT /id="VAR_035237" FT VARIANT 43 FT /note="F -> L (in Louisville; unstable; dbSNP:rs33924146)" FT /evidence="ECO:0000269|Ref.6" FT /id="VAR_002931" FT VARIANT 43 FT /note="F -> S (in Hammersmith; dbSNP:rs34378160)" FT /evidence="ECO:0000269|PubMed:6259091" FT /id="VAR_035239" FT VARIANT 43 FT /note="Missing (in Bruxelles)" FT /evidence="ECO:0000269|PubMed:2599881" FT /id="VAR_035238" FT VARIANT 44 FT /note="E -> Q (in Hoshida/Chaya; dbSNP:rs33922842)" FT /id="VAR_002932" FT VARIANT 45 FT /note="S -> C (in Mississippi; dbSNP:rs34868397)" FT /id="VAR_002933" FT VARIANT 46 FT /note="F -> S (in Cheverly; unstable; dbSNP:rs33978338)" FT /id="VAR_002934" FT VARIANT 47 FT /note="G -> E (in K-Ibadan; dbSNP:rs35303218)" FT /id="VAR_002935" FT VARIANT 48 FT /note="D -> A (in Avicenna; dbSNP:rs33980484)" FT /id="VAR_002936" FT VARIANT 48 FT /note="D -> G (in Gavello; dbSNP:rs33980484)" FT /id="VAR_002937" FT VARIANT 48 FT /note="D -> Y (in Maputo; dbSNP:rs33932070)" FT /evidence="ECO:0000269|PubMed:6629824" FT /id="VAR_002938" FT VARIANT 49 FT /note="L -> P (in Bab-Saadoum; slightly unstable; FT dbSNP:rs33952850)" FT /id="VAR_002939" FT VARIANT 50 FT /note="S -> F (in Las Palmas; slightly unstable; FT dbSNP:rs33960931)" FT /evidence="ECO:0000269|PubMed:3384708, ECO:0000269|Ref.13" FT /id="VAR_002940" FT VARIANT 51 FT /note="T -> K (in Edmonton)" FT /id="VAR_002941" FT VARIANT 52 FT /note="P -> R (in Willamette; O(2) affinity up; unstable; FT dbSNP:rs33969727)" FT /id="VAR_002942" FT VARIANT 53 FT /note="D -> A (in Ocho Rios; dbSNP:rs33919924)" FT /id="VAR_002943" FT VARIANT 53 FT /note="D -> H (in Summer Hill; dbSNP:rs33961886)" FT /id="VAR_002944" FT VARIANT 55 FT /note="V -> D (in Jacksonville; O(2) affinity up; unstable; FT dbSNP:rs34037627)" FT /evidence="ECO:0000269|PubMed:2101840" FT /id="VAR_002945" FT VARIANT 56 FT /note="M -> K (in Matera; unstable; dbSNP:rs35094013)" FT /evidence="ECO:0000269|PubMed:2384314" FT /id="VAR_002946" FT VARIANT 57 FT /note="G -> R (in Hamadan; dbSNP:rs33935983)" FT /id="VAR_002947" FT VARIANT 58 FT /note="N -> K (in G-ferrara; unstable; dbSNP:rs35278874)" FT /id="VAR_002948" FT VARIANT 59 FT /note="P -> R (in Dhofar/Yukuhashi; dbSNP:rs33991472)" FT /id="VAR_002949" FT VARIANT 60 FT /note="K -> E (in I-High Wycombe; dbSNP:rs33969400)" FT /id="VAR_002950" FT VARIANT 61 FT /note="V -> A (in Collingwood; unstable; dbSNP:rs33931779)" FT /id="VAR_002951" FT VARIANT 62 FT /note="K -> E (in N-Seatlle; dbSNP:rs33995148)" FT /id="VAR_002952" FT VARIANT 62 FT /note="K -> M (in Bologna; O(2) affinity down; FT dbSNP:rs34974709)" FT /id="VAR_002953" FT VARIANT 62 FT /note="K -> N (in Hikari; dbSNP:rs34446260)" FT /id="VAR_002954" FT VARIANT 63 FT /note="A -> D (in J-Europa; dbSNP:rs34151786)" FT /evidence="ECO:0000269|PubMed:8811317" FT /id="VAR_002955" FT VARIANT 63 FT /note="A -> P (in Duarte; unstable; dbSNP:rs34933455)" FT /id="VAR_002956" FT VARIANT 64 FT /note="H -> Y (in M-Saskatoon; O(2) affinity up; FT dbSNP:rs33922873)" FT /evidence="ECO:0000269|PubMed:13897827" FT /id="VAR_002957" FT VARIANT 66 FT /note="K -> M (in J-Antakya; dbSNP:rs33932548)" FT /evidence="ECO:0000269|PubMed:3707969" FT /id="VAR_002958" FT VARIANT 66 FT /note="K -> N (in J-Sicilia; dbSNP:rs35747961)" FT /evidence="ECO:0000269|PubMed:4852224" FT /id="VAR_002959" FT VARIANT 66 FT /note="K -> Q (in J-Cairo; dbSNP:rs35353749)" FT /evidence="ECO:0000269|PubMed:1247583" FT /id="VAR_002960" FT VARIANT 67 FT /note="K -> I (in Vigo; O(2) affinity down)" FT /evidence="ECO:0000269|PubMed:28066926" FT /id="VAR_079528" FT VARIANT 67 FT /note="K -> T (in Chico; O(2) affinity down; FT dbSNP:rs35939489)" FT /id="VAR_002961" FT VARIANT 68 FT /note="V -> A (in Sydney; unstable; dbSNP:rs33918343)" FT /id="VAR_002962" FT VARIANT 68 FT /note="V -> D (in Bristol)" FT /evidence="ECO:0000269|PubMed:8704193" FT /id="VAR_035240" FT VARIANT 68 FT /note="V -> G (in non-spherocytic haemolytic anemia; FT Manukau; dbSNP:rs33918343)" FT /evidence="ECO:0000269|PubMed:8280608" FT /id="VAR_040060" FT VARIANT 68 FT /note="V -> M (in Alesha; unstable; dbSNP:rs36008922)" FT /evidence="ECO:0000269|PubMed:8330974" FT /id="VAR_002963" FT VARIANT 69 FT /note="L -> H (in Brisbane; O(2) affinity up; FT dbSNP:rs33972593)" FT /evidence="ECO:0000269|PubMed:6166590" FT /id="VAR_002964" FT VARIANT 69 FT /note="L -> P (in Mizuho; unstable; dbSNP:rs33972593)" FT /evidence="ECO:0000269|PubMed:893142" FT /id="VAR_002965" FT VARIANT 70 FT /note="G -> D (in Rambam; dbSNP:rs34718174)" FT /evidence="ECO:0000269|PubMed:9761252" FT /id="VAR_002966" FT VARIANT 70 FT /note="G -> R (in Kenitra; dbSNP:rs33947415)" FT /id="VAR_002967" FT VARIANT 70 FT /note="G -> S (in City of Hope; dbSNP:rs33947415)" FT /evidence="ECO:0000269|PubMed:6434492" FT /id="VAR_002968" FT VARIANT 71 FT /note="A -> D (in Seattle; O(2) affinity down; unstable; FT dbSNP:rs33946401)" FT /id="VAR_002969" FT VARIANT 72 FT /note="F -> S (in Christchurch; unstable; FT dbSNP:rs34362537)" FT /id="VAR_002970" FT VARIANT 74 FT /note="D -> G (in Tilburg; O(2) affinity down; FT dbSNP:rs33967755)" FT /id="VAR_002971" FT VARIANT 74 FT /note="D -> V (in Mobile; O(2) affinity down; FT dbSNP:rs33967755)" FT /id="VAR_002972" FT VARIANT 74 FT /note="D -> Y (in Vancouver; O(2) affinity down; FT dbSNP:rs33945705)" FT /id="VAR_002973" FT VARIANT 75 FT /note="G -> R (in Aalborg; unstable; dbSNP:rs33916541)" FT /id="VAR_002974" FT VARIANT 75 FT /note="G -> V (in Bushwick; unstable; dbSNP:rs33976006)" FT /id="VAR_002975" FT VARIANT 76 FT /note="L -> P (in Atlanta; unstable; dbSNP:rs33950542)" FT /evidence="ECO:0000269|Ref.13" FT /id="VAR_002976" FT VARIANT 76 FT /note="L -> R (in Pasadena; O(2) affinity up; unstable; FT dbSNP:rs33950542)" FT /id="VAR_002977" FT VARIANT 77 FT /note="A -> D (in J-Chicago; dbSNP:rs33985847)" FT /id="VAR_002978" FT VARIANT 78 FT /note="H -> D (in J-Iran; dbSNP:rs33991294)" FT /id="VAR_002979" FT VARIANT 78 FT /note="H -> R (in Costa Rica; dbSNP:rs33952543)" FT /evidence="ECO:0000269|PubMed:8641705" FT /id="VAR_002980" FT VARIANT 78 FT /note="H -> Y (in Fukuyama; dbSNP:rs33991294)" FT /id="VAR_002981" FT VARIANT 79 FT /note="L -> R (in Quin-hai; dbSNP:rs34870172)" FT /evidence="ECO:0000269|PubMed:6629822" FT /id="VAR_002982" FT VARIANT 80 FT /note="D -> Y (in Tampa; dbSNP:rs33990858)" FT /id="VAR_002983" FT VARIANT 81 FT /note="N -> K (in G-Szuhu/Gifu; dbSNP:rs35890380)" FT /id="VAR_002984" FT VARIANT 82 FT /note="L -> H (in La Roche-sur-Yon; unstable and O(2) FT affinity up; dbSNP:rs33936967)" FT /evidence="ECO:0000269|PubMed:1540659" FT /id="VAR_012663" FT VARIANT 82 FT /note="L -> R (in Baylor; unstable; dbSNP:rs33936967)" FT /id="VAR_002985" FT VARIANT 82 FT /note="L -> V (in dbSNP:rs11549406)" FT /id="VAR_049273" FT VARIANT 83 FT /note="K -> M (in Helsinki; O(2) affinity up; FT dbSNP:rs33987903)" FT /evidence="ECO:0000269|PubMed:826083" FT /id="VAR_002986" FT VARIANT 83 FT /note="K -> N (in Providence; dbSNP:rs33991993)" FT /id="VAR_012664" FT VARIANT 84 FT /note="G -> D (in Pyrgos; dbSNP:rs1803195)" FT /evidence="ECO:0000269|PubMed:12144064" FT /id="VAR_025396" FT VARIANT 84 FT /note="G -> R (in Muskegon; dbSNP:rs33930385)" FT /id="VAR_002987" FT VARIANT 85 FT /note="T -> I (in Kofu; dbSNP:rs35914488)" FT /evidence="ECO:0000269|PubMed:3744871" FT /id="VAR_002988" FT VARIANT 87 FT /note="A -> D (in Olomouc; O(2) affinity up; FT dbSNP:rs35819837)" FT /evidence="ECO:0000269|PubMed:3623975" FT /id="VAR_002989" FT VARIANT 88 FT /note="T -> I (in Quebec-Chori; dbSNP:rs33993568)" FT /id="VAR_002990" FT VARIANT 88 FT /note="T -> K (in D-Ibadan; dbSNP:rs33993568)" FT /id="VAR_002991" FT VARIANT 88 FT /note="T -> P (in Valletta; dbSNP:rs35553496)" FT /id="VAR_002992" FT VARIANT 89 FT /note="L -> P (in Santa Ana; unstable; dbSNP:rs33940204)" FT /id="VAR_002993" FT VARIANT 89 FT /note="L -> R (in Boras; unstable; dbSNP:rs33940204)" FT /id="VAR_002994" FT VARIANT 90 FT /note="S -> N (in Creteil; O(2) affinity up; FT dbSNP:rs33917628)" FT /id="VAR_002995" FT VARIANT 90 FT /note="S -> R (in Vanderbilt; O(2) affinity up; FT dbSNP:rs35351128)" FT /id="VAR_002996" FT VARIANT 91 FT /note="E -> D (in Pierre-Benite; O(2) affinity up; FT dbSNP:rs35002698)" FT /evidence="ECO:0000269|PubMed:3384709" FT /id="VAR_002997" FT VARIANT 91 FT /note="E -> K (in Agenogi; O(2) affinity down; FT dbSNP:rs33913712)" FT /id="VAR_002998" FT VARIANT 92 FT /note="L -> P (in Sabine; unstable; dbSNP:rs33917785)" FT /id="VAR_002999" FT VARIANT 92 FT /note="L -> R (in Caribbean; O(2) affinity down; unstable; FT dbSNP:rs33917785)" FT /evidence="ECO:0000269|PubMed:992050" FT /id="VAR_003000" FT VARIANT 93 FT /note="H -> D (in J-Altgelds Gardens; unstable; FT dbSNP:rs33924775)" FT /evidence="ECO:0000269|PubMed:721609" FT /id="VAR_003001" FT VARIANT 93 FT /note="H -> N (in Isehara; unstable; dbSNP:rs33924775)" FT /evidence="ECO:0000269|PubMed:1787097" FT /id="VAR_003002" FT VARIANT 93 FT /note="H -> P (in Newcastle and Duino; associated in cis FT with S-104 in Duino; unstable; dbSNP:rs33974325)" FT /evidence="ECO:0000269|PubMed:1511986" FT /id="VAR_003003" FT VARIANT 93 FT /note="H -> Q (in Istambul; unstable; dbSNP:rs34083951)" FT /evidence="ECO:0000269|PubMed:4639022" FT /id="VAR_003004" FT VARIANT 94 FT /note="C -> R (in Okazaki; O(2) affinity up; unstable; FT dbSNP:rs33972927)" FT /id="VAR_003005" FT VARIANT 95 FT /note="D -> G (in Chandigarh; dbSNP:rs34579351)" FT /id="VAR_003006" FT VARIANT 95 FT /note="D -> H (in Barcelona; O(2) affinity up; FT dbSNP:rs33959340)" FT /id="VAR_003007" FT VARIANT 95 FT /note="D -> N (in Bunbury; O(2) affinity up; FT dbSNP:rs33959340)" FT /evidence="ECO:0000269|PubMed:6629823" FT /id="VAR_003008" FT VARIANT 96 FT /note="K -> M (in J-Cordoba; dbSNP:rs35204496)" FT /id="VAR_003009" FT VARIANT 96 FT /note="K -> N (in Detroit; dbSNP:rs36038739)" FT /id="VAR_003010" FT VARIANT 97 FT /note="L -> P (in Debrousse; unstable; O(2) affinity up; FT dbSNP:rs36081208)" FT /evidence="ECO:0000269|PubMed:8602627" FT /id="VAR_003011" FT VARIANT 97 FT /note="L -> V (in Regina; O(2) affinity up; FT dbSNP:rs34665886)" FT /id="VAR_003012" FT VARIANT 98 FT /note="H -> L (in Wood; O(2) affinity up; FT dbSNP:rs33951978)" FT /id="VAR_003013" FT VARIANT 98 FT /note="H -> P (in Nagoya; O(2) affinity up; unstable; FT dbSNP:rs33951978)" FT /evidence="ECO:0000269|PubMed:3838976" FT /id="VAR_003014" FT VARIANT 98 FT /note="H -> Q (in Malmoe; O(2) affinity up; FT dbSNP:rs34515413)" FT /id="VAR_003015" FT VARIANT 98 FT /note="H -> Y (in Moriguchi; dbSNP:rs33950993)" FT /id="VAR_003016" FT VARIANT 99 FT /note="V -> G (in Nottingham; unstable; dbSNP:rs33985510)" FT /id="VAR_003017" FT VARIANT 100 FT /note="D -> E (in Coimbra; O(2) affinity up; FT dbSNP:rs34013622)" FT /evidence="ECO:0000269|PubMed:1814856" FT /id="VAR_003018" FT VARIANT 101 FT /note="P -> L (in Brigham; O(2) affinity up; FT dbSNP:rs33965000)" FT /id="VAR_003019" FT VARIANT 101 FT /note="P -> R (in New Mexico; dbSNP:rs33965000)" FT /id="VAR_003020" FT VARIANT 102 FT /note="E -> D (in Potomac; O(2) affinity up; FT dbSNP:rs35209591)" FT /id="VAR_003021" FT VARIANT 102 FT /note="E -> G (in Alberta; O(2) affinity up; FT dbSNP:rs33937393)" FT /id="VAR_003022" FT VARIANT 102 FT /note="E -> K (in British Columbia; O(2) affinity up; FT dbSNP:rs33966487)" FT /id="VAR_003023" FT VARIANT 102 FT /note="E -> Q (in Rush; unstable; dbSNP:rs33966487)" FT /evidence="ECO:0000269|PubMed:4129558" FT /id="VAR_003024" FT VARIANT 103 FT /note="N -> S (in Beth Israel; O(2) affinity down; FT unstable; dbSNP:rs33948057)" FT /id="VAR_003025" FT VARIANT 103 FT /note="N -> Y (in St Mande; O(2) affinity down; FT dbSNP:rs33927739)" FT /evidence="ECO:0000269|PubMed:7238856" FT /id="VAR_003026" FT VARIANT 104 FT /note="F -> L (in Heathrow; O(2) affinity up; FT dbSNP:rs35067717)" FT /id="VAR_003027" FT VARIANT 105 FT /note="R -> S (in Camperdown and Duino; associated in cis FT with P-92 in Duino; unstable; dbSNP:rs33914944)" FT /evidence="ECO:0000269|PubMed:1138922, FT ECO:0000269|PubMed:1511986" FT /id="VAR_003028" FT VARIANT 105 FT /note="R -> T (in Sherwood Forest; dbSNP:rs33911434)" FT /id="VAR_003029" FT VARIANT 108 FT /note="G -> R (in Burke; O(2) affinity down; unstable; FT dbSNP:rs35017910)" FT /evidence="ECO:0000269|PubMed:8401300" FT /id="VAR_003030" FT VARIANT 109 FT /note="N -> K (in Presbyterian; O(2) affinity down; FT unstable; dbSNP:rs34933751)" FT /evidence="ECO:0000269|PubMed:668922" FT /id="VAR_003031" FT VARIANT 110 FT /note="V -> M (in San Diego; O(2) affinity up; FT dbSNP:rs33969677)" FT /id="VAR_003032" FT VARIANT 111 FT /note="L -> P (in Showa-Yakushiji; dbSNP:rs35256489)" FT /id="VAR_003033" FT VARIANT 112 FT /note="V -> A (in Stanmore; O(2) affinity down; unstable; FT dbSNP:rs35871407)" FT /evidence="ECO:0000269|PubMed:1917537" FT /id="VAR_003034" FT VARIANT 113 FT /note="C -> F (in Canterbury; dbSNP:rs33932908)" FT /evidence="ECO:0000269|PubMed:11939514" FT /id="VAR_025397" FT VARIANT 113 FT /note="C -> R (in Indianapolis; dbSNP:rs35849199)" FT /evidence="ECO:0000269|PubMed:429365, ECO:0000269|Ref.5" FT /id="VAR_003035" FT VARIANT 113 FT /note="C -> Y (in Yahata; dbSNP:rs33932908)" FT /evidence="ECO:0000269|PubMed:1917530" FT /id="VAR_003036" FT VARIANT 115 FT /note="L -> M (in Zengcheng; dbSNP:rs33917394)" FT /evidence="ECO:0000269|PubMed:2079435" FT /id="VAR_010144" FT VARIANT 115 FT /note="L -> P (in B-THAL; Durham-N.C./Brescia; FT dbSNP:rs36015961)" FT /evidence="ECO:0000269|PubMed:1301199, FT ECO:0000269|PubMed:8111050, ECO:0000269|Ref.7" FT /id="VAR_010145" FT VARIANT 116 FT /note="A -> D (in B-THAL; Hradec Kralove; unstable; FT dbSNP:rs35485099)" FT /evidence="ECO:0000269|PubMed:7693620" FT /id="VAR_003037" FT VARIANT 116 FT /note="A -> P (in Madrid; unstable; dbSNP:rs34945623)" FT /id="VAR_003038" FT VARIANT 117 FT /note="H -> L (in Vexin; increased oxygen affinity; FT dbSNP:rs33978082)" FT /evidence="ECO:0000269|PubMed:12908805" FT /id="VAR_025398" FT VARIANT 117 FT /note="H -> Q (in Hafnia; dbSNP:rs35209776)" FT /id="VAR_003039" FT VARIANT 118 FT /note="H -> P (in Saitama; unstable; dbSNP:rs33935673)" FT /evidence="ECO:0000269|PubMed:6687721" FT /id="VAR_003040" FT VARIANT 118 FT /note="H -> R (in P-Galveston; dbSNP:rs33935673)" FT /id="VAR_003041" FT VARIANT 118 FT /note="H -> Y (in Tsukumi; dbSNP:rs33935527)" FT /evidence="ECO:0000269|PubMed:11300344" FT /id="VAR_025399" FT VARIANT 120 FT /note="G -> A (in Iowa; dbSNP:rs33947020)" FT /id="VAR_003042" FT VARIANT 121 FT /note="K -> E (in Hijiyama; dbSNP:rs33924134)" FT /id="VAR_003043" FT VARIANT 121 FT /note="K -> I (in Jianghua; dbSNP:rs34303736)" FT /evidence="ECO:0000269|PubMed:6618888" FT /id="VAR_003044" FT VARIANT 121 FT /note="K -> Q (in Takamatsu; dbSNP:rs33924134)" FT /id="VAR_003045" FT VARIANT 122 FT /note="E -> A (in D-Neath; dbSNP:rs33987957)" FT /evidence="ECO:0000269|PubMed:8330979" FT /id="VAR_003046" FT VARIANT 122 FT /note="E -> G (in St Francis; dbSNP:rs33987957)" FT /id="VAR_003047" FT VARIANT 122 FT /note="E -> K (in O-Arab; dbSNP:rs33946267)" FT /id="VAR_003049" FT VARIANT 122 FT /note="E -> Q (in D-Los FT Angeles/D-Punjab/D-Portugal/D-Chicago/D-Oak Ridge; FT dbSNP:rs33946267)" FT /id="VAR_003048" FT VARIANT 122 FT /note="E -> V (in D-Camperdown/Beograd; dbSNP:rs33987957)" FT /id="VAR_003050" FT VARIANT 124 FT /note="T -> I (in Villejuif; asymptomatic variant; FT dbSNP:rs33935383)" FT /evidence="ECO:0000269|PubMed:11300351" FT /id="VAR_003051" FT VARIANT 125 FT /note="P -> Q (in Ty Gard; O(2) affinity up; FT dbSNP:rs33983276)" FT /evidence="ECO:0000269|Ref.8" FT /id="VAR_003053" FT VARIANT 125 FT /note="P -> R (in Khartoum; unstable; dbSNP:rs33983276)" FT /id="VAR_003052" FT VARIANT 125 FT /note="P -> S (in Tunis; dbSNP:rs35461710)" FT /id="VAR_003054" FT VARIANT 127 FT /note="V -> A (in Beirut; dbSNP:rs33925391)" FT /id="VAR_003055" FT VARIANT 127 FT /note="V -> E (in Hofu; unstable; dbSNP:rs33925391)" FT /id="VAR_003057" FT VARIANT 127 FT /note="V -> G (in B-THAL; Dhonburi/Neapolis; unstable; FT dbSNP:rs33925391)" FT /evidence="ECO:0000269|PubMed:2399911" FT /id="VAR_003056" FT VARIANT 128 FT /note="Q -> E (in Complutense; dbSNP:rs33971634)" FT /evidence="ECO:0000269|PubMed:3707969" FT /id="VAR_003058" FT VARIANT 128 FT /note="Q -> K (in Brest; unstable; dbSNP:rs33971634)" FT /evidence="ECO:0000269|PubMed:3384710" FT /id="VAR_003059" FT VARIANT 129 FT /note="A -> D (in J-Guantanamo; unstable; FT dbSNP:rs33957286)" FT /id="VAR_003060" FT VARIANT 130 FT /note="A -> P (in Crete; O(2) affinity up; unstable; FT dbSNP:rs35939430)" FT /id="VAR_003061" FT VARIANT 130 FT /note="A -> V (in La Desirade; O(2) affinity down; FT unstable; dbSNP:rs111645889)" FT /evidence="ECO:0000269|PubMed:3557994" FT /id="VAR_003062" FT VARIANT 131 FT /note="Y -> D (in Wien; unstable; dbSNP:rs35834416)" FT /id="VAR_003063" FT VARIANT 131 FT /note="Y -> S (in Nevers; dbSNP:rs33937535)" FT /id="VAR_003064" FT VARIANT 132 FT /note="Q -> E (in Camden/Tokuchi/Motown; dbSNP:rs33910209)" FT /id="VAR_003065" FT VARIANT 132 FT /note="Q -> K (in Shelby/Leslie/Deaconess; unstable; FT dbSNP:rs33910209)" FT /evidence="ECO:0000269|PubMed:6526653" FT /id="VAR_003066" FT VARIANT 132 FT /note="Q -> P (in Shangai; unstable; dbSNP:rs33950778)" FT /id="VAR_003067" FT VARIANT 132 FT /note="Q -> R (in Sarrebourg; unstable; dbSNP:rs33950778)" FT /id="VAR_003068" FT VARIANT 133 FT /note="K -> N (in Yamagata; O(2) affinity down; FT dbSNP:rs33946775)" FT /id="VAR_003069" FT VARIANT 133 FT /note="K -> Q (in K-Woolwich; dbSNP:rs33953406)" FT /id="VAR_003070" FT VARIANT 134 FT /note="V -> L (in Extredemura; dbSNP:rs34095019)" FT /id="VAR_003071" FT VARIANT 135 FT /note="V -> E (in North Shore-Caracas; unstable; FT dbSNP:rs33966761)" FT /evidence="ECO:0000269|PubMed:891976" FT /id="VAR_003072" FT VARIANT 136 FT /note="A -> D (in Beckman; originally reported as E-136; FT O(2) affinity down; unstable; dbSNP:rs35669628)" FT /evidence="ECO:0000269|PubMed:19453576, FT ECO:0000269|PubMed:26209877, ECO:0000269|Ref.140" FT /id="VAR_003073" FT VARIANT 136 FT /note="A -> P (in Altdorf; O(2) affinity up; unstable; FT dbSNP:rs35492035)" FT /id="VAR_003074" FT VARIANT 137 FT /note="G -> D (in Hope; O(2) affinity down; unstable; FT dbSNP:rs33949486)" FT /id="VAR_003075" FT VARIANT 139 FT /note="A -> P (in Brockton; unstable; dbSNP:rs33919821)" FT /id="VAR_003076" FT VARIANT 140 FT /note="N -> D (in Geelong; unstable; dbSNP:rs33910475)" FT /evidence="ECO:0000269|PubMed:1917539" FT /id="VAR_003077" FT VARIANT 140 FT /note="N -> K (in Hinsdale; O(2) affinity down; FT dbSNP:rs34240441)" FT /evidence="ECO:0000269|PubMed:2513289" FT /id="VAR_003078" FT VARIANT 140 FT /note="N -> S (in S-Wake; associated in cis with V-6)" FT /evidence="ECO:0000269|Ref.10" FT /id="VAR_025335" FT VARIANT 140 FT /note="N -> Y (in Aurora; O(2) affinity up; FT dbSNP:rs33910475)" FT /evidence="ECO:0000269|PubMed:8718692" FT /id="VAR_003079" FT VARIANT 141 FT /note="A -> D (in Himeji; unstable; O(2) affinity down; FT dbSNP:rs33927093)" FT /evidence="ECO:0000269|PubMed:3754244" FT /id="VAR_003080" FT VARIANT 141 FT /note="A -> T (in St Jacques; O(2) affinity up; FT dbSNP:rs34980264)" FT /id="VAR_003081" FT VARIANT 141 FT /note="A -> V (in Puttelange; polycythemia; O(2) affinity FT up; dbSNP:rs33927093)" FT /evidence="ECO:0000269|PubMed:8522332" FT /id="VAR_003082" FT VARIANT 142 FT /note="L -> R (in Olmsted; unstable; dbSNP:rs35854892)" FT /id="VAR_003083" FT VARIANT 143 FT /note="A -> D (in Ohio; O(2) affinity up; FT dbSNP:rs33921821)" FT /id="VAR_003084" FT VARIANT 144 FT /note="H -> D (in Rancho Mirage; dbSNP:rs33929415)" FT /id="VAR_003085" FT VARIANT 144 FT /note="H -> P (in Syracuse; O(2) affinity up; FT dbSNP:rs33918338)" FT /id="VAR_003087" FT VARIANT 144 FT /note="H -> Q (in Little Rock; O(2) affinity up; FT dbSNP:rs36020563)" FT /id="VAR_003086" FT VARIANT 144 FT /note="H -> R (in Abruzzo; O(2) affinity up; FT dbSNP:rs33918338)" FT /id="VAR_003088" FT VARIANT 145 FT /note="K -> E (in Mito; O(2) affinity up; FT dbSNP:rs33964352)" FT /id="VAR_003089" FT VARIANT 146 FT /note="Y -> C (in Rainier; O(2) affinity up; FT dbSNP:rs35117167)" FT /id="VAR_003090" FT VARIANT 146 FT /note="Y -> H (in Bethesda; O(2) affinity up; FT dbSNP:rs33949869)" FT /id="VAR_003091" FT VARIANT 147 FT /note="H -> D (in Hiroshima; O(2) affinity up; FT dbSNP:rs33961444)" FT /id="VAR_003092" FT VARIANT 147 FT /note="H -> L (in Cowtown; O(2) affinity up; FT dbSNP:rs33954264)" FT /id="VAR_003093" FT VARIANT 147 FT /note="H -> P (in York; O(2) affinity up; FT dbSNP:rs33954264)" FT /id="VAR_003094" FT VARIANT 147 FT /note="H -> Q (in Kodaira; O(2) affinity up; FT dbSNP:rs33985739)" FT /evidence="ECO:0000269|PubMed:1634367" FT /id="VAR_003095" FT CONFLICT 26 FT /note="Missing (in Ref. 15; ACD39349)" FT /evidence="ECO:0000305" FT CONFLICT 42 FT /note="F -> L (in Ref. 13; AAR96398)" FT /evidence="ECO:0000305" FT HELIX 6..17 FT /evidence="ECO:0007829|PDB:2W72" FT HELIX 21..35 FT /evidence="ECO:0007829|PDB:2W72" FT HELIX 37..42 FT /evidence="ECO:0007829|PDB:2W72" FT HELIX 44..46 FT /evidence="ECO:0007829|PDB:1IRD" FT HELIX 52..57 FT /evidence="ECO:0007829|PDB:2W72" FT HELIX 59..75 FT /evidence="ECO:0007829|PDB:2W72" FT TURN 78..80 FT /evidence="ECO:0007829|PDB:1IRD" FT HELIX 82..95 FT /evidence="ECO:0007829|PDB:2W72" FT HELIX 102..119 FT /evidence="ECO:0007829|PDB:2W72" FT HELIX 120..122 FT /evidence="ECO:0007829|PDB:2W72" FT HELIX 125..143 FT /evidence="ECO:0007829|PDB:2W72" FT HELIX 144..146 FT /evidence="ECO:0007829|PDB:1IRD" SQ SEQUENCE 147 AA; 15998 MW; A31F6D621C6556A1 CRC64; MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG KEFTPPVQAA YQKVVAGVAN ALAHKYH //