HBB_HUMAN
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 03-AUG-2022, entry version 200.
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/bf02346198;
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 anemia (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 ---------------------------------------------------------------------------
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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; 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; 7VDE; EM; 3.20 A; B/D=1-147.
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; 7PCF; -.
DR PDBsum; 7PCH; -.
DR PDBsum; 7PCQ; -.
DR PDBsum; 7UD7; -.
DR PDBsum; 7UD8; -.
DR PDBsum; 7UF6; -.
DR PDBsum; 7UF7; -.
DR PDBsum; 7VDE; -.
DR AlphaFoldDB; P68871; -.
DR BMRB; P68871; -.
DR SMR; P68871; -.
DR BioGRID; 109293; 204.
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; 50.
DR MINT; P68871; -.
DR STRING; 9606.ENSP00000333994; -.
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-Linked glycan (3 sites).
DR GlyGen; P68871; 4 sites, 2 O-linked glycans (4 sites).
DR iPTMnet; P68871; -.
DR PhosphoSitePlus; P68871; -.
DR BioMuta; HBB; -.
DR DMDM; 56749856; -.
DR REPRODUCTION-2DPAGE; IPI00654755; -.
DR REPRODUCTION-2DPAGE; P68871; -.
DR SWISS-2DPAGE; P68871; -.
DR UCD-2DPAGE; P68871; -.
DR EPD; P68871; -.
DR jPOST; P68871; -.
DR MassIVE; P68871; -.
DR MaxQB; P68871; -.
DR PaxDb; P68871; -.
DR PeptideAtlas; P68871; -.
DR PRIDE; P68871; -.
DR ProteomicsDB; 57543; -.
DR TopDownProteomics; P68871; -.
DR ABCD; P68871; 2 sequenced antibodies.
DR Antibodypedia; 34986; 407 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 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; TPDAVMN; -.
DR OrthoDB; 1479834at2759; -.
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; 13 hits in 1071 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 204 other tissues.
DR ExpressionAtlas; P68871; baseline and differential.
DR Genevisible; P68871; HS.
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:0015670; P:carbon dioxide transport; IC:ComplexPortal.
DR GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:BHF-UCL.
DR GO; GO:0030185; P:nitric oxide transport; IDA:ComplexPortal.
DR GO; GO:0015671; P:oxygen transport; IDA:ComplexPortal.
DR GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB.
DR GO; GO:0010942; P:positive regulation of cell death; IDA:BHF-UCL.
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; -; 1.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR002337; Hemoglobin_b.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00814; BETAHAEM.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
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 J-Baltimore/J-Trinidad/J-Ireland/J-
FT Georgia/N-New Haven; 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 with S-
FT 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 with P-
FT 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 Angeles/D-Punjab/D-Portugal/D-
FT Chicago/D-Oak Ridge; 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 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
