ID   HBB1_MOUSE              Reviewed;         147 AA.
AC   P02088; Q54AI0; Q91V86; Q9CRZ2; Q9CXH5; Q9CY12; Q9CY54; Q9R0S6;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 197.
DE   RecName: Full=Hemoglobin subunit beta-1;
DE   AltName: Full=Beta-1-globin;
DE   AltName: Full=Hemoglobin beta-1 chain;
DE   AltName: Full=Hemoglobin beta-major chain;
GN   Name=Hbb-b1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2926808; DOI=10.1016/0022-2836(89)90363-x;
RA   Shehee W.R., Loeb D.D., Adey N.B., Burton F.H., Casavant N.C., Cole P.,
RA   Davies C.J., McGraw R.A., Schichman S.A., Severynse D.M., Voliva C.F.,
RA   Weyter F.W., Wisely G.B., Edgell M.H., Hutchison C.A. III;
RT   "Nucleotide sequence of the BALB/c mouse beta-globin complex.";
RL   J. Mol. Biol. 205:41-62(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/cJ;
RX   PubMed=519759; DOI=10.1016/0092-8674(79)90138-7;
RA   Konkel D.A., Maizel J.V. Jr., Leder P.;
RT   "The evolution and sequence comparison of two recently diverged mouse
RT   chromosomal beta-globin genes.";
RL   Cell 18:865-873(1979).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=482942; DOI=10.1126/science.482942;
RA   van Ooyen A., van den Berg J., Mantei N., Weissmann C.;
RT   "Comparison of total sequence of a cloned rabbit beta-globin gene and its
RT   flanking regions with a homologous mouse sequence.";
RL   Science 206:337-344(1979).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE S).
RC   STRAIN=C57BL/10;
RX   PubMed=3870864; DOI=10.1093/oxfordjournals.molbev.a040353;
RA   Erhart M.A., Simons K.S., Weaver S.;
RT   "Evolution of the mouse beta-globin genes: a recent gene conversion in the
RT   Hbbs haplotype.";
RL   Mol. Biol. Evol. 2:304-320(1985).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELES P AND W1).
RX   PubMed=10441738; DOI=10.1007/s003359901107;
RA   Ueda Y., Miyashita N., Imai K., Yamaguchi Y., Takamura K., Notohara M.,
RA   Shiroishi T., Kawashima T., Ning L., Wang C., Wu X., Moriwaki K.;
RT   "Nucleotide sequences of the mouse globin beta gene cDNAs in a wild derived
RT   new haplotype Hbb(w1).";
RL   Mamm. Genome 10:879-882(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Head, Heart, Kidney, Liver, Placenta, Spleen, Stomach, and
RC   Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [7]
RP   PROTEIN SEQUENCE OF 19-41; 32-60 AND 67-145, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 86-109.
RX   PubMed=277329; DOI=10.1101/sqb.1978.042.01.098;
RA   Curtis P.J., Mantei N., Weissmann C.;
RT   "Characterization and kinetics of synthesis of 15S beta-globin RNA, a
RT   putative precursor of beta-globin mRNA.";
RL   Cold Spring Harb. Symp. Quant. Biol. 42:971-984(1978).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-44 AND 100-115.
RX   PubMed=264241; DOI=10.1038/276037a0;
RA   van den Berg J., van Ooyen A., Mantei N., Schamboeck A., Grosveld G.,
RA   Flavell R.A., Weissmann C.;
RT   "Comparison of cloned rabbit and mouse beta-globin genes showing strong
RT   evolutionary divergence of two homologous pairs of introns.";
RL   Nature 276:37-44(1978).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-105.
RX   PubMed=273235; DOI=10.1073/pnas.75.2.725;
RA   Tilghman S.M., Tiemeier D.C., Seidman J.G., Peterlin B.M., Sullivan M.,
RA   Maizel J.V. Jr., Leder P.;
RT   "Intervening sequence of DNA identified in the structural portion of a
RT   mouse beta-globin gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 75:725-729(1978).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [13]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-18, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-147 IN COMPLEX WITH HEME.
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   [15]
RP   VARIANTS ALLELIC.
RX   PubMed=999642; DOI=10.1042/bj1590043;
RA   Gilman J.G.;
RT   "Mouse haemoglobin beta chains. Comparative sequence data on adult major
RT   and minor beta chains from two species, Mus musculus and Mus cervicolor.";
RL   Biochem. J. 159:43-53(1976).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- POLYMORPHISM: Inbred mouse strains possess 1 of 4 alleles at the HBB
CC       locus: D (diffuse), S (single), P and W1. The D and P alleles are
CC       actually closely linked doublets that coordinately express a major and
CC       a minor chain, the minor chain being slightly different in the two
CC       alleles. The S allele produces only 1 chain, it is characteristic of
CC       North American wild mice. The W1 allele is observed mainly in
CC       Northwestern China. {ECO:0000269|PubMed:10441738,
CC       ECO:0000269|PubMed:3870864, ECO:0000269|PubMed:999642}.
CC   -!- MISCELLANEOUS: The D-major sequence is shown. See also the entry for
CC       the beta D and P-minor chain.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; X14061; CAA32224.1; -; Genomic_DNA.
DR   EMBL; J00413; AAA37791.1; -; Genomic_DNA.
DR   EMBL; AB020013; BAA77353.1; -; mRNA.
DR   EMBL; AB020015; BAA77355.1; -; mRNA.
DR   EMBL; AK002258; BAB21971.1; -; mRNA.
DR   EMBL; AK002394; BAB22067.1; -; mRNA.
DR   EMBL; AK003096; BAB22562.1; -; mRNA.
DR   EMBL; AK003472; BAB22806.1; -; mRNA.
DR   EMBL; AK005442; BAB24036.1; -; mRNA.
DR   EMBL; AK005490; BAB24075.1; -; mRNA.
DR   EMBL; AK005496; BAB24080.1; -; mRNA.
DR   EMBL; AK010873; BAB27237.1; -; mRNA.
DR   EMBL; AK010902; BAB27255.1; -; mRNA.
DR   EMBL; AK010980; BAB27302.1; -; mRNA.
DR   EMBL; AK010981; BAB27303.1; -; mRNA.
DR   EMBL; AK010991; BAB27310.1; -; mRNA.
DR   EMBL; AK010993; BAB27312.1; -; mRNA.
DR   EMBL; AK011006; BAB27325.1; -; mRNA.
DR   EMBL; AK011013; BAB27331.1; -; mRNA.
DR   EMBL; AK011016; BAB27334.1; -; mRNA.
DR   EMBL; AK011027; BAB27343.1; -; mRNA.
DR   EMBL; AK011033; BAB27347.1; -; mRNA.
DR   EMBL; AK011050; BAB27360.1; -; mRNA.
DR   EMBL; AK011052; BAB27361.1; -; mRNA.
DR   EMBL; AK011053; BAB27362.1; -; mRNA.
DR   EMBL; AK011057; BAB27365.1; -; mRNA.
DR   EMBL; AK011067; BAB27374.1; -; mRNA.
DR   EMBL; AK011069; BAB27376.1; -; mRNA.
DR   EMBL; AK011075; BAB27380.1; -; mRNA.
DR   EMBL; AK011077; BAB27382.1; -; mRNA.
DR   EMBL; AK011083; BAB27387.1; -; mRNA.
DR   EMBL; AK011102; BAB27399.1; -; mRNA.
DR   EMBL; AK012551; BAB28311.1; -; mRNA.
DR   EMBL; AK014364; BAB29299.1; -; mRNA.
DR   EMBL; AK027903; BAC25655.1; -; mRNA.
DR   EMBL; AK027904; BAC25656.1; -; mRNA.
DR   EMBL; AK028067; BAC25734.1; -; mRNA.
DR   EMBL; AK088149; BAC40173.1; -; mRNA.
DR   EMBL; AK133714; BAE21794.1; -; mRNA.
DR   EMBL; AK147001; BAE27598.1; -; mRNA.
DR   EMBL; AK160629; BAE35926.1; -; mRNA.
DR   EMBL; AK161021; BAE36152.1; -; mRNA.
DR   EMBL; AK165490; BAE38217.1; -; mRNA.
DR   EMBL; AK167615; BAE39668.1; -; mRNA.
DR   EMBL; AK168412; BAE40327.1; -; mRNA.
DR   EMBL; AK168477; BAE40366.1; -; mRNA.
DR   EMBL; AK168562; BAE40435.1; -; mRNA.
DR   EMBL; AK168584; BAE40453.1; -; mRNA.
DR   EMBL; AK168819; BAE40646.1; -; mRNA.
DR   EMBL; AK168826; BAE40653.1; -; mRNA.
DR   EMBL; AK168846; BAE40669.1; -; mRNA.
DR   EMBL; M19236; AAA37788.1; -; mRNA.
DR   EMBL; M10828; AAA37786.1; -; Genomic_DNA.
DR   EMBL; M10830; AAA37787.1; -; Genomic_DNA.
DR   EMBL; M10829; AAA37787.1; JOINED; Genomic_DNA.
DR   EMBL; M10688; AAA37790.1; -; Genomic_DNA.
DR   PIR; A90790; HBMS.
DR   RefSeq; NP_001188320.1; NM_001201391.1.
DR   RefSeq; NP_001265090.1; NM_001278161.1.
DR   RefSeq; NP_032246.2; NM_008220.5.
DR   PDB; 1JEB; X-ray; 2.10 A; B/D=2-147.
DR   PDB; 3HRW; X-ray; 2.80 A; B/D=2-147.
DR   PDBsum; 1JEB; -.
DR   PDBsum; 3HRW; -.
DR   AlphaFoldDB; P02088; -.
DR   SMR; P02088; -.
DR   BioGRID; 1639840; 3.
DR   BioGRID; 200219; 9.
DR   BioGRID; 3405151; 3.
DR   ComplexPortal; CPX-2922; Hemoglobin HbA complex, variant HBB1.
DR   IntAct; P02088; 7.
DR   MINT; P02088; -.
DR   STRING; 10090.ENSMUSP00000023934; -.
DR   CarbonylDB; P02088; -.
DR   GlyGen; P02088; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P02088; -.
DR   PhosphoSitePlus; P02088; -.
DR   SwissPalm; P02088; -.
DR   REPRODUCTION-2DPAGE; IPI00553333; -.
DR   REPRODUCTION-2DPAGE; P02088; -.
DR   jPOST; P02088; -.
DR   MaxQB; P02088; -.
DR   PaxDb; 10090-ENSMUSP00000023934; -.
DR   PeptideAtlas; P02088; -.
DR   ProteomicsDB; 269721; -.
DR   DNASU; 15129; -.
DR   GeneID; 100503605; -.
DR   GeneID; 101488143; -.
DR   GeneID; 15129; -.
DR   KEGG; mmu:100503605; -.
DR   KEGG; mmu:101488143; -.
DR   KEGG; mmu:15129; -.
DR   UCSC; uc009iuq.3; mouse.
DR   AGR; MGI:96021; -.
DR   CTD; 100503605; -.
DR   CTD; 101488143; -.
DR   CTD; 15129; -.
DR   MGI; MGI:96021; Hbb-b1.
DR   eggNOG; KOG3378; Eukaryota.
DR   InParanoid; P02088; -.
DR   OrthoDB; 5356926at2759; -.
DR   PhylomeDB; P02088; -.
DR   BioGRID-ORCS; 100503605; 0 hits in 23 CRISPR screens.
DR   BioGRID-ORCS; 101488143; 0 hits in 23 CRISPR screens.
DR   BioGRID-ORCS; 15129; 3 hits in 18 CRISPR screens.
DR   EvolutionaryTrace; P02088; -.
DR   PRO; PR:P02088; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P02088; Protein.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0031838; C:haptoglobin-hemoglobin complex; ISO:MGI.
DR   GO; GO:0005833; C:hemoglobin complex; IDA:MGI.
DR   GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0031721; F:hemoglobin alpha binding; ISO:MGI.
DR   GO; GO:0031722; F:hemoglobin beta binding; ISO:MGI.
DR   GO; GO:0030492; F:hemoglobin binding; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0005344; F:oxygen carrier activity; IMP:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0015670; P:carbon dioxide transport; NAS:ComplexPortal.
DR   GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR   GO; GO:0048821; P:erythrocyte development; IGI:MGI.
DR   GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0030185; P:nitric oxide transport; ISO:ComplexPortal.
DR   GO; GO:0015671; P:oxygen transport; IMP:MGI.
DR   GO; GO:0010999; P:regulation of eIF2 alpha phosphorylation by heme; IMP:MGI.
DR   CDD; cd08925; Hb-beta-like; 1.
DR   Gene3D; 1.10.490.10; Globins; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR002337; Hemoglobin_b.
DR   PANTHER; PTHR11442; HEMOGLOBIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR11442:SF42; HEMOGLOBIN SUBUNIT BETA; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00814; BETAHAEM.
DR   SUPFAM; SSF46458; Globin-like; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
DR   SWISS-2DPAGE; P02088; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Heme; Iron;
KW   Metal-binding; Methylation; Oxygen transport; Phosphoprotein;
KW   Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02086"
FT   CHAIN           2..147
FT                   /note="Hemoglobin subunit beta-1"
FT                   /id="PRO_0000053024"
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                   /evidence="ECO:0000250|UniProtKB:P80044"
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                   /evidence="ECO:0000269|PubMed:11747442,
FT                   ECO:0007744|PDB:1JEB, ECO:0007744|PDB:3HRW"
FT   MOD_RES         2
FT                   /note="N-acetylvaline"
FT                   /evidence="ECO:0000250|UniProtKB:P02086"
FT   MOD_RES         18
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02091"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02091"
FT   MOD_RES         60
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02089"
FT   MOD_RES         105
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P02089"
FT   MOD_RES         124
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P11517"
FT   VARIANT         14
FT                   /note="C -> G (in allele S and allele W1)"
FT                   /evidence="ECO:0000269|PubMed:10441738,
FT                   ECO:0000269|PubMed:3870864, ECO:0000269|PubMed:999642"
FT   VARIANT         21
FT                   /note="S -> A (in allele S)"
FT                   /evidence="ECO:0000269|PubMed:3870864,
FT                   ECO:0000269|PubMed:999642"
FT   VARIANT         74
FT                   /note="D -> E (in allele W1)"
FT                   /evidence="ECO:0000269|PubMed:10441738,
FT                   ECO:0000269|PubMed:999642"
FT   VARIANT         135
FT                   /note="V -> M (in allele W1)"
FT                   /evidence="ECO:0000269|PubMed:10441738,
FT                   ECO:0000269|PubMed:999642"
FT   VARIANT         140
FT                   /note="T -> A (in allele S)"
FT                   /evidence="ECO:0000269|PubMed:3870864,
FT                   ECO:0000269|PubMed:999642"
FT   CONFLICT        15
FT                   /note="L -> Q (in Ref. 6; BAB27362)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="T -> A (in Ref. 6; BAB29299)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63
FT                   /note="A -> T (in Ref. 6; BAB27237)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91
FT                   /note="E -> Q (in Ref. 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        109
FT                   /note="N -> S (in Ref. 6; BAB29299)"
FT                   /evidence="ECO:0000305"
FT   HELIX           6..18
FT                   /evidence="ECO:0007829|PDB:1JEB"
FT   HELIX           21..35
FT                   /evidence="ECO:0007829|PDB:1JEB"
FT   HELIX           37..42
FT                   /evidence="ECO:0007829|PDB:1JEB"
FT   HELIX           52..56
FT                   /evidence="ECO:0007829|PDB:1JEB"
FT   HELIX           59..77
FT                   /evidence="ECO:0007829|PDB:1JEB"
FT   HELIX           82..94
FT                   /evidence="ECO:0007829|PDB:1JEB"
FT   TURN            95..97
FT                   /evidence="ECO:0007829|PDB:1JEB"
FT   HELIX           102..119
FT                   /evidence="ECO:0007829|PDB:1JEB"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:1JEB"
FT   HELIX           125..143
FT                   /evidence="ECO:0007829|PDB:1JEB"
SQ   SEQUENCE   147 AA;  15840 MW;  8190EAEEFD9036A3 CRC64;
     MVHLTDAEKA AVSCLWGKVN SDEVGGEALG RLLVVYPWTQ RYFDSFGDLS SASAIMGNAK
     VKAHGKKVIT AFNDGLNHLD SLKGTFASLS ELHCDKLHVD PENFRLLGNM IVIVLGHHLG
     KDFTPAAQAA FQKVVAGVAT ALAHKYH
//