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Hemoglobin subunit beta-1 (Beta-1-globin) (Hemoglobin beta-1 chain) (Hemoglobin beta-major chain)

 HBB1_MOUSE              Reviewed;         147 AA.
P02088; Q54AI0; Q91V86; Q9CRZ2; Q9CXH5; Q9CY12; Q9CY54; Q9R0S6;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-FEB-2018, entry version 169.
RecName: Full=Hemoglobin subunit beta-1;
AltName: Full=Beta-1-globin;
AltName: Full=Hemoglobin beta-1 chain;
AltName: Full=Hemoglobin beta-major chain;
Name=Hbb-b1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2926808; DOI=10.1016/0022-2836(89)90363-X;
Shehee W.R., Loeb D.D., Adey N.B., Burton F.H., Casavant N.C.,
Cole P., Davies C.J., McGraw R.A., Schichman S.A., Severynse D.M.,
Voliva C.F., Weyter F.W., Wisely G.B., Edgell M.H.,
Hutchison C.A. III;
"Nucleotide sequence of the BALB/c mouse beta-globin complex.";
J. Mol. Biol. 205:41-62(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ;
PubMed=519759; DOI=10.1016/0092-8674(79)90138-7;
Konkel D.A., Maizel J.V. Jr., Leder P.;
"The evolution and sequence comparison of two recently diverged mouse
chromosomal beta-globin genes.";
Cell 18:865-873(1979).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=482942; DOI=10.1126/science.482942;
van Ooyen A., van den Berg J., Mantei N., Weissmann C.;
"Comparison of total sequence of a cloned rabbit beta-globin gene and
its flanking regions with a homologous mouse sequence.";
Science 206:337-344(1979).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE S).
STRAIN=C57BL/10;
PubMed=3870864;
Erhart M.A., Simons K.S., Weaver S.;
"Evolution of the mouse beta-globin genes: a recent gene conversion in
the Hbbs haplotype.";
Mol. Biol. Evol. 2:304-320(1985).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELES P AND W1).
PubMed=10441738; DOI=10.1007/s003359901107;
Ueda Y., Miyashita N., Imai K., Yamaguchi Y., Takamura K.,
Notohara M., Shiroishi T., Kawashima T., Ning L., Wang C., Wu X.,
Moriwaki K.;
"Nucleotide sequences of the mouse globin beta gene cDNAs in a wild
derived new haplotype Hbb(w1).";
Mamm. Genome 10:879-882(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Head, Heart, Kidney, Liver, Placenta, Spleen, Stomach, and
Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[7]
PROTEIN SEQUENCE OF 19-41; 32-60 AND 67-145, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 86-109.
PubMed=277329;
Curtis P.J., Mantei N., Weissmann C.;
"Characterization and kinetics of synthesis of 15S beta-globin RNA, a
putative precursor of beta-globin mRNA.";
Cold Spring Harb. Symp. Quant. Biol. 42:971-984(1978).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-44 AND 100-115.
PubMed=264241; DOI=10.1038/276037a0;
van den Berg J., van Ooyen A., Mantei N., Schamboeck A., Grosveld G.,
Flavell R.A., Weissmann C.;
"Comparison of cloned rabbit and mouse beta-globin genes showing
strong evolutionary divergence of two homologous pairs of introns.";
Nature 276:37-44(1978).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-105.
PubMed=273235; DOI=10.1073/pnas.75.2.725;
Tilghman S.M., Tiemeier D.C., Seidman J.G., Peterlin B.M.,
Sullivan M., Maizel J.V. Jr., Leder P.;
"Intervening sequence of DNA identified in the structural portion of a
mouse beta-globin gene.";
Proc. Natl. Acad. Sci. U.S.A. 75:725-729(1978).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-18, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[14]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-147 IN COMPLEX WITH HEME.
PubMed=11747442; DOI=10.1021/bi011329f;
Kidd R.D., Russell J.E., Watmough N.J., Baker E.N., Brittain T.;
"The role of beta chains in the control of the hemoglobin oxygen
binding function: chimeric human/mouse proteins, structure, and
function.";
Biochemistry 40:15669-15675(2001).
[15]
VARIANTS ALLELIC.
PubMed=999642; DOI=10.1042/bj1590043;
Gilman J.G.;
"Mouse haemoglobin beta chains. Comparative sequence data on adult
major and minor beta chains from two species, Mus musculus and Mus
cervicolor.";
Biochem. J. 159:43-53(1976).
-!- FUNCTION: Involved in oxygen transport from the lung to the
various peripheral tissues.
-!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
-!- TISSUE SPECIFICITY: Red blood cells.
-!- POLYMORPHISM: Inbred mouse strains possess 1 of 4 alleles at the
HBB locus: D (diffuse), S (single), P and W1. The D and P alleles
are actually closely linked doublets that coordinately express a
major and a minor chain, the minor chain being slightly different
in the two alleles. The S allele produces only 1 chain, it is
characteristic of North American wild mice. The W1 allele is
observed mainly in Northwestern China.
{ECO:0000269|PubMed:10441738, ECO:0000269|PubMed:3870864,
ECO:0000269|PubMed:999642}.
-!- MISCELLANEOUS: The D-major sequence is shown. See also the entry
for the beta D and P-minor chain.
-!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
ProRule:PRU00238}.
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EMBL; X14061; CAA32224.1; -; Genomic_DNA.
EMBL; J00413; AAA37791.1; -; Genomic_DNA.
EMBL; AB020013; BAA77353.1; -; mRNA.
EMBL; AB020015; BAA77355.1; -; mRNA.
EMBL; AK002258; BAB21971.1; -; mRNA.
EMBL; AK002394; BAB22067.1; -; mRNA.
EMBL; AK003096; BAB22562.1; -; mRNA.
EMBL; AK003472; BAB22806.1; -; mRNA.
EMBL; AK005442; BAB24036.1; -; mRNA.
EMBL; AK005490; BAB24075.1; -; mRNA.
EMBL; AK005496; BAB24080.1; -; mRNA.
EMBL; AK010873; BAB27237.1; -; mRNA.
EMBL; AK010902; BAB27255.1; -; mRNA.
EMBL; AK010980; BAB27302.1; -; mRNA.
EMBL; AK010981; BAB27303.1; -; mRNA.
EMBL; AK010991; BAB27310.1; -; mRNA.
EMBL; AK010993; BAB27312.1; -; mRNA.
EMBL; AK011006; BAB27325.1; -; mRNA.
EMBL; AK011013; BAB27331.1; -; mRNA.
EMBL; AK011016; BAB27334.1; -; mRNA.
EMBL; AK011027; BAB27343.1; -; mRNA.
EMBL; AK011033; BAB27347.1; -; mRNA.
EMBL; AK011050; BAB27360.1; -; mRNA.
EMBL; AK011052; BAB27361.1; -; mRNA.
EMBL; AK011053; BAB27362.1; -; mRNA.
EMBL; AK011057; BAB27365.1; -; mRNA.
EMBL; AK011067; BAB27374.1; -; mRNA.
EMBL; AK011069; BAB27376.1; -; mRNA.
EMBL; AK011075; BAB27380.1; -; mRNA.
EMBL; AK011077; BAB27382.1; -; mRNA.
EMBL; AK011083; BAB27387.1; -; mRNA.
EMBL; AK011102; BAB27399.1; -; mRNA.
EMBL; AK012551; BAB28311.1; -; mRNA.
EMBL; AK014364; BAB29299.1; -; mRNA.
EMBL; AK027903; BAC25655.1; -; mRNA.
EMBL; AK027904; BAC25656.1; -; mRNA.
EMBL; AK028067; BAC25734.1; -; mRNA.
EMBL; AK088149; BAC40173.1; -; mRNA.
EMBL; AK133714; BAE21794.1; -; mRNA.
EMBL; AK147001; BAE27598.1; -; mRNA.
EMBL; AK160629; BAE35926.1; -; mRNA.
EMBL; AK161021; BAE36152.1; -; mRNA.
EMBL; AK165490; BAE38217.1; -; mRNA.
EMBL; AK167615; BAE39668.1; -; mRNA.
EMBL; AK168412; BAE40327.1; -; mRNA.
EMBL; AK168477; BAE40366.1; -; mRNA.
EMBL; AK168562; BAE40435.1; -; mRNA.
EMBL; AK168584; BAE40453.1; -; mRNA.
EMBL; AK168819; BAE40646.1; -; mRNA.
EMBL; AK168826; BAE40653.1; -; mRNA.
EMBL; AK168846; BAE40669.1; -; mRNA.
EMBL; M19236; AAA37788.1; -; mRNA.
EMBL; M10828; AAA37786.1; -; Genomic_DNA.
EMBL; M10830; AAA37787.1; -; Genomic_DNA.
EMBL; M10829; AAA37787.1; JOINED; Genomic_DNA.
EMBL; M10688; AAA37790.1; -; Genomic_DNA.
PIR; A90790; HBMS.
RefSeq; NP_001188320.1; NM_001201391.1.
RefSeq; NP_001265090.1; NM_001278161.1.
RefSeq; NP_032246.2; NM_008220.5.
UniGene; Mm.288567; -.
UniGene; Mm.467412; -.
PDB; 1JEB; X-ray; 2.10 A; B/D=2-147.
PDB; 3HRW; X-ray; 2.80 A; B/D=2-147.
PDBsum; 1JEB; -.
PDBsum; 3HRW; -.
ProteinModelPortal; P02088; -.
SMR; P02088; -.
BioGrid; 200219; 5.
IntAct; P02088; 11.
MINT; P02088; -.
STRING; 10090.ENSMUSP00000095794; -.
CarbonylDB; P02088; -.
iPTMnet; P02088; -.
PhosphoSitePlus; P02088; -.
SwissPalm; P02088; -.
REPRODUCTION-2DPAGE; IPI00553333; -.
REPRODUCTION-2DPAGE; P02088; -.
SWISS-2DPAGE; P02088; -.
MaxQB; P02088; -.
PaxDb; P02088; -.
PeptideAtlas; P02088; -.
PRIDE; P02088; -.
DNASU; 15129; -.
GeneID; 100503605; -.
GeneID; 101488143; -.
GeneID; 15129; -.
KEGG; mmu:100503605; -.
KEGG; mmu:101488143; -.
KEGG; mmu:15129; -.
UCSC; uc009iuq.3; mouse.
CTD; 100503605; -.
CTD; 101488143; -.
CTD; 15129; -.
MGI; MGI:96021; Hbb-b1.
eggNOG; KOG3378; Eukaryota.
eggNOG; COG1018; LUCA.
HOVERGEN; HBG009709; -.
InParanoid; P02088; -.
KO; K13823; -.
PhylomeDB; P02088; -.
ChiTaRS; Hbb-b1; mouse.
EvolutionaryTrace; P02088; -.
PRO; PR:P02088; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_HBB-B1; -.
GO; GO:0005833; C:hemoglobin complex; IDA:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0019825; F:oxygen binding; IEA:InterPro.
GO; GO:0005344; F:oxygen carrier activity; IMP:MGI.
GO; GO:0048821; P:erythrocyte development; IGI:MGI.
GO; GO:0030097; P:hemopoiesis; IMP:MGI.
GO; GO:0015671; P:oxygen transport; IMP:MGI.
GO; GO:0010999; P:regulation of eIF2 alpha phosphorylation by heme; IMP:MGI.
CDD; cd08925; Hb-beta_like; 1.
InterPro; IPR000971; Globin.
InterPro; IPR009050; Globin-like_sf.
InterPro; IPR002337; Haemoglobin_b.
Pfam; PF00042; Globin; 1.
PRINTS; PR00814; BETAHAEM.
SUPFAM; SSF46458; SSF46458; 1.
PROSITE; PS01033; GLOBIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Heme; Iron; Metal-binding; Methylation;
Oxygen transport; Phosphoprotein; Polymorphism; Reference proteome;
Transport.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P02086}.
CHAIN 2 147 Hemoglobin subunit beta-1.
/FTId=PRO_0000053024.
METAL 64 64 Iron (heme distal ligand).
{ECO:0000250|UniProtKB:P80044}.
METAL 93 93 Iron (heme proximal ligand).
{ECO:0000244|PDB:1JEB,
ECO:0000244|PDB:3HRW,
ECO:0000269|PubMed:11747442}.
MOD_RES 2 2 N-acetylvaline.
{ECO:0000250|UniProtKB:P02086}.
MOD_RES 18 18 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000250|UniProtKB:P02091}.
MOD_RES 51 51 Phosphoserine.
{ECO:0000250|UniProtKB:P02091}.
MOD_RES 60 60 N6-succinyllysine.
{ECO:0000250|UniProtKB:P02089}.
MOD_RES 105 105 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:P02089}.
MOD_RES 124 124 Phosphothreonine.
{ECO:0000250|UniProtKB:P11517}.
VARIANT 14 14 C -> G (in allele S and allele W1).
{ECO:0000269|PubMed:10441738,
ECO:0000269|PubMed:3870864,
ECO:0000269|PubMed:999642}.
VARIANT 21 21 S -> A (in allele S).
{ECO:0000269|PubMed:3870864,
ECO:0000269|PubMed:999642}.
VARIANT 74 74 D -> E (in allele W1).
{ECO:0000269|PubMed:10441738,
ECO:0000269|PubMed:999642}.
VARIANT 135 135 V -> M (in allele W1).
{ECO:0000269|PubMed:10441738,
ECO:0000269|PubMed:999642}.
VARIANT 140 140 T -> A (in allele S).
{ECO:0000269|PubMed:3870864,
ECO:0000269|PubMed:999642}.
CONFLICT 15 15 L -> Q (in Ref. 6; BAB27362).
{ECO:0000305}.
CONFLICT 39 39 T -> A (in Ref. 6; BAB29299).
{ECO:0000305}.
CONFLICT 63 63 A -> T (in Ref. 6; BAB27237).
{ECO:0000305}.
CONFLICT 91 91 E -> Q (in Ref. 3). {ECO:0000305}.
CONFLICT 109 109 N -> S (in Ref. 6; BAB29299).
{ECO:0000305}.
HELIX 6 18 {ECO:0000244|PDB:1JEB}.
HELIX 21 35 {ECO:0000244|PDB:1JEB}.
HELIX 37 42 {ECO:0000244|PDB:1JEB}.
HELIX 52 56 {ECO:0000244|PDB:1JEB}.
HELIX 59 77 {ECO:0000244|PDB:1JEB}.
HELIX 82 94 {ECO:0000244|PDB:1JEB}.
TURN 95 97 {ECO:0000244|PDB:1JEB}.
HELIX 102 119 {ECO:0000244|PDB:1JEB}.
HELIX 120 122 {ECO:0000244|PDB:1JEB}.
HELIX 125 143 {ECO:0000244|PDB:1JEB}.
SEQUENCE 147 AA; 15840 MW; 8190EAEEFD9036A3 CRC64;
MVHLTDAEKA AVSCLWGKVN SDEVGGEALG RLLVVYPWTQ RYFDSFGDLS SASAIMGNAK
VKAHGKKVIT AFNDGLNHLD SLKGTFASLS ELHCDKLHVD PENFRLLGNM IVIVLGHHLG
KDFTPAAQAA FQKVVAGVAT ALAHKYH


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E0996Rb ELISA Gamma-globin,HBG,Hemoglobin beta-3,Hemoglobin gamma chain,Hemoglobin subunit gamma,Oryctolagus cuniculus,Rabbit 96T


 

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