HBB2_MOUSE
ID HBB2_MOUSE Reviewed; 147 AA.
AC P02089; Q5D0E8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Hemoglobin subunit beta-2;
DE AltName: Full=Beta-2-globin;
DE AltName: Full=Hemoglobin beta-2 chain;
DE AltName: Full=Hemoglobin beta-minor chain;
GN Name=Hbb-b2;
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.
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 [LARGE SCALE MRNA], AND VARIANT 24-ALA--ILE-25.
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland, and Salivary gland;
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 [4]
RP POLYMORPHISM, AND VARIANT 23-ALA-ILE-24.
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-42; SER-45 AND SER-53, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-18 AND LYS-60, AND
RP IDENTIFICATION BY MASS 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 [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-105, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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 3 alleles at the HBB
CC locus: D (diffuse), S (single), and P. The D and P alleles are actually
CC closely linked doublets that coordinately express a major and a minor
CC chain, the minor chain being slightly different in the two alleles. The
CC S allele produces only 1 chain, it is characteristic of North American
CC wild mice. {ECO:0000269|PubMed:999642}.
CC -!- MISCELLANEOUS: The D-minor sequence is shown. See also the entry for
CC the beta D-major chain and the S allele.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; V00722; CAA24101.1; -; Genomic_DNA.
DR EMBL; X14061; CAA32225.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC027434; AAH27434.1; -; mRNA.
DR EMBL; BC032264; AAH32264.1; -; mRNA.
DR PIR; B90790; HBMSN1.
DR RefSeq; NP_058652.1; NM_016956.3.
DR PDB; 1FNE; X-ray; 1.90 A; B/D=65-77.
DR PDB; 1FNG; X-ray; 1.90 A; B/D=65-77.
DR PDB; 1I3R; X-ray; 2.40 A; B/D/F/H=65-77.
DR PDBsum; 1FNE; -.
DR PDBsum; 1FNG; -.
DR PDBsum; 1I3R; -.
DR AlphaFoldDB; P02089; -.
DR SMR; P02089; -.
DR BioGRID; 200220; 4.
DR ComplexPortal; CPX-2924; Hemoglobin HbA complex, variant HBB2.
DR IntAct; P02089; 8.
DR MINT; P02089; -.
DR ChEMBL; CHEMBL4007; -.
DR CarbonylDB; P02089; -.
DR iPTMnet; P02089; -.
DR PhosphoSitePlus; P02089; -.
DR SwissPalm; P02089; -.
DR CPTAC; non-CPTAC-4038; -.
DR jPOST; P02089; -.
DR PeptideAtlas; P02089; -.
DR PRIDE; P02089; -.
DR ProteomicsDB; 270896; -.
DR DNASU; 15130; -.
DR GeneID; 15130; -.
DR KEGG; mmu:15130; -.
DR UCSC; uc009iup.1; mouse.
DR CTD; 15130; -.
DR MGI; MGI:96022; Hbb-b2.
DR InParanoid; P02089; -.
DR OrthoDB; 1370439at2759; -.
DR BioGRID-ORCS; 15130; 0 hits in 17 CRISPR screens.
DR EvolutionaryTrace; P02089; -.
DR PRO; PR:P02089; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P02089; 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; IMP:MGI.
DR GO; GO:0031720; F:haptoglobin binding; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central.
DR GO; GO:0004601; F:peroxidase activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0015670; P:carbon dioxide transport; IC:ComplexPortal.
DR GO; GO:0048821; P:erythrocyte development; IGI:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; ISO:MGI.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI.
DR GO; GO:0015671; P:oxygen transport; ISO:MGI.
DR GO; GO:0045639; P:positive regulation of myeloid cell differentiation; IMP:MGI.
DR GO; GO:0045646; P:regulation of erythrocyte differentiation; IMP:MGI.
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; Heme; Iron; Metal-binding; Methylation;
KW Oxygen transport; Phosphoprotein; 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-2"
FT /id="PRO_0000053025"
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 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 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 42
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02091"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 60
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 105
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11517"
FT VARIANT 23..24
FT /note="EV -> AI (in allele P)"
FT /evidence="ECO:0000269|PubMed:999642"
SQ SEQUENCE 147 AA; 15878 MW; 1FABBDC2D0ABC4FD CRC64;
MVHLTDAEKS AVSCLWAKVN PDEVGGEALG RLLVVYPWTQ RYFDSFGDLS SASAIMGNPK
VKAHGKKVIT AFNEGLKNLD NLKGTFASLS ELHCDKLHVD PENFRLLGNA IVIVLGHHLG
KDFTPAAQAA FQKVVAGVAT ALAHKYH
