HBB_PANTR
ID HBB_PANTR Reviewed; 147 AA.
AC P68873; P02023; Q13852; Q14481; Q14510; Q28799; Q9BX96; Q9UCP8; Q9UCP9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-121.
RX PubMed=3999143; DOI=10.1016/0022-2836(85)90024-5;
RA Savatier P., Trabuchet G., Faure C., Chebloune Y., Gouy M., Verdier G.,
RA Nigon V.M.;
RT "Evolution of the primate beta-globin gene region. High rate of variation
RT in CpG dinucleotides and in short repeated sequences between man and
RT chimpanzee.";
RL J. Mol. Biol. 182:21-29(1985).
RN [2]
RP PROTEIN SEQUENCE OF 2-147.
RX PubMed=5855051; DOI=10.1016/0304-4165(65)90350-8;
RA Rifkin D.B., Konigsberg W.;
RT "The characterization of the tryptic peptides from the hemoglobin of the
RT chimpanzee (Pan troglodytes).";
RL Biochim. Biophys. Acta 104:457-461(1965).
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 in
CC adult hemoglobin A (HbA).
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA26204.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X02345; CAA26204.1; ALT_SEQ; Genomic_DNA.
DR PIR; B93303; HBCZ.
DR RefSeq; XP_508242.1; XM_508242.4.
DR AlphaFoldDB; P68873; -.
DR SMR; P68873; -.
DR STRING; 9598.ENSPTRP00000005700; -.
DR PaxDb; P68873; -.
DR PRIDE; P68873; -.
DR Ensembl; ENSPTRT00000006177; ENSPTRP00000005700; ENSPTRG00000040047.
DR GeneID; 450978; -.
DR KEGG; ptr:450978; -.
DR CTD; 3043; -.
DR VGNC; VGNC:3255; HBB.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000163476; -.
DR HOGENOM; CLU_003827_10_0_1; -.
DR InParanoid; P68873; -.
DR OMA; TPDAVMN; -.
DR OrthoDB; 1370439at2759; -.
DR TreeFam; TF333268; -.
DR Proteomes; UP000002277; Chromosome 11.
DR Bgee; ENSPTRG00000040047; Expressed in bone marrow and 20 other tissues.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IBA:GO_Central.
DR GO; GO:0005833; C:hemoglobin complex; IBA:GO_Central.
DR GO; GO:0031720; F:haptoglobin binding; IEA:Ensembl.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0031721; F:hemoglobin alpha binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central.
DR GO; GO:0004601; F:peroxidase activity; IEA:Ensembl.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0030185; P:nitric oxide transport; IEA:Ensembl.
DR GO; GO:0010942; P:positive regulation of cell death; IEA:Ensembl.
DR GO; GO:0070293; P:renal absorption; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
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 Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Phosphoprotein; Reference proteome; S-nitrosylation;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02086,
FT ECO:0000269|PubMed:5855051"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000053060"
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 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 94
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 145
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
SQ SEQUENCE 147 AA; 15998 MW; A31F6D621C6556A1 CRC64;
MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK
VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG
KEFTPPVQAA YQKVVAGVAN ALAHKYH
