MYG_HUMAN
ID MYG_HUMAN Reviewed; 154 AA.
AC P02144; Q52H51; Q5THY7;
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=Myoglobin;
GN Name=MB;
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=6571704; DOI=10.1002/j.1460-2075.1984.tb01825.x;
RA Weller P., Jeffreys A.J., Wilson V., Blanchetot A.;
RT "Organization of the human myoglobin gene.";
RL EMBO J. 3:439-446(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2989088; DOI=10.1016/0378-1119(85)90231-8;
RA Akaboshi E.;
RT "Cloning of the human myoglobin gene.";
RL Gene 33:241-249(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
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 [8]
RP PROTEIN SEQUENCE OF 2-154.
RX PubMed=5285572; DOI=10.1038/newbio232149a0;
RA Romero-Herrera A.E., Lehmann H.;
RT "Primary structure of human myoglobin.";
RL Nature New Biol. 232:149-152(1971).
RN [9]
RP SEQUENCE REVISION TO 20-23 AND 84.
RX PubMed=11452891; DOI=10.1016/0005-2795(71)90140-1;
RA Romero-Herrera A.E., Lehmann H.;
RT "The myoglobin of primates. I. Hylobates agilis (gibbon).";
RL Biochim. Biophys. Acta 251:482-488(1971).
RN [10]
RP SEQUENCE REVISION TO 100-102.
RX PubMed=4627044; DOI=10.1016/0005-2795(72)90107-9;
RA Romero-Herrera A.E., Lehmann H.;
RT "The myoglobin of primates. II. Pan troglodytes (chimpanzee).";
RL Biochim. Biophys. Acta 278:62-67(1972).
RN [11]
RP PROTEIN SEQUENCE OF 2-21.
RC TISSUE=Heart;
RX PubMed=7895732; DOI=10.1002/elps.11501501209;
RA Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.;
RT "The human myocardial two-dimensional gel protein database: update 1994.";
RL Electrophoresis 15:1459-1465(1994).
RN [12]
RP VARIANT LYS-55.
RX PubMed=5805522; DOI=10.1038/223832a0;
RA Boulton F.E., Huntsman R.G., Lorkin P.A., Lehmann H.;
RT "Abnormal human myoglobin: 53 (D4) glutamic acid-->lysine.";
RL Nature 223:832-833(1969).
RN [13]
RP VARIANT TRP-140.
RX PubMed=5555219; DOI=10.1016/0005-2795(71)90288-1;
RA Boulton F.E., Huntsman R.G., Romero Herrera A., Lorkin P.A., Lehmann H.;
RT "The third variant of human myoglobin showing an unusual amino acid
RT substitution: 138(H16)arginine-->tryptophan.";
RL Biochim. Biophys. Acta 229:716-719(1971).
RN [14]
RP VARIANT ASN-134.
RX PubMed=5555226; DOI=10.1016/0005-2795(71)90309-6;
RA Boulton F.E., Huntsman R.G., Romero Herrera A.E., Lorkin P.A., Lehmann H.;
RT "A human myoglobin variant 133 (H-10)lysine-->asparagine.";
RL Biochim. Biophys. Acta 229:871-876(1971).
RN [15]
RP VARIANT GLN-140.
RX PubMed=5540041; DOI=10.1111/j.1365-2141.1971.tb00787.x;
RA Boulton F.E., Huntsman R.G., Yawson G.I., Romero-Herrera A.E., Lorkin P.A.;
RT "The second variant of human myoglobin; 138(H16) arginine leads to
RT glutamine.";
RL Br. J. Haematol. 20:69-74(1971).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ARG-46 AND ALA-111 IN
RP COMPLEX WITH HEME.
RX PubMed=2342104; DOI=10.1016/s0022-2836(05)80181-0;
RA Hubbard S.R., Hendrickson W.A., Lambright D.G., Boxer S.G.;
RT "X-ray crystal structure of a recombinant human myoglobin mutant at 2.8-A
RT resolution.";
RL J. Mol. Biol. 213:215-218(1990).
CC -!- FUNCTION: Serves as a reserve supply of oxygen and facilitates the
CC movement of oxygen within muscles.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mb/";
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DR EMBL; X00371; CAA25109.1; -; Genomic_DNA.
DR EMBL; X00372; CAA25109.1; JOINED; Genomic_DNA.
DR EMBL; X00373; CAA25109.1; JOINED; Genomic_DNA.
DR EMBL; M14603; AAA59595.1; -; Genomic_DNA.
DR EMBL; M10090; AAA59595.1; JOINED; Genomic_DNA.
DR EMBL; M14602; AAA59595.1; JOINED; Genomic_DNA.
DR EMBL; CR456516; CAG30402.1; -; mRNA.
DR EMBL; CR541949; CAG46747.1; -; mRNA.
DR EMBL; DQ003030; AAX84516.1; -; Genomic_DNA.
DR EMBL; AL022334; CAI21837.1; -; Genomic_DNA.
DR EMBL; AL049747; CAI21837.1; JOINED; Genomic_DNA.
DR EMBL; BC014547; AAH14547.1; -; mRNA.
DR CCDS; CCDS13917.1; -.
DR PIR; I53991; MYHU.
DR RefSeq; NP_005359.1; NM_005368.2.
DR RefSeq; NP_976311.1; NM_203377.1.
DR RefSeq; NP_976312.1; NM_203378.1.
DR RefSeq; XP_005261662.1; XM_005261605.2.
DR PDB; 3RGK; X-ray; 1.65 A; A=2-154.
DR PDBsum; 3RGK; -.
DR AlphaFoldDB; P02144; -.
DR SMR; P02144; -.
DR BioGRID; 110321; 10.
DR IntAct; P02144; 4.
DR STRING; 9606.ENSP00000380489; -.
DR BindingDB; P02144; -.
DR ChEMBL; CHEMBL2406892; -.
DR DrugBank; DB02671; 1-Methylimidazole.
DR DrugBank; DB03385; 4-Methylimidazole.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB02073; Biliverdine IX Alpha.
DR DrugBank; DB11588; Carbon monoxide.
DR DrugBank; DB03399; Ethyl Isocyanide.
DR DrugBank; DB03366; Imidazole.
DR DrugBank; DB04337; Isocyanomethane.
DR DrugBank; DB02396; Methylethylamine.
DR DrugBank; DB01826; N-Butyl Isocyanide.
DR DrugBank; DB04050; N-Propyl Isocyanide.
DR DrugBank; DB02646; Nitrosoethane.
DR DrugBank; DB09112; Nitrous acid.
DR DrugBank; DB01710; Porphyrin Fe(III).
DR DrugBank; DB02528; Tetrazolyl Histidine.
DR DrugCentral; P02144; -.
DR TCDB; 1.A.107.1.3; the pore-forming globin (globin) family.
DR CarbonylDB; P02144; -.
DR iPTMnet; P02144; -.
DR PhosphoSitePlus; P02144; -.
DR BioMuta; MB; -.
DR DMDM; 127661; -.
DR UCD-2DPAGE; P02144; -.
DR jPOST; P02144; -.
DR MassIVE; P02144; -.
DR MaxQB; P02144; -.
DR PaxDb; P02144; -.
DR PeptideAtlas; P02144; -.
DR PRIDE; P02144; -.
DR ProteomicsDB; 51517; -.
DR ABCD; P02144; 1 sequenced antibody.
DR Antibodypedia; 292; 1357 antibodies from 46 providers.
DR DNASU; 4151; -.
DR Ensembl; ENST00000359787.5; ENSP00000352835.1; ENSG00000198125.13.
DR Ensembl; ENST00000397326.7; ENSP00000380489.2; ENSG00000198125.13.
DR Ensembl; ENST00000397328.5; ENSP00000380491.1; ENSG00000198125.13.
DR Ensembl; ENST00000406324.5; ENSP00000384239.1; ENSG00000198125.13.
DR GeneID; 4151; -.
DR KEGG; hsa:4151; -.
DR MANE-Select; ENST00000397326.7; ENSP00000380489.2; NM_005368.3; NP_005359.1.
DR UCSC; uc003anz.4; human.
DR CTD; 4151; -.
DR DisGeNET; 4151; -.
DR GeneCards; MB; -.
DR HGNC; HGNC:6915; MB.
DR HPA; ENSG00000198125; Group enriched (heart muscle, skeletal muscle, tongue).
DR MIM; 160000; gene.
DR neXtProt; NX_P02144; -.
DR OpenTargets; ENSG00000198125; -.
DR PharmGKB; PA30658; -.
DR VEuPathDB; HostDB:ENSG00000198125; -.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000160809; -.
DR InParanoid; P02144; -.
DR OMA; MRLFQDH; -.
DR OrthoDB; 1405713at2759; -.
DR PhylomeDB; P02144; -.
DR TreeFam; TF332967; -.
DR PathwayCommons; P02144; -.
DR Reactome; R-HSA-8981607; Intracellular oxygen transport.
DR SignaLink; P02144; -.
DR BioGRID-ORCS; 4151; 10 hits in 1071 CRISPR screens.
DR ChiTaRS; MB; human.
DR GeneWiki; Myoglobin; -.
DR GenomeRNAi; 4151; -.
DR Pharos; P02144; Tbio.
DR PRO; PR:P02144; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P02144; protein.
DR Bgee; ENSG00000198125; Expressed in heart right ventricle and 139 other tissues.
DR ExpressionAtlas; P02144; baseline and differential.
DR Genevisible; P02144; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019825; F:oxygen binding; IBA:GO_Central.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0043353; P:enucleate erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0015671; P:oxygen transport; IBA:GO_Central.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR002335; Myoglobin.
DR PANTHER; PTHR47132; PTHR47132; 1.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00613; MYOGLOBIN.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Muscle protein; Oxygen transport; Phosphoprotein; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:5285572,
FT ECO:0000269|PubMed:7895732"
FT CHAIN 2..154
FT /note="Myoglobin"
FT /id="PRO_0000053303"
FT BINDING 65
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:0000269|PubMed:2342104"
FT BINDING 94
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:2342104,
FT ECO:0007744|PDB:3RGK"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ76"
FT MOD_RES 68
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04247"
FT VARIANT 55
FT /note="E -> K (in dbSNP:rs145465287)"
FT /evidence="ECO:0000269|PubMed:5805522"
FT /id="VAR_003180"
FT VARIANT 134
FT /note="K -> N (in dbSNP:rs766095327)"
FT /evidence="ECO:0000269|PubMed:5555226"
FT /id="VAR_003181"
FT VARIANT 140
FT /note="R -> Q (in dbSNP:rs142225854)"
FT /evidence="ECO:0000269|PubMed:5540041"
FT /id="VAR_003182"
FT VARIANT 140
FT /note="R -> W (in dbSNP:rs767663245)"
FT /evidence="ECO:0000269|PubMed:5555219"
FT /id="VAR_003183"
FT CONFLICT 106
FT /note="E -> Q (in Ref. 5; AAX84516)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="Q -> E (in Ref. 2; AAA59595)"
FT /evidence="ECO:0000305"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:3RGK"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3RGK"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:3RGK"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:3RGK"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:3RGK"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:3RGK"
FT HELIX 60..77
FT /evidence="ECO:0007829|PDB:3RGK"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:3RGK"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:3RGK"
FT HELIX 102..119
FT /evidence="ECO:0007829|PDB:3RGK"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:3RGK"
FT HELIX 126..149
FT /evidence="ECO:0007829|PDB:3RGK"
SQ SEQUENCE 154 AA; 17184 MW; F6A41F19A525F09C CRC64;
MGLSDGEWQL VLNVWGKVEA DIPGHGQEVL IRLFKGHPET LEKFDKFKHL KSEDEMKASE
DLKKHGATVL TALGGILKKK GHHEAEIKPL AQSHATKHKI PVKYLEFISE CIIQVLQSKH
PGDFGADAQG AMNKALELFR KDMASNYKEL GFQG
