Full text data of MB
MB
[Confidence: low (only semi-automatic identification from reviews)]
Myoglobin
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Myoglobin
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P02144
ID MYG_HUMAN Reviewed; 154 AA.
AC P02144; Q52H51; Q5THY7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=Myoglobin;
GN Name=MB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6571704;
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.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA 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.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA 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.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-154.
RX PubMed=5285572;
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;
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;
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
RT 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;
RA Boulton F.E., Huntsman R.G., Romero Herrera A., Lorkin P.A.,
RA 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;
RA Boulton F.E., Huntsman R.G., Romero Herrera A.E., Lorkin P.A.,
RA 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.,
RA 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
RT 2.8-A 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.
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 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_005261605.1.
DR UniGene; Hs.517586; -.
DR PDB; 3RGK; X-ray; 1.65 A; A=2-154.
DR PDBsum; 3RGK; -.
DR ProteinModelPortal; P02144; -.
DR SMR; P02144; 2-150.
DR STRING; 9606.ENSP00000352835; -.
DR PhosphoSite; P02144; -.
DR DMDM; 127661; -.
DR UCD-2DPAGE; P02144; -.
DR PaxDb; P02144; -.
DR PeptideAtlas; P02144; -.
DR PRIDE; P02144; -.
DR DNASU; 4151; -.
DR Ensembl; ENST00000359787; ENSP00000352835; ENSG00000198125.
DR Ensembl; ENST00000397326; ENSP00000380489; ENSG00000198125.
DR Ensembl; ENST00000397328; ENSP00000380491; ENSG00000198125.
DR Ensembl; ENST00000406324; ENSP00000384239; ENSG00000198125.
DR GeneID; 4151; -.
DR KEGG; hsa:4151; -.
DR UCSC; uc003anz.3; human.
DR CTD; 4151; -.
DR GeneCards; GC22M036002; -.
DR HGNC; HGNC:6915; MB.
DR HPA; CAB000060; -.
DR HPA; HPA003123; -.
DR MIM; 160000; gene.
DR neXtProt; NX_P02144; -.
DR PharmGKB; PA30658; -.
DR eggNOG; NOG276460; -.
DR HOGENOM; HOG000070111; -.
DR HOVERGEN; HBG107340; -.
DR InParanoid; P02144; -.
DR OMA; TKHKIPI; -.
DR PhylomeDB; P02144; -.
DR ChiTaRS; MB; human.
DR GeneWiki; Myoglobin; -.
DR GenomeRNAi; 4151; -.
DR NextBio; 16322; -.
DR PRO; PR:P02144; -.
DR ArrayExpress; P02144; -.
DR Bgee; P02144; -.
DR CleanEx; HS_MB; -.
DR Genevestigator; P02144; -.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019825; F:oxygen binding; IEA:Ensembl.
DR GO; GO:0005344; F:oxygen transporter 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:0009725; P:response to hormone stimulus; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0031444; P:slow-twitch skeletal muscle fiber contraction; IEA:Ensembl.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like.
DR InterPro; IPR012292; Globin_dom.
DR InterPro; IPR002335; Myoglobin.
DR PANTHER; PTHR11442:SF5; PTHR11442:SF5; 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; Complete proteome; Direct protein sequencing; Heme;
KW Iron; Metal-binding; Muscle protein; Oxygen transport; Polymorphism;
KW Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 154 Myoglobin.
FT /FTId=PRO_0000053303.
FT METAL 65 65 Iron (heme distal ligand).
FT METAL 94 94 Iron (heme proximal ligand).
FT VARIANT 55 55 E -> K.
FT /FTId=VAR_003180.
FT VARIANT 134 134 K -> N.
FT /FTId=VAR_003181.
FT VARIANT 140 140 R -> Q (in dbSNP:rs142225854).
FT /FTId=VAR_003182.
FT VARIANT 140 140 R -> W.
FT /FTId=VAR_003183.
FT CONFLICT 106 106 E -> Q (in Ref. 5; AAX84516).
FT CONFLICT 129 129 Q -> E (in Ref. 2; AAA59595).
FT HELIX 5 18
FT HELIX 19 21
FT HELIX 22 36
FT HELIX 38 43
FT HELIX 45 47
FT HELIX 53 57
FT HELIX 60 77
FT TURN 78 81
FT HELIX 84 96
FT HELIX 102 119
FT TURN 121 123
FT HELIX 126 149
SQ SEQUENCE 154 AA; 17184 MW; F6A41F19A525F09C CRC64;
MGLSDGEWQL VLNVWGKVEA DIPGHGQEVL IRLFKGHPET LEKFDKFKHL KSEDEMKASE
DLKKHGATVL TALGGILKKK GHHEAEIKPL AQSHATKHKI PVKYLEFISE CIIQVLQSKH
PGDFGADAQG AMNKALELFR KDMASNYKEL GFQG
//
ID MYG_HUMAN Reviewed; 154 AA.
AC P02144; Q52H51; Q5THY7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=Myoglobin;
GN Name=MB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6571704;
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.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA 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.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA 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.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-154.
RX PubMed=5285572;
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;
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;
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
RT 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;
RA Boulton F.E., Huntsman R.G., Romero Herrera A., Lorkin P.A.,
RA 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;
RA Boulton F.E., Huntsman R.G., Romero Herrera A.E., Lorkin P.A.,
RA 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.,
RA 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
RT 2.8-A 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.
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 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_005261605.1.
DR UniGene; Hs.517586; -.
DR PDB; 3RGK; X-ray; 1.65 A; A=2-154.
DR PDBsum; 3RGK; -.
DR ProteinModelPortal; P02144; -.
DR SMR; P02144; 2-150.
DR STRING; 9606.ENSP00000352835; -.
DR PhosphoSite; P02144; -.
DR DMDM; 127661; -.
DR UCD-2DPAGE; P02144; -.
DR PaxDb; P02144; -.
DR PeptideAtlas; P02144; -.
DR PRIDE; P02144; -.
DR DNASU; 4151; -.
DR Ensembl; ENST00000359787; ENSP00000352835; ENSG00000198125.
DR Ensembl; ENST00000397326; ENSP00000380489; ENSG00000198125.
DR Ensembl; ENST00000397328; ENSP00000380491; ENSG00000198125.
DR Ensembl; ENST00000406324; ENSP00000384239; ENSG00000198125.
DR GeneID; 4151; -.
DR KEGG; hsa:4151; -.
DR UCSC; uc003anz.3; human.
DR CTD; 4151; -.
DR GeneCards; GC22M036002; -.
DR HGNC; HGNC:6915; MB.
DR HPA; CAB000060; -.
DR HPA; HPA003123; -.
DR MIM; 160000; gene.
DR neXtProt; NX_P02144; -.
DR PharmGKB; PA30658; -.
DR eggNOG; NOG276460; -.
DR HOGENOM; HOG000070111; -.
DR HOVERGEN; HBG107340; -.
DR InParanoid; P02144; -.
DR OMA; TKHKIPI; -.
DR PhylomeDB; P02144; -.
DR ChiTaRS; MB; human.
DR GeneWiki; Myoglobin; -.
DR GenomeRNAi; 4151; -.
DR NextBio; 16322; -.
DR PRO; PR:P02144; -.
DR ArrayExpress; P02144; -.
DR Bgee; P02144; -.
DR CleanEx; HS_MB; -.
DR Genevestigator; P02144; -.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019825; F:oxygen binding; IEA:Ensembl.
DR GO; GO:0005344; F:oxygen transporter 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:0009725; P:response to hormone stimulus; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0031444; P:slow-twitch skeletal muscle fiber contraction; IEA:Ensembl.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like.
DR InterPro; IPR012292; Globin_dom.
DR InterPro; IPR002335; Myoglobin.
DR PANTHER; PTHR11442:SF5; PTHR11442:SF5; 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; Complete proteome; Direct protein sequencing; Heme;
KW Iron; Metal-binding; Muscle protein; Oxygen transport; Polymorphism;
KW Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 154 Myoglobin.
FT /FTId=PRO_0000053303.
FT METAL 65 65 Iron (heme distal ligand).
FT METAL 94 94 Iron (heme proximal ligand).
FT VARIANT 55 55 E -> K.
FT /FTId=VAR_003180.
FT VARIANT 134 134 K -> N.
FT /FTId=VAR_003181.
FT VARIANT 140 140 R -> Q (in dbSNP:rs142225854).
FT /FTId=VAR_003182.
FT VARIANT 140 140 R -> W.
FT /FTId=VAR_003183.
FT CONFLICT 106 106 E -> Q (in Ref. 5; AAX84516).
FT CONFLICT 129 129 Q -> E (in Ref. 2; AAA59595).
FT HELIX 5 18
FT HELIX 19 21
FT HELIX 22 36
FT HELIX 38 43
FT HELIX 45 47
FT HELIX 53 57
FT HELIX 60 77
FT TURN 78 81
FT HELIX 84 96
FT HELIX 102 119
FT TURN 121 123
FT HELIX 126 149
SQ SEQUENCE 154 AA; 17184 MW; F6A41F19A525F09C CRC64;
MGLSDGEWQL VLNVWGKVEA DIPGHGQEVL IRLFKGHPET LEKFDKFKHL KSEDEMKASE
DLKKHGATVL TALGGILKKK GHHEAEIKPL AQSHATKHKI PVKYLEFISE CIIQVLQSKH
PGDFGADAQG AMNKALELFR KDMASNYKEL GFQG
//
MIM
160000
*RECORD*
*FIELD* NO
160000
*FIELD* TI
*160000 MYOGLOBIN; MB
*FIELD* TX
CLONING
Weller et al. (1984) and Akaboshi (1985) independently cloned human MB,
read morewhich encodes a protein of 152 residues.
GENE STRUCTURE
Weller et al. (1984) determined that the MB gene contains 3 exons
spanning 10.4 kb.
MAPPING
Jeffreys et al. (1984) used DNA probes isolated from the cloned
myoglobin gene to map the gene in human-rodent somatic cell hybrids. The
myoglobin locus mapped to chromosome 22q11-q13. Julier et al. (1985)
confirmed assignment to chromosome 22. Julier et al. (1985) concluded
from multilocus linkage tests that the oncogene SIS locus is most likely
distal to MB and that both are distal to IGL. The following tentative
map was derived: cen--IGL--0.10--D22S1--0.20--MB--0.07--(SIS, P1).
MOLECULAR GENETICS
Two structural variants of myoglobin were described by Boyer et al.
(1963). Boulton et al. (1969) studied postmortem muscle from 2,500
persons. Two myoglobin variants were found, and in one of these
substitution of lysine for glutamic acid at residue 53 was demonstrated.
Later Boulton et al. (1970) described a variant myoglobin with
substitution of glutamine for arginine at residue 139. A third
substitution is tryptophan for arginine at residue 139 and a fourth is
asparagine for lysine at residue 133 (Romero-Herrera and Lehmann, 1971,
1974).
HISTORY
For a DNA sequence that contains tandem repeats but represents only a
single locus, White (see Nakamura et al., 1987) introduced the
designation variable number of tandem repeats (VNTR) locus. The first
polymorphic locus discovered with an arbitrary DNA probe represented
such a locus (Wyman and White, 1980; see 107750) with fragments of more
than 15 different lengths observed in a small sample of unrelated
persons. Subsequently, similar systems were observed in several other
loci, such as the insulin gene (176730), the Harvey-ras gene (190020),
the zeta-globin pseudogene (see 142310), the myoglobin gene, and the
X-gene region of hepatitis B virus. This region of the HBV genome is
thought to be the viral site of integration into the human genome and
thus could be considered recombinogenic in a manner similar to the long
terminal repeat regions of retroviruses. The repeats in these
hypervariable loci have 11 to 60 basepairs. The length of each
restriction fragment is a function of the number of copies of the tandem
repeat sequence within the fragment. These hypervariable loci are highly
informative markers for linkage studies. Jeffreys et al. (1985) found
that a DNA probe based on a set of tandem repeats associated with the
myoglobin locus can detect by hybridization to human genomic DNA a
number of loci containing tandem repeats of similar sequence. The
restriction fragment pattern revealed by the sum of the VNTR loci
containing such related sequences, scattered through the genome,
constitutes a 'fingerprint' unique to the individual.
ANIMAL MODEL
Garry et al. (1998) created mice without myoglobin by targeted
disruption of the myoglobin gene. The mice were fertile and exhibited
normal exercise capacity and a normal ventilatory response to hypoxia.
Although heart and soleus muscles were depigmented, they functioned
normally in standard in vitro assays of muscle performance across a
range of work conditions and oxygen availability. These data
demonstrated that myoglobin is not essential to meet the metabolic
requirements of pregnancy or exercise in a terrestrial mammal, and raise
new questions about oxygen transport and metabolic regulation in working
muscles. Whether simple diffusion is enough or other mechanisms exist to
facilitate high rates of oxygen transport to working myocytes remained
to be elucidated.
Godecke et al. (1999) used homologous recombination to delete exon 2 of
the mouse Mb gene. They found that Mb -/- mice appeared phenotypically
normal but had significantly elevated levels of hemoglobin and an
increase in coronary flow and coronary reserve. Histologic analysis
demonstrated increased capillary density in the hearts of Mb-deficient
mice. Godecke et al. (1999) concluded that disruption of myoglobin
results in the activation of multiple compensatory mechanisms that
steepen the pO2 gradient to mitochondria, suggesting that myoglobin is
important for the delivery of oxygen to mitochondria.
*FIELD* SA
Boulton et al. (1971); Boyer (1977); Dozier et al. (1986); Julier
et al. (1985); Julier et al. (1985)
*FIELD* RF
1. Akaboshi, E.: Cloning of the human myoglobin gene. Gene 33:
241-249, 1985.
2. Boulton, F. E.; Huntsman, R. G.; Lehmann, H.; Lorkin, P. A.; Romero-Herrera,
A. E.: Myoglobin variants. (Abstract) Biochem. J. 118: 39P only,
1970.
3. Boulton, F. E.; Huntsman, R. G.; Lorkin, P. A.; Lehmann, H.: Abnormal
human myoglobin: 53(D4) glutamic acid lysine. Nature 223: 832-833,
1969.
4. Boulton, F. E.; Huntsman, R. G.; Yawson, G. I.; Romero-Herrera,
A. E.; Lorkin, P. A.: The second variant of human myoglobin: 138(H16)
arginine to glutamine. Brit. J. Haemat. 20A: 69-74, 1971.
5. Boyer, S. H.: Similar incidence and non-randomness among human
myoglobin and hemoglobin mutants in general populations: implications
for the study of myoglobin in muscle disease.In: Pathogenesis of Human
Muscular Dystrophies. Proc. Vth Int. Cong. of Muscular Dystrophy Assoc.,
Durango, Colo., June 21-25, 1976. Amsterdam: Excerpta Medica (pub.)
1977.
6. Boyer, S. H.; Fainer, D. C.; Naughton, M. A.: Myoglobin inherited
structural variation in man. Science 140: 1228-1231, 1963.
7. Dozier, C.; Walbaum, S.; Leprince, D.; Stehelin, D.: EcoRI RFLP
linked to the human myb gene. Nucleic Acids Res. 14: 1928 only,
1986.
8. Garry, D. J.; Ordway, G. A.; Lorenz, J. N.; Radford, N. B.; Chin,
E. R.; Grange, R. W.; Bassel-Duby, R.; Williams, R. S.: Mice without
myoglobin. Nature 395: 905-908, 1998.
9. Godecke, A.; Flogel, U.; Zanger, K.; Ding, Z.; Hirchenhain, J.;
Decking, U. K. M.; Schrader, J.: Disruption of myoglobin in mice
induces multiple compensatory mechanisms. Proc. Nat. Acad. Sci. 96:
10495-10500, 1999.
10. Jeffreys, A.; Wilson, V.; Thein, S.: Hypervariable 'minisatellite'
regions in human DNA. Science 314: 67-73, 1985.
11. Jeffreys, A. J.; Wilson, V.; Blanchetot, A.; Weller, P.; Geurts
van Kessel, A.; Spurr, N.; Solomon, E.; Goodfellow, P.: The human
myoglobin gene: a third dispersed globin locus in the human genome. Nucleic
Acids Res. 12: 3235-3243, 1984.
12. Julier, C.; Lathrop, M.; Lalouel, J. M.; Kaplan, J. C.: Use of
multilocus tests of gene order: example for chromosome 22. (Abstract) Cytogenet.
Cell Genet. 40: 663-664, 1985.
13. Julier, C.; Lathrop, M.; Lalouel, J. M.; Reghis, A.; Szajnert,
M. F.; Kaplan, J. C.: New restriction fragment length polymorphisms
on human chromosome 22 at loci SIS, MB and IGLV. (Abstract) Cytogenet.
Cell Genet. 40: 664 only, 1985.
14. Julier, C.; Reghis, A.; Szajnert, M. F.; Kaplan, J. C.; Lathrop,
G. M.; Lalouel, J. M.: A preliminary linkage map of human chromosome
22. (Abstract) Cytogenet. Cell Genet. 40: 665 only, 1985.
15. Nakamura, Y.; Leppert, M.; O'Connell, P.; Wolff, R.; Holm, T.;
Culver, M.; Martin, C.; Fujimoto, E.; Hoff, M.; Kumlin, E.; White,
R.: Variable number of tandem repeat (VNTR) markers for human gene
mapping. Science 235: 1616-1622, 1987.
16. Romero-Herrera, A. E.; Lehmann, H.: The amino acid sequence of
human myoglobin and its minor fractions. Proc. Roy. Soc. London 186B:
249-279, 1974.
17. Romero-Herrera, A. E.; Lehmann, H.: Primary structure of human
myoglobin. Nature N.B. 232: 149-152, 1971.
18. Weller, P.; Jeffreys, A. J.; Wilson, V.; Blanchetot, A.: Organization
of the human myoglobin gene. EMBO J. 3: 439-446, 1984.
19. Wyman, A. R.; White, R.: A highly polymorphic locus in human
DNA. Proc. Nat. Acad. Sci. 77: 6754-6758, 1980.
*FIELD* CN
Paul J. Converse - updated: 8/17/2001
Ada Hamosh - updated: 10/28/1998
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 05/20/2010
terry: 12/16/2009
wwang: 10/1/2008
cwells: 11/10/2003
carol: 1/2/2002
mgross: 8/17/2001
terry: 2/13/2001
alopez: 10/28/1998
terry: 6/18/1998
mark: 2/21/1997
mimadm: 12/2/1994
davew: 7/27/1994
carol: 4/29/1994
warfield: 3/30/1994
supermim: 3/16/1992
carol: 8/24/1990
*RECORD*
*FIELD* NO
160000
*FIELD* TI
*160000 MYOGLOBIN; MB
*FIELD* TX
CLONING
Weller et al. (1984) and Akaboshi (1985) independently cloned human MB,
read morewhich encodes a protein of 152 residues.
GENE STRUCTURE
Weller et al. (1984) determined that the MB gene contains 3 exons
spanning 10.4 kb.
MAPPING
Jeffreys et al. (1984) used DNA probes isolated from the cloned
myoglobin gene to map the gene in human-rodent somatic cell hybrids. The
myoglobin locus mapped to chromosome 22q11-q13. Julier et al. (1985)
confirmed assignment to chromosome 22. Julier et al. (1985) concluded
from multilocus linkage tests that the oncogene SIS locus is most likely
distal to MB and that both are distal to IGL. The following tentative
map was derived: cen--IGL--0.10--D22S1--0.20--MB--0.07--(SIS, P1).
MOLECULAR GENETICS
Two structural variants of myoglobin were described by Boyer et al.
(1963). Boulton et al. (1969) studied postmortem muscle from 2,500
persons. Two myoglobin variants were found, and in one of these
substitution of lysine for glutamic acid at residue 53 was demonstrated.
Later Boulton et al. (1970) described a variant myoglobin with
substitution of glutamine for arginine at residue 139. A third
substitution is tryptophan for arginine at residue 139 and a fourth is
asparagine for lysine at residue 133 (Romero-Herrera and Lehmann, 1971,
1974).
HISTORY
For a DNA sequence that contains tandem repeats but represents only a
single locus, White (see Nakamura et al., 1987) introduced the
designation variable number of tandem repeats (VNTR) locus. The first
polymorphic locus discovered with an arbitrary DNA probe represented
such a locus (Wyman and White, 1980; see 107750) with fragments of more
than 15 different lengths observed in a small sample of unrelated
persons. Subsequently, similar systems were observed in several other
loci, such as the insulin gene (176730), the Harvey-ras gene (190020),
the zeta-globin pseudogene (see 142310), the myoglobin gene, and the
X-gene region of hepatitis B virus. This region of the HBV genome is
thought to be the viral site of integration into the human genome and
thus could be considered recombinogenic in a manner similar to the long
terminal repeat regions of retroviruses. The repeats in these
hypervariable loci have 11 to 60 basepairs. The length of each
restriction fragment is a function of the number of copies of the tandem
repeat sequence within the fragment. These hypervariable loci are highly
informative markers for linkage studies. Jeffreys et al. (1985) found
that a DNA probe based on a set of tandem repeats associated with the
myoglobin locus can detect by hybridization to human genomic DNA a
number of loci containing tandem repeats of similar sequence. The
restriction fragment pattern revealed by the sum of the VNTR loci
containing such related sequences, scattered through the genome,
constitutes a 'fingerprint' unique to the individual.
ANIMAL MODEL
Garry et al. (1998) created mice without myoglobin by targeted
disruption of the myoglobin gene. The mice were fertile and exhibited
normal exercise capacity and a normal ventilatory response to hypoxia.
Although heart and soleus muscles were depigmented, they functioned
normally in standard in vitro assays of muscle performance across a
range of work conditions and oxygen availability. These data
demonstrated that myoglobin is not essential to meet the metabolic
requirements of pregnancy or exercise in a terrestrial mammal, and raise
new questions about oxygen transport and metabolic regulation in working
muscles. Whether simple diffusion is enough or other mechanisms exist to
facilitate high rates of oxygen transport to working myocytes remained
to be elucidated.
Godecke et al. (1999) used homologous recombination to delete exon 2 of
the mouse Mb gene. They found that Mb -/- mice appeared phenotypically
normal but had significantly elevated levels of hemoglobin and an
increase in coronary flow and coronary reserve. Histologic analysis
demonstrated increased capillary density in the hearts of Mb-deficient
mice. Godecke et al. (1999) concluded that disruption of myoglobin
results in the activation of multiple compensatory mechanisms that
steepen the pO2 gradient to mitochondria, suggesting that myoglobin is
important for the delivery of oxygen to mitochondria.
*FIELD* SA
Boulton et al. (1971); Boyer (1977); Dozier et al. (1986); Julier
et al. (1985); Julier et al. (1985)
*FIELD* RF
1. Akaboshi, E.: Cloning of the human myoglobin gene. Gene 33:
241-249, 1985.
2. Boulton, F. E.; Huntsman, R. G.; Lehmann, H.; Lorkin, P. A.; Romero-Herrera,
A. E.: Myoglobin variants. (Abstract) Biochem. J. 118: 39P only,
1970.
3. Boulton, F. E.; Huntsman, R. G.; Lorkin, P. A.; Lehmann, H.: Abnormal
human myoglobin: 53(D4) glutamic acid lysine. Nature 223: 832-833,
1969.
4. Boulton, F. E.; Huntsman, R. G.; Yawson, G. I.; Romero-Herrera,
A. E.; Lorkin, P. A.: The second variant of human myoglobin: 138(H16)
arginine to glutamine. Brit. J. Haemat. 20A: 69-74, 1971.
5. Boyer, S. H.: Similar incidence and non-randomness among human
myoglobin and hemoglobin mutants in general populations: implications
for the study of myoglobin in muscle disease.In: Pathogenesis of Human
Muscular Dystrophies. Proc. Vth Int. Cong. of Muscular Dystrophy Assoc.,
Durango, Colo., June 21-25, 1976. Amsterdam: Excerpta Medica (pub.)
1977.
6. Boyer, S. H.; Fainer, D. C.; Naughton, M. A.: Myoglobin inherited
structural variation in man. Science 140: 1228-1231, 1963.
7. Dozier, C.; Walbaum, S.; Leprince, D.; Stehelin, D.: EcoRI RFLP
linked to the human myb gene. Nucleic Acids Res. 14: 1928 only,
1986.
8. Garry, D. J.; Ordway, G. A.; Lorenz, J. N.; Radford, N. B.; Chin,
E. R.; Grange, R. W.; Bassel-Duby, R.; Williams, R. S.: Mice without
myoglobin. Nature 395: 905-908, 1998.
9. Godecke, A.; Flogel, U.; Zanger, K.; Ding, Z.; Hirchenhain, J.;
Decking, U. K. M.; Schrader, J.: Disruption of myoglobin in mice
induces multiple compensatory mechanisms. Proc. Nat. Acad. Sci. 96:
10495-10500, 1999.
10. Jeffreys, A.; Wilson, V.; Thein, S.: Hypervariable 'minisatellite'
regions in human DNA. Science 314: 67-73, 1985.
11. Jeffreys, A. J.; Wilson, V.; Blanchetot, A.; Weller, P.; Geurts
van Kessel, A.; Spurr, N.; Solomon, E.; Goodfellow, P.: The human
myoglobin gene: a third dispersed globin locus in the human genome. Nucleic
Acids Res. 12: 3235-3243, 1984.
12. Julier, C.; Lathrop, M.; Lalouel, J. M.; Kaplan, J. C.: Use of
multilocus tests of gene order: example for chromosome 22. (Abstract) Cytogenet.
Cell Genet. 40: 663-664, 1985.
13. Julier, C.; Lathrop, M.; Lalouel, J. M.; Reghis, A.; Szajnert,
M. F.; Kaplan, J. C.: New restriction fragment length polymorphisms
on human chromosome 22 at loci SIS, MB and IGLV. (Abstract) Cytogenet.
Cell Genet. 40: 664 only, 1985.
14. Julier, C.; Reghis, A.; Szajnert, M. F.; Kaplan, J. C.; Lathrop,
G. M.; Lalouel, J. M.: A preliminary linkage map of human chromosome
22. (Abstract) Cytogenet. Cell Genet. 40: 665 only, 1985.
15. Nakamura, Y.; Leppert, M.; O'Connell, P.; Wolff, R.; Holm, T.;
Culver, M.; Martin, C.; Fujimoto, E.; Hoff, M.; Kumlin, E.; White,
R.: Variable number of tandem repeat (VNTR) markers for human gene
mapping. Science 235: 1616-1622, 1987.
16. Romero-Herrera, A. E.; Lehmann, H.: The amino acid sequence of
human myoglobin and its minor fractions. Proc. Roy. Soc. London 186B:
249-279, 1974.
17. Romero-Herrera, A. E.; Lehmann, H.: Primary structure of human
myoglobin. Nature N.B. 232: 149-152, 1971.
18. Weller, P.; Jeffreys, A. J.; Wilson, V.; Blanchetot, A.: Organization
of the human myoglobin gene. EMBO J. 3: 439-446, 1984.
19. Wyman, A. R.; White, R.: A highly polymorphic locus in human
DNA. Proc. Nat. Acad. Sci. 77: 6754-6758, 1980.
*FIELD* CN
Paul J. Converse - updated: 8/17/2001
Ada Hamosh - updated: 10/28/1998
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 05/20/2010
terry: 12/16/2009
wwang: 10/1/2008
cwells: 11/10/2003
carol: 1/2/2002
mgross: 8/17/2001
terry: 2/13/2001
alopez: 10/28/1998
terry: 6/18/1998
mark: 2/21/1997
mimadm: 12/2/1994
davew: 7/27/1994
carol: 4/29/1994
warfield: 3/30/1994
supermim: 3/16/1992
carol: 8/24/1990