ENTRY MYHU #type complete TITLE myoglobin [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 12-Jul-1996 #text_change 12-Jul-2004 ACCESSIONS I53991; A90999; A93398; A90582; A90584; A02464 REFERENCE I53991 #authors Akaboshi, E. #journal Gene (1985) 33:241-249 #title Cloning of the human myoglobin gene. #cross-references MUID:85232026; PMID:2989088 #accession I53991 ##status preliminary; translated from GB/EMBL/DDBJ ##molecule_type DNA ##residues 1-128,'E',130-154 ##label RES ##cross-references UNIPROT:P02144; UNIPARC:UPI000016AD31; GB:M14603; NID:g187582; PIDN:AAA59595.1; PID:g386872 REFERENCE A90999 #authors Weller, P.; Jeffreys, A.J.; Wilson, V.; Blanchetot, A. #journal EMBO J. (1984) 3:439-446 #title Organization of the human myoglobin gene. #cross-references MUID:84182508; PMID:6571704 #accession A90999 ##molecule_type DNA ##residues 2-154 ##label WEL ##cross-references UNIPARC:UPI000012FB3D; GB:X00371; NID:g34607; PIDN:CAA25109.1; PID:g1235527 ##note initiator Met not shown REFERENCE A93398 #authors Romero-Herrera, A.E.; Lehmann, H. #journal Nature New Biol. (1971) 232:149-152 #title Primary structure of human myoglobin. #cross-references MUID:71291923; PMID:5285572 #accession A93398 ##molecule_type protein ##residues 2-19,'IDPA',24-83,'Q',85-99,'VPI',103-154 ##label ROM ##cross-references UNIPARC:UPI00001738E0 ##note this sequence has been revised in references A90582 and A90584 REFERENCE A90582 #authors Romero-Herrera, A.E.; Lehmann, H. #journal Biochim. Biophys. Acta (1971) 251:482-488 #title The myoglobin of primates. I. Hylobates agilis (gibbon). #accession A90582 ##molecule_type protein ##residues 20-23;84 ##label RO2 ##cross-references UNIPARC:UPI000011EC2D; UNIPARC:UPI00001738E1 ##note revision to human sequence REFERENCE A90584 #authors Romero-Herrera, A.E.; Lehmann, H. #journal Biochim. Biophys. Acta (1972) 278:62-67 #title The myoglobin of primates. II. Pan troglodytes (chimpanzee). #cross-references MUID:73002055; PMID:4627044 #accession A90584 ##molecule_type protein ##residues 100-102 ##label RO3 ##cross-references UNIPARC:UPI00001738E2 ##note revision to human sequence REFERENCE A30619 #authors Hubbard, S.R.; Hendrickson, W.A.; Lambright, D.G.; Boxer, S.G. #journal J. Mol. Biol. (1990) 213:215-218 #title X-ray crystal structure of a recombinant human myoglobin mutant at 2.8 angstroms resolution. #cross-references MUID:90258028; PMID:2342104 #contents annotation; X-ray crystallography, 2.8 angstroms of engineered mutant with 46-Arg and 111-Ala expressed in Escherichia coli GENETICS #gene GDB:MB ##cross-references GDB:119378; OMIM:160000 #map_position 22q12-22q12 #introns 32/2; 106/3 FUNCTION #description binds molecular oxygen for intracellular storage and transport, primarily in muscle CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; monomer; muscle; oxygen carrier FEATURE 2-154 #product myoglobin #status experimental #label MAT\ 3-148 #domain globin homology #label GLB\ 65 #binding_site oxygen (His) (distal axial ligand) #status experimental\ 94 #binding_site heme iron (His) (proximal axial ligand) #status experimental SUMMARY #length 154 #molecular-weight 17184 #checksum 7061 SEQUENCE 5 10 15 20 25 30 1 M G L S D G E W Q L V L N V W G K V E A D I P G H G Q E V L 31 I R L F K G H P E T L E K F D K F K H L K S E D E M K A S E 61 D L K K H G A T V L T A L G G I L K K K G H H E A E I K P L 91 A Q S H A T K H K I P V K Y L E F I S E C I I Q V L Q S K H 121 P G D F G A D A Q G A M N K A L E L F R K D M A S N Y K E L 151 G F Q G