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P02144 (MYG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myoglobin
Gene names
Name:MB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length154 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.

Sequence similarities

Belongs to the globin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.11
Chain2 – 154153Myoglobin
PRO_0000053303

Sites

Metal binding651Iron (heme distal ligand)
Metal binding941Iron (heme proximal ligand)

Natural variations

Natural variant551E → K. Ref.12
VAR_003180
Natural variant1341K → N. Ref.14
VAR_003181
Natural variant1401R → Q. Ref.15
Corresponds to variant rs142225854 [ dbSNP | Ensembl ].
VAR_003182
Natural variant1401R → W. Ref.13
VAR_003183

Experimental info

Sequence conflict1061E → Q in AAX84516. Ref.5
Sequence conflict1291Q → E in AAA59595. Ref.2

Secondary structure

...................... 154
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02144 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F6A41F19A525F09C

FASTA15417,184
        10         20         30         40         50         60 
MGLSDGEWQL VLNVWGKVEA DIPGHGQEVL IRLFKGHPET LEKFDKFKHL KSEDEMKASE 

        70         80         90        100        110        120 
DLKKHGATVL TALGGILKKK GHHEAEIKPL AQSHATKHKI PVKYLEFISE CIIQVLQSKH 

       130        140        150 
PGDFGADAQG AMNKALELFR KDMASNYKEL GFQG 

« Hide

References

« Hide 'large scale' references
[1]"Organization of the human myoglobin gene."
Weller P., Jeffreys A.J., Wilson V., Blanchetot A.
EMBO J. 3:439-446(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning of the human myoglobin gene."
Akaboshi E.
Gene 33:241-249(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]NIEHS SNPs program
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skeletal muscle.
[8]"Primary structure of human myoglobin."
Romero-Herrera A.E., Lehmann H.
Nature New Biol. 232:149-152(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-154.
[9]"The myoglobin of primates. I. Hylobates agilis (gibbon)."
Romero-Herrera A.E., Lehmann H.
Biochim. Biophys. Acta 251:482-488(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 20-23 AND 84.
[10]"The myoglobin of primates. II. Pan troglodytes (chimpanzee)."
Romero-Herrera A.E., Lehmann H.
Biochim. Biophys. Acta 278:62-67(1972) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 100-102.
[11]"The human myocardial two-dimensional gel protein database: update 1994."
Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.
Electrophoresis 15:1459-1465(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21.
Tissue: Heart.
[12]"Abnormal human myoglobin: 53 (D4) glutamic acid-->lysine."
Boulton F.E., Huntsman R.G., Lorkin P.A., Lehmann H.
Nature 223:832-833(1969) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LYS-55.
[13]"The third variant of human myoglobin showing an unusual amino acid substitution: 138(H16)arginine-->tryptophan."
Boulton F.E., Huntsman R.G., Romero Herrera A., Lorkin P.A., Lehmann H.
Biochim. Biophys. Acta 229:716-719(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TRP-140.
[14]"A human myoglobin variant 133 (H-10)lysine-->asparagine."
Boulton F.E., Huntsman R.G., Romero Herrera A.E., Lorkin P.A., Lehmann H.
Biochim. Biophys. Acta 229:871-876(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASN-134.
[15]"The second variant of human myoglobin; 138(H16) arginine leads to glutamine."
Boulton F.E., Huntsman R.G., Yawson G.I., Romero-Herrera A.E., Lorkin P.A.
Br. J. Haematol. 20:69-74(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLN-140.
[16]"X-ray crystal structure of a recombinant human myoglobin mutant at 2.8-A resolution."
Hubbard S.R., Hendrickson W.A., Lambright D.G., Boxer S.G.
J. Mol. Biol. 213:215-218(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ARG-46 AND ALA-111 IN COMPLEX WITH HEME.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00371, X00372, X00373 Genomic DNA. Translation: CAA25109.1.
M14603, M10090, M14602 Genomic DNA. Translation: AAA59595.1.
CR456516 mRNA. Translation: CAG30402.1.
CR541949 mRNA. Translation: CAG46747.1.
DQ003030 Genomic DNA. Translation: AAX84516.1.
AL022334, AL049747 Genomic DNA. Translation: CAI21837.1.
BC014547 mRNA. Translation: AAH14547.1.
CCDSCCDS13917.1.
PIRMYHU. I53991.
RefSeqNP_005359.1. NM_005368.2.
NP_976311.1. NM_203377.1.
NP_976312.1. NM_203378.1.
XP_005261662.1. XM_005261605.2.
UniGeneHs.517586.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RGKX-ray1.65A2-154[»]
ProteinModelPortalP02144.
SMRP02144. Positions 2-150.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110321. 3 interactions.
STRING9606.ENSP00000352835.

Chemistry

ChEMBLCHEMBL2406892.

PTM databases

PhosphoSiteP02144.

Polymorphism databases

DMDM127661.

2D gel databases

UCD-2DPAGEP02144.

Proteomic databases

MaxQBP02144.
PaxDbP02144.
PeptideAtlasP02144.
PRIDEP02144.

Protocols and materials databases

DNASU4151.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359787; ENSP00000352835; ENSG00000198125.
ENST00000397326; ENSP00000380489; ENSG00000198125.
ENST00000397328; ENSP00000380491; ENSG00000198125.
ENST00000406324; ENSP00000384239; ENSG00000198125.
GeneID4151.
KEGGhsa:4151.
UCSCuc003anz.3. human.

Organism-specific databases

CTD4151.
GeneCardsGC22M036002.
HGNCHGNC:6915. MB.
HPACAB000060.
HPA003123.
MIM160000. gene.
neXtProtNX_P02144.
PharmGKBPA30658.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG276460.
HOGENOMHOG000070111.
HOVERGENHBG107340.
InParanoidP02144.
OMADAQGAMN.
PhylomeDBP02144.
TreeFamTF332967.

Gene expression databases

ArrayExpressP02144.
BgeeP02144.
CleanExHS_MB.
GenevestigatorP02144.

Family and domain databases

Gene3D1.10.490.10. 1 hit.
InterProIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002335. Myoglobin.
[Graphical view]
PANTHERPTHR11442:SF5. PTHR11442:SF5. 1 hit.
PfamPF00042. Globin. 1 hit.
[Graphical view]
PRINTSPR00613. MYOGLOBIN.
SUPFAMSSF46458. SSF46458. 1 hit.
PROSITEPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMB. human.
GeneWikiMyoglobin.
GenomeRNAi4151.
NextBio16322.
PROP02144.
SOURCESearch...

Entry information

Entry nameMYG_HUMAN
AccessionPrimary (citable) accession number: P02144
Secondary accession number(s): Q52H51, Q5THY7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM