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P02144

- MYG_HUMAN

UniProt

P02144 - MYG_HUMAN

Protein

Myoglobin

Gene

MB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi65 – 651Iron (heme distal ligand)
    Metal bindingi94 – 941Iron (heme proximal ligand)

    GO - Molecular functioni

    1. heme binding Source: InterPro
    2. iron ion binding Source: InterPro
    3. oxygen binding Source: Ensembl
    4. oxygen transporter activity Source: UniProtKB-KW

    GO - Biological processi

    1. brown fat cell differentiation Source: Ensembl
    2. enucleate erythrocyte differentiation Source: Ensembl
    3. heart development Source: Ensembl
    4. response to hormone Source: Ensembl
    5. response to hydrogen peroxide Source: Ensembl
    6. response to hypoxia Source: Ensembl
    7. slow-twitch skeletal muscle fiber contraction Source: Ensembl

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Biological processi

    Oxygen transport, Transport

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myoglobin
    Gene namesi
    Name:MB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:6915. MB.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30658.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 154153MyoglobinPRO_0000053303Add
    BLAST

    Proteomic databases

    MaxQBiP02144.
    PaxDbiP02144.
    PeptideAtlasiP02144.
    PRIDEiP02144.

    2D gel databases

    UCD-2DPAGEP02144.

    PTM databases

    PhosphoSiteiP02144.

    Expressioni

    Gene expression databases

    ArrayExpressiP02144.
    BgeeiP02144.
    CleanExiHS_MB.
    GenevestigatoriP02144.

    Organism-specific databases

    HPAiCAB000060.
    HPA003123.

    Interactioni

    Protein-protein interaction databases

    BioGridi110321. 3 interactions.
    STRINGi9606.ENSP00000352835.

    Structurei

    Secondary structure

    1
    154
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 1814
    Helixi19 – 213
    Helixi22 – 3615
    Helixi38 – 436
    Helixi45 – 473
    Helixi53 – 575
    Helixi60 – 7718
    Turni78 – 814
    Helixi84 – 9613
    Helixi102 – 11918
    Turni121 – 1233
    Helixi126 – 14924

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3RGKX-ray1.65A2-154[»]
    ProteinModelPortaliP02144.
    SMRiP02144. Positions 2-150.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the globin family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG276460.
    HOGENOMiHOG000070111.
    HOVERGENiHBG107340.
    InParanoidiP02144.
    OMAiDAQGAMN.
    PhylomeDBiP02144.
    TreeFamiTF332967.

    Family and domain databases

    Gene3Di1.10.490.10. 1 hit.
    InterProiIPR000971. Globin.
    IPR009050. Globin-like.
    IPR012292. Globin_dom.
    IPR002335. Myoglobin.
    [Graphical view]
    PANTHERiPTHR11442:SF5. PTHR11442:SF5. 1 hit.
    PfamiPF00042. Globin. 1 hit.
    [Graphical view]
    PRINTSiPR00613. MYOGLOBIN.
    SUPFAMiSSF46458. SSF46458. 1 hit.
    PROSITEiPS01033. GLOBIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P02144-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLSDGEWQL VLNVWGKVEA DIPGHGQEVL IRLFKGHPET LEKFDKFKHL    50
    KSEDEMKASE DLKKHGATVL TALGGILKKK GHHEAEIKPL AQSHATKHKI 100
    PVKYLEFISE CIIQVLQSKH PGDFGADAQG AMNKALELFR KDMASNYKEL 150
    GFQG 154
    Length:154
    Mass (Da):17,184
    Last modified:January 23, 2007 - v2
    Checksum:iF6A41F19A525F09C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti106 – 1061E → Q in AAX84516. 1 PublicationCurated
    Sequence conflicti129 – 1291Q → E in AAA59595. (PubMed:2989088)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551E → K.1 Publication
    VAR_003180
    Natural varianti134 – 1341K → N.1 Publication
    VAR_003181
    Natural varianti140 – 1401R → Q.1 Publication
    Corresponds to variant rs142225854 [ dbSNP | Ensembl ].
    VAR_003182
    Natural varianti140 – 1401R → W.1 Publication
    VAR_003183

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS13917.1.
    PIRiI53991. MYHU.
    RefSeqiNP_005359.1. NM_005368.2.
    NP_976311.1. NM_203377.1.
    NP_976312.1. NM_203378.1.
    XP_005261662.1. XM_005261605.2.
    UniGeneiHs.517586.

    Genome annotation databases

    EnsembliENST00000359787; ENSP00000352835; ENSG00000198125.
    ENST00000397326; ENSP00000380489; ENSG00000198125.
    ENST00000397328; ENSP00000380491; ENSG00000198125.
    ENST00000406324; ENSP00000384239; ENSG00000198125.
    GeneIDi4151.
    KEGGihsa:4151.
    UCSCiuc003anz.3. human.

    Polymorphism databases

    DMDMi127661.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS13917.1.
    PIRi I53991. MYHU.
    RefSeqi NP_005359.1. NM_005368.2.
    NP_976311.1. NM_203377.1.
    NP_976312.1. NM_203378.1.
    XP_005261662.1. XM_005261605.2.
    UniGenei Hs.517586.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3RGK X-ray 1.65 A 2-154 [» ]
    ProteinModelPortali P02144.
    SMRi P02144. Positions 2-150.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110321. 3 interactions.
    STRINGi 9606.ENSP00000352835.

    Chemistry

    ChEMBLi CHEMBL2406892.

    PTM databases

    PhosphoSitei P02144.

    Polymorphism databases

    DMDMi 127661.

    2D gel databases

    UCD-2DPAGE P02144.

    Proteomic databases

    MaxQBi P02144.
    PaxDbi P02144.
    PeptideAtlasi P02144.
    PRIDEi P02144.

    Protocols and materials databases

    DNASUi 4151.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359787 ; ENSP00000352835 ; ENSG00000198125 .
    ENST00000397326 ; ENSP00000380489 ; ENSG00000198125 .
    ENST00000397328 ; ENSP00000380491 ; ENSG00000198125 .
    ENST00000406324 ; ENSP00000384239 ; ENSG00000198125 .
    GeneIDi 4151.
    KEGGi hsa:4151.
    UCSCi uc003anz.3. human.

    Organism-specific databases

    CTDi 4151.
    GeneCardsi GC22M036002.
    HGNCi HGNC:6915. MB.
    HPAi CAB000060.
    HPA003123.
    MIMi 160000. gene.
    neXtProti NX_P02144.
    PharmGKBi PA30658.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG276460.
    HOGENOMi HOG000070111.
    HOVERGENi HBG107340.
    InParanoidi P02144.
    OMAi DAQGAMN.
    PhylomeDBi P02144.
    TreeFami TF332967.

    Miscellaneous databases

    ChiTaRSi MB. human.
    GeneWikii Myoglobin.
    GenomeRNAii 4151.
    NextBioi 16322.
    PROi P02144.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02144.
    Bgeei P02144.
    CleanExi HS_MB.
    Genevestigatori P02144.

    Family and domain databases

    Gene3Di 1.10.490.10. 1 hit.
    InterProi IPR000971. Globin.
    IPR009050. Globin-like.
    IPR012292. Globin_dom.
    IPR002335. Myoglobin.
    [Graphical view ]
    PANTHERi PTHR11442:SF5. PTHR11442:SF5. 1 hit.
    Pfami PF00042. Globin. 1 hit.
    [Graphical view ]
    PRINTSi PR00613. MYOGLOBIN.
    SUPFAMi SSF46458. SSF46458. 1 hit.
    PROSITEi PS01033. GLOBIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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.

    Entry informationi

    Entry nameiMYG_HUMAN
    AccessioniPrimary (citable) accession number: P02144
    Secondary accession number(s): Q52H51, Q5THY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3