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P02144

- MYG_HUMAN

UniProt

P02144 - MYG_HUMAN

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Protein

Myoglobin

Gene

MB

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

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
Complete GO annotation...

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.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

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

BgeeiP02144.
CleanExiHS_MB.
ExpressionAtlasiP02144. baseline and differential.
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.
GeneTreeiENSGT00730000110844.
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

        10         20         30         40         50
MGLSDGEWQL VLNVWGKVEA DIPGHGQEVL IRLFKGHPET LEKFDKFKHL
60 70 80 90 100
KSEDEMKASE DLKKHGATVL TALGGILKKK GHHEAEIKPL AQSHATKHKI
110 120 130 140 150
PVKYLEFISE CIIQVLQSKH PGDFGADAQG AMNKALELFR KDMASNYKEL

GFQG
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.
GeneTreei ENSGT00730000110844.
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

Bgeei P02144.
CleanExi HS_MB.
ExpressionAtlasi P02144. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 149 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