Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P12979 (MYOG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myogenin
Alternative name(s):
MYOD1-related protein
Gene names
Name:Myog
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation, cell cycle exit and muscle atrophy. Essential for the development of functional embryonic skeletal fiber muscle differentiation. However is dispensable for postnatal skeletal muscle growth; phosphorylation by CAMK2G inhibits its transcriptional activity in respons to muscle activity. Required for the recruitment of the FACT complex to muscle-specific promoter regions, thus promoting gene expression initiation. During terminal myoblast differentiation, plays a role as a strong activator of transcription at loci with an open chromatin structure previously initiated by MYOD1. Together with MYF5 and MYOD1, co-occupies muscle-specific gene promoter core regions during myogenesis. Cooperates also with myocyte-specific enhancer factor MEF2D and BRG1-dependent recruitment of SWI/SNF chromatin-remodeling enzymes to alter chromatin structure at myogenic late gene promoters. Facilitates cell cycle exit during terminal muscle differentiation through the up-regulation of miR-20a expression, which in turn represses genes involved in cell cycle progression. Binds to the E-box containing (E1) promoter region of the miR-20a gene. Plays also a role in preventing reversal of muscle cell differentiation. Contributes to the atrophy-related gene expression in adult denervated muscles. Induces fibroblasts to differentiate into myoblasts. Ref.8 Ref.9 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20

Subunit structure

Homodimer and heterodimer with E12; heterodimerization enhances MYOG DNA-binding and transcriptional activities. Interacts with SMARCA4/BRG1/BAF190A. Interacts (via C-terminal region) with SSRP1 and SUPT16H; the interaction is indicative of an interaction with the FACT complex. Ref.11 Ref.14 Ref.20

Subcellular location

Nucleus. Note: Recruited to late myogenic gene promoter regulatory sequences with SMARCA4/BRG1/BAF190A and SWI/SNF chromatin-remodeling enzymes to promote chromatin-remodeling and transcription initiation in developing embryos. Ref.14

Tissue specificity

Expressed in myoblast cells. Expressed weakly in myotubes (at protein level). Expressed strongly in denervated muscles and in satellite cells isolated from denervated muscles. Expressed weakly in innervated muscle and in satellite cells isolated from innervated muscles. Ref.16 Ref.17

Developmental stage

Expressed in the myotome of the somites at 8.5 dpc, onward (at protein level). Expressed in proximal region of both the hindlimb and the forelimb at 11.5 dpc, onward. Expressed during muscle maturation between 15 and 17 dpc and decreases thereafter. Not detected within the heart. Ref.6 Ref.7 Ref.10

Induction

Up-regulated in denervated muscles (at protein level). Up-regulated during myogenesis in the embryo and in cell culture models of myogenic differentiation via the p38 MAPK signaling pathway. Ref.16 Ref.17 Ref.18

Post-translational modification

Phosphorylated by CAMK2G on threonine and serine amino acids in a muscle activity-dependent manner. Phosphorylation of Thr-87 impairs both DNA-binding and trans-activation functions in contracting muscles By similarity.

Disruption phenotype

Display normal myoblast formation during embryogenesis, but show perinatal lethality because of a deficiency during the later stages of skeletal muscle fiber formation. Show no abnormalities for smooth muscles and cardiocytes differentiation. Conditional mutant with expression abrogated in muscle cells from 15.5 or 17.5 dpc are viable, fertil and exhibit no noticeable muscle growth and reduction of myofiber diameter defects but show smaller body size and mass. Conditional mutant in muscle cells of denervated hindlimb muscles show an inhibition of the denervation-dependent reductions in mass, force and atrophy of slow fiber-type soleus muscles, without increased in satellite cell proliferation and fusion. Ref.8 Ref.9

Sequence similarities

Contains 1 bHLH (basic helix-loop-helix) domain.

Ontologies

Keywords
   Biological processCell cycle
Differentiation
Myogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
Developmental protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to estradiol stimulus

Inferred from direct assay Ref.12. Source: UniProtKB

cellular response to growth factor stimulus

Inferred from direct assay PubMed 15322112. Source: MGI

cellular response to lithium ion

Inferred from direct assay PubMed 15673614. Source: MGI

mRNA transcription from RNA polymerase II promoter

Inferred by curator PubMed 19783823. Source: BHF-UCL

muscle organ development

Inferred from genetic interaction PubMed 8587605. Source: MGI

myotube differentiation

Inferred from genetic interaction PubMed 22106411. Source: MGI

negative regulation of cell proliferation

Inferred from direct assay Ref.18. Source: UniProtKB

ossification

Inferred from mutant phenotype PubMed 8587605. Source: MGI

positive regulation of cell cycle arrest

Inferred from direct assay Ref.18. Source: UniProtKB

positive regulation of muscle atrophy

Inferred from mutant phenotype Ref.16. Source: UniProtKB

positive regulation of myoblast differentiation

Inferred from direct assay Ref.18. Source: UniProtKB

positive regulation of myotube differentiation

Inferred from direct assay Ref.18. Source: UniProtKB

positive regulation of skeletal muscle fiber development

Inferred from mutant phenotype Ref.8. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.12Ref.16Ref.18. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 17904117. Source: MGI

regulation of myoblast fusion

Inferred from mutant phenotype Ref.16. Source: UniProtKB

regulation of satellite cell proliferation

Inferred from mutant phenotype Ref.16. Source: UniProtKB

response to denervation involved in regulation of muscle adaptation

Inferred from direct assay Ref.16. Source: UniProtKB

response to electrical stimulus involved in regulation of muscle adaptation

Inferred from sequence or structural similarity. Source: UniProtKB

response to muscle activity involved in regulation of muscle adaptation

Inferred from sequence or structural similarity. Source: UniProtKB

skeletal muscle fiber development

Inferred from mutant phenotype Ref.8. Source: MGI

skeletal muscle tissue development

Inferred from direct assay PubMed 14762206. Source: MGI

striated muscle atrophy

Inferred from mutant phenotype Ref.16. Source: UniProtKB

   Cellular_componentnucleus

Inferred from direct assay PubMed 16554364PubMed 19319192PubMed 21177767. Source: MGI

protein-DNA complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay PubMed 10835421PubMed 12486129PubMed 14762206PubMed 16140986. Source: MGI

E-box binding

Inferred from direct assay PubMed 19783823. Source: BHF-UCL

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Traceable author statement PubMed 1846704. Source: MGI

RNA polymerase II regulatory region sequence-specific DNA binding

Inferred from direct assay PubMed 19783823. Source: BHF-UCL

RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred by curator PubMed 19783823. Source: BHF-UCL

chromatin DNA binding

Inferred from direct assay Ref.12Ref.18. Source: UniProtKB

core promoter binding

Inferred from direct assay Ref.12Ref.18. Source: UniProtKB

core promoter proximal region sequence-specific DNA binding

Inferred from direct assay PubMed 20399744. Source: MGI

protein binding

Inferred from physical interaction PubMed 19319192. Source: MGI

sequence-specific DNA binding

Inferred from direct assay PubMed 22638570. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.16. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 224224Myogenin
PRO_0000127376

Regions

Domain81 – 13252bHLH

Amino acid modifications

Modified residue771Phosphoserine; by CaMK2G By similarity
Modified residue791Phosphoserine; by CaMK2G By similarity
Modified residue871Phosphothreonine; by CaMK2G By similarity

Sequences

Sequence LengthMass (Da)Tools
P12979 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: CC7352C1EDF9D3D8

FASTA22425,203
        10         20         30         40         50         60 
MELYETSPYF YQEPHFYDGE NYLPVHLQGF EPPGYERTEL SLSPEARGPL EEKGLGTPEH 

        70         80         90        100        110        120 
CPGQCLPWAC KVCKRKSVSV DRRRAATLRE KRRLKKVNEA FEALKRSTLL NPNQRLPKVE 

       130        140        150        160        170        180 
ILRSAIQYIE RLQALLSSLN QEERDLRYRG GGGPQPMVPS ECNSHSASCS PEWGNALEFG 

       190        200        210        220 
PNPGDHLLAA DPTDAHNLHS LTSIVDSITV EDMSVAFPDE TMPN 

« Hide

References

« Hide 'large scale' references
[1]"A gene with homology to the myc similarity region of MyoD1 is expressed during myogenesis and is sufficient to activate the muscle differentiation program."
Edmondson D.G., Olson E.N.
Genes Dev. 3:628-640(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Muscle.
[2]Erratum
Edmondson D.G., Olson E.N.
Genes Dev. 4:1450-1450(1990) [PubMed] [Europe PMC] [Abstract]
[3]"Analysis of the myogenin promoter reveals an indirect pathway for positive autoregulation mediated by the muscle-specific enhancer factor MEF-2."
Edmondson D.G., Cheng T.C., Cserjesi P., Chakraborty T., Olson E.N.
Mol. Cell. Biol. 12:3665-3677(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Myogenin contains two domains conserved among myogenic factors."
Fujisawa-Sehara A., Nabeshima Y., Hosoda Y., Obinata T., Nabeshima Y.
J. Biol. Chem. 265:15219-15223(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"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: Limb.
[6]"Expression of two myogenic regulatory factors myogenin and MyoD1 during mouse embryogenesis."
Sassoon D., Lyons G., Wright W.E., Lin V., Lassar A., Weintraub H., Buckingham M.
Nature 341:303-307(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[7]"Myogenin and MyoD join a family of skeletal muscle genes regulated by electrical activity."
Eftimie R., Brenner H.R., Buonanno A.
Proc. Natl. Acad. Sci. U.S.A. 88:1349-1353(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[8]"Muscle deficiency and neonatal death in mice with a targeted mutation in the myogenin gene."
Hasty P., Bradley A., Morris J.H., Edmondson D.G., Venuti J.M., Olson E.N., Klein W.H.
Nature 364:501-506(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[9]"Myogenin gene disruption results in perinatal lethality because of severe muscle defect."
Nabeshima Y., Hanaoka K., Hayasaka M., Esumi E., Li S., Nonaka I., Nabeshima Y.
Nature 364:532-535(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[10]"Somite subdomains, muscle cell origins, and the four muscle regulatory factor proteins."
Smith T.H., Kachinsky A.M., Miller J.B.
J. Cell Biol. 127:95-105(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[11]"Analysis of the DNA-binding properties of MyoD, myogenin, and E12 by fluorescence anisotropy."
Maleki S.J., Royer C.A., Hurlburt B.K.
Biochemistry 41:10888-10894(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[12]"An initial blueprint for myogenic differentiation."
Blais A., Tsikitis M., Acosta-Alvear D., Sharan R., Kluger Y., Dynlacht B.D.
Genes Dev. 19:553-569(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PROMOTER BINDING.
[13]"Loss of myogenin in postnatal life leads to normal skeletal muscle but reduced body size."
Knapp J.R., Davie J.K., Myer A., Meadows E., Olson E.N., Klein W.H.
Development 133:601-610(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CONDITIONAL KNOCKOUT IN MUSCLE CELLS.
[14]"Skeletal muscle specification by myogenin and Mef2D via the SWI/SNF ATPase Brg1."
Ohkawa Y., Marfella C.G., Imbalzano A.N.
EMBO J. 25:490-501(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SMARCA4, SUBCELLULAR LOCATION.
[15]"Global and gene-specific analyses show distinct roles for Myod and Myog at a common set of promoters."
Cao Y., Kumar R.M., Penn B.H., Berkes C.A., Kooperberg C., Boyer L.A., Young R.A., Tapscott S.J.
EMBO J. 25:502-511(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Myogenin regulates denervation-dependent muscle atrophy in mouse soleus muscle."
Macpherson P.C., Wang X., Goldman D.
J. Cell. Biochem. 112:2149-2159(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CONDITIONAL KNOCKOUT IN MUSCLE CELLS, INDUCTION, TISSUE SPECIFICITY.
[17]"Sequential association of myogenic regulatory factors and E proteins at muscle-specific genes."
Londhe P., Davie J.K.
Skelet. Muscle 1:14-14(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PROMOTER BINDING, INDUCTION, TISSUE SPECIFICITY.
[18]"Comparative expression profiling identifies differential roles for Myogenin and p38alpha MAPK signaling in myogenesis."
Liu Q.C., Zha X.H., Faralli H., Yin H., Louis-Jeune C., Perdiguero E., Pranckeviciene E., Munoz-Canoves P., Rudnicki M.A., Brand M., Perez-Iratxeta C., Dilworth F.J.
J. Mol. Cell Biol. 4:386-397(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[19]"Down-regulation of myogenin can reverse terminal muscle cell differentiation."
Mastroyiannopoulos N.P., Nicolaou P., Anayasa M., Uney J.B., Phylactou L.A.
PLoS ONE 7:E29896-E29896(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MUSCLE DEDIFFERENTIATION INHIBITION.
[20]"Myogenin recruits the histone chaperone facilitates chromatin transcription (FACT) to promote nucleosome disassembly at muscle-specific genes."
Lolis A.A., Londhe P., Beggs B.C., Byrum S.D., Tackett A.J., Davie J.K.
J. Biol. Chem. 288:7676-7687(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SSRP1 AND SUPT16H.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M95800 Genomic DNA. Translation: AAB59676.1.
X15784 mRNA. Translation: CAA33785.1. Sequence problems.
D90156 mRNA. Translation: BAA14187.1.
BC048683 mRNA. Translation: AAH48683.1.
BC068019 mRNA. Translation: AAH68019.1.
CCDSCCDS15306.1.
PIRA36675. A35882.
RefSeqNP_112466.1. NM_031189.2.
UniGeneMm.16528.

3D structure databases

ProteinModelPortalP12979.
SMRP12979. Positions 74-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201674. 9 interactions.
DIPDIP-29976N.
IntActP12979. 3 interactions.
MINTMINT-1958829.
STRING10090.ENSMUSP00000027730.

PTM databases

PhosphoSiteP12979.

Proteomic databases

PRIDEP12979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027730; ENSMUSP00000027730; ENSMUSG00000026459.
GeneID17928.
KEGGmmu:17928.
UCSCuc007crl.2. mouse.

Organism-specific databases

CTD4656.
MGIMGI:97276. Myog.

Phylogenomic databases

eggNOGNOG285405.
GeneTreeENSGT00530000063004.
HOGENOMHOG000234799.
HOVERGENHBG006429.
InParanoidP12979.
OMAFYQEPHF.
OrthoDBEOG76QFK1.
PhylomeDBP12979.
TreeFamTF316344.

Gene expression databases

BgeeP12979.
CleanExMM_MYOG.
GenevestigatorP12979.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR002546. Basic.
IPR011598. bHLH_dom.
[Graphical view]
PfamPF01586. Basic. 1 hit.
PF00010. HLH. 1 hit.
[Graphical view]
SMARTSM00520. BASIC. 1 hit.
SM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio292801.
PROP12979.
SOURCESearch...

Entry information

Entry nameMYOG_MOUSE
AccessionPrimary (citable) accession number: P12979
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: December 1, 1992
Last modified: July 9, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot