Myogenin

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• chromatin DNA binding Source: UniProtKB
• cis-regulatory region sequence-specific DNA binding Source: RGDInferred from sequence orthologyⁱ
  • "TRIM72, a novel negative feedback regulator of myogenesis, is transcriptionally activated by the synergism of MyoD (or myogenin) and MEF2."
    Jung S.Y., Ko Y.G.
    Biochem. Biophys. Res. Commun. 396:238-245(2010) [PubMed] [Europe PMC] [Abstract]
• DNA binding Source: RGDInferred from sequence orthologyⁱ
  • "The basic helix-loop-helix transcription factors myogenin and Id2 mediate specific induction of caveolin-3 gene expression during embryonic development."
    Biederer C.H., Ries S.J., Moser M., Florio M., Israel M.A., McCormick F., Buettner R.
    J. Biol. Chem. 275:26245-26251(2000) [PubMed] [Europe PMC] [Abstract]
  • "The homeodomain protein Barx2 promotes myogenic differentiation and is regulated by myogenic regulatory factors."
    Meech R., Makarenkova H., Edelman D.B., Jones F.S.
    J. Biol. Chem. 278:8269-8278(2003) [PubMed] [Europe PMC] [Abstract]
  • "VITO-1 is an essential cofactor of TEF1-dependent muscle-specific gene regulation."
    Gunther S., Mielcarek M., Kruger M., Braun T.
    Nucleic Acids Res. 32:791-802(2004) [PubMed] [Europe PMC] [Abstract]
  • "Centronuclear myopathy in mice lacking a novel muscle-specific protein kinase transcriptionally regulated by MEF2."
    Nakagawa O., Arnold M., Nakagawa M., Hamada H., Shelton J.M., Kusano H., Harris T.M., Childs G., Campbell K.P., Richardson J.A., Nishino I., Olson E.N.
    Genes Dev. 19:2066-2077(2005) [PubMed] [Europe PMC] [Abstract]
• DNA-binding transcription activator activity, RNA polymerase II-specific Source: RGDInferred from sequence orthologyⁱ
  • "Cloning of human acetyl-CoA carboxylase beta promoter and its regulation by muscle regulatory factors."
    Lee J.J., Moon Y.A., Ha J.H., Yoon D.J., Ahn Y.H., Kim K.S.
    J. Biol. Chem. 276:2576-2585(2001) [PubMed] [Europe PMC] [Abstract]
  • "Regulation of the promoter of CUG triplet repeat binding protein, Cugbp1, during myogenesis."
    Huichalaf C.H., Sakai K., Wang G.L., Timchenko N.A., Timchenko L.
    Gene 396:391-402(2007) [PubMed] [Europe PMC] [Abstract]
  • "Kbtbd5 is regulated by MyoD and restricted to the myogenic lineage."
    Bowlin K.M., Embree L.J., Garry M.G., Garry D.J., Shi X.
    Differentiation 86:184-191(2013) [PubMed] [Europe PMC] [Abstract]
• DNA-binding transcription factor activity Source: UniProtKB
• DNA-binding transcription factor activity, RNA polymerase II-specific Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• E-box binding Source: UniProtKB
• protein dimerization activity Source: InterPro
• RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: RGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.4

    "CaM kinase II-dependent phosphorylation of myogenin contributes to activity-dependent suppression of nAChR gene expression in developing rat myotubes."
    Tang H., Macpherson P., Argetsinger L.S., Cieslak D., Suhr S.T., Carter-Su C., Goldman D.
    Cell. Signal. 16:551-563(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, PHOSPHORYLATION AT SER-77; SER-79 AND THR-87, DNA-BINDING, MUTAGENESIS OF SER-77; SER-79 AND THR-87.
• RNA polymerase II regulatory region sequence-specific DNA binding Source: RGDInferred from sequence orthologyⁱ
  • "Cloning of human acetyl-CoA carboxylase beta promoter and its regulation by muscle regulatory factors."
    Lee J.J., Moon Y.A., Ha J.H., Yoon D.J., Ahn Y.H., Kim K.S.
    J. Biol. Chem. 276:2576-2585(2001) [PubMed] [Europe PMC] [Abstract]
  • "SMYD1, the myogenic activator, is a direct target of serum response factor and myogenin."
    Li D., Niu Z., Yu W., Qian Y., Wang Q., Li Q., Yi Z., Luo J., Wu X., Wang Y., Schwartz R.J., Liu M.
    Nucleic Acids Res. 37:7059-7071(2009) [PubMed] [Europe PMC] [Abstract]
• sequence-specific DNA binding Source: RGDInferred from sequence orthologyⁱ
  • "Cloning of human acetyl-CoA carboxylase beta promoter and its regulation by muscle regulatory factors."
    Lee J.J., Moon Y.A., Ha J.H., Yoon D.J., Ahn Y.H., Kim K.S.
    J. Biol. Chem. 276:2576-2585(2001) [PubMed] [Europe PMC] [Abstract]
  • "Myh7b/miR-499 gene expression is transcriptionally regulated by MRFs and Eos."
    Yeung F., Chung E., Guess M.G., Bell M.L., Leinwand L.A.
    Nucleic Acids Res. 40:7303-7318(2012) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• cell cycle Source: UniProtKB-KW
• cellular response to estradiol stimulus Source: UniProtKB
• cellular response to growth factor stimulus Source: RGDInferred from sequence orthologyⁱ
  • "Myogenin protein stability is decreased by BMP-2 through a mechanism implicating Id1."
    Vinals F., Ventura F.
    J. Biol. Chem. 279:45766-45772(2004) [PubMed] [Europe PMC] [Abstract]
• cellular response to lithium ion Source: RGDInferred from sequence orthologyⁱ
  • "Wnt10b deficiency promotes coexpression of myogenic and adipogenic programs in myoblasts."
    Vertino A.M., Taylor-Jones J.M., Longo K.A., Bearden E.D., Lane T.F., McGehee R.E. Jr., MacDougald O.A., Peterson C.A.
    Mol. Biol. Cell 16:2039-2048(2005) [PubMed] [Europe PMC] [Abstract]
• cellular response to magnetism Source: RGD <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • "Differentiation of myoblasts is accelerated in culture in a magnetic field."
    Yuge L., Kataoka K.
    In Vitro Cell. Dev. Biol. Anim. 36:383-386(2000) [PubMed] [Europe PMC] [Abstract]
• cellular response to retinoic acid Source: RGDInferred from expression patternⁱ
  • "Retinoic acid induces myogenin synthesis and myogenic differentiation in the rat rhabdomyosarcoma cell line BA-Han-1C."
    Arnold H.H., Gerharz C.D., Gabbert H.E., Salminen A.
    J. Cell Biol. 118:877-887(1992) [PubMed] [Europe PMC] [Abstract]
• cellular response to tumor necrosis factor Source: RGDInferred from sequence orthologyⁱ
  • "MicroRNA-494, upregulated by tumor necrosis factor-alpha, desensitizes insulin effect in C2C12 muscle cells."
    Lee H., Jee Y., Hong K., Hwang G.S., Chun K.H.
    PLoS ONE 8:e83471-e83471(2013) [PubMed] [Europe PMC] [Abstract]
• muscle organ development Source: RGDInferred from sequence orthologyⁱ
  • "Functional redundancy of the muscle-specific transcription factors Myf5 and myogenin."
    Wang Y., Schnegelsberg P.N., Dausman J., Jaenisch R.
    Nature 379:823-825(1996) [PubMed] [Europe PMC] [Abstract]
• myoblast differentiation Source: RGDInferred from expression patternⁱ
  • "Simultaneous myogenin expression and overall DNA hypomethylation promote in vitro myoblast differentiation."
    Scarpa S., Lucarelli M., Palitti F., Carotti D., Strom R.
    Cell Growth Differ. 7:1051-1058(1996) [PubMed] [Europe PMC] [Abstract]
• myotube differentiation Source: RGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Highly specific inhibition of IGF-I-stimulated differentiation by an antisense oligodeoxyribonucleotide to myogenin mRNA. No effects on other actions of IGF-T."
    Florini J.R., Ewton D.Z.
    J. Biol. Chem. 265:13435-13437(1990) [PubMed] [Europe PMC] [Abstract]
• negative regulation of cell population proliferation Source: UniProtKB
• negative regulation of glycolytic process Source: RGDInferred from direct assayⁱ
  • "Myogenin induces a shift of enzyme activity from glycolytic to oxidative metabolism in muscles of transgenic mice."
    Hughes S.M., Chi M.M., Lowry O.H., Gundersen K.
    J. Cell Biol. 145:633-642(1999) [PubMed] [Europe PMC] [Abstract]
• ossification Source: RGDInferred from sequence orthologyⁱ
  • "Functional redundancy of the muscle-specific transcription factors Myf5 and myogenin."
    Wang Y., Schnegelsberg P.N., Dausman J., Jaenisch R.
    Nature 379:823-825(1996) [PubMed] [Europe PMC] [Abstract]
• positive regulation of cell cycle arrest Source: UniProtKB
• positive regulation of muscle atrophy Source: UniProtKB
• positive regulation of myoblast differentiation Source: UniProtKB
• positive regulation of myoblast fusion Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation of myotube differentiation Source: UniProtKB
• positive regulation of oxidative phosphorylation Source: RGDInferred from direct assayⁱ
  • "Myogenin induces a shift of enzyme activity from glycolytic to oxidative metabolism in muscles of transgenic mice."
    Hughes S.M., Chi M.M., Lowry O.H., Gundersen K.
    J. Cell Biol. 145:633-642(1999) [PubMed] [Europe PMC] [Abstract]
• positive regulation of skeletal muscle fiber development Source: UniProtKB
• positive regulation of transcription, DNA-templated Source: RGDInferred from sequence orthologyⁱ
  • "Target gene selectivity of the myogenic basic helix-loop-helix transcription factor myogenin in embryonic muscle."
    Davie J.K., Cho J.H., Meadows E., Flynn J.M., Knapp J.R., Klein W.H.
    Dev. Biol. 311:650-664(2007) [PubMed] [Europe PMC] [Abstract]
• positive regulation of transcription by RNA polymerase II Source: UniProtKBInferred from direct assayⁱ
  • Ref.4

    "CaM kinase II-dependent phosphorylation of myogenin contributes to activity-dependent suppression of nAChR gene expression in developing rat myotubes."
    Tang H., Macpherson P., Argetsinger L.S., Cieslak D., Suhr S.T., Carter-Su C., Goldman D.
    Cell. Signal. 16:551-563(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, PHOSPHORYLATION AT SER-77; SER-79 AND THR-87, DNA-BINDING, MUTAGENESIS OF SER-77; SER-79 AND THR-87.
• regulation of myoblast fusion Source: UniProtKB
• regulation of skeletal muscle satellite cell proliferation Source: UniProtKB
• response to denervation involved in regulation of muscle adaptation Source: UniProtKB
• response to electrical stimulus involved in regulation of muscle adaptation Source: UniProtKBInferred from direct assayⁱ
  • "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]
• response to gravity Source: RGDInferred from expression patternⁱ
  • "Effects of microgravity on myogenic factor expressions during postnatal development of rat skeletal muscle."
    Inobe M., Inobe I., Adams G.R., Baldwin K.M., Takeda S., Baldwin K.M.
    J. Appl. Physiol. 92:1936-1942(2002) [PubMed] [Europe PMC] [Abstract]
• response to muscle activity Source: RGDInferred from expression patternⁱ
  • "Myogenin and oxidative enzyme gene expression levels are elevated in rat soleus muscles after endurance training."
    Siu P.M., Donley D.A., Bryner R.W., Alway S.E.
    J. Appl. Physiol. 97:277-285(2004) [PubMed] [Europe PMC] [Abstract]
• response to muscle activity involved in regulation of muscle adaptation Source: UniProtKBInferred from direct assayⁱ
  • Ref.4

    "CaM kinase II-dependent phosphorylation of myogenin contributes to activity-dependent suppression of nAChR gene expression in developing rat myotubes."
    Tang H., Macpherson P., Argetsinger L.S., Cieslak D., Suhr S.T., Carter-Su C., Goldman D.
    Cell. Signal. 16:551-563(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, PHOSPHORYLATION AT SER-77; SER-79 AND THR-87, DNA-BINDING, MUTAGENESIS OF SER-77; SER-79 AND THR-87.
• skeletal muscle atrophy Source: RGDInferred from expression patternⁱ
  • "Nerve activity-independent regulation of skeletal muscle atrophy: role of MyoD and myogenin in satellite cells and myonuclei."
    Hyatt J.P., Roy R.R., Baldwin K.M., Edgerton V.R.
    Am. J. Physiol., Cell Physiol. 285:C1161-73(2003) [PubMed] [Europe PMC] [Abstract]
• skeletal muscle cell differentiation Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• skeletal muscle fiber development Source: RGDInferred from sequence orthologyⁱ
  • "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]
• skeletal muscle tissue development Source: RGDInferred from sequence orthologyⁱ
  • "VITO-1 is an essential cofactor of TEF1-dependent muscle-specific gene regulation."
    Gunther S., Mielcarek M., Kruger M., Braun T.
    Nucleic Acids Res. 32:791-802(2004) [PubMed] [Europe PMC] [Abstract]
• skeletal muscle tissue regeneration Source: RGDInferred from expression patternⁱ
  • "Expression of MyoD and myogenin in dystrophic mice, mdx and dy, during regeneration."
    Jin Y., Murakami N., Saito Y., Goto Y., Koishi K., Nonaka I.
    Acta Neuropathol. 99:619-627(2000) [PubMed] [Europe PMC] [Abstract]
• striated muscle atrophy Source: UniProtKB

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductionⁱ

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

GO - Molecular functionⁱ

• protein dimerization activity Source: InterPro

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MELYETSPYF YQEPHFYDGE NYLPVHLQGF EPPGYERTEL SLSPEARGPL 
        60         70         80         90        100
EEKGLGTPEH CPGQCLPWAC KVCKRKSVSV DRRRAATLRE KRRLKKVNEA 
       110        120        130        140        150
FEALKRSTLL NPNQRLPKVE ILRSAIQYIE RLQALLSSLN QEERDLRYRG 
       160        170        180        190        200
GGGPSRWYPV NATPTAPPAV RSGAMHWSLV PTQEIICSQL TLQVPTTCTP 
       210        220        230        240        250
LRPSWTASRW RICLSPSQMK PCPTEIVCQA GCAWEPLSWC QTPPLLQQGP 
       260        270        280 
FKWGCPGAQK TALGCHKPDY PPSIHIRLTP SPAREFN               

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ