MyoD

MYOD1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1MDY
Identifiers
Aliases	MYOD1, MYF3, MYOD, PUM, bHLHc1, myogenic differentiation 1, MYODRIF
External IDs	OMIM: 159970; MGI: 97275; HomoloGene: 7857; GeneCards: MYOD1; OMA:MYOD1 - orthologs
Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11p15.1 Start 17,719,571 bp[1] End 17,722,136 bp[1]
Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7 B3|7 30.03 cM Start 46,025,898 bp[2] End 46,028,523 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in triceps brachii muscle Skeletal muscle tissue of biceps brachii glutes vastus lateralis muscle Skeletal muscle tissue of rectus abdominis muscle of thigh gastrocnemius muscle testicle deltoid muscle gonad Top expressed in myotome wrist tongue muscle muscle of thigh triceps brachii muscle sternocleidomastoid muscle temporal muscle skeletal muscle tissue knee joint extensor digitorum longus muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA binding sequence-specific DNA binding RNA polymerase II transcription regulatory region sequence-specific DNA binding protein dimerization activity DNA-binding transcription activator activity, RNA polymerase II-specific DNA-binding transcription factor activity transcription factor binding chromatin binding RNA polymerase II cis-regulatory region sequence-specific DNA binding E-box binding protein binding protein heterodimerization activity enzyme binding transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding chromatin DNA binding ubiquitin protein ligase binding transcription coactivator activity DNA-binding transcription factor activity, RNA polymerase II-specific promoter-specific chromatin binding Cellular component transcription regulator complex nucleoplasm myofibril nucleus cytoplasm cytosol nuclear body Biological process cell differentiation myotube differentiation regulation of transcription, DNA-templated regulation of transcription by RNA polymerase II cellular response to starvation muscle cell fate commitment cellular response to estradiol stimulus skeletal muscle fiber adaptation muscle organ development regulation of alternative mRNA splicing, via spliceosome myotube cell development positive regulation of skeletal muscle fiber development negative regulation of myoblast proliferation transcription, DNA-templated multicellular organism development positive regulation of transcription, DNA-templated protein phosphorylation regulation of RNA splicing positive regulation of myoblast fusion myoblast fate determination cellular response to glucocorticoid stimulus positive regulation of myoblast differentiation skeletal muscle fiber development histone H3 acetylation myotube differentiation involved in skeletal muscle regeneration histone H4 acetylation skeletal muscle cell differentiation positive regulation of skeletal muscle tissue regeneration regulation of gene expression striated muscle cell differentiation cellular response to oxygen levels myoblast fusion myoblast differentiation skeletal muscle tissue development positive regulation of transcription by RNA polymerase II transcription by RNA polymerase II positive regulation of muscle cell differentiation cellular response to tumor necrosis factor positive regulation of snRNA transcription by RNA polymerase II Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4654 17927 Ensembl ENSG00000129152 ENSMUSG00000009471 UniProt P15172 P10085 RefSeq (mRNA) NM_002478 NM_010866 RefSeq (protein) NP_002469 NP_034996 Location (UCSC) Chr 11: 17.72 – 17.72 Mb Chr 7: 46.03 – 46.03 Mb PubMed search [3] [4]
Wikidata
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MyoD, also known as myoblast determination protein 1,^[5] is a protein in animals that plays a major role in regulating muscle differentiation. MyoD, which was discovered in the laboratory of Harold M. Weintraub,^[6] belongs to a family of proteins known as myogenic regulatory factors (MRFs).^[7] These bHLH (basic helix loop helix) transcription factors act sequentially in myogenic differentiation. Vertebrate MRF family members include MyoD1, Myf5, myogenin, and MRF4 (Myf6). In non-vertebrate animals, a single MyoD protein is typically found.

MyoD is one of the earliest markers of myogenic commitment. MyoD is expressed at extremely low and essentially undetectable levels in quiescent satellite cells, but expression of MyoD is activated in response to exercise or muscle tissue damage. The effect of MyoD on satellite cells is dose-dependent; high MyoD expression represses cell renewal, promotes terminal differentiation and can induce apoptosis. Although MyoD marks myoblast commitment, muscle development is not dramatically ablated in mouse mutants lacking the MyoD gene. This is likely due to functional redundancy from Myf5 and/or Mrf4. Nevertheless, the combination of MyoD and Myf5 is vital to the success of myogenesis.^[8][9]