MYOG_MOUSE
ID MYOG_MOUSE Reviewed; 224 AA.
AC P12979;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Myogenin;
DE AltName: Full=MYOD1-related protein;
GN Name=Myog;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Muscle;
RX PubMed=2473006; DOI=10.1101/gad.3.5.628;
RA Edmondson D.G., Olson E.N.;
RT "A gene with homology to the myc similarity region of MyoD1 is expressed
RT during myogenesis and is sufficient to activate the muscle differentiation
RT program.";
RL Genes Dev. 3:628-640(1989).
RN [2]
RP ERRATUM OF PUBMED:2473006.
RX PubMed=2172083; DOI=10.1101/gad.4.8.1450;
RA Edmondson D.G., Olson E.N.;
RL Genes Dev. 4:1450-1450(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1324403; DOI=10.1128/mcb.12.9.3665-3677.1992;
RA Edmondson D.G., Cheng T.C., Cserjesi P., Chakraborty T., Olson E.N.;
RT "Analysis of the myogenin promoter reveals an indirect pathway for positive
RT autoregulation mediated by the muscle-specific enhancer factor MEF-2.";
RL Mol. Cell. Biol. 12:3665-3677(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2168405; DOI=10.1016/s0021-9258(18)77244-x;
RA Fujisawa-Sehara A., Nabeshima Y., Hosoda Y., Obinata T., Nabeshima Y.;
RT "Myogenin contains two domains conserved among myogenic factors.";
RL J. Biol. Chem. 265:15219-15223(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=2552320; DOI=10.1038/341303a0;
RA Sassoon D., Lyons G., Wright W.E., Lin V., Lassar A., Weintraub H.,
RA Buckingham M.;
RT "Expression of two myogenic regulatory factors myogenin and MyoD1 during
RT mouse embryogenesis.";
RL Nature 341:303-307(1989).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=1705035; DOI=10.1073/pnas.88.4.1349;
RA Eftimie R., Brenner H.R., Buonanno A.;
RT "Myogenin and MyoD join a family of skeletal muscle genes regulated by
RT electrical activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:1349-1353(1991).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8393145; DOI=10.1038/364501a0;
RA Hasty P., Bradley A., Morris J.H., Edmondson D.G., Venuti J.M., Olson E.N.,
RA Klein W.H.;
RT "Muscle deficiency and neonatal death in mice with a targeted mutation in
RT the myogenin gene.";
RL Nature 364:501-506(1993).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8393146; DOI=10.1038/364532a0;
RA Nabeshima Y., Hanaoka K., Hayasaka M., Esumi E., Li S., Nonaka I.,
RA Nabeshima Y.;
RT "Myogenin gene disruption results in perinatal lethality because of severe
RT muscle defect.";
RL Nature 364:532-535(1993).
RN [10]
RP DEVELOPMENTAL STAGE.
RX PubMed=7929574; DOI=10.1083/jcb.127.1.95;
RA Smith T.H., Kachinsky A.M., Miller J.B.;
RT "Somite subdomains, muscle cell origins, and the four muscle regulatory
RT factor proteins.";
RL J. Cell Biol. 127:95-105(1994).
RN [11]
RP SUBUNIT.
RX PubMed=12196028; DOI=10.1021/bi025528q;
RA Maleki S.J., Royer C.A., Hurlburt B.K.;
RT "Analysis of the DNA-binding properties of MyoD, myogenin, and E12 by
RT fluorescence anisotropy.";
RL Biochemistry 41:10888-10894(2002).
RN [12]
RP FUNCTION, AND PROMOTER BINDING.
RX PubMed=15706034; DOI=10.1101/gad.1281105;
RA Blais A., Tsikitis M., Acosta-Alvear D., Sharan R., Kluger Y.,
RA Dynlacht B.D.;
RT "An initial blueprint for myogenic differentiation.";
RL Genes Dev. 19:553-569(2005).
RN [13]
RP FUNCTION, AND CONDITIONAL KNOCKOUT IN MUSCLE CELLS.
RX PubMed=16407395; DOI=10.1242/dev.02249;
RA Knapp J.R., Davie J.K., Myer A., Meadows E., Olson E.N., Klein W.H.;
RT "Loss of myogenin in postnatal life leads to normal skeletal muscle but
RT reduced body size.";
RL Development 133:601-610(2006).
RN [14]
RP FUNCTION, INTERACTION WITH SMARCA4, AND SUBCELLULAR LOCATION.
RX PubMed=16424906; DOI=10.1038/sj.emboj.7600943;
RA Ohkawa Y., Marfella C.G., Imbalzano A.N.;
RT "Skeletal muscle specification by myogenin and Mef2D via the SWI/SNF ATPase
RT Brg1.";
RL EMBO J. 25:490-501(2006).
RN [15]
RP FUNCTION.
RX PubMed=16437161; DOI=10.1038/sj.emboj.7600958;
RA Cao Y., Kumar R.M., Penn B.H., Berkes C.A., Kooperberg C., Boyer L.A.,
RA Young R.A., Tapscott S.J.;
RT "Global and gene-specific analyses show distinct roles for Myod and Myog at
RT a common set of promoters.";
RL EMBO J. 25:502-511(2006).
RN [16]
RP FUNCTION, CONDITIONAL KNOCKOUT IN MUSCLE CELLS, INDUCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=21465538; DOI=10.1002/jcb.23136;
RA Macpherson P.C., Wang X., Goldman D.;
RT "Myogenin regulates denervation-dependent muscle atrophy in mouse soleus
RT muscle.";
RL J. Cell. Biochem. 112:2149-2159(2011).
RN [17]
RP FUNCTION, PROMOTER BINDING, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=21798092; DOI=10.1186/2044-5040-1-14;
RA Londhe P., Davie J.K.;
RT "Sequential association of myogenic regulatory factors and E proteins at
RT muscle-specific genes.";
RL Skelet. Muscle 1:14-14(2011).
RN [18]
RP FUNCTION, AND INDUCTION.
RX PubMed=22847234; DOI=10.1093/jmcb/mjs045;
RA Liu Q.C., Zha X.H., Faralli H., Yin H., Louis-Jeune C., Perdiguero E.,
RA Pranckeviciene E., Munoz-Canoves P., Rudnicki M.A., Brand M.,
RA Perez-Iratxeta C., Dilworth F.J.;
RT "Comparative expression profiling identifies differential roles for
RT Myogenin and p38alpha MAPK signaling in myogenesis.";
RL J. Mol. Cell Biol. 4:386-397(2012).
RN [19]
RP FUNCTION IN MUSCLE DEDIFFERENTIATION INHIBITION.
RX PubMed=22235349; DOI=10.1371/journal.pone.0029896;
RA Mastroyiannopoulos N.P., Nicolaou P., Anayasa M., Uney J.B.,
RA Phylactou L.A.;
RT "Down-regulation of myogenin can reverse terminal muscle cell
RT differentiation.";
RL PLoS ONE 7:E29896-E29896(2012).
RN [20]
RP FUNCTION, AND INTERACTION WITH SSRP1 AND SUPT16H.
RX PubMed=23364797; DOI=10.1074/jbc.m112.426718;
RA Lolis A.A., Londhe P., Beggs B.C., Byrum S.D., Tackett A.J., Davie J.K.;
RT "Myogenin recruits the histone chaperone facilitates chromatin
RT transcription (FACT) to promote nucleosome disassembly at muscle-specific
RT genes.";
RL J. Biol. Chem. 288:7676-7687(2013).
CC -!- FUNCTION: Acts as a transcriptional activator that promotes
CC transcription of muscle-specific target genes and plays a role in
CC muscle differentiation, cell cycle exit and muscle atrophy. Essential
CC for the development of functional embryonic skeletal fiber muscle
CC differentiation. However is dispensable for postnatal skeletal muscle
CC growth; phosphorylation by CAMK2G inhibits its transcriptional activity
CC in respons to muscle activity. Required for the recruitment of the FACT
CC complex to muscle-specific promoter regions, thus promoting gene
CC expression initiation. During terminal myoblast differentiation, plays
CC a role as a strong activator of transcription at loci with an open
CC chromatin structure previously initiated by MYOD1. Together with MYF5
CC and MYOD1, co-occupies muscle-specific gene promoter core regions
CC during myogenesis. Cooperates also with myocyte-specific enhancer
CC factor MEF2D and BRG1-dependent recruitment of SWI/SNF chromatin-
CC remodeling enzymes to alter chromatin structure at myogenic late gene
CC promoters. Facilitates cell cycle exit during terminal muscle
CC differentiation through the up-regulation of miR-20a expression, which
CC in turn represses genes involved in cell cycle progression. Binds to
CC the E-box containing (E1) promoter region of the miR-20a gene. Plays
CC also a role in preventing reversal of muscle cell differentiation.
CC Contributes to the atrophy-related gene expression in adult denervated
CC muscles. Induces fibroblasts to differentiate into myoblasts.
CC {ECO:0000269|PubMed:15706034, ECO:0000269|PubMed:16407395,
CC ECO:0000269|PubMed:16424906, ECO:0000269|PubMed:16437161,
CC ECO:0000269|PubMed:21465538, ECO:0000269|PubMed:21798092,
CC ECO:0000269|PubMed:22235349, ECO:0000269|PubMed:22847234,
CC ECO:0000269|PubMed:23364797, ECO:0000269|PubMed:8393145,
CC ECO:0000269|PubMed:8393146}.
CC -!- SUBUNIT: Homodimer and heterodimer with E12; heterodimerization
CC enhances MYOG DNA-binding and transcriptional activities. Interacts
CC with SMARCA4/BRG1/BAF190A. Interacts (via C-terminal region) with SSRP1
CC and SUPT16H; the interaction is indicative of an interaction with the
CC FACT complex. nteracts with CSRP3 (By similarity).
CC {ECO:0000250|UniProtKB:P20428, ECO:0000269|PubMed:12196028,
CC ECO:0000269|PubMed:16424906, ECO:0000269|PubMed:23364797}.
CC -!- INTERACTION:
CC P12979; Q60929: Mef2a; NbExp=2; IntAct=EBI-7132875, EBI-2639094;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:16424906}. Note=Recruited to late myogenic gene
CC promoter regulatory sequences with SMARCA4/BRG1/BAF190A and SWI/SNF
CC chromatin-remodeling enzymes to promote chromatin-remodeling and
CC transcription initiation in developing embryos.
CC -!- TISSUE SPECIFICITY: Expressed in myoblast cells. Expressed weakly in
CC myotubes (at protein level). Expressed strongly in denervated muscles
CC and in satellite cells isolated from denervated muscles. Expressed
CC weakly in innervated muscle and in satellite cells isolated from
CC innervated muscles. {ECO:0000269|PubMed:21465538,
CC ECO:0000269|PubMed:21798092}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the myotome of the somites at 8.5
CC dpc, onward (at protein level). Expressed in proximal region of both
CC the hindlimb and the forelimb at 11.5 dpc, onward. Expressed during
CC muscle maturation between 15 and 17 dpc and decreases thereafter. Not
CC detected within the heart. {ECO:0000269|PubMed:1705035,
CC ECO:0000269|PubMed:2552320, ECO:0000269|PubMed:7929574}.
CC -!- INDUCTION: Up-regulated in denervated muscles (at protein level). Up-
CC regulated during myogenesis in the embryo and in cell culture models of
CC myogenic differentiation via the p38 MAPK signaling pathway.
CC {ECO:0000269|PubMed:21465538, ECO:0000269|PubMed:21798092,
CC ECO:0000269|PubMed:22847234}.
CC -!- PTM: Phosphorylated by CAMK2G on threonine and serine amino acids in a
CC muscle activity-dependent manner. Phosphorylation of Thr-87 impairs
CC both DNA-binding and trans-activation functions in contracting muscles
CC (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Display normal myoblast formation during
CC embryogenesis, but show perinatal lethality because of a deficiency
CC during the later stages of skeletal muscle fiber formation. Show no
CC abnormalities for smooth muscles and cardiocytes differentiation.
CC Conditional mutant with expression abrogated in muscle cells from 15.5
CC or 17.5 dpc are viable, fertil and exhibit no noticeable muscle growth
CC and reduction of myofiber diameter defects but show smaller body size
CC and mass. Conditional mutant in muscle cells of denervated hindlimb
CC muscles show an inhibition of the denervation-dependent reductions in
CC mass, force and atrophy of slow fiber-type soleus muscles, without
CC increased in satellite cell proliferation and fusion.
CC {ECO:0000269|PubMed:8393145, ECO:0000269|PubMed:8393146}.
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DR EMBL; M95800; AAB59676.1; -; Genomic_DNA.
DR EMBL; X15784; CAA33785.1; ALT_SEQ; mRNA.
DR EMBL; D90156; BAA14187.1; -; mRNA.
DR EMBL; BC048683; AAH48683.1; -; mRNA.
DR EMBL; BC068019; AAH68019.1; -; mRNA.
DR CCDS; CCDS15306.1; -.
DR PIR; A35882; A36675.
DR RefSeq; NP_112466.1; NM_031189.2.
DR AlphaFoldDB; P12979; -.
DR SMR; P12979; -.
DR BioGRID; 201674; 7.
DR CORUM; P12979; -.
DR DIP; DIP-29976N; -.
DR IntAct; P12979; 6.
DR MINT; P12979; -.
DR STRING; 10090.ENSMUSP00000027730; -.
DR iPTMnet; P12979; -.
DR PhosphoSitePlus; P12979; -.
DR EPD; P12979; -.
DR PaxDb; P12979; -.
DR PRIDE; P12979; -.
DR ABCD; P12979; 1 sequenced antibody.
DR Antibodypedia; 20659; 1098 antibodies from 41 providers.
DR DNASU; 17928; -.
DR Ensembl; ENSMUST00000027730; ENSMUSP00000027730; ENSMUSG00000026459.
DR GeneID; 17928; -.
DR KEGG; mmu:17928; -.
DR UCSC; uc007crl.2; mouse.
DR CTD; 4656; -.
DR MGI; MGI:97276; Myog.
DR VEuPathDB; HostDB:ENSMUSG00000026459; -.
DR eggNOG; KOG3960; Eukaryota.
DR GeneTree; ENSGT00950000182959; -.
DR HOGENOM; CLU_100258_0_0_1; -.
DR InParanoid; P12979; -.
DR OMA; PWACKIC; -.
DR OrthoDB; 1471470at2759; -.
DR PhylomeDB; P12979; -.
DR TreeFam; TF316344; -.
DR Reactome; R-MMU-525793; Myogenesis.
DR BioGRID-ORCS; 17928; 0 hits in 71 CRISPR screens.
DR PRO; PR:P12979; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P12979; protein.
DR Bgee; ENSMUSG00000026459; Expressed in myotome and 111 other tissues.
DR Genevisible; P12979; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
DR GO; GO:0071285; P:cellular response to lithium ion; IDA:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:MGI.
DR GO; GO:0042692; P:muscle cell differentiation; IDA:ARUK-UCL.
DR GO; GO:0007517; P:muscle organ development; IGI:MGI.
DR GO; GO:0014902; P:myotube differentiation; IGI:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0045820; P:negative regulation of glycolytic process; ISO:MGI.
DR GO; GO:0001503; P:ossification; IMP:MGI.
DR GO; GO:0014737; P:positive regulation of muscle atrophy; IMP:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IDA:UniProtKB.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; IDA:UniProtKB.
DR GO; GO:1903862; P:positive regulation of oxidative phosphorylation; ISO:MGI.
DR GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:1901739; P:regulation of myoblast fusion; IMP:UniProtKB.
DR GO; GO:0014842; P:regulation of skeletal muscle satellite cell proliferation; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; IDA:UniProtKB.
DR GO; GO:0014878; P:response to electrical stimulus involved in regulation of muscle adaptation; ISS:UniProtKB.
DR GO; GO:0014873; P:response to muscle activity involved in regulation of muscle adaptation; ISS:UniProtKB.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IBA:GO_Central.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
DR GO; GO:0007519; P:skeletal muscle tissue development; IDA:MGI.
DR GO; GO:0014891; P:striated muscle atrophy; IMP:UniProtKB.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR002546; MyoD_N.
DR InterPro; IPR039704; Myogenic_factor.
DR PANTHER; PTHR11534; PTHR11534; 1.
DR Pfam; PF01586; Basic; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00520; BASIC; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Activator; Cell cycle; Developmental protein; Differentiation; DNA-binding;
KW Myogenesis; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..224
FT /note="Myogenin"
FT /id="PRO_0000127376"
FT DOMAIN 81..132
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT MOD_RES 77
FT /note="Phosphoserine; by CaMK2G"
FT /evidence="ECO:0000250|UniProtKB:P20428"
FT MOD_RES 79
FT /note="Phosphoserine; by CaMK2G"
FT /evidence="ECO:0000250|UniProtKB:P20428"
FT MOD_RES 87
FT /note="Phosphothreonine; by CaMK2G"
FT /evidence="ECO:0000250|UniProtKB:P20428"
SQ SEQUENCE 224 AA; 25203 MW; CC7352C1EDF9D3D8 CRC64;
MELYETSPYF YQEPHFYDGE NYLPVHLQGF EPPGYERTEL SLSPEARGPL EEKGLGTPEH
CPGQCLPWAC KVCKRKSVSV DRRRAATLRE KRRLKKVNEA FEALKRSTLL NPNQRLPKVE
ILRSAIQYIE RLQALLSSLN QEERDLRYRG GGGPQPMVPS ECNSHSASCS PEWGNALEFG
PNPGDHLLAA DPTDAHNLHS LTSIVDSITV EDMSVAFPDE TMPN
