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Myogenin (MYOD1-related protein)

 MYOG_MOUSE              Reviewed;         224 AA.
P12979;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 2.
25-OCT-2017, entry version 146.
RecName: Full=Myogenin;
AltName: Full=MYOD1-related protein;
Name=Myog;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Muscle;
PubMed=2473006; DOI=10.1101/gad.3.5.628;
Edmondson D.G., Olson E.N.;
"A gene with homology to the myc similarity region of MyoD1 is
expressed during myogenesis and is sufficient to activate the muscle
differentiation program.";
Genes Dev. 3:628-640(1989).
[2]
ERRATUM.
PubMed=2172083; DOI=10.1101/gad.4.8.1450;
Edmondson D.G., Olson E.N.;
Genes Dev. 4:1450-1450(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1324403; DOI=10.1128/MCB.12.9.3665;
Edmondson D.G., Cheng T.C., Cserjesi P., Chakraborty T., Olson E.N.;
"Analysis of the myogenin promoter reveals an indirect pathway for
positive autoregulation mediated by the muscle-specific enhancer
factor MEF-2.";
Mol. Cell. Biol. 12:3665-3677(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2168405;
Fujisawa-Sehara A., Nabeshima Y., Hosoda Y., Obinata T., Nabeshima Y.;
"Myogenin contains two domains conserved among myogenic factors.";
J. Biol. Chem. 265:15219-15223(1990).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Limb;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
DEVELOPMENTAL STAGE.
PubMed=2552320; DOI=10.1038/341303a0;
Sassoon D., Lyons G., Wright W.E., Lin V., Lassar A., Weintraub H.,
Buckingham M.;
"Expression of two myogenic regulatory factors myogenin and MyoD1
during mouse embryogenesis.";
Nature 341:303-307(1989).
[7]
DEVELOPMENTAL STAGE.
PubMed=1705035; DOI=10.1073/pnas.88.4.1349;
Eftimie R., Brenner H.R., Buonanno A.;
"Myogenin and MyoD join a family of skeletal muscle genes regulated by
electrical activity.";
Proc. Natl. Acad. Sci. U.S.A. 88:1349-1353(1991).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=8393145; DOI=10.1038/364501a0;
Hasty P., Bradley A., Morris J.H., Edmondson D.G., Venuti J.M.,
Olson E.N., Klein W.H.;
"Muscle deficiency and neonatal death in mice with a targeted mutation
in the myogenin gene.";
Nature 364:501-506(1993).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=8393146; DOI=10.1038/364532a0;
Nabeshima Y., Hanaoka K., Hayasaka M., Esumi E., Li S., Nonaka I.,
Nabeshima Y.;
"Myogenin gene disruption results in perinatal lethality because of
severe muscle defect.";
Nature 364:532-535(1993).
[10]
DEVELOPMENTAL STAGE.
PubMed=7929574; DOI=10.1083/jcb.127.1.95;
Smith T.H., Kachinsky A.M., Miller J.B.;
"Somite subdomains, muscle cell origins, and the four muscle
regulatory factor proteins.";
J. Cell Biol. 127:95-105(1994).
[11]
SUBUNIT.
PubMed=12196028; DOI=10.1021/bi025528q;
Maleki S.J., Royer C.A., Hurlburt B.K.;
"Analysis of the DNA-binding properties of MyoD, myogenin, and E12 by
fluorescence anisotropy.";
Biochemistry 41:10888-10894(2002).
[12]
FUNCTION, AND PROMOTER BINDING.
PubMed=15706034; DOI=10.1101/gad.1281105;
Blais A., Tsikitis M., Acosta-Alvear D., Sharan R., Kluger Y.,
Dynlacht B.D.;
"An initial blueprint for myogenic differentiation.";
Genes Dev. 19:553-569(2005).
[13]
FUNCTION, AND CONDITIONAL KNOCKOUT IN MUSCLE CELLS.
PubMed=16407395; DOI=10.1242/dev.02249;
Knapp J.R., Davie J.K., Myer A., Meadows E., Olson E.N., Klein W.H.;
"Loss of myogenin in postnatal life leads to normal skeletal muscle
but reduced body size.";
Development 133:601-610(2006).
[14]
FUNCTION, INTERACTION WITH SMARCA4, AND SUBCELLULAR LOCATION.
PubMed=16424906; DOI=10.1038/sj.emboj.7600943;
Ohkawa Y., Marfella C.G., Imbalzano A.N.;
"Skeletal muscle specification by myogenin and Mef2D via the SWI/SNF
ATPase Brg1.";
EMBO J. 25:490-501(2006).
[15]
FUNCTION.
PubMed=16437161; DOI=10.1038/sj.emboj.7600958;
Cao Y., Kumar R.M., Penn B.H., Berkes C.A., Kooperberg C., Boyer L.A.,
Young R.A., Tapscott S.J.;
"Global and gene-specific analyses show distinct roles for Myod and
Myog at a common set of promoters.";
EMBO J. 25:502-511(2006).
[16]
FUNCTION, CONDITIONAL KNOCKOUT IN MUSCLE CELLS, INDUCTION, AND TISSUE
SPECIFICITY.
PubMed=21465538; DOI=10.1002/jcb.23136;
Macpherson P.C., Wang X., Goldman D.;
"Myogenin regulates denervation-dependent muscle atrophy in mouse
soleus muscle.";
J. Cell. Biochem. 112:2149-2159(2011).
[17]
FUNCTION, PROMOTER BINDING, INDUCTION, AND TISSUE SPECIFICITY.
PubMed=21798092; DOI=10.1186/2044-5040-1-14;
Londhe P., Davie J.K.;
"Sequential association of myogenic regulatory factors and E proteins
at muscle-specific genes.";
Skelet. Muscle 1:14-14(2011).
[18]
FUNCTION, AND INDUCTION.
PubMed=22847234; DOI=10.1093/jmcb/mjs045;
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.;
"Comparative expression profiling identifies differential roles for
Myogenin and p38alpha MAPK signaling in myogenesis.";
J. Mol. Cell Biol. 4:386-397(2012).
[19]
FUNCTION IN MUSCLE DEDIFFERENTIATION INHIBITION.
PubMed=22235349; DOI=10.1371/journal.pone.0029896;
Mastroyiannopoulos N.P., Nicolaou P., Anayasa M., Uney J.B.,
Phylactou L.A.;
"Down-regulation of myogenin can reverse terminal muscle cell
differentiation.";
PLoS ONE 7:E29896-E29896(2012).
[20]
FUNCTION, AND INTERACTION WITH SSRP1 AND SUPT16H.
PubMed=23364797; DOI=10.1074/jbc.M112.426718;
Lolis A.A., Londhe P., Beggs B.C., Byrum S.D., Tackett A.J.,
Davie J.K.;
"Myogenin recruits the histone chaperone facilitates chromatin
transcription (FACT) to promote nucleosome disassembly at muscle-
specific genes.";
J. Biol. Chem. 288:7676-7687(2013).
-!- 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. {ECO:0000269|PubMed:15706034,
ECO:0000269|PubMed:16407395, ECO:0000269|PubMed:16424906,
ECO:0000269|PubMed:16437161, ECO:0000269|PubMed:21465538,
ECO:0000269|PubMed:21798092, ECO:0000269|PubMed:22235349,
ECO:0000269|PubMed:22847234, ECO:0000269|PubMed:23364797,
ECO:0000269|PubMed:8393145, ECO:0000269|PubMed:8393146}.
-!- SUBUNIT: 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. nteracts with CSRP3 (By
similarity). {ECO:0000250|UniProtKB:P20428,
ECO:0000269|PubMed:12196028, ECO:0000269|PubMed:16424906,
ECO:0000269|PubMed:23364797}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00981, ECO:0000269|PubMed:16424906}. 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.
-!- 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. {ECO:0000269|PubMed:21465538,
ECO:0000269|PubMed:21798092}.
-!- 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.
{ECO:0000269|PubMed:1705035, ECO:0000269|PubMed:2552320,
ECO:0000269|PubMed:7929574}.
-!- 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. {ECO:0000269|PubMed:21465538,
ECO:0000269|PubMed:21798092, ECO:0000269|PubMed:22847234}.
-!- PTM: 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). {ECO:0000250}.
-!- 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.
{ECO:0000269|PubMed:8393145, ECO:0000269|PubMed:8393146}.
-----------------------------------------------------------------------
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EMBL; M95800; AAB59676.1; -; Genomic_DNA.
EMBL; X15784; CAA33785.1; ALT_SEQ; mRNA.
EMBL; D90156; BAA14187.1; -; mRNA.
EMBL; BC048683; AAH48683.1; -; mRNA.
EMBL; BC068019; AAH68019.1; -; mRNA.
CCDS; CCDS15306.1; -.
PIR; A35882; A36675.
RefSeq; NP_112466.1; NM_031189.2.
UniGene; Mm.16528; -.
ProteinModelPortal; P12979; -.
SMR; P12979; -.
BioGrid; 201674; 8.
CORUM; P12979; -.
DIP; DIP-29976N; -.
IntAct; P12979; 5.
MINT; MINT-1958829; -.
STRING; 10090.ENSMUSP00000027730; -.
iPTMnet; P12979; -.
PhosphoSitePlus; P12979; -.
EPD; P12979; -.
PaxDb; P12979; -.
PRIDE; P12979; -.
Ensembl; ENSMUST00000027730; ENSMUSP00000027730; ENSMUSG00000026459.
GeneID; 17928; -.
KEGG; mmu:17928; -.
UCSC; uc007crl.2; mouse.
CTD; 4656; -.
MGI; MGI:97276; Myog.
eggNOG; KOG3960; Eukaryota.
eggNOG; ENOG4111SED; LUCA.
GeneTree; ENSGT00530000063004; -.
HOGENOM; HOG000234799; -.
HOVERGEN; HBG006429; -.
InParanoid; P12979; -.
KO; K18483; -.
OMA; PNPGDHL; -.
OrthoDB; EOG091G0GKD; -.
PhylomeDB; P12979; -.
TreeFam; TF316344; -.
Reactome; R-MMU-375170; CDO in myogenesis.
PRO; PR:P12979; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026459; -.
CleanEx; MM_MYOG; -.
Genevisible; P12979; MM.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0000987; F:core promoter proximal region sequence-specific DNA binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0070888; F:E-box binding; IDA:BHF-UCL.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; TAS:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:MGI.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
GO; GO:0071285; P:cellular response to lithium ion; IDA:MGI.
GO; GO:0071259; P:cellular response to magnetism; IEA:Ensembl.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0042789; P:mRNA transcription from RNA polymerase II promoter; IC:BHF-UCL.
GO; GO:0007517; P:muscle organ development; IGI:MGI.
GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
GO; GO:0014902; P:myotube differentiation; IGI:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0045820; P:negative regulation of glycolytic process; IEA:Ensembl.
GO; GO:0001503; P:ossification; IMP:MGI.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IDA:UniProtKB.
GO; GO:0014737; P:positive regulation of muscle atrophy; IMP:UniProtKB.
GO; GO:0045663; P:positive regulation of myoblast differentiation; IDA:UniProtKB.
GO; GO:1901741; P:positive regulation of myoblast fusion; IBA:GO_Central.
GO; GO:0010831; P:positive regulation of myotube differentiation; IDA:UniProtKB.
GO; GO:1903862; P:positive regulation of oxidative phosphorylation; IEA:Ensembl.
GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:1901739; P:regulation of myoblast fusion; IMP:UniProtKB.
GO; GO:0014842; P:regulation of skeletal muscle satellite cell proliferation; IMP:UniProtKB.
GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; IDA:UniProtKB.
GO; GO:0014878; P:response to electrical stimulus involved in regulation of muscle adaptation; ISS:UniProtKB.
GO; GO:0009629; P:response to gravity; IEA:Ensembl.
GO; GO:0014873; P:response to muscle activity involved in regulation of muscle adaptation; ISS:UniProtKB.
GO; GO:0014732; P:skeletal muscle atrophy; IEA:Ensembl.
GO; GO:0035914; P:skeletal muscle cell differentiation; IBA:GO_Central.
GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
GO; GO:0007519; P:skeletal muscle tissue development; IDA:MGI.
GO; GO:0043403; P:skeletal muscle tissue regeneration; IEA:Ensembl.
GO; GO:0014891; P:striated muscle atrophy; IMP:UniProtKB.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR002546; Basic.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
Pfam; PF01586; Basic; 1.
Pfam; PF00010; HLH; 1.
SMART; SM00520; BASIC; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
Activator; Cell cycle; Complete proteome; Developmental protein;
Differentiation; DNA-binding; Myogenesis; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 224 Myogenin.
/FTId=PRO_0000127376.
DOMAIN 81 132 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
MOD_RES 77 77 Phosphoserine; by CaMK2G.
{ECO:0000250|UniProtKB:P20428}.
MOD_RES 79 79 Phosphoserine; by CaMK2G.
{ECO:0000250|UniProtKB:P20428}.
MOD_RES 87 87 Phosphothreonine; by CaMK2G.
{ECO:0000250|UniProtKB:P20428}.
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


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