MYOG_RAT
ID MYOG_RAT Reviewed; 287 AA.
AC P20428;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Myogenin;
GN Name=Myog;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2537150; DOI=10.1016/0092-8674(89)90583-7;
RA Wright W.E., Sassoon D.A., Lin V.K.;
RT "Myogenin, a factor regulating myogenesis, has a domain homologous to
RT MyoD.";
RL Cell 56:607-617(1989).
RN [2]
RP INDUCTION.
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 [3]
RP INTERACTION WITH CSRP3.
RX PubMed=9234731; DOI=10.1128/mcb.17.8.4750;
RA Kong Y., Flick M.J., Kudla A.J., Konieczny S.F.;
RT "Muscle LIM protein promotes myogenesis by enhancing the activity of
RT MyoD.";
RL Mol. Cell. Biol. 17:4750-4760(1997).
RN [4]
RP FUNCTION, PHOSPHORYLATION AT SER-77; SER-79 AND THR-87, DNA-BINDING, AND
RP MUTAGENESIS OF SER-77; SER-79 AND THR-87.
RX PubMed=14751541; DOI=10.1016/j.cellsig.2003.09.006;
RA Tang H., Macpherson P., Argetsinger L.S., Cieslak D., Suhr S.T.,
RA Carter-Su C., Goldman D.;
RT "CaM kinase II-dependent phosphorylation of myogenin contributes to
RT activity-dependent suppression of nAChR gene expression in developing rat
RT myotubes.";
RL Cell. Signal. 16:551-563(2004).
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:14751541}.
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 (By similarity). Interacts with CSRP3. {ECO:0000250,
CC ECO:0000269|PubMed:9234731}.
CC -!- SUBCELLULAR LOCATION: Nucleus. 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. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in muscle (at protein level).
CC -!- INDUCTION: Up-regulated in denerved muscles cells. Down-regulated in
CC soleus muscle in an electrical activity-dependent manner.
CC {ECO:0000269|PubMed:1705035}.
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 {ECO:0000269|PubMed:14751541}.
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DR EMBL; M24393; AAA41662.1; -; mRNA.
DR PIR; A31876; A31876.
DR RefSeq; NP_058811.2; NM_017115.2.
DR AlphaFoldDB; P20428; -.
DR SMR; P20428; -.
DR DIP; DIP-52N; -.
DR STRING; 10116.ENSRNOP00000039817; -.
DR iPTMnet; P20428; -.
DR PaxDb; P20428; -.
DR PRIDE; P20428; -.
DR GeneID; 29148; -.
DR KEGG; rno:29148; -.
DR UCSC; RGD:620432; rat.
DR CTD; 4656; -.
DR RGD; 620432; Myog.
DR eggNOG; KOG3960; Eukaryota.
DR HOGENOM; CLU_969646_0_0_1; -.
DR InParanoid; P20428; -.
DR OMA; KPCPTEI; -.
DR OrthoDB; 1471470at2759; -.
DR PhylomeDB; P20428; -.
DR TreeFam; TF316344; -.
DR Reactome; R-RNO-525793; Myogenesis.
DR PRO; PR:P20428; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000030743; Expressed in quadriceps femoris and 3 other tissues.
DR ExpressionAtlas; P20428; baseline and differential.
DR Genevisible; P20428; RN.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS: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; ISS: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:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISS:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:RGD.
DR GO; GO:0071285; P:cellular response to lithium ion; ISO:RGD.
DR GO; GO:0071259; P:cellular response to magnetism; IEP:RGD.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:RGD.
DR GO; GO:0042692; P:muscle cell differentiation; ISO:RGD.
DR GO; GO:0007517; P:muscle organ development; ISO:RGD.
DR GO; GO:0045445; P:myoblast differentiation; IEP:RGD.
DR GO; GO:0014902; P:myotube differentiation; IMP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045820; P:negative regulation of glycolytic process; IDA:RGD.
DR GO; GO:0001503; P:ossification; ISO:RGD.
DR GO; GO:0014737; P:positive regulation of muscle atrophy; ISS:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; ISS:UniProtKB.
DR GO; GO:1903862; P:positive regulation of oxidative phosphorylation; IDA:RGD.
DR GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; ISS: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; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:1901739; P:regulation of myoblast fusion; ISS:UniProtKB.
DR GO; GO:0014842; P:regulation of skeletal muscle satellite cell proliferation; ISS: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; ISS:UniProtKB.
DR GO; GO:0014878; P:response to electrical stimulus involved in regulation of muscle adaptation; IDA:UniProtKB.
DR GO; GO:0009629; P:response to gravity; IEP:RGD.
DR GO; GO:0014850; P:response to muscle activity; IEP:RGD.
DR GO; GO:0014873; P:response to muscle activity involved in regulation of muscle adaptation; IDA:UniProtKB.
DR GO; GO:0014732; P:skeletal muscle atrophy; IEP:RGD.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IBA:GO_Central.
DR GO; GO:0048741; P:skeletal muscle fiber development; ISO:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:RGD.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IEP:RGD.
DR GO; GO:0014891; P:striated muscle atrophy; ISS: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..287
FT /note="Myogenin"
FT /id="PRO_0000127378"
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:0000269|PubMed:14751541"
FT MOD_RES 79
FT /note="Phosphoserine; by CaMK2G"
FT /evidence="ECO:0000269|PubMed:14751541"
FT MOD_RES 87
FT /note="Phosphothreonine; by CaMK2G"
FT /evidence="ECO:0000269|PubMed:14751541"
FT MUTAGEN 77
FT /note="S->A: Reduces phosphorylation."
FT /evidence="ECO:0000269|PubMed:14751541"
FT MUTAGEN 79
FT /note="S->A: Reduces phosphorylation."
FT /evidence="ECO:0000269|PubMed:14751541"
FT MUTAGEN 87
FT /note="T->A: Reduces phosphorylation and inhibits DNA-
FT binding and transcriptional activation."
FT /evidence="ECO:0000269|PubMed:14751541"
SQ SEQUENCE 287 AA; 32503 MW; BE454E59B1464B40 CRC64;
MELYETSPYF YQEPHFYDGE NYLPVHLQGF EPPGYERTEL SLSPEARGPL EEKGLGTPEH
CPGQCLPWAC KVCKRKSVSV DRRRAATLRE KRRLKKVNEA FEALKRSTLL NPNQRLPKVE
ILRSAIQYIE RLQALLSSLN QEERDLRYRG GGGPSRWYPV NATPTAPPAV RSGAMHWSLV
PTQEIICSQL TLQVPTTCTP LRPSWTASRW RICLSPSQMK PCPTEIVCQA GCAWEPLSWC
QTPPLLQQGP FKWGCPGAQK TALGCHKPDY PPSIHIRLTP SPAREFN
