MYOG_BOVIN
ID MYOG_BOVIN Reviewed; 224 AA.
AC Q7YS81; A7L032; Q148H1; Q1MW35;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Myogenin;
GN Name=MYOG;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RA Muroya S., Nakajima I., Chikuni K.;
RT "Effect of myogenic regulatory factor siRNAs on differentiation of bovine
RT skeletal muscle cells.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Japanese black; TISSUE=Skeletal muscle;
RA Shibata M., Matsumoto K., Aikawa K., Muramoto T., Fujimura S., Kadowaki M.;
RT "Gene expression of MRFs during development of skeletal muscle in Japanese
RT black cattle.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zhang Y.M., Li J., Zhong J.C.;
RT "Cloning and sequence analysis of the MYOG gene in cattle from China.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
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. Interacts with CSRP3 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P20428}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC Note=Recruited to late myogenic gene promoter regulatory sequences with
CC SMARCA4/BRG1/BAF190A and SWI/SNF chromatin-remodeling enzymes to
CC promote chromatin-remodeling and transcription initiation in developing
CC embryos. {ECO:0000250}.
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}.
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DR EMBL; AB110600; BAC76803.1; -; mRNA.
DR EMBL; AB257560; BAE93440.1; -; mRNA.
DR EMBL; EF636458; ABS12328.2; -; Genomic_DNA.
DR EMBL; BC118336; AAI18337.1; -; mRNA.
DR RefSeq; NP_001104795.1; NM_001111325.1.
DR AlphaFoldDB; Q7YS81; -.
DR SMR; Q7YS81; -.
DR STRING; 9913.ENSBTAP00000007923; -.
DR PaxDb; Q7YS81; -.
DR PRIDE; Q7YS81; -.
DR Ensembl; ENSBTAT00000007923; ENSBTAP00000007923; ENSBTAG00000006030.
DR GeneID; 281343; -.
DR KEGG; bta:281343; -.
DR CTD; 4656; -.
DR VEuPathDB; HostDB:ENSBTAG00000006030; -.
DR VGNC; VGNC:31837; MYOG.
DR eggNOG; KOG3960; Eukaryota.
DR GeneTree; ENSGT00950000182959; -.
DR HOGENOM; CLU_100258_0_0_1; -.
DR InParanoid; Q7YS81; -.
DR OMA; PWACKIC; -.
DR OrthoDB; 1471470at2759; -.
DR TreeFam; TF316344; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000006030; Expressed in tongue muscle and 24 other tissues.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
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; IBA:GO_Central.
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:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
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:0048743; P:positive regulation of skeletal muscle fiber development; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
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; 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: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 2: Evidence at transcript 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_0000244386"
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"
FT CONFLICT 36
FT /note="E -> K (in Ref. 1; BAC76803)"
FT /evidence="ECO:0000305"
FT CONFLICT 100..102
FT /note="AFE -> GFQ (in Ref. 1; BAC76803)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="A -> P (in Ref. 4; AAI18337)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="S -> N (in Ref. 2; BAE93440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 24962 MW; 914D122EED85BB14 CRC64;
MELYETSPYF YQEPHFYDGE NYLPVHLQGF EPPGYERAEL SLSPEARVPL EDKGLGPAEH
CPGQCLPWAC KVCKRKSVSV DRRRAATLRE KRRLKKVNEA FEALKRSTLL NPNQRLPKVE
ILRSAIQYIE RLQALLSSLN QEERDLRYRG GGGPQAAVPS ECSSHSASCS PQWGSALEFG
PNPGDHLLPA DPTDAHNLHS LTSIVDSITV EDVAAAFPDE TIPN
