MYOG_HUMAN
ID MYOG_HUMAN Reviewed; 224 AA.
AC P15173; Q53XW6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Myogenin;
DE AltName: Full=Class C basic helix-loop-helix protein 3;
DE Short=bHLHc3;
DE AltName: Full=Myogenic factor 4;
DE Short=Myf-4;
GN Name=MYOG; Synonyms=BHLHC3, MYF4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=2583111; DOI=10.1002/j.1460-2075.1989.tb08535.x;
RA Braun T., Bober E., Buschhausen-Denker G., Kohtz S., Grzeschik K.-H.,
RA Arnold H.H.;
RT "Differential expression of myogenic determination genes in muscle cells:
RT possible autoactivation by the Myf gene products.";
RL EMBO J. 8:3617-3625(1989).
RN [2]
RP ERRATUM OF PUBMED:2583111, AND SEQUENCE REVISION.
RA Braun T., Bober E., Buschhausen-Denker G., Kohtz S., Grzeschik K.-H.,
RA Arnold H.H.;
RL EMBO J. 9:592-592(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1659574; DOI=10.1083/jcb.115.4.905;
RA Salminen A., Braun T., Buchberger A., Juers S., Winter B., Arnold H.H.;
RT "Transcription of the muscle regulatory gene Myf4 is regulated by serum
RT components, peptide growth factors and signaling pathways involving G
RT proteins.";
RL J. Cell Biol. 115:905-917(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [7]
RP INTERACTION WITH CSRP3.
RX PubMed=24860983; DOI=10.1111/febs.12859;
RA Vafiadaki E., Arvanitis D.A., Papalouka V., Terzis G., Roumeliotis T.I.,
RA Spengos K., Garbis S.D., Manta P., Kranias E.G., Sanoudou D.;
RT "Muscle lim protein isoform negatively regulates striated muscle actin
RT dynamics and differentiation.";
RL FEBS J. 281:3261-3279(2014).
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 (By similarity). Interacts with CSRP3. {ECO:0000250,
CC ECO:0000269|PubMed:24860983}.
CC -!- INTERACTION:
CC P15173; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-3906629, EBI-11096309;
CC P15173; Q96RK4: BBS4; NbExp=3; IntAct=EBI-3906629, EBI-1805814;
CC P15173; Q13515: BFSP2; NbExp=3; IntAct=EBI-3906629, EBI-10229433;
CC P15173; Q7RTS1: BHLHA15; NbExp=3; IntAct=EBI-3906629, EBI-8844218;
CC P15173; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-3906629, EBI-744556;
CC P15173; Q7Z6N9: CCDC28A; NbExp=6; IntAct=EBI-3906629, EBI-10258115;
CC P15173; Q8IWP9: CCDC28A; NbExp=4; IntAct=EBI-3906629, EBI-355471;
CC P15173; Q96M91: CFAP53; NbExp=3; IntAct=EBI-3906629, EBI-742422;
CC P15173; Q96AJ1: CLUAP1; NbExp=7; IntAct=EBI-3906629, EBI-739780;
CC P15173; O95639-2: CPSF4; NbExp=3; IntAct=EBI-3906629, EBI-13063650;
CC P15173; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-3906629, EBI-11962928;
CC P15173; O60573: EIF4E2; NbExp=4; IntAct=EBI-3906629, EBI-398610;
CC P15173; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-3906629, EBI-1752811;
CC P15173; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-3906629, EBI-6658203;
CC P15173; Q6QHK4: FIGLA; NbExp=5; IntAct=EBI-3906629, EBI-11976617;
CC P15173; P02792: FTL; NbExp=4; IntAct=EBI-3906629, EBI-713279;
CC P15173; P55040: GEM; NbExp=3; IntAct=EBI-3906629, EBI-744104;
CC P15173; O75409: H2AP; NbExp=6; IntAct=EBI-3906629, EBI-6447217;
CC P15173; P41134: ID1; NbExp=4; IntAct=EBI-3906629, EBI-1215527;
CC P15173; Q70UQ0: IKBIP; NbExp=4; IntAct=EBI-3906629, EBI-2557212;
CC P15173; Q70UQ0-4: IKBIP; NbExp=4; IntAct=EBI-3906629, EBI-12190633;
CC P15173; Q14005-2: IL16; NbExp=3; IntAct=EBI-3906629, EBI-17178971;
CC P15173; Q9P2K6: KLHL42; NbExp=3; IntAct=EBI-3906629, EBI-739890;
CC P15173; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-3906629, EBI-11742507;
CC P15173; O60336: MAPKBP1; NbExp=3; IntAct=EBI-3906629, EBI-947402;
CC P15173; O95983-2: MBD3; NbExp=3; IntAct=EBI-3906629, EBI-11978579;
CC P15173; P40692: MLH1; NbExp=12; IntAct=EBI-3906629, EBI-744248;
CC P15173; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-3906629, EBI-11750983;
CC P15173; Q96NG3: ODAD4; NbExp=3; IntAct=EBI-3906629, EBI-1046387;
CC P15173; Q8N7B6: PACRGL; NbExp=3; IntAct=EBI-3906629, EBI-3925298;
CC P15173; Q8N7B6-2: PACRGL; NbExp=3; IntAct=EBI-3906629, EBI-10694433;
CC P15173; P52435: POLR2J; NbExp=3; IntAct=EBI-3906629, EBI-394753;
CC P15173; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-3906629, EBI-742688;
CC P15173; Q08117-2: TLE5; NbExp=3; IntAct=EBI-3906629, EBI-11741437;
CC P15173; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-3906629, EBI-3918381;
CC P15173; O14530: TXNDC9; NbExp=4; IntAct=EBI-3906629, EBI-707554;
CC P15173; Q8N6Y0: USHBP1; NbExp=5; IntAct=EBI-3906629, EBI-739895;
CC P15173; Q8WYQ9: ZCCHC14; NbExp=3; IntAct=EBI-3906629, EBI-3937908;
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 -!- 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; X17651; CAA35641.1; ALT_SEQ; mRNA.
DR EMBL; X62155; CAA44080.1; -; Genomic_DNA.
DR EMBL; BT007233; AAP35897.1; -; mRNA.
DR EMBL; CH471067; EAW91463.1; -; Genomic_DNA.
DR EMBL; BC053899; AAH53899.1; -; mRNA.
DR CCDS; CCDS1433.1; -.
DR PIR; A41128; A41128.
DR RefSeq; NP_002470.2; NM_002479.5.
DR AlphaFoldDB; P15173; -.
DR SMR; P15173; -.
DR BioGRID; 110739; 61.
DR DIP; DIP-159N; -.
DR IntAct; P15173; 52.
DR MINT; P15173; -.
DR STRING; 9606.ENSP00000241651; -.
DR iPTMnet; P15173; -.
DR PhosphoSitePlus; P15173; -.
DR BioMuta; MYOG; -.
DR DMDM; 127625; -.
DR EPD; P15173; -.
DR MassIVE; P15173; -.
DR PaxDb; P15173; -.
DR PeptideAtlas; P15173; -.
DR PRIDE; P15173; -.
DR Antibodypedia; 20659; 1098 antibodies from 41 providers.
DR DNASU; 4656; -.
DR Ensembl; ENST00000241651.5; ENSP00000241651.4; ENSG00000122180.5.
DR GeneID; 4656; -.
DR KEGG; hsa:4656; -.
DR MANE-Select; ENST00000241651.5; ENSP00000241651.4; NM_002479.6; NP_002470.2.
DR UCSC; uc001gzd.5; human.
DR CTD; 4656; -.
DR DisGeNET; 4656; -.
DR GeneCards; MYOG; -.
DR HGNC; HGNC:7612; MYOG.
DR HPA; ENSG00000122180; Group enriched (skeletal muscle, tongue).
DR MIM; 159980; gene.
DR neXtProt; NX_P15173; -.
DR OpenTargets; ENSG00000122180; -.
DR PharmGKB; PA31417; -.
DR VEuPathDB; HostDB:ENSG00000122180; -.
DR eggNOG; KOG3960; Eukaryota.
DR GeneTree; ENSGT00950000182959; -.
DR HOGENOM; CLU_100258_0_0_1; -.
DR InParanoid; P15173; -.
DR OMA; PWACKIC; -.
DR OrthoDB; 1471470at2759; -.
DR PhylomeDB; P15173; -.
DR TreeFam; TF316344; -.
DR PathwayCommons; P15173; -.
DR Reactome; R-HSA-525793; Myogenesis.
DR SignaLink; P15173; -.
DR SIGNOR; P15173; -.
DR BioGRID-ORCS; 4656; 11 hits in 1088 CRISPR screens.
DR ChiTaRS; MYOG; human.
DR GeneWiki; Myogenin; -.
DR GenomeRNAi; 4656; -.
DR Pharos; P15173; Tbio.
DR PRO; PR:P15173; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P15173; protein.
DR Bgee; ENSG00000122180; Expressed in hindlimb stylopod muscle and 80 other tissues.
DR Genevisible; P15173; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISS:BHF-UCL.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
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; IEA:Ensembl.
DR GO; GO:0071285; P:cellular response to lithium ion; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0042693; P:muscle cell fate commitment; ISS:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
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; IDA:NTNU_SB.
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:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
DR GO; GO:0007519; P:skeletal muscle tissue development; TAS:ProtInc.
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..224
FT /note="Myogenin"
FT /id="PRO_0000127375"
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; 25037 MW; 91421D69B57551FB CRC64;
MELYETSPYF YQEPRFYDGE NYLPVHLQGF EPPGYERTEL TLSPEAPGPL EDKGLGTPEH
CPGQCLPWAC KVCKRKSVSV DRRRAATLRE KRRLKKVNEA FEALKRSTLL NPNQRLPKVE
ILRSAIQYIE RLQALLSSLN QEERDLRYRG GGGPQPGVPS ECSSHSASCS PEWGSALEFS
ANPGDHLLTA DPTDAHNLHS LTSIVDSITV EDVSVAFPDE TMPN
