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   27-MAR-2024, entry version 202.
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; 62.
DR   DIP; DIP-159N; -.
DR   IntAct; P15173; 53.
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; 9606-ENSP00000241651; -.
DR   PeptideAtlas; P15173; -.
DR   Antibodypedia; 20659; 1176 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   AGR; HGNC:7612; -.
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; 5392786at2759; -.
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 1166 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 cell types or tissues.
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; IEA:Ensembl.
DR   GO; GO:0001216; F:DNA-binding transcription activator activity; 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: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   CDD; cd18935; bHLH_TS_MYOG_Myf4; 1.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 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; MYOGENIC FACTOR; 1.
DR   PANTHER; PTHR11534:SF5; MYOGENIN; 1.
DR   Pfam; PF01586; Basic; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00520; BASIC; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   PROSITE; PS50888; BHLH; 1.
DR   Genevisible; P15173; HS.
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
//