ID MYOD1_RAT Reviewed; 318 AA. AC Q02346; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 08-NOV-2023, entry version 157. DE RecName: Full=Myoblast determination protein 1; GN Name=Myod1; Synonyms=Myod; 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 [GENOMIC DNA]. RX PubMed=1321778; DOI=10.1016/0378-1119(92)90519-u; RA Vaidya T.B., Rhodes S.J., Moore J.L., Sherman D.A., Konieczny S.F., RA Taparowsky E.J.; RT "Isolation and structural analysis of the rat MyoD gene."; RL Gene 116:223-230(1992). RN [2] 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). CC -!- FUNCTION: Acts as a transcriptional activator that promotes CC transcription of muscle-specific target genes and plays a role in CC muscle differentiation. Together with MYF5 and MYOG, co-occupies CC muscle-specific gene promoter core region during myogenesis. Induces CC fibroblasts to differentiate into myoblasts. Interacts with and is CC inhibited by the twist protein. This interaction probably involves the CC basic domains of both proteins (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH CC protein. Seems to form active heterodimers with ITF-2. Interacts with CC SUV39H1. Interacts with DDX5. Interacts with CHD2. Interacts with CC TSC22D3 (By similarity). Interacts with SETD3 (By similarity). CC Interacts with P-TEFB complex; promotes the transcriptional activity of CC MYOD1 through its CDK9-mediated phosphorylation (By similarity). CC Interacts with CSRP3 (PubMed:9234731). Interacts with NUPR1 (By CC similarity). {ECO:0000250|UniProtKB:P10085, CC ECO:0000269|PubMed:9234731}. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- PTM: Phosphorylated by CDK9. This phosphorylation promotes its function CC in muscle differentiation (By similarity). {ECO:0000250}. CC -!- PTM: Acetylated by a complex containing EP300 and PCAF. The acetylation CC is essential to activate target genes. Conversely, its deacetylation by CC SIRT1 inhibits its function (By similarity). {ECO:0000250}. CC -!- PTM: Ubiquitinated on the N-terminus; which is required for proteasomal CC degradation. {ECO:0000250}. CC -!- PTM: Methylation at Lys-104 by EHMT2/G9a inhibits myogenic activity. CC {ECO:0000250}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M84176; AAA41661.1; -; Genomic_DNA. DR PIR; JC1171; JC1171. DR RefSeq; NP_788268.1; NM_176079.1. DR AlphaFoldDB; Q02346; -. DR SMR; Q02346; -. DR STRING; 10116.ENSRNOP00000015109; -. DR PhosphoSitePlus; Q02346; -. DR PaxDb; 10116-ENSRNOP00000015109; -. DR GeneID; 337868; -. DR KEGG; rno:337868; -. DR UCSC; RGD:631429; rat. DR AGR; RGD:631429; -. DR CTD; 4654; -. DR RGD; 631429; Myod1. DR eggNOG; KOG3960; Eukaryota. DR InParanoid; Q02346; -. DR OrthoDB; 5392786at2759; -. DR PhylomeDB; Q02346; -. DR Reactome; R-RNO-525793; Myogenesis. DR PRO; PR:Q02346; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0000785; C:chromatin; ISO:RGD. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0000791; C:euchromatin; ISO:RGD. DR GO; GO:0030016; C:myofibril; ISO:RGD. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD. DR GO; GO:0043425; F:bHLH transcription factor binding; ISO:RGD. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0031490; F:chromatin DNA binding; ISO:RGD. DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:RGD. 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; ISO:RGD. DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD. 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; IDA:RGD. DR GO; GO:0019899; F:enzyme binding; ISO:RGD. DR GO; GO:0016922; F:nuclear receptor binding; ISO:RGD. DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor 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:0031625; F:ubiquitin protein ligase binding; ISO:RGD. DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISS:UniProtKB. DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISO:RGD. DR GO; GO:0071453; P:cellular response to oxygen levels; ISO:RGD. DR GO; GO:0009267; P:cellular response to starvation; ISO: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; ISS:UniProtKB. DR GO; GO:0007518; P:myoblast fate determination; ISS:UniProtKB. DR GO; GO:0007520; P:myoblast fusion; ISO:RGD. DR GO; GO:0014904; P:myotube cell development; ISO:RGD. DR GO; GO:0014902; P:myotube differentiation; ISO:RGD. DR GO; GO:0014908; P:myotube differentiation involved in skeletal muscle regeneration; ISO:RGD. DR GO; GO:2000818; P:negative regulation of myoblast proliferation; ISO:RGD. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:RGD. DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; ISS:UniProtKB. DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IBA:GO_Central. DR GO; GO:1901741; P:positive regulation of myoblast fusion; ISO:RGD. DR GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; IBA:GO_Central. DR GO; GO:0043415; P:positive regulation of skeletal muscle tissue regeneration; ISS:UniProtKB. DR GO; GO:1905382; P:positive regulation of snRNA transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB. DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD. DR GO; GO:0043484; P:regulation of RNA splicing; ISO:RGD. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0035994; P:response to muscle stretch; IEP:RGD. DR GO; GO:0014732; P:skeletal muscle atrophy; IEP:RGD. DR GO; GO:0035914; P:skeletal muscle cell differentiation; ISO:RGD. DR GO; GO:0043503; P:skeletal muscle fiber adaptation; ISO:RGD. DR GO; GO:0048741; P:skeletal muscle fiber development; ISO:RGD. DR GO; GO:0007519; P:skeletal muscle tissue development; ISS:UniProtKB. DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IMP:RGD. DR GO; GO:0051146; P:striated muscle cell differentiation; ISS:UniProtKB. DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:RGD. DR CDD; cd18936; bHLH_TS_MYOD1_Myf3; 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; IPR022032; Myf5. DR InterPro; IPR002546; MyoD_N. DR InterPro; IPR039704; Myogenic_factor. DR PANTHER; PTHR11534:SF2; MYOBLAST DETERMINATION PROTEIN 1; 1. DR PANTHER; PTHR11534; MYOGENIC FACTOR; 1. DR Pfam; PF01586; Basic; 1. DR Pfam; PF00010; HLH; 1. DR Pfam; PF12232; Myf5; 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. PE 1: Evidence at protein level; KW Acetylation; Activator; Developmental protein; Differentiation; KW DNA-binding; Methylation; Myogenesis; Nucleus; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..318 FT /note="Myoblast determination protein 1" FT /id="PRO_0000127363" FT DOMAIN 109..160 FT /note="bHLH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981" FT REGION 175..224 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 262..318 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 193..207 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 268..282 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 283..309 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 104 FT /note="N6-methyllysine; by EHMT2" FT /evidence="ECO:0000250|UniProtKB:P15172" FT CROSSLNK 1 FT /note="Peptide (Met-Gly) (interchain with G-Cter in FT ubiquitin)" FT /evidence="ECO:0000250" SQ SEQUENCE 318 AA; 34359 MW; FC43E46BB1287F5F CRC64; MELLSPPLRD TDLLGPDGSL CSFATRDDFY DDPCFDSPDL RFFEDLDPRL VHVGALLKPE EHAHFPTTVH PGPGAREDEH VRAPSGHHQA GRCLLWACKA CKRKTTNADR RKAATMRERR RLSKVNEAFE TLKRCTSSNP NQRLPKVEIL RNAIRYIEGL QALLRDQDAA PPGAAAFYAP GPLPPGRGSE HYSGDSDASS PRSNCSDGMM DYSGPPSGPR RQNGYDAAYY SEASSEPRPG KSAAVSSLDC LSSIVERIST DSPAAPSLLL PDAPPESPPG PPEETSSSDA EQGTQTPSPD STPQCPAGSK PNPIYQVL //