MYOD1_RAT
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 25-MAY-2022, entry version 152.
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}.
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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; Q02346; -.
DR GeneID; 337868; -.
DR KEGG; rno:337868; -.
DR UCSC; RGD:631429; rat.
DR CTD; 4654; -.
DR RGD; 631429; Myod1.
DR eggNOG; KOG3960; Eukaryota.
DR InParanoid; Q02346; -.
DR OrthoDB; 1471470at2759; -.
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; IDA:RGD.
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; 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; 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:0043966; P:histone H3 acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
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:0035562; P:negative regulation of chromatin binding; ISO:RGD.
DR GO; GO:2000818; P:negative regulation of myoblast proliferation; ISO:RGD.
DR GO; GO:0051099; P:positive regulation of binding; 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:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
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 Gene3D; 4.10.280.10; -; 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; PTHR11534; 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; SSF47459; 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
