MYOD1_BOVIN
ID MYOD1_BOVIN Reviewed; 318 AA.
AC Q7YS82;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Myoblast determination protein 1;
GN Name=MYOD1; Synonyms=MYOD;
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.
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 (By similarity). Interacts with NUPR1 (By
CC similarity). {ECO:0000250|UniProtKB:P10085,
CC ECO:0000250|UniProtKB:Q02346}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
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; AB110599; BAC76802.1; -; mRNA.
DR AlphaFoldDB; Q7YS82; -.
DR SMR; Q7YS82; -.
DR STRING; 9913.ENSBTAP00000002868; -.
DR PaxDb; Q7YS82; -.
DR eggNOG; KOG3960; Eukaryota.
DR InParanoid; Q7YS82; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISS:AgBase.
DR GO; GO:0043425; F:bHLH transcription factor binding; ISS:AgBase.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:AgBase.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISS:UniProtKB.
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; ISS:AgBase.
DR GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0007518; P:myoblast fate determination; ISS:UniProtKB.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; ISS:UniProtKB.
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:0006355; P:regulation of transcription, DNA-templated; ISS:AgBase.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISS:UniProtKB.
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 2: Evidence at transcript 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_0000247561"
FT DOMAIN 109..160
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 174..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..208
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; 34207 MW; BD467B506D0A5447 CRC64;
MEVLSPPLRD VDLTGPDGSL CNFATADDFY DDPCFDSPDL RFFEDLDPRL VHVGALLKPE
EHSHFPAAAH PAPGAREDEH VRAPSGHHQA GRCLLWACKA CKRKTTNADR RKAATMRERR
RLSKVNEAFE TLKRCTSSNP NQRLPKVEIL RNAIRYIEGL QALLRDQDAA PPGAAAAFYA
PGPLPPGRSG EHYSGDSDAS SPRSNCSDGM MDYSGPPSGA RRRNCYDRTY YSEAPNEPRP
GKSAAVSSLD CLSSIVERIS TESPAAPALL LADAPPESSP GPQEAAGSEV ERGTPAPSPD
TAPQGLAGAN PNPIYQVL
