MYOD1_MOUSE
ID MYOD1_MOUSE Reviewed; 318 AA.
AC P10085; Q8C6B1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Myoblast determination protein 1;
GN Name=Myod1; Synonyms=Myod;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3690668; DOI=10.1016/0092-8674(87)90585-x;
RA Davis R.L., Weintraub H., Lassar A.B.;
RT "Expression of a single transfected cDNA converts fibroblasts to
RT myoblasts.";
RL Cell 51:987-1000(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1754380; DOI=10.1093/nar/19.23.6433;
RA Zingg J.-M., Alva G.P., Jost J.-P.;
RT "Characterisation of a genomic clone covering the structural mouse MyoD1
RT gene and its promoter region.";
RL Nucleic Acids Res. 19:6433-6439(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3286015; DOI=10.1016/0092-8674(88)90095-5;
RA Pinney D.F., Pearson-White S.H., Konieczny S.F., Latham K.E.,
RA Emerson C.P. Jr.;
RT "Myogenic lineage determination and differentiation: evidence for a
RT regulatory gene pathway.";
RL Cell 53:781-793(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP FUNCTION.
RX PubMed=3175662; DOI=10.1126/science.3175662;
RA Tapscott S.J., Davis R.L., Thayer M.J., Cheng P.-F., Weintraub H.,
RA Lassar A.B.;
RT "MyoD1: a nuclear phosphoprotein requiring a Myc homology region to convert
RT fibroblasts to myoblasts.";
RL Science 242:405-411(1988).
RN [7]
RP ACETYLATION.
RX PubMed=9029156; DOI=10.1093/emboj/16.2.369;
RA Puri P.L., Avantaggiati M.L., Balsano C., Sang N., Graessmann A.,
RA Giordano A., Levrero M.;
RT "p300 is required for MyoD-dependent cell cycle arrest and muscle-specific
RT gene transcription.";
RL EMBO J. 16:369-383(1997).
RN [8]
RP INHIBITION BY TWIST.
RX PubMed=9343420; DOI=10.1128/mcb.17.11.6563;
RA Hamamori Y., Wu H.Y., Sartorelli V., Kedes L.;
RT "The basic domain of myogenic basic helix-loop-helix (bHLH) proteins is the
RT novel target for direct inhibition by another bHLH protein, Twist.";
RL Mol. Cell. Biol. 17:6563-6573(1997).
RN [9]
RP REVIEW ON ACETYLATION/DEACETYLATION.
RX PubMed=11532390; DOI=10.1016/s0959-437x(00)00224-0;
RA McKinsey T.A., Zhang C.L., Olson E.N.;
RT "Control of muscle development by dueling HATs and HDACs.";
RL Curr. Opin. Genet. Dev. 11:497-504(2001).
RN [10]
RP INTERACTION WITH P-TEFB COMPLEX.
RX PubMed=12037670; DOI=10.1038/sj.onc.1205493;
RA Simone C., Stiegler P., Bagella L., Pucci B., Bellan C., De Falco G.,
RA De Luca A., Guanti G., Puri P.L., Giordano A.;
RT "Activation of MyoD-dependent transcription by cdk9/cyclin T2.";
RL Oncogene 21:4137-4148(2002).
RN [11]
RP DEACETYLATION BY SIRT1.
RX PubMed=12887892; DOI=10.1016/s1097-2765(03)00226-0;
RA Fulco M., Schiltz R.L., Iezzi S., King M.T., Zhao P., Kashiwaya Y.,
RA Hoffman E., Veech R.L., Sartorelli V.;
RT "Sir2 regulates skeletal muscle differentiation as a potential sensor of
RT the redox state.";
RL Mol. Cell 12:51-62(2003).
RN [12]
RP INTERACTION WITH DDX5.
RX PubMed=17011493; DOI=10.1016/j.devcel.2006.08.003;
RA Caretti G., Schiltz R.L., Dilworth F.J., Di Padova M., Zhao P., Ogryzko V.,
RA Fuller-Pace F.V., Hoffman E.P., Tapscott S.J., Sartorelli V.;
RT "The RNA helicases p68/p72 and the noncoding RNA SRA are coregulators of
RT MyoD and skeletal muscle differentiation.";
RL Dev. Cell 11:547-560(2006).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16901893; DOI=10.1074/jbc.m605445200;
RA Wilson E.M., Rotwein P.;
RT "Control of MyoD function during initiation of muscle differentiation by an
RT autocrine signaling pathway activated by insulin-like growth factor-II.";
RL J. Biol. Chem. 281:29962-29971(2006).
RN [14]
RP INTERACTION WITH NUPR1.
RX PubMed=19723804; DOI=10.1242/jcs.048678;
RA Sambasivan R., Cheedipudi S., Pasupuleti N., Saleh A., Pavlath G.K.,
RA Dhawan J.;
RT "The small chromatin-binding protein p8 coordinates the association of
RT anti-proliferative and pro-myogenic proteins at the myogenin promoter.";
RL J. Cell Sci. 122:3481-3491(2009).
RN [15]
RP INTERACTION WITH TSC22D3.
RC STRAIN=DBA/2J; TISSUE=Myoblast;
RX PubMed=20124407; DOI=10.1074/jbc.m109.070136;
RA Bruscoli S., Donato V., Velardi E., Di Sante M., Migliorati G., Donato R.,
RA Riccardi C.;
RT "Glucocorticoid-induced leucine zipper (GILZ) and long GILZ inhibit
RT myogenic differentiation and mediate anti-myogenic effects of
RT glucocorticoids.";
RL J. Biol. Chem. 285:10385-10396(2010).
RN [16]
RP INTERACTION WITH SETD3.
RX PubMed=21832073; DOI=10.1074/jbc.m110.203307;
RA Eom G.H., Kim K.B., Kim J.H., Kim J.Y., Kim J.R., Kee H.J., Kim D.W.,
RA Choe N., Park H.J., Son H.J., Choi S.Y., Kook H., Seo S.B.;
RT "Histone methyltransferase SETD3 regulates muscle differentiation.";
RL J. Biol. Chem. 286:34733-34742(2011).
RN [17]
RP FUNCTION, AND PROMOTER BINDING.
RX PubMed=21798092; DOI=10.1186/2044-5040-1-14;
RA Londhe P., Davie J.K.;
RT "Sequential association of myogenic regulatory factors and E proteins at
RT muscle-specific genes.";
RL Skelet. Muscle 1:14-14(2011).
RN [18]
RP INTERACTION WITH CHD2.
RX PubMed=22569126; DOI=10.1038/emboj.2012.136;
RA Harada A., Okada S., Konno D., Odawara J., Yoshimi T., Yoshimura S.,
RA Kumamaru H., Saiwai H., Tsubota T., Kurumizaka H., Akashi K., Tachibana T.,
RA Imbalzano A.N., Ohkawa Y.;
RT "Chd2 interacts with H3.3 to determine myogenic cell fate.";
RL EMBO J. 31:2994-3007(2012).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 102-166.
RX PubMed=8181063; DOI=10.1016/0092-8674(94)90159-7;
RA Ma P.C.M., Rould M.A., Weintraub H., Pabo C.O.;
RT "Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA
RT recognition and implications for transcriptional activation.";
RL Cell 77:451-459(1994).
CC -!- FUNCTION: Acts as a transcriptional activator that promotes
CC transcription of muscle-specific target genes and plays a role in
CC muscle differentiation (PubMed:16901893). Together with MYF5 and MYOG,
CC co-occupies muscle-specific gene promoter core region during
CC myogenesis. Induces fibroblasts to differentiate into myoblasts.
CC Interacts with and is inhibited by the twist protein. This interaction
CC probably involves the basic domains of both proteins (PubMed:21798092,
CC PubMed:3175662). {ECO:0000269|PubMed:16901893,
CC ECO:0000269|PubMed:21798092, ECO:0000269|PubMed:3175662}.
CC -!- SUBUNIT: Interacts with SUV39H1 (By similarity). Efficient DNA binding
CC requires dimerization with another bHLH protein. Seems to form active
CC heterodimers with ITF-2. Interacts with DDX5. Interacts with CHD2.
CC Interacts with TSC22D3 isoform 1 and isoform 4. Interacts with SETD3
CC (PubMed:21832073). Interacts with P-TEFB complex; promotes the
CC transcriptional activity of MYOD1 through its CDK9-mediated
CC phosphorylation (PubMed:12037670). Interacts with CSRP3 (By
CC similarity). Interacts with NUPR1 (PubMed:19723804).
CC {ECO:0000250|UniProtKB:P15172, ECO:0000269|PubMed:12037670,
CC ECO:0000269|PubMed:17011493, ECO:0000269|PubMed:19723804,
CC ECO:0000269|PubMed:20124407, ECO:0000269|PubMed:21832073,
CC ECO:0000269|PubMed:22569126}.
CC -!- INTERACTION:
CC P10085; Q8VIM5-1: Myocd; NbExp=2; IntAct=EBI-4405734, EBI-15626132;
CC P10085; Q6P9Z1: Smarcd3; NbExp=6; IntAct=EBI-4405734, EBI-7525857;
CC P10085; O54864: Suv39h1; NbExp=3; IntAct=EBI-4405734, EBI-302230;
CC P10085; P50463: Csrp3; Xeno; NbExp=3; IntAct=EBI-4405734, EBI-12502290;
CC P10085; P17844: DDX5; Xeno; NbExp=3; IntAct=EBI-4405734, EBI-351962;
CC P10085; Q92993: KAT5; Xeno; NbExp=5; IntAct=EBI-4405734, EBI-399080;
CC P10085; Q02078: MEF2A; Xeno; NbExp=2; IntAct=EBI-4405734, EBI-2656305;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16901893}.
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. {ECO:0000269|PubMed:9029156}.
CC -!- PTM: Ubiquitinated on the N-terminus; which is required for proteasomal
CC degradation. {ECO:0000250}.
CC -!- PTM: Phosphorylated by CDK9. This phosphorylation promotes its function
CC in muscle differentiation (By similarity). {ECO:0000250}.
CC -!- PTM: Methylation at Lys-104 by EHMT2/G9a inhibits myogenic activity.
CC {ECO:0000250}.
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DR EMBL; M18779; AAA39799.1; -; mRNA.
DR EMBL; X61655; CAA43836.1; -; Genomic_DNA.
DR EMBL; M84918; AAA39798.1; -; mRNA.
DR EMBL; AK076157; BAC36224.1; -; mRNA.
DR EMBL; AK142859; BAE25213.1; -; mRNA.
DR EMBL; BC103613; AAI03614.1; -; mRNA.
DR EMBL; BC103618; AAI03619.1; -; mRNA.
DR EMBL; BC103619; AAI03620.1; -; mRNA.
DR CCDS; CCDS21277.1; -.
DR PIR; A29636; A29636.
DR RefSeq; NP_034996.2; NM_010866.2.
DR PDB; 1MDY; X-ray; 2.80 A; A=102-166, B/C/D=105-166.
DR PDBsum; 1MDY; -.
DR AlphaFoldDB; P10085; -.
DR SMR; P10085; -.
DR BioGRID; 201673; 30.
DR CORUM; P10085; -.
DR DIP; DIP-37N; -.
DR ELM; P10085; -.
DR IntAct; P10085; 20.
DR MINT; P10085; -.
DR STRING; 10090.ENSMUSP00000072330; -.
DR iPTMnet; P10085; -.
DR PhosphoSitePlus; P10085; -.
DR PaxDb; P10085; -.
DR PRIDE; P10085; -.
DR Antibodypedia; 12172; 1102 antibodies from 46 providers.
DR DNASU; 17927; -.
DR Ensembl; ENSMUST00000072514; ENSMUSP00000072330; ENSMUSG00000009471.
DR GeneID; 17927; -.
DR KEGG; mmu:17927; -.
DR UCSC; uc012fkv.1; mouse.
DR CTD; 4654; -.
DR MGI; MGI:97275; Myod1.
DR VEuPathDB; HostDB:ENSMUSG00000009471; -.
DR eggNOG; KOG3960; Eukaryota.
DR GeneTree; ENSGT00950000182959; -.
DR HOGENOM; CLU_066887_0_0_1; -.
DR InParanoid; P10085; -.
DR OMA; GPMEMTE; -.
DR OrthoDB; 1471470at2759; -.
DR PhylomeDB; P10085; -.
DR TreeFam; TF316344; -.
DR Reactome; R-MMU-525793; Myogenesis.
DR BioGRID-ORCS; 17927; 2 hits in 71 CRISPR screens.
DR EvolutionaryTrace; P10085; -.
DR PRO; PR:P10085; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P10085; protein.
DR Bgee; ENSMUSG00000009471; Expressed in mesenchyme from somatopleure and 94 other tissues.
DR Genevisible; P10085; MM.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0000791; C:euchromatin; IDA:ARUK-UCL.
DR GO; GO:0030016; C:myofibril; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:UniProtKB.
DR GO; GO:0043425; F:bHLH transcription factor binding; IPI:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
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:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:ARUK-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:ARUK-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:MGI.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; NAS:UniProtKB.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IDA:MGI.
DR GO; GO:0071453; P:cellular response to oxygen levels; IDA:MGI.
DR GO; GO:0009267; P:cellular response to starvation; IDA:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:MGI.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IDA:MGI.
DR GO; GO:0045445; P:myoblast differentiation; IDA:MGI.
DR GO; GO:0007518; P:myoblast fate determination; IDA:MGI.
DR GO; GO:0007520; P:myoblast fusion; IMP:MGI.
DR GO; GO:0014904; P:myotube cell development; ISO:MGI.
DR GO; GO:0014902; P:myotube differentiation; IDA:MGI.
DR GO; GO:0014908; P:myotube differentiation involved in skeletal muscle regeneration; IMP:MGI.
DR GO; GO:0035562; P:negative regulation of chromatin binding; IDA:MGI.
DR GO; GO:2000818; P:negative regulation of myoblast proliferation; IMP:MGI.
DR GO; GO:0051099; P:positive regulation of binding; IDA:MGI.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IDA: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:MGI.
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; IMP:MGI.
DR GO; GO:1905382; P:positive regulation of snRNA transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IDA:CACAO.
DR GO; GO:0043484; P:regulation of RNA splicing; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IDA:MGI.
DR GO; GO:0043503; P:skeletal muscle fiber adaptation; IMP:MGI.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
DR GO; GO:0007519; P:skeletal muscle tissue development; IDA:MGI.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IDA:MGI.
DR GO; GO:0051146; P:striated muscle cell differentiation; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI.
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 3D-structure; Acetylation; Activator; Developmental protein;
KW Differentiation; DNA-binding; Methylation; Myogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..318
FT /note="Myoblast determination protein 1"
FT /id="PRO_0000127361"
FT DOMAIN 109..160
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 175..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..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 287..318
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"
FT CONFLICT 53
FT /note="M -> V (in Ref. 1; AAA39799, 2; CAA43836 and 3;
FT AAA39798)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="P -> S (in Ref. 1; AAA39799, 2; CAA43836 and 3;
FT AAA39798)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="A -> V (in Ref. 1; AAA39799, 2; CAA43836 and 3;
FT AAA39798)"
FT /evidence="ECO:0000305"
FT HELIX 106..133
FT /evidence="ECO:0007829|PDB:1MDY"
FT HELIX 146..162
FT /evidence="ECO:0007829|PDB:1MDY"
SQ SEQUENCE 318 AA; 34233 MW; AEC6572277A78D54 CRC64;
MELLSPPLRD IDLTGPDGSL CSFETADDFY DDPCFDSPDL RFFEDLDPRL VHMGALLKPE
EHAHFPTAVH PGPGAREDEH VRAPSGHHQA GRCLLWACKA CKRKTTNADR RKAATMRERR
RLSKVNEAFE TLKRCTSSNP NQRLPKVEIL RNAIRYIEGL QALLRDQDAA PPGAAAFYAP
GPLPPGRGSE HYSGDSDASS PRSNCSDGMM DYSGPPSGPR RQNGYDTAYY SEAARESRPG
KSAAVSSLDC LSSIVERIST DSPAAPALLL ADAPPESPPG PPEGASLSDT EQGTQTPSPD
AAPQCPAGSN PNAIYQVL
