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P10085 (MYOD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myoblast determination protein 1
Gene names
Name:Myod1
Synonyms:Myod
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length318 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation. Together with MYF5 and MYOG, co-occupies muscle-specific gene promoter core region during myogenesis. Induces fibroblasts to differentiate into myoblasts. Interacts with and is inhibited by the twist protein. This interaction probably involves the basic domains of both proteins. Ref.6 Ref.13

Subunit structure

Interacts with SUV39H1 and CDK9 By similarity. Efficient DNA binding requires dimerization with another bHLH protein. Seems to form active heterodimers with ITF-2. Interacts with DDX5. Interacts with CHD2. Ref.7 Ref.14

Subcellular location

Nucleus.

Post-translational modification

Acetylated by a complex containing EP300 and PCAF. The acetylation is essential to activate target genes. Conversely, its deacetylation by SIRT1 inhibits its function. Ref.10 Ref.11

Ubiquitinated on the N-terminus; which is required for proteasomal degradation By similarity.

Phosphorylated by CDK9. This phosphorylation promotes its function in muscle differentiation By similarity.

Methylation at Lys-104 by EHMT2/G9a inhibits myogenic activity By similarity.

Sequence similarities

Contains 1 bHLH (basic helix-loop-helix) domain.

Ontologies

Keywords
   Biological processDifferentiation
Myogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
Developmental protein
   PTMAcetylation
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle cell differentiation

Non-traceable author statement PubMed 21556048. Source: UniProtKB

cellular response to estradiol stimulus

Inferred from direct assay PubMed 15706034. Source: UniProtKB

cellular response to glucocorticoid stimulus

Inferred from direct assay PubMed 19319192. Source: MGI

cellular response to oxygen levels

Inferred from direct assay PubMed 19319192. Source: MGI

cellular response to starvation

Inferred from direct assay PubMed 19319192. Source: MGI

histone H3 acetylation

Inferred from direct assay PubMed 15706034. Source: UniProtKB

histone H4 acetylation

Inferred from direct assay PubMed 15706034. Source: UniProtKB

muscle organ development

Inferred from direct assay PubMed 15192231. Source: MGI

myoblast differentiation

Inferred from direct assay PubMed 12037571PubMed 12486129. Source: MGI

myoblast fate determination

Inferred from direct assay PubMed 12486129. Source: MGI

myotube differentiation involved in skeletal muscle regeneration

Inferred from mutant phenotype PubMed 1348494. Source: MGI

positive regulation of muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of myoblast fusion

Inferred from electronic annotation. Source: Ensembl

positive regulation of skeletal muscle tissue regeneration

Inferred from mutant phenotype PubMed 17028574. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15706034. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12782625PubMed 15520228PubMed 17904117. Source: MGI

regulation of alternative mRNA splicing, via spliceosome

Inferred from direct assay PubMed 9525963. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19796622. Source: MGI

skeletal muscle cell differentiation

Non-traceable author statement PubMed 21556048. Source: UniProtKB

skeletal muscle fiber adaptation

Inferred from mutant phenotype PubMed 19319192. Source: MGI

skeletal muscle fiber development

Inferred from mutant phenotype PubMed 19319192. Source: MGI

skeletal muscle tissue development

Inferred from direct assay PubMed 12037571PubMed 14762206. Source: MGI

striated muscle cell differentiation

Inferred from mutant phenotype PubMed 17028574. Source: MGI

transcription from RNA polymerase II promoter

Traceable author statement PubMed 1846704. Source: GOC

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 19319192. Source: MGI

myofibril

Inferred from direct assay PubMed 19319192PubMed 21131290. Source: MGI

nuclear chromatin

Inferred from direct assay PubMed 20833138. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 20139084. Source: UniProtKB

transcription factor complex

Inferred from direct assay PubMed 2503252. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay PubMed 12486129. Source: MGI

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Traceable author statement PubMed 1846704. Source: MGI

chromatin DNA binding

Inferred from direct assay PubMed 15706034. Source: UniProtKB

core promoter binding

Inferred from direct assay PubMed 15706034. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 20833138. Source: BHF-UCL

protein heterodimerization activity

Inferred from physical interaction PubMed 15572127. Source: MGI

sequence-specific DNA binding

Inferred from direct assay PubMed 22638570. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 12486129. Source: MGI

transcription factor binding

Inferred from physical interaction PubMed 2503252. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 19319192. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DDX5P178443EBI-4405734,EBI-351962From a different organism.
KAT5Q929935EBI-4405734,EBI-399080From a different organism.
Smarcd3Q6P9Z16EBI-4405734,EBI-7525857
Suv39h1O548643EBI-4405734,EBI-302230

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 318318Myoblast determination protein 1
PRO_0000127361

Regions

Domain109 – 16052bHLH

Amino acid modifications

Modified residue1041N6-methyllysine; by EHMT2 By similarity
Cross-link1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict531M → V in AAA39799. Ref.1
Sequence conflict531M → V in CAA43836. Ref.2
Sequence conflict531M → V in AAA39798. Ref.3
Sequence conflict661P → S in AAA39799. Ref.1
Sequence conflict661P → S in CAA43836. Ref.2
Sequence conflict661P → S in AAA39798. Ref.3
Sequence conflict2341A → V in AAA39799. Ref.1
Sequence conflict2341A → V in CAA43836. Ref.2
Sequence conflict2341A → V in AAA39798. Ref.3

Secondary structure

..... 318
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10085 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: AEC6572277A78D54

FASTA31834,233
        10         20         30         40         50         60 
MELLSPPLRD IDLTGPDGSL CSFETADDFY DDPCFDSPDL RFFEDLDPRL VHMGALLKPE 

        70         80         90        100        110        120 
EHAHFPTAVH PGPGAREDEH VRAPSGHHQA GRCLLWACKA CKRKTTNADR RKAATMRERR 

       130        140        150        160        170        180 
RLSKVNEAFE TLKRCTSSNP NQRLPKVEIL RNAIRYIEGL QALLRDQDAA PPGAAAFYAP 

       190        200        210        220        230        240 
GPLPPGRGSE HYSGDSDASS PRSNCSDGMM DYSGPPSGPR RQNGYDTAYY SEAARESRPG 

       250        260        270        280        290        300 
KSAAVSSLDC LSSIVERIST DSPAAPALLL ADAPPESPPG PPEGASLSDT EQGTQTPSPD 

       310 
AAPQCPAGSN PNAIYQVL 

« Hide

References

« Hide 'large scale' references
[1]"Expression of a single transfected cDNA converts fibroblasts to myoblasts."
Davis R.L., Weintraub H., Lassar A.B.
Cell 51:987-1000(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Characterisation of a genomic clone covering the structural mouse MyoD1 gene and its promoter region."
Zingg J.-M., Alva G.P., Jost J.-P.
Nucleic Acids Res. 19:6433-6439(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Myogenic lineage determination and differentiation: evidence for a regulatory gene pathway."
Pinney D.F., Pearson-White S.H., Konieczny S.F., Latham K.E., Emerson C.P. Jr.
Cell 53:781-793(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Head.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"MyoD1: a nuclear phosphoprotein requiring a Myc homology region to convert fibroblasts to myoblasts."
Tapscott S.J., Davis R.L., Thayer M.J., Cheng P.-F., Weintraub H., Lassar A.B.
Science 242:405-411(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"The RNA helicases p68/p72 and the noncoding RNA SRA are coregulators of MyoD and skeletal muscle differentiation."
Caretti G., Schiltz R.L., Dilworth F.J., Di Padova M., Zhao P., Ogryzko V., Fuller-Pace F.V., Hoffman E.P., Tapscott S.J., Sartorelli V.
Dev. Cell 11:547-560(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDX5.
[8]"Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation."
Ma P.C.M., Rould M.A., Weintraub H., Pabo C.O.
Cell 77:451-459(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 102-166.
[9]"The basic domain of myogenic basic helix-loop-helix (bHLH) proteins is the novel target for direct inhibition by another bHLH protein, Twist."
Hamamori Y., Wu H.Y., Sartorelli V., Kedes L.
Mol. Cell. Biol. 17:6563-6573(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION BY TWIST.
[10]"p300 is required for MyoD-dependent cell cycle arrest and muscle-specific gene transcription."
Puri P.L., Avantaggiati M.L., Balsano C., Sang N., Graessmann A., Giordano A., Levrero M.
EMBO J. 16:369-383(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION.
[11]"Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state."
Fulco M., Schiltz R.L., Iezzi S., King M.T., Zhao P., Kashiwaya Y., Hoffman E., Veech R.L., Sartorelli V.
Mol. Cell 12:51-62(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DEACETYLATION BY SIRT1.
[12]"Control of muscle development by dueling HATs and HDACs."
McKinsey T.A., Zhang C.L., Olson E.N.
Curr. Opin. Genet. Dev. 11:497-504(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ACETYLATION/DEACETYLATION.
[13]"Sequential association of myogenic regulatory factors and E proteins at muscle-specific genes."
Londhe P., Davie J.K.
Skelet. Muscle 1:14-14(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PROMOTER BINDING.
[14]"Chd2 interacts with H3.3 to determine myogenic cell fate."
Harada A., Okada S., Konno D., Odawara J., Yoshimi T., Yoshimura S., Kumamaru H., Saiwai H., Tsubota T., Kurumizaka H., Akashi K., Tachibana T., Imbalzano A.N., Ohkawa Y.
EMBO J. 31:2994-3007(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHD2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18779 mRNA. Translation: AAA39799.1.
X61655 Genomic DNA. Translation: CAA43836.1.
M84918 mRNA. Translation: AAA39798.1.
AK076157 mRNA. Translation: BAC36224.1.
AK142859 mRNA. Translation: BAE25213.1.
BC103613 mRNA. Translation: AAI03614.1.
BC103618 mRNA. Translation: AAI03619.1.
BC103619 mRNA. Translation: AAI03620.1.
PIRA29636.
RefSeqNP_034996.2. NM_010866.2.
UniGeneMm.1526.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MDYX-ray2.80A102-166[»]
B/C/D105-166[»]
ProteinModelPortalP10085.
SMRP10085. Positions 102-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201673. 31 interactions.
DIPDIP-37N.
IntActP10085. 15 interactions.
MINTMINT-263097.
STRING10090.ENSMUSP00000072330.

PTM databases

PhosphoSiteP10085.

Proteomic databases

PRIDEP10085.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000072514; ENSMUSP00000072330; ENSMUSG00000009471.
GeneID17927.
KEGGmmu:17927.
UCSCuc012fkv.1. mouse.

Organism-specific databases

CTD4654.
MGIMGI:97275. Myod1.

Phylogenomic databases

eggNOGNOG292792.
GeneTreeENSGT00530000063004.
HOGENOMHOG000234800.
HOVERGENHBG006429.
InParanoidQ8C6B1.
KOK09064.
OMATYYSEAP.
OrthoDBEOG76QFK1.
TreeFamTF316344.

Enzyme and pathway databases

ReactomeREACT_188576. Developmental Biology.

Gene expression databases

BgeeP10085.
CleanExMM_MYOD1.
GenevestigatorP10085.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR002546. Basic.
IPR011598. bHLH_dom.
IPR022032. Myf5.
[Graphical view]
PfamPF01586. Basic. 1 hit.
PF00010. HLH. 1 hit.
PF12232. Myf5. 1 hit.
[Graphical view]
SMARTSM00520. BASIC. 1 hit.
SM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10085.
NextBio292797.
PROP10085.
SOURCESearch...

Entry information

Entry nameMYOD1_MOUSE
AccessionPrimary (citable) accession number: P10085
Secondary accession number(s): Q8C6B1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot