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P15172 (MYOD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myoblast determination protein 1
Alternative name(s):
Class C basic helix-loop-helix protein 1
Short name=bHLHc1
Myogenic factor 3
Short name=Myf-3
Gene names
Name:MYOD1
Synonyms:BHLHC1, MYF3, MYOD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length320 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 By similarity.

Subunit structure

Efficient DNA binding requires dimerization with another bHLH protein. Seems to form active heterodimers with ITF-2. Interacts with SUV39H1 and CDK9. Interacts with DDX5. Interacts with CHD2. Interacts with TSC22D3 By similarity. Ref.9 Ref.10

Subcellular location

Nucleus.

Post-translational modification

Phosphorylated by CDK9. This phosphorylation promotes its function in muscle differentiation. Ref.9

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

Ubiquitinated on the N-terminus; which is required for proteasomal degradation. Ref.7

Methylation at Lys-104 by EHMT2/G9a inhibits myogenic activity. Ref.11

Sequence similarities

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

Ontologies

Keywords
   Biological processDifferentiation
Myogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   LigandDNA-binding
   Molecular functionActivator
Developmental protein
   PTMAcetylation
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to estradiol stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to glucocorticoid stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to oxygen levels

Inferred from electronic annotation. Source: Ensembl

cellular response to starvation

Inferred from electronic annotation. Source: Ensembl

histone H3 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H4 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

muscle cell differentiation

Traceable author statement. Source: Reactome

muscle cell fate commitment

Inferred from sequence or structural similarity. Source: BHF-UCL

muscle organ development

Traceable author statement PubMed 1846704. Source: ProtInc

myoblast fate determination

Inferred from electronic annotation. Source: Ensembl

myotube cell development

Inferred from direct assay PubMed 10672515. Source: BHF-UCL

myotube differentiation involved in skeletal muscle regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of muscle cell differentiation

Inferred from direct assay PubMed 10672515. Source: BHF-UCL

positive regulation of myoblast fusion

Inferred from direct assay PubMed 10672515. Source: BHF-UCL

positive regulation of skeletal muscle tissue regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Traceable author statement PubMed 3175662. Source: ProtInc

regulation of RNA splicing

Inferred from direct assay PubMed 10672515. Source: BHF-UCL

regulation of alternative mRNA splicing, via spliceosome

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 1846704. Source: ProtInc

skeletal muscle fiber adaptation

Inferred from electronic annotation. Source: Ensembl

skeletal muscle fiber development

Inferred from electronic annotation. Source: Ensembl

skeletal muscle tissue development

Traceable author statement PubMed 3175662. Source: ProtInc

transcription from RNA polymerase II promoter

Traceable author statement PubMed 1846704. Source: GOC

   Cellular_componentmyofibril

Inferred from electronic annotation. Source: Ensembl

nuclear chromatin

Inferred from sequence or structural similarity. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Traceable author statement PubMed 3175662. Source: ProtInc

transcription factor complex

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionE-box binding

Inferred from sequence or structural similarity. Source: BHF-UCL

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

Traceable author statement PubMed 1846704. Source: ProtInc

chromatin DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

core promoter binding

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear hormone receptor binding

Inferred from physical interaction PubMed 9862959. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12887892. Source: UniProtKB

protein heterodimerization activity

Inferred from sequence or structural similarity. Source: BHF-UCL

transcription coactivator activity

Traceable author statement PubMed 1846704. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TCF3P15923-12EBI-488878,EBI-769645

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 320320Myoblast determination protein 1
PRO_0000127360

Regions

Domain109 – 16052bHLH

Amino acid modifications

Modified residue1041N6-methyllysine; by EHMT2 Ref.11
Cross-link1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)

Natural variations

Natural variant2621E → K in a breast cancer sample; somatic mutation. Ref.12
VAR_036392
Natural variant3091A → V in a breast cancer sample; somatic mutation. Ref.12
VAR_036393

Experimental info

Sequence conflict1241K → E in CAA35640. Ref.6
Sequence conflict1771Missing in CAA40000. Ref.1
Sequence conflict1771Missing in CAA35640. Ref.6
Sequence conflict2511C → Y in CAA40000. Ref.1
Sequence conflict2511C → Y in CAA35640. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P15172 [UniParc].

Last modified October 14, 2008. Version 3.
Checksum: 75E624D2ED5B0B33

FASTA32034,501
        10         20         30         40         50         60 
MELLSPPLRD VDLTAPDGSL CSFATTDDFY DDPCFDSPDL RFFEDLDPRL MHVGALLKPE 

        70         80         90        100        110        120 
EHSHFPAAVH PAPGAREDEH VRAPSGHHQA GRCLLWACKA CKRKTTNADR RKAATMRERR 

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

       190        200        210        220        230        240 
PGPLPPGRGG EHYSGDSDAS SPRSNCSDGM MDYSGPPSGA RRRNCYEGAY YNEAPSEPRP 

       250        260        270        280        290        300 
GKSAAVSSLD CLSSIVERIS TESPAAPALL LADVPSESPP RRQEAAAPSE GESSGDPTQS 

       310        320 
PDAAPQCPAG ANPNPIYQVL 

« Hide

References

« Hide 'large scale' references
[1]"Human MyoD: cDNA and deduced amino acid sequence."
Pearson-White S.H.
Nucleic Acids Res. 19:1148-1148(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Methylation alterations of the MyoD1 upstream region are predictive of subclassification of human rhabdomyosarcomas."
Chen B., Dias P., Jenkins J.J. III, Savell V.H., Parham D.M.
Am. J. Pathol. 152:1071-1079(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Muscle.
[6]"Differential expression of myogenic determination genes in muscle cells: possible autoactivation by the Myf gene products."
Braun T., Bober E., Buschhausen-Denker G., Kohtz S., Grzeschik K.-H., Arnold H.H.
EMBO J. 8:3617-3625(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 53-320.
Tissue: Skeletal muscle.
[7]"A novel site for ubiquitination: the N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein."
Breitschopf K., Bengal E., Ziv T., Admon A., Ciechanover A.
EMBO J. 17:5964-5973(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT MET-1.
[8]"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.
[9]"Activation of MyoD-dependent transcription by cdk9/cyclin T2."
Simone C., Stiegler P., Bagella L., Pucci B., Bellan C., De Falco G., De Luca A., Guanti G., Puri P.L., Giordano A.
Oncogene 21:4137-4148(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY CDK9, INTERACTION WITH CDK9.
[10]"Histone methyltransferase Suv39h1 represses MyoD-stimulated myogenic differentiation."
Mal A.K.
EMBO J. 25:3323-3334(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUV39H1.
[11]"Lysine methyltransferase G9a methylates the transcription factor MyoD and regulates skeletal muscle differentiation."
Ling B.M., Bharathy N., Chung T.K., Kok W.K., Li S., Tan Y.H., Rao V.K., Gopinadhan S., Sartorelli V., Walsh M.J., Taneja R.
Proc. Natl. Acad. Sci. U.S.A. 109:841-846(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-104.
[12]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-262 AND VAL-309.
+Additional computationally mapped references.

Web resources

Wikipedia

MyoD entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56677 mRNA. Translation: CAA40000.1.
AF027148 Genomic DNA. Translation: AAC29001.1.
BT007157 mRNA. Translation: AAP35821.1.
CH471064 Genomic DNA. Translation: EAW68427.1.
BC064493 mRNA. Translation: AAH64493.1.
X17650 mRNA. Translation: CAA35640.1.
CCDSCCDS7826.1.
PIRS26827.
RefSeqNP_002469.2. NM_002478.4.
UniGeneHs.181768.

3D structure databases

ProteinModelPortalP15172.
SMRP15172. Positions 102-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110737. 67 interactions.
DIPDIP-704N.
IntActP15172. 9 interactions.
MINTMINT-128965.
STRING9606.ENSP00000250003.

PTM databases

PhosphoSiteP15172.

Polymorphism databases

DMDM209572729.

Proteomic databases

PaxDbP15172.
PRIDEP15172.

Protocols and materials databases

DNASU4654.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250003; ENSP00000250003; ENSG00000129152.
GeneID4654.
KEGGhsa:4654.
UCSCuc001mni.3. human.

Organism-specific databases

CTD4654.
GeneCardsGC11P017741.
H-InvDBHIX0035989.
HGNCHGNC:7611. MYOD1.
HPACAB002511.
HPA051362.
MIM159970. gene.
neXtProtNX_P15172.
PharmGKBPA31416.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG292792.
HOGENOMHOG000234800.
HOVERGENHBG006429.
InParanoidP15172.
KOK09064.
OMARISTDSP.
OrthoDBEOG76QFK1.
PhylomeDBP15172.
TreeFamTF316344.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
SignaLinkP15172.

Gene expression databases

BgeeP15172.
CleanExHS_MYOD1.
GenevestigatorP15172.

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

GeneWikiMyoD.
GenomeRNAi4654.
NextBio17940.
PROP15172.
SOURCESearch...

Entry information

Entry nameMYOD1_HUMAN
AccessionPrimary (citable) accession number: P15172
Secondary accession number(s): O75321
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 14, 2008
Last modified: July 9, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM