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P15173 (MYOG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myogenin
Alternative name(s):
Class C basic helix-loop-helix protein 3
Short name=bHLHc3
Myogenic factor 4
Short name=Myf-4
Gene names
Name:MYOG
Synonyms:BHLHC3, MYF4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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, cell cycle exit and muscle atrophy. Essential for the development of functional embryonic skeletal fiber muscle differentiation. However is dispensable for postnatal skeletal muscle growth; phosphorylation by CAMK2G inhibits its transcriptional activity in respons to muscle activity. Required for the recruitment of the FACT complex to muscle-specific promoter regions, thus promoting gene expression initiation. During terminal myoblast differentiation, plays a role as a strong activator of transcription at loci with an open chromatin structure previously initiated by MYOD1. Together with MYF5 and MYOD1, co-occupies muscle-specific gene promoter core regions during myogenesis. Cooperates also with myocyte-specific enhancer factor MEF2D and BRG1-dependent recruitment of SWI/SNF chromatin-remodeling enzymes to alter chromatin structure at myogenic late gene promoters. Facilitates cell cycle exit during terminal muscle differentiation through the up-regulation of miR-20a expression, which in turn represses genes involved in cell cycle progression. Binds to the E-box containing (E1) promoter region of the miR-20a gene. Plays also a role in preventing reversal of muscle cell differentiation. Contributes to the atrophy-related gene expression in adult denervated muscles. Induces fibroblasts to differentiate into myoblasts By similarity.

Subunit structure

Homodimer and heterodimer with E12; heterodimerization enhances MYOG DNA-binding and transcriptional activities. Interacts with SMARCA4/BRG1/BAF190A. Interacts (via C-terminus region) with SSRP1 and SUPT16H; the interaction is indicative of an interaction with the FACT complex By similarity.

Subcellular location

Nucleus. Note: Recruited to late myogenic gene promoter regulatory sequences with SMARCA4/BRG1/BAF190A and SWI/SNF chromatin-remodeling enzymes to promote chromatin-remodeling and transcription initiation in developing embryos By similarity.

Post-translational modification

Phosphorylated by CAMK2G on threonine and serine amino acids in a muscle activity-dependent manner. Phosphorylation of Thr-87 impairs both DNA-binding and trans-activation functions in contracting muscles By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processCell cycle
Differentiation
Myogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
Developmental protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to estradiol stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to lithium ion

Inferred from electronic annotation. Source: Ensembl

mRNA transcription from RNA polymerase II promoter

Traceable author statement PubMed 19783823. Source: BHF-UCL

muscle cell differentiation

Traceable author statement. Source: Reactome

muscle cell fate commitment

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

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

ossification

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell cycle arrest

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of muscle atrophy

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of muscle cell differentiation

Traceable author statement. Source: Reactome

positive regulation of myoblast differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of myotube differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of skeletal muscle fiber development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of myoblast fusion

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of satellite cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

response to denervation involved in regulation of muscle adaptation

Inferred from sequence or structural similarity. Source: UniProtKB

response to electrical stimulus involved in regulation of muscle adaptation

Inferred from sequence or structural similarity. Source: UniProtKB

response to muscle activity involved in regulation of muscle adaptation

Inferred from sequence or structural similarity. Source: UniProtKB

skeletal muscle fiber development

Inferred from electronic annotation. Source: Ensembl

skeletal muscle tissue development

Traceable author statement PubMed 10329008. Source: ProtInc

striated muscle atrophy

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

protein-DNA complex

Inferred from sequence or structural similarity. Source: UniProtKB

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 regulatory region sequence-specific DNA binding

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

RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Traceable author statement PubMed 19783823. Source: BHF-UCL

chromatin DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

core promoter binding

Inferred from sequence or structural similarity. Source: UniProtKB

core promoter proximal region sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

protein heterodimerization activity

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

sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 224224Myogenin
PRO_0000127375

Regions

Domain81 – 13252bHLH

Amino acid modifications

Modified residue771Phosphoserine; by CaMK2G By similarity
Modified residue791Phosphoserine; by CaMK2G By similarity
Modified residue871Phosphothreonine; by CaMK2G By similarity

Sequences

Sequence LengthMass (Da)Tools
P15173 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: 91421D69B57551FB

FASTA22425,037
        10         20         30         40         50         60 
MELYETSPYF YQEPRFYDGE NYLPVHLQGF EPPGYERTEL TLSPEAPGPL EDKGLGTPEH 

        70         80         90        100        110        120 
CPGQCLPWAC KVCKRKSVSV DRRRAATLRE KRRLKKVNEA FEALKRSTLL NPNQRLPKVE 

       130        140        150        160        170        180 
ILRSAIQYIE RLQALLSSLN QEERDLRYRG GGGPQPGVPS ECSSHSASCS PEWGSALEFS 

       190        200        210        220 
ANPGDHLLTA DPTDAHNLHS LTSIVDSITV EDVSVAFPDE TMPN 

« Hide

References

« Hide 'large scale' references
[1]"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: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skeletal muscle.
[2]Erratum
Braun T., Bober E., Buschhausen-Denker G., Kohtz S., Grzeschik K.-H., Arnold H.H.
EMBO J. 9:592-592(1990)
Cited for: SEQUENCE REVISION.
[3]"Transcription of the muscle regulatory gene Myf4 is regulated by serum components, peptide growth factors and signaling pathways involving G proteins."
Salminen A., Braun T., Buchberger A., Juers S., Winter B., Arnold H.H.
J. Cell Biol. 115:905-917(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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].
[5]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17651 mRNA. Translation: CAA35641.1. Sequence problems.
X62155 Genomic DNA. Translation: CAA44080.1.
BT007233 mRNA. Translation: AAP35897.1.
CH471067 Genomic DNA. Translation: EAW91463.1.
BC053899 mRNA. Translation: AAH53899.1.
PIRA41128.
RefSeqNP_002470.2. NM_002479.5.
UniGeneHs.2830.

3D structure databases

ProteinModelPortalP15173.
SMRP15173. Positions 74-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110739. 17 interactions.
DIPDIP-159N.
IntActP15173. 7 interactions.
MINTMINT-1516099.
STRING9606.ENSP00000241651.

PTM databases

PhosphoSiteP15173.

Polymorphism databases

DMDM127625.

Proteomic databases

PaxDbP15173.
PRIDEP15173.

Protocols and materials databases

DNASU4656.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000241651; ENSP00000241651; ENSG00000122180.
GeneID4656.
KEGGhsa:4656.
UCSCuc001gzd.4. human.

Organism-specific databases

CTD4656.
GeneCardsGC01M203052.
HGNCHGNC:7612. MYOG.
HPAHPA038093.
MIM159980. gene.
neXtProtNX_P15173.
PharmGKBPA31417.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG285405.
HOGENOMHOG000234799.
HOVERGENHBG006429.
InParanoidP15173.
OMAFYQEPHF.
OrthoDBEOG76QFK1.
PhylomeDBP15173.
TreeFamTF316344.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
SignaLinkP15173.

Gene expression databases

BgeeP15173.
CleanExHS_MYOG.
GenevestigatorP15173.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR002546. Basic.
IPR011598. bHLH_dom.
[Graphical view]
PfamPF01586. Basic. 1 hit.
PF00010. HLH. 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

ChiTaRSMYOG. human.
GeneWikiMyogenin.
GenomeRNAi4656.
NextBio17946.
PROP15173.
SOURCESearch...

Entry information

Entry nameMYOG_HUMAN
AccessionPrimary (citable) accession number: P15173
Secondary accession number(s): Q53XW6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: December 1, 1992
Last modified: April 16, 2014
This is version 132 of the entry and version 2 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 chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM