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P15173

- MYOG_HUMAN

UniProt

P15173 - MYOG_HUMAN

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Protein

Myogenin

Gene

MYOG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. chromatin DNA binding Source: UniProtKB
  2. core promoter binding Source: UniProtKB
  3. E-box binding Source: BHF-UCL
  4. protein heterodimerization activity Source: BHF-UCL
  5. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  6. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  7. RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
  8. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  9. sequence-specific DNA binding Source: NTNU_SB
  10. sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cellular response to estradiol stimulus Source: UniProtKB
  3. cellular response to growth factor stimulus Source: Ensembl
  4. cellular response to lithium ion Source: Ensembl
  5. mRNA transcription from RNA polymerase II promoter Source: BHF-UCL
  6. muscle cell differentiation Source: Reactome
  7. muscle cell fate commitment Source: BHF-UCL
  8. negative regulation of cell proliferation Source: UniProtKB
  9. ossification Source: Ensembl
  10. positive regulation of cell cycle arrest Source: UniProtKB
  11. positive regulation of muscle atrophy Source: UniProtKB
  12. positive regulation of muscle cell differentiation Source: Reactome
  13. positive regulation of myoblast differentiation Source: UniProtKB
  14. positive regulation of myotube differentiation Source: UniProtKB
  15. positive regulation of skeletal muscle fiber development Source: UniProtKB
  16. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  17. regulation of myoblast fusion Source: UniProtKB
  18. regulation of satellite cell proliferation Source: UniProtKB
  19. response to denervation involved in regulation of muscle adaptation Source: UniProtKB
  20. response to electrical stimulus involved in regulation of muscle adaptation Source: UniProtKB
  21. response to muscle activity involved in regulation of muscle adaptation Source: UniProtKB
  22. skeletal muscle fiber development Source: Ensembl
  23. skeletal muscle tissue development Source: ProtInc
  24. striated muscle atrophy Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Cell cycle, Differentiation, Myogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_21402. CDO in myogenesis.
SignaLinkiP15173.

Names & Taxonomyi

Protein namesi
Recommended name:
Myogenin
Alternative name(s):
Class C basic helix-loop-helix protein 3
Short name:
bHLHc3
Myogenic factor 4
Short name:
Myf-4
Gene namesi
Name:MYOG
Synonyms:BHLHC3, MYF4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:7612. MYOG.

Subcellular locationi

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

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: UniProtKB
  3. protein-DNA complex Source: UniProtKB
  4. transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31417.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 224224MyogeninPRO_0000127375Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei77 – 771Phosphoserine; by CaMK2GBy similarity
Modified residuei79 – 791Phosphoserine; by CaMK2GBy similarity
Modified residuei87 – 871Phosphothreonine; by CaMK2GBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP15173.
PRIDEiP15173.

PTM databases

PhosphoSiteiP15173.

Expressioni

Gene expression databases

BgeeiP15173.
CleanExiHS_MYOG.
GenevestigatoriP15173.

Organism-specific databases

HPAiHPA038093.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi110739. 22 interactions.
DIPiDIP-159N.
IntActiP15173. 8 interactions.
MINTiMINT-1516099.
STRINGi9606.ENSP00000241651.

Structurei

3D structure databases

ProteinModelPortaliP15173.
SMRiP15173. Positions 74-136.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 13252bHLHPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG285405.
GeneTreeiENSGT00530000063004.
HOGENOMiHOG000234799.
HOVERGENiHBG006429.
InParanoidiP15173.
KOiK18483.
OMAiFYQEPHF.
OrthoDBiEOG76QFK1.
PhylomeDBiP15173.
TreeFamiTF316344.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR002546. Basic.
IPR011598. bHLH_dom.
[Graphical view]
PfamiPF01586. Basic. 1 hit.
PF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00520. BASIC. 1 hit.
SM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15173 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELYETSPYF YQEPRFYDGE NYLPVHLQGF EPPGYERTEL TLSPEAPGPL
60 70 80 90 100
EDKGLGTPEH CPGQCLPWAC KVCKRKSVSV DRRRAATLRE KRRLKKVNEA
110 120 130 140 150
FEALKRSTLL NPNQRLPKVE ILRSAIQYIE RLQALLSSLN QEERDLRYRG
160 170 180 190 200
GGGPQPGVPS ECSSHSASCS PEWGSALEFS ANPGDHLLTA DPTDAHNLHS
210 220
LTSIVDSITV EDVSVAFPDE TMPN
Length:224
Mass (Da):25,037
Last modified:December 1, 1992 - v2
Checksum:i91421D69B57551FB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1433.1.
PIRiA41128.
RefSeqiNP_002470.2. NM_002479.5.
UniGeneiHs.2830.

Genome annotation databases

EnsembliENST00000241651; ENSP00000241651; ENSG00000122180.
GeneIDi4656.
KEGGihsa:4656.
UCSCiuc001gzd.4. human.

Polymorphism databases

DMDMi127625.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1433.1.
PIRi A41128.
RefSeqi NP_002470.2. NM_002479.5.
UniGenei Hs.2830.

3D structure databases

ProteinModelPortali P15173.
SMRi P15173. Positions 74-136.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110739. 22 interactions.
DIPi DIP-159N.
IntActi P15173. 8 interactions.
MINTi MINT-1516099.
STRINGi 9606.ENSP00000241651.

PTM databases

PhosphoSitei P15173.

Polymorphism databases

DMDMi 127625.

Proteomic databases

PaxDbi P15173.
PRIDEi P15173.

Protocols and materials databases

DNASUi 4656.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000241651 ; ENSP00000241651 ; ENSG00000122180 .
GeneIDi 4656.
KEGGi hsa:4656.
UCSCi uc001gzd.4. human.

Organism-specific databases

CTDi 4656.
GeneCardsi GC01M203052.
HGNCi HGNC:7612. MYOG.
HPAi HPA038093.
MIMi 159980. gene.
neXtProti NX_P15173.
PharmGKBi PA31417.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG285405.
GeneTreei ENSGT00530000063004.
HOGENOMi HOG000234799.
HOVERGENi HBG006429.
InParanoidi P15173.
KOi K18483.
OMAi FYQEPHF.
OrthoDBi EOG76QFK1.
PhylomeDBi P15173.
TreeFami TF316344.

Enzyme and pathway databases

Reactomei REACT_21402. CDO in myogenesis.
SignaLinki P15173.

Miscellaneous databases

ChiTaRSi MYOG. human.
GeneWikii Myogenin.
GenomeRNAii 4656.
NextBioi 17946.
PROi P15173.
SOURCEi Search...

Gene expression databases

Bgeei P15173.
CleanExi HS_MYOG.
Genevestigatori P15173.

Family and domain databases

Gene3Di 4.10.280.10. 1 hit.
InterProi IPR002546. Basic.
IPR011598. bHLH_dom.
[Graphical view ]
Pfami PF01586. Basic. 1 hit.
PF00010. HLH. 1 hit.
[Graphical view ]
SMARTi SM00520. BASIC. 1 hit.
SM00353. HLH. 1 hit.
[Graphical view ]
SUPFAMi SSF47459. SSF47459. 1 hit.
PROSITEi PS50888. BHLH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiMYOG_HUMAN
AccessioniPrimary (citable) accession number: P15173
Secondary accession number(s): Q53XW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: December 1, 1992
Last modified: October 29, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3