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P15172

- MYOD1_HUMAN

UniProt

P15172 - MYOD1_HUMAN

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Protein

Myoblast determination protein 1

Gene

MYOD1

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

Functioni

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).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. nuclear hormone receptor binding Source: UniProtKB
  5. protein heterodimerization activity Source: BHF-UCL
  6. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  7. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: ProtInc
  8. RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
  9. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  10. transcription coactivator activity Source: ProtInc

GO - Biological processi

  1. cellular response to estradiol stimulus Source: UniProtKB
  2. cellular response to glucocorticoid stimulus Source: Ensembl
  3. cellular response to oxygen levels Source: Ensembl
  4. cellular response to starvation Source: Ensembl
  5. histone H3 acetylation Source: UniProtKB
  6. histone H4 acetylation Source: UniProtKB
  7. muscle cell differentiation Source: Reactome
  8. muscle cell fate commitment Source: BHF-UCL
  9. muscle organ development Source: ProtInc
  10. myoblast fate determination Source: Ensembl
  11. myotube cell development Source: BHF-UCL
  12. myotube differentiation involved in skeletal muscle regeneration Source: Ensembl
  13. positive regulation of muscle cell differentiation Source: BHF-UCL
  14. positive regulation of myoblast fusion Source: BHF-UCL
  15. positive regulation of skeletal muscle tissue regeneration Source: Ensembl
  16. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  17. protein phosphorylation Source: ProtInc
  18. regulation of alternative mRNA splicing, via spliceosome Source: Ensembl
  19. regulation of RNA splicing Source: BHF-UCL
  20. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  21. skeletal muscle fiber adaptation Source: Ensembl
  22. skeletal muscle fiber development Source: Ensembl
  23. skeletal muscle tissue development Source: ProtInc
  24. transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Differentiation, Myogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_21402. CDO in myogenesis.
SignaLinkiP15172.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:MYOD1
Synonyms:BHLHC1, MYF3, MYOD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:7611. MYOD1.

Subcellular locationi

GO - Cellular componenti

  1. myofibril Source: Ensembl
  2. nuclear chromatin Source: BHF-UCL
  3. nucleoplasm Source: Reactome
  4. nucleus Source: ProtInc
  5. transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31416.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 320320Myoblast determination protein 1PRO_0000127360Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki1 – 1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei104 – 1041N6-methyllysine; by EHMT21 Publication

Post-translational modificationi

Phosphorylated by CDK9. This phosphorylation promotes its function in muscle differentiation.1 Publication
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).By similarity
Ubiquitinated on the N-terminus; which is required for proteasomal degradation.1 Publication
Methylation at Lys-104 by EHMT2/G9a inhibits myogenic activity.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP15172.
PRIDEiP15172.

PTM databases

PhosphoSiteiP15172.

Expressioni

Gene expression databases

BgeeiP15172.
CleanExiHS_MYOD1.
GenevestigatoriP15172.

Organism-specific databases

HPAiCAB002511.
HPA051362.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
TCF3P15923-12EBI-488878,EBI-769645

Protein-protein interaction databases

BioGridi110737. 69 interactions.
DIPiDIP-704N.
IntActiP15172. 10 interactions.
MINTiMINT-128965.
STRINGi9606.ENSP00000250003.

Structurei

3D structure databases

ProteinModelPortaliP15172.
SMRiP15172. Positions 102-166.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini109 – 16052bHLHPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG292792.
GeneTreeiENSGT00530000063004.
HOGENOMiHOG000234800.
HOVERGENiHBG006429.
InParanoidiP15172.
KOiK09064.
OMAiRISTDSP.
OrthoDBiEOG76QFK1.
PhylomeDBiP15172.
TreeFamiTF316344.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR002546. Basic.
IPR011598. bHLH_dom.
IPR022032. Myf5.
[Graphical view]
PfamiPF01586. Basic. 1 hit.
PF00010. HLH. 1 hit.
PF12232. Myf5. 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.

P15172-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELLSPPLRD VDLTAPDGSL CSFATTDDFY DDPCFDSPDL RFFEDLDPRL
60 70 80 90 100
MHVGALLKPE EHSHFPAAVH PAPGAREDEH VRAPSGHHQA GRCLLWACKA
110 120 130 140 150
CKRKTTNADR RKAATMRERR RLSKVNEAFE TLKRCTSSNP NQRLPKVEIL
160 170 180 190 200
RNAIRYIEGL QALLRDQDAA PPGAAAAFYA PGPLPPGRGG EHYSGDSDAS
210 220 230 240 250
SPRSNCSDGM MDYSGPPSGA RRRNCYEGAY YNEAPSEPRP GKSAAVSSLD
260 270 280 290 300
CLSSIVERIS TESPAAPALL LADVPSESPP RRQEAAAPSE GESSGDPTQS
310 320
PDAAPQCPAG ANPNPIYQVL
Length:320
Mass (Da):34,501
Last modified:October 14, 2008 - v3
Checksum:i75E624D2ED5B0B33
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241K → E in CAA35640. (PubMed:2583111)Curated
Sequence conflicti177 – 1771Missing in CAA40000. (PubMed:1850513)Curated
Sequence conflicti177 – 1771Missing in CAA35640. (PubMed:2583111)Curated
Sequence conflicti251 – 2511C → Y in CAA40000. (PubMed:1850513)Curated
Sequence conflicti251 – 2511C → Y in CAA35640. (PubMed:2583111)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti262 – 2621E → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_036392
Natural varianti309 – 3091A → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_036393

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7826.1.
PIRiS26827.
RefSeqiNP_002469.2. NM_002478.4.
UniGeneiHs.181768.

Genome annotation databases

EnsembliENST00000250003; ENSP00000250003; ENSG00000129152.
GeneIDi4654.
KEGGihsa:4654.
UCSCiuc001mni.3. human.

Polymorphism databases

DMDMi209572729.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

MyoD entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS7826.1.
PIRi S26827.
RefSeqi NP_002469.2. NM_002478.4.
UniGenei Hs.181768.

3D structure databases

ProteinModelPortali P15172.
SMRi P15172. Positions 102-166.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110737. 69 interactions.
DIPi DIP-704N.
IntActi P15172. 10 interactions.
MINTi MINT-128965.
STRINGi 9606.ENSP00000250003.

PTM databases

PhosphoSitei P15172.

Polymorphism databases

DMDMi 209572729.

Proteomic databases

PaxDbi P15172.
PRIDEi P15172.

Protocols and materials databases

DNASUi 4654.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000250003 ; ENSP00000250003 ; ENSG00000129152 .
GeneIDi 4654.
KEGGi hsa:4654.
UCSCi uc001mni.3. human.

Organism-specific databases

CTDi 4654.
GeneCardsi GC11P017741.
H-InvDB HIX0035989.
HGNCi HGNC:7611. MYOD1.
HPAi CAB002511.
HPA051362.
MIMi 159970. gene.
neXtProti NX_P15172.
PharmGKBi PA31416.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG292792.
GeneTreei ENSGT00530000063004.
HOGENOMi HOG000234800.
HOVERGENi HBG006429.
InParanoidi P15172.
KOi K09064.
OMAi RISTDSP.
OrthoDBi EOG76QFK1.
PhylomeDBi P15172.
TreeFami TF316344.

Enzyme and pathway databases

Reactomei REACT_21402. CDO in myogenesis.
SignaLinki P15172.

Miscellaneous databases

ChiTaRSi MYOD1. human.
GeneWikii MyoD.
GenomeRNAii 4654.
NextBioi 17940.
PROi P15172.
SOURCEi Search...

Gene expression databases

Bgeei P15172.
CleanExi HS_MYOD1.
Genevestigatori P15172.

Family and domain databases

Gene3Di 4.10.280.10. 1 hit.
InterProi IPR002546. Basic.
IPR011598. bHLH_dom.
IPR022032. Myf5.
[Graphical view ]
Pfami PF01586. Basic. 1 hit.
PF00010. HLH. 1 hit.
PF12232. Myf5. 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. "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. 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. 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. Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-262 AND VAL-309.

Entry informationi

Entry nameiMYOD1_HUMAN
AccessioniPrimary (citable) accession number: P15172
Secondary accession number(s): O75321
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 14, 2008
Last modified: November 26, 2014
This is version 155 of the entry and version 3 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3