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P13349 (MYF5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. 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:
Myogenic factor 5

Short name=Myf-5
Alternative name(s):
Class C basic helix-loop-helix protein 2
Short name=bHLHc2
Gene names
Name:MYF5
Synonyms:BHLHC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length255 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. Together with MYOG and MYOD1, co-occupies muscle-specific gene promoter core region during myogenesis. Induces fibroblasts to differentiate into myoblasts. Probable sequence specific DNA-binding protein.

Subunit structure

Efficient DNA binding requires dimerization with another bHLH protein.

Subcellular location

Nucleus.

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
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcamera-type eye development

Inferred from electronic annotation. Source: Ensembl

cartilage condensation

Inferred from electronic annotation. Source: Ensembl

embryonic skeletal system morphogenesis

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Inferred from electronic annotation. Source: Ensembl

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 2311584. Source: ProtInc

muscle tissue morphogenesis

Inferred from electronic annotation. Source: Ensembl

ossification

Inferred from electronic annotation. Source: Ensembl

positive regulation of muscle cell differentiation

Traceable author statement. Source: Reactome

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 2311584. Source: ProtInc

skeletal muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

skeletal muscle tissue development

Traceable author statement Ref.1. Source: ProtInc

somitogenesis

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Traceable author statement PubMed 2311584. Source: GOC

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

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

Traceable author statement PubMed 2311584. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 19829708. Source: UniProtKB

protein heterodimerization activity

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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 255255Myogenic factor 5
PRO_0000127344

Regions

Domain83 – 13452bHLH

Experimental info

Sequence conflict2411A → R in CAA33025. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P13349 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 62F00454C729BE66

FASTA25528,296
        10         20         30         40         50         60 
MDVMDGCQFS PSEYFYDGSC IPSPEGEFGD EFVPRVAAFG AHKAELQGSD EDEHVRAPTG 

        70         80         90        100        110        120 
HHQAGHCLMW ACKACKRKST TMDRRKAATM RERRRLKKVN QAFETLKRCT TTNPNQRLPK 

       130        140        150        160        170        180 
VEILRNAIRY IESLQELLRE QVENYYSLPG QSCSEPTSPT SNCSDGMPEC NSPVWSRKSS 

       190        200        210        220        230        240 
TFDSIYCPDV SNVYATDKNS LSSLDCLSNI VDRITSSEQP GLPLQDLASL SPVASTDSQP 

       250 
ATPGASSSRL IYHVL 

« Hide

References

« Hide 'large scale' references
[1]"A novel human muscle factor related to but distinct from MyoD1 induces myogenic conversion in 10T1/2 fibroblasts."
Braun T., Buschhausen-Denker G., Bober E., Tannich E., Arnold H.H.
EMBO J. 8:701-709(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skeletal muscle.
[2]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].
[3]"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].
[4]Thompson D.B.
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14894 mRNA. Translation: CAA33025.1.
CH471054 Genomic DNA. Translation: EAW97368.1.
BC069373 mRNA. Translation: AAH69373.1.
U27313 Genomic DNA. Translation: AAA69824.1.
CCDSCCDS9020.1.
PIRS04105.
RefSeqNP_005584.2. NM_005593.2.
UniGeneHs.178023.

3D structure databases

ProteinModelPortalP13349.
SMRP13349. Positions 76-140.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110702. 6 interactions.
MINTMINT-1526584.
STRING9606.ENSP00000228644.

PTM databases

PhosphoSiteP13349.

Polymorphism databases

DMDM215274028.

Proteomic databases

PaxDbP13349.
PRIDEP13349.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228644; ENSP00000228644; ENSG00000111049.
GeneID4617.
KEGGhsa:4617.
UCSCuc001szg.2. human.

Organism-specific databases

CTD4617.
GeneCardsGC12P081085.
HGNCHGNC:7565. MYF5.
HPAHPA041691.
MIM159990. gene.
neXtProtNX_P13349.
PharmGKBPA31363.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239177.
HOGENOMHOG000234800.
HOVERGENHBG006429.
InParanoidP13349.
OMAMMDGCQF.
OrthoDBEOG76QFK1.
PhylomeDBP13349.
TreeFamTF316344.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
SignaLinkP13349.

Gene expression databases

BgeeP13349.
CleanExHS_MYF5.
GenevestigatorP13349.

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

GenomeRNAi4617.
NextBio17772.
PROP13349.
SOURCESearch...

Entry information

Entry nameMYF5_HUMAN
AccessionPrimary (citable) accession number: P13349
Secondary accession number(s): Q6ISR9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 126 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 12

Human chromosome 12: entries, gene names and cross-references to MIM