Myoblast determination protein 1 - Homo sapiens (Human)

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P15172 (MYOD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 124. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	MYOD1
Synonyms:	BHLHC1, MYF3, MYOD

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	320 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in muscle differentiation (myogenic factor). Induces fibroblasts to differentiate into myoblasts. Activates muscle-specific promoters. 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. 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
Sequence similarities	Contains 1 basic helix-loop-helix (bHLH) domain.

Ontologies

Keywords
Biological process	Differentiation Myogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	Developmental protein
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	muscle cell fate commitment Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of muscle cell differentiation Traceable author statement. Source: Reactome positive regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: BHF-UCL protein phosphorylation Traceable author statement. Source: ProtInc
Cellular component	nuclear chromatin Inferred from sequence or structural similarity. Source: BHF-UCL transcription factor complex Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular function	E-box binding Inferred from sequence or structural similarity. Source: BHF-UCL protein heterodimerization activity Inferred from sequence or structural similarity. Source: BHF-UCL sequence-specific distal enhancer binding RNA polymerase II transcription factor activity Traceable author statement. Source: ProtInc transcription coactivator activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TCF3	P15923-1	2	EBI-488878,EBI-769645

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 320

320

Myoblast determination protein 1

PRO_0000127360

Regions

Domain

122 – 161

Helix-loop-helix motif

DNA binding

109 – 121

Basic motif

Amino acid modifications

Cross-link

Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)

Natural variations

Natural variant

262

E → K in a breast cancer sample; somatic mutation. Ref.11

VAR_036392

Natural variant

309

A → V in a breast cancer sample; somatic mutation. Ref.11

VAR_036393

Experimental info

Sequence conflict

124

K → E in CAA35640. Ref.6

Sequence conflict

177

Missing in CAA40000. Ref.1

Sequence conflict

177

Missing in CAA35640. Ref.6

Sequence conflict

251

C → Y in CAA40000. Ref.1

Sequence conflict

251

C → Y in CAA35640. Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

P15172 [UniParc].

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

320

34,501

        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' referencesShow 'large scale' references »
[1]	"Human MyoD: cDNA and deduced amino acid sequence." Pearson-White S.H. Nucleic Acids Res. 19:1148-1148(1991) [PubMed: 1850513] [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: 9546368] [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. 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: 15489334] [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: 2583111] [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: 9774340] [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: 11532390] [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: 12037670] [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: 16858404] [Abstract] Cited for: INTERACTION WITH SUV39H1.
[11]	"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. Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [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.
IPI	IPI00102339.
PIR	S26827.
RefSeq	NP_002469.2. NM_002478.4.
UniGene	Hs.181768.
3D structure databases
ProteinModelPortal	P15172.
SMR	P15172. Positions 102-166.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-704N.
IntAct	P15172. 7 interactions.
MINT	MINT-128965.
STRING	P15172.
PTM databases
PhosphoSite	P15172.
Polymorphism databases
DMDM	209572729.
Proteomic databases
PRIDE	P15172.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000250003; ENSP00000250003; ENSG00000129152.
GeneID	4654.
KEGG	hsa:4654.
Organism-specific databases
CTD	4654.
GeneCards	GC11P017741.
H-InvDB	HIX0035989.
HGNC	HGNC:7611. MYOD1.
MIM	159970. gene.
neXtProt	NX_P15172.
PharmGKB	PA31416.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05543.
GeneTree	ENSGT00530000063004.
HOGENOM	HBG714454.
HOVERGEN	HBG006429.
InParanoid	P15172.
OMA	TYYSEAP.
OrthoDB	EOG47WNPM.
PhylomeDB	P15172.
Enzyme and pathway databases
Pathway_Interaction_DB	smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling. hdac_classiii_pathway. Signaling events mediated by HDAC Class III.
Reactome	REACT_111045. Developmental Biology.
Gene expression databases
ArrayExpress	P15172.
Bgee	P15172.
CleanEx	HS_MYOD1.
Genevestigator	P15172.
GermOnline	ENSG00000129152. Homo sapiens.
Family and domain databases
InterPro	IPR002546. Basic. IPR011598. HLH_DNA-bd. IPR022032. Myf5. [Graphical view]
Gene3D	G3DSA:4.10.280.10. HLH_DNA_bd. 1 hit.
KO	K09064.
Pfam	PF01586. Basic. 1 hit. PF00010. HLH. 1 hit. PF12232. Myf5. 1 hit. [Graphical view]
SMART	SM00520. BASIC. 1 hit. SM00353. HLH. 1 hit. [Graphical view]
SUPFAM	SSF47459. HLH_basic. 1 hit.
PROSITE	PS50888. HLH. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

MYOD1_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 124 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Human chromosome 11

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents