P10085 (MYOD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myoblast determination protein 1

Gene names

Name:	Myod1
Synonyms:	Myod

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	318 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. Ref.6
Subunit structure	Interacts with SUV39H1 and CDK9 By similarity. Efficient DNA binding requires dimerization with another bHLH protein. Seems to form active heterodimers with ITF-2. Interacts with DDX5. Ref.7
Subcellular location	Nucleus.
Post-translational modification	Acetylated by a complex containing EP300 and PCAF. The acetylation is essential to activate target genes. Conversely, its deacetylation by SIRT1 inhibits its function. Ubiquitinated on the N-terminus; which is required for proteasomal degradation By similarity. Phosphorylated by CDK9. This phosphorylation promotes its function in muscle differentiation By similarity.
Sequence similarities	Contains 1 bHLH (basic helix-loop-helix) domain.

Ontologies

Keywords
Biological process	Differentiation Myogenesis Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Developmental protein
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cardiac muscle cell differentiation Inferred from expression pattern PubMed 21556048. Source: UniProtKB cellular response to glucocorticoid stimulus Inferred from direct assay PubMed 19319192. Source: MGI cellular response to oxygen levels Inferred from direct assay PubMed 19319192. Source: MGI cellular response to starvation Inferred from direct assay PubMed 19319192. Source: MGI myoblast cell fate determination Inferred from direct assay PubMed 12486129. Source: MGI myotube differentiation involved in skeletal muscle regeneration Inferred from mutant phenotype PubMed 1348494. Source: MGI positive regulation of skeletal muscle tissue regeneration Inferred from mutant phenotype PubMed 17028574. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 12486129PubMed 17855775PubMed 17940050PubMed 7659522. Source: MGI regulation of alternative mRNA splicing, via spliceosome Inferred from direct assay PubMed 9525963. Source: MGI skeletal muscle fiber adaptation Inferred from mutant phenotype PubMed 19319192. Source: MGI skeletal muscle fiber development Inferred from mutant phenotype PubMed 19319192. Source: MGI
Cellular_component	myofibril Inferred from direct assay PubMed 19319192PubMed 21131290. Source: MGI nuclear chromatin Inferred from direct assay PubMed 20833138. Source: BHF-UCL transcription factor complex Inferred from direct assay PubMed 2503252. Source: UniProtKB
Molecular_function	DNA binding Inferred from direct assay PubMed 12486129. Source: MGI RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Traceable author statement PubMed 1846704. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DDX5	P17844	3	EBI-4405734,EBI-351962	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 318

318

Myoblast determination protein 1

PRO_0000127361

Regions

Domain

109 – 160

52

bHLH

Amino acid modifications

Cross-link

1

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

Experimental info

Sequence conflict

53

1

M → V in AAA39799. Ref.1

Sequence conflict

53

1

M → V in CAA43836. Ref.2

Sequence conflict

53

1

M → V in AAA39798. Ref.3

Sequence conflict

66

1

P → S in AAA39799. Ref.1

Sequence conflict

66

1

P → S in CAA43836. Ref.2

Sequence conflict

66

1

P → S in AAA39798. Ref.3

Sequence conflict

234

1

A → V in AAA39799. Ref.1

Sequence conflict

234

1

A → V in CAA43836. Ref.2

Sequence conflict

234

1

A → V in AAA39798. Ref.3

Secondary structure

1

.

.

.

.

.

318

Helix Strand Turn

Details...

Helix

109 – 133

25

Helix

146 – 162

17

Sequences

	Sequence		Length	Mass (Da)
	P10085 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: AEC6572277A78D54	FASTA	318	34,233
	10 20 30 40 50 60 MELLSPPLRD IDLTGPDGSL CSFETADDFY DDPCFDSPDL RFFEDLDPRL VHMGALLKPE 70 80 90 100 110 120 EHAHFPTAVH PGPGAREDEH VRAPSGHHQA GRCLLWACKA CKRKTTNADR RKAATMRERR 130 140 150 160 170 180 RLSKVNEAFE TLKRCTSSNP NQRLPKVEIL RNAIRYIEGL QALLRDQDAA PPGAAAFYAP 190 200 210 220 230 240 GPLPPGRGSE HYSGDSDASS PRSNCSDGMM DYSGPPSGPR RQNGYDTAYY SEAARESRPG 250 260 270 280 290 300 KSAAVSSLDC LSSIVERIST DSPAAPALLL ADAPPESPPG PPEGASLSDT EQGTQTPSPD 310 AAPQCPAGSN PNAIYQVL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of a single transfected cDNA converts fibroblasts to myoblasts." Davis R.L., Weintraub H., Lassar A.B. Cell 51:987-1000(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Characterisation of a genomic clone covering the structural mouse MyoD1 gene and its promoter region." Zingg J.-M., Alva G.P., Jost J.-P. Nucleic Acids Res. 19:6433-6439(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Myogenic lineage determination and differentiation: evidence for a regulatory gene pathway." Pinney D.F., Pearson-White S.H., Konieczny S.F., Latham K.E., Emerson C.P. Jr. Cell 53:781-793(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Head.
[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].
[6]	"MyoD1: a nuclear phosphoprotein requiring a Myc homology region to convert fibroblasts to myoblasts." Tapscott S.J., Davis R.L., Thayer M.J., Cheng P.-F., Weintraub H., Lassar A.B. Science 242:405-411(1988) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"The RNA helicases p68/p72 and the noncoding RNA SRA are coregulators of MyoD and skeletal muscle differentiation." Caretti G., Schiltz R.L., Dilworth F.J., Di Padova M., Zhao P., Ogryzko V., Fuller-Pace F.V., Hoffman E.P., Tapscott S.J., Sartorelli V. Dev. Cell 11:547-560(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DDX5.
[8]	"Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation." Ma P.C.M., Rould M.A., Weintraub H., Pabo C.O. Cell 77:451-459(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 102-166.
[9]	"The basic domain of myogenic basic helix-loop-helix (bHLH) proteins is the novel target for direct inhibition by another bHLH protein, Twist." Hamamori Y., Wu H.Y., Sartorelli V., Kedes L. Mol. Cell. Biol. 17:6563-6573(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INHIBITION BY TWIST.
[10]	"p300 is required for MyoD-dependent cell cycle arrest and muscle-specific gene transcription." Puri P.L., Avantaggiati M.L., Balsano C., Sang N., Graessmann A., Giordano A., Levrero M. EMBO J. 16:369-383(1997) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION.
[11]	"Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state." Fulco M., Schiltz R.L., Iezzi S., King M.T., Zhao P., Kashiwaya Y., Hoffman E., Veech R.L., Sartorelli V. Mol. Cell 12:51-62(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DEACETYLATION BY SIRT1.
[12]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M18779 mRNA. Translation: AAA39799.1.
X61655 Genomic DNA. Translation: CAA43836.1.
M84918 mRNA. Translation: AAA39798.1.
AK076157 mRNA. Translation: BAC36224.1.
AK142859 mRNA. Translation: BAE25213.1.
BC103613 mRNA. Translation: AAI03614.1.
BC103618 mRNA. Translation: AAI03619.1.
BC103619 mRNA. Translation: AAI03620.1.

IPI

IPI00137502.

PIR

A29636.

RefSeq

NP_034996.2. NM_010866.2.

UniGene

Mm.1526.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MDY	X-ray	2.80	A	102-166	[»]
			B/C/D	105-166	[»]

ProteinModelPortal

P10085.

SMR

P10085. Positions 102-166.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-37N.

IntAct

P10085. 9 interactions.

MINT

MINT-263097.

STRING

10090.ENSMUSP00000072330.

PTM databases

PhosphoSite

P10085.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000072514; ENSMUSP00000072330; ENSMUSG00000009471.

GeneID

17927.

KEGG

mmu:17927.

Organism-specific databases

CTD

4654.

MGI

MGI:97275. Myod1.

Phylogenomic databases

eggNOG

NOG292792.

GeneTree

ENSGT00530000063004.

HOGENOM

HOG000234800.

HOVERGEN

HBG006429.

InParanoid

Q8C6B1.

KO

K09064.

OMA

TYYSEAP.

OrthoDB

EOG47WNPM.

Enzyme and pathway databases

Reactome

REACT_127416. Developmental Biology.

Gene expression databases

Bgee

P10085.

CleanEx

MM_MYOD1.

Genevestigator

P10085.

GermOnline

ENSMUSG00000009471. Mus musculus.

Family and domain databases

Gene3D

4.10.280.10. 1 hit.

InterPro

IPR002546. Basic.
IPR011598. bHLH_dom.
IPR022032. Myf5.
[Graphical view]

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. BHLH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P10085.

NextBio

292797.

SOURCE

Search...

Entry information

Entry name

MYOD1_MOUSE

Accession

Primary (citable) accession number: P10085
Secondary accession number(s): Q8C6B1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program