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Protein

Twist-related protein 1

Gene

Twist1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a transcriptional regulator. Inhibits myogenesis by sequestrating E proteins, inhibiting trans-activation by MEF2, and inhibiting DNA-binding by MYOD1 through physical interaction. This interaction probably involves the basic domains of both proteins. Also represses expression of proinflammatory cytokines such as TNFA and IL1B. Regulates cranial suture patterning and fusion. Activates transcription as a heterodimer with E proteins. Regulates gene expression differentially, depending on dimer composition. Homodimers induce expression of FGFR2 and POSTN while heterodimers repress FGFR2 and POSTN expression and induce THBS1 expression. Heterodimerization is also required for osteoblast differentiation. Represses the activity of the circadian transcriptional activator: NPAS2-ARNTL/BMAL1 heterodimer.5 Publications

GO - Molecular functioni

  • bHLH transcription factor binding Source: MGI
  • E-box binding Source: UniProtKB
  • protein domain specific binding Source: MGI
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
  • sequence-specific DNA binding RNA polymerase II transcription factor activity Source: MGI
  • sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • transcription factor binding Source: BHF-UCL

GO - Biological processi

  • aortic valve morphogenesis Source: BHF-UCL
  • cardiac neural crest cell development involved in outflow tract morphogenesis Source: MGI
  • cardiac neural crest cell migration involved in outflow tract morphogenesis Source: MGI
  • cell differentiation Source: MGI
  • cell proliferation involved in heart valve development Source: BHF-UCL
  • cellular response to growth factor stimulus Source: Ensembl
  • cellular response to hypoxia Source: BHF-UCL
  • cranial suture morphogenesis Source: UniProtKB
  • embryonic camera-type eye formation Source: MGI
  • embryonic cranial skeleton morphogenesis Source: BHF-UCL
  • embryonic digit morphogenesis Source: MGI
  • embryonic forelimb morphogenesis Source: MGI
  • embryonic hindlimb morphogenesis Source: BHF-UCL
  • embryonic limb morphogenesis Source: MGI
  • embryonic skeletal system morphogenesis Source: MGI
  • endocardial cushion morphogenesis Source: MGI
  • eyelid development in camera-type eye Source: MGI
  • hindlimb morphogenesis Source: MGI
  • in utero embryonic development Source: MGI
  • mitral valve morphogenesis Source: BHF-UCL
  • muscle organ development Source: UniProtKB-KW
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of cell differentiation Source: UniProtKB
  • negative regulation of cellular senescence Source: MGI
  • negative regulation of DNA damage response, signal transduction by p53 class mediator Source: MGI
  • negative regulation of double-strand break repair Source: MGI
  • negative regulation of histone acetylation Source: BHF-UCL
  • negative regulation of histone phosphorylation Source: MGI
  • negative regulation of molecular function Source: MGI
  • negative regulation of osteoblast differentiation Source: MGI
  • negative regulation of oxidative phosphorylation uncoupler activity Source: BHF-UCL
  • negative regulation of peroxisome proliferator activated receptor signaling pathway Source: BHF-UCL
  • negative regulation of phosphatidylinositol 3-kinase signaling Source: MGI
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • negative regulation of skeletal muscle tissue development Source: MGI
  • negative regulation of striated muscle tissue development Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • negative regulation of tumor necrosis factor production Source: MGI
  • neural tube closure Source: MGI
  • neuron migration Source: MGI
  • odontogenesis Source: Ensembl
  • ossification Source: MGI
  • osteoblast differentiation Source: MGI
  • palate development Source: Ensembl
  • positive regulation of cell motility Source: BHF-UCL
  • positive regulation of DNA-templated transcription, initiation Source: MGI
  • positive regulation of endocardial cushion to mesenchymal transition involved in heart valve formation Source: BHF-UCL
  • positive regulation of epithelial cell proliferation Source: Ensembl
  • positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
  • positive regulation of fatty acid beta-oxidation Source: MGI
  • positive regulation of gene expression Source: MGI
  • positive regulation of interleukin-6 secretion Source: MGI
  • positive regulation of monocyte chemotactic protein-1 production Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of transcription regulatory region DNA binding Source: MGI
  • positive regulation of tumor necrosis factor production Source: MGI
  • regulation of bone mineralization Source: MGI
  • rhythmic process Source: UniProtKB-KW
  • transcription from RNA polymerase II promoter Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Repressor

Keywords - Biological processi

Biological rhythms, Differentiation, Myogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Twist-related protein 1
Alternative name(s):
M-twist
Gene namesi
Name:Twist1
Synonyms:Twist
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:98872. Twist1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi179 – 1791C → G: High transactivation activity. 1 Publication
Mutagenesisi185 – 1851E → D, K or R: High transactivation activity. 1 Publication
Mutagenesisi186 – 1861R → A or K: High transactivation activity. 1 Publication
Mutagenesisi187 – 1871L → G: Low transactivation activity. 1 Publication
Mutagenesisi188 – 1881S → A: High transactivation activity. 1 Publication
Mutagenesisi191 – 1911F → A, G or P: Low transactivation activity. 1 Publication
Mutagenesisi192 – 1921S → A: High transactivation activity. 1 Publication
Mutagenesisi192 – 1921S → P: Intermediate transactivation activity. 1 Publication
Mutagenesisi195 – 1951R → E: Intermediate transactivation activity. 1 Publication
Mutagenesisi195 – 1951R → G: Low transactivation activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 206206Twist-related protein 1PRO_0000127488Add
BLAST

Proteomic databases

PRIDEiP26687.

PTM databases

PhosphoSiteiP26687.

Miscellaneous databases

PMAP-CutDBP26687.

Expressioni

Tissue specificityi

Subset of mesodermal cells.1 Publication

Inductioni

By TNF-alpha.1 Publication

Gene expression databases

BgeeiP26687.
CleanExiMM_TWIST1.
GenevestigatoriP26687.

Interactioni

Subunit structurei

Efficient DNA binding requires dimerization with another bHLH protein. Homodimer or heterodimer with E proteins such as TCF3. ID1 binds preferentially to TCF3 but does not interact efficiently with TWIST1 so ID1 levels control the amount of TCF3 available to dimerize with TWIST1 and thus determine the type of dimer formed.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TP53P046374EBI-6123119,EBI-366083From a different organism.

Protein-protein interaction databases

BioGridi204385. 5 interactions.
IntActiP26687. 5 interactions.
STRINGi10090.ENSMUSP00000040089.

Structurei

3D structure databases

ProteinModelPortaliP26687.
SMRiP26687. Positions 113-171.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini112 – 16352bHLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni165 – 19531Sufficient for transactivation activityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi80 – 10223Gly-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG258515.
GeneTreeiENSGT00760000119097.
HOGENOMiHOG000261629.
InParanoidiP26687.
KOiK09069.
OMAiDRQPKRC.
OrthoDBiEOG7TJ3M9.
TreeFamiTF315153.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P26687-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMQDVSSSPV SPADDSLSNS EEEPDRQQPA SGKRGARKRR SSRRSAGGSA
60 70 80 90 100
GPGGATGGGI GGGDEPGSPA QGKRGKKSAG GGGGGGAGGG GGGGGGSSSG
110 120 130 140 150
GGSPQSYEEL QTQRVMANVR ERQRTQSLNE AFAALRKIIP TLPSDKLSKI
160 170 180 190 200
QTLKLAARYI DFLYQVLQSD ELDSKMASCS YVAHERLSYA FSVWRMEGAW

SMSASH
Length:206
Mass (Da):21,198
Last modified:August 1, 1992 - v1
Checksum:i618AD8E9BE87C555
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361A → R in AAA40515 (PubMed:1840517).Curated
Sequence conflicti91 – 911G → P in AAA40515 (PubMed:1840517).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63649 Genomic DNA. Translation: AAA40514.1.
M63650 mRNA. Translation: AAA40515.1.
BC033434 mRNA. Translation: AAH33434.1.
BC083139 mRNA. Translation: AAH83139.1.
CCDSiCCDS25879.1.
PIRiI53066.
RefSeqiNP_035788.1. NM_011658.2.
UniGeneiMm.3280.

Genome annotation databases

EnsembliENSMUST00000049089; ENSMUSP00000040089; ENSMUSG00000035799.
GeneIDi22160.
KEGGimmu:22160.
UCSCiuc007niw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63649 Genomic DNA. Translation: AAA40514.1.
M63650 mRNA. Translation: AAA40515.1.
BC033434 mRNA. Translation: AAH33434.1.
BC083139 mRNA. Translation: AAH83139.1.
CCDSiCCDS25879.1.
PIRiI53066.
RefSeqiNP_035788.1. NM_011658.2.
UniGeneiMm.3280.

3D structure databases

ProteinModelPortaliP26687.
SMRiP26687. Positions 113-171.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204385. 5 interactions.
IntActiP26687. 5 interactions.
STRINGi10090.ENSMUSP00000040089.

PTM databases

PhosphoSiteiP26687.

Proteomic databases

PRIDEiP26687.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049089; ENSMUSP00000040089; ENSMUSG00000035799.
GeneIDi22160.
KEGGimmu:22160.
UCSCiuc007niw.1. mouse.

Organism-specific databases

CTDi7291.
MGIiMGI:98872. Twist1.

Phylogenomic databases

eggNOGiNOG258515.
GeneTreeiENSGT00760000119097.
HOGENOMiHOG000261629.
InParanoidiP26687.
KOiK09069.
OMAiDRQPKRC.
OrthoDBiEOG7TJ3M9.
TreeFamiTF315153.

Miscellaneous databases

NextBioi302090.
PMAP-CutDBP26687.
PROiP26687.
SOURCEiSearch...

Gene expression databases

BgeeiP26687.
CleanExiMM_TWIST1.
GenevestigatoriP26687.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The M-twist gene of Mus is expressed in subsets of mesodermal cells and is closely related to the Xenopus X-twi and the Drosophila twist genes."
    Wolf C., Thisse C., Stoetzel C., Thisse B., Gerlinger P., Perrin-Schmitt F.
    Dev. Biol. 143:363-373(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
  2. "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].
    Strain: FVB/N.
    Tissue: Limb.
  3. "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: FUNCTION.
  4. "Twist regulates cytokine gene expression through a negative feedback loop that represses NF-kappaB activity."
    Sosic D., Richardson J.A., Yu K., Ornitz D.M., Olson E.N.
    Cell 112:169-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  5. "Histone acetyltransferase-dependent chromatin remodeling and the vascular clock."
    Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M., Chakravarti D., FitzGerald G.A., McNamara P.
    J. Biol. Chem. 279:7091-7097(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Twist1 dimer selection regulates cranial suture patterning and fusion."
    Connerney J., Andreeva V., Leshem Y., Muentener C., Mercado M.A., Spicer D.B.
    Dev. Dyn. 235:1345-1357(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  7. "Mechanism of transcriptional activation by the proto-oncogene Twist1."
    Laursen K.B., Mielke E., Iannaccone P., Fuchtbauer E.M.
    J. Biol. Chem. 282:34623-34633(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF CYS-179; GLU-185; ARG-186; LEU-187; SER-188; PHE-191; SER-192 AND ARG-195.

Entry informationi

Entry nameiTWST1_MOUSE
AccessioniPrimary (citable) accession number: P26687
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: May 27, 2015
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.