TWST1_MOUSE
ID TWST1_MOUSE Reviewed; 206 AA.
AC P26687;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Twist-related protein 1;
DE AltName: Full=M-twist;
GN Name=Twist1; Synonyms=Twist;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RX PubMed=1840517; DOI=10.1016/0012-1606(91)90086-i;
RA Wolf C., Thisse C., Stoetzel C., Thisse B., Gerlinger P.,
RA Perrin-Schmitt F.;
RT "The M-twist gene of Mus is expressed in subsets of mesodermal cells and is
RT closely related to the Xenopus X-twi and the Drosophila twist genes.";
RL Dev. Biol. 143:363-373(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Limb;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION.
RX PubMed=9343420; DOI=10.1128/mcb.17.11.6563;
RA Hamamori Y., Wu H.Y., Sartorelli V., Kedes L.;
RT "The basic domain of myogenic basic helix-loop-helix (bHLH) proteins is the
RT novel target for direct inhibition by another bHLH protein, Twist.";
RL Mol. Cell. Biol. 17:6563-6573(1997).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=12553906; DOI=10.1016/s0092-8674(03)00002-3;
RA Sosic D., Richardson J.A., Yu K., Ornitz D.M., Olson E.N.;
RT "Twist regulates cytokine gene expression through a negative feedback loop
RT that represses NF-kappaB activity.";
RL Cell 112:169-180(2003).
RN [5]
RP FUNCTION.
RX PubMed=14645221; DOI=10.1074/jbc.m311973200;
RA Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M.,
RA Chakravarti D., FitzGerald G.A., McNamara P.;
RT "Histone acetyltransferase-dependent chromatin remodeling and the vascular
RT clock.";
RL J. Biol. Chem. 279:7091-7097(2004).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=16502419; DOI=10.1002/dvdy.20717;
RA Connerney J., Andreeva V., Leshem Y., Muentener C., Mercado M.A.,
RA Spicer D.B.;
RT "Twist1 dimer selection regulates cranial suture patterning and fusion.";
RL Dev. Dyn. 235:1345-1357(2006).
RN [7]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF CYS-179; GLU-185; ARG-186; LEU-187;
RP SER-188; PHE-191; SER-192 AND ARG-195.
RX PubMed=17893140; DOI=10.1074/jbc.m707085200;
RA Laursen K.B., Mielke E., Iannaccone P., Fuchtbauer E.M.;
RT "Mechanism of transcriptional activation by the proto-oncogene Twist1.";
RL J. Biol. Chem. 282:34623-34633(2007).
RN [8]
RP INTERACTION WITH TCF3.
RX PubMed=23395635; DOI=10.1016/j.celrep.2013.01.017;
RA Davies O.R., Lin C.Y., Radzisheuskaya A., Zhou X., Taube J., Blin G.,
RA Waterhouse A., Smith A.J., Lowell S.;
RT "Tcf15 primes pluripotent cells for differentiation.";
RL Cell Rep. 3:472-484(2013).
CC -!- FUNCTION: Acts as a transcriptional regulator. Inhibits myogenesis by
CC sequestrating E proteins, inhibiting trans-activation by MEF2, and
CC inhibiting DNA-binding by MYOD1 through physical interaction. This
CC interaction probably involves the basic domains of both proteins. Also
CC represses expression of pro-inflammatory cytokines such as TNFA and
CC IL1B. Regulates cranial suture patterning and fusion. Activates
CC transcription as a heterodimer with E proteins. Regulates gene
CC expression differentially, depending on dimer composition. Homodimers
CC induce expression of FGFR2 and POSTN while heterodimers repress FGFR2
CC and POSTN expression and induce THBS1 expression. Heterodimerization is
CC also required for osteoblast differentiation. Represses the activity of
CC the circadian transcriptional activator: NPAS2-ARNTL/BMAL1 heterodimer.
CC {ECO:0000269|PubMed:12553906, ECO:0000269|PubMed:14645221,
CC ECO:0000269|PubMed:16502419, ECO:0000269|PubMed:17893140,
CC ECO:0000269|PubMed:9343420}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein (PubMed:16502419, PubMed:17893140). Homodimer or heterodimer
CC with E proteins such as TCF3 (PubMed:16502419, PubMed:17893140,
CC PubMed:23395635). ID1 binds preferentially to TCF3 but does not
CC interact efficiently with TWIST1 so ID1 levels control the amount of
CC TCF3 available to dimerize with TWIST1 and thus determine the type of
CC dimer formed (PubMed:16502419, PubMed:17893140).
CC {ECO:0000269|PubMed:16502419, ECO:0000269|PubMed:17893140,
CC ECO:0000269|PubMed:23395635}.
CC -!- INTERACTION:
CC P26687; Q9UN86: G3BP2; Xeno; NbExp=2; IntAct=EBI-6123119, EBI-1044298;
CC P26687; P04637: TP53; Xeno; NbExp=4; IntAct=EBI-6123119, EBI-366083;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Subset of mesodermal cells.
CC {ECO:0000269|PubMed:1840517}.
CC -!- INDUCTION: By TNF-alpha. {ECO:0000269|PubMed:12553906}.
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DR EMBL; M63649; AAA40514.1; -; Genomic_DNA.
DR EMBL; M63650; AAA40515.1; -; mRNA.
DR EMBL; BC033434; AAH33434.1; -; mRNA.
DR EMBL; BC083139; AAH83139.1; -; mRNA.
DR CCDS; CCDS25879.1; -.
DR PIR; I53066; I53066.
DR RefSeq; NP_035788.1; NM_011658.2.
DR AlphaFoldDB; P26687; -.
DR SMR; P26687; -.
DR BioGRID; 204385; 7.
DR DIP; DIP-61633N; -.
DR IntAct; P26687; 6.
DR STRING; 10090.ENSMUSP00000040089; -.
DR iPTMnet; P26687; -.
DR PhosphoSitePlus; P26687; -.
DR jPOST; P26687; -.
DR PaxDb; P26687; -.
DR PRIDE; P26687; -.
DR ProteomicsDB; 298339; -.
DR Antibodypedia; 11900; 649 antibodies from 39 providers.
DR DNASU; 22160; -.
DR Ensembl; ENSMUST00000049089; ENSMUSP00000040089; ENSMUSG00000035799.
DR GeneID; 22160; -.
DR KEGG; mmu:22160; -.
DR UCSC; uc007niw.1; mouse.
DR CTD; 7291; -.
DR MGI; MGI:98872; Twist1.
DR VEuPathDB; HostDB:ENSMUSG00000035799; -.
DR eggNOG; KOG4447; Eukaryota.
DR GeneTree; ENSGT00940000162831; -.
DR HOGENOM; CLU_112073_0_0_1; -.
DR InParanoid; P26687; -.
DR OMA; XSSSAGI; -.
DR OrthoDB; 1595261at2759; -.
DR PhylomeDB; P26687; -.
DR TreeFam; TF315153; -.
DR BioGRID-ORCS; 22160; 4 hits in 111 CRISPR screens.
DR ChiTaRS; Twist1; mouse.
DR PRO; PR:P26687; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P26687; protein.
DR Bgee; ENSMUSG00000035799; Expressed in pharyngeal arch 1 and 225 other tissues.
DR Genevisible; P26687; MM.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0043425; F:bHLH transcription factor binding; IPI:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; TAS:BHF-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:BHF-UCL.
DR GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL.
DR GO; GO:0061309; P:cardiac neural crest cell development involved in outflow tract morphogenesis; IMP:MGI.
DR GO; GO:0003253; P:cardiac neural crest cell migration involved in outflow tract morphogenesis; IMP:MGI.
DR GO; GO:2000793; P:cell proliferation involved in heart valve development; IMP:BHF-UCL.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IMP:BHF-UCL.
DR GO; GO:0060363; P:cranial suture morphogenesis; IMP:UniProtKB.
DR GO; GO:0032502; P:developmental process; IBA:GO_Central.
DR GO; GO:0060900; P:embryonic camera-type eye formation; ISO:MGI.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:BHF-UCL.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:BHF-UCL.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0003203; P:endocardial cushion morphogenesis; IMP:MGI.
DR GO; GO:0061029; P:eyelid development in camera-type eye; ISO:MGI.
DR GO; GO:0035137; P:hindlimb morphogenesis; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0003183; P:mitral valve morphogenesis; IMP:BHF-UCL.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IDA:UniProtKB.
DR GO; GO:2000773; P:negative regulation of cellular senescence; ISO:MGI.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; ISO:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:2000780; P:negative regulation of double-strand break repair; ISO:MGI.
DR GO; GO:0035067; P:negative regulation of histone acetylation; IDA:BHF-UCL.
DR GO; GO:0033128; P:negative regulation of histone phosphorylation; ISO:MGI.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; IGI:MGI.
DR GO; GO:0044092; P:negative regulation of molecular function; IDA:MGI.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:MGI.
DR GO; GO:2000276; P:negative regulation of oxidative phosphorylation uncoupler activity; IDA:BHF-UCL.
DR GO; GO:0035359; P:negative regulation of peroxisome proliferator activated receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; IDA:MGI.
DR GO; GO:0045843; P:negative regulation of striated muscle tissue development; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IGI:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0042476; P:odontogenesis; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; IMP:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR GO; GO:2000147; P:positive regulation of cell motility; IMP:BHF-UCL.
DR GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; ISO:MGI.
DR GO; GO:2000802; P:positive regulation of endocardial cushion to mesenchymal transition involved in heart valve formation; IDA:BHF-UCL.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0030500; P:regulation of bone mineralization; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0048863; P:stem cell differentiation; IMP:MGI.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR015789; Twist-related.
DR PANTHER; PTHR23349:SF64; PTHR23349:SF64; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Activator; Biological rhythms; Developmental protein; Differentiation;
KW DNA-binding; Myogenesis; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..206
FT /note="Twist-related protein 1"
FT /id="PRO_0000127488"
FT DOMAIN 112..163
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..195
FT /note="Sufficient for transactivation activity"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 179
FT /note="C->G: High transactivation activity."
FT /evidence="ECO:0000269|PubMed:17893140"
FT MUTAGEN 185
FT /note="E->D,K,R: High transactivation activity."
FT /evidence="ECO:0000269|PubMed:17893140"
FT MUTAGEN 186
FT /note="R->A,K: High transactivation activity."
FT /evidence="ECO:0000269|PubMed:17893140"
FT MUTAGEN 187
FT /note="L->G: Low transactivation activity."
FT /evidence="ECO:0000269|PubMed:17893140"
FT MUTAGEN 188
FT /note="S->A: High transactivation activity."
FT /evidence="ECO:0000269|PubMed:17893140"
FT MUTAGEN 191
FT /note="F->A,G,P: Low transactivation activity."
FT /evidence="ECO:0000269|PubMed:17893140"
FT MUTAGEN 192
FT /note="S->A: High transactivation activity."
FT /evidence="ECO:0000269|PubMed:17893140"
FT MUTAGEN 192
FT /note="S->P: Intermediate transactivation activity."
FT /evidence="ECO:0000269|PubMed:17893140"
FT MUTAGEN 195
FT /note="R->E: Intermediate transactivation activity."
FT /evidence="ECO:0000269|PubMed:17893140"
FT MUTAGEN 195
FT /note="R->G: Low transactivation activity."
FT /evidence="ECO:0000269|PubMed:17893140"
FT CONFLICT 36
FT /note="A -> R (in Ref. 1; AAA40515)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="G -> P (in Ref. 1; AAA40515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 206 AA; 21198 MW; 618AD8E9BE87C555 CRC64;
MMQDVSSSPV SPADDSLSNS EEEPDRQQPA SGKRGARKRR SSRRSAGGSA GPGGATGGGI
GGGDEPGSPA QGKRGKKSAG GGGGGGAGGG GGGGGGSSSG GGSPQSYEEL QTQRVMANVR
ERQRTQSLNE AFAALRKIIP TLPSDKLSKI QTLKLAARYI DFLYQVLQSD ELDSKMASCS
YVAHERLSYA FSVWRMEGAW SMSASH
