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Twist-related protein 1 (Class A basic helix-loop-helix protein 38) (bHLHa38) (H-twist)

 TWST1_HUMAN             Reviewed;         202 AA.
Q15672; A4D128; Q92487; Q99804;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
12-SEP-2018, entry version 192.
RecName: Full=Twist-related protein 1;
AltName: Full=Class A basic helix-loop-helix protein 38;
Short=bHLHa38;
AltName: Full=H-twist;
Name=TWIST1; Synonyms=BHLHA38, TWIST;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Lung;
PubMed=9073070; DOI=10.1016/S0378-1119(96)00727-5;
Wang S.M., Coljee V.W., Pignolo R.J., Rotenberg M.O., Cristofalo V.J.,
Sierra F.;
"Cloning of the human twist gene: its expression is retained in adult
mesodermally-derived tissues.";
Gene 187:83-92(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=8995765; DOI=10.1007/s003359900269;
Bourgeois P., Stoetzel C., Bolcato-Bellemin A.-L., Mattei M.-G.,
Perrin-Schmitt F.;
"The human H-twist gene is located at 7p21 and encodes a B-HLH protein
that is 96% similar to its murine M-twist counterpart.";
Mamm. Genome 7:915-917(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SCS PRO-119;
ALA-ALA-LEU-ARG-LYS-ILE-ILE-135 INS AND
LYS-ILE-ILE-PRO-THR-LEU-PRO-139 INS.
PubMed=8988166; DOI=10.1038/ng0197-36;
Howard T.D., Paznekas W.A., Green E.D., Chiang L.C., Ma N.,
Ortiz de Luna R.I., Delgado C.G., Gonzalez-Ramos M., Kline A.D.,
Jabs E.W.;
"Mutations in TWIST, a basic helix-loop-helix transcription factor, in
Saethre-Chotzen syndrome.";
Nat. Genet. 15:36-41(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9215678; DOI=10.1093/hmg/6.7.1079;
Krebs I., Weis I., Hudler M., Rommens J.M., Roth H., Scherer S.W.,
Tsui L.-C., Fuchtbauer E.-M., Grzeschik K.-H., Tsuji K., Kunz J.;
"Translocation breakpoint maps 5 kb 3-prime from TWIST in a patient
affected with Saethre-Chotzen syndrome.";
Hum. Mol. Genet. 6:1079-1086(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION.
PubMed=12553906; DOI=10.1016/S0092-8674(03)00002-3;
Sosic D., Richardson J.A., Yu K., Ornitz D.M., Olson E.N.;
"Twist regulates cytokine gene expression through a negative feedback
loop that represses NF-kappaB activity.";
Cell 112:169-180(2003).
[9]
VARIANTS SCS PRO-131 AND LYS-ILE-ILE-PRO-THR-LEU-PRO-139 INS.
PubMed=8988167; DOI=10.1038/ng0197-42;
el Ghouzzi V., le Merrer M., Perrin-Schmitt F., Lajeunie E., Benit P.,
Renier D., Bourgeois P., Bolcato-Bellemin A.-L., Munnich A.,
Bonaventure J.;
"Mutations of the TWIST gene in the Saethre-Chotzen syndrome.";
Nat. Genet. 15:42-46(1997).
[10]
INVOLVEMENT IN RSS.
PubMed=10465122;
Kunz J., Hudler M., Fritz B.;
"Identification of a frameshift mutation in the gene TWIST in a family
affected with Robinow-Sorauf syndrome.";
J. Med. Genet. 36:650-652(1999).
[11]
VARIANT SCS VAL-156.
PubMed=11754069; DOI=10.1002/ajmg.10065;
Seto M.L., Lee S.J., Sze R.W., Cunningham M.L.;
"Another TWIST on Baller-Gerold syndrome.";
Am. J. Med. Genet. 104:323-330(2001).
[12]
VARIANTS CRS1 THR-186 AND LEU-188.
PubMed=17343269; DOI=10.1002/ajmg.a.31630;
Seto M.L., Hing A.V., Chang J., Hu M., Kapp-Simon K.A., Patel P.K.,
Burton B.K., Kane A.A., Smyth M.D., Hopper R., Ellenbogen R.G.,
Stevenson K., Speltz M.L., Cunningham M.L.;
"Isolated sagittal and coronal craniosynostosis associated with TWIST
box mutations.";
Am. J. Med. Genet. A 143:678-686(2007).
[13]
VARIANTS SER-83 AND GLY-95, FUNCTION, AND CHARACTERIZATION OF VARIANTS
SER-83 AND GLY-95.
PubMed=25981568; DOI=10.1007/s00246-015-1202-9;
Deng X., Pan H., Wang J., Wang B., Cheng Z., Cheng L., Zhao L., Li H.,
Ma X.;
"Functional analysis of two novel mutations in TWIST1 protein motifs
found in ventricular septal defect patients.";
Pediatr. Cardiol. 36:1602-1609(2015).
[14]
INVOLVEMENT IN SWCOS, AND VARIANTS SWCOS GLY-117 AND VAL-117.
PubMed=28369379; DOI=10.1093/hmg/ddx107;
Kim S., Twigg S.R.F., Scanlon V.A., Chandra A., Hansen T.J.,
Alsubait A., Fenwick A.L., McGowan S.J., Lord H., Lester T.,
Sweeney E., Weber A., Cox H., Wilkie A.O.M., Golden A., Corsi A.K.;
"Localized TWIST1 and TWIST2 basic domain substitutions cause four
distinct human diseases that can be modeled in Caenorhabditis
elegans.";
Hum. Mol. Genet. 26:2118-2132(2017).
-!- FUNCTION: 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 (By
similarity). {ECO:0000250|UniProtKB:P26687,
ECO:0000269|PubMed:12553906, ECO:0000269|PubMed:25981568}.
-!- SUBUNIT: 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 (By similarity). {ECO:0000250|UniProtKB:P26687}.
-!- INTERACTION:
O60885:BRD4; NbExp=7; IntAct=EBI-1797287, EBI-723869;
O60885-1:BRD4; NbExp=9; IntAct=EBI-1797287, EBI-9345088;
P15036:ETS2; NbExp=2; IntAct=EBI-1797287, EBI-1646991;
Q9UN86:G3BP2; NbExp=2; IntAct=EBI-1797287, EBI-1044298;
Q92831:KAT2B; NbExp=2; IntAct=EBI-1797287, EBI-477430;
Q92993:KAT5; NbExp=2; IntAct=EBI-1797287, EBI-399080;
Q9NQR1:KMT5A; NbExp=5; IntAct=EBI-1797287, EBI-1268946;
P15884:TCF4; NbExp=3; IntAct=EBI-1797287, EBI-533224;
P04637:TP53; NbExp=10; IntAct=EBI-1797287, EBI-366083;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: Subset of mesodermal cells.
-!- DISEASE: Saethre-Chotzen syndrome (SCS) [MIM:101400]: A
craniosynostosis syndrome characterized by coronal synostosis,
brachycephaly, low frontal hairline, facial asymmetry,
hypertelorism, broad halluces, and clinodactyly.
{ECO:0000269|PubMed:11754069, ECO:0000269|PubMed:8988166,
ECO:0000269|PubMed:8988167}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Robinow-Sorauf syndrome (RSS) [MIM:180750]: An autosomal
dominant syndrome characterized by craniosynostosis, asymmetry of
orbits, flat face, hypertelorism, a thin, long, and pointed nose,
shallow orbits, strabismus, and broad great toes with a
duplication of the distal phalanx. RSS is clinically similar to
Saethre-Chotzen syndrome, with the most characteristic additional
feature in Robinow-Sorauf syndrome being a bifid or partially
duplicated hallux. {ECO:0000269|PubMed:10465122}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Craniosynostosis 1 (CRS1) [MIM:123100]: A primary
abnormality of skull growth involving premature fusion of one or
more cranial sutures. The growth velocity of the skull often
cannot match that of the developing brain resulting in an abnormal
head shape and, in some cases, increased intracranial pressure,
which must be treated promptly to avoid permanent
neurodevelopmental disability. {ECO:0000269|PubMed:17343269}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Sweeney-Cox syndrome (SWCOS) [MIM:617746]: An autosomal
dominant syndrome characterized by facial dysostosis, including
hypertelorism, deficiencies of the eyelids and facial bones, cleft
palate/velopharyngeal insufficiency, and low-set cupped ears.
{ECO:0000269|PubMed:28369379}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TWIST1ID44296ch7p21.html";
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EMBL; X91662; CAA62850.1; -; Genomic_DNA.
EMBL; X99268; CAA67664.1; -; mRNA.
EMBL; U80998; AAC50930.1; -; Genomic_DNA.
EMBL; Y10871; CAA71821.1; -; Genomic_DNA.
EMBL; AC003986; AAC60381.2; -; Genomic_DNA.
EMBL; CH236948; EAL24279.1; -; Genomic_DNA.
EMBL; BC036704; AAH36704.1; -; mRNA.
CCDS; CCDS5367.1; -.
PIR; G01204; G01204.
RefSeq; NP_000465.1; NM_000474.3.
RefSeq; XP_011513798.1; XM_011515496.1.
UniGene; Hs.644998; -.
UniGene; Hs.66744; -.
PDB; 2MJV; NMR; -; A=68-79.
PDBsum; 2MJV; -.
ProteinModelPortal; Q15672; -.
SMR; Q15672; -.
BioGrid; 113142; 42.
DIP; DIP-45974N; -.
IntAct; Q15672; 26.
MINT; Q15672; -.
STRING; 9606.ENSP00000242261; -.
iPTMnet; Q15672; -.
PhosphoSitePlus; Q15672; -.
BioMuta; TWIST1; -.
DMDM; 2498009; -.
PaxDb; Q15672; -.
PeptideAtlas; Q15672; -.
PRIDE; Q15672; -.
ProteomicsDB; 60700; -.
DNASU; 7291; -.
Ensembl; ENST00000242261; ENSP00000242261; ENSG00000122691.
GeneID; 7291; -.
KEGG; hsa:7291; -.
UCSC; uc003sum.3; human.
CTD; 7291; -.
DisGeNET; 7291; -.
EuPathDB; HostDB:ENSG00000122691.12; -.
GeneCards; TWIST1; -.
GeneReviews; TWIST1; -.
HGNC; HGNC:12428; TWIST1.
MalaCards; TWIST1; -.
MIM; 101400; phenotype.
MIM; 123100; phenotype.
MIM; 180750; phenotype.
MIM; 601622; gene.
MIM; 617746; phenotype.
neXtProt; NX_Q15672; -.
OpenTargets; ENSG00000122691; -.
Orphanet; 35099; Isolated brachycephaly.
Orphanet; 35093; Isolated scaphocephaly.
Orphanet; 794; Saethre-Chotzen syndrome.
PharmGKB; PA37088; -.
eggNOG; KOG4447; Eukaryota.
eggNOG; ENOG4111QFU; LUCA.
GeneTree; ENSGT00760000119097; -.
HOGENOM; HOG000261629; -.
InParanoid; Q15672; -.
KO; K09069; -.
OMA; DRQPKRC; -.
OrthoDB; EOG091G07PB; -.
PhylomeDB; Q15672; -.
TreeFam; TF315153; -.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
Reactome; R-HSA-8878166; Transcriptional regulation by RUNX2.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
SignaLink; Q15672; -.
SIGNOR; Q15672; -.
ChiTaRS; TWIST1; human.
GeneWiki; Twist_transcription_factor; -.
GenomeRNAi; 7291; -.
PRO; PR:Q15672; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000122691; Expressed in 200 organ(s), highest expression level in testis.
CleanEx; HS_TWIST1; -.
ExpressionAtlas; Q15672; baseline and differential.
Genevisible; Q15672; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043425; F:bHLH transcription factor binding; IPI:BHF-UCL.
GO; GO:0070888; F:E-box binding; IDA:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL.
GO; GO:0003253; P:cardiac neural crest cell migration involved in outflow tract morphogenesis; IEA:Ensembl.
GO; GO:2000793; P:cell proliferation involved in heart valve development; IMP:BHF-UCL.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IMP:BHF-UCL.
GO; GO:0060363; P:cranial suture morphogenesis; TAS:BHF-UCL.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0060900; P:embryonic camera-type eye formation; IMP:BHF-UCL.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:BHF-UCL.
GO; GO:0042733; P:embryonic digit morphogenesis; TAS:BHF-UCL.
GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
GO; GO:0003203; P:endocardial cushion morphogenesis; IEA:Ensembl.
GO; GO:0061029; P:eyelid development in camera-type eye; IMP:BHF-UCL.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0003183; P:mitral valve morphogenesis; IEA:Ensembl.
GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:2000773; P:negative regulation of cellular senescence; IMP:BHF-UCL.
GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:BHF-UCL.
GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IEA:Ensembl.
GO; GO:2000780; P:negative regulation of double-strand break repair; IMP:BHF-UCL.
GO; GO:0035067; P:negative regulation of histone acetylation; IEA:Ensembl.
GO; GO:0033128; P:negative regulation of histone phosphorylation; IMP:BHF-UCL.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:BHF-UCL.
GO; GO:2000276; P:negative regulation of oxidative phosphorylation uncoupler activity; IEA:Ensembl.
GO; GO:0035359; P:negative regulation of peroxisome proliferator activated receptor signaling pathway; IEA:Ensembl.
GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IMP:BHF-UCL.
GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0042476; P:odontogenesis; IEA:Ensembl.
GO; GO:0001503; P:ossification; TAS:BHF-UCL.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0042473; P:outer ear morphogenesis; TAS:BHF-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; NAS:BHF-UCL.
GO; GO:2000147; P:positive regulation of cell motility; IMP:BHF-UCL.
GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IDA:CACAO.
GO; GO:2000802; P:positive regulation of endocardial cushion to mesenchymal transition involved in heart valve formation; IEA:Ensembl.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IMP:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IMP:BHF-UCL.
GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IMP:BHF-UCL.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:BHF-UCL.
GO; GO:0030500; P:regulation of bone mineralization; IMP:BHF-UCL.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR015789; Twist-related.
PANTHER; PTHR23349:SF64; PTHR23349:SF64; 1.
Pfam; PF00010; HLH; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
3D-structure; Activator; Biological rhythms; Complete proteome;
Craniosynostosis; Developmental protein; Differentiation;
Disease mutation; DNA-binding; Myogenesis; Nucleus; Polymorphism;
Reference proteome; Repressor; Transcription;
Transcription regulation.
CHAIN 1 202 Twist-related protein 1.
/FTId=PRO_0000127483.
DOMAIN 108 159 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 161 191 Sufficient for transactivation activity.
{ECO:0000250}.
COMPBIAS 80 98 Gly-rich.
VARIANT 83 83 G -> S (found in a patient with non-
syndromic ventricular septal defect;
unknown pathological significance; loss
of function in negative regulation of
transcription from E-cadherin promoter;
dbSNP:rs545987863).
{ECO:0000269|PubMed:25981568}.
/FTId=VAR_077470.
VARIANT 95 95 S -> G (rare polymorphism; no effect on
negative regulation of transcription from
E-cadherin promoter; dbSNP:rs575299986).
{ECO:0000269|PubMed:25981568}.
/FTId=VAR_077471.
VARIANT 117 117 E -> G (in SWCOS).
{ECO:0000269|PubMed:28369379}.
/FTId=VAR_080515.
VARIANT 117 117 E -> V (in SWCOS).
{ECO:0000269|PubMed:28369379}.
/FTId=VAR_080516.
VARIANT 119 119 Q -> P (in SCS; dbSNP:rs104894057).
{ECO:0000269|PubMed:8988166}.
/FTId=VAR_004495.
VARIANT 131 131 L -> P (in SCS; dbSNP:rs121909189).
{ECO:0000269|PubMed:8988167}.
/FTId=VAR_004496.
VARIANT 135 135 I -> IAALRKII (in SCS).
/FTId=VAR_004497.
VARIANT 139 139 P -> PKIIPTLP (in SCS).
/FTId=VAR_004498.
VARIANT 156 156 I -> V (in SCS; variant form with
features overlapping Baller-Gerold
syndrome; dbSNP:rs104894059).
{ECO:0000269|PubMed:11754069}.
/FTId=VAR_015219.
VARIANT 186 186 A -> T (in CRS1; dbSNP:rs121909190).
{ECO:0000269|PubMed:17343269}.
/FTId=VAR_034985.
VARIANT 188 188 S -> L (in CRS1; dbSNP:rs121909191).
{ECO:0000269|PubMed:17343269}.
/FTId=VAR_034986.
CONFLICT 32 32 G -> A (in Ref. 2; CAA67664).
{ECO:0000305}.
CONFLICT 36 36 G -> A (in Ref. 2; CAA67664).
{ECO:0000305}.
CONFLICT 41 41 S -> T (in Ref. 1; CAA62850 and 4;
CAA71821). {ECO:0000305}.
CONFLICT 45 45 S -> T (in Ref. 1; CAA62850 and 4;
CAA71821). {ECO:0000305}.
CONFLICT 56 56 Missing (in Ref. 1; CAA62850 and 4;
CAA71821). {ECO:0000305}.
CONFLICT 59 59 G -> A (in Ref. 2; CAA67664).
{ECO:0000305}.
CONFLICT 92 92 G -> GGGGG (in Ref. 2; CAA67664).
{ECO:0000305}.
SEQUENCE 202 AA; 20954 MW; 9394E4351BA1D081 CRC64;
MMQDVSSSPV SPADDSLSNS EEEPDRQQPP SGKRGGRKRR SSRRSAGGGA GPGGAAGGGV
GGGDEPGSPA QGKRGKKSAG CGGGGGAGGG GGSSSGGGSP QSYEELQTQR VMANVRERQR
TQSLNEAFAA LRKIIPTLPS DKLSKIQTLK LAARYIDFLY QVLQSDELDS KMASCSYVAH
ERLSYAFSVW RMEGAWSMSA SH


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