TWST1_PANTR
ID TWST1_PANTR Reviewed; 201 AA.
AC Q8MI03;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Twist-related protein 1;
GN Name=TWIST1; Synonyms=TWIST;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Hair;
RX PubMed=12523351; DOI=10.1007/s00427-002-0263-y;
RA Gachot-Neveu H., Stoetzel C., Quillet R., Dollfus H., Perrin-Schmitt F.;
RT "Natural Twist protein variants in a panel of eleven non-human primates:
RT possible implications of Twist gene-tree for primate species tree.";
RL Dev. Genes Evol. 212:496-503(2002).
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 (By similarity). {ECO:0000250|UniProtKB:P26687}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Homodimer or heterodimer with E proteins such as TCF3. ID1
CC binds preferentially to TCF3 but does not interact efficiently with
CC TWIST1 so ID1 levels control the amount of TCF3 available to dimerize
CC with TWIST and thus determine the type of dimer formed (By similarity).
CC {ECO:0000250|UniProtKB:P26687}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
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DR EMBL; AJ488168; CAD32482.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8MI03; -.
DR SMR; Q8MI03; -.
DR PaxDb; Q8MI03; -.
DR PRIDE; Q8MI03; -.
DR eggNOG; KOG4447; Eukaryota.
DR InParanoid; Q8MI03; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0032502; P:developmental process; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
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 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 3: Inferred from homology;
KW Activator; Biological rhythms; Developmental protein; Differentiation;
KW DNA-binding; Myogenesis; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..201
FT /note="Twist-related protein 1"
FT /id="PRO_0000127486"
FT DOMAIN 109..160
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..190
FT /note="Sufficient for transactivation activity"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 201 AA; 20762 MW; B63D192CADB0242D CRC64;
MMQDVSSSPV SPADDSLSNS EEEPDRQQPP SGKRGGRKRR SSRRSAGGGA GPGGAAGGGV
GGGDEPGSPA QGKRGKKSAG CGGGGGGGAG GGGSSSGGGS PQSYEELQTQ RVMANVRERQ
RTQSLNEAFA ALPKIIPTLP SDKLSKIQTL KLAARYIDFL YQVLQSDELD SKMASYVAHE
RLSYAFSVWR MEGAWSMSAS H