TWST2_MOUSE
ID TWST2_MOUSE Reviewed; 160 AA.
AC Q9D030;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Twist-related protein 2;
DE AltName: Full=Dermis-expressed protein 1;
DE Short=Dermo-1;
GN Name=Twist2; Synonyms=Dermo1;
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 {ECO:0000312|EMBL:BAB27885.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND SUBUNIT.
RC STRAIN=SWR/J {ECO:0000269|PubMed:7589808};
RC TISSUE=Brain {ECO:0000269|PubMed:7589808}, and
RC Embryonic head {ECO:0000269|PubMed:7589808};
RX PubMed=7589808; DOI=10.1006/dbio.1995.0023;
RA Li L., Cserjesi P., Olson E.N.;
RT "Dermo-1: a novel twist-related bHLH protein expressed in the developing
RT dermis.";
RL Dev. Biol. 172:280-292(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-86.
RX PubMed=11809751; DOI=10.1074/jbc.m110228200;
RA Gong X.Q., Li L.;
RT "Dermo-1, a multifunctional basic helix-loop-helix protein, represses MyoD
RT transactivation via the HLH domain, MEF2 interaction, and chromatin
RT deacetylation.";
RL J. Biol. Chem. 277:12310-12317(2002).
RN [4] {ECO:0000305}
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).
CC -!- FUNCTION: Binds to the E-box consensus sequence 5'-CANNTG-3' as a
CC heterodimer and inhibits transcriptional activation by MYOD1, MYOG,
CC MEF2A and MEF2C. Also represses expression of pro-inflammatory
CC cytokines such as TNFA and IL1B. Involved in postnatal glycogen storage
CC and energy metabolism. Inhibits the premature or ectopic
CC differentiation of preosteoblast cells during osteogenesis, possibly by
CC changing the internal signal transduction response of osteoblasts to
CC external growth factors (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11809751, ECO:0000269|PubMed:12553906,
CC ECO:0000269|PubMed:7589808}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Forms a heterodimer with TCF3/E12. Also interacts with MEF2C.
CC {ECO:0000269|PubMed:7589808}.
CC -!- INTERACTION:
CC Q9D030; Q08775: Runx2; NbExp=2; IntAct=EBI-2903190, EBI-903354;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:11809751}. Cytoplasm {ECO:0000269|PubMed:11809751}.
CC Note=Mainly nuclear during embryonic development. Cytoplasmic in adult
CC tissues.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in sclerotome and dermatome
CC of somites, and in limb buds at 10.5 dpc. Accumulates predominantly in
CC dermatome, prevertebrae and derivatives of branchial arches by 13 dpc.
CC Also expressed near surface of embryo and in chondrogenic cells. In
CC adult, expressed at low levels in skin, bladder, uterus, aorta and
CC heart. {ECO:0000269|PubMed:7589808}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, expression is detected at 10.5 dpc,
CC increases continuously through to 17.5 dpc and is also high in
CC neonates. Down-regulated in adults. {ECO:0000269|PubMed:7589808}.
CC -!- INDUCTION: By TNF-alpha. {ECO:0000269|PubMed:12553906}.
CC -!- DOMAIN: The C-terminal and HLH domains are essential for
CC transcriptional repression. {ECO:0000269|PubMed:11809751}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U36384; AAC52319.1; -; mRNA.
DR EMBL; AK011861; BAB27885.1; -; mRNA.
DR EMBL; AK011180; BAB27450.1; -; mRNA.
DR RefSeq; NP_031881.1; NM_007855.3.
DR AlphaFoldDB; Q9D030; -.
DR SMR; Q9D030; -.
DR BioGRID; 199209; 1.
DR IntAct; Q9D030; 1.
DR STRING; 10090.ENSMUSP00000139531; -.
DR iPTMnet; Q9D030; -.
DR PhosphoSitePlus; Q9D030; -.
DR jPOST; Q9D030; -.
DR PaxDb; Q9D030; -.
DR PRIDE; Q9D030; -.
DR ProteomicsDB; 298068; -.
DR DNASU; 13345; -.
DR GeneID; 13345; -.
DR KEGG; mmu:13345; -.
DR CTD; 117581; -.
DR MGI; MGI:104685; Twist2.
DR eggNOG; KOG4447; Eukaryota.
DR InParanoid; Q9D030; -.
DR OrthoDB; 1595261at2759; -.
DR PhylomeDB; Q9D030; -.
DR BioGRID-ORCS; 13345; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q9D030; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D030; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IPI:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
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:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0061303; P:cornea development in camera-type eye; IMP:MGI.
DR GO; GO:0032502; P:developmental process; IBA:GO_Central.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IGI:MGI.
DR GO; GO:0060325; P:face morphogenesis; IMP:MGI.
DR GO; GO:0043616; P:keratinocyte proliferation; IMP:MGI.
DR GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:MGI.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; IMP:MGI.
DR GO; GO:0044092; P:negative regulation of molecular function; IDA:MGI.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IMP:MGI.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
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; IMP:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA: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:SF70; PTHR23349:SF70; 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 Cytoplasm; Developmental protein; Differentiation; DNA-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..160
FT /note="Twist-related protein 2"
FT /id="PRO_0000127490"
FT DOMAIN 66..117
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 86
FT /note="F->P: Abrogates transcriptional repression of
FT MYOD1."
FT /evidence="ECO:0000269|PubMed:11809751"
FT CONFLICT 145
FT /note="Y -> F (in Ref. 2; BAB27885)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 160 AA; 18140 MW; 6394750916940C12 CRC64;
MEEGSSSPVS PVDSLGTSEE ELERQPKRFG RKRRYSKKSS EDGSPTPGKR GKKGSPSAQS
FEELQSQRIL ANVRERQRTQ SLNEAFAALR KIIPTLPSDK LSKIQTLKLA ARYIDFLYQV
LQSDEMDNKM TSCSYVAHER LSYAYSVWRM EGAWSMSASH
