Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9D030 (TWST2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Twist-related protein 2
Alternative name(s):
Dermis-expressed protein 1
Short name=Dermo-1
Gene names
Name:Twist2
Synonyms:Dermo1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length160 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to the E-box consensus sequence 5'-CANNTG-3' as a heterodimer and inhibits transcriptional activation by MYOD1, MYOG, MEF2A and MEF2C. Also represses expression of proinflammatory cytokines such as TNFA and IL1B. Involved in postnatal glycogen storage and energy metabolism. Inhibits the premature or ectopic differentiation of preosteoblast cells during osteogenesis, possibly by changing the internal signal transduction response of osteoblasts to external growth factors By similarity. Ref.1 Ref.3 Ref.4

Subunit structure

Efficient DNA binding requires dimerization with another bHLH protein. Forms a heterodimer with TCF3/E12. Also interacts with MEF2C. Ref.1 Ref.3

Subcellular location

Nucleus. Cytoplasm. Note: Mainly nuclear during embryonic development. Cytoplasmic in adult tissues. Ref.3

Tissue specificity

Expressed at low levels in sclerotome and dermatome of somites, and in limb buds at 10.5 dpc. Accumulates predominantly in dermatome, prevertebrae and derivatives of branchial arches by 13 dpc. Also expressed near surface of embryo and in chondrogenic cells. In adult, expressed at low levels in skin, bladder, uterus, aorta and heart. Ref.1

Developmental stage

In the embryo, expression is detected at 10.5 dpc, increases continuously through to 17.5 dpc and is also high in neonates. Down-regulated in adults. Ref.1

Induction

By TNF-alpha. Ref.4

Domain

The C-terminal and HLH domains are essential for transcriptional repression. Ref.3

Sequence similarities

Contains 1 bHLH (basic helix-loop-helix) domain.

Ontologies

Keywords
   Biological processDifferentiation
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   LigandDNA-binding
   Molecular functionDevelopmental protein
Repressor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcornea development in camera-type eye

Inferred from mutant phenotype PubMed 20574024. Source: MGI

embryonic cranial skeleton morphogenesis

Inferred from genetic interaction PubMed 15030764. Source: MGI

face morphogenesis

Inferred from mutant phenotype PubMed 20574024PubMed 20691403. Source: MGI

negative regulation of DNA binding

Inferred from direct assay PubMed 14654692. Source: MGI

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 19090621. Source: MGI

negative regulation of molecular function

Inferred from direct assay PubMed 15030764. Source: MGI

negative regulation of myeloid cell differentiation

Inferred from mutant phenotype PubMed 19090621. Source: MGI

negative regulation of osteoblast differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 16831897. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: UniProtKB

negative regulation of tumor necrosis factor production

Inferred from mutant phenotype PubMed 16831897. Source: MGI

osteoblast differentiation

Inferred from mutant phenotype PubMed 15030764. Source: MGI

positive regulation of keratinocyte proliferation

Inferred from mutant phenotype PubMed 20574024. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1. Source: MGI

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 14654692. Source: GOC

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

transcription factor complex

Inferred from physical interaction Ref.1. Source: MGI

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II transcription factor binding transcription factor activity

Inferred from direct assay PubMed 14654692. Source: MGI

chromatin binding

Inferred from direct assay PubMed 16831897. Source: MGI

protein binding

Inferred from physical interaction PubMed 20655471. Source: IntAct

protein domain specific binding

Inferred from physical interaction PubMed 15030764. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Runx2Q087752EBI-2903190,EBI-903354

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 160160Twist-related protein 2
PRO_0000127490

Regions

Domain66 – 11752bHLH

Experimental info

Mutagenesis861F → P: Abrogates transcriptional repression of MYOD1. Ref.3
Sequence conflict1451Y → F in BAB27885. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9D030 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 6394750916940C12

FASTA16018,140
        10         20         30         40         50         60 
MEEGSSSPVS PVDSLGTSEE ELERQPKRFG RKRRYSKKSS EDGSPTPGKR GKKGSPSAQS 

        70         80         90        100        110        120 
FEELQSQRIL ANVRERQRTQ SLNEAFAALR KIIPTLPSDK LSKIQTLKLA ARYIDFLYQV 

       130        140        150        160 
LQSDEMDNKM TSCSYVAHER LSYAYSVWRM EGAWSMSASH 

« Hide

References

« Hide 'large scale' references
[1]"Dermo-1: a novel twist-related bHLH protein expressed in the developing dermis."
Li L., Cserjesi P., Olson E.N.
Dev. Biol. 172:280-292(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBUNIT.
Strain: Swiss.
Tissue: Brain and Embryonic head.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
[3]"Dermo-1, a multifunctional basic helix-loop-helix protein, represses MyoD transactivation via the HLH domain, MEF2 interaction, and chromatin deacetylation."
Gong X.Q., Li L.
J. Biol. Chem. 277:12310-12317(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-86.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U36384 mRNA. Translation: AAC52319.1.
AK011861 mRNA. Translation: BAB27885.1.
AK011180 mRNA. Translation: BAB27450.1.
CCDSCCDS15166.1.
RefSeqNP_031881.1. NM_007855.2.
UniGeneMm.9474.

3D structure databases

ProteinModelPortalQ9D030.
SMRQ9D030. Positions 67-125.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199209. 1 interaction.
IntActQ9D030. 1 interaction.

PTM databases

PhosphoSiteQ9D030.

Proteomic databases

PRIDEQ9D030.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID13345.
KEGGmmu:13345.

Organism-specific databases

CTD117581.
MGIMGI:104685. Twist2.

Phylogenomic databases

eggNOGNOG258515.
HOGENOMHOG000261629.
HOVERGENHBG019071.
InParanoidQ9D030.
KOK09069.
PhylomeDBQ9D030.

Gene expression databases

CleanExMM_TWIST2.
GenevestigatorQ9D030.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
[Graphical view]
PfamPF00010. HLH. 1 hit.
[Graphical view]
SMARTSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio283658.
PROQ9D030.
SOURCESearch...

Entry information

Entry nameTWST2_MOUSE
AccessionPrimary (citable) accession number: Q9D030
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot