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Protein

Twisted gastrulation protein homolog 1

Gene

Twsg1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in dorsoventral axis formation. Seems to antagonize BMP signaling by forming ternary complexes with CHRD and BMPs, thereby preventing BMPs from binding to their receptors. In addition to the anti-BMP function, also has pro-BMP activity, partly mediated by cleavage and degradation of CHRD, which releases BMPs from ternary complexes. May be an important modulator of BMP-regulated cartilage development and chondrocyte differentiation. May play a role in thymocyte development.4 Publications

GO - Biological processi

  • BMP signaling pathway Source: MGI
  • camera-type eye development Source: MGI
  • cell differentiation Source: MGI
  • forebrain development Source: MGI
  • hemopoiesis Source: MGI
  • mesoderm formation Source: MGI
  • negative regulation of BMP signaling pathway Source: MGI
  • negative regulation of osteoblast differentiation Source: MGI
  • ossification Source: MGI
  • positive regulation of BMP signaling pathway Source: MGI
  • salivary gland morphogenesis Source: MGI
  • tissue development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Names & Taxonomyi

Protein namesi
Recommended name:
Twisted gastrulation protein homolog 1
Gene namesi
Name:Twsg1
Synonyms:Tsg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:2137520. Twsg1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality and sirenomelia were observed only in BMP null embryos in which one or two copies of TSG were also missing. When TSG and BMP7 are mutated, the siren phenotype results from the fusion of the limb buds in the ventroposterior midline owing to a paucity of posterior ventral mesoderm.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 222198Twisted gastrulation protein homolog 1PRO_0000278809Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9EP52.
PaxDbiQ9EP52.
PRIDEiQ9EP52.

Expressioni

Tissue specificityi

Expressed in lymph node, liver, kidney, and lung. Expression in the kidney was stronger in the medulla than in the cortex, particularly in the cells surrounding the medullary tubules. Expressed in growth plate cartilage of long bones, ribs, and digits and to a lesser extent also in the resting zone of the epiphysis, trabecular bone, and vertebral cartilage. Expression seems to be absent from other skeletal tissues including muscle, skin, and fibroblasts.1 Publication

Developmental stagei

Expressed at all embryonic stages examined. Expression was low and distribution was diffuse. At the primitive streak stage, detected in the extraembryonic region. Signal first appeared in the embryo during the neural plate stage. Stronger and more localized expression is seen after embryonic turning. Higher expression is seen in the branchial arch mesenchyme, the endoderm of the developing pharynx, all levels of the developing gut, the myotome compartment of the somites, and some regions of surface ectoderm. At 8.25 and 9.0 dpc expressed in head mesenchyme and ventral mesoderm.2 Publications

Gene expression databases

BgeeiQ9EP52.
CleanExiMM_TWSG1.
GenevestigatoriQ9EP52.

Interactioni

Subunit structurei

Interacts with CHRD and/or BMP4. This interaction enhances CHRD/BMP4 complex formation. Interacts with BMP7.3 Publications

Protein-protein interaction databases

BioGridi211157. 1 interaction.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi18 – 7659Cys-richAdd
BLAST

Domaini

The N-terminal domain is sufficient to interact with BMP4.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG70213.
GeneTreeiENSGT00390000007058.
HOGENOMiHOG000044674.
HOVERGENiHBG055753.
InParanoidiQ9EP52.
OMAiCCSCVEL.
OrthoDBiEOG7J70GN.
PhylomeDBiQ9EP52.
TreeFamiTF323922.

Family and domain databases

InterProiIPR006761. Tsg.
[Graphical view]
PANTHERiPTHR12312. PTHR12312. 1 hit.
PfamiPF04668. Tsg. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9EP52-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSHYIVLAL ASLTFLLCLP VSQSCNKALC ASDVSKCLIQ ELCQCRPGEG
60 70 80 90 100
NCPCCKECML CLGALWDECC DCVGMCNPRN YSDTPPTSKS TVEELHEPIP
110 120 130 140 150
SLFRALTEGD TQLNWNIVSF PVAEELSHHE NLVSFLETVN QLHHQNVSVP
160 170 180 190 200
SNNVHAPFPS DKERMCTVVY FDDCMSIHQC KISCESMGAS KYRWFHNACC
210 220
ECIGPECIDY GSKTVKCMNC MF
Length:222
Mass (Da):24,801
Last modified:March 1, 2001 - v1
Checksum:iF9B0CEE2A8DF8CA7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61I → IA in AAG10080 (Ref. 3) Curated
Sequence conflicti75 – 751M → R in AAG10080 (Ref. 3) Curated
Sequence conflicti75 – 751M → R in AAH04850 (PubMed:15489334).Curated
Sequence conflicti168 – 1681V → E in BAC28326 (PubMed:16141072).Curated
Sequence conflicti203 – 2042IG → MR in AAG10080 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297390 mRNA. Translation: CAC05586.1.
AF292033 mRNA. Translation: AAG00605.1.
AF295097 mRNA. Translation: AAG10080.1.
AK018524 mRNA. Translation: BAC25557.1.
AK033504 mRNA. Translation: BAC28326.1.
AK049646 mRNA. Translation: BAC33857.1.
AK168547 mRNA. Translation: BAE40422.1.
AK168633 mRNA. Translation: BAE40493.1.
BC004850 mRNA. Translation: AAH04850.1.
CCDSiCCDS28942.1.
RefSeqiNP_075540.1. NM_023053.3.
UniGeneiMm.10153.

Genome annotation databases

EnsembliENSMUST00000024906; ENSMUSP00000024906; ENSMUSG00000024098.
GeneIDi65960.
KEGGimmu:65960.
UCSCiuc008dgq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297390 mRNA. Translation: CAC05586.1.
AF292033 mRNA. Translation: AAG00605.1.
AF295097 mRNA. Translation: AAG10080.1.
AK018524 mRNA. Translation: BAC25557.1.
AK033504 mRNA. Translation: BAC28326.1.
AK049646 mRNA. Translation: BAC33857.1.
AK168547 mRNA. Translation: BAE40422.1.
AK168633 mRNA. Translation: BAE40493.1.
BC004850 mRNA. Translation: AAH04850.1.
CCDSiCCDS28942.1.
RefSeqiNP_075540.1. NM_023053.3.
UniGeneiMm.10153.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211157. 1 interaction.

Proteomic databases

MaxQBiQ9EP52.
PaxDbiQ9EP52.
PRIDEiQ9EP52.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024906; ENSMUSP00000024906; ENSMUSG00000024098.
GeneIDi65960.
KEGGimmu:65960.
UCSCiuc008dgq.2. mouse.

Organism-specific databases

CTDi57045.
MGIiMGI:2137520. Twsg1.

Phylogenomic databases

eggNOGiNOG70213.
GeneTreeiENSGT00390000007058.
HOGENOMiHOG000044674.
HOVERGENiHBG055753.
InParanoidiQ9EP52.
OMAiCCSCVEL.
OrthoDBiEOG7J70GN.
PhylomeDBiQ9EP52.
TreeFamiTF323922.

Miscellaneous databases

NextBioi320380.
PROiQ9EP52.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EP52.
CleanExiMM_TWSG1.
GenevestigatoriQ9EP52.

Family and domain databases

InterProiIPR006761. Tsg.
[Graphical view]
PANTHERiPTHR12312. PTHR12312. 1 hit.
PfamiPF04668. Tsg. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Evolutionary conservation, developmental expression, and genomic mapping of mammalian Twisted gastrulation."
    Graf D., Timmons P.M., Hitchins M., Episkopou V., Moore G., Ito T., Fujiyama A., Fisher A.G., Merkenschlager M.
    Mamm. Genome 12:554-560(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CHRD AND BMP4.
    Tissue: Thymus.
  2. "Characterization of the mouse homolog of Twisted gastrulation."
    Zakin L., Oelgeschlager M., Geissert D., De Robertis E.M.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Mouse twisted gastrulation protein: a new signal pathway of spermatogenesis."
    Li J.M., Sha J.H., Zhou Z.M.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  4. "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.
    , 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: Amnion, Colon, Liver and Spinal cord.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary tumor.
  6. "Homologues of Twisted gastrulation are extracellular cofactors in antagonism of BMP signalling."
    Scott I.C., Blitz I.L., Pappano W.N., Maas S.A., Cho K.W.Y., Greenspan D.S.
    Nature 410:475-478(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH CHRD AND BMP4.
  7. "The developmentally regulated expression of Twisted gastrulation reveals a role for bone morphogenetic proteins in the control of T cell development."
    Graf D., Nethisinghe S., Palmer D.B., Fisher A.G., Merkenschlager M.
    J. Exp. Med. 196:163-171(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Sirenomelia in Bmp7 and Tsg compound mutant mice: requirement for Bmp signaling in the development of ventral posterior mesoderm."
    Zakin L., Reversade B., Kuroda H., Lyons K.M., De Robertis E.M.
    Development 132:2489-2499(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, INTERACTION WITH BMP7.
  9. "Twisted gastrulation modulates bone morphogenetic protein-induced collagen II and X expression in chondrocytes in vitro and in vivo."
    Schmidl M., Adam N., Surmann-Schmitt C., Hattori T., Stock M., Dietz U., de Crombrugghe B., Poeschl E., von der Mark K.
    J. Biol. Chem. 281:31790-31800(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiTWSG1_MOUSE
AccessioniPrimary (citable) accession number: Q9EP52
Secondary accession number(s): Q8CCB1
, Q8CEM6, Q99K77, Q9ERN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: March 1, 2001
Last modified: May 27, 2015
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.