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http://purl.uniprot.org/citations/7566156http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7566156http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7566156http://www.w3.org/2000/01/rdf-schema#comment"Transforming growth factor-beta (TGF-beta) is the prototype for a family of extracellular polypeptides that affect cell proliferation and differentiation, and tissue morphogenesis. TGF-beta signalling is mediated by two types of serine/threonine kinase receptors, the type I and II receptors, which are able to form a heteromeric complex. No cytoplasmic proteins that associate with these receptors in vivo, or are their kinase targets, have yet been described. We have now identified a WD-domain-containing protein, TRIP-1, which specifically associates with the type II TGF-beta receptor in a kinase-dependent way. TRIP-1 does not interact with the type II activin or type I receptors, but associates with the heteromeric TGF-beta receptor complex. TRIP-1 is phosphorylated on serine and threonine by the receptor kinase, strongly suggesting that it has a role in TGF-beta signalling. This is supported by coexpression of TRIP-1 and type II receptor during development. The existence of TRIP-1 homologues in plant and yeast suggests a conserved function in all eukaryotes."xsd:string
http://purl.uniprot.org/citations/7566156http://purl.org/dc/terms/identifier"doi:10.1038/377548a0"xsd:string
http://purl.uniprot.org/citations/7566156http://purl.org/dc/terms/identifier"doi:10.1038/377548a0"xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/author"Derynck R."xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/author"Derynck R."xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/author"Chen R.H."xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/author"Chen R.H."xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/author"Choy L."xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/author"Choy L."xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/author"Maruka E.M."xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/author"Maruka E.M."xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/author"Miettinen P.J."xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/author"Miettinen P.J."xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/pages"548-552"xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/pages"548-552"xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/title"A WD-domain protein that is associated with and phosphorylated by the type II TGF-beta receptor."xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/title"A WD-domain protein that is associated with and phosphorylated by the type II TGF-beta receptor."xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/volume"377"xsd:string
http://purl.uniprot.org/citations/7566156http://purl.uniprot.org/core/volume"377"xsd:string