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http://purl.uniprot.org/citations/9843967http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9843967http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9843967http://www.w3.org/2000/01/rdf-schema#comment"beta-catenin, the vertebrate homolog of the Drosophila Armadillo protein, has been shown to have dual cellular functions, as a component of both the cadherin-catenin cell adhesion complex and the Wnt signaling pathway. At Wnt signaling, beta-catenin becomes stabilized in the cytoplasm and subsequently available for interaction with transcription factors of the lymphocyte enhancer factor-1/T-cell factor family, resulting in a nuclear localization of beta-catenin. Although beta-catenin does not bind DNA directly, its carboxyl- and amino-terminal regions exhibit a transactivating activity still not well understood molecularly. Here we report the identification of an interaction partner of beta-catenin, a nuclear protein designated Pontin52. Pontin52 binds beta-catenin in the region of Armadillo repeats 2-5 and, more importantly, also binds the TATA box binding protein. We provide evidence for an in vivo multiprotein complex composed of Pontin52, beta-catenin, and lymphocyte enhancer factor-1/T-cell factor. Our results suggest involvement of Pontin52 in the nuclear function of beta-catenin."xsd:string
http://purl.uniprot.org/citations/9843967http://purl.org/dc/terms/identifier"doi:10.1073/pnas.95.25.14787"xsd:string
http://purl.uniprot.org/citations/9843967http://purl.org/dc/terms/identifier"doi:10.1073/pnas.95.25.14787"xsd:string
http://purl.uniprot.org/citations/9843967http://purl.uniprot.org/core/author"Huber O."xsd:string
http://purl.uniprot.org/citations/9843967http://purl.uniprot.org/core/author"Huber O."xsd:string
http://purl.uniprot.org/citations/9843967http://purl.uniprot.org/core/author"Bauer A."xsd:string
http://purl.uniprot.org/citations/9843967http://purl.uniprot.org/core/author"Bauer A."xsd:string
http://purl.uniprot.org/citations/9843967http://purl.uniprot.org/core/author"Kemler R."xsd:string
http://purl.uniprot.org/citations/9843967http://purl.uniprot.org/core/author"Kemler R."xsd:string
http://purl.uniprot.org/citations/9843967http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9843967http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9843967http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/9843967http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/9843967http://purl.uniprot.org/core/pages"14787-14792"xsd:string
http://purl.uniprot.org/citations/9843967http://purl.uniprot.org/core/pages"14787-14792"xsd:string
http://purl.uniprot.org/citations/9843967http://purl.uniprot.org/core/title"Pontin52, an interaction partner of beta-catenin, binds to the TATA box binding protein."xsd:string
http://purl.uniprot.org/citations/9843967http://purl.uniprot.org/core/title"Pontin52, an interaction partner of beta-catenin, binds to the TATA box binding protein."xsd:string
http://purl.uniprot.org/citations/9843967http://purl.uniprot.org/core/volume"95"xsd:string
http://purl.uniprot.org/citations/9843967http://purl.uniprot.org/core/volume"95"xsd:string
http://purl.uniprot.org/citations/9843967http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9843967
http://purl.uniprot.org/citations/9843967http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9843967
http://purl.uniprot.org/citations/9843967http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9843967
http://purl.uniprot.org/citations/9843967http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9843967