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http://purl.uniprot.org/citations/7644498http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7644498http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7644498http://www.w3.org/2000/01/rdf-schema#comment"The WW domain has previously been described as a motif of 38 semiconserved residues found in seemingly unrelated proteins, such as dystrophin, Yes-associated protein (YAP), and two transcriptional regulators, Rsp-5 and FE65. The molecular function of the WW domain has been unknown until this time. Using a functional screen of a cDNA expression library, we have identified two putative ligands of the WW domain of YAP, which we named WBP-1 and WBP-2. Peptide sequence comparison between the two partial clones revealed a homologous region consisting of a proline-rich domain followed by a tyrosine residue (with the shared sequence PPPPY), which we shall call the PY motif. Binding assays and site-specific mutagenesis have shown that the PY motif binds with relatively high affinity and specificity to the WW domain of YAP, with the preliminary consensus XPPXY being critical for binding. Herein, we have implicated the WW domain with a role in mediating protein-protein interactions, as a variant of the paradigm set by Src homology 3 domains and their proline-rich ligands."xsd:string
http://purl.uniprot.org/citations/7644498http://purl.org/dc/terms/identifier"doi:10.1073/pnas.92.17.7819"xsd:string
http://purl.uniprot.org/citations/7644498http://purl.org/dc/terms/identifier"doi:10.1073/pnas.92.17.7819"xsd:string
http://purl.uniprot.org/citations/7644498http://purl.uniprot.org/core/author"Sudol M."xsd:string
http://purl.uniprot.org/citations/7644498http://purl.uniprot.org/core/author"Sudol M."xsd:string
http://purl.uniprot.org/citations/7644498http://purl.uniprot.org/core/author"Chen H.I."xsd:string
http://purl.uniprot.org/citations/7644498http://purl.uniprot.org/core/author"Chen H.I."xsd:string
http://purl.uniprot.org/citations/7644498http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7644498http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7644498http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/7644498http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/7644498http://purl.uniprot.org/core/pages"7819-7823"xsd:string
http://purl.uniprot.org/citations/7644498http://purl.uniprot.org/core/pages"7819-7823"xsd:string
http://purl.uniprot.org/citations/7644498http://purl.uniprot.org/core/title"The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules."xsd:string
http://purl.uniprot.org/citations/7644498http://purl.uniprot.org/core/title"The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules."xsd:string
http://purl.uniprot.org/citations/7644498http://purl.uniprot.org/core/volume"92"xsd:string
http://purl.uniprot.org/citations/7644498http://purl.uniprot.org/core/volume"92"xsd:string
http://purl.uniprot.org/citations/7644498http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7644498
http://purl.uniprot.org/citations/7644498http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7644498
http://purl.uniprot.org/citations/7644498http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7644498
http://purl.uniprot.org/citations/7644498http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7644498
http://purl.uniprot.org/uniprot/P46938http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7644498
http://purl.uniprot.org/uniprot/P97764http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7644498