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http://purl.uniprot.org/citations/11178875http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11178875http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11178875http://www.w3.org/2000/01/rdf-schema#comment"The Shank family of proteins (also termed CortBP, ProSAP, or Synamon) is highly enriched in the postsynaptic density (PSD) of excitatory synapses in brain. Shank contains multiple domains for protein-protein interactions, including ankyrin repeats, SH3 domain, PDZ domain, SAM domain, and an extensive proline-rich region. We have identified a novel protein, termed Sharpin, that directly interacts with the ankyrin repeats of Shank. Sharpin is enriched in the PSD and forms a complex with Shank in heterologous cells and brain. Immunostaining reveals the presence of Sharpin at excitatory synapses and its colocalization with Shank. While the C-terminal half of Sharpin interacts with Shank, the N-terminal half of Sharpin mediates homomultimerization. Considering the fact that the ankyrin repeats and the SH3 domain of Shank can be truncated by alternative splicing, these results define Sharpin as a novel PSD protein that may regulate the complexity of the Shank-based protein network in an alternative splicing-dependent manner."xsd:string
http://purl.uniprot.org/citations/11178875http://purl.org/dc/terms/identifier"doi:10.1006/mcne.2000.0940"xsd:string
http://purl.uniprot.org/citations/11178875http://purl.org/dc/terms/identifier"doi:10.1006/mcne.2000.0940"xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/author"Kim E."xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/author"Kim E."xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/author"Park S."xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/author"Park S."xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/author"Kuroda S."xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/author"Kuroda S."xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/author"Lim S."xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/author"Lim S."xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/author"Sala C."xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/author"Sala C."xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/author"Yoon J."xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/author"Yoon J."xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/author"Sheng M."xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/author"Sheng M."xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/name"Mol. Cell. Neurosci."xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/name"Mol. Cell. Neurosci."xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/pages"385-397"xsd:string
http://purl.uniprot.org/citations/11178875http://purl.uniprot.org/core/pages"385-397"xsd:string