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http://purl.uniprot.org/citations/29503074http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29503074http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29503074http://www.w3.org/2000/01/rdf-schema#comment"The pseudo-kinase and signaling protein Pragmin has been linked to cancer by regulating protein tyrosine phosphorylation via unknown mechanisms. Here we present the crystal structure of the Pragmin 906-1,368 amino acid C terminus, which encompasses its kinase domain. We show that Pragmin contains a classical protein-kinase fold devoid of catalytic activity, despite a conserved catalytic lysine (K997). By proteomics, we discovered that this pseudo-kinase uses the tyrosine kinase CSK to induce protein tyrosine phosphorylation in human cells. Interestingly, the protein-kinase domain is flanked by N- and C-terminal extensions forming an original dimerization domain that regulates Pragmin self-association and stimulates CSK activity. A1329E mutation in the C-terminal extension destabilizes Pragmin dimerization and reduces CSK activation. These results reveal a dimerization mechanism by which a pseudo-kinase can induce protein tyrosine phosphorylation. Further sequence-structure analysis identified an additional member (C19orf35) of the superfamily of dimeric Pragmin/SgK269/PEAK1 pseudo-kinases."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2018.01.017"xsd:string
http://purl.uniprot.org/citations/29503074http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2018.01.017"xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Allemand F."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Allemand F."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Simon V."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Simon V."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Urbach S."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Urbach S."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Roche S."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Roche S."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Labesse G."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Labesse G."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Pons J.L."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Pons J.L."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Lecointre C."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Lecointre C."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Gelin M."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Gelin M."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Brignatz C."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Brignatz C."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Fournet A."xsd:string
http://purl.uniprot.org/citations/29503074http://purl.uniprot.org/core/author"Fournet A."xsd:string